Datasets:

lhallee

/

exp_new_unprocessed

like 0

A0A1D5Q9W4

MAALSGGGGGGAEPGQALFNGDMEPEAGAAASSAADPAIPEEVWNIKQMIKLTQEHIEALLDKFGGEHNPPSIYLEAYEEYTSKLDALQQREQQLLEYLGNGTDFSVSSSASMDTVTSSSSSSLSVLPSSLSVFQNPTDVSRSNPKSPQKPIVRVFLPNKQRTVVPARCGVTVRDSLKKALMMRGLIPECCAVYRIQDGEKKPIGWDTDISWLTGEELHVEVLENVPLTTHNFVRKTFFTLAFCDFCRKLLFQGFRCQTCGYKFHQRCSTEVPLMCVNYDQLDLLFVSKFFEHHPIPQEEASLAETALTSGSSPSAPTSDSLGPQILTSPSPSKSIPIPQPFRPADEDHRNQFGQRDRSSSAPNVHINTIEPVNIDDLIRDQGFRGDGGSTTGLSATPPASLPGSLTNVKALQKSPGPQRERKSSSSSEDRNRMKTLGRRDSSDDWEIPDGQITVGQRIGSGSFGTVYKGKWHGDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQLAIVTQWCEGSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSGSHQFEQLSGSILWMAPEVIRMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGYLSPDLSKVRSNCPKAMKRLMAECLKKKRDERPLFPQILASIELLARSLPKIHRSASEPSLNRAGFQTEDFSLYACASPKTPIQAGGYGEFAAFK

Macaca mulatta (Rhesus macaque)

2.7.11.1

CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00001433}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};

COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|ARBA:ARBA00001947};

ATP-binding;Kinase;Metal-binding;Nucleotide-binding;Phosphoprotein;Reference proteome;Serine/threonine-protein kinase;Transferase;Zinc

CD4-positive or CD8-positive, alpha-beta T cell lineage commitment [GO:0043369]; CD4-positive, alpha-beta T cell differentiation [GO:0043367]; cellular response to calcium ion [GO:0071277]; cellular response to xenobiotic stimulus [GO:0071466]; endothelial cell apoptotic process [GO:0072577]; epidermal growth factor receptor signaling pathway [GO:0007173]; ERK1 and ERK2 cascade [GO:0070371]; establishment of protein localization to membrane [GO:0090150]; face development [GO:0060324]; head morphogenesis [GO:0060323]; long-term synaptic potentiation [GO:0060291]; myeloid progenitor cell differentiation [GO:0002318]; negative regulation of endothelial cell apoptotic process [GO:2000352]; negative regulation of fibroblast migration [GO:0010764]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of synaptic vesicle exocytosis [GO:2000301]; phosphorylation [GO:0016310]; positive regulation of axon regeneration [GO:0048680]; positive regulation of axonogenesis [GO:0050772]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of gene expression [GO:0010628]; positive regulation of glucose transmembrane transport [GO:0010828]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; positive regulation of stress fiber assembly [GO:0051496]; positive regulation of substrate adhesion-dependent cell spreading [GO:1900026]; protein modification process [GO:0036211]; Ras protein signal transduction [GO:0007265]; regulation of cell population proliferation [GO:0042127]; regulation of T cell differentiation [GO:0045580]; somatic stem cell population maintenance [GO:0035019]; stress fiber assembly [GO:0043149]; substrate adhesion-dependent cell spreading [GO:0034446]; synaptic vesicle exocytosis [GO:0016079]; T cell differentiation in thymus [GO:0033077]; T cell receptor signaling pathway [GO:0050852]; thymus development [GO:0048538]; thyroid gland development [GO:0030878]; trehalose metabolism in response to stress [GO:0070413]; visual learning [GO:0008542]

cell body [GO:0044297]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; presynapse [GO:0098793]

ATP binding [GO:0005524]; calcium ion binding [GO:0005509]; identical protein binding [GO:0042802]; MAP kinase kinase activity [GO:0004708]; protein kinase activity [GO:0004672]; protein serine/threonine kinase activity [GO:0004674]; scaffold protein binding [GO:0097110]

IPR046349;IPR020454;IPR011009;IPR002219;IPR000719;IPR017441;IPR003116;IPR001245;IPR008271;IPR029071;

3.30.60.20;1.10.510.10;

A0A1D5QCC6

PLCPGMDIRNNLTRLHELENCSVIEGHLQILLMFKTRPEDFRDLSFPKLIMITDYLLLFRVYGLESLKDLFPNLTVIRGSRLFFNYALVIFEMVHLKELGLYNLMNITRGSVRIEKNNELCYLATIDWSRILDSVEDNYIVLNKDDNEECGDICPGTAKGKTNCPATVINGQFVERCWTHSHCQKVCPTICKSHGCTAEGLCCHSECLGNCSEPDDPTKCVACRNFYLDGRCVETCPPPYYHFQDWRCVNFSFCQDLHHKCKNSRRQGCHQYVIHNNKCIPECPSGYTMNSSNLLCTPCLGPCPKVCHLLEGEKTIDSVTSAQELRGCTVINGSLIINIRGGNNLAAELEANLGLIEEISGETLEIGNYSFYALDNQNLRQLWDWSKHNLTITQGKLFFHYNPKLCLSEIHKMEEVSGTKGRQERNDIALKTNGDQASCENELLKFSYIRTSFDKILLRWEPYWPPDFRDLLGFMLFYKEAPYQNVTEFDGQDACGSNSWTVVDIDPPLRSNDPKSQNHPGWLMRGLKPWTQYAIFVKTLVTFSDERRTYGAKSDIIYVQTDATSECVLGIDVSPAFLFLSPGLKLPSRTWSPPFESEDSQKHNQSEYEDSAGECCSCPKTDSQILKELEESSFRKTFEDYLHNVVFVPRSGLGAGPSRKRRSLGDVGNVTVAVPTVAAFPNTSSTSTPTSPEEHRPFEKVVNKESLVISGLRHFTGYRIELQACNQDTPEERCSVAAYVSARTSKADDIVGPVTHEIFENNIVHLMWQEPKEPNGLIVLYEVSYRRYGDEELHLCVSRKHFALERGCRLRGLSPGNYSVRVRATSLAGNGSWTEPTYFYVTDYLDVPSNIAKIIIGPLIFVFLFSIVIGSIYLFLRKRQPDGPLGPLYASSNPEYLSASDVFPCSVYVPDEWEVPREKITLLRELGQGSFGMVYEGNARDIIKGEAETRVAVKTVNESASLRERIEFLNEASVMKGFTCHHVVRLLGVVSKGQPTLVVMELMAHGDLKSYLRSLRPEAENNPGRLPPTLQEMIQMAAEIADGMAYLNAKKFVHRDLAARNCMVAHDFTVKIGDFGMTRDIYETDYYRKGGKGLLPVRWMAPESLKDGVFTTSSDMWSFGVVLWEITSLAEQPYQGLSNEQVLKFVMDGGYLDQPDNCPERVTDLMRMCWQFNPKMRPTFLEIVNLLKDDLHPSFPEVSFFHSEENKAPENEELEMEFEDMENVPLDRSSHCQREEAGGRDGGSSLGFKRSYEEHIPYTHMNGGKKNGRILTLPRSNPS

Macaca mulatta (Rhesus macaque)

2.7.10.1

CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence={ECO:0000256|ARBA:ARBA00001171, ECO:0000256|RuleBase:RU000312};

ATP-binding;Glycoprotein;Kinase;Membrane;Nucleotide-binding;Phosphoprotein;Receptor;Reference proteome;Signal;Transferase;Transmembrane;Transmembrane helix;Tyrosine-protein kinase

G protein-coupled receptor signaling pathway [GO:0007186]; glucose homeostasis [GO:0042593]; heart morphogenesis [GO:0003007]; phosphorylation [GO:0016310]; positive regulation of cell migration [GO:0030335]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of developmental growth [GO:0048639]; positive regulation of glucose import [GO:0046326]; positive regulation of glycogen biosynthetic process [GO:0045725]; positive regulation of glycolytic process [GO:0045821]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of mitotic nuclear division [GO:0045840]; positive regulation of nitric oxide biosynthetic process [GO:0045429]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of receptor internalization [GO:0002092]; positive regulation of respiratory burst [GO:0060267]; regulation of DNA-templated transcription [GO:0006355]; regulation of embryonic development [GO:0045995]; symbiont entry into host cell [GO:0046718]

axon [GO:0030424]; caveola [GO:0005901]; insulin receptor complex [GO:0005899]; nuclear envelope [GO:0005635]; nuclear lumen [GO:0031981]

amyloid-beta binding [GO:0001540]; ATP binding [GO:0005524]; GTP binding [GO:0005525]; insulin binding [GO:0043559]; insulin receptor activity [GO:0005009]; insulin receptor substrate binding [GO:0043560]; insulin-like growth factor I binding [GO:0031994]; insulin-like growth factor II binding [GO:0031995]; insulin-like growth factor receptor binding [GO:0005159]; phosphatidylinositol 3-kinase binding [GO:0043548]; protein-containing complex binding [GO:0044877]; PTB domain binding [GO:0051425]

SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.

IPR003961;IPR036116;IPR006211;IPR006212;IPR009030;IPR013783;IPR040969;IPR011009;IPR000719;IPR017441;IPR000494;IPR036941;IPR001245;IPR008266;IPR020635;IPR016246;IPR002011;

2.60.40.10;3.80.20.20;1.10.510.10;

A0A1D5QD89

MLQLMDSGITICLRNGAASVFKKKEWSTQGEENKQDSKLKKLSEDSLTKQPEEVFDVLEKLGEGSYGSVFKAIHKESGQVVAIKQVPVESDLQEIIKEISIMQQCDSPYVVKYYGSYFKNTDLWIVMEYCGAGSVSDIIRLRNKTLTEDEIATILKSTLKGLEYLHFMRKIHRDIKAGNILLNTEGHAKLADFGVAGQLTDTMAKRNTVIGTPFWMAPEVIQEIGYNCVADIWSLGITSIEMAEGKPPYADIHPMRAIFMIPTNPPPTFRKPELWSDDFTDFVKKCLVKNPEQRATATQLLQHPFIKNAKPVSILRDLITEAMEIKAKRHEEQQRELEEEEENSDEDELDSHTMVKTSVESVGTMRATSTMSEGAQTMIEHNSTMLESDLGTMVINSEDEEEEDGTMKRNATSPQVQRPSFMDYFDKQDFKNKSHENCNQNMHEPFPLSKNVFPDNWKVPQDGDFDFLKNLSLEELQMRLKALDPMMEREIEELRQRYTAKRQPILDAMDAKKRRQQNF

Macaca mulatta (Rhesus macaque)

2.7.11.1

CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00001433}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|ARBA:ARBA00001946};

Apoptosis;ATP-binding;Coiled coil;Kinase;Nucleotide-binding;Reference proteome;Transferase

canonical Wnt signaling pathway [GO:0060070]; cell differentiation involved in embryonic placenta development [GO:0060706]; central nervous system development [GO:0007417]; endocardium development [GO:0003157]; epithelial cell proliferation [GO:0050673]; extrinsic apoptotic signaling pathway via death domain receptors [GO:0008625]; hepatocyte apoptotic process [GO:0097284]; hippo signaling [GO:0035329]; intracellular signal transduction [GO:0035556]; JNK cascade [GO:0007254]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of epithelial cell proliferation [GO:0050680]; negative regulation of organ growth [GO:0046621]; neural tube formation [GO:0001841]; organ growth [GO:0035265]; phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0043491]; phosphorylation [GO:0016310]; positive regulation of extrinsic apoptotic signaling pathway via death domain receptors [GO:1902043]; positive regulation of fat cell differentiation [GO:0045600]; positive regulation of JNK cascade [GO:0046330]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; primitive hemopoiesis [GO:0060215]; protein import into nucleus [GO:0006606]; protein localization to centrosome [GO:0071539]; protein stabilization [GO:0050821]; protein tetramerization [GO:0051262]; regulation of cell differentiation involved in embryonic placenta development [GO:0060800]; regulation of MAPK cascade [GO:0043408]

centrosome [GO:0005813]; cytoplasm [GO:0005737]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]

ATP binding [GO:0005524]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; protein serine/threonine kinase activity [GO:0004674]

IPR011009;IPR024205;IPR049568;IPR036674;IPR000719;IPR017441;IPR011524;

1.10.287.4270;4.10.170.10;1.10.510.10;

A0A1D5QDK1

MRPSGTAGAALLALLAALCPASRALEEKKVCQGTSNKLTQLGTFEDHFLSLQRMFNNCEVVLGNLEITYVQRNYDLSFLKTIQEVAGYVLIALNTVERIPLENLQIIRGNMYYENSYALAVLSNYDANKTGLKELPMRNLQEILHGAVRFSNNPALCNVESIQWRDIVSSEFLSNMSMDFQNHLGSCQKCDPSCPNGSCWGAGEENCQKLTKIICAQQCSGRCRGKSPSDCCHNQCAAGCTGPRESDCLVCRKFRDEATCKDTCPPLMLYNPTTYQMDVNPEGKYSFGATCVKKCPRNYVVTDHGSCVRACGADSYEMEEDGVRKCKKCEGPCRKVCNGIGIGEFKDTLSINATNIKHFKNCTSISGDLHILPVAFRGDSFTHTPPLDPQELDILKTVKEITGFLLIQAWPENRTDLHAFENLEIIRGRTKQHGQFSLAVVSLNITSLGLRSLKEISDGDVIISGNKNLCYANTINWKKLFGTSSQKTKIISNRGENSCKATGQVCHALCSPEGCWGPEPRDCVSCQNVSRGRECVDKCNILEGEPREFVENSECIQCHPECLPQVMNITCTGRGPDNCIQCAHYIDGPHCVKTCPAGVMGENNTLVWKYADAGHVCHLCHPNCTYGCTGPGLEGCARNGPKIPSIATGMVGALLLLLVVALGIGLFMRRRHIVRKRTLRRLLQERELVEPLTPSGEAPNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLITQLMPFGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDVYMIMVKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEEDMDDVVDADEYLIPQQGFFSSPSTSRTPLLSSLSATSNNSTVACIDRNGLQSCPIKEDSFLQRYSSDPTGALTEDSIDDTFLPVPEYINQSVPKRPAGSVQNPVYHNQPLNPAPSRDPHYQDPHSTAVGNPEYLNTVQPTCVNSTFDSPAHWAQKGSHQISLDNPDYQQDFFPKEAKPNGIFKGSTAENAEYLRVAPQSSEFIGA

Macaca mulatta (Rhesus macaque)

2.7.10.1

CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence={ECO:0000256|ARBA:ARBA00001171};

ATP-binding;Kinase;Membrane;Nucleotide-binding;Phosphoprotein;Receptor;Reference proteome;Signal;Transferase;Transmembrane;Transmembrane helix;Tyrosine-protein kinase

cell-cell adhesion [GO:0098609]; cellular response to cadmium ion [GO:0071276]; cellular response to estradiol stimulus [GO:0071392]; cellular response to reactive oxygen species [GO:0034614]; ERBB2-EGFR signaling pathway [GO:0038134]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cardiocyte differentiation [GO:1905208]; negative regulation of protein catabolic process [GO:0042177]; neurogenesis [GO:0022008]; phosphorylation [GO:0016310]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of cell growth [GO:0030307]; positive regulation of cell migration [GO:0030335]; positive regulation of DNA repair [GO:0045739]; positive regulation of DNA replication [GO:0045740]; positive regulation of epithelial cell proliferation [GO:0050679]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of G1/S transition of mitotic cell cycle [GO:1900087]; positive regulation of miRNA transcription [GO:1902895]; positive regulation of non-canonical NF-kappaB signal transduction [GO:1901224]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of protein localization to plasma membrane [GO:1903078]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of JNK cascade [GO:0046328]; regulation of peptidyl-tyrosine phosphorylation [GO:0050730]; response to UV-A [GO:0070141]

basal plasma membrane [GO:0009925]; basolateral plasma membrane [GO:0016323]; cell junction [GO:0030054]; cell surface [GO:0009986]; early endosome membrane [GO:0031901]; membrane raft [GO:0045121]; multivesicular body, internal vesicle lumen [GO:0097489]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; receptor complex [GO:0043235]; ruffle membrane [GO:0032587]

actin filament binding [GO:0051015]; ATP binding [GO:0005524]; chromatin binding [GO:0003682]; epidermal growth factor binding [GO:0048408]; epidermal growth factor receptor activity [GO:0005006]; identical protein binding [GO:0042802]; kinase binding [GO:0019900]; protein phosphatase binding [GO:0019903]; protein tyrosine kinase activator activity [GO:0030296]; ubiquitin protein ligase binding [GO:0031625]

SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.

IPR006211;IPR006212;IPR032778;IPR009030;IPR011009;IPR000719;IPR017441;IPR000494;IPR036941;IPR001245;IPR049328;IPR008266;IPR020635;IPR016245;

1.20.5.420;3.80.20.20;1.10.510.10;

A0A1D5QF63

MALDCLLLLLLASAVAAMEETLMDTRTATAELGWTANPASGWEEVSGYDENLNTIRTYQVCNVFEPNQNNWLLTTFINRRGAHRIYTEMRFTVRDCSSLPNVPGSCKETFNLYYYETDSVIATKKSAFWSEAPYLKVDTIAADESFSQVDFGGRLMKVNTEVRSFGPLTRNGFYLAFQDYGACMSLLSVRVFFKKCPSIVQNFAVFPETMTGAESTSLVIARGTCIPNAEEVDVPIKLYCNGDGEWMVPIGRCTCKPGYEPENSVACKACPAGTFKASQEAEGCSHCPSNSRSPAEASPICTCRTGYYRADFDPPEVACTSVPSGPRNVISIVNETSIILEWHPPRETGGRDDVTYNIICKKCRADRRSCSRCDDNVEFVPRQLGLTECRVSISSLWAHTPYTFDIQAINGVSSKSPFPPQHVSVNITTNQAAPSTVPIMHQVSATMRSITLSWPQPEQPNGIILDYEIRYYEKEHNEFNSSMARSQTNTARIDGLRPGMVYVVQVRARTVAGYGKFSGKMCFQTLTDDDYKSELREQLPLIAGSAAAGVVFVVSLVAISIVCSRKRAYSKEAVYSDKLQHYSTGRGSPGMKIYIDPFTYEDPNEAVREFAKEIDVSFVKIEEVIGAGEFGEVYKGRLKLPGKREIYVAIKTLKAGYSEKQRRDFLSEASIMGQFDHPNIIRLEGVVTKSRPVMIITEFMENGALDSFLRQNDGQFTVIQLVGMLRGIAAGMKYLAEMNYVHRDLAARNILVNSNLVCKVSDFGLSRYLQDDTSDPTYTSSLGGKIPVRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSFGERPYWDMSNQDVINAIEQDYRLPPPMDCPAALHQLMLDCWQKDRNSRPRFAEIVNTLDKMIRNPASLKTVATITAVPSQPLLDRSIPDFTAFTTVDDWLSAIKMVQYRDSFLTAGFTSLQLVTQMTSEDLLRIGVTLAGHQKKILNSIHSMRVQMSQSPTAMA

Macaca mulatta (Rhesus macaque)

2.7.10.1

CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence={ECO:0000256|ARBA:ARBA00001171};

ATP-binding;Disulfide bond;Kinase;Membrane;Neurogenesis;Nucleotide-binding;Phosphoprotein;Receptor;Reference proteome;Signal;Transferase;Transmembrane;Transmembrane helix;Tyrosine-protein kinase

angiogenesis [GO:0001525]; axon guidance [GO:0007411]; camera-type eye morphogenesis [GO:0048593]; cell chemotaxis [GO:0060326]; cell-substrate adhesion [GO:0031589]; central nervous system projection neuron axonogenesis [GO:0021952]; dendritic spine morphogenesis [GO:0060997]; detection of temperature stimulus involved in sensory perception of pain [GO:0050965]; ephrin receptor signaling pathway [GO:0048013]; establishment of cell polarity [GO:0030010]; modulation of chemical synaptic transmission [GO:0050804]; negative regulation of satellite cell differentiation [GO:1902725]; negative regulation of skeletal muscle satellite cell proliferation [GO:1902723]; neural precursor cell proliferation [GO:0061351]; optic nerve morphogenesis [GO:0021631]; positive regulation of synapse assembly [GO:0051965]; regulation of ERK1 and ERK2 cascade [GO:0070372]; regulation of JNK cascade [GO:0046328]; retinal ganglion cell axon guidance [GO:0031290]; skeletal muscle satellite cell activation [GO:0014719]

axon [GO:0030424]; cytosol [GO:0005829]; dendrite [GO:0030425]; early endosome membrane [GO:0031901]; endoplasmic reticulum [GO:0005783]; filopodium tip [GO:0032433]; glutamatergic synapse [GO:0098978]; membrane raft [GO:0045121]; plasma membrane [GO:0005886]

ATP binding [GO:0005524]; axon guidance receptor activity [GO:0008046]; protein-containing complex binding [GO:0044877]; transmembrane-ephrin receptor activity [GO:0005005]

SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}. Cell projection, dendrite {ECO:0000256|ARBA:ARBA00004279}. Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.

IPR027936;IPR034231;IPR042819;IPR001090;IPR003961;IPR036116;IPR008979;IPR009030;IPR013783;IPR011009;IPR000719;IPR017441;IPR001660;IPR013761;IPR001245;IPR008266;IPR020635;IPR016257;IPR001426;

2.60.40.1770;2.60.120.260;2.60.40.10;1.10.150.50;1.10.510.10;2.10.50.10;

A0A1D5QGA0

MDAAGRGCHLLPLPAARGPARAPAAAAAAASAASPPGLCSGAACAPSAAAGVGAMNPSSSAGEEKGATGGSSSSGSGAGSCCLGAEGGADPRGAGAAAAAGAAALDEPAAAGQKEKDEALEEKLRNLTFRKQVSYRKAISRAGLQHLAPAHPLSLPVANGPAKEPRATLDWSENAVNGEHLWLETNVSGDLCYLGEENCQVRFAKSALRRKCAVCKIVVHTACIEQLEKINFRCKPTFREGGSRSPRENFVRHHWVHRRRQEGKCKQCGKGFQQKFSFHSKEIVAISCSWCKQAFHNKVTCFMLHHIEEPCSLGAHAAVIVPPTWIIKVKKPQVISIPGDELELGWAGDEPGWAGDWSPSENLGFFHFYWEGWQNSLKASNRKKKRTSFKRKASKRGMEQENKGRPFVIKPISSPLMKPLLVFVNPKSGGNQGTKVLQMFMWYLNPRQVFDLSQEGPKDALELYRKVPNLRILACGGDGTVGWILSILDELQLSPQPPVGVLPLGTGNDLARTLNWGGGYTDEPVSKILCQVEDGTIVQLDRWNLHVERNPDLPPEELEDGVCKLPLNVFNNYFSLGFDAHVTLEFHESREANPEKFNSRFRNKMFYAGAAFSDFLQRSSRDLSKHVKVVCDGTDLTPKIQELKFQCIVFLNIPRYCAGTMPWGNPGDHHDFEPQRHDDGYIEVIGFTMASLAALQVGGHGERLHQCREVMLLTYKSIPMQVDGEPCRLAPAMIRISLRNQANMVQKSKRRTSMPLLNDPQSVPDRLRIRVNKISLQDYEGFHYDKEKLREASIPLGILVVRGDCDLETCRMYIDRLQEDLQSVSSGSQRVHYQDHETSFPRALSAQRLSPRWCFLDATSADRFYRIDRSQEHLHFVMEISQDEIFILDPDMVVSQPAGTPPGMPDLVVEQASGISDWWNPALRKRMLSDSGLGMIAPYYEDSDLKDLSHSRVLQSPVSSEDHAILQAVIAGDLMKLIESYKNGGSLLIQGPDHCSLLHYAAKTGNGEIVKYILDHGPSELLDMADSETGETALHKAACQRNRAVCQLLVDAGASLRKTDSKGKTPQERAQQAGDPDLAAYLESRQNYKVIGHEDLETAV

Macaca mulatta (Rhesus macaque)

2.7.1.107

CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycerol + ATP = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:40327, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:52333, ChEBI:CHEBI:74546, ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00023371}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40328; Evidence={ECO:0000256|ARBA:ARBA00023371}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycerol + ATP = 1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:40323, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:75728, ChEBI:CHEBI:77091, ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00023400}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40324; Evidence={ECO:0000256|ARBA:ARBA00023400}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycerol + ATP = a 1,2-diacyl-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:10272, ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:30616, ChEBI:CHEBI:58608, ChEBI:CHEBI:456216; EC=2.7.1.107; Evidence={ECO:0000256|RuleBase:RU361128};

PATHWAY: Lipid metabolism; glycerolipid metabolism. {ECO:0000256|ARBA:ARBA00005175}.

ANK repeat;ATP-binding;Kinase;Lipid metabolism;Metal-binding;Nucleotide-binding;Reference proteome;Repeat;Transferase;Zinc

diacylglycerol metabolic process [GO:0046339]; excitatory postsynaptic potential [GO:0060079]; habituation [GO:0046959]; intracellular signal transduction [GO:0035556]; lipid phosphorylation [GO:0046834]; neurotransmitter secretion [GO:0007269]; platelet activation [GO:0030168]; positive regulation of Ras protein signal transduction [GO:0046579]; presynaptic modulation of chemical synaptic transmission [GO:0099171]; protein kinase C-activating G protein-coupled receptor signaling pathway [GO:0007205]; Ras protein signal transduction [GO:0007265]; regulation of long-term synaptic depression [GO:1900452]; regulation of synaptic transmission, glutamatergic [GO:0051966]

glutamatergic synapse [GO:0098978]; guanyl-nucleotide exchange factor complex [GO:0032045]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; postsynapse [GO:0098794]; presynapse [GO:0098793]; Schaffer collateral - CA1 synapse [GO:0098685]

ATP binding [GO:0005524]; ATP-dependent diacylglycerol kinase activity [GO:0004143]; GTPase inhibitor activity [GO:0005095]; metal ion binding [GO:0046872]; small GTPase binding [GO:0031267]

IPR002110;IPR036770;IPR017438;IPR047486;IPR047487;IPR037607;IPR000756;IPR001206;IPR016064;IPR002219;

2.60.200.40;3.30.60.20;1.25.40.20;

A0A1D5QGI6

MTLVWRHLLRPLFLVTSAPRILEMRPFLSRASWTSVPKLSLHTRPRMPPCDFIPERYQSLGYNRVLEIHKDHLSPVVTAYFQKPLLLHQGHMEWLFDAEGNRYLDFFSGIVTVSVGHCHPKVNAVAQKQLGRLWHTSTVFFHPPMHEYAEKLAALLPEPLKVIFLVNSGSEANELAMLMARAHSNNIDIISFRGAYHGGSPYTLGLTNVGTYKMELPGGTGCQPTMCPDVFRGPWGGSHCRDSPVQTIRKCSCAPDCCQAKDQYIEQFKDTLSTSVAKSIAGFFAEPIQGVNGVVQYPKGFLKEAFELVRARGGVCIADEVQTGFGRLGSHFWGFQTHDVLPDIVTMAKGIGNGFPMAAVVTTPEIAKSLAKRLQYFNTFGGNPMACAIGSAVLEVIKEENLQENSQEVGTYMLLKFAKLRDEFEIVGDVRGKGLMIGIEMVQDKMSRRPLPREEVNQIHEDCKHMGLLVGRGGIFSQTFRIAPSMCITKPEVDFATEVFRSALTQHMERRAKSHSQK

Macaca mulatta (Rhesus macaque)

2.6.1.18; 2.6.1.40; 2.6.1.44

CATALYTIC ACTIVITY: Reaction=(2S)-2-aminobutanoate + glyoxylate = 2-oxobutanoate + glycine; Xref=Rhea:RHEA:77339, ChEBI:CHEBI:16763, ChEBI:CHEBI:36655, ChEBI:CHEBI:57305, ChEBI:CHEBI:74359; Evidence={ECO:0000256|ARBA:ARBA00043679}; CATALYTIC ACTIVITY: Reaction=(R)-3-amino-2-methylpropanoate + pyruvate = 2-methyl-3-oxopropanoate + L-alanine; Xref=Rhea:RHEA:18393, ChEBI:CHEBI:15361, ChEBI:CHEBI:57700, ChEBI:CHEBI:57731, ChEBI:CHEBI:57972; EC=2.6.1.40; Evidence={ECO:0000256|ARBA:ARBA00043726}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18394; Evidence={ECO:0000256|ARBA:ARBA00043726}; CATALYTIC ACTIVITY: Reaction=2-oxobutanoate + L-alanine = (2S)-2-aminobutanoate + pyruvate; Xref=Rhea:RHEA:77355, ChEBI:CHEBI:15361, ChEBI:CHEBI:16763, ChEBI:CHEBI:57972, ChEBI:CHEBI:74359; EC=2.6.1.44; Evidence={ECO:0000256|ARBA:ARBA00043751}; CATALYTIC ACTIVITY: Reaction=2-oxobutanoate + N(omega),N(omega)-dimethyl-L-arginine = (2S)-2-aminobutanoate + 5-(3,3-dimethylguanidino)-2-oxopentanoate; Xref=Rhea:RHEA:77351, ChEBI:CHEBI:16763, ChEBI:CHEBI:58326, ChEBI:CHEBI:74359, ChEBI:CHEBI:197301; Evidence={ECO:0000256|ARBA:ARBA00043779}; CATALYTIC ACTIVITY: Reaction=2-oxohexanoate + N(omega),N(omega)-dimethyl-L-arginine = 5-(3,3-dimethylguanidino)-2-oxopentanoate + L-2-aminohexanoate; Xref=Rhea:RHEA:77363, ChEBI:CHEBI:35177, ChEBI:CHEBI:58326, ChEBI:CHEBI:58455, ChEBI:CHEBI:197301; Evidence={ECO:0000256|ARBA:ARBA00043837}; CATALYTIC ACTIVITY: Reaction=2-oxopentanoate + N(omega),N(omega)-dimethyl-L-arginine = 5-(3,3-dimethylguanidino)-2-oxopentanoate + L-2-aminopentanoate; Xref=Rhea:RHEA:77359, ChEBI:CHEBI:28644, ChEBI:CHEBI:58326, ChEBI:CHEBI:58441, ChEBI:CHEBI:197301; Evidence={ECO:0000256|ARBA:ARBA00043826}; CATALYTIC ACTIVITY: Reaction=3-oxopropanoate + L-alanine = beta-alanine + pyruvate; Xref=Rhea:RHEA:14077, ChEBI:CHEBI:15361, ChEBI:CHEBI:33190, ChEBI:CHEBI:57966, ChEBI:CHEBI:57972; EC=2.6.1.18; Evidence={ECO:0000256|ARBA:ARBA00043825}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:14079; Evidence={ECO:0000256|ARBA:ARBA00043825}; CATALYTIC ACTIVITY: Reaction=L-alanine + oxaloacetate = L-aspartate + pyruvate; Xref=Rhea:RHEA:77347, ChEBI:CHEBI:15361, ChEBI:CHEBI:16452, ChEBI:CHEBI:29991, ChEBI:CHEBI:57972; Evidence={ECO:0000256|ARBA:ARBA00043764}; CATALYTIC ACTIVITY: Reaction=L-ornithine + pyruvate = 5-amino-2-oxopentanoate + L-alanine; Xref=Rhea:RHEA:77327, ChEBI:CHEBI:15361, ChEBI:CHEBI:46911, ChEBI:CHEBI:57972, ChEBI:CHEBI:58802; Evidence={ECO:0000256|ARBA:ARBA00043777}; CATALYTIC ACTIVITY: Reaction=N(omega),N('omega)-dimethyl-L-arginine + pyruvate = 5-(3,3'-dimethylguanidino)-2-oxopentanoate + L-alanine; Xref=Rhea:RHEA:77307, ChEBI:CHEBI:15361, ChEBI:CHEBI:57972, ChEBI:CHEBI:197308, ChEBI:CHEBI:197310; Evidence={ECO:0000256|ARBA:ARBA00043798}; CATALYTIC ACTIVITY: Reaction=N(omega),N(omega)-dimethyl-L-arginine + oxaloacetate = 5-(3,3-dimethylguanidino)-2-oxopentanoate + L-aspartate; Xref=Rhea:RHEA:77343, ChEBI:CHEBI:16452, ChEBI:CHEBI:29991, ChEBI:CHEBI:58326, ChEBI:CHEBI:197301; Evidence={ECO:0000256|ARBA:ARBA00043749}; CATALYTIC ACTIVITY: Reaction=N(omega),N(omega)-dimethyl-L-arginine + pyruvate = 5-(3,3-dimethylguanidino)-2-oxopentanoate + L-alanine; Xref=Rhea:RHEA:77303, ChEBI:CHEBI:15361, ChEBI:CHEBI:57972, ChEBI:CHEBI:58326, ChEBI:CHEBI:197301; Evidence={ECO:0000256|ARBA:ARBA00043669}; CATALYTIC ACTIVITY: Reaction=N(omega)-methyl-L-arginine + pyruvate = 5-(3-methylguanidino)-2-oxopentanoate + L-alanine; Xref=Rhea:RHEA:77319, ChEBI:CHEBI:15361, ChEBI:CHEBI:57972, ChEBI:CHEBI:114953, ChEBI:CHEBI:197314; Evidence={ECO:0000256|ARBA:ARBA00043758}; CATALYTIC ACTIVITY: Reaction=glyoxylate + L-alanine = glycine + pyruvate; Xref=Rhea:RHEA:24248, ChEBI:CHEBI:15361, ChEBI:CHEBI:36655, ChEBI:CHEBI:57305, ChEBI:CHEBI:57972; EC=2.6.1.44; Evidence={ECO:0000256|ARBA:ARBA00033660}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24249; Evidence={ECO:0000256|ARBA:ARBA00033660}; CATALYTIC ACTIVITY: Reaction=glyoxylate + L-ornithine = 5-amino-2-oxopentanoate + glycine; Xref=Rhea:RHEA:77331, ChEBI:CHEBI:36655, ChEBI:CHEBI:46911, ChEBI:CHEBI:57305, ChEBI:CHEBI:58802; Evidence={ECO:0000256|ARBA:ARBA00043808}; CATALYTIC ACTIVITY: Reaction=glyoxylate + N(omega),N('omega)-dimethyl-L-arginine = 5-(3,3'-dimethylguanidino)-2-oxopentanoate + glycine; Xref=Rhea:RHEA:77315, ChEBI:CHEBI:36655, ChEBI:CHEBI:57305, ChEBI:CHEBI:197308, ChEBI:CHEBI:197310; Evidence={ECO:0000256|ARBA:ARBA00043659}; CATALYTIC ACTIVITY: Reaction=glyoxylate + N(omega),N(omega)-dimethyl-L-arginine = 5-(3,3-dimethylguanidino)-2-oxopentanoate + glycine; Xref=Rhea:RHEA:77311, ChEBI:CHEBI:36655, ChEBI:CHEBI:57305, ChEBI:CHEBI:58326, ChEBI:CHEBI:197301; Evidence={ECO:0000256|ARBA:ARBA00043815}; CATALYTIC ACTIVITY: Reaction=glyoxylate + N(omega)-methyl-L-arginine = 5-(3-methylguanidino)-2-oxopentanoate + glycine; Xref=Rhea:RHEA:77323, ChEBI:CHEBI:36655, ChEBI:CHEBI:57305, ChEBI:CHEBI:114953, ChEBI:CHEBI:197314; Evidence={ECO:0000256|ARBA:ARBA00043652};

COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000256|ARBA:ARBA00001933};

Pyridoxal phosphate;Reference proteome;Signal

glycine biosynthetic process, by transamination of glyoxylate [GO:0019265]; glyoxylate catabolic process [GO:0009436]; L-alanine catabolic process, by transamination [GO:0019481]; positive regulation of nitric oxide biosynthetic process [GO:0045429]

mitochondrion [GO:0005739]

(R)-3-amino-2-methylpropionate-pyruvate transaminase activity [GO:0047305]; alanine-glyoxylate transaminase activity [GO:0008453]; pyridoxal phosphate binding [GO:0030170]

IPR005814;IPR049704;IPR015424;IPR015421;IPR015422;

3.90.1150.10;3.40.640.10;

A0A1D5QHM1

MDSKHQRVKLNDGHFMPVLGFGTYAPPEVPRSKALEVTKLAIEAGFRHIDSAHLYNNEEQVGLAIRSKIADGTVKREDIFYTSKLWSTFHRPELVRPALENSLKKAQLDYVDLYLIHSPVSLKPGEELSPTDENGKLIFDIVDLCTTWEAMEKCKDAGLAKSIGVSNFNHRQLEMILNKPGLKYKPVCNQVECHPYFNQSKLLDFCKSKDIVLVAYSALGSQRDKRWVDQNSPVLLEDPVLCALAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRENVQVFEFQLTSEDMKAIDGLNRNLRYFNSDSLASHPNYPYSDEY

Macaca mulatta (Rhesus macaque)

CATALYTIC ACTIVITY: Reaction=(20S)-hydroxypregn-4-en-3-one + NAD(+) = H(+) + NADH + progesterone; Xref=Rhea:RHEA:42108, ChEBI:CHEBI:15378, ChEBI:CHEBI:17026, ChEBI:CHEBI:28453, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence={ECO:0000256|ARBA:ARBA00023933}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42109; Evidence={ECO:0000256|ARBA:ARBA00023933}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:42110; Evidence={ECO:0000256|ARBA:ARBA00023933}; CATALYTIC ACTIVITY: Reaction=(20S)-hydroxypregn-4-en-3-one + NADP(+) = H(+) + NADPH + progesterone; Xref=Rhea:RHEA:42112, ChEBI:CHEBI:15378, ChEBI:CHEBI:17026, ChEBI:CHEBI:28453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; Evidence={ECO:0000256|ARBA:ARBA00023980}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42113; Evidence={ECO:0000256|ARBA:ARBA00023980}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:42114; Evidence={ECO:0000256|ARBA:ARBA00023980}; CATALYTIC ACTIVITY: Reaction=17beta-estradiol + NAD(+) = estrone + H(+) + NADH; Xref=Rhea:RHEA:24612, ChEBI:CHEBI:15378, ChEBI:CHEBI:16469, ChEBI:CHEBI:17263, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.62; Evidence={ECO:0000256|ARBA:ARBA00023927}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24613; Evidence={ECO:0000256|ARBA:ARBA00023927}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:24614; Evidence={ECO:0000256|ARBA:ARBA00023927}; CATALYTIC ACTIVITY: Reaction=17beta-estradiol + NADP(+) = estrone + H(+) + NADPH; Xref=Rhea:RHEA:24616, ChEBI:CHEBI:15378, ChEBI:CHEBI:16469, ChEBI:CHEBI:17263, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.62; Evidence={ECO:0000256|ARBA:ARBA00023984}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24617; Evidence={ECO:0000256|ARBA:ARBA00023984}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:24618; Evidence={ECO:0000256|ARBA:ARBA00023984}; CATALYTIC ACTIVITY: Reaction=a 3alpha-hydroxysteroid + NAD(+) = a 3-oxosteroid + H(+) + NADH; Xref=Rhea:RHEA:34779, ChEBI:CHEBI:15378, ChEBI:CHEBI:36835, ChEBI:CHEBI:47788, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.357; Evidence={ECO:0000256|ARBA:ARBA00023972}; CATALYTIC ACTIVITY: Reaction=a 3alpha-hydroxysteroid + NADP(+) = a 3-oxosteroid + H(+) + NADPH; Xref=Rhea:RHEA:34783, ChEBI:CHEBI:15378, ChEBI:CHEBI:36835, ChEBI:CHEBI:47788, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.357; Evidence={ECO:0000256|ARBA:ARBA00023921};

PATHWAY: Steroid metabolism. {ECO:0000256|ARBA:ARBA00004854}.

NADP;Reference proteome

cellular response to calcium ion [GO:0071277]; cellular response to corticosteroid stimulus [GO:0071384]; cellular response to jasmonic acid stimulus [GO:0071395]; cellular response to prostaglandin D stimulus [GO:0071799]; cellular response to starvation [GO:0009267]; daunorubicin metabolic process [GO:0044597]; doxorubicin metabolic process [GO:0044598]; farnesol catabolic process [GO:0016488]; G protein-coupled receptor signaling pathway [GO:0007186]; keratinocyte differentiation [GO:0030216]; male gonad development [GO:0008584]; negative regulation of retinoic acid biosynthetic process [GO:1900053]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of endothelial cell apoptotic process [GO:2000353]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of reactive oxygen species metabolic process [GO:2000379]; progesterone metabolic process [GO:0042448]; prostaglandin metabolic process [GO:0006693]; regulation of retinoic acid receptor signaling pathway [GO:0048385]; regulation of testosterone biosynthetic process [GO:2000224]; response to nutrient [GO:0007584]; retinal metabolic process [GO:0042574]; testosterone biosynthetic process [GO:0061370]

cytosol [GO:0005829]; nucleus [GO:0005634]

15-hydroxyprostaglandin-D dehydrogenase (NADP+) activity [GO:0047020]; alditol:NADP+ 1-oxidoreductase activity [GO:0004032]; androsterone dehydrogenase activity [GO:0047023]; bile acid binding [GO:0032052]; delta4-3-oxosteroid 5beta-reductase activity [GO:0047787]; dihydrotestosterone 17-beta-dehydrogenase activity [GO:0035410]; estradiol 17-beta-dehydrogenase [NAD(P)] activity [GO:0004303]; geranylgeranyl reductase activity [GO:0045550]; ketoreductase activity [GO:0045703]; ketosteroid monooxygenase activity [GO:0047086]; NAD-retinol dehydrogenase activity [GO:0004745]; oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor [GO:0016655]; phenanthrene 9,10-monooxygenase activity [GO:0018636]; retinal dehydrogenase activity [GO:0001758]

IPR020471;IPR044482;IPR018170;IPR023210;IPR036812;

3.20.20.100;

A0A1D5QK37

MGWLEELNWQLHIFLLILLSMHTRANFLDNMLLRSAGKLNVGTKKEDGESTAPTPRPKILRCKCHHHCPEDSVNNICSTDGYCFTMIEEDDSGMPVVTSGCLGLEGSDFQCRDTPIPHQRRSIECCTERNECNKDLHPTLPPLKNRDFVDGPIHHKALLISVTVCSLLLVLIILFCYFRYKRQETRPRYSIGLEQDETYIPPGESLRDLIEQSQSSGSGSGLPLLVQRTIAKQIQMVKQIGKGRYGEVWMGKWRGEKVAVKVFFTTEEASWFRETEIYQTVLMRHENILGFIAADIKGTGSWTQLYLITDYHENGSLYDYLKSTTLDTKSMLKLAYSSVSGLCHLHTEIFSTQGKPAIAHRDLKSKNILVKKNGTCCIADLGLAVKFISDTNEVDIPPNTRVGTKRYMPPEVLDESLNRNHFQSYIMADMYSFGLILWEVARRCVSGGIVEEYQLPYHDLVPSDPSYEDMREVVCIKKLRPSFPNRWSSDECLRQMGKLMTECWAHNPASRLTALRVKKTLAKMSESQDIKL

Macaca mulatta (Rhesus macaque)

2.7.11.30

CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[receptor-protein] = ADP + H(+) + O-phospho-L-threonyl-[receptor-protein]; Xref=Rhea:RHEA:44880, Rhea:RHEA-COMP:11024, Rhea:RHEA-COMP:11025, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.30; Evidence={ECO:0000256|RuleBase:RU361271};

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|RuleBase:RU361271}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|RuleBase:RU361271};

ATP-binding;Kinase;Magnesium;Manganese;Membrane;Metal-binding;Nucleotide-binding;Receptor;Reference proteome;Serine/threonine-protein kinase;Signal;Transferase;Transmembrane;Transmembrane helix

BMP signaling pathway [GO:0030509]; bone development [GO:0060348]; cartilage condensation [GO:0001502]; cellular response to growth factor stimulus [GO:0071363]; central nervous system neuron differentiation [GO:0021953]; chondrocyte differentiation [GO:0002062]; dorsal/ventral pattern formation [GO:0009953]; inflammatory response [GO:0006954]; osteoblast differentiation [GO:0001649]; ovarian cumulus expansion [GO:0001550]; phosphorylation [GO:0016310]; positive regulation of bone mineralization [GO:0030501]; positive regulation of extrinsic apoptotic signaling pathway via death domain receptors [GO:1902043]; positive regulation of gene expression [GO:0010628]; positive regulation of osteoblast differentiation [GO:0045669]; positive regulation of transcription by RNA polymerase II [GO:0045944]; retina development in camera-type eye [GO:0060041]; retinal ganglion cell axon guidance [GO:0031290]

plasma membrane [GO:0005886]; plasma membrane signaling receptor complex [GO:0098802]; receptor complex [GO:0043235]

ATP binding [GO:0005524]; BMP binding [GO:0036122]; BMP receptor activity [GO:0098821]; metal ion binding [GO:0046872]; SMAD binding [GO:0046332]; transforming growth factor beta receptor activity, type I [GO:0005025]

SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU361271}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU361271}.

IPR000472;IPR003605;IPR011009;IPR000719;IPR017441;IPR001245;IPR008271;IPR045860;IPR000333;

2.10.60.10;1.10.510.10;

A0A1D5QL11

MINCDYLCCHKKRQEQRWHRRTMAGIFYFALFSCLFGICDAVTGSRVYPANEVTLLDSRSVQGELGWIASPLEGGWEEVSIMDEKNTPIRTYQVCNVMEPSQNNWLRTDWITREGAQRVYIEIKFTLRDCNSLPGVMGTCKETFNLYYYESDNDKERFIRENQFVKIDTIAADESFTQVDIGDRIMKLNTEIRDVGPLSKKGFYLAFQDVGACIALVSVRVFYKKCPLTVRNLAQFPDTITGADTSSLVEVRGSCVNNSEEKDVPKMYCGADGEWLVPIGNCLCNAGHEERSGECQACKIGYYKALSTDATCAKCPPHSYSVWEGATSCTCDRGFFRADNDAASMPCTRPPSAPLNLISNVNETSVNLEWSSPQNTGGRQDISYNVVCKKCGAGDPSKCRPCGSGVHYTPQQNGLKTTKVSITDLLAHTNYTFEIWAVNGVSKYNPSPDQSVSVTVTTNQAAPSSIVLVQAKEVTRYSVALAWLEPDRPNGVILEYEVKYYEKDQNERSYRIVRTAARNTDIKGLNPLTSYVFHVRARTAAGYGDFSEPLEVTTNTVPSRIIGDGANSTVLLVSVSGSVVLVVILIAAFVISRRRSKYSKAKQEADEEKHLNQGVRTYVDPFTYEDPNQAVREFAKEIDASCIKIEKVIGVGEFGEVCSGRLKVPGKREICVAIKTLKAGYTDKQRRDFLSEASIMGQFDHPNIIHLEGVVTKCKPVMIITEYMENGSLDAFLRKNDGRFTVIQLVGMLRGIGSGMKYLSDMSYVHRDLAARNILVNSNLVCKVSDFGMSRVLEDDPEAAYTTRGGKIPIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSYGERPYWDMSNQDVIKAIEEGYRLPPPMDCPIALHQLMLDCWQKERSDRPKFGQIVNMLDKLIRNPNSLKRTGTESSRPNTALLDPSSPEFSAVVSVGDWLQAIKMDRYKDNFTAAGYTTLEAVVHVNQEDLARIGITAITHQNKILSSVQAMRTQMQQMHGRMVPV

Macaca mulatta (Rhesus macaque)

2.7.10.1

CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence={ECO:0000256|ARBA:ARBA00001171};

ATP-binding;Cell membrane;Developmental protein;Disulfide bond;Endosome;Kinase;Membrane;Nucleotide-binding;Phosphoprotein;Receptor;Reference proteome;Signal;Transferase;Transmembrane;Transmembrane helix;Tyrosine-protein kinase

adherens junction organization [GO:0034332]; adult walking behavior [GO:0007628]; axon guidance [GO:0007411]; cellular response to amyloid-beta [GO:1904646]; cochlea development [GO:0090102]; corticospinal tract morphogenesis [GO:0021957]; ephrin receptor signaling pathway [GO:0048013]; fasciculation of motor neuron axon [GO:0097156]; fasciculation of sensory neuron axon [GO:0097155]; motor neuron axon guidance [GO:0008045]; negative regulation of axon regeneration [GO:0048681]; negative regulation of cell adhesion [GO:0007162]; negative regulation of cell migration [GO:0030336]; negative regulation of cellular response to hypoxia [GO:1900038]; negative regulation of epithelial to mesenchymal transition [GO:0010719]; negative regulation of ERK1 and ERK2 cascade [GO:0070373]; negative regulation of long-term synaptic potentiation [GO:1900272]; negative regulation of proteolysis involved in protein catabolic process [GO:1903051]; nephric duct morphogenesis [GO:0072178]; positive regulation of amyloid-beta formation [GO:1902004]; positive regulation of cell adhesion [GO:0045785]; positive regulation of cell migration [GO:0030335]; positive regulation of cell population proliferation [GO:0008284]; protein stabilization [GO:0050821]; regulation of astrocyte differentiation [GO:0048710]; regulation of axonogenesis [GO:0050770]; regulation of dendritic spine morphogenesis [GO:0061001]; regulation of modification of synaptic structure [GO:1905244]; synapse pruning [GO:0098883]

axon [GO:0030424]; dendrite [GO:0030425]; early endosome membrane [GO:0031901]; glutamatergic synapse [GO:0098978]; postsynaptic membrane [GO:0045211]; presynaptic membrane [GO:0042734]; Schaffer collateral - CA1 synapse [GO:0098685]

ATP binding [GO:0005524]; DH domain binding [GO:0097161]; GPI-linked ephrin receptor activity [GO:0005004]; identical protein binding [GO:0042802]; PH domain binding [GO:0042731]; protein tyrosine kinase binding [GO:1990782]; transmembrane-ephrin receptor activity [GO:0005005]

SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}. Early endosome {ECO:0000256|ARBA:ARBA00004412}. Endosome {ECO:0000256|ARBA:ARBA00004177}. Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.

IPR027936;IPR034270;IPR030602;IPR001090;IPR003961;IPR036116;IPR008979;IPR013783;IPR011009;IPR000719;IPR017441;IPR001660;IPR013761;IPR001245;IPR011641;IPR008266;IPR020635;IPR016257;IPR001426;

2.60.40.1770;2.60.120.260;2.60.40.10;1.10.150.50;1.10.510.10;2.10.50.10;

A0A1D5QL55

MASPSCLWLLAVALLPWTCAARALHHLDPPAPLPLVIWHGMGDSCCNPLSMGAIKMVEKKIPGIYVLSLEIGKTLMEGRGNSFFLNVNSQVTTVCQTLAKDKLQQGYNAMGFSQGGQFLRAVAQRCPSPPMINLISVGGQHQGVFGLPRCPGESSHICDFIRKTLNAGAYSKVVQERLVQAEYWHDPIKEDVYRNHSIFLADINQERGINESYKKNLMALKKFVMVKFLNDSIVDPVDSEWFGFYRSGQAKETIPLQETSLYTQDRLGLKEMDNAGQLVFLATEGDHLQLSEEWFYAHIIPFLG

Macaca mulatta (Rhesus macaque)

3.1.2.22

CATALYTIC ACTIVITY: Reaction=H2O + S-hexadecanoyl-L-cysteinyl-[protein] = H(+) + hexadecanoate + L-cysteinyl-[protein]; Xref=Rhea:RHEA:19233, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:74151; EC=3.1.2.22; Evidence={ECO:0000256|ARBA:ARBA00000072};

Disulfide bond;Hydrolase;Reference proteome;Signal

adult locomotory behavior [GO:0008344]; associative learning [GO:0008306]; brain development [GO:0007420]; grooming behavior [GO:0007625]; lipid catabolic process [GO:0016042]; lysosomal lumen acidification [GO:0007042]; membrane raft organization [GO:0031579]; negative regulation of cell growth [GO:0030308]; negative regulation of neuron apoptotic process [GO:0043524]; nervous system development [GO:0007399]; neurotransmitter secretion [GO:0007269]; pinocytosis [GO:0006907]; positive regulation of pinocytosis [GO:0048549]; positive regulation of receptor-mediated endocytosis [GO:0048260]; protein catabolic process [GO:0030163]; protein transport [GO:0015031]; receptor-mediated endocytosis [GO:0006898]; visual perception [GO:0007601]

axon [GO:0030424]; dendrite [GO:0030425]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; lysosome [GO:0005764]; membrane raft [GO:0045121]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]; synaptic vesicle [GO:0008021]

long-chain fatty acyl-CoA hydrolase activity [GO:0052816]; lysophosphatidic acid binding [GO:0035727]; palmitoyl-(protein) hydrolase activity [GO:0008474]; sulfatide binding [GO:0120146]

IPR029058;IPR002472;

3.40.50.1820;

A0A1D5QML3

MCLLAHCQVLATRVLTWPSFVLTRIVLPGWQRDPSGTMSALGVSVALLVWVAVLLLVSIWRQVHSSWNLPPGPFPLPIIGNLFQLEWKNLPKSFTRLAQRFGPVFTLYVGSRRVVVVHGYKAVREVLLDHKDEFSGRGDIPAFHAHRDRGIIFNNGPTWKDIRRFSLTTLRNYGMGKQGNESRIQREAHFLLEALRKTQGQPFDPTFLIGCAPCNVIADILFRKHFDYNDEKFLRLMYLFNENFQLLSTPWLQLYNNFPSLLHYLPGSHRKVMKNVAEIKEYVSERVKEHLQSLDPNCPRDLTDCLLVEMEKEKHSAERLYTMDGITVTVADLFFAGTETTSTTLRYGLLILMKYPEIEEKLHEEIDRVIGPSRIPAIKDRQEMPYMDAVVHEIQRFITLVPSNLPHEATRDTIFRGYIIPKGTVIVPTLDSVLYDNQEFPDPEKFKPEHFLDESGKFKYSDYFKPFSAGKRVCAGEGLARMELFLLLSAILQHFNLKPLVDPKDIDISPVNIGFGCIPPRFKLCVIPRS

Macaca mulatta (Rhesus macaque)

FUNCTION: A cytochrome P450 monooxygenase involved in the metabolism of fatty acids. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase). Catalyzes the hydroxylation of carbon-hydrogen bonds. Hydroxylates fatty acids specifically at the omega-1 position displaying the highest catalytic activity for saturated fatty acids. May be involved in the oxidative metabolism of xenobiotics. {ECO:0000256|RuleBase:RU368050}.

1.14.13.n7; 1.14.14.1

CATALYTIC ACTIVITY: Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 + reduced [NADPH--hemoprotein reductase] = 21-hydroxy-(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:50088, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:77016, ChEBI:CHEBI:132025; Evidence={ECO:0000256|ARBA:ARBA00000615, ECO:0000256|RuleBase:RU368050}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50089; Evidence={ECO:0000256|ARBA:ARBA00000615, ECO:0000256|RuleBase:RU368050}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z)-eicosatrienoate + O2 + reduced [NADPH--hemoprotein reductase] = 19-hydroxy-(5Z,8Z,11Z)-eicosatrienoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:50076, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:78043, ChEBI:CHEBI:132024; Evidence={ECO:0000256|ARBA:ARBA00001354, ECO:0000256|RuleBase:RU368050}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50077; Evidence={ECO:0000256|ARBA:ARBA00001354, ECO:0000256|RuleBase:RU368050}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 + reduced [NADPH--hemoprotein reductase] = 19-hydroxy-(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:39787, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:58562, ChEBI:CHEBI:76636; Evidence={ECO:0000256|ARBA:ARBA00000326, ECO:0000256|RuleBase:RU368050}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39788; Evidence={ECO:0000256|ARBA:ARBA00000326, ECO:0000256|RuleBase:RU368050}; CATALYTIC ACTIVITY: Reaction=O2 + reduced [NADPH--hemoprotein reductase] + tetradecanoate = 13-hydroxytetradecanoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:50096, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30807, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:132031; Evidence={ECO:0000256|ARBA:ARBA00000338, ECO:0000256|RuleBase:RU368050}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50097; Evidence={ECO:0000256|ARBA:ARBA00000338, ECO:0000256|RuleBase:RU368050}; CATALYTIC ACTIVITY: Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30879, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:142491; EC=1.14.14.1; Evidence={ECO:0000256|ARBA:ARBA00000089}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17150; Evidence={ECO:0000256|ARBA:ARBA00000089}; CATALYTIC ACTIVITY: Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30879, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:142491; Evidence={ECO:0000256|RuleBase:RU368050}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17150; Evidence={ECO:0000256|RuleBase:RU368050}; CATALYTIC ACTIVITY: Reaction=dodecanoate + O2 + reduced [NADPH--hemoprotein reductase] = 11-hydroxydodecanoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:39751, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:18262, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:76628; Evidence={ECO:0000256|ARBA:ARBA00001427, ECO:0000256|RuleBase:RU368050}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39752; Evidence={ECO:0000256|ARBA:ARBA00001427, ECO:0000256|RuleBase:RU368050};

COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000256|ARBA:ARBA00001971, ECO:0000256|PIRSR:PIRSR602401-1, ECO:0000256|RuleBase:RU368050};

PATHWAY: Lipid metabolism; fatty acid metabolism. {ECO:0000256|ARBA:ARBA00004872, ECO:0000256|RuleBase:RU368050}.

Endoplasmic reticulum;Fatty acid metabolism;Heme;Iron;Lipid metabolism;Membrane;Metal-binding;Microsome;Mitochondrion;Mitochondrion inner membrane;Monooxygenase;NADP;Oxidoreductase;Reference proteome;Transmembrane;Transmembrane helix

epoxygenase P450 pathway [GO:0019373]; xenobiotic metabolic process [GO:0006805]

cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; intracellular membrane-bounded organelle [GO:0043231]; mitochondrial inner membrane [GO:0005743]

arachidonic acid epoxygenase activity [GO:0008392]; aromatase activity [GO:0070330]; heme binding [GO:0020037]; Hsp70 protein binding [GO:0030544]; Hsp90 protein binding [GO:0051879]; iron ion binding [GO:0005506]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen [GO:0016712]

SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000256|RuleBase:RU368050}; Peripheral membrane protein {ECO:0000256|RuleBase:RU368050}. Microsome membrane {ECO:0000256|ARBA:ARBA00004174, ECO:0000256|RuleBase:RU368050}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004174, ECO:0000256|RuleBase:RU368050}. Mitochondrion inner membrane {ECO:0000256|RuleBase:RU368050}; Peripheral membrane protein {ECO:0000256|RuleBase:RU368050}. Membrane {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.

IPR001128;IPR017972;IPR002401;IPR008070;IPR036396;

1.10.630.10;

A0A1D5QNQ2

MAALVLEDGSVLRGQPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNYGIPPDEMDEFGLCKWFESSGIHVAGLVVGECCPTPSHWSATCTLHEWLQQHGIPGLQGVDTRELTKKLREQGSLLGKLVQNGTEPSSLPFLDPNARPLVPEVSIKTPRVFNTGGAPRILALDCGLKYNQIRCLCRRGAEVTVVPWDHALDSQEYEGLFLSNGPGDPASYPSVVSMLSCVLSEPNPRPVFGICLGHQLLALAIGAKTYKMRYGNRGHNQPCLLVGSGRCFLTSQNHGFAVETDSLPADWAPLFTNANDGSNEGIVHNSLPFFSVQFHPEHQAGPSDMELLFDIFLETVKEATAGNPGGQTVRERLTERLCSPGIPTPSSGLPPPRKVLILGSGGLSIGQAGEFDYSGSQAIKALKEENIQTLLINPNIATVQTSQGLADKVYFLPITPHYVTQVIRNERPDGVLLTFGGQTALNCGVELTKAGVLARYGVRVLGTPVETIELTEDRRAFAARMAEIGEHVAPSEAANSLEQAQAAAERLGYPVLVRSAFALGGLGSGFASNREELSGLVASAFAHTSQVLVDKSLKGWKEIEYEVVRDAYGNCVTVCNMENLDPLGIHTGESIVVAPSQTLNDREYQLLRQTAIKVTQHLGIVGECNVQYALNPESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLALGIPLPELRNSVTGGTAAFEPSLDYCVVKIPRWDLSKFLRVSTKIGSCMKSVGEVMGIGRSFEEAFQKALRMVDENCVGFDHTVKPVSDVELETPTDKRIFVVAAALWSGYSVDRLYELTRIDRWFLHRMKRIITHAQLLEQHRGQPLPPDLLQQAKCLGFSDKQIALAVLSTELAVRKLRQELGICPAVKQIDTVAAEWPAQTNYLYLTYWGTTHDLTFRTPHVLVLGSGVYRIGSSVEFDWCAVGCIQQLRKMGYKTIMVNYNPETVSTDYDMCDRLYFDEISFEVVMDIYELENPEGVILSMGGQLPNNMAMALHRQQCRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCQTVGYPCVVRPSYVLSGAAMNVAYTDGDLERFLSSAAAVSKEHPVVISKFIQEAKEIDVDAVASDGVVAAIAISEHVENAGVHSGDATLVTPPQDITAKTLERIKAIVHAVGQELQVTGPFNLQLIAKDDQLKVIECNVRVSRSFPFVSKTLGVDLVALATRVIMGEEVEPVGLMTGSGVVGVKVPQFSFSRLAGADVVLGVEMTSTGEVAGFGESRCEAYLKAMLSTGFKIPKKNILLTIGSYKNKSELLPTVRLLESLGYSLYASLGTADFYTEHGVKVTAVDWHFEEAVDGECPPQRSILEQLAEKNFELVINLSMRGAGGRRLSSFVTKGYRTRRLAADFSVPLIIDIKCTKLFVEALGQIGPAPPLKVHVDCMTSQKLVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMPNTRPPIIDAPALALAQKLAEASARCDFALFLGASSENAGMLGTVAGSAAGLKLYLNETFSELRLDSVVQWMEHFETWPSHLPIVAHAEQQTLAAVLMVAQLTQRSVHICHVARKEEVRVYQSSCCLCCFPSNTKGQGSPWGQETAGGESRASGRRVSSQRPCRSTSSFFKQRCWPMGLCVGQGIWMVPLLNLPIVPQILLIKAAKARGLPVTCEVAPHHLFLSHDDLERLGPGKGEVRPELGSRQDVEALWENMAVIDCFASDHAPHTLEEKCGSRPPPGFPGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLPPQEDTYVEVDLEHEWTIPSHMPFSKAHWTPFEGQKVKGTIRRVVLRGEVAYIDGQVLVPPGYGQDVRKWPQGAVPQLPPSAPTTSEMTTTPERPRRGIPGLPDGRFHLPPRIHRASDPGLPAEEPKEKSSRKVAEPELMGTPDGTCYPPPPVPRQASPQNLGTPGLLHPQTSPLLHSLVGQHILSVQQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEATSSVQKGESLADSVQTMSCYADVVVLRHPQPGAVELAAKHCRRPVINAGDGVGEHPTQALLDIFTIREELGTVNGMTITMVGDLKHGRTVHSLACLLTQYRVSLRYVAPPSLRMPPTVRAFVASRGTKQEEFESIEEALPDTDVLYMTRIQKERFGSTQEYEACFGQFILTPHIMTRAKKKMVVMHPMPRVNEISVEVDSDPRAAYFRQAENGMYIRMALLATVLGRF

Macaca mulatta (Rhesus macaque)

CATALYTIC ACTIVITY: Reaction=(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate; Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30864, ChEBI:CHEBI:32814; EC=3.5.2.3; Evidence={ECO:0000256|ARBA:ARBA00000462}; CATALYTIC ACTIVITY: Reaction=2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate; Xref=Rhea:RHEA:18633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.5.5; Evidence={ECO:0000256|ARBA:ARBA00001777}; CATALYTIC ACTIVITY: Reaction=2 ATP + hydrogencarbonate + NH4(+) = 2 ADP + carbamoyl phosphate + 2 H(+) + phosphate; Xref=Rhea:RHEA:18029, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:28938, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:456216; EC=6.3.4.16; Evidence={ECO:0000256|ARBA:ARBA00043687}; CATALYTIC ACTIVITY: Reaction=H2O + L-glutamine = L-glutamate + NH4(+); Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; EC=3.5.1.2; Evidence={ECO:0000256|ARBA:ARBA00001062}; CATALYTIC ACTIVITY: Reaction=carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-aspartate + phosphate; Xref=Rhea:RHEA:20013, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:32814, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228; EC=2.1.3.2; Evidence={ECO:0000256|ARBA:ARBA00001363};

COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|ARBA:ARBA00001947};

PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3. {ECO:0000256|ARBA:ARBA00004812}.; PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3. {ECO:0000256|ARBA:ARBA00004852}.; PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. {ECO:0000256|ARBA:ARBA00004880}.

ATP-binding;Glutamine amidotransferase;Hydrolase;Ligase;Metal-binding;Multifunctional enzyme;Nucleotide-binding;Pyrimidine biosynthesis;Reference proteome;Repeat;Transferase

'de novo' pyrimidine nucleobase biosynthetic process [GO:0006207]; 'de novo' UMP biosynthetic process [GO:0044205]; citrulline biosynthetic process [GO:0019240]; glutamine metabolic process [GO:0006541]; UDP biosynthetic process [GO:0006225]; UTP biosynthetic process [GO:0006228]

cytoplasm [GO:0005737]; cytosol [GO:0005829]; nuclear matrix [GO:0016363]

amino acid binding [GO:0016597]; aspartate carbamoyltransferase activity [GO:0004070]; ATP binding [GO:0005524]; carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity [GO:0004088]; dihydroorotase activity [GO:0004151]; enzyme binding [GO:0019899]; identical protein binding [GO:0042802]; zinc ion binding [GO:0008270]

IPR006680;IPR006132;IPR006130;IPR036901;IPR002082;IPR006131;IPR011761;IPR013815;IPR006275;IPR005480;IPR036897;IPR006274;IPR002474;IPR036480;IPR005479;IPR005483;IPR029062;IPR035686;IPR002195;IPR017926;IPR011059;IPR032466;IPR011607;IPR036914;IPR016185;

3.40.50.20;3.40.50.880;3.40.50.1370;3.30.1490.20;3.30.470.20;3.50.30.20;1.10.1030.10;3.20.20.140;3.40.50.1380;

A0A1D5QP34

MALRRLGAALLLLPLLAAVEETLMDSTTATAELGWMVHPPSGWEEVSGYDENMNTIRTYQVCNVFESSQNNWLRTKFIRRRGAHRIHVEMKFSVRDCSSIPSVPGSCKETFNLYYYEADFDSATKTFPNWMENPWVKVDTIAADESFSQVDLGGRVMKINTEVRSFGPVSRSGFYLAFQDYGGCMSLIAVRVFYRKCPRIIQNGAIFQETLSGAESTSLVAARGSCIANAEEVDVPIKLYCNGDGEWLVPIGRCMCKAGFEAVENGTVCRGCPSGTFKANQGDKACTHCPINSRTTSEGATNCVCRNGYYRADLDPLDMPCTTIPSAPQAVISSVNETSLMLEWTPPRDSGGREDLVYNIICKSCGSGRGACTRCGDNVQYAPRQLGLTEPRIYISDLLAHTQYTFEIQAVNGVTDQSPFSPQFASVNITTNQAAPSAVSIMHQVSRTVDSITLSWSQPDQPNGVILDYELQYYEKELSEYNATAIKSPTNTVTVQGLKAGAIYVFQVRARTVAGYGRYSGKMYFQTMTEAEYQTSIQEKLPLIIGSSAAGLVFLIAVVVIAIVCNRRGFERADSEYTDKLQHYTSGHMTPGMKIYIDPFTYEDPNEAVREFAKEIDISCVKIEQVIGAGEFGEVCSGHLKLPGKREIFVAIKTLKSGYTEKQRRDFLSEASIMGQFDHPNVIHLEGVVTKSTPVMIITEFMENGSLDSFLRQNDGQFTVIQLVGMLRGIAAGMKYLADMNYVHRDLAARNILVNSNLVCKVSDFGLSRFLEDDTSDPTYTSALGGKIPIRWTAPEAIQYRKFTSASDVWSYGIVMWEVMSYGERPYWDMTNQDVINAIEQDYRLPPPMDCPSALHQLMLDCWQKDRNHRPKFGQIVNTLDKMIRNPNSLKAMAPLSSGINLPLLDRTIPDYTSFNTVDEWLEAIKMGQYKESFANAGFTSFDVVSQMMMEDILRVGVTLAGHQKKILNSIQVMRAQMNQIQSVEGQPPARRPRATGRTKRHQPRDITMKTCNSSDGNKKGMGKKKTDPGRGREIQGIFFKEDSHKESNDCSCGGIKKGLGDSCDVSNRTPKAVSLQLPLGR

Macaca mulatta (Rhesus macaque)

2.7.10.1

CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence={ECO:0000256|ARBA:ARBA00001171};

ATP-binding;Developmental protein;Disulfide bond;Kinase;Membrane;Nucleotide-binding;Phosphoprotein;Receptor;Reference proteome;Signal;Transferase;Transmembrane;Transmembrane helix;Tyrosine-protein kinase

angiogenesis [GO:0001525]; axon guidance [GO:0007411]; axonal fasciculation [GO:0007413]; B cell activation [GO:0042113]; camera-type eye morphogenesis [GO:0048593]; central nervous system projection neuron axonogenesis [GO:0021952]; commissural neuron axon guidance [GO:0071679]; corpus callosum development [GO:0022038]; dendritic spine morphogenesis [GO:0060997]; ephrin receptor signaling pathway [GO:0048013]; inner ear morphogenesis [GO:0042472]; learning [GO:0007612]; negative regulation of axonogenesis [GO:0050771]; negative regulation of cell adhesion [GO:0007162]; negative regulation of ERK1 and ERK2 cascade [GO:0070373]; negative regulation of protein phosphorylation [GO:0001933]; negative regulation of Ras protein signal transduction [GO:0046580]; neuron projection retraction [GO:0106028]; optic nerve morphogenesis [GO:0021631]; phosphorylation [GO:0016310]; positive regulation of B cell proliferation [GO:0030890]; positive regulation of cell migration [GO:0030335]; positive regulation of immunoglobulin production [GO:0002639]; positive regulation of long-term neuronal synaptic plasticity [GO:0048170]; positive regulation of long-term synaptic potentiation [GO:1900273]; positive regulation of synapse assembly [GO:0051965]; positive regulation of synaptic plasticity [GO:0031915]; positive regulation of tumor necrosis factor production [GO:0032760]; regulation of autophagosome assembly [GO:2000785]; regulation of blood coagulation [GO:0030193]; retinal ganglion cell axon guidance [GO:0031290]; roof of mouth development [GO:0060021]; trans-synaptic signaling by trans-synaptic complex, modulating synaptic transmission [GO:0099557]; urogenital system development [GO:0001655]

axon [GO:0030424]; dendrite [GO:0030425]; glutamatergic synapse [GO:0098978]; hippocampal mossy fiber to CA3 synapse [GO:0098686]; neuronal cell body [GO:0043025]; nucleoplasm [GO:0005654]; postsynaptic membrane [GO:0045211]; presynaptic membrane [GO:0042734]

amyloid-beta binding [GO:0001540]; ATP binding [GO:0005524]; axon guidance receptor activity [GO:0008046]; identical protein binding [GO:0042802]; protein-containing complex binding [GO:0044877]; signaling receptor binding [GO:0005102]; transmembrane-ephrin receptor activity [GO:0005005]

SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}. Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.

IPR027936;IPR034238;IPR001090;IPR003961;IPR036116;IPR008979;IPR009030;IPR013783;IPR011009;IPR000719;IPR017441;IPR001660;IPR013761;IPR001245;IPR011641;IPR008266;IPR020635;IPR016257;IPR001426;

2.60.40.1770;2.60.120.260;2.60.40.10;1.10.150.50;1.10.510.10;2.10.50.10;

A0A1D5QSM3

MSTERDSETTFDEDSQPNDEVVPYSDDETEDELDDQGSTVEPEQNRVNREAEENQEPFRKECTWQVKANDRKYHGQPHFMNTKFFCIKKSKYANNAIKTYKYNALTFIPMNLFEQFKRSANLYFLVLLILQAIPQISTLAWYTTLVPLLLVLGVTAIKDLVDDVARHKMDKEINNRTCEVIKDGRFKVAKWKDIQVGDVIRLKKNDFVPADILLLSSSEPNSLCYVETAELDGETNLKFKMSLEITDQYLQREDTLATFDGLVECEEPNNRLDKFTGTLFWRNTSFPLDADKILLRGCVIRNTDFCHGLVIFAGADTKIMKNSGKTRFKRTKIDYLMNYMVYTIFVVLSLLSAGLAIGHAYWEAQVGNYSWYLYDGEDFTPSYRGFLNFWGYIIVLNTMVPISLYVSVEVIRLGQSHFINWDLQMYYAEKDTPAKARTTTLNEQLGQIHYIFSDKTGTLTQNIMTFKKCCINGQIYGDHRDASQHNHNKIEQVDFSWNTYADGKLAFYDHYLIEQIQSGKEPEVRQFFFLLAVCHTVMVDRIDGQLNYQAASPDEGALVNAARNFGFAFLARTQNTITISELGTERTYNVLAILDFNSDRKRMSIIVRTPEGNIRLYCKGADTVIYERLHRMNPTKQETQDALDIFANETLRTLCLCYKEIEEKEFAQWNKKFMAASVASTNRDEALDKVYEEIEKDLILLGATAIEDKLQDGVPETISKLAKADIKIWVLTGDKKETAENIGFACELLTEDTTICYGEDINSLLHARMENQRNRGGVYAKFAPPVQERFFPPGGNRALIITGSWLNEILLEKKTKRSKILKLKFPRTEEERRMRTQSKRRLEAKKEQQQKNFVDLACECSAVICCRVTPKQKAMVVDLVKRYKKAITLAIGDGANDVNMIKTAHIGVGISGQEGMQAVMSSDYSFAQFRYLQRLLLVHGRWSYIRMCKFLRYFFYKNFAFTLVHFWYSFFNGYSAQTAYEDWFITLYNVLYSSLPVLLMGLLDQDVSDKLSLRFPGLYIVGQRDLLFNYKRFFVSLLHGVLTSMILFFIPLGAYLQTVGQDGEAPSDYQSFAVTIASALVITVNFQIGLDTSYWTFVNAFSIFGSIALYFGIMFDFHSAGIHVLFPSMFQFTGTASNALRQPYIWLTIILTVAVCLLPVVAIRFLSMTIWPSESDKIQKHRKRLKAEEQWQRRQQVFRRGVSSRRSAYAFSHQRGYADLISSGRSIRKKRSPLDAIVADGTAEYRRTGDS

Macaca mulatta (Rhesus macaque)

7.6.2.1

CATALYTIC ACTIVITY: Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate + phospholipidSide 2.; EC=7.6.2.1; Evidence={ECO:0000256|ARBA:ARBA00034036, ECO:0000256|RuleBase:RU362033};

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|ARBA:ARBA00001946};

ATP-binding;Lipid transport;Magnesium;Membrane;Metal-binding;Nucleotide-binding;Reference proteome;Translocase;Transmembrane;Transmembrane helix;Transport

apical protein localization [GO:0045176]; bile acid and bile salt transport [GO:0015721]; bile acid metabolic process [GO:0008206]; Golgi organization [GO:0007030]; inner ear receptor cell development [GO:0060119]; negative regulation of DNA-templated transcription [GO:0045892]; phospholipid translocation [GO:0045332]; regulation of chloride transport [GO:2001225]; regulation of microvillus assembly [GO:0032534]; regulation of plasma membrane organization [GO:1903729]; sensory perception of sound [GO:0007605]; vestibulocochlear nerve formation [GO:0021650]; xenobiotic transmembrane transport [GO:0006855]

apical plasma membrane [GO:0016324]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; nuclear body [GO:0016604]; phospholipid-translocating ATPase complex [GO:1990531]; plasma membrane [GO:0005886]; stereocilium [GO:0032420]; trans-Golgi network [GO:0005802]

aminophospholipid flippase activity [GO:0015247]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled intramembrane lipid transporter activity [GO:0140326]; cardiolipin binding [GO:1901612]; magnesium ion binding [GO:0000287]; phosphatidylcholine flippase activity [GO:0140345]

SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362033}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362033}.

IPR023299;IPR018303;IPR023298;IPR008250;IPR036412;IPR023214;IPR006539;IPR032631;IPR001757;IPR032630;IPR044492;

3.40.1110.10;2.70.150.10;3.40.50.1000;

A0A1D5QUB0

MRRRRRRDGFYPAPDFRDREAEDMAGVFDIDLDQPEDAGSEDELEEGGQLNESMDHGGVGPYELGMEHCEKFEISETSVNRGPEKIRPECFELLRVLGKGGYGKVFQVRKVTGANTGKIFAMKVLKKAMIVRNAKDTAHTKAERNILEEVKHPFIVDLIYAFQTGGKLYLILEYLSGGVSLFSPRMECRGVISAHRNFRLPGGELFMQLEREGIFMEDTACFYLAEISMALGHLHQKGIIYRDLKPENIMLNHQGHVKLTDFGLCKESIHDGTVTHTFCGTIEYMAPEILMRSGHNRAVDWWSLGALMYDMLTGAPPFTGENRKKTIDKILKCKLNLPPYLTQEARDLLKKLLKRNAASRLGAGPGDAGEVQAHPFFRHINWEELLARKVEPPFKPLLQSEEDVSQFDSKFTRQTPVDSPDDSTLSESANQVFLGFTYVAPSVLESVKEKFSFEPKIRSPRRFIGSPRTPVSPVKFSPGDFWGRGASASTANPQTPVEYPMETSGIEQMDVTMSGEASAPLPIRQPNSGPYKKQAFPMISKRPEHLRMNL

Macaca mulatta (Rhesus macaque)

2.7.11.1

CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00001433, ECO:0000256|PIRNR:PIRNR000605}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775, ECO:0000256|PIRNR:PIRNR000605};

ATP-binding;Kinase;Nucleotide-binding;Phosphoprotein;Reference proteome;Serine/threonine-protein kinase;Transferase

behavioral fear response [GO:0001662]; cellular response to dexamethasone stimulus [GO:0071549]; cellular response to growth factor stimulus [GO:0071363]; cellular response to insulin stimulus [GO:0032869]; cellular response to nutrient [GO:0031670]; cellular response to type II interferon [GO:0071346]; G1/S transition of mitotic cell cycle [GO:0000082]; germ cell development [GO:0007281]; long-chain fatty acid import into cell [GO:0044539]; modulation of chemical synaptic transmission [GO:0050804]; negative regulation of extrinsic apoptotic signaling pathway [GO:2001237]; negative regulation of insulin receptor signaling pathway [GO:0046627]; phosphorylation [GO:0016310]; positive regulation of mitotic cell cycle [GO:0045931]; positive regulation of TORC1 signaling [GO:1904263]; positive regulation of translational initiation [GO:0045948]; TOR signaling [GO:0031929]

cytoplasm [GO:0005737]; glutamatergic synapse [GO:0098978]; mitochondrial outer membrane [GO:0005741]; nucleoplasm [GO:0005654]

ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein serine/threonine/tyrosine kinase activity [GO:0004712]

SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00004294}.

IPR000961;IPR011009;IPR017892;IPR000719;IPR017441;IPR016238;IPR008271;

1.10.510.10;

A0A1D5QUK7

MEAAAAAPRPRLLLLVLAATAAAAAALLPGATALQCFCHLCTKDNFTCVTDGLCFVSVTETTDKVIHNSMCIAEIDLIPRDRPFVCAPSSKTGSVTTTYCCNQDHCNKIELPTTVKSSPGLGPVELAAVIAGPVCFVCISLMLMVYICHNRTVIHHRVPNEEDPSLDRPFISEGTTLKDLIYDMTTSGSGSGLPLLVQRTIARTIVLQESIGKGRFGEVWRGKWRGEEVAVKIFSSREERSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVSDYHEHGSLFDYLNRYTVTVEGMIKLALSTASGLAHLHMEIVGTQGKPAIAHRDLKSKNILVKKNGTCCIADLGLAVRHDSATDTIDIAPNHRVGTKRYMAPEVLDDSINMKHFESFKRADIYAMGLVFWEIARRCSIGGIHEDYQLPYYDLVPSDPSVEEMRKVVCEQKLRPNIPNRWQSCEALRVMAKIMRECWYANGAARLTALRIKKTLSQLSQQEGIKMFVN

Macaca mulatta (Rhesus macaque)

2.7.11.30

CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[receptor-protein] = ADP + H(+) + O-phospho-L-seryl-[receptor-protein]; Xref=Rhea:RHEA:18673, Rhea:RHEA-COMP:11022, Rhea:RHEA-COMP:11023, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.30; Evidence={ECO:0000256|ARBA:ARBA00023945}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[receptor-protein] = ADP + H(+) + O-phospho-L-threonyl-[receptor-protein]; Xref=Rhea:RHEA:44880, Rhea:RHEA-COMP:11024, Rhea:RHEA-COMP:11025, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.30; Evidence={ECO:0000256|ARBA:ARBA00023948};

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|ARBA:ARBA00001946}; COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|ARBA:ARBA00001936};

Apoptosis;ATP-binding;Cell junction;Differentiation;Growth regulation;Isopeptide bond;Kinase;Magnesium;Manganese;Membrane;Nucleotide-binding;Phosphoprotein;Receptor;Reference proteome;Serine/threonine-protein kinase;Signal;Tight junction;Transferase;Transmembrane;Transmembrane helix;Ubl conjugation

activin receptor signaling pathway [GO:0032924]; angiogenesis involved in coronary vascular morphogenesis [GO:0060978]; anterior/posterior pattern specification [GO:0009952]; apoptotic process [GO:0006915]; blastocyst development [GO:0001824]; cellular response to growth factor stimulus [GO:0071363]; collagen fibril organization [GO:0030199]; coronary artery morphogenesis [GO:0060982]; embryonic cranial skeleton morphogenesis [GO:0048701]; endothelial cell migration [GO:0043542]; endothelial cell proliferation [GO:0001935]; epicardium morphogenesis [GO:1905223]; epithelial to mesenchymal transition [GO:0001837]; filopodium assembly [GO:0046847]; germ cell migration [GO:0008354]; heart development [GO:0007507]; kidney development [GO:0001822]; lens development in camera-type eye [GO:0002088]; male gonad development [GO:0008584]; myofibroblast differentiation [GO:0036446]; negative regulation of cell migration [GO:0030336]; negative regulation of chondrocyte differentiation [GO:0032331]; negative regulation of endothelial cell proliferation [GO:0001937]; negative regulation of extrinsic apoptotic signaling pathway [GO:2001237]; nervous system development [GO:0007399]; neuron fate commitment [GO:0048663]; parathyroid gland development [GO:0060017]; pharyngeal system development [GO:0060037]; positive regulation of apoptotic signaling pathway [GO:2001235]; positive regulation of cell growth [GO:0030307]; positive regulation of cell migration [GO:0030335]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of epithelial to mesenchymal transition involved in endocardial cushion formation [GO:1905007]; positive regulation of extracellular matrix assembly [GO:1901203]; positive regulation of filopodium assembly [GO:0051491]; positive regulation of gene expression [GO:0010628]; positive regulation of mesenchymal stem cell proliferation [GO:1902462]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of SMAD protein signal transduction [GO:0060391]; positive regulation of stress fiber assembly [GO:0051496]; positive regulation of tight junction disassembly [GO:1905075]; positive regulation of vasculature development [GO:1904018]; post-embryonic development [GO:0009791]; regulation of cardiac muscle cell proliferation [GO:0060043]; regulation of protein ubiquitination [GO:0031396]; response to cholesterol [GO:0070723]; roof of mouth development [GO:0060021]; thymus development [GO:0048538]; transforming growth factor beta receptor signaling pathway [GO:0007179]; ventricular compact myocardium morphogenesis [GO:0003223]; ventricular septum morphogenesis [GO:0060412]; ventricular trabecula myocardium morphogenesis [GO:0003222]

activin receptor complex [GO:0048179]; bicellular tight junction [GO:0005923]; cell surface [GO:0009986]; endosome [GO:0005768]; membrane raft [GO:0045121]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; transforming growth factor beta ligand-receptor complex [GO:0070021]

activin binding [GO:0048185]; activin receptor activity, type I [GO:0016361]; ATP binding [GO:0005524]; I-SMAD binding [GO:0070411]; SMAD binding [GO:0046332]; transforming growth factor beta binding [GO:0050431]; transforming growth factor beta receptor activity, type I [GO:0005025]; type II transforming growth factor beta receptor binding [GO:0005114]; ubiquitin protein ligase binding [GO:0031625]

SUBCELLULAR LOCATION: Cell junction, tight junction {ECO:0000256|ARBA:ARBA00004435}. Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}. Cell surface {ECO:0000256|ARBA:ARBA00004241}. Membrane raft {ECO:0000256|ARBA:ARBA00004285}. Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.

IPR000472;IPR003605;IPR011009;IPR000719;IPR017441;IPR008271;IPR045860;IPR000333;

2.10.60.10;1.10.510.10;

A0A1D5QVT2

MQIRAPGSSWDLSTEPRDSQFLSRRAGPRCRSLPGRGASGPDALQPPARGKRGGRANPGPAPAAPRRASRVPGQQPPPTQVLLGRPVAPPALNSSHRGAPPPRNFHRERVPESQLLPGQRFQAKDPEEQGDIVVALYPYDGIHPDDLSFKKGEKMKVLEEHGEWWKAKSLLTKKEGFIPSNYVAKLNTLETEEWFFKDITRKDAERQLLAPGNSAGAFLIRESETLKGSFSLSVRDFDPVHGDVIKHYKIRSLDNGGYYISPRITFPCISDMIKHYQKQPDGLCRRLEKACISPKPQKPWDKDAWEIPRESIKLVKRLGAGQFGEVWMGYYNNSTKVAVKTLKPGTMSVQAFLEEANLMKTLQHDKLVRLYAVVTREEPIYIITEYMAKGSLLDFLKSDEGGKVLLPKLIDFSAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFGLARVIEDNEYTAREGAKFPIKWTAPEAINFGCFTIKSDVWSFGILLYEIVTYGKIPYPGRTNADVMTALSQGYRMPRVENCPDELYDIMKMCWKEKAEERPTFDYLQSVLDDFYTATEGQYQQQP

Macaca mulatta (Rhesus macaque)

2.7.10.2

CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000256|ARBA:ARBA00001149, ECO:0000256|RuleBase:RU362096};

ATP-binding;Cytoplasm;Kinase;Nucleotide-binding;Reference proteome;SH2 domain;SH3 domain;Transferase;Tyrosine-protein kinase

B cell homeostasis [GO:0001782]; B cell receptor signaling pathway [GO:0050853]; C-X-C chemokine receptor CXCR4 signaling pathway [GO:0038159]; cellular response to retinoic acid [GO:0071300]; dendritic cell differentiation [GO:0097028]; DNA damage checkpoint signaling [GO:0000077]; DNA damage response [GO:0006974]; eosinophil differentiation [GO:0030222]; erythrocyte differentiation [GO:0030218]; Fc receptor mediated inhibitory signaling pathway [GO:0002774]; Fc receptor mediated stimulatory signaling pathway [GO:0002431]; hematopoietic progenitor cell differentiation [GO:0002244]; innate immune response [GO:0045087]; interleukin-5-mediated signaling pathway [GO:0038043]; lipopolysaccharide-mediated signaling pathway [GO:0031663]; negative regulation of B cell proliferation [GO:0030889]; negative regulation of ERK1 and ERK2 cascade [GO:0070373]; negative regulation of mast cell proliferation [GO:0070667]; negative regulation of myeloid leukocyte differentiation [GO:0002762]; negative regulation of protein phosphorylation [GO:0001933]; negative regulation of toll-like receptor 2 signaling pathway [GO:0034136]; negative regulation of toll-like receptor 4 signaling pathway [GO:0034144]; neuron projection development [GO:0031175]; phosphorylation [GO:0016310]; platelet degranulation [GO:0002576]; positive regulation of cell migration [GO:0030335]; positive regulation of dendritic cell apoptotic process [GO:2000670]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of mast cell proliferation [GO:0070668]; positive regulation of neuron projection development [GO:0010976]; positive regulation of tyrosine phosphorylation of STAT protein [GO:0042531]; regulation of B cell apoptotic process [GO:0002902]; regulation of B cell receptor signaling pathway [GO:0050855]; regulation of cell adhesion mediated by integrin [GO:0033628]; regulation of cytokine production [GO:0001817]; regulation of erythrocyte differentiation [GO:0045646]; regulation of inflammatory response [GO:0050727]; regulation of mast cell activation [GO:0033003]; regulation of mast cell degranulation [GO:0043304]; regulation of monocyte chemotaxis [GO:0090025]; regulation of platelet aggregation [GO:0090330]; regulation of release of sequestered calcium ion into cytosol [GO:0051279]; response to hormone [GO:0009725]; tolerance induction to self antigen [GO:0002513]; toll-like receptor 4 signaling pathway [GO:0034142]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]

cell surface [GO:0009986]; cytosol [GO:0005829]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; Golgi apparatus [GO:0005794]; membrane raft [GO:0045121]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; protein-containing complex [GO:0032991]

ATP binding [GO:0005524]; ephrin receptor binding [GO:0046875]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; phosphatidylinositol 3-kinase activator activity [GO:0141038]; phosphorylation-dependent protein binding [GO:0140031]; protein-containing complex binding [GO:0044877]; scaffold protein binding [GO:0097110]; SH3 domain binding [GO:0017124]; signaling receptor binding [GO:0005102]; transmembrane transporter binding [GO:0044325]

IPR011009;IPR035852;IPR035748;IPR000719;IPR017441;IPR001245;IPR000980;IPR036860;IPR036028;IPR001452;IPR008266;IPR020635;

3.30.505.10;2.30.30.40;1.10.510.10;

A0A1D5QX27

MEDPRGINGQSVQTSQASSDVAVSSSCRSMEMQDLTSPHSRLSGSSESPSGPKLDNSHINSNSMTPNGTEVKTEPMSSSETASTTADGSLDNFSGSAIGSSSFSPRPTHQFSPPQIYPSNRPYPHILPTPSSQTMAAYGQTQFTTGMQQATAYATYPQPGQPYGISSYGALWAGIKTEGGLSQSQSPGQTGFLSYGTSFSTPQPGQAPYSYQMQGSSFTTSSGLYTGNNSLTNSSGFNSSQQDYPSYPSFGQGQYAQYYNSSPYPAHYMTSSNTSPTTPSTNATYQLQEPPSGITSQAVTDPTAEYNTIHSPSTPIKDSDSDRLRRGSDGKSRGRGRRNNNPSPPPDSDLERVFIWDLDETIIVFHSLLTGSYANRYGRDPPTSVSLGLRMEEMIFNLADTHLFFNDLEECDQVHIDDVSSDDNGQDLSTYNFGTDGFPAAATSANLCLATGVRGGVDWMRKLAFRYRRVKEIYNTYKNNVGGLLGPAKREAWLQLRAEIEALTDSWLTLALKALSLIHSRTNCVNILVTTTQLIPALAKVLLYGLGIVFPIENIYSATKIGKESCFERIIQRFGRKVVYVVIGDGVEEEQGAKKHAMPFWRISSHSDLMALHHALELEYL

Macaca mulatta (Rhesus macaque)

3.1.3.48

CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000256|ARBA:ARBA00001490, ECO:0000256|RuleBase:RU362036};

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|PIRSR:PIRSR628472-2, ECO:0000256|RuleBase:RU362036}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR628472-2, ECO:0000256|RuleBase:RU362036};

Activator;Hydrolase;Magnesium;Metal-binding;Nucleus;Protein phosphatase;Reference proteome;Transcription;Transcription regulation

aorta morphogenesis [GO:0035909]; branching involved in ureteric bud morphogenesis [GO:0001658]; cell differentiation [GO:0030154]; cochlea morphogenesis [GO:0090103]; double-strand break repair [GO:0006302]; embryonic skeletal system morphogenesis [GO:0048704]; epithelial cell proliferation [GO:0050673]; extrinsic apoptotic signaling pathway in absence of ligand [GO:0097192]; mesodermal cell fate specification [GO:0007501]; metanephros development [GO:0001656]; middle ear morphogenesis [GO:0042474]; negative regulation of extrinsic apoptotic signaling pathway in absence of ligand [GO:2001240]; neuron fate specification [GO:0048665]; otic vesicle morphogenesis [GO:0071600]; outer ear morphogenesis [GO:0042473]; outflow tract morphogenesis [GO:0003151]; pattern specification process [GO:0007389]; pharyngeal system development [GO:0060037]; positive regulation of DNA repair [GO:0045739]; positive regulation of epithelial cell proliferation [GO:0050679]; positive regulation of secondary heart field cardioblast proliferation [GO:0072513]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein sumoylation [GO:0016925]; regulation of neuron differentiation [GO:0045664]; response to ionizing radiation [GO:0010212]; semicircular canal morphogenesis [GO:0048752]; striated muscle tissue development [GO:0014706]

cytoplasm [GO:0005737]; nuclear body [GO:0016604]; nucleus [GO:0005634]; protein-DNA complex [GO:0032993]

histone H2AXY142 phosphatase activity [GO:0140793]; metal ion binding [GO:0046872]; protein tyrosine phosphatase activity [GO:0004725]; RNA binding [GO:0003723]

SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.

IPR006545;IPR042577;IPR038102;IPR028472;

3.40.50.12350;

A0A1D5QYM8

MASNPERGEIMLTELQGDSRSLPFSENVSAVQKLDFSDTVVQQKLDDIKDRIKREIRKELKIKEGAENLRKVTTDKKSLAYVDNILKKSNKKLEELHHKLQELNAHIVVSDPEDITDCPRTPDTPNSDPRCSTSNNRLKALQKQLDIELKVKQGAENMIQMYSNGSSKDRKLHGTAQQLLQDSKTKIEVIRMQILQAVQTNELAFDNAKPVISPLELRMEELRHHFRIEFAVAEGAKNVMKLLGSGKVTDRKALSEAQARFNESSQKLDLLKYSLEQRLNELPKNHPKSSIIIEELSLVASPTLSPRQSMISTQNQYSTLSKPAALTGTLEVRLMGCQDILENVPGRSKATSVALPGWSPSETRSSFMSRTSKSKSGSSRNLLKTDDLSNDVCAVLKLDNTVVGQTSWKPISNQSWDQKFTLELDRSRELEISVYWRDWRSLCAVKFLRLEDFLDNQRHGMCLYLEPQGTLFAEVTFFNPVIERRPKLQRQKKIFSKRKTFLRAPQMNINIATWGRLVRRAIPTVNHSGTFSPQAPVPTTVPVVDVRIPELAPPASDSTVTKLDFDLEPEPPPAPPRASSLGEIDESSELRVLDTPGQDSETVFDIENDRNSILPKSQSEYKPDTPQSGLEYSGIQELEDKRSQQRFQFNLQDFRCCAVLGRGHFGKVLLAEYKHTNEMFAIKALKKGDIVARDEVDSLMCEKRIFETVNSVRHPFLVNLFACFQTKEHVCFVMEYAAGGDLMMHIHTDVFSEPRAVFYAACVVLGLQYLHEHKIVYRDLKLDNLLLDTEGFVKIADFGLCKEGMGYGDRTSTFCGTPEFLAPEVLTETSYTRAVDWWGLGVLIYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSTEAISIMRRLLRRNPERRLGASEKDAEDVKKHPFFRLIDWSALMDKKVKPPFIPTIRGREDVSNFDDEFTSEAPILTPPREPRILSEEEQEMFRDFDYIADWC

Macaca mulatta (Rhesus macaque)

2.7.11.13

CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.13; Evidence={ECO:0000256|ARBA:ARBA00000946}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.13; Evidence={ECO:0000256|ARBA:ARBA00000569};

ATP-binding;Coiled coil;Cytoplasm;Kinase;Nucleotide-binding;Nucleus;Phosphoprotein;Reference proteome;Repeat;Serine/threonine-protein kinase;Transcription;Transcription regulation;Transferase

apical junction assembly [GO:0043297]; epithelial cell migration [GO:0010631]; intracellular signal transduction [GO:0035556]; phosphorylation [GO:0016310]; positive regulation of cytokinesis [GO:0032467]; positive regulation of mitotic cell cycle [GO:0045931]; positive regulation of viral genome replication [GO:0045070]; regulation of cell motility [GO:2000145]

apical junction complex [GO:0043296]; centrosome [GO:0005813]; cleavage furrow [GO:0032154]; cytosol [GO:0005829]; intermediate filament cytoskeleton [GO:0045111]; lamellipodium [GO:0030027]; midbody [GO:0030496]; nuclear body [GO:0016604]; perinuclear region of cytoplasm [GO:0048471]; protein-containing complex [GO:0032991]

ATP binding [GO:0005524]; diacylglycerol-dependent serine/threonine kinase activity [GO:0004697]; histone deacetylase binding [GO:0042826]; protein serine/threonine kinase activity [GO:0004674]; RNA polymerase binding [GO:0070063]; small GTPase binding [GO:0031267]

SUBCELLULAR LOCATION: Cleavage furrow {ECO:0000256|ARBA:ARBA00004626}. Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Midbody {ECO:0000256|ARBA:ARBA00004214}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.

IPR000961;IPR000008;IPR035892;IPR037784;IPR011072;IPR036274;IPR011009;IPR017892;IPR037313;IPR000719;IPR017441;IPR008271;

2.60.40.150;1.10.287.160;1.10.510.10;

A0A1D5QZ26

MKGSCRQGGRRVLSAAAAAVPGRRPGSPPARKRASGAATEAPRRSEPPPGSGVPSGERAPERRRRRGGEGAARDGSCLARRARSSPELWLARRCGWAGDAAAVAARPGEMSTEAGEGITFSVPPFAPSGFCTIPEGGICRRGGAAAVGESEEHQLPPPPPGSFWNVESAAAPGIGCPAATSASSATRGRGSSVGGGSRRTTVAYVINEASQGQLVVAESEALQSLREACETVGATLETLHFGKLDFGETTVLDRFYNADIAVVEMSDAFRQPSLFYHLGVRESFSMANNIILYCDTNSDSLQSLKELICQKNTMCTGNYTFVPYMITPHNKVYCCDSSFMKGLTELMQPNFELLLGPICLPLVDRFIQLLKVAQASSSQYFRESILNDIRKARNLYTGKELAAELARIRQRVDNIEVLTADIVINLLLSYRDIQDYDSIVKLVETLEKLPTFDLASHHHVKFHYAFALNRRNLPGDRAKALDIMIPMVQSEGQVASDMYCLVGRIYKDMFLDSNFTDTESRDHGASWFKKAFESEPTLQSGINYAVLLLAAGHQFESSFELRKVGVKLSSLLGKKGNLEKLQSYWEVGFFLGASVLANDHMRVIQASEKLFKLKTPAWYLKSIVETILIYKHFVKLTTEQPVAKQELVDFWMDFLVEATKTDVTVVRFPVLILEPTKIYQPSYLSINNEVEEKTISIWHVLPDDKKGIHEWNFSASSVRGVSISKFEERCCFLYVLHNSDDFQIYFCTELHCKKFFEMVNTITEEKGRSTEEGDCESDSLEYDYEYDENGDRVVLGKGTYGIVYAGRDLSNQVRIAIKEIPERDSRYSQPLHEEIALHKHLKHKNIVQYLGSFSENGFIKIFMEQVPGGSLSALLRSKWGPLKDNEQTIGFYTKQILEGLKYLHDNQIVHRDIKGDNVLINTYSGVLKISDFGTSKRLAGINPCTETFTGTLQYMAPEIIDKGPRGYGKAADIWSLGCTIIEMATGKPPFYELGEPQAAMFKVGMFKVHPEIPESMSAEAKAFILKCFEPDPDKRACANDLLVDEFLKVSSKKKKTQPKLSALSAGSNEYLRSISLPVPVLVEDTSSSSEYGSVSPDTELKADPFSFKTRAKSCGERDVKGIRTLFLGIPDENFEDHSAPPSPEEKDSGFFMLRKDSERRATLHRILTEDQDKVVRNLMESLAQGSEEPKLKWEHITTLIASLREFVRSTDRKIIATTLSKLKLELDFDSHGISQVQVVLFGFQDAVNKVLRNHNIKPHWMFALDSIIRKAVQTAITILVPELRPHFSLASESDTADQEDLDVEDDHEEQPSNQTVRRPQPVIEDAVATSGVSTLSSTVSHDSQSAHRSLNVQLGRMKIETNRLLEELVRKEKELQALLHRAIEEKDQEIKHLKLKSQPIEIPELPVFHLNSPGTNTEDSELTDWLRVNGADEDTISRFLAEDYTLLDVLYYVTRDDLKCLRLRGGMLCTLWKAIIDFRNKQT

Macaca mulatta (Rhesus macaque)

2.7.11.25

CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.25; Evidence={ECO:0000256|ARBA:ARBA00000478}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.25; Evidence={ECO:0000256|ARBA:ARBA00000106};

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|ARBA:ARBA00001946};

ATP-binding;Coiled coil;Kinase;Magnesium;Metal-binding;Nucleotide-binding;Reference proteome;Serine/threonine-protein kinase;Transferase

cellular response to amino acid starvation [GO:0034198]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to reactive nitrogen species [GO:1902170]; intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress [GO:0070059]; intrinsic apoptotic signaling pathway in response to oxidative stress [GO:0008631]; JNK cascade [GO:0007254]; neuron intrinsic apoptotic signaling pathway in response to oxidative stress [GO:0036480]; p38MAPK cascade [GO:0038066]; positive regulation of apoptotic process [GO:0043065]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of JNK cascade [GO:0046330]; positive regulation of myoblast differentiation [GO:0045663]; programmed necrotic cell death [GO:0097300]; stress-activated MAPK cascade [GO:0051403]

IRE1-TRAF2-ASK1 complex [GO:1990604]; protein kinase complex [GO:1902911]

ATP binding [GO:0005524]; JUN kinase kinase kinase activity [GO:0004706]; magnesium ion binding [GO:0000287]; MAP kinase kinase kinase activity [GO:0004709]; protein domain specific binding [GO:0019904]; protein homodimerization activity [GO:0042803]; protein kinase binding [GO:0019901]; protein phosphatase binding [GO:0019903]

IPR046872;IPR046873;IPR011009;IPR043969;IPR025136;IPR000719;IPR017441;IPR013761;IPR008271;

1.10.510.10;

A0A1D5QZ91

MAAAAAQGGGGGEPRRAEGVGPGVPGEVEMVKGQPFDVGPRYTQLQYIGEGAYGMVSSAYDHVRKTRVAIKKISPFEHQTYCQRTLREIQILLRFRHENVIGIRDILRASTLEAMRDVYIVQDLMETDLYKLLKSQQLSNDHICYFLYQILRGLKYIHSANVLHRDLKPSNLLINTTCDLKICDFGLARIADPEHDHTGFLTEYVATRWYRAPEIMLNSKGYTKSIDIWSVGCILAEMLSNRPIFPGKHYLDQLNHILGILGSPSQEDLNCIINMKARNYLQSLPSKTKVAWAKLFPKSDSKALDLLDRMLTFNPNKRITVEEALAHPYLEQYYDPTDEPVAEEPFTFAMELDDLPKERLKELIFQETARFQPGALEAP

Macaca mulatta (Rhesus macaque)

2.7.11.24

CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.24; Evidence={ECO:0000256|ARBA:ARBA00000494}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.24; Evidence={ECO:0000256|ARBA:ARBA00000088, ECO:0000256|RuleBase:RU361165};

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|RuleBase:RU361165};

ATP-binding;Kinase;Magnesium;Nucleotide-binding;Reference proteome;Serine/threonine-protein kinase;Transferase

Bergmann glial cell differentiation [GO:0060020]; BMP signaling pathway [GO:0030509]; cardiac neural crest cell development involved in heart development [GO:0061308]; cartilage development [GO:0051216]; caveolin-mediated endocytosis [GO:0072584]; cellular response to amino acid starvation [GO:0034198]; cellular response to cadmium ion [GO:0071276]; cellular response to mechanical stimulus [GO:0071260]; cellular response to reactive oxygen species [GO:0034614]; cellular response to tumor necrosis factor [GO:0071356]; DNA-templated transcription [GO:0006351]; ERBB2-ERBB3 signaling pathway [GO:0038133]; ERK1 and ERK2 cascade [GO:0070371]; face development [GO:0060324]; insulin receptor signaling pathway [GO:0008286]; insulin-like growth factor receptor signaling pathway [GO:0048009]; interleukin-1-mediated signaling pathway [GO:0070498]; intracellular signal transduction [GO:0035556]; lipopolysaccharide-mediated signaling pathway [GO:0031663]; lung morphogenesis [GO:0060425]; modulation of chemical synaptic transmission [GO:0050804]; myelination [GO:0042552]; negative regulation of TORC1 signaling [GO:1904262]; outer ear morphogenesis [GO:0042473]; phosphorylation [GO:0016310]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of macrophage chemotaxis [GO:0010759]; positive regulation of macrophage proliferation [GO:0120041]; positive regulation of telomere capping [GO:1904355]; positive regulation of telomere maintenance via telomerase [GO:0032212]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of xenophagy [GO:1904417]; regulation of cellular pH [GO:0030641]; regulation of cytoskeleton organization [GO:0051493]; regulation of early endosome to late endosome transport [GO:2000641]; regulation of Golgi inheritance [GO:0090170]; regulation of ossification [GO:0030278]; regulation of stress-activated MAPK cascade [GO:0032872]; response to epidermal growth factor [GO:0070849]; response to exogenous dsRNA [GO:0043330]; Schwann cell development [GO:0014044]; sensory perception of pain [GO:0019233]; signal transduction in response to DNA damage [GO:0042770]; stress-activated MAPK cascade [GO:0051403]; thymus development [GO:0048538]; thyroid gland development [GO:0030878]; trachea formation [GO:0060440]; xenophagy [GO:0098792]

caveola [GO:0005901]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; early endosome [GO:0005769]; focal adhesion [GO:0005925]; glutamatergic synapse [GO:0098978]; Golgi apparatus [GO:0005794]; late endosome [GO:0005770]; nuclear envelope [GO:0005635]; nucleus [GO:0005634]; pseudopodium [GO:0031143]

ATP binding [GO:0005524]; DNA-binding transcription factor binding [GO:0140297]; identical protein binding [GO:0042802]; MAP kinase activity [GO:0004707]; phosphatase binding [GO:0019902]; phosphotyrosine residue binding [GO:0001784]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]

SUBCELLULAR LOCATION: Cell junction, focal adhesion {ECO:0000256|ARBA:ARBA00004246}. Membrane, caveola {ECO:0000256|ARBA:ARBA00004345}.

IPR011009;IPR003527;IPR008349;IPR000719;IPR017441;IPR008271;

1.10.510.10;

A0A1D5QZE0

MGPGVLLLLLVVTAWHGQGIPVIEPSGPELVVKPGEMVTLRCVGNGSVEWDGPISPHWTLYSDGPSSVLTTTNATFQNTRTYRCTEPGDPLGGSAAIHLYVKDPARPWNVLAKEVVVFEDQDALLPCLLTDPVLEAGVSLVRLRGRPLLRHTNYSFSPWHGFTIHRAKFIQGQDYQCSALMGSRKVMSISIRLKVQKVIPGPPALTLVPEELVRIRGEAAQIVCSASNIDVDFDVFLQHNTTKLAIPQRSDFHDNRYQKVLTLSLGQVDFQHAGNYSCVASNVQGKHSTSMFFRVVESAYLDLSSEQNLIQEVTVGEGLNLKVMVEAYPGLQGFNWTYLGPFSDHQPEPKLANATTKDTYRHTFTLSLPRLKPSEAGRYSFLARNPGGWRALTFELTLRYPPEVSVIWTSINGSGTLLCAASGYPQPNVTWLQCAGHTDRCDEAQVLQVWVDPHPEVLSQEPFQKVTVQSLLTAETLEHNQTYECRAHNSVGSGSWAFIPISAGARTHPPDEFLFTPVVVACMSVMALLLLLLLLLLYKYKQKPKYQVRWKIIESYEGNSYTFIDPTQLPYNEKWEFPRNNLQFGKTLGAGAFGKVVEATAFGLGKEDAVLKVAVKMLKSTAHADEKEALMSELKIMSHLGQHENIVNLLGACTHGGPVLVITEYCCYGDLLNFLRRKAEAMLGPSLSPGQDPEGGADYKNIHLEKKYVRRDSGFSSQGVDTYVEMRPVSTSSNDSFSEQDLDKEDGRPLELWDLLHFSSQVAQGMAFLASKNCIHRDVAARNVLLTNGHVAKIGDFGLARDIMNDSNYIVKGNARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLDTASCRPAGPWSPPTDPLSSRSAPSFRSKPKRTGESGTIPICQAAAEAVVAVAAAAAAAVSRRRRALVSTWPAASKGISPSPCCSPTTISSAEEPTTGSTTLPSCKLQLLHGRGDVGRTHKLCLRSFHSTAWPSAETWEGEGSRGGLRIPLPERGPSLPVRGWGLSPHPLSPTVLMVLASCLLCQLVDVLHLLS

Macaca mulatta (Rhesus macaque)

2.7.10.1

CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence={ECO:0000256|ARBA:ARBA00001171};

ATP-binding;Cell membrane;Disulfide bond;Glycoprotein;Immunoglobulin domain;Kinase;Magnesium;Membrane;Metal-binding;Nucleotide-binding;Phosphoprotein;Receptor;Reference proteome;Repeat;Signal;Transferase;Transmembrane;Transmembrane helix;Tyrosine-protein kinase

axon guidance [GO:0007411]; cell-cell junction maintenance [GO:0045217]; forebrain neuron differentiation [GO:0021879]; microglial cell proliferation [GO:0061518]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cell population proliferation [GO:0008285]; olfactory bulb development [GO:0021772]; osteoclast differentiation [GO:0030316]; positive regulation by host of viral process [GO:0044794]; positive regulation of cell migration [GO:0030335]; positive regulation of chemokine production [GO:0032722]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of macrophage chemotaxis [GO:0010759]; positive regulation of macrophage proliferation [GO:0120041]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of tyrosine phosphorylation of STAT protein [GO:0042531]; regulation of actin cytoskeleton organization [GO:0032956]; regulation of cell shape [GO:0008360]; regulation of MAPK cascade [GO:0043408]; response to ischemia [GO:0002931]; ruffle organization [GO:0031529]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]

cell surface [GO:0009986]; CSF1-CSF1R complex [GO:1990682]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]

ATP binding [GO:0005524]; cytokine binding [GO:0019955]; growth factor binding [GO:0019838]; macrophage colony-stimulating factor receptor activity [GO:0005011]; metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803]; protein phosphatase binding [GO:0019903]

SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}. Membrane {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU000311}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU000311}.

IPR030658;IPR007110;IPR036179;IPR013783;IPR003599;IPR003598;IPR013151;IPR011009;IPR000719;IPR017441;IPR001245;IPR008266;IPR020635;IPR001824;

2.60.40.10;1.10.510.10;

A0A1D5QZT5

MDQREILQKFLDEAQSKKINKEEFTNEFLKLKRQSTKYKADKTYPTTVAEKPKNIKKNRYKDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKTYIATQGPLSTTLLDFWRMIWEYNVLIIVMACMEYEMGKKKCERYWAEPGEMQLEFGPFSISCEAEKRKSDYIIRTLKVKFNSDTRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIIPENFSVFSLIQEMRTQRPSLVQTQEQYELVYNAVLELFKRQMDVIRDKHSGTESQAKYCIPEQNHTLQADSYSPNLPKSTIKAAKMMNQQRTKMENTESSSFDFRTSEISAKEELVLHPAKSSTSFDFLELNYGFDKNADTTMKRQTKAFPTVGEPLQKHQSLDLGSLLFEACSNSKPVNAAGRYFDSKVPITRTKSTPFELIQQRETKEVDSKENFSYLESEPHDSSFVEMQSQKVMHVSSAELNYSLPYDSKHQICNASNVKHHDSGALDVCSYIPLVEDPYFSSWPPSGTGSKMSLDLPEKQDGTVFPSSLLPTSSTSLSSYYNSHDSLSLNSPTNISPLLNQESAVLATAPRIDDEIPPPLPVRTPESFIVVEEAGEFSPSISKSLSSAVKAKIGTSLEWDGASEPKKFDDSVRLRPSKSVKLRSPKSELHQDRSSPPPPLPERTLESFFLADEDCMQAQSIETYSTSCPDTMENSTSSKQTLKTPGKSFTRSKVKKIRVLGNMPEAFSYCICNSCPPNKPTESVQSNNSSSFLNFGFANRFSKPKGPRNPPPTWNI

Macaca mulatta (Rhesus macaque)

3.1.3.48

Disulfide bond;Hydrolase;Reference proteome

cellular response to muramyl dipeptide [GO:0071225]; negative regulation of interleukin-6 production [GO:0032715]; negative regulation of interleukin-8 production [GO:0032717]; negative regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway [GO:0070433]; negative regulation of p38MAPK cascade [GO:1903753]; negative regulation of T cell activation [GO:0050868]; negative regulation of tumor necrosis factor production [GO:0032720]; phosphoanandamide dephosphorylation [GO:0035644]; positive regulation of CD8-positive, alpha-beta T cell proliferation [GO:2000566]; positive regulation of defense response to virus by host [GO:0002230]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of granzyme B production [GO:0071663]; positive regulation of interferon-alpha production [GO:0032727]; positive regulation of interferon-beta production [GO:0032728]; positive regulation of NLRP3 inflammasome complex assembly [GO:1900227]; positive regulation of protein import into nucleus [GO:0042307]; positive regulation of protein K63-linked ubiquitination [GO:1902523]; positive regulation of toll-like receptor 3 signaling pathway [GO:0034141]; positive regulation of toll-like receptor 4 signaling pathway [GO:0034145]; positive regulation of toll-like receptor 7 signaling pathway [GO:0034157]; positive regulation of toll-like receptor 9 signaling pathway [GO:0034165]; regulation of leukocyte migration [GO:0002685]; regulation of non-canonical NF-kappaB signal transduction [GO:1901222]; regulation of T cell receptor signaling pathway [GO:0050856]; T cell differentiation [GO:0030217]; T cell receptor signaling pathway [GO:0050852]

cytoplasm [GO:0005737]; cytoplasmic side of plasma membrane [GO:0009898]; nucleus [GO:0005634]

kinase binding [GO:0019900]; non-membrane spanning protein tyrosine phosphatase activity [GO:0004726]; protein tyrosine phosphatase activity [GO:0004725]; SH3 domain binding [GO:0017124]

IPR029021;IPR047170;IPR047253;IPR000242;IPR016276;IPR016130;IPR003595;IPR000387;

3.90.190.10;

A0A1D5R032

MGQQPGKVLGDQRRPSLPALHFIKGAGKKESSRHGGPHCNVFVEHEALQRPVASDFEPQGLSEAARWNSKENLLAGPSENDPNLFVALYDFVASGDNTLSITKGEKLRVLGYNHNGEWCEAQTKNGQGWVPSNYITPVNSLEKHSWYHGPVSRNAAEYLLSSGINGSFLVRESESSPGQRSISLRYEGRVYHYRINTASDGKLYVSSESRFNTLAELVHHHSTVADGLITTLHYPAPKRNKPTVYGVSPNYDKWEMERTDITMKHKLGGGQYGEVYEGVWKKYSLTVAVKTLKEDTMEVEEFLKEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMTYGNLLDYLRECNRQEVNAVVLLYMATQISSAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLSRLMTGDTYTAHAGAKFPIKWTAPESLAYNKFSIKSDVWAFGVLLWEIATYGMSPYPGIDLSQVYELLEKDYRMERPEGCPEKVYELMRACWQWNPSDRPSFAEIHQAFETMFQESSISDEVEKELGKQGIRGAVSTLLQAPELPTKTRTSRRAAEHRDATDVPEMPHSKGQGESDPLDHEPAVSPLLPRKERGPLEGGLNEDERLLPKDKKTNLFSALIKKKKKTAPTPPKRSSSFREMDGQPERRGAGEEEGRDISNGALALTPLDTADPAKSPKPSNGAGVPNGALRESGGSGFRSPHLWKKSSTLTSSRLATGEEEGGGSSSKRFLRSCSASCVPHGAKDTEWRSVTLPRDLQSTGRQFDSSTFGGHKSEKPALPRKRAGENRSDQVARGTVTPPPRLVKKNEEAADEVFKDIMESSPGSSPPNLTPKPLRRQVMMAPASGLPHKEEAGKGSALGTPAAAEPVTPTSKAGSGAPGGTSKGPAEESRIRRHKHSSESPGRDKGKLSRLKPAPPPPPAASAGKAGGKPSQSPSQEAAGEAGPGAKTKATSLVDAVNSDAAKPSQPGEGLKKPVLPATAKPQSTKLSGTPISPAPIPSTLPTASSALAGDQPSSTAFIPLISTRVSLRKTRQPPERIASGAITKGVVLDSTEALCLAISRNSEQMASHSAVLEAGKNLYTFCVSYVDSIQQMRNKFAFREAINKLENNLRELQICPATAGSGPAATQDFSKLLSSVKEISDIVQR

Macaca mulatta (Rhesus macaque)

2.7.10.2

CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000256|ARBA:ARBA00001149, ECO:0000256|RuleBase:RU362096};

ATP-binding;Cytoplasm;Kinase;Nucleotide-binding;Reference proteome;SH2 domain;SH3 domain;Transferase;Tyrosine-protein kinase

actin cytoskeleton organization [GO:0030036]; activated T cell proliferation [GO:0050798]; alpha-beta T cell differentiation [GO:0046632]; B cell proliferation involved in immune response [GO:0002322]; B cell receptor signaling pathway [GO:0050853]; B-1 B cell homeostasis [GO:0001922]; Bergmann glial cell differentiation [GO:0060020]; BMP signaling pathway [GO:0030509]; canonical NF-kappaB signal transduction [GO:0007249]; cell-cell adhesion [GO:0098609]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to lipopolysaccharide [GO:0071222]; cellular senescence [GO:0090398]; cerebellum morphogenesis [GO:0021587]; circulatory system development [GO:0072359]; DN4 thymocyte differentiation [GO:1904157]; DNA conformation change [GO:0071103]; endothelial cell migration [GO:0043542]; epidermal growth factor receptor signaling pathway [GO:0007173]; ERK1 and ERK2 cascade [GO:0070371]; establishment of localization in cell [GO:0051649]; integrin-mediated signaling pathway [GO:0007229]; microspike assembly [GO:0030035]; negative regulation of BMP signaling pathway [GO:0030514]; negative regulation of cell-cell adhesion [GO:0022408]; negative regulation of cellular senescence [GO:2000773]; negative regulation of double-strand break repair via homologous recombination [GO:2000042]; negative regulation of endothelial cell apoptotic process [GO:2000352]; negative regulation of ERK1 and ERK2 cascade [GO:0070373]; negative regulation of long-term synaptic potentiation [GO:1900272]; negative regulation of mitotic cell cycle [GO:0045930]; neural tube closure [GO:0001843]; neuroepithelial cell differentiation [GO:0060563]; neuromuscular process controlling balance [GO:0050885]; neuron apoptotic process [GO:0051402]; neuron differentiation [GO:0030182]; neuropilin signaling pathway [GO:0038189]; phagocytosis [GO:0006909]; phosphorylation [GO:0016310]; platelet-derived growth factor receptor-beta signaling pathway [GO:0035791]; positive regulation of blood vessel branching [GO:1905555]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of cell migration involved in sprouting angiogenesis [GO:0090050]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of establishment of T cell polarity [GO:1903905]; positive regulation of focal adhesion assembly [GO:0051894]; positive regulation of interleukin-2 production [GO:0032743]; positive regulation of mitotic cell cycle [GO:0045931]; positive regulation of neuron apoptotic process [GO:0043525]; positive regulation of osteoblast proliferation [GO:0033690]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of release of sequestered calcium ion into cytosol [GO:0051281]; positive regulation of stress fiber assembly [GO:0051496]; positive regulation of substrate adhesion-dependent cell spreading [GO:1900026]; positive regulation of T cell migration [GO:2000406]; positive regulation of type II interferon production [GO:0032729]; positive regulation of Wnt signaling pathway, planar cell polarity pathway [GO:2000096]; post-embryonic development [GO:0009791]; protein localization to cytoplasmic microtubule plus-end [GO:1904518]; regulation of axon extension [GO:0030516]; regulation of Cdc42 protein signal transduction [GO:0032489]; regulation of extracellular matrix organization [GO:1903053]; regulation of microtubule polymerization [GO:0031113]; regulation of modification of synaptic structure [GO:1905244]; regulation of T cell differentiation [GO:0045580]; signal transduction in response to DNA damage [GO:0042770]; spleen development [GO:0048536]; substrate adhesion-dependent cell spreading [GO:0034446]; T cell receptor signaling pathway [GO:0050852]; thymus development [GO:0048538]; transitional one stage B cell differentiation [GO:0002333]

actin cytoskeleton [GO:0015629]; cell leading edge [GO:0031252]; cytosol [GO:0005829]; nuclear body [GO:0016604]; nucleolus [GO:0005730]; perinuclear region of cytoplasm [GO:0048471]; protein-containing complex [GO:0032991]

actin filament binding [GO:0051015]; ATP binding [GO:0005524]; bubble DNA binding [GO:0000405]; ephrin receptor binding [GO:0046875]; four-way junction DNA binding [GO:0000400]; magnesium ion binding [GO:0000287]; manganese ion binding [GO:0030145]; mitogen-activated protein kinase binding [GO:0051019]; neuropilin binding [GO:0038191]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; phosphotyrosine residue binding [GO:0001784]; proline-rich region binding [GO:0070064]; protein kinase C binding [GO:0005080]; protein self-association [GO:0043621]; protein tyrosine kinase activity [GO:0004713]; sequence-specific double-stranded DNA binding [GO:1990837]; SH2 domain binding [GO:0042169]; SH3 domain binding [GO:0017124]; syntaxin binding [GO:0019905]

IPR035837;IPR015015;IPR011009;IPR000719;IPR017441;IPR001245;IPR000980;IPR036860;IPR036028;IPR001452;IPR008266;IPR020635;

1.20.120.330;3.30.505.10;2.30.30.40;1.10.510.10;

A0A1D5R142

MTMCLWLKLLAFVFAFLDTEVFVTGQGSTLSPTGRRTTKMPSVPLSSDPLPTHTTAFSPASISERENDFSETTPSLSSDNTSTHVSPDSLDNASAFNTTGVSSALTPHLPTHADSQTPSTGTDTQTPSGSAANTTLSPTPRSNDISDVPGERSTASTFPTDPISPLATTLIPARNSSAALPARTSNTTITANTSVSYLNASETTTPSPSGSTVISTPTIATTTSKPTCAEKYATIPVDYLYNNKTKLFTAKLNVNENVECTNNNHTHNICTNNEVLNLPECKEMNVFVSHNSCTDRHKELKLDVPPEVEKFQLDDCTPDVEANTTICLKWKIIETFACDKSKITYRFQCGNKTYNKEGIYLENLEPEYEYKCDSEILYNNHKYINITKLIKTDFGIPGQPQNVVCRHEDAHQGVITWNPPQRSFHNFTLCYVSKTAKKCLSLDKHLTTYHLQNLKPYTNYSLSLHAYIIAKVQRNGTAATCNFTTESAPPSQVQNMIVSTSDNSMRVKCEAPRDVNGPTELYLLEVEAGNTLVRNLSQSECDFSVNNLQYSTYYNLKAYYHNGKYSGEPVILRESTSYNSKALIAFLAFLIIVTSIALLVVLYKIYDLHKKRSCNLDEQQELVERDDEKQLMNVEPIHADILLETYKRKIADEGRLFLAEFQSIPRVFSKFPIKEARKPFNQNKNRYVDILPYDYNRVELSEINGDAGSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSMEEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVEYNQFGETEVNLSELHPYLHNMKKRDPPSEPSPLEAEFQRLPSYRSWRTQHIGNQEENKNKNRNSNVIPYDYNRVPLKHELEMSKESDHDSDESSDDDSDSEEPSKYINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYWGEGKQTYGDIEVDMKDTNKSSTYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELVSLIQVLKEKLPQKNSSEGNKHHKSTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDIIASTYPAQNGQVKKNNHQEDKIEFDNEVDKVKQDANCVNPLGATEKLPEAKEQATGSEPTSGTEGPEHSVNGPASPALNQGS

Macaca mulatta (Rhesus macaque)

3.1.3.48

CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000256|ARBA:ARBA00001490};

Glycoprotein;Hydrolase;Membrane;Protein phosphatase;Reference proteome;Signal;Transmembrane;Transmembrane helix

alpha-beta T cell proliferation [GO:0046633]; B cell differentiation [GO:0030183]; B cell proliferation [GO:0042100]; B cell receptor signaling pathway [GO:0050853]; bone marrow development [GO:0048539]; calcium-mediated signaling using intracellular calcium source [GO:0035584]; cell cycle phase transition [GO:0044770]; cellular response to extracellular stimulus [GO:0031668]; defense response to virus [GO:0051607]; dephosphorylation [GO:0016311]; extrinsic apoptotic signaling pathway [GO:0097191]; gamma-delta T cell differentiation [GO:0042492]; hematopoietic progenitor cell differentiation [GO:0002244]; heterotypic cell-cell adhesion [GO:0034113]; leukocyte cell-cell adhesion [GO:0007159]; MAPK cascade [GO:0000165]; natural killer cell differentiation [GO:0001779]; negative regulation of cell adhesion involved in substrate-bound cell migration [GO:0006933]; negative regulation of cytokine-mediated signaling pathway [GO:0001960]; negative regulation of ERK1 and ERK2 cascade [GO:0070373]; negative regulation of interleukin-2 production [GO:0032703]; negative regulation of peptidyl-tyrosine phosphorylation [GO:0050732]; negative regulation of protein autophosphorylation [GO:0031953]; negative regulation of T cell mediated cytotoxicity [GO:0001915]; negative thymic T cell selection [GO:0045060]; plasma membrane raft distribution [GO:0044855]; positive regulation of alpha-beta T cell proliferation [GO:0046641]; positive regulation of antigen receptor-mediated signaling pathway [GO:0050857]; positive regulation of B cell proliferation [GO:0030890]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of extrinsic apoptotic signaling pathway [GO:2001238]; positive regulation of Fc receptor mediated stimulatory signaling pathway [GO:0060369]; positive regulation of gamma-delta T cell differentiation [GO:0045588]; positive regulation of hematopoietic stem cell migration [GO:2000473]; positive regulation of humoral immune response mediated by circulating immunoglobulin [GO:0002925]; positive regulation of interleukin-2 production [GO:0032743]; positive regulation of isotype switching to IgG isotypes [GO:0048304]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of phagocytosis [GO:0050766]; positive regulation of stem cell proliferation [GO:2000648]; positive regulation of T cell mediated cytotoxicity [GO:0001916]; positive regulation of tumor necrosis factor production [GO:0032760]; positive thymic T cell selection [GO:0045059]; regulation of cell cycle [GO:0051726]; regulation of interleukin-8 production [GO:0032677]; regulation of receptor signaling pathway via JAK-STAT [GO:0046425]; release of sequestered calcium ion into cytosol [GO:0051209]; stem cell development [GO:0048864]; synaptic membrane adhesion [GO:0099560]; T cell receptor signaling pathway [GO:0050852]

bleb [GO:0032059]; external side of plasma membrane [GO:0009897]; focal adhesion [GO:0005925]; membrane raft [GO:0045121]

ankyrin binding [GO:0030506]; heparan sulfate proteoglycan binding [GO:0043395]; heparin binding [GO:0008201]; protein kinase binding [GO:0019901]; protein tyrosine phosphatase activity [GO:0004725]; signaling receptor binding [GO:0005102]; spectrin binding [GO:0030507]

IPR003961;IPR036116;IPR013783;IPR029021;IPR000242;IPR024739;IPR016335;IPR016130;IPR003595;IPR000387;

2.60.40.10;3.90.190.10;

A0A1D5R152

MLSGKKAAAAAAAAAAAAAGTEAGPGTAGGSENGSEVAAQPAGLSGPAEVGPGAAGERTPRKKEPPRASPPGGLAEPPGSAGPQAGPTVVPGSATPMETGIAETPEGRRTSRRKRAKVEYREMDESLANLSEDEYYSEEERNAKAEKEKKLPPPPPQAPPEEENESEPEEPSGQAGGLQDDSSGGYGDGQASGVEGAAFQSRLPHDRMTSQEAACFPDIISGPQQTQKVFLFIRNRTLQLWLDNPKIQLTFEATLQQLEAPYNSDTVLVHRVHSYLERHGLINFGIYKRIKPLPTKKTGKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRKGNYVADLGAMVVTGLGGNPMAVVSKQVNMELAKIKQKCPLYEANGQAVPKEKDEMVEQEFNRLLEATSYLSHQLDFNVLNNKPVSLGQALEVVIQLQEKHVKDEQIEHWKKIVKTQEELKELLNKMVNLKEKIKELHQQYKEASEVKPPRDITAEFLVKSKHRDLTALCKEYDELAETQGKLEEKLQELEANPPSDVYLSSRDRQILDWHFANLEFANATPLSTLSLKHWDQDDDFEFTGSHLTVRNGYSCVPVALAEGLDIKLNTAVRQVRYTASGCEVIAVNTRSTSQTFIYKCDAVLCTLPLGVLKQQPPAVQFVPPLPEWKTSAVQRMGFGNLNKVVLCFDRVFWDPSVNLFGHVGSTTASRGELFLFWNLYKAPILLALVAGEAAGIMENISDDVIVGRCLAILKGIFGSSAVPQPKETVVSRWRADPWARGSYSYVAAGSSGNDYDLMAQPITPGPSIPGAPQPIPRLFFAGEHTIRNYPATVHGALLSGLREAGRIADQFLGAMYTLPRQATPGVPAQQSPSM

Macaca mulatta (Rhesus macaque)

FUNCTION: Histone demethylase that can demethylate both 'Lys-4' (H3K4me) and 'Lys-9' (H3K9me) of histone H3, thereby acting as a coactivator or a corepressor, depending on the context. Acts by oxidizing the substrate by FAD to generate the corresponding imine that is subsequently hydrolyzed. Acts as a corepressor by mediating demethylation of H3K4me, a specific tag for epigenetic transcriptional activation. Demethylates both mono- (H3K4me1) and di-methylated (H3K4me2) H3K4me. May play a role in the repression of neuronal genes. Alone, it is unable to demethylate H3K4me on nucleosomes and requires the presence of RCOR1/CoREST to achieve such activity. {ECO:0000256|PIRNR:PIRNR038051}.

1.14.99.66

CATALYTIC ACTIVITY: Reaction=2 A + 2 H2O + N(6),N(6)-dimethyl-L-lysyl(4)-[histone H3] = 2 AH2 + 2 formaldehyde + L-lysyl(4)-[histone H3]; Xref=Rhea:RHEA:60244, Rhea:RHEA-COMP:15540, Rhea:RHEA-COMP:15547, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:16842, ChEBI:CHEBI:17499, ChEBI:CHEBI:29969, ChEBI:CHEBI:61976; EC=1.14.99.66; Evidence={ECO:0000256|PIRNR:PIRNR038051};

COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000256|ARBA:ARBA00001974, ECO:0000256|PIRNR:PIRNR038051, ECO:0000256|PIRSR:PIRSR038051-1};

Chromatin regulator;Coiled coil;FAD;Flavoprotein;Nucleus;Oxidoreductase;Reference proteome;Repressor;Transcription;Transcription regulation

cellular response to gamma radiation [GO:0071480]; cellular response to UV [GO:0034644]; DNA repair-dependent chromatin remodeling [GO:0140861]; negative regulation of DNA damage response, signal transduction by p53 class mediator [GO:0043518]; negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator [GO:1902166]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of neuroblast proliferation [GO:0002052]; positive regulation of protein ubiquitination [GO:0031398]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of DNA methylation-dependent heterochromatin formation [GO:0090308]; regulation of double-strand break repair via homologous recombination [GO:0010569]; regulation of protein localization [GO:0032880]

chromatin [GO:0000785]; chromosome, telomeric region [GO:0000781]; DNA repair complex [GO:1990391]; nucleoplasm [GO:0005654]

chromatin binding [GO:0003682]; enzyme binding [GO:0019899]; FAD-dependent H3K4me/H3K4me3 demethylase activity [GO:0140682]; flavin adenine dinucleotide binding [GO:0050660]; histone H3K9 demethylase activity [GO:0032454]; identical protein binding [GO:0042802]; MRF binding [GO:0043426]; nuclear androgen receptor binding [GO:0050681]; nuclear receptor coactivator activity [GO:0030374]; oxidoreductase activity [GO:0016491]; p53 binding [GO:0002039]; telomeric repeat-containing RNA binding [GO:0061752]

SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR038051}.

DOMAIN: The SWIRM domain may act as an anchor site for a histone tail. {ECO:0000256|PIRNR:PIRNR038051}.

IPR002937;IPR036188;IPR017366;IPR009057;IPR007526;IPR036388;

3.90.660.10;1.10.287.80;3.50.50.60;1.10.10.10;

A0A1D5R1C7

MDISPQCFSILLVLCIFIQSSAHGQSLKPEPFGRRAQAVETNKTLHEMKTRFLLFGETNQGCQIRINHLDTLQECGFNSSRPLVMIIHGWSVDGLLENWIWQMVAALKSQPAQPVNVGLVDWITLAHHHYTIAVRNTRLVGKEVAALLRWLEESVQFSRSHVHLIGYSLGAHVSGFAGSSIGGTRKIGRITGLDAAGPLFEGSSPSNRLSPDDANFVDAIHTFTREHMGLSVGIKQPIGHYDFYPNGGSFQPGCHFLELYRHIAKHGLNAASRSCGEDAGSGGAEGTRHTQCPTITQTIKCSHERSVHLFIDSLLHAGTQSVAYLCSDMDSFSQGLCLSCKKGRCNTLGYHVRQEPRSKSKKLFLVTRAQSPFKVYHYQFKIQFINQTETPIQTTFTMSLLGTKEKMQKIAITLGKGIASNKTYSFLITLDVDIGELIMIKFKWESSAVWANVWNTVQTIIPWSTGPRHPGLVLKTIRVKAGETQQRMTFCSENTDDLQLRPTQEKIFVKCEIKSKTSKQKIR

Macaca mulatta (Rhesus macaque)

3.1.1.3; 3.1.1.32; 3.1.1.5

CATALYTIC ACTIVITY: Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + 2,3-di-(9Z)-octadecenoyl-sn-glycerol + H(+); Xref=Rhea:RHEA:38391, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:53753, ChEBI:CHEBI:75824; Evidence={ECO:0000256|ARBA:ARBA00001610}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38392; Evidence={ECO:0000256|ARBA:ARBA00001610}; CATALYTIC ACTIVITY: Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + di-(9Z)-octadecenoylglycerol + H(+); Xref=Rhea:RHEA:38575, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:53753, ChEBI:CHEBI:75945; Evidence={ECO:0000256|ARBA:ARBA00000652}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38576; Evidence={ECO:0000256|ARBA:ARBA00000652}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = (9Z)-octadecenoate + (9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:38699, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:74669, ChEBI:CHEBI:76083; Evidence={ECO:0000256|ARBA:ARBA00001885}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38700; Evidence={ECO:0000256|ARBA:ARBA00001885}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycerol + H2O = (9Z)-octadecenoate + 2-(9Z-octadecenoyl)-glycerol + H(+); Xref=Rhea:RHEA:38511, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:52333, ChEBI:CHEBI:73990; Evidence={ECO:0000256|ARBA:ARBA00001101}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38512; Evidence={ECO:0000256|ARBA:ARBA00001101}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) + hexadecanoate + hexadecanoyl-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:41384, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:64563, ChEBI:CHEBI:72999; Evidence={ECO:0000256|ARBA:ARBA00000879}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41385; Evidence={ECO:0000256|ARBA:ARBA00000879}; CATALYTIC ACTIVITY: Reaction=1,3-di-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + 3-(9Z-octadecenoyl)-sn-glycerol + H(+); Xref=Rhea:RHEA:38651, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:75735, ChEBI:CHEBI:75938; Evidence={ECO:0000256|ARBA:ARBA00000265}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38652; Evidence={ECO:0000256|ARBA:ARBA00000265}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine + H2O = (9Z)-octadecenoate + H(+) + sn-glycero-3-phospho-L-serine; Xref=Rhea:RHEA:40499, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:64765, ChEBI:CHEBI:74617; Evidence={ECO:0000256|ARBA:ARBA00000834}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40500; Evidence={ECO:0000256|ARBA:ARBA00000834}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) + hexadecanoate + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40435, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:72998; Evidence={ECO:0000256|ARBA:ARBA00000597}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436; Evidence={ECO:0000256|ARBA:ARBA00000597}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:18689, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:57875; EC=3.1.1.32; Evidence={ECO:0000256|ARBA:ARBA00000111}; CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5; Evidence={ECO:0000256|ARBA:ARBA00000960}; CATALYTIC ACTIVITY: Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3; Evidence={ECO:0000256|ARBA:ARBA00001024};

Calcium;HDL;Heparin-binding;Metal-binding;Reference proteome;Secreted;Signal

cholesterol homeostasis [GO:0042632]; cholesterol metabolic process [GO:0008203]; cholesterol transport [GO:0030301]; fatty acid biosynthetic process [GO:0006633]; high-density lipoprotein particle remodeling [GO:0034375]; low-density lipoprotein particle remodeling [GO:0034374]; triglyceride catabolic process [GO:0019433]; triglyceride homeostasis [GO:0070328]; very-low-density lipoprotein particle remodeling [GO:0034372]

extracellular space [GO:0005615]; high-density lipoprotein particle [GO:0034364]

1-acyl-2-lysophosphatidylserine acylhydrolase activity [GO:0052740]; apolipoprotein binding [GO:0034185]; heparin binding [GO:0008201]; lipoprotein lipase activity [GO:0004465]; lysophospholipase activity [GO:0004622]; metal ion binding [GO:0046872]; phosphatidyl phospholipase B activity [GO:0102545]; phosphatidylserine 1-acylhydrolase activity [GO:0052739]; phospholipase A1 activity [GO:0008970]

SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.

IPR029058;IPR013818;IPR002333;IPR016272;IPR033906;IPR001024;IPR036392;IPR000734;

3.40.50.1820;2.60.60.20;

A0A1D5R1I4

MSGGLRGRHGQQQRSWAEVPGRAGAERRGKQGLGGGRGAAASAASPRAAAAAAQRAPGPPAAASTRRAAAPGPAPAAAAAMGNAAAAKKGSEQESVKEFLAKAKEDFLKKWESPAQNTAHLDQFERIKTLGTGSFGRVMLVKHKETGNHYAMKILDKQKVVKLKQIEHTLNEKRILQAVNFPFLVKLEFSFKDNSNLYMVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDQQGYIQVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVNDIKNHKWFATTDWIAIYQRKVEAPFIPKFKGPGDTSNFDDYEEEEIRVSINEKCGKEFSEF

Macaca mulatta (Rhesus macaque)

2.7.11.11

CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.11; Evidence={ECO:0000256|ARBA:ARBA00001036}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.11; Evidence={ECO:0000256|ARBA:ARBA00000541};

ATP-binding;cAMP;Kinase;Lipoprotein;Mitochondrion;Myristate;Nucleotide-binding;Reference proteome;Serine/threonine-protein kinase;Transferase

adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; cellular response to cold [GO:0070417]; cellular response to glucagon stimulus [GO:0071377]; cellular response to glucose stimulus [GO:0071333]; cellular response to heat [GO:0034605]; cellular response to parathyroid hormone stimulus [GO:0071374]; mesoderm formation [GO:0001707]; mRNA processing [GO:0006397]; negative regulation of glycolytic process through fructose-6-phosphate [GO:1904539]; negative regulation of smoothened signaling pathway [GO:0045879]; negative regulation of TORC1 signaling [GO:1904262]; neural tube closure [GO:0001843]; phosphorylation [GO:0016310]; positive regulation of gluconeogenesis [GO:0045722]; positive regulation of insulin secretion [GO:0032024]; positive regulation of protein export from nucleus [GO:0046827]; postsynaptic modulation of chemical synaptic transmission [GO:0099170]; protein export from nucleus [GO:0006611]; protein kinase A signaling [GO:0010737]; protein localization to lipid droplet [GO:1990044]; regulation of bicellular tight junction assembly [GO:2000810]; regulation of cell cycle [GO:0051726]; regulation of osteoblast differentiation [GO:0045667]; regulation of proteasomal protein catabolic process [GO:0061136]; regulation of protein processing [GO:0070613]; sperm capacitation [GO:0048240]

acrosomal vesicle [GO:0001669]; axoneme [GO:0005930]; cAMP-dependent protein kinase complex [GO:0005952]; centrosome [GO:0005813]; ciliary base [GO:0097546]; cytosol [GO:0005829]; dendritic spine [GO:0043197]; glutamatergic synapse [GO:0098978]; mitochondrion [GO:0005739]; neuromuscular junction [GO:0031594]; nuclear speck [GO:0016607]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane raft [GO:0044853]; sperm flagellum [GO:0036126]

AMP-activated protein kinase activity [GO:0004679]; ATP binding [GO:0005524]; cAMP-dependent protein kinase activity [GO:0004691]; magnesium ion binding [GO:0000287]; manganese ion binding [GO:0030145]; protein domain specific binding [GO:0019904]; protein kinase A regulatory subunit binding [GO:0034237]; protein kinase binding [GO:0019901]; protein serine kinase activity [GO:0106310]; protein serine/threonine/tyrosine kinase activity [GO:0004712]; ubiquitin protein ligase binding [GO:0031625]

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Membrane {ECO:0000256|ARBA:ARBA00004635}; Lipid-anchor {ECO:0000256|ARBA:ARBA00004635}. Mitochondrion {ECO:0000256|ARBA:ARBA00004173}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.

IPR000961;IPR011009;IPR000719;IPR017441;IPR008271;IPR044109;

1.10.510.10;

A0A1D5R5B1

MISPFLVLAIGTCLTNSLVPEKEKDPKYWRDQAQETLKYALELQKLNTNVAKNVIMFLGDGMGVSTVTATRILKGQLHHNPGEETRLEMDKFPFVALSKTYNTNAQVPDSAGTATAYLCGVKANEGTVGVSAATERSRCNTTQGNEVTSILRWAKDAGKSVGIVTTTRVNHATPSAAYAHSADRDWYSDNEMPPEALSQGCKDIAYQLVHNIRDIDVIMGGGRKYMYPKNKTDVEYEIDEKARGTRLDGLDLVNIWKSFKPRHKHSHFIWNRTELLTLDPHNVDYLLGLFEPGDMEYELNRNNVTDPSLSEMVVVAIQILRKNPKGFFLLVEGGRIDHGHHEGKAKQALHEAVEMDRAIGQAGSMTSLEDTLTVVTADHSHVFTFGGYTPRGNSIFGLAPMLSDTDKKPFTAILYGNGPGYKVVGGERENVSMVDYAHNNYQAQSAVPLRHETHGGEDVAVFSKGPMAHLLHGVHEQNYIPHVMAYAACIGANLDHCAPASSAGSLAAGPLLLPLALFPLSILF

Macaca mulatta (Rhesus macaque)

3.1.3.1

CATALYTIC ACTIVITY: Reaction=ADP + H2O = AMP + H(+) + phosphate; Xref=Rhea:RHEA:61436, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00036139}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61437; Evidence={ECO:0000256|ARBA:ARBA00036139}; CATALYTIC ACTIVITY: Reaction=AMP + H2O = adenosine + phosphate; Xref=Rhea:RHEA:29375, ChEBI:CHEBI:15377, ChEBI:CHEBI:16335, ChEBI:CHEBI:43474, ChEBI:CHEBI:456215; Evidence={ECO:0000256|ARBA:ARBA00036923}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29376; Evidence={ECO:0000256|ARBA:ARBA00036923}; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00034440}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066; Evidence={ECO:0000256|ARBA:ARBA00034440}; CATALYTIC ACTIVITY: Reaction=H2O + N-phosphocreatine = creatine + phosphate; Xref=Rhea:RHEA:12977, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57947, ChEBI:CHEBI:58092; EC=3.9.1.1; Evidence={ECO:0000256|ARBA:ARBA00036122}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12978; Evidence={ECO:0000256|ARBA:ARBA00036122}; CATALYTIC ACTIVITY: Reaction=H2O + phosphoethanolamine = ethanolamine + phosphate; Xref=Rhea:RHEA:16089, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57603, ChEBI:CHEBI:58190; Evidence={ECO:0000256|ARBA:ARBA00036048}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16090; Evidence={ECO:0000256|ARBA:ARBA00036048}; CATALYTIC ACTIVITY: Reaction=H2O + pyridoxal 5'-phosphate = phosphate + pyridoxal; Xref=Rhea:RHEA:20533, ChEBI:CHEBI:15377, ChEBI:CHEBI:17310, ChEBI:CHEBI:43474, ChEBI:CHEBI:597326; Evidence={ECO:0000256|ARBA:ARBA00035851}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20534; Evidence={ECO:0000256|ARBA:ARBA00035851}; CATALYTIC ACTIVITY: Reaction=a phosphate monoester + H2O = an alcohol + phosphate; Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.1; Evidence={ECO:0000256|ARBA:ARBA00036105}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15018; Evidence={ECO:0000256|ARBA:ARBA00036105}; CATALYTIC ACTIVITY: Reaction=diphosphate + H2O = H(+) + 2 phosphate; Xref=Rhea:RHEA:24576, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474; Evidence={ECO:0000256|ARBA:ARBA00035865}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24577; Evidence={ECO:0000256|ARBA:ARBA00035865};

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|PIRSR:PIRSR601952-2}; Note=Binds 1 Mg(2+) ion. {ECO:0000256|PIRSR:PIRSR601952-2}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|PIRSR:PIRSR601952-2}; Note=Binds 2 Zn(2+) ions. {ECO:0000256|PIRSR:PIRSR601952-2};

Cell membrane;Disulfide bond;Glycoprotein;GPI-anchor;Hydrolase;Lipoprotein;Magnesium;Membrane;Metal-binding;Phosphoprotein;Reference proteome;Signal;Zinc

bone mineralization [GO:0030282]; calcium ion homeostasis [GO:0055074]; cellular homeostasis [GO:0019725]; cellular response to organic cyclic compound [GO:0071407]; dephosphorylation [GO:0016311]; developmental process involved in reproduction [GO:0003006]; endochondral ossification [GO:0001958]; futile creatine cycle [GO:0140651]; inhibition of non-skeletal tissue mineralization [GO:0140928]; phosphate ion homeostasis [GO:0055062]; positive regulation of cold-induced thermogenesis [GO:0120162]; pyridoxal phosphate metabolic process [GO:0042822]; response to antibiotic [GO:0046677]; response to sodium phosphate [GO:1904383]; response to vitamin B6 [GO:0034516]; response to vitamin D [GO:0033280]

extracellular matrix [GO:0031012]; extracellular membrane-bounded organelle [GO:0065010]; mitochondrial intermembrane space [GO:0005758]; mitochondrial membrane [GO:0031966]; plasma membrane [GO:0005886]; side of membrane [GO:0098552]

alkaline phosphatase activity [GO:0004035]; calcium ion binding [GO:0005509]; phosphoamidase activity [GO:0050187]; phosphoethanolamine phosphatase activity [GO:0052732]; pyridoxal phosphatase activity [GO:0033883]; pyrophosphatase activity [GO:0016462]

SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}. Extracellular vesicle membrane {ECO:0000256|ARBA:ARBA00037828}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00037828}. Membrane {ECO:0000256|ARBA:ARBA00004589}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004589}. Mitochondrion intermembrane space {ECO:0000256|ARBA:ARBA00004569}. Mitochondrion membrane {ECO:0000256|ARBA:ARBA00037800}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00037800}.

IPR001952;IPR018299;IPR017850;

3.40.720.10;

A0A1D5R8E9

MAGAASPCANGCGPGAPSDAEVLHLCRSLEVGTVMTLFYSKKSQRPERKTFQVKLETRQITWSRGADKIEGAIDIREIKEIRPGKTSRDFDRYQEDPAFRPDQSHCFVILYGMEFRLKTLSLQATSEDEVNMWIKGLTWLMEDTLQAPTPLQIERWLRKQFYSVDRNREDRISAKDLKNMLSQVNYRVPNMRFLRERLTDLEQRSGDITYGQFAQLYRSLMYSAQKTMDLPFLEASTLRAGERPELCRVSLPEFQQFLLDYQGELWAVDRLQVQEFMLSFLRDPLREIEEPYFFLDEFVTFLFSKENSVWNSQLDAVCPDTMNNPLSHYWISSSHNTYLTGDQFSSESSLEAYARCLRMGCRCIELDCWDGPDGMPVIYHGHTLTTKIKFSDVLQTIKEHAFVASEYPVILSIEDHCSIAQQRNMAQHFKKVLGDTLLTKPVEISADGLPSPNQLKRKILIKHKKLAEGSAYEEVPTSMMYSENDISNSIKNGILYLEDPVNHEWYPHYFVLTSSKIYYSEETSSDQGNEDEEEPKEVSSSTELHSNEKWFHGKLGAGRDGRHIAERLLTEYCIETGAPDGSFLVRESETFVGDYTLSFWRNGKVQHCRIHSRQDAGTPKFFLTDNLVFDSLYDLITHYQQVPLRCNEFEMRLSEPVPQTNAHESKEWYHASLTRAQAEHMLMRVPRDGAFLVRKRNEPNSYAISFRAEGKIKHCRVQQEGQTVMLGNSEFDSLVDLISYYEKHPLYRKMKLRYPINEEALEKIGTAEPDYGALYEGRNPGFYVEANPMPTFKCAVKALFDYKAQREDELTFTKSAIIQNVEKQEGGWWRGDYGGKKQLWFPSNYVEEMVNPVALEPEREHLDENSPLGDLLRGVLDVPACQIAIRPEGKNNRLFVFSISMASVAHWSLDVAADSQEELQDWVKKIREVAQTADARLTEGKIMERRKKIALELSELVVYCRPVPFDEEKIGTERACYRDMSSFPETKAEKYVNKAKGKKFLQYNRLQLSRIYPKGQRLDSSNYDPLPMWICGSQLVALNFQTPDKPMQMNQALFMTGRHCGYVLQPSTMRDEAFDPFDKSSLRGLEPCAISVEVLGARHLPKNGRGIVCPFVEIEVAGAEYDSTKQKTEFVVDNGLNPVWPAKPFHFQISNPEFAFLRFVVYEEDMFSDQNFLAQATFPVKGLKTGYRAVPLKNNYSEDLELASLLIKIDIFPAKQENGDLSPFSGTSLRERGSDASGQLFHGRAREGSFESRYQQPFEDFRVSQEHLADHFDSRERRAPRRTRVNGDNRL

Macaca mulatta (Rhesus macaque)

FUNCTION: Mediates the production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3). Plays an important role in the regulation of intracellular signaling cascades. {ECO:0000256|PIRNR:PIRNR000952}.

3.1.4.11

CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + H2O = 1D-myo-inositol 1,4,5-trisphosphate + a 1,2-diacyl-sn-glycerol + H(+); Xref=Rhea:RHEA:33179, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:58456, ChEBI:CHEBI:203600; EC=3.1.4.11; Evidence={ECO:0000256|ARBA:ARBA00023674}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33180; Evidence={ECO:0000256|ARBA:ARBA00023674};

COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000256|ARBA:ARBA00001913};

Calcium;Hydrolase;Lipid degradation;Lipid metabolism;Metal-binding;Phosphoprotein;Reference proteome;Repeat;SH2 domain;SH3 domain;Transducer

calcium-mediated signaling [GO:0019722]; cell migration [GO:0016477]; cellular response to epidermal growth factor stimulus [GO:0071364]; epidermal growth factor receptor signaling pathway [GO:0007173]; in utero embryonic development [GO:0001701]; modulation of chemical synaptic transmission [GO:0050804]; phosphatidylinositol metabolic process [GO:0046488]; phosphatidylinositol-mediated signaling [GO:0048015]; phospholipid catabolic process [GO:0009395]; positive regulation of angiogenesis [GO:0045766]; positive regulation of blood vessel endothelial cell migration [GO:0043536]; positive regulation of endothelial cell apoptotic process [GO:2000353]; positive regulation of epithelial cell migration [GO:0010634]; positive regulation of release of sequestered calcium ion into cytosol [GO:0051281]; positive regulation of vascular endothelial cell proliferation [GO:1905564]; release of sequestered calcium ion into cytosol [GO:0051209]; T cell receptor signaling pathway [GO:0050852]

cell-cell junction [GO:0005911]; COP9 signalosome [GO:0008180]; cytosol [GO:0005829]; glutamatergic synapse [GO:0098978]; lamellipodium [GO:0030027]; ruffle membrane [GO:0032587]; Schaffer collateral - CA1 synapse [GO:0098685]

calcium ion binding [GO:0005509]; glutamate receptor binding [GO:0035254]; neurotrophin TRKA receptor binding [GO:0005168]; phosphatidylinositol phospholipase C activity [GO:0004435]; receptor tyrosine kinase binding [GO:0030971]

IPR000008;IPR035892;IPR011992;IPR018247;IPR002048;IPR011993;IPR001849;IPR001192;IPR016279;IPR035023;IPR035024;IPR017946;IPR035724;IPR000909;IPR001711;IPR000980;IPR036860;IPR036028;IPR001452;

2.60.40.150;3.20.20.190;2.30.29.30;3.30.505.10;2.30.30.40;

A0A1D5R8U8

MPLNRGPQMHASRACKCTGVGWGGGLLCFFFSGVLGGPKASAALGLNAGNRSPRVPARSNGGPLGSVRSSQDPERGMSEPRSWSLLEQLGLAGADLAAPGVQQQLELERERLRREIRKELKLKEGAENLRRATTDLGRSLGPVELLLRGSSRRLDLLHQQLQELHAHVVLPDPAATHDGPQSPGAGGPTCSATNLSRVAGLEKQLAIELKVKQGAENMIQTYSNGSTKDRKLLLTAQQMLQDSKTKIDIIRMQLRRALQAGQLENQAAPDETQGSPDLGAVELRIEELRHHFRVEHAVAEGAKNVLRLLSAAKAPDRKAVSEAQEKLTESNQKLGLLREALERRLGELPADHPKGRLLREELAAASSAAFSARLAGPFPATHYSTLCKPAPLTGTLEVRVVGCRDLPETIPWNPTPSGGGPGTPDSRPPFLSRPARGLYSRSGSLSGRSSLKADAENTSEVSTVLKLDNTVVGQTSWKPCGPSAWDQSFTLELERARELELAVFWRDQRGLCALKFLKLEDFLDNERHEVQLDMEPQGCLVAEVTFRNPVIERIPRLRRQKKIFSKQQGKAFQRARQMNIDVATWVRLLRRLIPNATGTGTFSPGASPGSEARTTGDISVEKLNLGTDSDGSPQKSSRDPPSRLSSLSSPIQESSITPKLPSETQETPGPALCSPLRKSPLTLEDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILAAVTNAGHPFLVNLFGCFQTPEHVCFVMEYSAGGDLMLHIHSDVFSEPRAVFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKITDFGLCKEGMGYGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSAEAIGIMRRLLRRNPERRLGSSERDAEDVKKQPFFRTLGWEALLARRLPPPFVPTLSGRTDVSNFDEEFTGEAPTLSPPRDARPLTAAEQAAFLDFDFVAGGC

Macaca mulatta (Rhesus macaque)

2.7.11.13

CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.13; Evidence={ECO:0000256|ARBA:ARBA00000946}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.13; Evidence={ECO:0000256|ARBA:ARBA00000569};

ATP-binding;Coiled coil;Cytoplasm;Kinase;Nucleotide-binding;Nucleus;Phosphoprotein;Reference proteome;Repeat;Serine/threonine-protein kinase;Transcription;Transcription regulation;Transferase

B cell apoptotic process [GO:0001783]; B cell homeostasis [GO:0001782]; epithelial cell migration [GO:0010631]; hyperosmotic response [GO:0006972]; intracellular signal transduction [GO:0035556]; negative regulation of B cell proliferation [GO:0030889]; negative regulation of protein phosphorylation [GO:0001933]; phosphorylation [GO:0016310]; post-translational protein modification [GO:0043687]; regulation of cell motility [GO:2000145]; regulation of germinal center formation [GO:0002634]; regulation of immunoglobulin production [GO:0002637]; regulation of transcription by RNA polymerase II [GO:0006357]; renal system process [GO:0003014]; spleen development [GO:0048536]

cleavage furrow [GO:0032154]; endosome [GO:0005768]; midbody [GO:0030496]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]

ATP binding [GO:0005524]; chromatin binding [GO:0003682]; diacylglycerol-dependent serine/threonine kinase activity [GO:0004697]; histone binding [GO:0042393]; histone deacetylase binding [GO:0042826]; histone H3T11 kinase activity [GO:0035402]; nuclear androgen receptor binding [GO:0050681]; nuclear receptor coactivator activity [GO:0030374]; protein kinase C binding [GO:0005080]; protein serine/threonine kinase activity [GO:0004674]; small GTPase binding [GO:0031267]

SUBCELLULAR LOCATION: Cleavage furrow {ECO:0000256|ARBA:ARBA00004626}. Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Midbody {ECO:0000256|ARBA:ARBA00004214}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.

IPR000961;IPR000008;IPR035892;IPR037784;IPR011072;IPR036274;IPR011009;IPR017892;IPR037317;IPR037313;IPR000719;IPR017441;IPR008271;

1.10.287.160;1.10.510.10;

A0A1D5R9B8

MGAASGRQGPGPLLQPLLLLLLLPPQPALALDPGLQPGNFSADEAGAQLFAQSYNSSAEQVLFQSVAASWAHDTNITAENARRQEEAALLSQEFAEAWGQKAKELYEPIWQNFTDPELRKIIGAVGTLGSANLPLAKRQQYNALLSNMSRIYSTAKVCLPNKTATCWSLDPDLTNILASSRSYAMLLFAWEGWHNAAGIPLKPLYEDFTALSNEAYKQDGFTDTGAYWRSWYNSPTFEDDLEHLYQQLEPLYLNLHAFVRRALHRRYGDRYINLRGPIPAHLLGDMWAQSWENIYDMVVPFPDKPNLDVTSTMLQQGWNATHMFRVAEEFFTSLELSPMPPEFWEGSMLEKPADGREVVCHASAWDFYNRKDFRIKQCTRVTMDQLSTVHHEMGHIQYYLQYKDLPVSLRGGANPGFHEAIGDVLALSVSTPAHLHKIGLLDHVTNDTESDINYLLKMALEKIAFLPFGYLVDQWRWGVFNGRTPPSHYNFDWWYLRTKYQGICPPVTRNETHFDAGAKFHVPNVTPYIRYFVSFVLQFQFHEALCKEAGYEGPLHQCDIYQSTKAGAKLRKVLQAGSSRPWQEVLKDMVGSDALDAQPLLNYFQPVTQWLQEQNRQNGEVLGWPEYQWRPPLPDNYPEGIDLVTDEAEASKFVEEYDRTSQVVWNEYAEANWNYNTNITTETSKILLQKNMQIANHTLKYGTQARRFDVNHFQNTTIKRIIKKVQDLERAALPAQELEEYNKILLDMETTYSVATVCHTNGSCLQLEPDLTNVMATSRKYEELLWAWEGWRDKAGRAILQFYPKYVELINQAARLNGYVDAGDSWRSMYETPSLEQDLERLFQELQPLYLNLHAYVRRALHRHYGAQHINLEGPIPAHLLGNMWAQTWSNIYDLVVPFPSAPSMDPTEAMLKQGWTPRRMFKEADDFFTSLGLLPVPPEFWNKSMLEKPTDGREVVCHASAWDFYNGKDFRIKQCTTVNLEDLVVAHHEMGHIQYFMQYKDLPVALREGANPGFHEAIGDVLALSVSTPKHLHSLNLLSSEGGSHEHDINFLMKMALDKIAFIPFSYLVDQWRWRVFDGSITKENYNQEWWSLRLKYQGLCPPVPRTQGDFDPGAKFHVPSSVPYIRYFISFIIQFQFHEALCQAAGHTGPLHKCDIYQSKEAGQRLATAMKLGFSRPWPEAMQLITGQPNMSASAMLSYFKPLLDWLRTENELHGEKLGWPQYNWTPNSARSEGPLPDSGRVSFLGLDLDAQQARVGQWLLLFLGIALLVATLGLSQRLFSIRHQSLHQHPQGPQFGSEVELRHS

Macaca mulatta (Rhesus macaque)

FUNCTION: Soluble form that is released in blood plasma and other body fluids following proteolytic cleavage in the juxtamembrane stalk region. {ECO:0000256|ARBA:ARBA00037200}.

3.4.-.-

CATALYTIC ACTIVITY: Reaction=H2O + Leu-enkephalin = L-phenylalanyl-L-leucine + L-tyrosylglycylglycine; Xref=Rhea:RHEA:71487, ChEBI:CHEBI:15377, ChEBI:CHEBI:190689, ChEBI:CHEBI:190708, ChEBI:CHEBI:190710; Evidence={ECO:0000256|ARBA:ARBA00037024}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71488; Evidence={ECO:0000256|ARBA:ARBA00037024}; CATALYTIC ACTIVITY: Reaction=H2O + Met-enkephalin = L-phenylalanyl-L-methionine + L-tyrosylglycylglycine; Xref=Rhea:RHEA:71483, ChEBI:CHEBI:15377, ChEBI:CHEBI:189868, ChEBI:CHEBI:190708, ChEBI:CHEBI:190709; Evidence={ECO:0000256|ARBA:ARBA00036262}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71484; Evidence={ECO:0000256|ARBA:ARBA00036262}; CATALYTIC ACTIVITY: Reaction=H2O + Met-enkephalin-Arg-Phe = L-arginyl-L-phenylalanine + Met-enkephalin; Xref=Rhea:RHEA:70675, ChEBI:CHEBI:15377, ChEBI:CHEBI:189868, ChEBI:CHEBI:189869, ChEBI:CHEBI:189870; Evidence={ECO:0000256|ARBA:ARBA00036091}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70676; Evidence={ECO:0000256|ARBA:ARBA00036091}; CATALYTIC ACTIVITY: Reaction=H2O + neurotensin = L-isoleucyl-L-leucine + neurotensin(1-11); Xref=Rhea:RHEA:71475, ChEBI:CHEBI:15377, ChEBI:CHEBI:147362, ChEBI:CHEBI:190704, ChEBI:CHEBI:190706; Evidence={ECO:0000256|ARBA:ARBA00034019}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71476; Evidence={ECO:0000256|ARBA:ARBA00034019}; CATALYTIC ACTIVITY: Reaction=H2O + substance P = Gly-L-Leu-L-Met-NH2 + substance P(1-8); Xref=Rhea:RHEA:71463, ChEBI:CHEBI:15377, ChEBI:CHEBI:190692, ChEBI:CHEBI:190694, ChEBI:CHEBI:190699; Evidence={ECO:0000256|ARBA:ARBA00035850}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71464; Evidence={ECO:0000256|ARBA:ARBA00035850}; CATALYTIC ACTIVITY: Reaction=H2O + substance P = L-Leu-L-Met-NH2 + substance P(1-9); Xref=Rhea:RHEA:71459, ChEBI:CHEBI:15377, ChEBI:CHEBI:190692, ChEBI:CHEBI:190693, ChEBI:CHEBI:190700; Evidence={ECO:0000256|ARBA:ARBA00034071}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71460; Evidence={ECO:0000256|ARBA:ARBA00034071}; CATALYTIC ACTIVITY: Reaction=H2O + substance P = L-Phe-L-Phe-Gly-L-Leu-L-Met-NH2 + substance P(1-6); Xref=Rhea:RHEA:71471, ChEBI:CHEBI:15377, ChEBI:CHEBI:190692, ChEBI:CHEBI:190696, ChEBI:CHEBI:190697; Evidence={ECO:0000256|ARBA:ARBA00036862}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71472; Evidence={ECO:0000256|ARBA:ARBA00036862}; CATALYTIC ACTIVITY: Reaction=Release of a C-terminal dipeptide, oligopeptide-|-Xaa-Yaa, when Xaa is not Pro, and Yaa is neither Asp nor Glu. Thus, conversion of angiotensin I to angiotensin II, with increase in vasoconstrictor activity, but no action on angiotensin II.; EC=3.4.15.1; Evidence={ECO:0000256|ARBA:ARBA00036868}; CATALYTIC ACTIVITY: Reaction=angiotensin I + H2O = angiotensin II + L-histidyl-L-leucine; Xref=Rhea:RHEA:63560, ChEBI:CHEBI:15377, ChEBI:CHEBI:58506, ChEBI:CHEBI:147350, ChEBI:CHEBI:147392; EC=3.4.15.1; Evidence={ECO:0000256|ARBA:ARBA00036030}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63561; Evidence={ECO:0000256|ARBA:ARBA00036030}; CATALYTIC ACTIVITY: Reaction=bradykinin + H2O = bradykinin(1-7) + L-Phe-L-Arg; Xref=Rhea:RHEA:71451, ChEBI:CHEBI:15377, ChEBI:CHEBI:132988, ChEBI:CHEBI:133147, ChEBI:CHEBI:147352; Evidence={ECO:0000256|ARBA:ARBA00035977}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71452; Evidence={ECO:0000256|ARBA:ARBA00035977}; CATALYTIC ACTIVITY: Reaction=goralatide + H2O = L-lysyl-L-proline + N-acetyl-L-seryl-L-aspartate; Xref=Rhea:RHEA:71455, ChEBI:CHEBI:15377, ChEBI:CHEBI:190701, ChEBI:CHEBI:190702, ChEBI:CHEBI:190703; Evidence={ECO:0000256|ARBA:ARBA00036673}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71456; Evidence={ECO:0000256|ARBA:ARBA00036673};

COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|RuleBase:RU361144}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|RuleBase:RU361144}; COFACTOR: Name=chloride; Xref=ChEBI:CHEBI:17996; Evidence={ECO:0000256|ARBA:ARBA00001923};

Carboxypeptidase;Disulfide bond;Glycoprotein;Hydrolase;Membrane;Metal-binding;Metalloprotease;Protease;Reference proteome;Repeat;Signal;Transmembrane;Transmembrane helix;Zinc

amyloid-beta metabolic process [GO:0050435]; angiotensin maturation [GO:0002003]; angiotensin-activated signaling pathway [GO:0038166]; arachidonic acid secretion [GO:0050482]; bradykinin catabolic process [GO:0010815]; cell proliferation in bone marrow [GO:0071838]; heart contraction [GO:0060047]; hormone catabolic process [GO:0042447]; kidney development [GO:0001822]; male gonad development [GO:0008584]; negative regulation of gap junction assembly [GO:1903597]; negative regulation of gene expression [GO:0010629]; neutrophil mediated immunity [GO:0002446]; positive regulation of peptidyl-cysteine S-nitrosylation [GO:2000170]; positive regulation of systemic arterial blood pressure [GO:0003084]; post-transcriptional regulation of gene expression [GO:0010608]; regulation of angiotensin metabolic process [GO:0060177]; regulation of heart rate by cardiac conduction [GO:0086091]; regulation of hematopoietic stem cell proliferation [GO:1902033]; regulation of synaptic plasticity [GO:0048167]; regulation of systemic arterial blood pressure by renin-angiotensin [GO:0003081]; spermatogenesis [GO:0007283]; substance P catabolic process [GO:0010814]

endosome [GO:0005768]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; lysosome [GO:0005764]; plasma membrane [GO:0005886]

bradykinin receptor binding [GO:0031711]; carboxypeptidase activity [GO:0004180]; chloride ion binding [GO:0031404]; metallodipeptidase activity [GO:0070573]; metalloendopeptidase activity [GO:0004222]; metallopeptidase activity [GO:0008237]; mitogen-activated protein kinase binding [GO:0051019]; mitogen-activated protein kinase kinase binding [GO:0031434]; peptidyl-dipeptidase activity [GO:0008241]; tripeptidyl-peptidase activity [GO:0008240]; zinc ion binding [GO:0008270]

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}. Secreted {ECO:0000256|ARBA:ARBA00004613}.

IPR001548;

1.10.1370.30;

A0A1D5R9U8

MEHIQGAWKTISNGFGFKDAVFDGSSCISPTIVQQFGYQRRASDDGKLTDPSKTSNTIRVFLPNKQRTVVNVRNGMSLHDCLMKALKVRGLQPECCAVFRLLHEHKGKKARLDWNTDAASLIGEELQVDFLDHVPLTTHNFARKTFLKLAFCDICQKFLLNGFRCQTCGYKFHEHCSTKVPTMCVDWSNIRQLLLFPNSTIGDSGVPALPSLTMRRMRESVSRMPVSSQHRYSTPHAFTFNTSSPSSEGSLSQRQRSTSTPNVHMVSTTLPVDSRMIENNSLNASPRAWSRRFCLRGRDAIRSHSESASPSALSSSPNNLSPTGWSQPKTPVPAQRERAPVSGTQEKNKIRPRGQRDSSYYWEIEASEVMLSTRIGSGSFGTVYKGKWHGDVAVKILKVVDPTPEQFQAFRNEVAVLRKTRHVNILLFMGYMTKDNLAIVTQWCEGSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRWSGSQQVEQPTGSVLWMAPEVIRMQDNNPFSFQSDVYSYGIVLYELMTGELPYSHINNRDQIIFMVGRGYASPDLSKLYKNCPKAMKRLVADCVKKVKEERPLFPQILSSIELLQHSLPKINRSASEPSLHRAAHTEDINACTLTTSPRLPVF

Macaca mulatta (Rhesus macaque)

2.7.11.1

ATP-binding;Kinase;Metal-binding;Nucleotide-binding;Phosphoprotein;Reference proteome;Serine/threonine-protein kinase;Transferase;Zinc

death-inducing signaling complex assembly [GO:0071550]; ERBB2-ERBB3 signaling pathway [GO:0038133]; extrinsic apoptotic signaling pathway via death domain receptors [GO:0008625]; face development [GO:0060324]; insulin receptor signaling pathway [GO:0008286]; insulin secretion involved in cellular response to glucose stimulus [GO:0035773]; insulin-like growth factor receptor signaling pathway [GO:0048009]; intermediate filament cytoskeleton organization [GO:0045104]; MAPK cascade [GO:0000165]; myelination [GO:0042552]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of extrinsic apoptotic signaling pathway via death domain receptors [GO:1902042]; negative regulation of protein-containing complex assembly [GO:0031333]; neurotrophin TRK receptor signaling pathway [GO:0048011]; phosphorylation [GO:0016310]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein modification process [GO:0036211]; Ras protein signal transduction [GO:0007265]; response to muscle stretch [GO:0035994]; Schwann cell development [GO:0014044]; somatic stem cell population maintenance [GO:0035019]; thymus development [GO:0048538]; thyroid gland development [GO:0030878]; type B pancreatic cell proliferation [GO:0044342]

cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886]; pseudopodium [GO:0031143]

ATP binding [GO:0005524]; identical protein binding [GO:0042802]; MAP kinase kinase kinase activity [GO:0004709]; metal ion binding [GO:0046872]; small GTPase binding [GO:0031267]

SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.

IPR046349;IPR020454;IPR011009;IPR002219;IPR000719;IPR017441;IPR003116;IPR008271;IPR029071;

3.30.60.20;1.10.510.10;

A0A1D5RAG6

MGLHLRPCRVGLLPDGLLFLLLLLMLLADPALPAGRHPPVVLVPGDLGNQLEAKLDKPTVVHYLCSKKTESYFTIWLNLELLLPVIIDCWIDNIRLVYNKTSRATQFPDGVDVRVPGFGKTFSLEFLDPSKSSVGSYFHTMVESLVGWGYTRGEDVRGAPYDWRRAPNENGPYFLALREMIEEMYQLYGGPVVLVAHSMGNMYTLYFLQRQPQAWKDKYIRAFVSLGAPWGGVAKTLRVLASGDNNRIPVIGPLKIREQQRSAVSTSWLLPYSYTWSPEKVFVQTPTTNYTLRDYRRFFQDIGFEDGWLMRQDTEGLVEATMPPGVQLHCLYGTGVPTPDSFYYESFPDRDPKICFGDGDGTVNLKSALQCQAWQSLQEHQVLLQELPGSEHIEMLANATTLAYLKRVLLGP

Macaca mulatta (Rhesus macaque)

3.1.1.32; 3.1.1.4; 3.1.1.5

CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + 1-(9Z-octadecenoyl)-sn-glycerol = (9Z-octadecenoyl)-sn-glycero-3-phosphocholine + 1,3-di-(9Z-octadecenoyl)-glycerol; Xref=Rhea:RHEA:38739, ChEBI:CHEBI:74669, ChEBI:CHEBI:75735, ChEBI:CHEBI:75757, ChEBI:CHEBI:76083; Evidence={ECO:0000256|ARBA:ARBA00036246}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38740; Evidence={ECO:0000256|ARBA:ARBA00036246}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + 1-O-hexadecyl-2-O-methyl-sn-glycerol = (9Z-octadecenoyl)-sn-glycero-3-phosphocholine + 1-O-hexadecyl-2-O-methyl-3-(9Z)-octadecenoyl-sn-glycerol; Xref=Rhea:RHEA:38723, ChEBI:CHEBI:74669, ChEBI:CHEBI:76063, ChEBI:CHEBI:76064, ChEBI:CHEBI:76083; Evidence={ECO:0000256|ARBA:ARBA00036334}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38724; Evidence={ECO:0000256|ARBA:ARBA00036334}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + 1-O-hexadecyl-2-acetyl-sn-glycerol = (9Z-octadecenoyl)-sn-glycero-3-phosphocholine + 1-O-hexadecyl-2-acetyl-3-(9Z)-octadecenoyl-sn-glycerol; Xref=Rhea:RHEA:38707, ChEBI:CHEBI:74669, ChEBI:CHEBI:75936, ChEBI:CHEBI:76055, ChEBI:CHEBI:76083; Evidence={ECO:0000256|ARBA:ARBA00036286}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38708; Evidence={ECO:0000256|ARBA:ARBA00036286}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + 1-O-hexadecylglycerol = (9Z-octadecenoyl)-sn-glycero-3-phosphocholine + 1-O-hexadecyl-3-(9Z)-octadecenoylglycerol; Xref=Rhea:RHEA:38711, ChEBI:CHEBI:74669, ChEBI:CHEBI:76061, ChEBI:CHEBI:76062, ChEBI:CHEBI:76083; Evidence={ECO:0000256|ARBA:ARBA00036488}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38712; Evidence={ECO:0000256|ARBA:ARBA00036488}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + 1-hexadecanoyl-sn-glycerol = (9Z-octadecenoyl)-sn-glycero-3-phosphocholine + 1-hexadecanoyl-3-(9Z)-octadecenoyl-sn-glycerol; Xref=Rhea:RHEA:38727, ChEBI:CHEBI:74669, ChEBI:CHEBI:75542, ChEBI:CHEBI:75868, ChEBI:CHEBI:76083; Evidence={ECO:0000256|ARBA:ARBA00035806}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38728; Evidence={ECO:0000256|ARBA:ARBA00035806}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + 2-hexadecanoylglycerol = (9Z-octadecenoyl)-sn-glycero-3-phosphocholine + 1-(9Z)-octadecenoyl-2-hexadecanoylglycerol; Xref=Rhea:RHEA:38735, ChEBI:CHEBI:74669, ChEBI:CHEBI:75455, ChEBI:CHEBI:76065, ChEBI:CHEBI:76083; Evidence={ECO:0000256|ARBA:ARBA00036773}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38736; Evidence={ECO:0000256|ARBA:ARBA00036773}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + 3-(9Z-octadecenoyl)-sn-glycerol = (9Z-octadecenoyl)-sn-glycero-3-phosphocholine + 1,3-di-(9Z-octadecenoyl)-glycerol; Xref=Rhea:RHEA:38743, ChEBI:CHEBI:74669, ChEBI:CHEBI:75735, ChEBI:CHEBI:75938, ChEBI:CHEBI:76083; Evidence={ECO:0000256|ARBA:ARBA00036060}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38744; Evidence={ECO:0000256|ARBA:ARBA00036060}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + 3-hexadecanoyl-sn-glycerol = (9Z-octadecenoyl)-sn-glycero-3-phosphocholine + 1-(9Z)-octadecenoyl-3-hexadecanoyl-sn-glycerol; Xref=Rhea:RHEA:38731, ChEBI:CHEBI:64757, ChEBI:CHEBI:74669, ChEBI:CHEBI:75867, ChEBI:CHEBI:76083; Evidence={ECO:0000256|ARBA:ARBA00036450}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38732; Evidence={ECO:0000256|ARBA:ARBA00036450}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = (9Z)-octadecenoate + (9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:38699, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:74669, ChEBI:CHEBI:76083; Evidence={ECO:0000256|ARBA:ARBA00001885}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38700; Evidence={ECO:0000256|ARBA:ARBA00001885}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine = (9Z-octadecenoyl)-sn-glycero-3-phosphocholine + 2-[(5Z,8Z,11Z,14Z)-eicosatetraenoylamino]ethyl (9Z)-octadecenoate; Xref=Rhea:RHEA:38751, ChEBI:CHEBI:2700, ChEBI:CHEBI:74669, ChEBI:CHEBI:76070, ChEBI:CHEBI:76083; Evidence={ECO:0000256|ARBA:ARBA00036812}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38752; Evidence={ECO:0000256|ARBA:ARBA00036812}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + N-(9Z-octadecenoyl) ethanolamine = (9Z-octadecenoyl)-sn-glycero-3-phosphocholine + 2-[(9Z)-octadecenoylamino]ethyl (9Z)-octadecenoate; Xref=Rhea:RHEA:38747, ChEBI:CHEBI:71466, ChEBI:CHEBI:74669, ChEBI:CHEBI:76068, ChEBI:CHEBI:76083; Evidence={ECO:0000256|ARBA:ARBA00036160}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38748; Evidence={ECO:0000256|ARBA:ARBA00036160}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + N-(acetyl)-sphing-4-enine = 1-(9Z-octadecenoyl)-N-(acetyl)-sphing-4-enine + 1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:38703, ChEBI:CHEBI:28610, ChEBI:CHEBI:46979, ChEBI:CHEBI:74669, ChEBI:CHEBI:76054; Evidence={ECO:0000256|ARBA:ARBA00036964}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38704; Evidence={ECO:0000256|ARBA:ARBA00036964}; CATALYTIC ACTIVITY: Reaction=1-(9Z)-octadecenoyl-2-octadecanoyl-sn-glycero-3-phosphocholine + N-(acetyl)-sphing-4-enine = 1-(9Z-octadecenoyl)-N-(acetyl)-sphing-4-enine + 2-octadecanoyl-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:38791, ChEBI:CHEBI:46979, ChEBI:CHEBI:76054, ChEBI:CHEBI:76073, ChEBI:CHEBI:76076; Evidence={ECO:0000256|ARBA:ARBA00036379}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38792; Evidence={ECO:0000256|ARBA:ARBA00036379}; CATALYTIC ACTIVITY: Reaction=1-(9Z)-octadecenoyl-2-octadecanoyl-sn-glycero-3-phosphocholine + N-(acetyl)-sphing-4-enine = 1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + 1-octadecanoyl-N-(acetyl)-sphing-4-enine; Xref=Rhea:RHEA:38803, ChEBI:CHEBI:28610, ChEBI:CHEBI:46979, ChEBI:CHEBI:76073, ChEBI:CHEBI:76074; Evidence={ECO:0000256|ARBA:ARBA00036555}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38804; Evidence={ECO:0000256|ARBA:ARBA00036555}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-2-hexadecanoyl-sn-glycero-3-phosphocholine + N-(acetyl)-sphing-4-enine = 1-(9Z-octadecenoyl)-N-(acetyl)-sphing-4-enine + 2-hexadecanoyl-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:38767, ChEBI:CHEBI:46979, ChEBI:CHEBI:74667, ChEBI:CHEBI:76054, ChEBI:CHEBI:76078; Evidence={ECO:0000256|ARBA:ARBA00036618}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38768; Evidence={ECO:0000256|ARBA:ARBA00036618}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-2-hexadecanoyl-sn-glycero-3-phosphocholine + N-(acetyl)-sphing-4-enine = 1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + 1-hexadecanoyl-N-(acetyl)-sphing-4-enine; Xref=Rhea:RHEA:38763, ChEBI:CHEBI:28610, ChEBI:CHEBI:46979, ChEBI:CHEBI:74667, ChEBI:CHEBI:76077; Evidence={ECO:0000256|ARBA:ARBA00035794}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38764; Evidence={ECO:0000256|ARBA:ARBA00035794}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycero-3-phosphocholine + N-(acetyl)-sphing-4-enine = 1-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-N-(acetyl)-sphing-4-enine + 1-hexadecanoyl-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:38819, ChEBI:CHEBI:46979, ChEBI:CHEBI:72998, ChEBI:CHEBI:74963, ChEBI:CHEBI:76087; Evidence={ECO:0000256|ARBA:ARBA00036476}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38820; Evidence={ECO:0000256|ARBA:ARBA00036476}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycero-3-phosphocholine + N-(acetyl)-sphing-4-enine = 1-hexadecanoyl-N-(acetyl)-sphing-4-enine + 2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:38815, ChEBI:CHEBI:46979, ChEBI:CHEBI:74963, ChEBI:CHEBI:76077, ChEBI:CHEBI:76085; Evidence={ECO:0000256|ARBA:ARBA00035942}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38816; Evidence={ECO:0000256|ARBA:ARBA00035942}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(5-oxopentanoyl)-sn-glycero-3-phosphocholine + H2O = 2-(5-oxopentanoyl)-sn-glycero-3-phosphocholine + H(+) + hexadecanoate; Xref=Rhea:RHEA:62484, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:77890, ChEBI:CHEBI:145782; Evidence={ECO:0000256|ARBA:ARBA00036251}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62485; Evidence={ECO:0000256|ARBA:ARBA00036251}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine + N-(acetyl)-sphing-4-enine = 1-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-N-(acetyl)-sphing-4-enine + 1-hexadecanoyl-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:38771, ChEBI:CHEBI:46979, ChEBI:CHEBI:72998, ChEBI:CHEBI:73003, ChEBI:CHEBI:76080; Evidence={ECO:0000256|ARBA:ARBA00036327}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38772; Evidence={ECO:0000256|ARBA:ARBA00036327}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine + N-(acetyl)-sphing-4-enine = 1-hexadecanoyl-N-(acetyl)-sphing-4-enine + 2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:38775, ChEBI:CHEBI:46979, ChEBI:CHEBI:73003, ChEBI:CHEBI:76077, ChEBI:CHEBI:76079; Evidence={ECO:0000256|ARBA:ARBA00036198}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38776; Evidence={ECO:0000256|ARBA:ARBA00036198}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphoethanolamine + N-(acetyl)-sphing-4-enine = 1-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-N-(acetyl)-sphing-4-enine + 1-hexadecanoyl-sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:38839, ChEBI:CHEBI:46979, ChEBI:CHEBI:73004, ChEBI:CHEBI:73009, ChEBI:CHEBI:76080; Evidence={ECO:0000256|ARBA:ARBA00035931}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38840; Evidence={ECO:0000256|ARBA:ARBA00035931}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphoethanolamine + N-(acetyl)-sphing-4-enine = 1-hexadecanoyl-N-(acetyl)-sphing-4-enine + 2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:38843, ChEBI:CHEBI:46979, ChEBI:CHEBI:73009, ChEBI:CHEBI:76077, ChEBI:CHEBI:76091; Evidence={ECO:0000256|ARBA:ARBA00036513}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38844; Evidence={ECO:0000256|ARBA:ARBA00036513}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9-oxononanoyl)-sn-glycero-3-phosphocholine + H2O = 2-(9-oxononanoyl)-sn-glycero-3-phosphocholine + H(+) + hexadecanoate; Xref=Rhea:RHEA:62488, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:61042, ChEBI:CHEBI:145783; Evidence={ECO:0000256|ARBA:ARBA00035944}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62489; Evidence={ECO:0000256|ARBA:ARBA00035944}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphocholine + N-(acetyl)-sphing-4-enine = 1-(9Z,12Z-octadecadienoyl)-N-acetylsphing-4-enine + 1-hexadecanoyl-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:38807, ChEBI:CHEBI:46979, ChEBI:CHEBI:72998, ChEBI:CHEBI:73002, ChEBI:CHEBI:76086; Evidence={ECO:0000256|ARBA:ARBA00036046}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38808; Evidence={ECO:0000256|ARBA:ARBA00036046}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphocholine + N-(acetyl)-sphing-4-enine = 1-hexadecanoyl-N-(acetyl)-sphing-4-enine + 2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:38811, ChEBI:CHEBI:46979, ChEBI:CHEBI:73002, ChEBI:CHEBI:76077, ChEBI:CHEBI:76084; Evidence={ECO:0000256|ARBA:ARBA00036613}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38812; Evidence={ECO:0000256|ARBA:ARBA00036613}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphoethanolamine + N-(acetyl)-sphing-4-enine = 1-(9Z,12Z-octadecadienoyl)-N-acetylsphing-4-enine + 1-hexadecanoyl-sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:38835, ChEBI:CHEBI:46979, ChEBI:CHEBI:73004, ChEBI:CHEBI:73008, ChEBI:CHEBI:76086; Evidence={ECO:0000256|ARBA:ARBA00036667}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38836; Evidence={ECO:0000256|ARBA:ARBA00036667}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphoethanolamine + N-(acetyl)-sphing-4-enine = 1-hexadecanoyl-N-(acetyl)-sphing-4-enine + 2-(9Z,12Z)-octadecadienoyl-sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:38831, ChEBI:CHEBI:46979, ChEBI:CHEBI:73008, ChEBI:CHEBI:76077, ChEBI:CHEBI:76090; Evidence={ECO:0000256|ARBA:ARBA00036653}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38832; Evidence={ECO:0000256|ARBA:ARBA00036653}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:38779, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:72998, ChEBI:CHEBI:73001; Evidence={ECO:0000256|ARBA:ARBA00001126}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38780; Evidence={ECO:0000256|ARBA:ARBA00001126}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = 2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H(+) + hexadecanoate; Xref=Rhea:RHEA:38783, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:73001, ChEBI:CHEBI:76071; Evidence={ECO:0000256|ARBA:ARBA00036275}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38784; Evidence={ECO:0000256|ARBA:ARBA00036275}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + N-(acetyl)-sphing-4-enine = 1-(9Z-octadecenoyl)-N-(acetyl)-sphing-4-enine + 1-hexadecanoyl-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:38755, ChEBI:CHEBI:46979, ChEBI:CHEBI:72998, ChEBI:CHEBI:73001, ChEBI:CHEBI:76054; Evidence={ECO:0000256|ARBA:ARBA00036333}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38756; Evidence={ECO:0000256|ARBA:ARBA00036333}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + N-(acetyl)-sphing-4-enine = 1-hexadecanoyl-N-(acetyl)-sphing-4-enine + 2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:38759, ChEBI:CHEBI:46979, ChEBI:CHEBI:73001, ChEBI:CHEBI:76071, ChEBI:CHEBI:76077; Evidence={ECO:0000256|ARBA:ARBA00036331}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38760; Evidence={ECO:0000256|ARBA:ARBA00036331}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + N-(acetyl)-sphing-4-enine = 1-(9Z-octadecenoyl)-N-(acetyl)-sphing-4-enine + 1-hexadecanoyl-sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:38823, ChEBI:CHEBI:46979, ChEBI:CHEBI:73004, ChEBI:CHEBI:73007, ChEBI:CHEBI:76054; Evidence={ECO:0000256|ARBA:ARBA00036629}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38824; Evidence={ECO:0000256|ARBA:ARBA00036629}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + N-(acetyl)-sphing-4-enine = 1-hexadecanoyl-N-(acetyl)-sphing-4-enine + 2-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:38827, ChEBI:CHEBI:46979, ChEBI:CHEBI:73007, ChEBI:CHEBI:76077, ChEBI:CHEBI:76088; Evidence={ECO:0000256|ARBA:ARBA00036571}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38828; Evidence={ECO:0000256|ARBA:ARBA00036571}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-glutaroyl-sn-glycero-3-phosphocholine + H2O = 2-glutaroyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate; Xref=Rhea:RHEA:62480, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:77756, ChEBI:CHEBI:145781; Evidence={ECO:0000256|ARBA:ARBA00036312}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62481; Evidence={ECO:0000256|ARBA:ARBA00036312}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-nonadioyl-sn-glycero-3-phosphocholine + H2O = 2-nonadioyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate; Xref=Rhea:RHEA:62464, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:78207, ChEBI:CHEBI:145780; Evidence={ECO:0000256|ARBA:ARBA00036098}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62465; Evidence={ECO:0000256|ARBA:ARBA00036098}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-nonadioyl-sn-glycero-3-phosphocholine + N-(acetyl)-sphing-4-enine = 1-hexadecanoyl-N-(acetyl)-sphing-4-enine + 2-nonadioyl-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:62472, ChEBI:CHEBI:46979, ChEBI:CHEBI:76077, ChEBI:CHEBI:78207, ChEBI:CHEBI:145780; Evidence={ECO:0000256|ARBA:ARBA00036069}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62473; Evidence={ECO:0000256|ARBA:ARBA00036069}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) + hexadecanoate + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40435, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:72998; Evidence={ECO:0000256|ARBA:ARBA00000597}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436; Evidence={ECO:0000256|ARBA:ARBA00000597}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine + N-(acetyl)-sphing-4-enine = 1-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-N-(acetyl)-sphing-4-enine + 1-octadecanoyl-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:57116, ChEBI:CHEBI:46979, ChEBI:CHEBI:73858, ChEBI:CHEBI:74965, ChEBI:CHEBI:76080; Evidence={ECO:0000256|ARBA:ARBA00036713}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57117; Evidence={ECO:0000256|ARBA:ARBA00036713}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine + N-(acetyl)-sphing-4-enine = 1-octadecanoyl-N-(acetyl)-sphing-4-enine + 2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:57120, ChEBI:CHEBI:46979, ChEBI:CHEBI:74965, ChEBI:CHEBI:76074, ChEBI:CHEBI:76079; Evidence={ECO:0000256|ARBA:ARBA00036902}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57121; Evidence={ECO:0000256|ARBA:ARBA00036902}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(9Z,12Z)-octadecadienoyl-sn-glycero-3-phosphocholine + N-(acetyl)-sphing-4-enine = 1-(9Z,12Z-octadecadienoyl)-N-acetylsphing-4-enine + 1-octadecanoyl-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:57108, ChEBI:CHEBI:46979, ChEBI:CHEBI:73858, ChEBI:CHEBI:76086, ChEBI:CHEBI:84822; Evidence={ECO:0000256|ARBA:ARBA00035904}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57109; Evidence={ECO:0000256|ARBA:ARBA00035904}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-sn-glycerol) + N-(acetyl)-sphing-4-enine = 1-(9Z-octadecenoyl)-N-(acetyl)-sphing-4-enine + 1-octadecanoyl-sn-glycero-3-phospho-(1'-sn-glycerol); Xref=Rhea:RHEA:57148, ChEBI:CHEBI:46979, ChEBI:CHEBI:72827, ChEBI:CHEBI:72845, ChEBI:CHEBI:76054; Evidence={ECO:0000256|ARBA:ARBA00035877}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57149; Evidence={ECO:0000256|ARBA:ARBA00035877}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-sn-glycerol) + N-(acetyl)-sphing-4-enine = 1-octadecanoyl-N-(acetyl)-sphing-4-enine + 2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-sn-glycerol); Xref=Rhea:RHEA:57144, ChEBI:CHEBI:46979, ChEBI:CHEBI:72845, ChEBI:CHEBI:76074, ChEBI:CHEBI:141490; Evidence={ECO:0000256|ARBA:ARBA00035951}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57145; Evidence={ECO:0000256|ARBA:ARBA00035951}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine + N-(acetyl)-sphing-4-enine = 1-(9Z-octadecenoyl)-N-(acetyl)-sphing-4-enine + 1-octadecanoyl-sn-glycero-3-phosphoserine; Xref=Rhea:RHEA:57136, ChEBI:CHEBI:46979, ChEBI:CHEBI:76054, ChEBI:CHEBI:78260, ChEBI:CHEBI:84467; Evidence={ECO:0000256|ARBA:ARBA00036442}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57137; Evidence={ECO:0000256|ARBA:ARBA00036442}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine + N-(acetyl)-sphing-4-enine = 1-octadecanoyl-N-(acetyl)-sphing-4-enine + 2-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine; Xref=Rhea:RHEA:57140, ChEBI:CHEBI:46979, ChEBI:CHEBI:76074, ChEBI:CHEBI:77342, ChEBI:CHEBI:78260; Evidence={ECO:0000256|ARBA:ARBA00035838}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57141; Evidence={ECO:0000256|ARBA:ARBA00035838}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + N-(acetyl)-sphing-4-enine = 1-(9Z-octadecenoyl)-N-(acetyl)-sphing-4-enine + 1-octadecanoyl-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:38795, ChEBI:CHEBI:46979, ChEBI:CHEBI:73858, ChEBI:CHEBI:75034, ChEBI:CHEBI:76054; Evidence={ECO:0000256|ARBA:ARBA00036148}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38796; Evidence={ECO:0000256|ARBA:ARBA00036148}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + N-(acetyl)-sphing-4-enine = 1-octadecanoyl-N-(acetyl)-sphing-4-enine + 2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:38799, ChEBI:CHEBI:46979, ChEBI:CHEBI:75034, ChEBI:CHEBI:76071, ChEBI:CHEBI:76074; Evidence={ECO:0000256|ARBA:ARBA00036796}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38800; Evidence={ECO:0000256|ARBA:ARBA00036796}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000256|ARBA:ARBA00023422}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802; Evidence={ECO:0000256|ARBA:ARBA00023422}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:18689, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:57875; EC=3.1.1.32; Evidence={ECO:0000256|ARBA:ARBA00036688}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18690; Evidence={ECO:0000256|ARBA:ARBA00036688}; CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5; Evidence={ECO:0000256|ARBA:ARBA00000150}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15178; Evidence={ECO:0000256|ARBA:ARBA00000150};

Hydrolase;Membrane;Reference proteome;Signal;Zinc

ceramide metabolic process [GO:0006672]; diacylglycerol biosynthetic process [GO:0006651]; phosphatidylcholine catabolic process [GO:0034638]; phosphatidylcholine metabolic process [GO:0046470]; phosphatidylethanolamine catabolic process [GO:0046338]; phosphatidylglycerol metabolic process [GO:0046471]; phosphatidylserine metabolic process [GO:0006658]

extracellular space [GO:0005615]; lysosome [GO:0005764]; membrane [GO:0016020]; nucleoplasm [GO:0005654]

acylglycerol O-acyltransferase activity [GO:0016411]; calcium-independent phospholipase A2 activity [GO:0047499]; O-acyltransferase activity [GO:0008374]; phospholipase A1 activity [GO:0008970]; zinc ion binding [GO:0008270]

IPR029058;IPR003386;

3.40.50.1820;

A0A1D5RE99

MVTLRKRTLKVLTFLVLFIFLTSFFLNYSHTMVTTTWFPKQMVLELSENLKRLIKHRPCTCTHCIGQRKLSVWFDERFNQTVQPLLTAQNALLEDDTYRWWLRLQREKKPNNLNDTIKELFRVVPGNVDPMLEKRSVGCRRCAVVGNSGNLRESSYGPEIDRHDFVLRMNKAPTAGFEADVGTKTTHHLVYPESFRELGDNVSMILVPFKTIDLEWVVSATTTGTISHTYVPVPAKIRVKQDKILIYHPAFIKYVFDNWLQGHGRYPSTGILSVIFSMHVCDEVDLYGFGADSKGNWHHYWENNPSAGAFRKTGVHDADFESNVTATLASINKIRIFKGR

Macaca mulatta (Rhesus macaque)

2.4.3.2; 2.4.3.4

CATALYTIC ACTIVITY: Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GM1 (d18:1(4E)/18:0) = CMP + ganglioside GD1a (18:1(4E)/18:0) + H(+); Xref=Rhea:RHEA:48248, ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:73110, ChEBI:CHEBI:90153; Evidence={ECO:0000256|ARBA:ARBA00036879}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48249; Evidence={ECO:0000256|ARBA:ARBA00036879}; CATALYTIC ACTIVITY: Reaction=a beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl derivative + CMP-N-acetyl-beta-neuraminate = an N-acetyl-alpha-neuraminyl-(2->3)-beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl derivative + CMP + H(+); Xref=Rhea:RHEA:21616, ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:133470, ChEBI:CHEBI:139596; EC=2.4.3.4; Evidence={ECO:0000256|ARBA:ARBA00036292}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21617; Evidence={ECO:0000256|ARBA:ARBA00036292}; CATALYTIC ACTIVITY: Reaction=a ganglioside GA1 (d18:1(4E)) + CMP-N-acetyl-beta-neuraminate = a ganglioside GM1b (d18:1(4E)) + CMP + H(+); Xref=Rhea:RHEA:47560, ChEBI:CHEBI:15378, ChEBI:CHEBI:27938, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:78568; Evidence={ECO:0000256|ARBA:ARBA00043673}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47561; Evidence={ECO:0000256|ARBA:ARBA00043673}; CATALYTIC ACTIVITY: Reaction=a ganglioside GA1 + CMP-N-acetyl-beta-neuraminate = a ganglioside GM1b + CMP + H(+); Xref=Rhea:RHEA:48244, ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:88069, ChEBI:CHEBI:90151; Evidence={ECO:0000256|ARBA:ARBA00043816}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48245; Evidence={ECO:0000256|ARBA:ARBA00043816}; CATALYTIC ACTIVITY: Reaction=a ganglioside GM1 (d18:1(4E)) + CMP-N-acetyl-beta-neuraminate = a ganglioside GD1a (d18:1(4E)) + CMP + H(+); Xref=Rhea:RHEA:18021, ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:77709, ChEBI:CHEBI:78445; EC=2.4.3.2; Evidence={ECO:0000256|ARBA:ARBA00043773}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18022; Evidence={ECO:0000256|ARBA:ARBA00043773};

PATHWAY: Glycolipid biosynthesis. {ECO:0000256|ARBA:ARBA00004934}.; PATHWAY: Protein modification; protein glycosylation. {ECO:0000256|ARBA:ARBA00004922}.

Glycoprotein;Glycosyltransferase;Golgi apparatus;Membrane;Reference proteome;Secreted;Signal-anchor;Transferase;Transmembrane;Transmembrane helix

ganglioside biosynthetic process via lactosylceramide [GO:0010706]; memory B cell differentiation [GO:0002319]; negative regulation of activated CD8-positive, alpha-beta T cell apoptotic process [GO:1905403]; protein glycosylation [GO:0006486]; sialylation [GO:0097503]

extracellular region [GO:0005576]; Golgi medial cisterna membrane [GO:1990675]; Golgi trans cisterna membrane [GO:1990676]; membrane [GO:0016020]; trans-Golgi network membrane [GO:0032588]

beta-galactoside (CMP) alpha-2,3-sialyltransferase activity [GO:0003836]

SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000256|ARBA:ARBA00004447}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004447}. Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}. Secreted {ECO:0000256|ARBA:ARBA00004613}.

IPR001675;IPR038578;IPR012163;

3.90.1480.20;

A0A1D5REV0

MPVQAAQWTEFLSCPICYNEFDENVHKPISLGCSHTVCKTCLNKLHRKACPFDQTAINTDIDVLPVNFALLQLVGAQVPDHQSIKLSNLGENKHYEVAKKCVEDLALYLKPLSGGKGVASLNQSALSRPMQRKLVTLVNCQLVEEEGRVRAMRAARSLGERTVTELILQHQNPQQLSANLWAAVRARGCQFLGPAMQEEALKLVLLALEDGSALSRKVLVLFVVQRLEPRFPQASKTSIGHVVQLLYRASCFKVTKRDEDSSLMQLKEEFRSYEALRREHDAQIVHIAMEAGLRISPEQWSSLLYGDLAHKSHMQSIIDKLQSPESFAKSVQELTIVLQRTGDPANLNRLRPHLELLANIDPNPDAVSPTWEQLENAMVAVKTVVHGLVDFIQNYSRKGHETPQPQPNSKYKTSMCRDLRQQGGCPRGTNCTFAHSQEELEKYRLRNKKINATVRTFPLLNKVGVNNTVTTTAGNVISVIGSTETTGKIVPSTNGISNAENSVSQLISRSTDSTLRALETVKKVGKVGTNGQNAAGPSADSVTENKIGSPPKTPVSNVAATSAGPSNVGTELNSVPQKSSPFLTRVPVYPPHSENIQYFQDPRTQIPFEVPQYPQTGYYPPPPTVPAGVAPCVPRFVRSNNVPESSLPPASMPYADHYSTFSPRDRMNSSPYQPPPPQPYGPVPPVPSGMYAPVYDSRRIWRPPMYQRDDIIRSNSLPPMDVMHSSVYQTSLRERYNSLDGYYSVACQPPSEPRTTVPLPREPCGHLKTSCEEQIRRKPDQWAQYHTQKAPLVSSTLPVATQSPTPPSPLFSVDFRADFSESVSGTKFEEDHLSHYSPWSCGTIGSCINAIDSEPKDVIANSNAVLMDLDSGDVKRRVHLFETQRRTKEEDPIIPFSDGPIISKWGAISRSSRTGYHTTDPVQATASQGSATKPISVSDYVPYVNAVDSRWSSYGNEATSSAHYIERDRFIVTDLSGHRKHSSTGDLLSLELQQAKSNSLLLQREANALAMQQKWNSLDEGRHLTLNLLSKEIELRNGELQSDYTEDSTDTKPDRDIELELSALDTDEPDGQSEPIEEILDIQLGISSQNDQLLNGTAVENGHPVQQHQKEPPKQKKQSLGEDHVILEEQKTILPVTSCFSQPLPVSISNASCLPITTSVSVGNLILKTHVMSEDKNDFLKPVANGKMVNS

Macaca mulatta (Rhesus macaque)

2.3.2.27

CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};

Metal-binding;Reference proteome;Transferase;Zinc;Zinc-finger

B cell homeostasis [GO:0001782]; limb development [GO:0060173]; lung alveolus development [GO:0048286]; lymph node development [GO:0048535]; multicellular organism growth [GO:0035264]; negative regulation of T-helper 17 cell differentiation [GO:2000320]; nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:0000288]; positive regulation of non-canonical NF-kappaB signal transduction [GO:1901224]; post-embryonic development [GO:0009791]; protein polyubiquitination [GO:0000209]; regulation of miRNA metabolic process [GO:2000628]; spleen development [GO:0048536]; T cell homeostasis [GO:0043029]; T cell proliferation [GO:0042098]; T cell receptor signaling pathway [GO:0050852]; T follicular helper cell differentiation [GO:0061470]; ubiquitin-dependent protein catabolic process [GO:0006511]

cell surface [GO:0009986]; cytoplasmic stress granule [GO:0010494]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; P-body [GO:0000932]

DNA binding [GO:0003677]; double-stranded RNA binding [GO:0003725]; metal ion binding [GO:0046872]; mRNA binding [GO:0003729]; RNA stem-loop binding [GO:0035613]; ubiquitin protein ligase activity [GO:0061630]

SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000256|ARBA:ARBA00004201}.

IPR041523;IPR048575;IPR000571;IPR036855;IPR001841;IPR013083;IPR017907;

1.20.120.1790;4.10.1000.10;3.30.40.10;

A0A1D5RII7

MSEPKAIDPKLSTTDRVVKAVPFPPSHRLTAKEVFDNDGKPRVDILKAHLMKEGRLEESVALRIITEGASILRQEKNLLDIDAPVTVCGDIHGQFFDLMKLFEVGGSPANTRYLFLGDYVDRGYFSIECVLYLWALKILYPKTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYDACMDAFDCLPLAALMNQQFLCVHGGLSPEINTLDDIRKLDRFKEPPAYGPMCDILWSDPLEDFGNEKTQEHFTHNTVRGCSYFYSYPAVCEFLQHNNLLSILRAHEAQDAGYRMYRKSQTTGFPSLITIFSAPNYLDVYNNKACAVFPPVSLPLCLHSESSARCHSKRSAVLKYENNVMNIRQFNCSPHPYWLPNFMDVFTWSLPFVGEKVTEMLVNVLNICSDDELGSEEDGFDGATAAARKEVIRNKIRAIGKMARVFSVLREESESVLTLKGLTPTGMLPSGVLSGGKQTLQSATVEAIEADEAIKGFSPQHKITSFEEAKGLDRINERMPPRRDAMPSDANLNSINKALTSETNGTDSNGSNSSNIQ

Macaca mulatta (Rhesus macaque)

3.1.3.16

CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; Evidence={ECO:0000256|ARBA:ARBA00001512}; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16; Evidence={ECO:0000256|ARBA:ARBA00001482, ECO:0000256|RuleBase:RU004273};

COFACTOR: Name=Fe(3+); Xref=ChEBI:CHEBI:29034; Evidence={ECO:0000256|ARBA:ARBA00001965}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|ARBA:ARBA00001947};

Calmodulin-binding;Hydrolase;Iron;Metal-binding;Reference proteome

calcineurin-NFAT signaling cascade [GO:0033173]; calcium ion transport [GO:0006816]; cardiac muscle hypertrophy in response to stress [GO:0014898]; dendrite morphogenesis [GO:0048813]; dephosphorylation [GO:0016311]; excitatory postsynaptic potential [GO:0060079]; G1/S transition of mitotic cell cycle [GO:0000082]; keratinocyte differentiation [GO:0030216]; multicellular organismal response to stress [GO:0033555]; negative regulation of angiotensin-activated signaling pathway [GO:0110062]; negative regulation of dendrite morphogenesis [GO:0050774]; negative regulation of gene expression [GO:0010629]; positive regulation of activated T cell proliferation [GO:0042104]; positive regulation of cardiac muscle hypertrophy in response to stress [GO:1903244]; positive regulation of cell migration [GO:0030335]; positive regulation of connective tissue replacement [GO:1905205]; positive regulation of endocytosis [GO:0045807]; positive regulation of gene expression [GO:0010628]; positive regulation of glomerulus development [GO:0090193]; positive regulation of osteoblast differentiation [GO:0045669]; positive regulation of osteoclast differentiation [GO:0045672]; positive regulation of saliva secretion [GO:0046878]; positive regulation of transcription by RNA polymerase II [GO:0045944]; postsynaptic modulation of chemical synaptic transmission [GO:0099170]; protein import into nucleus [GO:0006606]; regulation of cell proliferation involved in kidney morphogenesis [GO:0061006]; renal filtration [GO:0097205]; response to calcium ion [GO:0051592]; skeletal muscle fiber development [GO:0048741]; transition between fast and slow fiber [GO:0014883]

calcineurin complex [GO:0005955]; cytoplasm [GO:0005737]; cytoplasmic side of plasma membrane [GO:0009898]; cytosol [GO:0005829]; dendritic spine [GO:0043197]; glutamatergic synapse [GO:0098978]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; Schaffer collateral - CA1 synapse [GO:0098685]; Z disc [GO:0030018]

ATPase binding [GO:0051117]; calmodulin binding [GO:0005516]; calmodulin-dependent protein phosphatase activity [GO:0033192]; cyclosporin A binding [GO:0016018]; metal ion binding [GO:0046872]; myosin phosphatase activity [GO:0017018]; protein dimerization activity [GO:0046983]

IPR004843;IPR029052;IPR041751;IPR043360;IPR006186;

3.60.21.10;

A0A1D5RJQ2

MAIGLPRLALGPVASDTRWDTEGSGAPAAAAAARGGDAREQREPARGTKVTRRCGRPGRWGSRSAKRAAAAAAGPPRRCCAGPGIIMGQTGKKSEKGPVCWRKRVKSEYMRLRQLKRFRRADEVKSMFSSNRQKILERTEILNQEWKQRRIQPVHILTSVSSLRGTRECSVTSDLDFPTQVIPLKTLNAVASVPIMYSWSPLQQNFMVEDETVLHNIPYMGDEVLDQDGTFIEELIKNYDGKVHGDRECGFINDEIFVELVNALGQYNDDDDDDDGDDPEEREEKQKDLEDHRDDKESRPPRKFPSDKIFEAISSMFPDKGTAEELKEKYKELTEQQLPGALPPECTPNIDGPNAKSVQREQSLHSFHTLFCRRCFKYDCFLHPFHATPNTYKRKNTETALDNKPCGPQCYQHLEGAKEFAAALTAERIKTPPKRPGGRRRGRLPNNSSRPSTPTINVLESKDTDSDREAGTETGGENNDKEEEEKKDETSSSSEANSRCQTPIKMKPNIEPPENVEWSGAEASMFRVLIGTYYDNFCAIARLIGTKTCRQVYEFRVKESSIIAPAPAEDVDTPPRKKKRKHRLWAAHCRKIQLKKDGSSNHVYNYQPCDHPRQPCDSSCPCVIAQNFCEKFCQCSSECQNRFPGCRCKAQCNTKQCPCYLAVRECDPDLCLTCGAADHWDSKNVSCKNCSIQRGSKKHLLLAPSDVAGWGIFIKDPVQKNEFISEYCGEIISQDEADRRGKVYDKYMCSFLFNLNNDFVVDATRKGNKIRFANHSVNPNCYAKVMMVNGDHRIGIFAKRAIQTGEELFFDYRYSQADALKYVGIEREMEIP

Macaca mulatta (Rhesus macaque)

2.1.1.356

CATALYTIC ACTIVITY: Reaction=L-lysyl(27)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(27)-[histone H3] + 3 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:60292, Rhea:RHEA-COMP:15535, Rhea:RHEA-COMP:15548, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.356; Evidence={ECO:0000256|ARBA:ARBA00000090};

Biological rhythms;Chromatin regulator;Methyltransferase;Nucleus;Reference proteome;Repressor;S-adenosyl-L-methionine;Transcription;Transcription regulation;Transferase

B cell differentiation [GO:0030183]; cardiac muscle hypertrophy in response to stress [GO:0014898]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to trichostatin A [GO:0035984]; cerebellar cortex development [GO:0021695]; facultative heterochromatin formation [GO:0140718]; G1 to G0 transition [GO:0070314]; G1/S transition of mitotic cell cycle [GO:0000082]; hepatocyte homeostasis [GO:0036333]; heterochromatin formation [GO:0031507]; keratinocyte differentiation [GO:0030216]; liver regeneration [GO:0097421]; methylation [GO:0032259]; negative regulation of G1/S transition of mitotic cell cycle [GO:2000134]; negative regulation of keratinocyte differentiation [GO:0045617]; negative regulation of retinoic acid receptor signaling pathway [GO:0048387]; negative regulation of stem cell differentiation [GO:2000737]; negative regulation of striated muscle cell differentiation [GO:0051154]; negative regulation of transcription by RNA polymerase II [GO:0000122]; negative regulation of transcription elongation by RNA polymerase II [GO:0034244]; positive regulation of cell cycle G1/S phase transition [GO:1902808]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of epithelial to mesenchymal transition [GO:0010718]; protein localization to chromatin [GO:0071168]; regulation of circadian rhythm [GO:0042752]; regulation of gliogenesis [GO:0014013]; regulation of protein phosphorylation [GO:0001932]; response to tetrachloromethane [GO:1904772]; rhythmic process [GO:0048511]; skeletal muscle satellite cell maintenance involved in skeletal muscle regeneration [GO:0014834]; stem cell differentiation [GO:0048863]; subtelomeric heterochromatin formation [GO:0031509]

chromatin silencing complex [GO:0005677]; chromosome, telomeric region [GO:0000781]; ESC/E(Z) complex [GO:0035098]; nucleus [GO:0005634]; pericentric heterochromatin [GO:0005721]; pronucleus [GO:0045120]

chromatin binding [GO:0003682]; chromatin DNA binding [GO:0031490]; histone H3K27 methyltransferase activity [GO:0046976]; histone H3K27 trimethyltransferase activity [GO:0140951]; lncRNA binding [GO:0106222]; primary miRNA binding [GO:0070878]; promoter-specific chromatin binding [GO:1990841]; ribonucleoprotein complex binding [GO:0043021]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II core promoter sequence-specific DNA binding [GO:0000979]; transcription corepressor activity [GO:0003714]; transcription corepressor binding [GO:0001222]

SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.

IPR026489;IPR045318;IPR048358;IPR021654;IPR044439;IPR041343;IPR041355;IPR001005;IPR001214;IPR046341;IPR033467;

1.20.58.1880;2.170.270.10;

A0A1D5RKD4

MLRRALLCLAVAAAAGVYADAPEEEDHVLVLRKSNFAEALAAHKYLLVEFYAPWCGHCKALAPEYAKAAGKLKAEGSEIRLAKVDATEESDLAQQYGVRGYPTIKFFRNGDTASPKEYTAGREADDIVNWLKKRTGPAATTLPDGAAAESLVESSEVAVIGFFKDVESDSAKQFLQAAEAIDDIPFGITSNSDVFSKYQLDKDGVVLFKKFDEGRNNFEGEVTKENLLDFIKYNQLPLVIEFTEQTAPKIFGGEIKTHILLFLPKSVSDYDGKLSSFRTAAESFKGKILFIFIDSDHTDNQRILEFFGLKKEECPAVRLITLEEEMTKYKPESDELTAERITEFCHRFLEGKIKPHLMSQELPEDWDKQPVKVLVGKNFEEVAFDENKNVFVEFYAPWCGHCKQLAPIWDKLGETYKDHENIVIAKMDSTANEVEAIKVHSFPTLKFFPASVDRTVIDYNGERTLDGFKKFLESGGQDGAGDDDDLEDLEEAEEPDMEEDDDQKAVKDEL

Macaca mulatta (Rhesus macaque)

5.3.4.1

CATALYTIC ACTIVITY: Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.; EC=5.3.4.1; Evidence={ECO:0000256|ARBA:ARBA00001182, ECO:0000256|RuleBase:RU361130};

Cell membrane;Chaperone;Disulfide bond;Endoplasmic reticulum;Isomerase;Membrane;Redox-active center;Reference proteome;Repeat;Signal

cellular response to hypoxia [GO:0071456]; cellular response to interleukin-7 [GO:0098761]; endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; insulin processing [GO:0030070]; positive regulation of substrate adhesion-dependent cell spreading [GO:1900026]; positive regulation of viral entry into host cell [GO:0046598]; protein folding [GO:0006457]; protein folding in endoplasmic reticulum [GO:0034975]; regulation of oxidative stress-induced intrinsic apoptotic signaling pathway [GO:1902175]; response to endoplasmic reticulum stress [GO:0034976]

cytoskeleton [GO:0005856]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum chaperone complex [GO:0034663]; endoplasmic reticulum lumen [GO:0005788]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; external side of plasma membrane [GO:0009897]; lamellipodium [GO:0030027]; melanosome [GO:0042470]; procollagen-proline 4-dioxygenase complex [GO:0016222]

actin binding [GO:0003779]; integrin binding [GO:0005178]; procollagen-proline 4-dioxygenase activity [GO:0004656]; protein disulfide isomerase activity [GO:0003756]; protein heterodimerization activity [GO:0046982]; protein-disulfide reductase activity [GO:0015035]; thiol oxidase activity [GO:0016972]

SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004202}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}. Endoplasmic reticulum lumen {ECO:0000256|ARBA:ARBA00004319}. Melanosome {ECO:0000256|ARBA:ARBA00004223}. Membrane {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.

IPR005788;IPR005792;IPR036249;IPR017937;IPR013766;

3.40.30.10;

A0A1D5RLD8

MVKVGVNGFGRIGRLVTRAATCSGKVEIVAINDPFIDLNYMVYMFQYDSTHGKFNGTVKAENGKLVINGKPITIFQERDPTNIKWGEAGAEYVVESTGVFTTMEKAGAHLKGGAKRVIISAPSADAPMFVMGVNHEKYDNSLKIVSNASCTTNCLAPLAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLWRDGRGAAQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTPNVSIVDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEDQVVSCDFNSNSHSSTFDAGAGIALNDNFVKLISWYDNEYGYSNRVVDLMAYMASKE

Mus musculus (Mouse)

1.2.1.12

CATALYTIC ACTIVITY: Reaction=D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3-phospho-glyceroyl phosphate + H(+) + NADH; Xref=Rhea:RHEA:10300, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57540, ChEBI:CHEBI:57604, ChEBI:CHEBI:57945, ChEBI:CHEBI:59776; EC=1.2.1.12; Evidence={ECO:0000256|ARBA:ARBA00001810, ECO:0000256|RuleBase:RU361160}; CATALYTIC ACTIVITY: Reaction=L-cysteinyl-[protein] + S-nitroso-L-cysteinyl-[GAPDH] = L-cysteinyl-[GAPDH] + S-nitroso-L-cysteinyl-[protein]; Xref=Rhea:RHEA:66684, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:17089, Rhea:RHEA-COMP:17090, Rhea:RHEA-COMP:17091, ChEBI:CHEBI:29950, ChEBI:CHEBI:149494; Evidence={ECO:0000256|ARBA:ARBA00024287}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66685; Evidence={ECO:0000256|ARBA:ARBA00024287};

PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5. {ECO:0000256|ARBA:ARBA00004869, ECO:0000256|RuleBase:RU361160}.

ADP-ribosylation;Apoptosis;Cytoplasm;Cytoskeleton;Glycolysis;Methylation;NAD;Nucleotide-binding;Nucleus;Oxidoreductase;Proteomics identification;Reference proteome;S-nitrosylation;Transferase;Translation regulation

cAMP-mediated signaling [GO:0019933]; gluconeogenesis [GO:0006094]; glycolytic process [GO:0006096]; microtubule cytoskeleton organization [GO:0000226]; negative regulation of vascular associated smooth muscle cell apoptotic process [GO:1905460]; neuron apoptotic process [GO:0051402]; nitric oxide mediated signal transduction [GO:0007263]; protein stabilization [GO:0050821]; regulation of translation [GO:0006417]

cytoplasm [GO:0005737]; cytosol [GO:0005829]; glutamatergic synapse [GO:0098978]; microtubule cytoskeleton [GO:0015630]; nucleus [GO:0005634]; postsynaptic density, intracellular component [GO:0099092]

glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity [GO:0004365]; identical protein binding [GO:0042802]; microtubule binding [GO:0008017]; NAD binding [GO:0051287]; NADP binding [GO:0050661]; peptidyl-cysteine S-nitrosylase activity [GO:0035605]

SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.

IPR020831;IPR020830;IPR020829;IPR020828;IPR006424;IPR036291;

3.40.50.720;

A0A1D6E0S8

MPSRSPACRPRGRNRRSAADAVARPLALALILVSTLPRAAHSQDLALPPVQPRGVRRTMTCDNIPEPFGTRSRGASRLPGFEVTCGPNREAMLSIGGDAYMIDFVSVSGSYVVVFAEPITQVCYDGKGKPTPDTGTGAKSSEGTTTTFTWSLEGTPFTFSKSNKLVNFGCNRTLMANFFIVPGDSSPLYTSCTTTCNTLQISGSCLGEACCEAPMDQVNGAKAFSLSFERTTANGTGEEDGTCSAAFFLDKDETVFTFSGDEVRPLKTALLPPGERRMVLDWAIGSTSCEQTQSYTFEKLCKYGTCVDAPTGAGYLCKCPSGYDGNPYVSDGCQDINECRNYNSNNCTYQNLCNNTLGGYTCSCPENNIGDGYRTGTGCNTTLATPVSPSQQPQGINVCDHPEKNPCTYIKYCIDLEGVVSCACPEGMSGDGRKNGRGCCFSCQKHFPLDTVLGVSLVLMVTTTTAASCYCWAVKKRELGRKRAELFRKNGGLLLQQRFSTITSQGEDQYSSKIFSAEELKAATDNYSESRILGRGGQGTVYKGILPDQTVVAIKKSKVFDESQVEQFVNEIAILSQIDHPNVVKLLGCCLETQVPLLVYEFISNGTLFQHIHNRNATRPLTWEDCLRIAAETADALAYLHSASSIPIIHRDIKSSNILLDGNFVAKIADFGASRSVPFDQTHITTLIQGTIGYLDPEYFQSSQLTEKSDVYSFGVVLAELLTRQKPISAARPEDSCNLAMHLVVLFNKGRLLQEIEPHILAEAGEDQCYAVAELSVRCLNVKGEERPAMVVVASVLQELRRSFTIDQAVGIKDESIQENSEQEEKHLHESRSIPSLQSSEVSTQCSMEAKMSSFC

Zea mays (Maize)

FUNCTION: [Isoform 1]: Kinase that contributes to activation of the hypersensitive response, a form of programmed cell death, upon fungal infection. {ECO:0000269|PubMed:36577386}.; FUNCTION: [Isoform 2]: Secreted protein that contributes to activation of the hypersensitive response, a form of programmed cell death, upon fungal infection (PubMed:36577386). May sense the presence of fungal material and relay the signal to WAK17 isoform 1 (Probable). {ECO:0000269|PubMed:36577386, ECO:0000305|PubMed:36577386}.

2.7.11.1

CATALYTIC ACTIVITY: [Isoform 1]: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q1MX30}; CATALYTIC ACTIVITY: [Isoform 1]: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q1MX30};

COFACTOR: [Isoform 1]: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q1MX30}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q1MX30};

Alternative splicing;ATP-binding;Calcium;Cell membrane;Disulfide bond;EGF-like domain;Glycoprotein;Kinase;Membrane;Nucleotide-binding;Receptor;Reference proteome;Repeat;Serine/threonine-protein kinase;Signal;Transferase;Transmembrane;Transmembrane helix

cell surface receptor signaling pathway [GO:0007166]; detection of symbiotic fungus [GO:0009603]; innate immune response [GO:0045087]; phosphorylation [GO:0016310]; positive regulation of plant-type hypersensitive response [GO:0034052]

external side of plasma membrane [GO:0009897]; plasma membrane [GO:0005886]

ATP binding [GO:0005524]; calcium ion binding [GO:0005509]; protein serine/threonine kinase activity [GO:0004674]

SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000269|PubMed:36577386}; Single-pass type I membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane {ECO:0000269|PubMed:36577386}; Peripheral membrane protein {ECO:0000305|PubMed:36577386}. Note=Associates with the plasma membrane via interactions with WAK17 isoform 1. {ECO:0000269|PubMed:36577386}.

IPR001881;IPR000742;IPR000152;IPR018097;IPR011009;IPR000719;IPR008271;IPR045274;

2.10.25.10;1.10.510.10;

A0A1D6EFT8

MAPSNIVVQSSSTPPVAGGDEEFAPSVWGDFFVTYATPVSQASEQRMSERAELLKAQVRQAFDAASMDVAGLITYVDTLERLGLDNHFRDLIGAALERIGAEELPEHGGGLHIVALRFRLLRQHGIWVSTDVFDAFREDAGGFCSSLCSDDPRGLLSLYNAAHMAVPGEVVLDDAIAFARGRLLDIISKGEVRSPVSEQITRALDIPLPRFTRRLETMHYIAEYEHEEAHDGLLLELARLNFVLVRALHLRELKDLSLWWRELYNTVKLPYARDRMVEIYFWTCGMLHEEEYSLARMFFAKTFGMVSLMDDTFDVHATLDECHKLKEAMQRWDESEVSILPEYLRLLYIKTLSNFKEFEEILEPNKKYRMAYTKEAYKLCSKNYLKEAIWSNQKYQPSFKEHEELSIMTSGLPMLTILTLMGFGDEATPEAFEWVSSVPEMVRAGSQVTRFLNDLSSYKLGKNKKDMPGSVETYMVENGLTGDEAAAAIAALLENRWRILNQTRMEIDHTLLPAAQVVLNMARANEIIYLHGRDAYTFGADLKDLVTTLFLKQVLPL

Zea mays (Maize)

FUNCTION: Component of the volatile terpenes biosynthesis pathways (PubMed:30187155). Dihydroxylated sesquiterpenoid synthase that generates dually hydroxylated products directly from (E,E)-farnesyl diphosphate, primarily eudesmane-2,11-diol, along with two closely related structural isomers (PubMed:29570233). {ECO:0000269|PubMed:29570233, ECO:0000303|PubMed:30187155}.

4.2.3.197

CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate + 2 H2O = 7-epi-ent-eudesmane-5,11-diol + diphosphate; Xref=Rhea:RHEA:58164, ChEBI:CHEBI:15377, ChEBI:CHEBI:33019, ChEBI:CHEBI:142536, ChEBI:CHEBI:175763; EC=4.2.3.197; Evidence={ECO:0000269|PubMed:29570233}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58165; Evidence={ECO:0000269|PubMed:29570233};

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7}; Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250|UniProtKB:A0A1C9J6A7};

PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000305|PubMed:30187155}.

Cytoplasm;Lyase;Magnesium;Manganese;Metal-binding;Plant defense;Reference proteome

defense response to fungus [GO:0050832]; diterpenoid biosynthetic process [GO:0016102]; sesquiterpene biosynthetic process [GO:0051762]; terpene biosynthetic process [GO:0046246]

cytoplasm [GO:0005737]

magnesium ion binding [GO:0000287]; terpene synthase activity [GO:0010333]

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6Q3H2}.

DOMAIN: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic activity, presumably through binding to Mg(2+). {ECO:0000250|UniProtKB:A0A1C9J6A7}.

IPR008949;IPR034741;IPR044814;IPR001906;IPR036965;IPR005630;IPR008930;

1.10.600.10;1.50.10.130;

A0A1D6HSP4

MELASTMSVAMALAAAIFVVLCSVVASARGRREKALKLPPGPRGWPVLGSLGALAGALPPHRALAALAARHGPLMHLRLGSYHTVVASSADAARLVLRTHDSALADRPDTAAGEITSYGYLGIVHTPRGAYWRMARRLCATELFSARRVESFQDVRAQEMRALARGLFGCAAGRRAVAVREHVAGATMRNILRMAVGEKWSGCYGSPEGEAFRRSLDEAFAATGAVSNVGEWVPWLGWLDVQGFKRKMKRLHDLHDHFYEKILVDHEERRRLAQASGGEFVATDLVDVLLQLSEESTKLESESEARLPRDGVKALIQDIIAGGTESSAVTIEWAMAELLRHPEAMAKATDELDRVVGSGRWVAERDLPELHYIDAVVKETLRLHPVGPLLVPHYARERTVVAGYDVPAGARVLVNAWAIARDPASWPDAPDAFQPERFLGAAAAVDVRGAHFELLPFGSGRRICPAYDLAMKLVAAGVANLVHGFAWRLPDGVAAEDVSMEEHVGLSTRRKVPLFAVAEPRLPVHLYSATE

Zea mays (Maize)

FUNCTION: Involved in the biosynthesis of homoterpenes, attractants of herbivores parasitoids and predators (e.g. predatory mites and parasitoid wasps) (By similarity). Component of the volatile terpenes biosynthesis pathways (PubMed:30187155). Converts mainly nerolidol to dimethylnonatriene (DMNT) and, to a lower extent, geranyllinalool to trimethyltridecatetraene (TMTT) (PubMed:27662898). {ECO:0000250|UniProtKB:Q9LSF8, ECO:0000269|PubMed:27662898, ECO:0000303|PubMed:30187155}.

1.14.14.58; 1.14.14.59

CATALYTIC ACTIVITY: Reaction=(6E,10E)-geranyllinalool + O2 + reduced [NADPH--hemoprotein reductase] = (3E,7E)-4,8,12-trimethyltrideca 1,3,7,11-tetraene + but-3-en-2-one + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:13545, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:48058, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:74299, ChEBI:CHEBI:74322; EC=1.14.14.58; Evidence={ECO:0000269|PubMed:27662898}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13546; Evidence={ECO:0000269|PubMed:27662898}; CATALYTIC ACTIVITY: Reaction=(3S,6E)-nerolidol + O2 + reduced [NADPH--hemoprotein reductase] = (3E)-4,8-dimethylnona-1,3,7-triene + but-3-en-2-one + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:55424, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:48058, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:59958, ChEBI:CHEBI:60158; EC=1.14.14.59; Evidence={ECO:0000269|PubMed:27662898}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55425; Evidence={ECO:0000269|PubMed:27662898};

COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:Q96242};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=14.2 uM for (E)-nerolidol {ECO:0000269|PubMed:27662898}; KM=5.6 uM for (6E,10E)-geranyllinalool {ECO:0000269|PubMed:27662898};

PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000305|PubMed:30187155}.

Heme;Iron;Membrane;Metal-binding;Monooxygenase;Oxidoreductase;Plant defense;Reference proteome;Transmembrane;Transmembrane helix

defense response [GO:0006952]; response to herbivore [GO:0080027]; terpenoid biosynthetic process [GO:0016114]

membrane [GO:0016020]

4,8,12-trimethyltrideca-1,3,7,11-tetraene synthase activity [GO:0097007]; DMNT synthase activity [GO:0102171]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; terpene synthase activity [GO:0010333]

SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.

IPR001128;IPR017972;IPR002401;IPR036396;

1.10.630.10;

A0A1D6K6U5

MVLSSSCTTVPHLSSLAVVQLGPWSSRIKKKTDAVAVPAAAGRWRARARAQDTSESAAVAKGSSLTPIVRTDAESRRTRWPTDDDDAEPLVDEIRAMLTSMSDGDISVSAYDTAWVGLVPRLDGGEGPQFPAAVRWIRNNQLPDGSWGDAALFSAYDRLINTLACVVTLTRWSLEPEMRGRGLSFLGRNMWKLATEDEESMPIGFELAFPSLIELAKSLGVHDFPYDHQALQAIYSSREIKVKRIPKEVMHTVPTSILHSLEGMPGLDWARLLKLQSSDGSFLFSPAATAYALMNTGDDRCFSYIDRTVKKFNGGVPNVYPVDLFEHIWAVDRLERLGISRYFQKEIEQCMDYVNRHWTEDGICWARNSDVKEVDDTAMAFRLLRLHGYSVSPDVFKNFEKDGEFFAFVGQSNQAVTGMYNLNRASQISFPGEDVLHRAGPFSYEFLRRKQAEGALRDKWIISKDLPGEVVYTLDFPWYGNLPRVEARDYLEQYGGGDDVWIGKTLYRMPLVNNDVYLELARMDFNHCQALHQLEWQGLKKWYTENRLMDFGVAQEDALRAYFLAAASVYEPCRAAERLAWARAAILANAVSTHLRNSPSFRERLEHSLRCRPSEETDGSWFNSSSGSDAVLVKAVLRLTDSLAREAQPIHGGDPEDIHKLLRSAWAEWVREKADAADSVCNGSSAVEQEGSRMVHDKQTCLLLARMIEISAGRAAGEAASEDGDRRIIQLTGSICDSLKQKMLVSQDPEKNEEMMSHVDDELKLRIREFVQYLLRLGEKKTGSSETRQTFLSIVKSCYYAAHCPPHVVDRHISRVIFEPVSAAK

Zea mays (Maize)

FUNCTION: Involved in gibberellin biosynthesis (PubMed:16307364). Catalyzes the conversion of geranylgeranyl diphosphate to the gibberellin precursor ent-copalyl diphosphate (ent-CPP) (PubMed:16307364). Involved in the production of antifungal dolabralexin phytoalexins in response to biotic and abiotic stresses (PubMed:29475898). In response to fungal infection and in associtation with KSL4, is involved in the production dolabradiene, a type of antifungal phytoalexin (PubMed:29475898). {ECO:0000269|PubMed:16307364, ECO:0000269|PubMed:29475898}.

5.5.1.13

CATALYTIC ACTIVITY: Reaction=(2E,6E,10E)-geranylgeranyl diphosphate = ent-copalyl diphosphate; Xref=Rhea:RHEA:14841, ChEBI:CHEBI:58553, ChEBI:CHEBI:58756; EC=5.5.1.13; Evidence={ECO:0000269|PubMed:16307364, ECO:0000269|PubMed:29475898}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14842; Evidence={ECO:0000269|PubMed:16307364, ECO:0000269|PubMed:29475898};

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q38802};

PATHWAY: Plant hormone biosynthesis; gibberellin biosynthesis. {ECO:0000305}.

Chloroplast;Isomerase;Magnesium;Metal-binding;Plant defense;Plastid;Reference proteome;Transit peptide

defense response [GO:0006952]; diterpene phytoalexin biosynthetic process [GO:0051502]; diterpenoid biosynthetic process [GO:0016102]; gibberellin biosynthetic process [GO:0009686]

chloroplast [GO:0009507]

ent-copalyl diphosphate synthase activity [GO:0009905]; isomerase activity [GO:0016853]; magnesium ion binding [GO:0000287]; terpene synthase activity [GO:0010333]

SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.

DOMAIN: The Asp-Xaa-Asp-Asp (DXDD) motif is important for the catalytic activity through binding to Mg(2+). {ECO:0000305}.

IPR008949;IPR001906;IPR036965;IPR008930;

1.50.10.160;1.10.600.10;1.50.10.130;

A0A1D6L709

MPHSVLARLPPGSVRLVAAFGLLLLVSLLVLHRRPGRPHVAAAAASDRLTDPSRSRLFLSQSPGANASIAADLRALTAGPHLAGTPASAGAAAHVLARLRAAGLQTLTREYEPLLSYPGHASLALLRPDGSLLARLSLEEPADEGRRVVPPYHAYAPSGGAVAEAVFVNLGREEDYVVLERLGVGVRGRVAVARRGGGYRGGVVARAADKGAVAVLIAGNADGGVERGVVLLGGPGDPLTPGWAATSGAERLKFDDKAVKQRFPSIPSMPVSAKTAAAIIRSLGGPAIPAEWKDGLGVDTGGLGPGPTLVNFTYQEDRKFYKIRDIFGIIKGQEEPDRYVILGNHRDAWTYGAVDPNSGTAALLDIARRLGIMLQSGWKPRRSIILCSWDGEEFGMIGSTEWVEDNLEDLHSKAVAYLNVDCAVQGVGFFAGSTPQLDKLLVDITRQVRDPDVTGKMVHDTWNEMSGGIKIERLARTDSDFAPFLHHAGIPSVDLYYGEEFPGYHTALDTYNWMEKHGDPFFLRHLAITEIWGLLALRLANDPVLPFDYQAYTSQLQEHIKTLSALTSNGHAVNLMNGCVNDLSGAAMEVLKEMKKLQQMDLYDEHARMRRRLLNDRLLLAERSFLQPEGLQGRGWFKHLLYSPPEDYESKLSFFPGIADAISRSANLSDKEQEVAMQHEVWKVCRAIQRAASVLRGEFSEQKPTNFSSLVTP

Zea mays (Maize)

FUNCTION: Involved in the regulation of meristem development and seed maturation processes. Mediates regulation of embryonic regulatory genes and genes controlling abscisic acid (ABA) biosynthesis and turnover in developing seeds. May be required for the synthesis of small signaling molecules that integrates meristem and embryo formation in seeds. {ECO:0000269|PubMed:18203869}.

3.4.17.21

CATALYTIC ACTIVITY: Reaction=Release of an unsubstituted, C-terminal glutamyl residue, typically from Ac-Asp-Glu or folylpoly-gamma-glutamates.; EC=3.4.17.21; Evidence={ECO:0000305};

COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q04609}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q04609};

Cell membrane;Developmental protein;Glycoprotein;Growth regulation;Hydrolase;Membrane;Metal-binding;Metalloprotease;Protease;Reference proteome;Signal-anchor;Transmembrane;Transmembrane helix;Zinc

embryo development ending in seed dormancy [GO:0009793]; flower development [GO:0009908]; leaf vascular tissue pattern formation [GO:0010305]; maintenance of meristem identity [GO:0010074]; photomorphogenesis [GO:0009640]; proteolysis [GO:0006508]; regulation of floral meristem growth [GO:0010080]; regulation of inflorescence meristem growth [GO:0010081]; regulation of root meristem growth [GO:0010082]; regulation of seed maturation [GO:2000034]

plasma membrane [GO:0005886]

carboxypeptidase activity [GO:0004180]; metal ion binding [GO:0046872]; metallocarboxypeptidase activity [GO:0004181]

SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Single-pass type II membrane protein {ECO:0000255}.

IPR046450;IPR007484;IPR039373;IPR007365;IPR036757;

3.50.30.30;1.20.930.40;3.40.630.10;

A0A1D6LAB7

MASLTLPALALALSNPGAVRLRAAAFRCWALRRRGWAAAGALASPNSVLSEHAFKRLQLGSDDEDGEGPYGSDADEGFEAGEGDNEELAIARLGLPDELVATLEKRGITHLFPIQRAVLIPALEGRDLIARAKTGTGKTLAFGIPMIKQLIEQDDGRITRRGRTPRVLVLAPTRELAKQVEKEIKESAPKLGTVCVYGGVSYNVQQNALSRGVDVVVGTPGRIIDLINGGSLQLGEVQYLVLDEADQMLAVGFEEDVETILQQLPAGRQSMLFSATMPSWVKKLSRRYLNNPLTIDLVGDQDEKLAEGIKLYAIPLTTTSKRTVLSDLITVYAKGGKTIVFTRTKKDADEVSLALTNSIASEALHGDISQHQRERTLNGFRQGKFTVLVATDVAARGLDIPNVDLIIHYELPNDPETFVHRSGRTGRAGKAGTAILMFTSSQKRTVKSLERDVGCNFEFISPPSIEEVLESSAEHVIATLRGVHPESTKYFLGAAEKLTEELGPHALASALAHLSGFSQPPSSRSLISHEQGWVTLQLTREQGFGRGFFSPRSVTGFLSDVCSAAADEVGKIYLTADENVQGAVFDLPEEIAKDLLTMELPPGNTLTKISKLPALQDDGPATDSYGRFSNDRGSRNNRRSRGGGASRGRGGWDTDGEDRFRRGGRSLRSDNDSWSDDDWSGGGRKSNRSSSFGSRSSSYSSRGSPSFGGRSSSFGGRESNRSFSGACFNCGESGHRATDCPNK

Zea mays (Maize)

FUNCTION: Nuclear genome-encoded factor involved in ribosome biogenesis in chloroplasts. Binds specific group II introns in chloroplasts and facilitates their splicing. Is required for rRNA maturation in plastids and may contribute to the assembly of the large (50S) ribosomal subunit. Required for normal development of chloroplasts. {ECO:0000269|PubMed:22576849}.

3.6.4.13

CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; Evidence={ECO:0000305};

ATP-binding;Chloroplast;Helicase;Hydrolase;Metal-binding;Nucleotide-binding;Plastid;Reference proteome;Ribosome biogenesis;RNA-binding;Transit peptide;Zinc;Zinc-finger

chloroplast organization [GO:0009658]; Group II intron splicing [GO:0000373]; ribosome biogenesis [GO:0042254]

chloroplast stroma [GO:0009570]; cytoplasm [GO:0005737]; cytosol [GO:0005829]

ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; zinc ion binding [GO:0008270]

SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000269|PubMed:22576849}.

DOMAIN: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis. {ECO:0000305}.

IPR011545;IPR012562;IPR014001;IPR001650;IPR027417;IPR014014;IPR001878;IPR036875;

3.40.50.300;4.10.60.10;

A0A1D6LTV0

MAGITGVMNMKLAARPSSGRHSRGCRPAVVPSAGKQMLLVRRHPPGSASWPTRATGGGGGGVPAGATAADSSGQAKEEEEEDRASRNTSSFEPSIWGDFFLTYSSPLATSSAQKARMVHRAEQLKKQVAKLIAASGACSLYHRIHLVDALERLCLDYLFEDEINDMVTQIHNVDVSGCDLQTVAMWFYLLRNHGYRVSSDVVFAKFRDEQGGFAANNPRDLLNLYNAACLRTHGETILDEAASFTSKCLKSLAPYTYMEASLASEIKRALEIPLPRSVRIYGAKSRIAEYGNQTEANELVLELAKLNYNLVQLQHQEELKIITRWWNDLELQTRLSFARDRVVECYFWMVGVYFEPSYSRARVILSKVLAIVSLLDDTYDVYGTSQECELFTKCIESWDPAATGGRLPGNMKFIFAKILDTCQSFEDELAPDEKYRMHYLKTFIIDLVRAYNEEVKWREQGYVPATVEEHLQVSARSGGCHLLSCTSFVGMGDVADQEAFEWVRGVPKIVKALCIILRLSDDLKSYEREKMSSHVASTMESCMKEHQVPLEVARVKIQETIDETWKDFNEEWLNLNTNSHLPRELLERIFNLTRTMVYIYQQDDAYTNCHVIKDTINSLFVEPVSIT

Zea mays (Maize)

FUNCTION: Component of the volatile terpenes biosynthesis pathways (PubMed:30187155). Mediates the synthesis of a blend of monoterpenes. Converts mainly geranyl diphosphate to alpha-terpineol. Triggers also the biosynthesis of minor monoterpenes including limonene, gamma-terpinene, beta-myrcene, terpinolene and 4-terpineol (PubMed:18218975). {ECO:0000269|PubMed:18218975, ECO:0000303|PubMed:30187155}.

4.2.3.-; 4.2.3.111; 4.2.3.113; 4.2.3.114; 4.2.3.15; 4.2.3.16

CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate + H2O = (S)-alpha-terpineol + diphosphate; Xref=Rhea:RHEA:32551, ChEBI:CHEBI:128, ChEBI:CHEBI:15377, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.111; Evidence={ECO:0000269|PubMed:18218975}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32552; Evidence={ECO:0000269|PubMed:18218975}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = (4S)-limonene + diphosphate; Xref=Rhea:RHEA:12869, ChEBI:CHEBI:15383, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.16; Evidence={ECO:0000269|PubMed:18218975}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12870; Evidence={ECO:0000269|PubMed:18218975}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = diphosphate + gamma-terpinene; Xref=Rhea:RHEA:32559, ChEBI:CHEBI:10577, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.114; Evidence={ECO:0000269|PubMed:18218975}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32560; Evidence={ECO:0000269|PubMed:18218975}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = beta-myrcene + diphosphate; Xref=Rhea:RHEA:16965, ChEBI:CHEBI:17221, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.15; Evidence={ECO:0000269|PubMed:18218975}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16966; Evidence={ECO:0000269|PubMed:18218975}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = diphosphate + terpinolene; Xref=Rhea:RHEA:25500, ChEBI:CHEBI:9457, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.113; Evidence={ECO:0000269|PubMed:18218975}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25501; Evidence={ECO:0000269|PubMed:18218975}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate + H2O = 4-terpineol + diphosphate; Xref=Rhea:RHEA:60028, ChEBI:CHEBI:15377, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057, ChEBI:CHEBI:78884; Evidence={ECO:0000269|PubMed:18218975}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60029; Evidence={ECO:0000269|PubMed:18218975};

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:B2C4D0}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:B2C4D0}; Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q5GJ60};

PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000305|PubMed:30187155}.

Alternative splicing;Chloroplast;Cobalt;Lyase;Magnesium;Manganese;Metal-binding;Plastid;Reference proteome;Transit peptide

diterpenoid biosynthetic process [GO:0016102]; response to wounding [GO:0009611]; terpenoid biosynthetic process [GO:0016114]

chloroplast [GO:0009507]

(4S)-limonene synthase activity [GO:0050552]; gamma-terpinene synthase activity [GO:0102903]; magnesium ion binding [GO:0000287]; myrcene synthase activity [GO:0050551]; terpene synthase activity [GO:0010333]

SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:18218975}.

DOMAIN: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic activity, presumably through binding to Mg(2+). {ECO:0000305}.

IPR008949;IPR034741;IPR044814;IPR001906;IPR036965;IPR005630;IPR008930;

1.10.600.10;1.50.10.130;

A0A1D6M217

MTLRPGKLPSEGIDNNALLLPGPSSEALMFLLGSHNNFVRLEGFDEGELGHNDVGGRDDRMTIDGGKLGAEDVAQRVGTTIPSPVVARSGWRKPAIVVGNGAEAHVGVSAATVSWGGMSPARVGWSVGALEPAWVPCVAWERVGAVAATKEALVTRLCEGTGPNANNALAAGVLATVGELAKVGGFAMRQYLPELMPVVVDSLLDGGAVSKREVAVSTLGQIIQSTGYVIAPYNEYPPLLGLLLKLLNGELEWSTRLEVLKVLGIMGALDPHAHKRNQHNLPGQHREVLRPTIETAQHIVSMEELPTDYWPSFSASEDYYSTSMGLGCVPYLPKVLPDLFRAVRMCEDGALKEFITWKLGTLISIVRQHIRKYLQDILSLISELWTSSFSLAAPNRTIQGPQGSPVLHLVEQLCLALNDEFRMYLLHILPSCIQVLGDAERCNDYYYVPDILHTLEVFGGNLDEHMHLVAPVLVRLFKVELVDIRRRAIVTLTNLIPKVQVFVSNTHCVYFTCPEQVGTHVSALVHHLKLVLDGNNDDLRKDAAEALCCLAHALGEDFTIFIPSIRKILVKHHLRYRKWDEIENRLLRRELLITENLSVQKYTQCPPDVISDPLDDCDGTPSEIADETQRQARSHQVNDVRLRSAGEASQRSTREDWAEWMRHFSIALLKESPSPALRTCARLAQLQPSVGRELFAAGFASCWAQMSESSQEQLVRSLKTAFSSQNIPPEILATLLNLAEFMEHDEKPLPIDTRLLGALAEKCRAFAKALHYKEMEFEAVCTKKMGANPVTVVESLIHINNQLQQHEAAIGILTYSQQNSEVQLKESWYEKLHRWDEALKAYTVKSSQTSGPLQNLDATLDENKLRMLGNATASGDGSSNGAFFRAVLLVRYKKYDDARMYVERARRCLATELAALVLESYERAYNNMVRVQQLSELEEVIDYCTLPMESPIADGRRELIRNMWNERIKGTKRNVEVWQALLAVRELVLPPNEDRDTWIKFAELCWKNGRISQARSTLVKLLQFDPESSPELTLYHAHPQVALAYLKYQYAVGDELKRRDAFSKLQELSVQVATTMGNLPGTSANHGTMSNAGVPLIARVYLTLGSWKKALSPALDDDSIQEILISYHNATLSAKDWGKAWHIWALFNTEVMSRYTFRGRPDIAGKYVVAAVTGYFYSIACASTTKGVDDSLQDILRLLTLWFNHGDTSEVQTALQKGFSLVKIEMWLVVLPQIIARIHSNNRVVRELIQSLLVRIGKGHPQALMYPLLVACKSISILRQRAAQEVVDKIRQHSGGLVDQAQLVSKELIRVAILWHEMWHEALEEASRMYFGEHNIEGMLAVLEPLHAMLERGDETIKENAFIQAYGHELLEAHECCLKYRATGEDAELTKAWDLYYHVFRRIDKQLPSLTTLDLHSVSPELLKCRKLELAVPGTYAADSPLVTIEYFVPQLIVITSKQRPRKLTIHGSDGNDYAFLLKGHEDLRQDERVMQLFGLVNTLLENSRKTSEKDLSIQRYAVIPLSPNSGLIGWVPNCDTLHALIREYRDARKIFLNQEHRLMLAFAPDYDHLPLIAKVEVFQHALQNTEGNDLAKVLWLKSRTSEVWLERRTNYARSLAVMSMVGYLLGLGDRHPSNLMLDRYSGKILHIDFGDCFEASMNREKFPEKVPFRLTRMLVKAMEVSGIEGTFRTTCENVMQVLRTNRDSVMAMMEAFVHDPLINWRLFNFNEVPQVSNYGNVHAHTVVSSEEAVANRELMQPQRGARERELLQAVNQLGDANEVLNERAVAVMARMSDKLTGRDFSSGSALAGAGGVRSGELSWKQ

Zea mays (Maize)

2.7.11.1

CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00001433}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775, ECO:0000256|RuleBase:RU364109};

ATP-binding;Kinase;Nucleotide-binding;Repeat;Serine/threonine-protein kinase;Transferase

dephosphorylation [GO:0016311]; embryo development ending in seed dormancy [GO:0009793]; gravitropism [GO:0009630]; negative regulation of defense response to virus [GO:0050687]; negative regulation of macroautophagy [GO:0016242]; phosphorylation [GO:0016310]; positive regulation of abscisic acid biosynthetic process [GO:0010116]; positive regulation of auxin mediated signaling pathway [GO:0010929]; positive regulation of brassinosteroid mediated signaling pathway [GO:1900459]; positive regulation of cell growth [GO:0030307]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of embryonic development [GO:0040019]; positive regulation of glucose mediated signaling pathway [GO:1902661]; positive regulation of rRNA processing [GO:2000234]; response to auxin [GO:0009733]; response to rapamycin [GO:1901355]; response to virus [GO:0009615]; rRNA transcription [GO:0009303]; sucrose mediated signaling [GO:0009745]; TOR signaling [GO:0031929]

cytoplasm [GO:0005737]; nucleus [GO:0005634]; ribosome [GO:0005840]; TORC1 complex [GO:0031931]; TORC2 complex [GO:0031932]

ATP binding [GO:0005524]; identical protein binding [GO:0042802]; protein self-association [GO:0043621]; protein serine/threonine kinase activity [GO:0004674]; protein-containing complex binding [GO:0044877]; transcription cis-regulatory region binding [GO:0000976]

IPR011989;IPR016024;IPR009076;IPR036738;IPR011009;IPR024585;IPR000403;IPR036940;IPR018936;IPR003151;IPR014009;IPR026683;IPR011990;

1.20.120.150;1.25.10.10;1.10.1070.11;1.25.40.10;

A0A1D6UPT7

MAAPAGVRLARCHVTRGCGPCPGGSVRDRAGSRAGGGSALAPPEQTCRRAGDTAVTTEPAGTNTAATAASRAGGAGDQAASLPPPPPRMPRRKRNAGSSSDGTEDSDFSTDPEHTDSSESDATSRRSARVTRSSARLSQSSQDSSPVRNPPSFGAEEPVYSTRRVTRSQQQPAPVTPKKYPLRQTRSSGSETEQVVDFSDRDTKNAADHDESPPRTPTGNAPSSESDIDISSPNVSHDESIAKDMSMKDSGSDLSHRPKRRRFHESYNFNMKCPTPGCNSLGHLTGKHERHFSISGCPLYHNLSADECKVRAQSRDKQIEERMLAHRQDDNNRHATRHQAPTERQLRYKEKVAELRKKRNSGLSKEQKEKYMEHRQTYGNTREPLLENLTSEYDLELFRRAQARASEDLEKLRLQGQITEGSNMIKTIAFGRYELDTWYHSPYPEEYARLGRLYMCEFCLKYMKSQTILRRHMAKCVWKHPPGDEIYRKGSISVFEVDGKKNKIYCQNLCLLAKLFLDHKTLYYDVEPFLFYVMTEADNTGCHLIGYFSKEKNSFLNYNVSCILTMPQYMRQGYGKMLIDFSYLLSKVEEKVGSPERPLSDLGLISYRSYWKEVLLRYLHNFQGKEISIKEISQETAVNPVDIVSTLQALQMLKYWKGKHLVLKRQDLIDEWIAKEAKRSNSNKIMDPSCLKWTPPKGT

Gallus gallus (Chicken)

2.3.1.48

Acetylation;Acyltransferase;Metal-binding;Nucleus;Proteomics identification;Reference proteome;Transcription;Transcription regulation;Transferase;Zinc;Zinc-finger

DNA replication-dependent chromatin disassembly [GO:0140889]; negative regulation of DNA-templated transcription [GO:0045892]; positive regulation of DNA replication [GO:0045740]; positive regulation of hematopoietic stem cell proliferation [GO:1902035]; positive regulation of protein localization to nucleus [GO:1900182]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of cell cycle [GO:0051726]; regulation of cell growth [GO:0001558]; regulation of DNA biosynthetic process [GO:2000278]; regulation of DNA-templated DNA replication initiation [GO:0030174]; regulation of nucleotide-excision repair [GO:2000819]; regulation of transcription by RNA polymerase II [GO:0006357]; response to actinomycin D [GO:0072716]; response to anisomycin [GO:0072739]; response to dithiothreitol [GO:0072720]; response to hydroxyurea [GO:0072710]; response to sorbitol [GO:0072708]; stress-activated protein kinase signaling cascade [GO:0031098]; transcription initiation-coupled chromatin remodeling [GO:0045815]

cytosol [GO:0005829]; histone H3-K14 acetyltransferase complex [GO:0036409]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; site of DNA damage [GO:0090734]

chromatin binding [GO:0003682]; DNA replication origin binding [GO:0003688]; histone H3 acetyltransferase activity [GO:0010484]; histone H3K14 acetyltransferase activity [GO:0036408]; histone H3K23 acetyltransferase activity [GO:0043994]; histone H3K4 acetyltransferase activity [GO:0044016]; histone H4 acetyltransferase activity [GO:0010485]; histone H4K12 acetyltransferase activity [GO:0043997]; histone H4K5 acetyltransferase activity [GO:0043995]; histone H4K8 acetyltransferase activity [GO:0043996]; transcription coregulator activity [GO:0003712]; zinc ion binding [GO:0008270]

SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.

IPR016181;IPR002717;IPR036388;IPR040706;IPR002515;IPR036060;

3.40.630.30;4.10.320.30;3.30.60.60;1.10.10.10;

A0A1D8PCA8

MSGNTVQRNTEQINNALNAIQHRRTTTGNESNTNTNQRQILQNPTGRDYTIYVTDDGEKYSTVERAVKSVDPPATFKPKDEQVFYPNGKPNHQFLKQHFIHEGRLHEHQAIQILKQATHLLSKEPNLLSVPAPVTICGDVHGQYYDLMKLFEVGGDPASTKYLFLGDYVDRGSFSIECLLYLYSLKINYPDTFWMLRGNHECRHLTEYFTFKNECLHKYSEELYEECLVSFNALPLAAIMNEQFFCVHGGLSPQLTSLDSLRKLHRFREPPTKGLMCDLLWADPIEEYDDDNLDQEYVTNVVRGCSFAFTYKAACKFLDRTKLLSVIRAHEAQNAGYRMYKRTKTMGFPSLLTMFSAPNYLDSYNNKAAVLKYENNVMNIRQFNASPHPYWLPHFMDVFTWSLPFVGEKVTDMLVSILNVCTEEELDEDLPFSEAEIGVTPTTTTTGATPVSPKAYPPSSRITSPHKSTKLVESRANEEEKSNDGDDDSEMTLEEKKQALRNKIIAIGKMSRMFQVLREEQENVAHLKELNRGSLPKGSLLHGADGLKNTINSFEEAKAADRVNEALPPSPEDLQRLKQEKNTRIRQQIENQEMSGPVFQRLIRRLSQS

Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)

3.1.3.16

CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; Evidence={ECO:0000256|ARBA:ARBA00001512}; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16; Evidence={ECO:0000256|ARBA:ARBA00001482, ECO:0000256|RuleBase:RU004273};

COFACTOR: Name=Fe(3+); Xref=ChEBI:CHEBI:29034; Evidence={ECO:0000256|ARBA:ARBA00001965}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|ARBA:ARBA00001947};

Calmodulin-binding;Hydrolase;Iron;Metal-binding;Reference proteome

calcineurin-mediated signaling [GO:0097720]; cellular response to cation stress [GO:0071473]; cellular response to starvation [GO:0009267]; filamentous growth [GO:0030447]; filamentous growth of a population of unicellular organisms [GO:0044182]; filamentous growth of a population of unicellular organisms in response to biotic stimulus [GO:0036180]; filamentous growth of a population of unicellular organisms in response to starvation [GO:0036170]; fungal-type cell wall organization [GO:0031505]; hyphal growth [GO:0030448]; regulation of apoptotic process [GO:0042981]

calcineurin complex [GO:0005955]; cytoplasm [GO:0005737]; cytosol [GO:0005829]

calcium-dependent protein serine/threonine phosphatase activity [GO:0004723]; calmodulin binding [GO:0005516]; calmodulin-dependent protein phosphatase activity [GO:0033192]; metal ion binding [GO:0046872]; myosin phosphatase activity [GO:0017018]

IPR004843;IPR029052;IPR041751;IPR043360;IPR006186;

3.60.21.10;

A0A1D8PCN0

MSNEYILVTGGAGYIGSHTVIELISNGYKVVIVDNLSNSSYDAVARIEFIVKQHVPFYDVDIRNYEQLNKVFQDYKISGVIHFAALKAVGESTKIPLAYYDNNVSGTVNLLEVCKANDVKTIVFSSSATVYGDVTRFGDNSMIPIPEHCPMDPTNPYGRTKFIIESILKDIYNSDDAWKVAILRYFNPIGAHPSGLLGEDPLGIPNNLLPYLAQVAIGRREKLSIFGNDYNSRDGTPIRDYIHVVDLAKGHIAALAYLKNLQSKGLYREWNLGTGKGSTVFEVYHAFSKVVGRELPHEVVGRRAGDVLDLTAKPDRANKELQWKTELAIDDACKDLWKWTTENPFGFNIENYSWKEFDGFNNRLHSFVAGDLKVNLANRGALIQAITLKDSNMVKAYNNAEDFKSETNPFFGTTVGRYANRISNGEFKLNGKVYKLTKNEGANNLHGGANGFDKQDFFGPVVKSRDGKFFVDFLLVDKDGNDGFPGELEAIVHYTIDDSSVEIEYECQLLSGEATIVNMTNHSYFNVSNSDTIEGTEVKLITDKMLEVDSQLLPTGKFIENEKAASPIVLNENDVFDNCFIVDEECGIDTRDKPLKQVFEATSFVTNNKLKISTTEPAFQFYTGDGVNTKGFGKRCGFCVEPSRFINAINHKEWSNQVILKKGDVYGSKIKYEFQ

Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)

5.1.3.2

CATALYTIC ACTIVITY: Reaction=UDP-alpha-D-glucose = UDP-alpha-D-galactose; Xref=Rhea:RHEA:22168, ChEBI:CHEBI:58885, ChEBI:CHEBI:66914; EC=5.1.3.2; Evidence={ECO:0000256|ARBA:ARBA00000083};

COFACTOR: Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000256|ARBA:ARBA00001911};

PATHWAY: Carbohydrate metabolism; galactose metabolism. {ECO:0000256|ARBA:ARBA00004947}.

Isomerase;Reference proteome

cellular response to glucose starvation [GO:0042149]; cellular response to oxidative stress [GO:0034599]; filamentous growth [GO:0030447]; filamentous growth of a population of unicellular organisms [GO:0044182]; fungal-type cell wall biogenesis [GO:0009272]; galactose catabolic process [GO:0019388]; galactose catabolic process via UDP-galactose [GO:0033499]; invasive growth in response to glucose limitation [GO:0001403]; negative regulation of filamentous growth of a population of unicellular organisms [GO:1900429]; negative regulation of flocculation [GO:0060257]; UDP-galactose biosynthetic process [GO:0052574]

cytosol [GO:0005829]

carbohydrate binding [GO:0030246]; UDP-glucose 4-epimerase activity [GO:0003978]

IPR008183;IPR011013;IPR047215;IPR014718;IPR016040;IPR036291;IPR005886;

2.70.98.10;3.40.50.720;3.90.25.10;

A0A1D8PCV9

MAEVLSLVDLEIPQVTDKYYKFDTFKHLICHLFKKTSTETDSNVPIVIIFPTNNDIPSRKTRSTTTTTTTTTTTNTSKLDNLPFSDKSLLIQFFFTHLNILMIQGENSDEGKLYQEISSAKELLTNRISRVGNWTGTTHFRYCRHENDCGLLNQHSKIAGIIPTMTYILNCNATRSEIATNQLIYLYRLMIEEINFIELLQDASTTRLSQLCYAVGHWSFPAHNLSNDDLVYCVYLMIDYAIKQVEGFDNIPLNELLAFIFIVRDTYKNGNPFHNFRHAVDVLQACFHFLIRLGSLPKFKQFVEDPKLDYTEVHDTHTVLIALQNNSSEEKASLNPIQTLGLLVAALGHDVGHPGTTNDFMIKFSAPTALLYNDRSVLESYHASLFINKVLRICWPDLLTCTIEEKSELTIRSLIISSILATDMGEHNEYVNRLKSFKTHNEILNHDNTVKLISALLIKCADISNVTRPLRVSAQWAMVLSREFAEVELLKSVIKKDIDLDFTKDLTYDHVPHELREILEIQPDIHKGQIFFINLFAENLFNSVSDLLPQLQYTCDIIMENKLFWLERAKK

Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)

3.1.4.-

COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000256|RuleBase:RU363067}; Note=Binds 2 divalent metal cations per subunit. Site 1 may preferentially bind zinc ions, while site 2 has a preference for magnesium and/or manganese ions. {ECO:0000256|RuleBase:RU363067};

Hydrolase;Metal-binding;Reference proteome

adhesion of symbiont to host [GO:0044406]; cAMP-mediated signaling [GO:0019933]; cell adhesion involved in single-species biofilm formation [GO:0043709]; cell-abiotic substrate adhesion [GO:0036164]; cellular developmental process [GO:0048869]; cellular response to carbon dioxide [GO:0071244]; cellular response to starvation [GO:0009267]; cGMP catabolic process [GO:0046069]; filamentous growth [GO:0030447]; fungal-type cell wall organization [GO:0031505]; negative regulation of filamentous growth [GO:0060258]; negative regulation of phenotypic switching [GO:1900240]; plasma membrane organization [GO:0007009]; regulation of cell morphogenesis [GO:0022604]; response to neutral pH [GO:0036176]

cytosol [GO:0005829]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]

3',5'-cyclic-AMP phosphodiesterase activity [GO:0004115]; 3',5'-cyclic-GMP phosphodiesterase activity [GO:0047555]; cyclic-nucleotide phosphodiesterase activity [GO:0004112]; metal ion binding [GO:0046872]

IPR003607;IPR002073;IPR036971;IPR023174;

1.10.1300.10;

A0A1D8PD38

MSFSFGINNISKGNNTYKDKPAGGALPLFYKDKVPAFHPAHTSKNKKRILMLLKGFMLSLVLYAVYHLASNGGQFMFDFSGQSKWERAQSEVRQAMLDSWHTYEKYGWGYDVYHPIKQEGEIMGPKPLGWMIVDSLDTLMIMDCPEEVSRARDWIKNDLDYTFDYNVNTFETTIRMLGGLLSAYHFSNDDVYLDKAVQLANALHGAYDSPSGIPYSSVNLKSGKGIKNHVDNGASSTAEAATVQLEMKYLSKLTGEILWWNLAEKVMQVLESNKPQDGLVPIYVNPDTGKYQGHLIRLGSRGDSYYEYLLKQYLQTNKQELVYWDMYRESVEGVKKHLVSDSYPSGLTFIGELDNGIGGKLSTKMDHLVCFYGGLLALGATGGLTLNEAQSLKSWNEEREADFKLGEELTYTCYKMYHDVSPTGLSPEIVVFNEDTSKSKDFIIKPLDRHNLQRPETVESLFYLYRLTGDVKYREMGYEIFQNFIKYTKVVNSEGEVSFSSLSDVTSFDSNGLPKFKDNTESFWWAETLKYLYLLFDDTNKIPLTDYVFNTEAHPFPRFDTNDYFKTGWRRKIDENEKAQMRESKVIDKSNLPEAQPVDKSADQEAKEIIEEIAG

Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)

3.2.1.-

COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000256|ARBA:ARBA00001913, ECO:0000256|PIRSR:PIRSR601382-2};

PATHWAY: Protein modification; protein glycosylation. {ECO:0000256|ARBA:ARBA00004922}.

Calcium;Disulfide bond;Glycosidase;Hydrolase;Membrane;Metal-binding;Reference proteome;Transmembrane;Transmembrane helix

cellular response to mechanical stimulus [GO:0071260]; filamentous growth [GO:0030447]; filamentous growth of a population of unicellular organisms [GO:0044182]; filamentous growth of a population of unicellular organisms in response to biotic stimulus [GO:0036180]; fungal-type cell wall polysaccharide biosynthetic process [GO:0051278]; hyphal growth [GO:0030448]; N-glycan processing [GO:0006491]

endoplasmic reticulum [GO:0005783]; endosome [GO:0005768]; membrane [GO:0016020]; trans-Golgi network [GO:0005802]

calcium ion binding [GO:0005509]; mannosyl-oligosaccharide 1,2-alpha-mannosidase activity [GO:0004571]

IPR012341;IPR001382;IPR036026;

1.50.10.10;

A0A1D8PDV7

MATLSQPQSALPKTKIATTFGLSKDLKSPISVKVCYLECTRNNVSLVPLSTKFEDPTVFKKLSQIYKNSDLFVEIRVYDGKNNNLISTPVRTSYKAFNNKGRTWNQQLKLNIDYNQISIDAYLKFSICEIIDTKPSVFGVSYLSLFSHDSSTLRSGSHKIPVFMEDDPQYSKNIQYGTLIGLTDLEKRLIDYENGKYPRLNWLDKMVLPKVDATFLKTNNKDHDYYLYIELPQFEFPIVYSDIIYQIPTIEPITETTSKIPPDDTLNSNIIINSIDIPMATSHDPSIMKVYDPDFHITANNHLNPNATTFDPVELKYRKLERNIDNNTILDKELKPTPQLRDELLRIMIKPSNAELTDNEKNLIWKFRYYFSKNNSGNDPSNKSVKSFLPKFLRSINWENDYELDHTFKEIIPFYWNVDKLQIGDALELLGDYFNPYTLGKPTYQDDSMTSKSSKMKSDEKRFIKIYNNVCFLRKLAVERLKLANSEELLLYLLQLVQALKYEALIYEKSPPFCERSDQIEDNASSTLKSPLADFLIERAVENEKLGNFFYWYVKVENEDQLNNPHIDGPIKIYMDILNRYIELLKAHCHENRLPYYKHLKHQIWFIKKLTSLVELLRASFKKNEATAKKVEYLREYLANSGNELLKFPEPFPLPLDPSVMICGCYPEESSVFKSSLAPLKITLKTIEKKKHGHATSQLFGKRSRYGKYPLMFKIGDDLRQDQLVIQIIDLMDQLLKNENLDLKLTPYKILATSPISGLIQFVPNETLDSILSKTYPTSVTYSGGGETSDVPPSVSNNGILNYLRLHSQEQQSEEPISKSILSTNTSQSNTEIPVLPRQPKPTITSDLGVSPILMDNYVKSCAGYCVITYILGVGDRHLDNLLLSPNGKFWHADFGYILGRDPKPFPPLMKLPIQVIDGMGGLHHENYNVFKSYCFITYTTLRKNSNLILNLFQLMLDANIPDIQFDPSRVIEKVQEKFCLQMTEEEAILHFQNLINDSVNAFLPVVIDRLHSLAQYWRA

Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)

FUNCTION: Multifunctional phosphatidylinositol 3-kinase involved in acidification of vacuoles, pH-dependent cell growth, and autophagocytosis (PubMed:15632428, PubMed:15861817). Plays an important role in protein transport and virulence (PubMed:11223944, PubMed:15632428). Component of the autophagy-specific VPS34 PI3-kinase complex I essential to recruit the ATG8-phosphatidylinositol conjugate and the ATG12-ATG5 conjugate to the pre-autophagosomal structure (By similarity). Also involved in endosome-to-Golgi retrograde transport as part of the VPS34 PI3-kinase complex II (By similarity). This second complex is required for the endosome-to-Golgi retrieval of PEP1 and KEX2, and the recruitment of VPS5 and VPS7, two components of the retromer complex, to endosomal membranes (probably through the synthesis of a specific pool of phosphatidylinositol 3-phosphate recruiting the retromer to the endosomes) (By similarity). Finally, it might also be involved in ethanol tolerance and cell wall integrity (By similarity). {ECO:0000250|UniProtKB:P22543, ECO:0000269|PubMed:11223944, ECO:0000269|PubMed:15632428, ECO:0000269|PubMed:15861817}.

2.7.1.137

CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + ADP + H(+); Xref=Rhea:RHEA:12709, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57880, ChEBI:CHEBI:58088, ChEBI:CHEBI:456216; EC=2.7.1.137; Evidence={ECO:0000269|PubMed:10870104, ECO:0000269|PubMed:15632428}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12710; Evidence={ECO:0000269|PubMed:10870104, ECO:0000269|PubMed:15632428};

ATP-binding;Endosome;Golgi apparatus;Kinase;Membrane;Nucleotide-binding;Reference proteome;Transferase

ascospore-type prospore membrane formation [GO:0032120]; autophagosome assembly [GO:0000045]; autophagy [GO:0006914]; cellular response to osmotic stress [GO:0071470]; cellular response to starvation [GO:0009267]; endocytosis [GO:0006897]; filamentous growth [GO:0030447]; filamentous growth of a population of unicellular organisms in response to biotic stimulus [GO:0036180]; filamentous growth of a population of unicellular organisms in response to starvation [GO:0036170]; nuclear division [GO:0000280]; nuclear migration along microtubule [GO:0030473]; pexophagy [GO:0000425]; phosphatidylinositol phosphate biosynthetic process [GO:0046854]; phosphatidylinositol-3-phosphate biosynthetic process [GO:0036092]; phosphatidylinositol-mediated signaling [GO:0048015]; phosphorylation [GO:0016310]; positive regulation of transcription elongation by RNA polymerase II [GO:0032968]; vacuolar protein processing [GO:0006624]; vacuolar transport [GO:0007034]; vacuole organization [GO:0007033]; vesicle-mediated transport [GO:0016192]

cytoplasm [GO:0005737]; endosome [GO:0005768]; endosome membrane [GO:0010008]; fungal-type vacuole membrane [GO:0000329]; Golgi apparatus [GO:0005794]; membrane [GO:0016020]; nucleus-vacuole junction [GO:0071561]; peroxisome [GO:0005777]; phagophore assembly site [GO:0000407]; phosphatidylinositol 3-kinase complex, class III, type I [GO:0034271]; phosphatidylinositol 3-kinase complex, class III, type II [GO:0034272]

1-phosphatidylinositol-3-kinase activity [GO:0016303]; ATP binding [GO:0005524]; protein kinase activity [GO:0004672]

SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:P22543}; Peripheral membrane protein {ECO:0000250|UniProtKB:P22543}. Endosome membrane {ECO:0000250|UniProtKB:P22543}; Peripheral membrane protein {ECO:0000250|UniProtKB:P22543}.

PTM: Autophosphorylated. {ECO:0000269|PubMed:15632428}.

IPR016024;IPR035892;IPR011009;IPR000403;IPR036940;IPR018936;IPR002420;IPR001263;IPR042236;IPR008290;IPR015433;

2.60.40.150;1.10.1070.11;1.25.40.70;

A0A1D8PF32

MSDSSATGFSKHQESAIVSDSEGDAIDSELHMSANPPLLRRSSSLFSLSSKDDLPKPDSKEYLKFIDDNRHFSMIRNLHMADFITLLNGFSGFYSIISCLRYTLTGQTHYVQRAHFFILLGLFFDFFDGRVARLRNKSSLMGQELDSLADLVSFGVSPATIAFAIGFRTTVDVLFLAFWVLCGLTRLARFNISVNNIPKDKHGKSQYFEGLPIPTNLFWVGFMALLVYKDWIHDNLPFGIVFQDTSFEFHLVTIGFVLQGCAEISKSLKIPKP

Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)

2.7.8.8

CATALYTIC ACTIVITY: Reaction=a CDP-1,2-diacyl-sn-glycerol + L-serine = a 1,2-diacyl-sn-glycero-3-phospho-L-serine + CMP + H(+); Xref=Rhea:RHEA:16913, ChEBI:CHEBI:15378, ChEBI:CHEBI:33384, ChEBI:CHEBI:57262, ChEBI:CHEBI:58332, ChEBI:CHEBI:60377; EC=2.7.8.8; Evidence={ECO:0000256|ARBA:ARBA00000287, ECO:0000256|PIRNR:PIRNR000852};

PATHWAY: Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step 1/2. {ECO:0000256|PIRNR:PIRNR000852}.

Endoplasmic reticulum;Lipid biosynthesis;Lipid metabolism;Membrane;Phospholipid biosynthesis;Phospholipid metabolism;Reference proteome;Transferase;Transmembrane;Transmembrane helix

cell wall organization or biogenesis [GO:0071554]; cellular response to starvation [GO:0009267]; filamentous growth [GO:0030447]; filamentous growth of a population of unicellular organisms in response to biotic stimulus [GO:0036180]; filamentous growth of a population of unicellular organisms in response to chemical stimulus [GO:0036171]; filamentous growth of a population of unicellular organisms in response to starvation [GO:0036170]; phosphatidylethanolamine biosynthetic process [GO:0006646]; phosphatidylserine biosynthetic process [GO:0006659]; phospholipid metabolic process [GO:0006644]; plasma membrane organization [GO:0007009]

endoplasmic reticulum membrane [GO:0005789]; mitochondrial outer membrane [GO:0005741]

CDP-diacylglycerol-serine O-phosphatidyltransferase activity [GO:0003882]; diacylglycerol binding [GO:0019992]; serine binding [GO:0070905]

SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.

IPR004533;IPR016271;IPR000462;IPR043130;IPR048254;

1.20.120.1760;

A0A1D8PFP3

MGIPKFFRFISERWPLISQLIDENQIPEFDNLYLDMNSILHTCTHSNDNTITRLSDDQMYAAIFNYIEHLFQIIKPQKTFYMAIDGVAPRAKMNQQRARRFRTAYEAEINLKKAIENGEEIPKEDPFDSNSITPGTEFMANLTNNLKYFIHKKITEDSSWANIEIILSGHEVPGEGEHKIMEYIRSIRSQDDYNPNLRHCIYGLDADLIMLGLVTHDPHFALLREEVTFGPQRKVGPKDLHDQKFYLLHLSLLREYLSLEFQEIENQLNFEYDFDRILDDFILIMYVIGNDFLPNLPDLFINKGAFPLLIAAFKQTLLESDGYINENGKINLVRLNIYIKILSKFEFENFEKHEVDVEWFNKKLDDISISGEKKRQRIGKLLILKEQKKLVGFIKPWLMEWASQPINEILNLDQQGKLPTLHLNKDDVEKNLEFIKEFAIEAGFLIIHSQSNDTYEAKLDIDGISPTESEEEHEERITELRKTIKQYQSANLIESEEVLNETKEVYSEKFQSWKNDYYQPKLHFSIDTEEGKGDLIEMTKHYIEGLQWVLYYYYRGCPSWNWYYRYHYAPRISDISLGLEELINEKTDLKFELSHPFKPFEQLMAVLPARSKKLMPVVYRPLMTDEKSPIINFYPHEVDIDMNGKTASWEAVVLLDFVDEKKLIEALKPIESKLTPEEKQRNSYGHAIKFIHNPQIDHVFSSPLPGFFHDIEHDQCYEEEFKLPKIENLKIGFIKGAKTGKDLLAGFPTLSTIPFTSELALNEVKIFNFPSRSESMILNVEDVWSDLTVAQFAQSFVNKLVYSKWPFLRECRVVKVVSEENKFESIKTNTGLKKVVTNELSVEDKKSFRSEVSNLKVTWDKFKGVKLGEINALVYVKPVNGLIRNHKGAYVKTYSKDVEVYPLQLIVKEVTNKDQRYLTRPPLPIDQEFPIDSQVVFLGDMAYGSPAKIVGYNEDKTKLGVKIFKIQSTAEPNIGKKRLTIEKNEIKYYPSFEVAKTLRLNPLLLSKITSQFMVQDSSKGKVNIGLELKFESKRQKVLGYTRKSSNGKFWEFSPLAINLINTYKTKFPGLFKKLVNNVSGSNFPTVDEISSLEELKEIRSWLKEVKSELIPVSLESESFTKFSYQAIEQYMDNYLSMNQIPTINKDIKGVPREAILNANESYQLLSDQRFELGDRIIYVQDFGKVSILSKGTVASILTVGSKTSLGVIFDQPLLSGNNMNGKLNSNRGLIIDSSLVLNLTNKQFVYHSHASKNRKKLTDEEKIAKLKAIEAKKNQKQQQQQKEQQTKQKQVEQQKQKGANELLSLLKKKSDMNSTTTTSTTDGDCKKTEEKDYDKNNGNEDERVDPNAIKQIYGHIYSNVMNQGNVRPPPPPPTGPGHPQQFPYGMPIPPPGAPMHPGYIPVVPGNPLPPSFYQQYPPNGQQFVNSQPPPPPPPPPSQQQQPQVAESTSDEKSKNDNKHNVNGRGRGGSRGRGGYRGRGGVRGGRGGNKSSHQNQPKDKVKQES

Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)

FUNCTION: Multifunctional protein that exhibits several independent functions at different levels of the cellular processes. 5'-3' exonuclease component of the nonsense-mediated mRNA decay (NMD) which is a highly conserved mRNA degradation pathway, an RNA surveillance system whose role is to identify and rid cells of mRNA with premature termination codons and thus prevents accumulation of potentially harmful truncated proteins. {ECO:0000256|PIRNR:PIRNR006743}.

3.1.13.-

Cytoplasm;Exonuclease;Hydrolase;Nonsense-mediated mRNA decay;Nuclease;Reference proteome;RNA-binding

cellular response to neutral pH [GO:0036244]; cellular response to starvation [GO:0009267]; filamentous growth [GO:0030447]; filamentous growth of a population of unicellular organisms in response to neutral pH [GO:0036178]; filamentous growth of a population of unicellular organisms in response to pH [GO:0036177]; filamentous growth of a population of unicellular organisms in response to starvation [GO:0036170]; mRNA destabilization [GO:0061157]; negative regulation of macroautophagy [GO:0016242]; nonfunctional rRNA decay [GO:0070651]; nuclear-transcribed mRNA catabolic process [GO:0000956]; nuclear-transcribed mRNA catabolic process, 5'-3' exonucleolytic nonsense-mediated decay [GO:0070479]; positive regulation of transcription elongation by RNA polymerase II [GO:0032968]; positive regulation of transcription initiation by RNA polymerase II [GO:0060261]; rRNA catabolic process [GO:0016075]; rRNA processing [GO:0006364]; single-species biofilm formation on inanimate substrate [GO:0044011]; sno(s)RNA processing [GO:0043144]; stress granule assembly [GO:0034063]; translational initiation [GO:0006413]; traversing start control point of mitotic cell cycle [GO:0007089]; tRNA catabolic process [GO:0016078]

cytoplasmic stress granule [GO:0010494]; eisosome membrane domain/MCC [GO:0090512]; nucleus [GO:0005634]; P-body [GO:0000932]

5'-3' RNA exonuclease activity [GO:0004534]; chromatin binding [GO:0003682]; DNA strand exchange activity [GO:0000150]; eukaryotic initiation factor 4G binding [GO:0031370]; microtubule binding [GO:0008017]; RNA binding [GO:0003723]

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR006743}.

IPR027073;IPR016494;IPR014722;IPR041385;IPR040992;IPR047007;IPR041106;IPR041412;IPR004859;IPR047008;

1.25.40.1050;2.170.260.40;2.30.30.30;2.30.30.750;3.30.1370.250;3.40.50.12390;6.10.140.950;

A0A1D8PG96

MRSSQSSWLPRIGLLYVALVILIPFLVSPKHAFAVAAVSDDESSTDNYGTVIGIDLGTTYSCVGVMKNGKVEILANDQGNRITPSYVSFNGDERLVGDAAKNQASSNVNNTVFDIKRLIGLKYNDDTVQKELKHLPYKIENKGNKPVVKVEYQGEEKTFSPEEISSMVLGKMKSIAEDYLGKKVTHAVVTVPAYFNDAQRQATKDAGTIAGLNVLRIVNEPTAAAIAYGLDKGDQEKQIIVYDLGGGTFDVSLLSIEGGVFEVLATAGDTHLGGEDFDFKIVRYLAKQFKKKHNIDITANAKAISKLKREAEKAKRTLSSQMSTRVEIDSFVDGIDFSETLSRAKFEELNIAAFRKTLKPVEQVLKDGGVKKSDIDDIVLVGGSTRIPKVQELLEGFFDGKKASKGINPDEAVAYGAAVQAGVLSGEEGVDDIVLLDVNPLTLGIETSGGVMTTLIKRNTAIPTKKSQIFSTAADNQPTVLIQVYEGERTMAKDNNRLGKFELTGIPPAPRGVPQIEVTFSLDANGILKVEAADKGTGKSESITITNEKGRLSKDEIDRMVEEAEKYAQQDQELKEKIEARNSLENYAHVLRGQLSDTSETGLGSKLDDDDKETLDDAIKETLEFIEDNFDTATAEEFEEQKQKLIDVANPITAKLYGGAAGEGAGGAGDAKFGDDDSDDEFDHDEL

Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)

FUNCTION: Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. Is required for secretory polypeptide translocation. May physically associate with SEC63 protein in the endoplasmic reticulum and this interaction may be regulated by ATP hydrolysis. {ECO:0000256|ARBA:ARBA00002226}.

3.6.4.10

CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.10; Evidence={ECO:0000256|ARBA:ARBA00001629};

ATP-binding;Endoplasmic reticulum;Nucleotide-binding;Reference proteome;Signal

chaperone cofactor-dependent protein refolding [GO:0051085]; endoplasmic reticulum unfolded protein response [GO:0030968]; ERAD pathway [GO:0036503]; fungal-type cell wall beta-glucan biosynthetic process [GO:0070880]; IRE1-mediated unfolded protein response [GO:0036498]; karyogamy involved in conjugation with cellular fusion [GO:0000742]; post-translational protein targeting to membrane, translocation [GO:0031204]; protein folding [GO:0006457]; protein refolding [GO:0042026]; SRP-dependent cotranslational protein targeting to membrane, translocation [GO:0006616]

cell surface [GO:0009986]; cortical endoplasmic reticulum lumen [GO:0099021]; cytoplasm [GO:0005737]; endoplasmic reticulum chaperone complex [GO:0034663]; endoplasmic reticulum lumen [GO:0005788]; extracellular region [GO:0005576]; luminal surveillance complex [GO:0034099]; membrane [GO:0016020]; nuclear membrane [GO:0031965]; nucleus [GO:0005634]; perinuclear endoplasmic reticulum lumen [GO:0099020]

ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent protein folding chaperone [GO:0140662]; heat shock protein binding [GO:0031072]; protein folding chaperone [GO:0044183]; protein-transporting ATPase activity [GO:0015450]; unfolded protein binding [GO:0051082]

IPR043129;IPR042050;IPR018181;IPR029048;IPR029047;IPR013126;

1.20.1270.10;3.30.30.30;3.30.420.40;

A0A1D8PHA3

MFRTAYKTMNQSMVQKFIAGGVGVTGLTASYLLYQDSMTADAMTAAEHGLHPPAYNWPHNGMFETFDHASIRRGFQVYREVCAACHSLDRIAWRNLVGVSHTTSEAKAMAEELEYDDEPDDEGKPRKRPGKLADYIPGPYENEQAARAANQGAYPPDLSLIVKARHGGSDYIFSLLTGYPDEPPAGVVLPEGSNYNPYFPGGAIAMGRVLFDDLVEYEDGTPATTSQMAKDVSTFLNWASEPEHDDRKKWGLKALVVLSSLYLLSIWVKRFKWTPIKNRKFRFDPPKK

Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)

FUNCTION: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation (PubMed:34525326, PubMed:36923588). The complex plays an important role in the uptake of multiple carbon sources present in different host niches (PubMed:36923588). {ECO:0000269|PubMed:34525326, ECO:0000269|PubMed:36923588}.

7.1.1.8

CATALYTIC ACTIVITY: Reaction=a quinol + 2 Fe(III)-[cytochrome c](out) = a quinone + 2 Fe(II)-[cytochrome c](out) + 2 H(+)(out); Xref=Rhea:RHEA:11484, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:132124; EC=7.1.1.8; Evidence={ECO:0000250|UniProtKB:P07143};

COFACTOR: Name=heme c; Xref=ChEBI:CHEBI:61717; Evidence={ECO:0000250|UniProtKB:P07143}; Note=Binds 1 heme c group covalently per subunit. {ECO:0000250|UniProtKB:P07143};

3D-structure;Electron transport;Heme;Iron;Membrane;Metal-binding;Mitochondrion;Mitochondrion inner membrane;Reference proteome;Respiratory chain;Translocase;Transmembrane;Transmembrane helix;Transport

mitochondrial electron transport, ubiquinol to cytochrome c [GO:0006122]

mitochondrial respiratory chain complex III [GO:0005750]; plasma membrane [GO:0005886]

electron transfer activity [GO:0009055]; heme binding [GO:0020037]; metal ion binding [GO:0046872]; ubiquinol-cytochrome-c reductase activity [GO:0008121]

SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P07143}; Multi-pass membrane protein {ECO:0000255}.

IPR009056;IPR036909;IPR002326;IPR021157;

1.10.760.10;1.20.5.100;

A0A1D8PHD2

MQEVLFTYHQRSDQPPPPPSQQSHLHASTPTPTPLSNMKRKQSSESDDPFKDRSCKSRKDASTANLLRLQQSLSNSTFIRNSNLSKSYKHNETTEVANNNLHDTTFSQTTETEEFVTPNQLDEQLEVAGRGGRGVVVEEEQREEEEEEEEVTLEVLENMQKLETNFPILATDYRLIDKIGEGTFSTVYKAESLTGKIRLGSDIWKSPPLKRNKRNILNFQQSRKKNPIVALKQIYVTSSPNRIFNELHLLYMLSGNSRVAPLLDVLRFQDQIVAILPYYNHCDFREFYRDLPVKGIKKYLWELFQALDYIHGKGVIHRDLKPTNFLYDPFRGKGVLVDFGLAERENISKNTKPETSTTSSSGTATTTTTATTTTTTTTTTTTNSSTASSSAISTACPCLNKDQKLINRTHTKRLNVKGAYPKNDNRPPRRANRAGTRGFRAPEVLFKCTNQSTKIDIWSAGIIGFSILLRKFPIFNSPTDTDAILELAWIFGYDKMAKCAELHGCGLEISMPEIHKSNGNLIKIMYDFLMQEHINGCFPSDSVVYDTLELINESGEKFVKPVYTIREGISDIEKMKINEDFTKRHDDYKDHKYLMELLYGCFKMDPSKRLSAREILQLPFFHEILQISEDDTQDEFMQQNQTQTQEEEEEDEVILS

Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)

2.7.11.1

Kinase;Reference proteome;Serine/threonine-protein kinase;Transferase

DNA replication initiation [GO:0006270]; double-strand break repair via break-induced replication [GO:0000727]; G1/S transition of mitotic cell cycle [GO:0000082]; mitotic DNA damage checkpoint signaling [GO:0044773]; mitotic DNA replication checkpoint signaling [GO:0033314]; mitotic DNA replication preinitiation complex assembly [GO:1902977]; negative regulation of exit from mitosis [GO:0001100]; negative regulation of filamentous growth [GO:0060258]; phosphorylation [GO:0016310]; positive regulation of kinetochore assembly [GO:1905561]; positive regulation of meiosis I [GO:0060903]; positive regulation of meiotic DNA double-strand break formation involved in reciprocal meiotic recombination [GO:1905263]; positive regulation of spindle attachment to meiosis I kinetochore [GO:1904968]; premeiotic DNA replication [GO:0006279]; protein-containing complex localization [GO:0031503]; regulation of G2/M transition of mitotic cell cycle [GO:0010389]; regulation of gene expression [GO:0010468]; response to organic substance [GO:0010033]; signal transduction [GO:0007165]

chromatin [GO:0000785]; chromosome, centromeric region [GO:0000775]; cyclin-dependent protein kinase holoenzyme complex [GO:0000307]; cytoplasm [GO:0005737]; Dbf4-dependent protein kinase complex [GO:0031431]; nucleus [GO:0005634]

ATP binding [GO:0005524]; cyclin binding [GO:0030332]; cyclin-dependent protein serine/threonine kinase activity [GO:0004693]; identical protein binding [GO:0042802]; protein kinase activity [GO:0004672]; protein serine/threonine kinase activity [GO:0004674]

IPR011009;IPR000719;IPR008271;

1.10.510.10;

A0A1D8PJA8

MKFSSTTLLAGLSSLTATVSAGCSFEGGNYYCSETKKVIYKGIGFSGTYMDVTNMDESTGKCTQQSYSFSGNLSPLDEELSVHFRGPLTLLQFGVYYPSSSGNSKRQIDDQDCNVKHVHHKHKRATEVVQVTQTVFVDGNGNTVTSQALQTSTVESSPAVSSAAADDNANSGSGSGSSAGSGSGYGSVSALDGEGKAYRSDISTKSAPTSTSAQPSSSETASVDGAWTRDSYYTPGSTDNCVFLNYHGGSGSGVWSAKFGNSLSYANADNSGGSSTPVPLEETTIKSGEEYIIFSGSKCGSSSDCGYYRKGTVAYHGFKGASKIFVFEFEMPSDTNGNGYNQDMPAVWLLNAKIPRTLQYGEATCSCWKTGCGELDLFEVLSSGSNKMISHLHDGQGSSQNSNNGGGGSQDYFERPTSGTFKGVVIFEGDEIHILQVDDETEFGSSLDEETVNAWLKEAGSVATIGY

Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)

FUNCTION: Probable circularly permuted 1,3-beta-glucanase involved in cell wall modification through beta-1,3-glucan network alterations such as increased branching or remodeling (By similarity). Plays a role in engulfment by host macrophages (PubMed:26087349). {ECO:0000250|UniProtKB:P38288, ECO:0000269|PubMed:26087349}.

3.2.1.39

CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.; EC=3.2.1.39; Evidence={ECO:0000250|UniProtKB:P38288};

Cell wall biogenesis/degradation;Glycosidase;Hydrolase;Reference proteome;Secreted;Signal;Virulence

cell wall organization [GO:0071555]; metabolic process [GO:0008152]

cell surface [GO:0009986]; extracellular region [GO:0005576]; fungal-type cell wall [GO:0009277]; hyphal cell wall [GO:0030446]

hydrolase activity, acting on glycosyl bonds [GO:0016798]

SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26453650, ECO:0000303|PubMed:17905924}.

PTM: Cleaved by KEX2 in vitro. {ECO:0000269|PubMed:18625069}.

DOMAIN: The conserved ExDxxE motif might be important for catalytic activity. {ECO:0000250|UniProtKB:P38288}.

IPR018805;IPR018807;

2.60.120.200;

A0A1D8PJX3

MSSLAFRTLRNGLGLKSSVRALSTTTTTLSNYQQPDYSSYLNNKSGQGSRNFTYFMVGSMGLLSAAGAKSTVEAFLSSFAASADVLAMAKVEVKLGAIPEGKNVIIKWQGKPVFIRHRTADEIEEANQVDIKTLRDPQNDADRVKKPEWLIMLGICTHLGCVPIGEAGDFGGWFCPCHGSHYDISGRIRKGPAPLNLEIPEYDFTDDETLLVG

Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)

FUNCTION: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation (PubMed:34525326, PubMed:36923588). The complex plays an important role in the uptake of multiple carbon sources present in different host niches (PubMed:36923588). {ECO:0000269|PubMed:34525326, ECO:0000269|PubMed:36923588}.

7.1.1.8

CATALYTIC ACTIVITY: Reaction=a quinol + 2 Fe(III)-[cytochrome c](out) = a quinone + 2 Fe(II)-[cytochrome c](out) + 2 H(+)(out); Xref=Rhea:RHEA:11484, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:132124; EC=7.1.1.8; Evidence={ECO:0000250|UniProtKB:P08067, ECO:0000255|RuleBase:RU004494};

COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000255|PROSITE-ProRule:PRU00628}; Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000255|PROSITE-ProRule:PRU00628};

2Fe-2S;3D-structure;Disulfide bond;Electron transport;Iron;Iron-sulfur;Membrane;Metal-binding;Mitochondrion;Mitochondrion inner membrane;Reference proteome;Respiratory chain;Transit peptide;Translocase;Transmembrane;Transmembrane helix;Transport

mitochondrial electron transport, ubiquinol to cytochrome c [GO:0006122]

mitochondrial respiratory chain complex III [GO:0005750]; plasma membrane [GO:0005886]

2 iron, 2 sulfur cluster binding [GO:0051537]; metal ion binding [GO:0046872]; oxidoreductase activity [GO:0016491]; ubiquinol-cytochrome-c reductase activity [GO:0008121]

SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P08067}; Single-pass membrane protein {ECO:0000250|UniProtKB:P08067}.

IPR037008;IPR017941;IPR036922;IPR014349;IPR005805;IPR004192;IPR006317;

2.102.10.10;1.20.5.270;

A0A1D8PJZ1

MEVTQRTQSQTQPTQQSPTTQTQTQSKEDQNRICQLICSTGQFGNYDLNINDKTIVQGKMTWYFGRDPNSDLQVASSSRISNKHFQIWFNFNDKSLWIKDTSTNGTHLNNSRLVKGSNYLLNQGDEIAVGVGRDEDVVRFVVVFGDKYNPAKLPDSTNTIKDEGIYKDFIVKNETIGQGAFATVKKAIERSTGESYAVKIINRRKALNTGGGSAMAGVDRELSILERLNHPNIVALKAFYEDMDNYYIVMELVPGGDLMDFVAANGAIGEDATQVITKQILEGIAYVHNLGISHRDLKPDNILIMQDDPILVKITDFGLAKFSDNSTFMKTFCGTLAYVAPEVITGKYGSSQMESQQKDNYSSLVDIWSLGCLVYVLLTSHLPFNGKNQQQMFAKIKRGEFHEAPLNSYDISEDGRDFLQCCLQVNPKLRMTAAEALKHKWLQDLYEEDSVKSLSLSQSQSQQSRKIDNGIHIESLSKIDEDVMLRPLDSERNRKSSKQQDFKVPKRVIPLSQHPATPLPMSQPKKRPYQIDPRTNKKVDLEEPSTSKKVKLSDSVVAEDYLKLEPLANSLFQETINISKSPFSFGRNDTCDCEIDDDRLSKLHCVITKENDSIWLLDKSTNSCLVNNTSVGKGNKVLLRGGEILHLFFDPLSSQHIGFKVVLVDQSSGEHKSQVEALKQTSEEMNIIPLISGLSSISS

Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)

FUNCTION: Controls S-phase checkpoint as well as G1 and G2 DNA damage checkpoints. Phosphorylates proteins on serine, threonine, and tyrosine. Prevents entry into anaphase and mitotic exit after DNA damage via regulation of the Polo kinase CDC5. {ECO:0000256|PIRNR:PIRNR000661}.

2.7.12.1

CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.12.1; Evidence={ECO:0000256|PIRNR:PIRNR000661};

ATP-binding;Cell cycle;DNA damage;Kinase;Nucleotide-binding;Nucleus;Reference proteome;Serine/threonine-protein kinase;Transferase;Tyrosine-protein kinase

autophagosome assembly [GO:0000045]; deoxyribonucleoside triphosphate biosynthetic process [GO:0009202]; DNA repair [GO:0006281]; DNA replication initiation [GO:0006270]; filamentous growth [GO:0030447]; filamentous growth of a population of unicellular organisms in response to chemical stimulus [GO:0036171]; meiotic recombination checkpoint signaling [GO:0051598]; mitotic DNA damage checkpoint signaling [GO:0044773]; negative regulation of phosphorylation [GO:0042326]; phosphorylation [GO:0016310]; positive regulation of filamentous growth of a population of unicellular organisms in response to chemical stimulus [GO:1900439]; protein localization [GO:0008104]; regulation of autophagy [GO:0010506]; signal transduction in response to DNA damage [GO:0042770]

cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]

ATP binding [GO:0005524]; DNA replication origin binding [GO:0003688]; protein serine/threonine kinase activity [GO:0004674]; protein serine/threonine/tyrosine kinase activity [GO:0004712]; protein tyrosine kinase activity [GO:0004713]

SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR000661}.

IPR000253;IPR011009;IPR000719;IPR017441;IPR008271;IPR016256;IPR008984;

2.60.200.20;1.10.510.10;

A0A1D8PKE2

MVEDKDIDLNINNLKIHDAPTRTPPVSSPPALPTPPTPSGISLNTTMQAKLMAFQQQRSKAAAAAAAAASVSSSSSGTQASSSSISASTSESSVSTIPANINRTVSGKKKPKPNLKLSDLPLSRNNSLHRSNTSASDSSVTTPEADTPTGKISNEPQPQGLFANYSDYVDIKSGQLNFAGKASLHSKGIDFSSGSSFRVSLDEFEYLEELGRGNYGSVSKVLHKPTGVLMAMKEVRLELDENKFTQILMELDILHKCDSPYIVDFYGAFFVEGAVYMCIEYMDGGSLDRIFGNDVGVKDEYELAYITESVILGLKELKDKHNIIHRDVKPTNILVNTQGKVKLCDFGVSGNLVASLAKTNIGCQSYMAPERINTMRPDDATYSVQSDVWSLGLTILELAVGHYPYPAETYDNIFSQLSAIVDGEPPKLYPKVYSKEAQIFVKSCLAKNPDLRPSYAALLNNPWLIKNRGKETNLAQTVKDRVEEIAKLEKNKSVSRSNSMNKSAAAVPPPRNVESVQSLLRNKVKAPALHRGGLQKVNRSFLNNH

Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)

2.7.12.2

ATP-binding;Kinase;Nucleotide-binding;Reference proteome;Transferase

actin filament organization [GO:0007015]; cellular hyperosmotic response [GO:0071474]; cellular response to osmotic stress [GO:0071470]; filamentous growth [GO:0030447]; fungal-type cell wall organization [GO:0031505]; MAPK cascade [GO:0000165]; osmosensory signaling pathway [GO:0007231]; p38MAPK cascade [GO:0038066]; phosphorylation [GO:0016310]; positive regulation of G2/M transition of mitotic cell cycle [GO:0010971]; protein import into nucleus [GO:0006606]; stress-activated protein kinase signaling cascade [GO:0031098]

cellular bud neck [GO:0005935]; cellular bud tip [GO:0005934]; Mcs4 RR-MAPKKK complex [GO:1990315]; NatB complex [GO:0031416]; nucleus [GO:0005634]

ATP binding [GO:0005524]; MAP kinase kinase activity [GO:0004708]; MAP-kinase scaffold activity [GO:0005078]; peptide alpha-N-acetyltransferase activity [GO:0004596]

IPR011009;IPR000719;IPR017441;IPR008271;

1.10.510.10;

A0A1D8PKY7

MIFPILPVISSPEDKQSIDEFSLVGQVLFPIESVSPKKHFIHQFPHDLDIFVNAIDNATTDQIVELLNVGIKQVFVNEKQYHDAIEAGSPSSRFVVAVDVPSTELLTSEASFVTSKPFSESDLKKYNANENRVIYIESNFTQDGAIELAKNYVPVIPSTKLTVKREEENKISISAVFVSTLTTDRPDGLYTTLITTPSPSYTALGIVYSSKDSIIAAIEEKVGVYQSRKRRDELWYKGKTSGATQKLVKLSKDCDSHVIQFMVEPRTGYGFCHRETKFTCFGDDIADSPARGLPKLDSTLQDRLENAPEVSYTKRLFDDEKLLIAKLKEELDELIEAKSKEEIAWECADLVYFAMVWCIKHGVRLADIEKNLDVKSLKVSRRKGDAKPQYQEAPVNSSYKLEIVSVDDAAAVERAMTRPVQKTADIMKLVLPIIEKVKSDGDKALIELTSKFDGVKLDAPVLQAPFPADLMDISEEMKAAIDLSMQNIEKFHAAQLPKEKVMTVETSPGVYCSRFAKPIENVGLYVPGGTAVLPSTAMMLGVPAKVAGCKNIIVASPPSRATGKLTPEVVYVAHKLGAKCIVMAGGAQAVTAMAYGTESVLKCDKILGPGNQFVTAAKMYVQNDTQALCSIDMPAGPSEVLVIADSNADADFVASDLLSQAEHGVDSQVILIGVGLSDEKLNEFQAAVERQAKVLPRKDIVAKCLAHSYILLAKTYKEAFDLSNQYAPEHLILQIDDAPSYVPDSIENAGSVFVGALSPESCGDYSSGTNHTLPTYGYARQYSGVNTATFQKFITSQEVTEKGLQNIGKAVMELARVEGLEAHRRAVEIRMERMAETK

Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)

1.1.1.23; 3.5.4.19; 3.6.1.31

CATALYTIC ACTIVITY: Reaction=1-(5-phospho-beta-D-ribosyl)-5'-AMP + H2O = 1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide; Xref=Rhea:RHEA:20049, ChEBI:CHEBI:15377, ChEBI:CHEBI:58435, ChEBI:CHEBI:59457; EC=3.5.4.19; Evidence={ECO:0000256|ARBA:ARBA00000024, ECO:0000256|PIRNR:PIRNR001257}; CATALYTIC ACTIVITY: Reaction=1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-ribosyl)-5'-AMP + diphosphate + H(+); Xref=Rhea:RHEA:22828, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:59457, ChEBI:CHEBI:73183; EC=3.6.1.31; Evidence={ECO:0000256|ARBA:ARBA00001460, ECO:0000256|PIRNR:PIRNR001257}; CATALYTIC ACTIVITY: Reaction=H2O + L-histidinol + 2 NAD(+) = 3 H(+) + L-histidine + 2 NADH; Xref=Rhea:RHEA:20641, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57595, ChEBI:CHEBI:57699, ChEBI:CHEBI:57945; EC=1.1.1.23; Evidence={ECO:0000256|ARBA:ARBA00001654, ECO:0000256|PIRNR:PIRNR001257};

COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|ARBA:ARBA00001947};

PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9. {ECO:0000256|ARBA:ARBA00005204}.; PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9. {ECO:0000256|ARBA:ARBA00005169}.; PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. {ECO:0000256|ARBA:ARBA00004940}.

Amino-acid biosynthesis;ATP-binding;Coiled coil;Histidine biosynthesis;Hydrolase;Metal-binding;Multifunctional enzyme;NAD;Nucleotide-binding;Oxidoreductase;Reference proteome;Zinc

adhesion of symbiont to host [GO:0044406]; cell adhesion [GO:0007155]; histidine biosynthetic process [GO:0000105]

cytoplasm [GO:0005737]; cytosol [GO:0005829]

ATP binding [GO:0005524]; histidinol dehydrogenase activity [GO:0004399]; metal ion binding [GO:0046872]; NAD binding [GO:0051287]; phosphoribosyl-AMP cyclohydrolase activity [GO:0004635]; phosphoribosyl-ATP diphosphatase activity [GO:0004636]

IPR016161;IPR008179;IPR016298;IPR001692;IPR012131;IPR021130;IPR002496;IPR038019;

1.20.5.1300;1.10.287.1080;3.40.50.1980;3.10.20.810;

A0A1D8PMF6

MSSPTYSPSRTISSPLLSLSSWRQFQLFDYTPIRDPNYHSSHALYSDPTLSCITATTTSYLIIAINHCTIKLINLSDLTCQLTFDAYNIDYRITFIEPIHNSNNLFVTLAEKQGMPSIIKLWDISKLLNLANNENNDSSKNSKLDQSEYRFEFQTQVLVNDHSSGTTGIGDNSYPISCFKFNYDLTCLAIGYTNGKVILVRGDLLRDRGAKQRLIYNSGNNDPITGVQFNETEQVLYVTTTEKLLTVATTGRNHEKPLKILSNKYGANLNCTDIDESNQNLIVGLNDSIQFYDCFTKISTINFKLAKSRIIKCKQYLLIVSPEERNKAGVSETDHGIDKSLMSRIVILDLVNNHISFNLLISDSSISHAFSLSNGTFLLLTTDGVLYKINEKSINQQIEIVLQRELFSVAFNLGQQYKLPNETLLRIQILHGDYLYDQNKFDEAIDVYIKCLELFKKSGKIVEQKQRNNRQDNQTEVEEEEDIDEFIINIITKFKEATNISNLTKFLIRLYEKSLANIDHITLLLCCYCKLKKIDNLNEFIDELDLSIENLQELNYELIINLFKECGFYDQVLKLLYKLNQPNLIVDIQLNDLHKPKLALNYMKTLTIDDLLLILIDHSTNLLDSCPLETTELLINVFTGKYQPNKPNAKYVFDVSNNGNTSTMNQPQKNPEKESSEREKSVDISNYRAFLNYLSLQSEETDNSDNYTESKTSQENPTLLSNKEPTYLPPKPNLIYASFTNHPKEFVIFLEASLEAFNKYDGNIVDKRETLLTLLEIYLSLNKSTGDKEWLDKAETLTRDYNQLLDNQALLLLSHIYNFKPGEVIAQEKSGNEIDLFMSCQLNQDVEGCFEILEKYGDTKPQLYELMLKFIISSKTIFDQIKYEDIQVILEQIKIYKLLTPIELVDILTENPDNEFITLGLVKDYFIDYFQQQTKEISNNTKLIEKYEQESTKNSFKLSELSKPFVIQNNKCSGCNLKLDFPVIHFKCKHSFHQKCLSTNLIATSTESSTSSTPTSMSTSMLNPNNNAVINHNDDDKFTCPICIHKFNDIKNAKLNQYKLGDAANQNKENFDVFINSLHSSNDKFKFVSDYIGKGVMEDQ

Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)

2.3.2.27

CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000256|PIRNR:PIRNR007860};

Membrane;Metal-binding;Protein transport;Reference proteome;Transferase;Transport;Ubl conjugation pathway;Vacuole;Zinc;Zinc-finger

cell growth mode switching, budding to filamentous [GO:0036187]; chlamydospore formation [GO:0001410]; development of symbiont in host [GO:0044114]; endosome organization [GO:0007032]; evasion of host immune response [GO:0042783]; filamentous growth [GO:0030447]; filamentous growth of a population of unicellular organisms [GO:0044182]; filamentous growth of a population of unicellular organisms in response to biotic stimulus [GO:0036180]; intracellular protein transport [GO:0006886]; organelle fusion [GO:0048284]; positive regulation of filamentous growth of a population of unicellular organisms in response to neutral pH [GO:1900442]; protein secretion [GO:0009306]; vacuolar transport [GO:0007034]; vacuole organization [GO:0007033]; vesicle docking involved in exocytosis [GO:0006904]

CORVET complex [GO:0033263]; endosome [GO:0005768]; fungal-type vacuole membrane [GO:0000329]; HOPS complex [GO:0030897]

metal ion binding [GO:0046872]; protein-macromolecule adaptor activity [GO:0030674]; transferase activity [GO:0016740]

SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000256|PIRNR:PIRNR007860}; Peripheral membrane protein {ECO:0000256|PIRNR:PIRNR007860}; Cytoplasmic side {ECO:0000256|PIRNR:PIRNR007860}.

IPR011990;IPR016528;IPR024763;IPR015943;IPR036322;IPR001841;IPR013083;

1.25.40.10;2.130.10.10;3.30.40.10;

A0A1D8PMM1

MSESESDYFTDGSEDDFVPTSKKSTKKNASSKSKQPLGDATNSTVSSSRSSTPKPTNASETYQKLSQLEHILKRPDTYIGSVEKTKTEMWCFDAETESMVFKEVTIVPGLYKIFDEILVNAADNKIRDPSMKNIRVKIDAENNIIEVMNDGKGIPIEMHTKENMYIPELIFGNLLTSSNYDDDQKKVTGGRNGFGAKLCNIFSTQFEVETADLNMGKLYKQSWTNNMSNVSKPKITTLRTKKEYTKITFRPDLSKFDMDCLDNDLLSVLRRRVYDLCGTVKNCNIYLNDKRLNISSFKGYVEMYVKAIKERSPEPEPQDGTIKNFTTIVHEVFNDRWEVAFAVSDGSFNQVSFVNSIATTSGGTHVKYVSDQIINKLVETLSKKEKGKKKLMIKPQEVRDNMFLFINCLIENPAFTSQTKEQLTTKVSQFGGKDKFVANDNLINRILKTSIVDKIRAIANANEDKALQKADGSRKSRIKGQVNLVDANKAGTKDGHNCTLILTEGLSAMNLAVAGLSVVGRDYYGCFPLRGKLLNVREASADQISKNAEINSLKQIIGLQHKKVYTAENIKSLRYGHIMIMTDQDQDGSHIKGLIINFLETSFPGLLDIPGFLLEFITPIVKVTVKARGAGGKRVIPFYTMPEFEHWRDTEGKQCRWTQKYYKGLGTSTPMEAREYFTALDRHLKRFHALQGEDKDYIDLAFSKKKADERKEWLQGFLPGTHLDPEITEIPISDFINKELILFSMSDNVRSIPSVLDGFKPGQRKVLYGCFKKKLRSEIKVAQLAGYVSENTGYHHGEQSLVQTIIGLAQNFVGSNNINVLKPNGSFGSRAAGGKDFSAARYIFTELSEITRKIFNPLDDPLYTYVQDDEQTVEPEWYLPVLPMILVNGAEGIGTGWSTNIPSYNPKDLVTNIRRLMNGEELQEMTPWYKGWGGDLEPMGPQKFKVSGRIEQIDSNTVEITEIPVKTWTNNVKEFLLSGFGNEKTQPWIKDMEEHHTTSIRFVVKLTDAEMQKSLRIGLLERFKLVSSLSLANMVAFDPMGRIKKYNDVLEIIKDFYYVRLEYYQKRKDYMTDNLQNQLLMLSEQARFIKMIIEKQLSVANKKKKQLVALLEEHNFTKFSKDGKPIKSSEELLTGDDADEEEETQEQEGDEDVGNTSVANIQEGEPEQAAHVPETIYSSYDYLLGMAIWSLTYERFMRIMQQRDQKEAELNALLSKSAKDLWNQDLDEFLAEFDKFLLRDEQERESLASNGKKKSTKRRAKATATKDQPNNKKVKVEPKEKKSISAKPVVKKEASNEPQASSSSKPKEKDDILSFFSSSSSSAKKITKPSGRATSNKEIETITLFSDDDDDEDIFNLNSSSSTKVKKEAKSRSATPAAEKSKKSKSSGKQSILDELEDLEILGNFDKPEPKERRTRETASTTKRNTKKKPVIIDSDDEDEDEEDDIVMSDGDDDDDFIVDE

Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)

FUNCTION: Control of topological states of DNA by transient breakage and subsequent rejoining of DNA strands. Topoisomerase II makes double-strand breaks. {ECO:0000256|RuleBase:RU362094}.

5.6.2.2

CATALYTIC ACTIVITY: Reaction=ATP-dependent breakage, passage and rejoining of double-stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000256|ARBA:ARBA00000185, ECO:0000256|RuleBase:RU362094};

COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000256|ARBA:ARBA00001913}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|ARBA:ARBA00001946};

ATP-binding;DNA-binding;Isomerase;Magnesium;Metal-binding;Nucleotide-binding;Phosphoprotein;Reference proteome;Topoisomerase

cellular response to neutral pH [GO:0036244]; cellular response to starvation [GO:0009267]; chromatin remodeling at centromere [GO:0031055]; DNA strand elongation involved in DNA replication [GO:0006271]; DNA topological change [GO:0006265]; filamentous growth [GO:0030447]; filamentous growth of a population of unicellular organisms in response to neutral pH [GO:0036178]; filamentous growth of a population of unicellular organisms in response to starvation [GO:0036170]; regulation of mitotic recombination [GO:0000019]; replication fork progression beyond termination site [GO:0097046]; resolution of meiotic recombination intermediates [GO:0000712]; rRNA transcription [GO:0009303]; sister chromatid segregation [GO:0000819]

DNA replication termination region [GO:0097047]; nucleus [GO:0005634]; synaptonemal complex [GO:0000795]

ATP binding [GO:0005524]; DNA binding [GO:0003677]; DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity [GO:0003918]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]

IPR003594;IPR036890;IPR020568;IPR014721;IPR001241;IPR013760;IPR013758;IPR013757;IPR013759;IPR013506;IPR002205;IPR001154;IPR031660;IPR006171;IPR034157;

3.30.1360.40;3.30.1490.30;3.30.230.10;3.40.50.670;3.30.565.10;3.90.199.10;1.10.268.10;

A0A1D8PMU9

MDTDNFEDVKAYTVGPNFCHAETRKSPVVDGIVRRNTHGKEIRYVTELTDEEKTMAKNVSSAFKQTICGFDLLRVNGKSFVIDVNGFSFVKDNNEYYDSCASILRGLFIDAKKSRDLLTRKIPKMLQTSQFEQKAQKWVFKGMVTVIRHADRTPKQKFKYSFRSPVFISLLKGHREEVIIRAVPDLQVVLETVKIAEAKGLEDLNKLKQLRIALEKKMDFPGTKIQLKPTLNAENPEVVDKVQLILKWGGEPTHSAKHQATDVGEQMRQNLQLLNREALDDVKVYTSSERRVIASAQYFSASLLSIDEPLADDFLIVRKDLLDDSNAAKDLMDKVKKKLKPLLREGAEAPPQFTWPPKMPQPFEVIKRVCELMNFYHQIMNYNFETKNVQEFQINWCCGEDPFLFKERWDKLFQEFISVEKTHPSKISELYDTMKYDALHNRHFLQKIFSYDPNDKVLLSRLTETCGSTVNSSGLVSEYPINILAMNNFKLPESASTSANNSSSNLNSNSAAGSLGWVLSGAATTMKCESKDTSASPQTPFDHPTFARLRELYRLSKVLFDFICPQEYGIKDEEKLDIGLLTSLPLAKQILSDIYDMKKNDRPALVNYFTKESHIYTLLNIIYGSQLPMKIARNALPELDYLSQIVFELYEAEDPSSPTGKKHSIRLSLSPGCHTQDPLDVQLDDDHYIGCIPRISLTRHLDMDLVTQRLKSRFSRVSLPKKFTPVNITGPLNSK

Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)

FUNCTION: Bifunctional inositol kinase that acts in concert with the IP6K kinases to synthesize the diphosphate group-containing inositol pyrophosphates diphosphoinositol pentakisphosphate, PP-InsP5, and bis-diphosphoinositol tetrakisphosphate, (PP)2-InsP4. PP-InsP5 and (PP)2-InsP4, also respectively called InsP7 and InsP8, may regulate a variety of cellular processes, including apoptosis, vesicle trafficking, cytoskeletal dynamics, and exocytosis. Phosphorylates inositol hexakisphosphate (InsP6). {ECO:0000256|RuleBase:RU365032}.

2.7.4.24

CATALYTIC ACTIVITY: Reaction=1D-myo-inositol hexakisphosphate + ATP = 1-diphospho-1D-myo-inositol 2,3,4,5,6-pentakisphosphate + ADP; Xref=Rhea:RHEA:37459, ChEBI:CHEBI:30616, ChEBI:CHEBI:58130, ChEBI:CHEBI:74946, ChEBI:CHEBI:456216; EC=2.7.4.24; Evidence={ECO:0000256|RuleBase:RU365032}; CATALYTIC ACTIVITY: Reaction=5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate + ATP + H(+) = 1,5-bis(diphospho)-1D-myo-inositol 2,3,4,6-tetrakisphosphate + ADP; Xref=Rhea:RHEA:10276, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58628, ChEBI:CHEBI:77983, ChEBI:CHEBI:456216; EC=2.7.4.24; Evidence={ECO:0000256|RuleBase:RU365032};

ATP-binding;Cytoplasm;Kinase;Nucleotide-binding;Reference proteome;Transferase

autophagy [GO:0006914]; inositol metabolic process [GO:0006020]; inositol phosphate biosynthetic process [GO:0032958]; inositol phosphate catabolic process [GO:0071545]; intracellular phosphate ion homeostasis [GO:0030643]; mitotic spindle assembly [GO:0090307]; phosphorylation [GO:0016310]; positive regulation of autophagy [GO:0010508]; regulation of bipolar cell growth [GO:0051516]; regulation of mitotic spindle elongation (spindle phase three) [GO:0110162]

cytoskeleton [GO:0005856]; cytosol [GO:0005829]

2 iron, 2 sulfur cluster binding [GO:0051537]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; diphosphoinositol-pentakisphosphate kinase activity [GO:0033857]; inositol heptakisphosphate kinase activity [GO:0000829]; inositol hexakisphosphate 1-kinase activity [GO:0052723]; inositol hexakisphosphate 3-kinase activity [GO:0052724]; inositol hexakisphosphate 5-kinase activity [GO:0000832]; inositol hexakisphosphate kinase activity [GO:0000828]; inositol-1,3,4,5,6-pentakisphosphate kinase activity [GO:0000827]; inositol-1,5-bisdiphosphate-2,3,4,6-tetrakisphosphate 1-diphosphatase activity [GO:0052846]; inositol-1-diphosphate-2,3,4,5,6-pentakisphosphate diphosphatase activity [GO:0052843]; kinase activity [GO:0016301]; phosphatase activity [GO:0016791]

SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000256|RuleBase:RU365032}.

IPR013651;IPR000560;IPR037446;IPR029033;

3.30.470.20;3.40.50.1240;

A0A1D8PN61

MSEQAQTQVSADQQQHQHNHHHHHHHHHHNENQSQQQVPIDPAANPANRIGRYQILKTLGEGSFGKVKLAQHLGTGQKVALKIINRKTLAKSDMQGRVEREISYLRLLRHPHIIKLYDVIKSKDEIIMVIEFAGKELFDYIVQRGKMPEDEARRFFQQIIAAVEYCHRHKIVHRDLKPENLLLDDQLNVKIADFGLSNIMTDGNFLKTSCGSPNYAAPEVISGKLYAGPEVDVWSAGVILYVMLCGRLPFDDEFIPALFKKISNGVYTLPNYLSAGAKHLLTRMLVVNPLNRITIHEIMEDEWFKQDMPDYLLPPDLSKNKNSKIDVDEDVIRALSVTMGYDRDEIVNVIEKANKQVAAGNSSSQQSKSSNEILDAYLLMKENHALVKDLKKSKSENIESFLSQSPPPSPFPNAGSTSSAPGVQQSLTYQTLATVPDLSTLPNSTIAILPTSLPSIHRAYMAETKQNGDPSQQHAPPPTKKSKTRWHFGIRSRSYPLDVMGEIYRALKNLGAEWAKPTEEELWTIRVRWKYDTSAQFECGSAPNLMKMQIQLFQLEPNNYLVDFKFDGWESAHGNAGTDSPQSHRQQDLDEVGSFSAYPFLHLATRLIMELAVNSQSG

Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)

CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00001433};

ATP-binding;Kinase;Nucleotide-binding;Reference proteome;Transferase

CAMKK-AMPK signaling cascade [GO:0061762]; establishment of mitotic spindle orientation [GO:0000132]; filamentous growth [GO:0030447]; filamentous growth of a population of unicellular organisms [GO:0044182]; fungal-type cell wall assembly [GO:0071940]; intracellular signal transduction [GO:0035556]; invasive growth in response to glucose limitation [GO:0001403]; negative regulation of filamentous growth of a population of unicellular organisms [GO:1900429]; negative regulation of TORC1 signaling [GO:1904262]; negative regulation of translation [GO:0017148]; phosphorylation [GO:0016310]; positive regulation of ascus development [GO:0075319]; positive regulation of filamentous growth of a population of unicellular organisms in response to starvation [GO:1900436]; positive regulation of gluconeogenesis [GO:0045722]; positive regulation of macroautophagy [GO:0016239]; positive regulation of pseudohyphal growth [GO:2000222]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of carbohydrate metabolic process [GO:0006109]; regulation of invasive growth in response to glucose limitation [GO:2000217]; response to endoplasmic reticulum stress [GO:0034976]; response to unfolded protein [GO:0006986]; single-species surface biofilm formation [GO:0090606]; SREBP signaling pathway [GO:0032933]

cellular bud neck septin ring [GO:0000144]; cytoplasm [GO:0005737]; nuclear envelope lumen [GO:0005641]; nucleotide-activated protein kinase complex [GO:0031588]; vacuolar membrane [GO:0005774]

AMP-activated protein kinase activity [GO:0004679]; ATP binding [GO:0005524]; guanyl-nucleotide exchange factor activity [GO:0005085]; identical protein binding [GO:0042802]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]

IPR032270;IPR028375;IPR011009;IPR000719;IPR017441;IPR008271;IPR013896;

3.30.310.80;1.10.510.10;

A0A1D8PP43

MSEQIPKTQKAVVFDTNGGQLVYKDYPVPTPKPNELLIHVKYSGVCHTDLHAWKGDWPLATKLPLVGGHEGAGVVVGMGENVKGWKIGDFAGIKWLNGSCMSCEFCQQGAEPNCGEADLSGYTHDGSFEQYATADAVQAAKIPAGTDLANVAPILCAGVTVYKALKTADLAAGQWVAISGAGGGLGSLAVQYARAMGLRVVAIDGGDEKGEFVKSLGAEAYVDFTKDKDIVEAVKKATDGGPHGAINVSVSEKAIDQSVEYVRPLGKVVLVGLPAHAKVTAPVFDAVVKSIEIKGSYVGNRKDTAEAIDFFSRGLIKCPIKIVGLSDLPEVFKLMEEGKILGRYVLDTSK

Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)

1.1.1.1

COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|ARBA:ARBA00001947, ECO:0000256|RuleBase:RU361277};

Metal-binding;Oxidoreductase;Reference proteome;Zinc

biological process involved in interaction with host [GO:0051701]; induction by symbiont of host defense response [GO:0044416]; single-species biofilm formation in or on host organism [GO:0044407]; single-species biofilm formation on inanimate substrate [GO:0044011]

cell surface [GO:0009986]; cytoplasm [GO:0005737]; extracellular region [GO:0005576]; fungal biofilm matrix [GO:0062040]; fungal-type cell wall [GO:0009277]; hyphal cell wall [GO:0030446]; plasma membrane [GO:0005886]; yeast-form cell wall [GO:0030445]

alcohol dehydrogenase (NAD+) activity [GO:0004022]; methylglyoxal reductase (NADH-dependent) activity [GO:0019170]; zinc ion binding [GO:0008270]

IPR013149;IPR013154;IPR002328;IPR011032;IPR036291;IPR020843;

3.90.180.10;3.40.50.720;

A0A1D8PPK1

MTIESTNSFVVPSDTELIDVTPLGSTKLFQPIKVGNNVLPQRIAYVPTTRFRASKDHIPSDLQLNYYNARSQYPGTLIITEATFASERGGIDLHVPGIYNDAQAKSWKKINEAIHGNGSFSSVQLWYLGRVANAKDLKDSGLPLIAPSAVYWDENSEKLAKEAGNELRALTEEEIDHIVEVEYPNAAKHALEAGFDYVEIHGAHGYLLDQFLNLASNKRTDKYGCGSIENRARLLLRVVDKLIEVVGANRLALRLSPWASFQGMEIEGEEIHSYILQQLQQRADNGQQLAYISLVEPRVTGIYDVSLKDQQGRSNEFAYKIWKGNFIRAGNYTYDAPEFKTLINDLKNDRTIIGFSRFFTSNPDLVEKLKLGKPLNYYNREEFYKYYNYGYNSYDESEKQVIGKPLA

Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)

FUNCTION: Oxidoreductase that binds mammalian estrogens with high affinity. {ECO:0000250|UniProtKB:P43084}.

1.6.99.1

CATALYTIC ACTIVITY: Reaction=A + H(+) + NADPH = AH2 + NADP(+); Xref=Rhea:RHEA:13149, ChEBI:CHEBI:13193, ChEBI:CHEBI:15378, ChEBI:CHEBI:17499, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.6.99.1; Evidence={ECO:0000250|UniProtKB:P43084};

COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250|UniProtKB:Q02899};

Flavoprotein;FMN;NADP;Oxidoreductase;Reference proteome

steroid metabolic process [GO:0008202]

cell surface [GO:0009986]; cytosol [GO:0005829]; fungal-type vacuole [GO:0000324]; hyphal cell wall [GO:0030446]

estrogen binding [GO:0099130]; FMN binding [GO:0010181]; hormone binding [GO:0042562]; NADPH dehydrogenase activity [GO:0003959]; steroid binding [GO:0005496]

IPR013785;IPR001155;IPR045247;

3.20.20.70;

A0A1D8PQK6

MSANPYDIEHKLPPQRANTPSLKYSQKSIEETAADLQTDIKLGLTNSQDVLNRRSIHGINELNGDEEESLLWKFISSFYQDPLILLLIGSAVISFWMGNKDDAISITLAITIVVTVGFVQEYRSEKSLEALNKLVPAEAKLTRTGSTSSVLAQVLVPGDLVHFSQGDRIPADIRLTEAVHLTIDESNLTGENRPVKKTVDTVNSSDPAVTERTDIAFMGTLVRDGHGSGIVVATAGQTVFGSVFEMMSDIEKPKTPLQQAMDKLGKDLSIFSFIVIGIICLIGIFQGRSWLDMFQISVSLAVAAIPEGLPIIVTVTLALGVLRMARQKAIVRRLPSVETLGSVNVICSDKTGTLTQNHMTVTKIWTADFKGSFNTPFLAVERLDDNTLHHQLTSNMHKVLECGNICNNARYSTESEKYVGNPSDIALVECLPHFGLEDMRGQKQRLYELPFSSNRKYMAVCVHTGDIEKSETIAKGATEKILQLCDRYYDENGSVKPLTEAIEESIHEKSRSLARDGLRVLAFAKNNKKFDEKTTEPTDLVFCGLIGMKDPPRPKVGQSIARLMQGGVHVIMITGDSPTTAVNIARQIGIPVVGDHAVLTGDQIDSLSEEALTKAIHDVSVFARTTPEHKVTIVKALQRRGDIVAMTGDGVNDAPALKLADIGIAMGKNGTDVAKEAADMVLTDDDFSTILSAIEEGKGIFNNIQNFITFQLSTSIAALTLVALSTFFGLPNPLNAMQILWINILMDGPPAQSLGVEPVDHEVMNKPPRKRNDVILTQQVIKRVLQSAAIIIVGTMYVFIKEMTDGVITARDTTMTFTCFVLFDMFNALSCRHYSKSIFELGMTNQMFNFAVLGSLIGQFCAVYVPFFQSIFQTEALNFGDILRLVILTSTVFAVDEIRKWLRRRKTVYTNNYSYGV

Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)

FUNCTION: Catalyzes the hydrolysis of ATP coupled with the transport of calcium. {ECO:0000256|RuleBase:RU361146}.

7.2.2.10

CATALYTIC ACTIVITY: Reaction=ATP + Ca(2+)(in) + H2O = ADP + Ca(2+)(out) + H(+) + phosphate; Xref=Rhea:RHEA:18105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29108, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.10; Evidence={ECO:0000256|RuleBase:RU361146};

ATP-binding;Calcium;Calcium transport;Ion transport;Membrane;Nucleotide-binding;Reference proteome;Translocase;Transmembrane;Transmembrane helix;Transport

calcium ion transmembrane transport [GO:0070588]; cellular response to mechanical stimulus [GO:0071260]; filamentous growth [GO:0030447]; filamentous growth of a population of unicellular organisms [GO:0044182]; fungal-type cell wall organization [GO:0031505]; Golgi calcium ion homeostasis [GO:0032468]; hyphal growth [GO:0030448]; intracellular calcium ion homeostasis [GO:0006874]; manganese ion transmembrane transport [GO:0071421]; manganese ion transport [GO:0006828]; protein glycosylation [GO:0006486]

endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; nuclear envelope [GO:0005635]; plasma membrane [GO:0005886]

ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; P-type calcium transporter activity [GO:0005388]; P-type ion transporter activity [GO:0015662]

SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361146}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361146}.

IPR006068;IPR004014;IPR023299;IPR018303;IPR023298;IPR008250;IPR036412;IPR023214;IPR006413;IPR001757;IPR044492;

3.40.1110.10;2.70.150.10;1.20.1110.10;3.40.50.1000;

A0A1D8PQT9

MPETSITSDLEHRQQDEISSISSIYGDIFKDITPTGLVWNKKPSPHFQVFLSSSNNPDRPTVSITLDIEFTPTYPLSPPKVKLLNARNLLKINIAKLEKKCKDLIKEYPEQEVSFTIISELIFMLDEIQTTTEKVLSLEEERELRLRNERRALEEKEAKQKKDEELARKKQNKELNEQIQKIQGEFDDDFTDDQDLDMSTTNDNNNSLIPLDKDQFFIFENAMEATIPNTRRKFKFRAISGFIRYNQKGVFNSIGSQYIVKPFIDNEIRNKIENKGSDLAFLLTVIDLTNEYWQTDKGKREIQDLESELQSIMSINHSNILKLIGFQIDKTNVWRVRLLTEFSPVSETLYDILPTAEFINWALARTWLIQLLPAMEYLHNAGFIHKLICPMTIVIFQEKDQLYYQNSTNELLSNSIGGGGGGGEDSLTISAKKVLKLCHPSYGYRLLEMISLHPNEGETLDRSPQVNPPAWLAPELKTSGYHYKSDIWDLGVLFLRVMLGFDILNTTYHTPSDFINKFSVKDFVGAEEYASLVYDVLSKMLQVKLSKRPSPLELNAVKFLRDGPIISKLQSETNLSRMKKNVETDLVSSTNTRHVQIQGHEQDSTATTKHLNIYHQNISRRRLSNQNTQHPYFGENSSLIMPSGSQRNMGRYARDFEEIGKLGRGGFGEVVKARSRMEGIFYAVKKIKHRADKLDSLLSEVLSLARLNHQYIVRYYGTWVEELEDTSAIPSNSTSAIASDDEEEEEEEDDTEGDFGDDDLESTFSSRVGRSSSVLPSYDNSFQVDYISTSFDPRIEFDESSEEDDQNEDDDPFVFANSTDDISNNETEDRSKSDSKEVSVKKPKDVVNSSKNASPKSILYIQMEFCENNTLLNLIEQGLPNNPDEYWRLFRQLLEAVSYIHREGFIHRDLKPMNIFIDRSNNIKVGDFGLAKNSQFSSVVSTNNQVEAKDNELSTVVGTLFYTANEVATGQYDEKVDMYSLGIIFFEMCYPLATGMQRAKTLNDLRLKSVEFPTNFIASKYKTEKKIIRLLLDHDPKIRPSAAQLLQSGWLPVEHQDQVIQEALKSLADPASPWQQQVREALFNQPYSLAKDLMFDKQNEHNSHNKHVELDTSNDYLLFDKIMKELTKIFTNHGAIENLNTNLVLPKAPSQSRELVYDFLDRSGAVLTLPYDLTLPTARFLSKTDMTIPKTFRHEFVYRPNVRGIGIPDRYSAVNFDIAGGSEVNKATLFAHDAECLKVIDEIVNTLPCFKNTIIVINHYDILDAVVSFSFGNIGIDDKKKLDIFGVLSQLGIDKSPDEIKRYLREDFQVPHTVTKDLVENFNFTCEVERARQKLQKLMVDSPQLLKVERAYTYLIEVVKILKQMNIKTSMIFNPLSNYNSKYYIHGIMFQAVFKPDRSKRYTRVVTGGRYDSLIESFSNVTTTTKQITPHGVGFSLTTSLLFILMKTLISRGKSKLDLVNKWKGNRCKVLISSTQQQFLSQVGYQLVSKFWNKNISADITSVAAKTQDEIFQNGNSEGAIWIVIIRSLPTTIGNSFSSLNGGSGGSSSSTTTTSTSIRRSKKSGSGFKPLKLRNIITGKDIDLDYDEVIDYLVTELLEDSEHEENDQDNGTMTNSTTLLTSSSLSSKTNQEEELLNGPIDSVEIDQKIIVVKNDAPRSRKNKRDKWESENDAKLAGQQCIKNLSGGPVVVIDARDEILDMISITSIHQQDEWIRKVVYTTNNFPKSFAMNIYNTLIKEFNKGSIWCILVSSRTQHTTIVDLRR

Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)

2.7.11.1

CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00001433}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};

ATP-binding;Coiled coil;Kinase;Nucleotide-binding;Reference proteome;Serine/threonine-protein kinase;Transferase

amino acid biosynthetic process [GO:0008652]; cellular response to amino acid starvation [GO:0034198]; cellular response to histidine [GO:0071232]; cellular response to N-acetyl-D-glucosamine [GO:0097316]; DNA damage checkpoint signaling [GO:0000077]; filamentous growth [GO:0030447]; filamentous growth of a population of unicellular organisms in response to chemical stimulus [GO:0036171]; GCN2-mediated signaling [GO:0140469]; negative regulation of cytoplasmic translational initiation in response to stress [GO:1990625]; positive regulation of cellular response to amino acid starvation [GO:1903833]; positive regulation of filamentous growth of a population of unicellular organisms in response to chemical stimulus [GO:1900439]; positive regulation of translational initiation in response to starvation [GO:0071264]

cytoplasm [GO:0005737]; cytosolic ribosome [GO:0022626]; large ribosomal subunit [GO:0015934]; nucleus [GO:0005634]; small ribosomal subunit [GO:0015935]

ATP binding [GO:0005524]; double-stranded RNA binding [GO:0003725]; eukaryotic translation initiation factor 2alpha kinase activity [GO:0004694]; protein homodimerization activity [GO:0042803]; protein kinase inhibitor activity [GO:0004860]; protein self-association [GO:0043621]; ribosomal large subunit binding [GO:0043023]; translation initiation factor binding [GO:0031369]; tRNA binding [GO:0000049]

IPR045864;IPR016255;IPR041715;IPR024435;IPR011009;IPR000719;IPR017441;IPR006575;IPR008271;IPR016135;

1.10.510.10;3.10.110.10;

A0A1D8PR83

MSFLRRDKSKANFRDGSATGLEEPVSPTTHFSPNAPPPLDGNHGDHYHDPDSPRSSVVSLPQLIHNSATHHLKENYRGFHANKRPKGIANVPPLAQPIKPRFKKKSNSLLNKLIYSTKKEDDETATSGKESRSSSIISDEKRKSASSASSGSSRQKFRFSSFDSNLSTSSSSPPKDKKASISDTVSDSSTVTASMSNMPTISIDLNLDEMHDIIKSPETPAPTVGLPTQKAEKKASPTAIKNWQAPESWDVKAPIKKEEPHAPKIEEVAENDVAIDNVLEKKRLPVLYGTHQVPHVTNSKDIKSSHIIRVFKEDNTFTTILCPLETTTSELLAIVQKKFFLESTTNFQLSVCIGNCVKVLEDFEKPLKIQMGLLLLSGYTEEDKLRMLGREDLSFVCKFVVENIFLRSLTHDEEVLLSRNYVDVNISSLNLKNVPIIFHQHTYEIEKLNVANNPSIYLPLDFIQGCTSLAYVDFSHNGCSKFPNNLLEAPQLTHLNLEMNFLDEIPQRISCLSNLTNLKLSSNQLYSLPHSFSTLTNLKQLDLSSNYFDSYPEAVNKLTNLVELNFSYNDLSIIPESIANLINLQKLNLCTNKLSGTLPGYLSQLKALKRLDIRYNYISNVDVLGIIPNLEVAYASKNAISTFSDQMKCLRLLHFDRNPITELKFNTQMQMLSVLDLSRAKITAFPAEFVEKVPNIEKLVLDKNHLVSLPNELCQLSKLVSLSVHANNLQSLPANIGDLRFLKYLDLHSNNLKSLPDQIWDLCHLTSLNVASNNLTSFPKAPYSVVKRLSSSLVDVHLESSQTLSLADSLLILILSDNRLSDDCFDEISFLIALKSLNVSYNDLIEIPQGTLSRLTRLNELYLSGNELTTLPADDLEVLKSLKLLYMNNNKLVSLPAELSRIANLQHLDVSSNQLKYNISNWPYDWSWHWNKNLKYLNFSGNKRFEIKQSHIKNPETGEDFDSLLVLKQLRVLGLIDVTLTTTNVPEQAVDLRLRTTASEFDNFGYGVSDSLGMRDHVSARDLFVQKFRGKENEMLLCAFDGKHGATNQGHRISLVAKNMFVRNFTKELDEIKNDDEIENALRKAFLNFNKEINGILTAKKNKSFTPVPNMSKEALELNLVDDGNAGCTVSVIYIKDKKLYSANIGDIEALLCRNNGDQFLLTEKHDPTNREEFERIRASGGYVSGGGELDGQLSVSRGVGFFNFLPHTHCGPTIRRFKITNDDDMIILGSKQLWDFISYESAVDIIRKDKNDPMVAAQKLRDFAICYGATDKICVIVLTFGNRQKQAANMYSNYGVDRRRRDKQQVVGGDSNLRKLEQEIEPPIGPLALVFTDIKNSTLLWDSYPAPMRSAIKIHNTIMRRQLRITGGYEVKTEGDAFMVAFPSPTAALLWCFQVQQNLVTADWPSEILETDQCCVVSDSENNTIFRGLSVRMGIHWGSPVCEPDVITGRMDYFGPMVNRASRISAIADGGQIAVSSDFLDVLNSLTVKHNNIKNNVESLIDAYQGNENAGMTIERELNALEDLGCNYFKIGERKLKGLETPEPITLVFTNRLKLRYDIFQKRLDANHSTRVAGTLPVEIIYGLRTVSLRLENLCSSINNGGNYCSEGFESSSGVISQKMNSSFKDSDLISLLNHVTTRIESCTTTLFLRQQLSQIKGNGGLIETNNSPSLDVIMDEIADIMKTVNELK

Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)

FUNCTION: Plays essential roles in regulation of cellular metabolism by catalyzing the synthesis of a second messenger, cAMP. {ECO:0000256|ARBA:ARBA00003896}.

4.6.1.1

ATP-binding;cAMP biosynthesis;Leucine-rich repeat;Lyase;Nucleotide-binding;Reference proteome;Repeat

adenylate cyclase-modulating G protein-coupled receptor signaling pathway [GO:0007188]; cAMP biosynthetic process [GO:0006171]; cell adhesion involved in single-species biofilm formation [GO:0043709]; cell-abiotic substrate adhesion [GO:0036164]; cellular response to carbon dioxide [GO:0071244]; cellular response to starvation [GO:0009267]; evasion of host immune response [GO:0042783]; filamentous growth [GO:0030447]; filamentous growth of a population of unicellular organisms [GO:0044182]; filamentous growth of a population of unicellular organisms in response to biotic stimulus [GO:0036180]; filamentous growth of a population of unicellular organisms in response to chemical stimulus [GO:0036171]; filamentous growth of a population of unicellular organisms in response to starvation [GO:0036170]; growth of unicellular organism as a thread of attached cells [GO:0070783]; phenotypic switching [GO:0036166]; positive regulation of apoptotic process [GO:0043065]; positive regulation of filamentous growth of a population of unicellular organisms [GO:1900430]; positive regulation of filamentous growth of a population of unicellular organisms in response to biotic stimulus [GO:1900445]; positive regulation of filamentous growth of a population of unicellular organisms in response to chemical stimulus [GO:1900439]; positive regulation of filamentous growth of a population of unicellular organisms in response to pH [GO:1900743]; positive regulation of filamentous growth of a population of unicellular organisms in response to starvation [GO:1900436]; positive regulation of growth of unicellular organism as a thread of attached cells [GO:0070786]; positive regulation of phenotypic switching [GO:1900241]; positive regulation of Ras protein signal transduction [GO:0046579]; quorum sensing [GO:0009372]; Ras protein signal transduction [GO:0007265]; regulation of phenotypic switching [GO:1900239]; regulation of single-species biofilm formation on inanimate substrate [GO:1900231]; signal transduction involved in filamentous growth [GO:0001402]; single-species biofilm formation on inanimate substrate [GO:0044011]

cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886]

adenylate cyclase activity [GO:0004016]; ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]

IPR001054;IPR013716;IPR048580;IPR001611;IPR003591;IPR032675;IPR029787;IPR036457;IPR001932;IPR000159;

3.30.70.1230;3.60.40.10;3.80.10.10;

A0A1D8PS50

MRDYKVVVLGAGGVGKSSITVQFVQGVYVESYDPTIEDSYRKQIEVDGRACDLEILDTAGVAQFTAMRELYIKSGKGFLLVYSVTDENSLKELLALREQVLRIKDSDNVPMVLVGNKCDLEDDRVLSIEDGVKVSQDWGLVPFYETSAMYKTNVDEAFIDVVRQIMRKEAAISAEKKQQKELQKQQQQQQQEQDAEGQQQQQKSGKSKSSATQKDATADGQTDVNARLKQSINDHPKSSSGSKCCTIM

Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)

3.6.5.2

CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2; Evidence={ECO:0000256|ARBA:ARBA00023421};

Lipoprotein;Prenylation;Reference proteome

actin cortical patch localization [GO:0051666]; axial cellular bud site selection [GO:0007120]; bipolar cellular bud site selection [GO:0007121]; cellular bud site selection [GO:0000282]; cellular response to cAMP [GO:0071320]; cellular response to electrical stimulus [GO:0071257]; cellular response to starvation [GO:0009267]; cytogamy [GO:0000755]; establishment of protein localization [GO:0045184]; establishment or maintenance of cell polarity [GO:0007163]; filamentous growth [GO:0030447]; filamentous growth of a population of unicellular organisms [GO:0044182]; filamentous growth of a population of unicellular organisms in response to biotic stimulus [GO:0036180]; filamentous growth of a population of unicellular organisms in response to starvation [GO:0036170]; hyphal growth [GO:0030448]; maintenance of cell polarity [GO:0030011]; maintenance of protein location in cell [GO:0032507]; mitochondrion organization [GO:0007005]; negative regulation of synaptic vesicle exocytosis [GO:2000301]; nuclear division [GO:0000280]; nuclear migration [GO:0007097]; positive regulation of Rho protein signal transduction [GO:0035025]; Rap protein signal transduction [GO:0032486]; regulation of cellular component organization [GO:0051128]; regulation of establishment of cell polarity [GO:2000114]; regulation of filamentous growth [GO:0010570]; septin ring organization [GO:0031106]; small GTPase-mediated signal transduction [GO:0007264]; thigmotropism [GO:0009652]; vacuole organization [GO:0007033]

cell cortex [GO:0005938]; cell division site [GO:0032153]; cell septum [GO:0030428]; cellular bud neck [GO:0005935]; fungal-type cell wall [GO:0009277]; hyphal tip [GO:0001411]; incipient cellular bud site [GO:0000131]; plasma membrane [GO:0005886]; vacuolar membrane [GO:0005774]

GDP binding [GO:0019003]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]

IPR027417;IPR041841;IPR005225;IPR001806;IPR020849;

3.40.50.300;

A0A1D8PS71

MVSVSKLINNGLLLTSQSVFQDVATPQQASVQQYNILNFLGGSAPYIQRNGYGISTDIPAGCEIAQIQLYSRHGERYPSKSNGKSLEAIYAKFKNYNGTFKGDLSFLNDYTYFVKDQSNYAKETSPKNSEGTYAGTTNALRHGAAFRAKYGSLYKENSTLPIFTSNSNRVHETSKYFARGFLGDDYEEGKTVKFNIISEDADVGANSLTPRSACSKNKESSSSTAKKYNTTYLNAIAERLVKPNPGLNLTTSDVNNLFSWCAYEINVRGSSPFCDLFTNEEFIKNSYGNDLSKYYSNGAGNNYTRIIGSVILNSSLELLKDTENSNQVWLSFAHDTDLEIFHSALGLLEPAEDLPTSYIPFPNPYVHSSIVPQGARIYTEKLQCGNDAYVRYIINDAVVPIPKCATGPGFSCKLDDFENFVKERIGDVDFIKQCGVNSTYPSELTFYWDYKNVTYNAPLEL

Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)

FUNCTION: Catalyzes the phosphate monoester hydrolysis of phytic acid (myo-inositol hexakisphosphate), which results in the stepwise formation of myo-inositol pentakis-, tetrakis-, tris-, bis-, and monophosphates, as well as the liberation of inorganic phosphate (PubMed:29216308). Myo-inositol 2-monophosphate is the end product (By similarity). Responsible of about 25% of the phytase activity (PubMed:29216308). The residual phytase activity might be contributed by other cytosolic or cellular enzymes such as acid phosphatase that also degraded the substrate phytate (PubMed:29216308). Is essential for human tissue damage during infection (PubMed:29216308). {ECO:0000250|UniProtKB:P34752, ECO:0000269|PubMed:29216308}.

3.1.3.-; 3.1.3.8

CATALYTIC ACTIVITY: Reaction=1D-myo-inositol hexakisphosphate + H2O = 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate; Xref=Rhea:RHEA:16989, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57798, ChEBI:CHEBI:58130; EC=3.1.3.8; Evidence={ECO:0000269|PubMed:29216308}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16990; Evidence={ECO:0000269|PubMed:29216308}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,2,4,5,6-pentakisphosphate + H2O = 1D-myo-inositol 1,2,5,6-tetrakisphosphate + phosphate; Xref=Rhea:RHEA:77115, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57798, ChEBI:CHEBI:195535; Evidence={ECO:0000250|UniProtKB:P34752}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77116; Evidence={ECO:0000250|UniProtKB:P34752}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,2,5,6-tetrakisphosphate + H2O = 1D-myo-inositol 1,2,6-trisphosphate + phosphate; Xref=Rhea:RHEA:77119, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:195535, ChEBI:CHEBI:195537; Evidence={ECO:0000250|UniProtKB:P34752}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77120; Evidence={ECO:0000250|UniProtKB:P34752}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,2,6-trisphosphate + H2O = 1D-myo-inositol 1,2-bisphosphate + phosphate; Xref=Rhea:RHEA:77131, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:195537, ChEBI:CHEBI:195539; Evidence={ECO:0000250|UniProtKB:P34752}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77132; Evidence={ECO:0000250|UniProtKB:P34752}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,2-bisphosphate + H2O = 1D-myo-inositol 2-phosphate + phosphate; Xref=Rhea:RHEA:77135, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:84142, ChEBI:CHEBI:195539; Evidence={ECO:0000250|UniProtKB:P34752}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77136; Evidence={ECO:0000250|UniProtKB:P34752};

Disulfide bond;Glycoprotein;Hydrolase;Reference proteome;Secreted;Virulence

hyphal growth [GO:0030448]

cell surface [GO:0009986]; cell wall-bounded periplasmic space [GO:0030287]; extracellular region [GO:0005576]; fungal-type cell wall [GO:0009277]

4-phytase activity [GO:0008707]; acid phosphatase activity [GO:0003993]

SUBCELLULAR LOCATION: Secreted {ECO:0000305}.

IPR033379;IPR000560;IPR029033;IPR016274;

3.40.50.1240;

A0A1D8PT03

MKIAIIQYSTYGHITQLAKAVQKGVADAGYKADIFQVPETLPQEVLDKMHAPAKPTDIPIATNDTLTEYDAFLFGVPTRYGTAPAQFFEFWGATGGLWANGSLAGKPAGVFVSTSGQGGGQETTVRNFLNFLAHHGMPYIPLGYANAFALQSSMEEVHGGSPYGAGTFANVDGSRQPSTLELEIAEKQGEAFVKSATKLVKGSKKTNTTTTSKSAATSDAAGTTSGTAAGTSAATGAATGTSAPKESTKEASSSAKKEATNGTATRTQQSTKAPETAEKSSCSKCIIM

Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)

FUNCTION: Flavodoxin-like protein (FLP) that plays a role in cell wall integrity, oxidative stress protection and virulence (PubMed:26087349, PubMed:26325183). FLPs act as NAD(P)H quinone oxidoreductases (PubMed:26325183). Reduces ubiquinone (coenzyme Q), enabling it to serve as an antioxidant in the membrane (PubMed:26325183). {ECO:0000269|PubMed:26087349, ECO:0000269|PubMed:26325183}.

1.6.5.2

CATALYTIC ACTIVITY: Reaction=a quinone + H(+) + NADH = a quinol + NAD(+); Xref=Rhea:RHEA:46160, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124; EC=1.6.5.2; Evidence={ECO:0000305|PubMed:26325183}; CATALYTIC ACTIVITY: Reaction=a quinone + H(+) + NADPH = a quinol + NADP(+); Xref=Rhea:RHEA:46164, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:132124; EC=1.6.5.2; Evidence={ECO:0000305|PubMed:26325183};

COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000255|PROSITE-ProRule:PRU00088};

Cell membrane;Flavoprotein;FMN;Membrane;NAD;Nucleotide-binding;Oxidoreductase;Reference proteome;Virulence

cellular response to oxidative stress [GO:0034599]

eisosome [GO:0032126]; fungal biofilm matrix [GO:0062040]; membrane [GO:0016020]; plasma membrane [GO:0005886]

FMN binding [GO:0010181]; NAD(P)H dehydrogenase (quinone) activity [GO:0003955]

SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26325183}; Peripheral membrane protein {ECO:0000269|PubMed:26325183}.

IPR008254;IPR029039;IPR010089;IPR005025;

3.40.50.360;

A0A1D8PT38

MKKSTGPTQTRQVVFNISQNFKVLKILGEGAYGIVALAVHLPTETKVAIKKIEPFERPLFCLRTLREIKLLTKFKNHDNIVRLYDVQKPMNYDSFNEVYLIQEYMPSDLHNIIHTHLLSDQHVQYFIYQILKGLKMIHSARVIHRDLKPSNILVNEKCDLKICDFGLARLDTKHYNFDEAPRISMLTEYVATRWYRAPEIMLSASNYSTAIDLWSVGCILAELLTYRALFPGSDYINQLKLIFEVLGTPTDEDLQIIKSERAQKFIRSLPTKVKIDLSEFINNHPYRNIKHRGRDQVNPLAIDLLEKLLVFDPAKRITVQDALEHPYLNSYHEQLDEPVTSPIPIEEFDFDIDKKNLDTNDLKKQIFEIVMS

Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)

2.7.11.24

CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.24; Evidence={ECO:0000256|RuleBase:RU361165};

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|RuleBase:RU361165};

ATP-binding;Kinase;Magnesium;Nucleotide-binding;Reference proteome;Serine/threonine-protein kinase;Transferase

cellular response to starvation [GO:0009267]; filamentous growth [GO:0030447]; filamentous growth of a population of unicellular organisms in response to biotic stimulus [GO:0036180]; filamentous growth of a population of unicellular organisms in response to starvation [GO:0036170]; intracellular signal transduction [GO:0035556]; invasive growth in response to glucose limitation [GO:0001403]; negative regulation of MAPK cascade [GO:0043409]; parasexual reproduction with cellular fusion [GO:1990277]; pheromone response MAPK cascade [GO:0071507]; pheromone-dependent signal transduction involved in conjugation with cellular fusion [GO:0000750]; phosphorylation [GO:0016310]; positive regulation of protein export from nucleus [GO:0046827]; retrotransposon silencing [GO:0010526]

cytoplasm [GO:0005737]; mating projection tip [GO:0043332]; nucleus [GO:0005634]

ATP binding [GO:0005524]; identical protein binding [GO:0042802]; MAP kinase activity [GO:0004707]; protein serine/threonine kinase activity [GO:0004674]

IPR011009;IPR003527;IPR000719;IPR017441;IPR008271;

1.10.510.10;

A0A1D8PTD0

MSSRPNAFKGSNSARFVKNQMTTNYRNTNDYRQQNNRNRQQQQPEDPYVANNPMLNDSIQKKELVERIDHIDSIMGFDRLEHGENDGNKPRKGWLINMHATTIPTDDYLAGYSGVDYYFLDEEGGSFKATLQFDPYFFVDVLPGDHESEVEEWMRKYLETANVKSYSRVIKEDLKLPNHLLGLQKTLIKLSFHNIQDLLAARRLLSPIIKDNQLKKESRNMYTFKEIETIMDPSVYIDDIREYDVPYHVRVSIDRNVRVGKWYDVYAKHSKVDFVEDKEKIAFADPVVLAFDIETTKAPLKFPDAKIDQIMMISYMIDGEGFLITNREIISEDIDDFEYTPKPEYPGLFTIFNEPDEKHVLKRFFEHIRDVKPTVIATFNGDFFDWPFVENRTRFHDMDMFEEIGFAKDNEGEYKSKYCVHMDCFRWVKRDSYLPQGSQGLKAVTTAKLGYNPTELDPELMTPYAYDKPQLLSEYSVSDAVATYYLYYKYVHPFIFSLCTIIPLNPDEVLRKGTGTLCEMLLSVQAYEGNILLPNKHSDPIERFYEGHLLESETYVGGHVESLEAGVFRSDIPTHFKIDPTAIDELLGNLHNSIKFCIEVENGKKMEDVENFDEIYTQIESSLLELKNNPSRQEKPLIYHVDVASMYPNIMTSNRLQPDSMKSEEDCAACDFNRPGKNCDRRLPWAWRGEYYPAEMNEYNMIKRTLQNETFPGARPWLPPRTFDELSYAEQAAKIKKRISDYSRKVYHRVKSSKVVTREAIICQRENPFYVDTVRSFRDRRYEFKGLAKVWKGKVGKIASNDTIARDEAKKMVVLYDSLQLAHKVILNSFYGYVMRKGSRWYSMEMAGVTCLTGATIIQMARALVERIGRPLELDTDGIWCILPKSFPENFNLKCKDGKKIFLEYPCSMLNYLVHERFTNHQYQDLVDPETFKYKTRSDNSIFFEVDGPYKAMILPTSKEEGKGLKKRYAVFNEDGSLAELKGFELKRRGELQLIKNFQSDIFKLFLEGDTLDTCYQAVATVANNWLDVLDTKGGMLEDEDLIELICENRSMSKSLADYGDQKSTSITTAKRLGEFLGEEMVKDAGLATKYIISAKPIGSPVTERAIPVSIFSSDKKEIFLKKWLKDPSLNKFSPRDVIDWNYYYERLASVVQKIITIPAALQDVKNPVPRVPHPDWLQKKVKNSEDIMQQKSISNFFKKTTKEDIKLKDIEDFGEVDASVPKGKVVKVTSRKRKSGKANMVEDAEEDEKNQAILNGPCPSMTEDYQGFLQYQKAKWKVQQAGRERRRRLFGANSESSQRSTVGGMFRKRAENIAGTNWEILEYKLDPTKPGDLKVYVRAGDKVHTFNFHVPKKVYASFKTKLSQRKSIPGCEIEESNAILPNGHDGTNLYKLTMAQSVFQEQMSDVDSLLQDSNIMGLYESNIDPVSRAIIDLGNTVKFDDTRVGALGKGLKTGFNTRELIKASSEAYLRKFDMDIVYLLHIVTNSYEFFALFNTWENDCQMFVLKPSANAQELPNNIHKIYREIFESKREKLDKVSNVVNYPAEMSFDVKYYHESAKLFKKLNQVIGKIHESRSNKAFLAIQSPYSSRILNVLNTTDDFPTIKMNISELSLPAVGWQSLISKRVINHYFVLGSWIKNLVAFAKYANVPLCNLQIENIGFLVDIEYARRLSENNIVLWWSPNPLPDLGGFEMDRMVDFDSLAFPTINNPEIYETACLEVEIGTLTINTILTSALINEAEGTDLADENMHFDNNNGASTFAEDSFSSPALSILRSMVKDWWDDALSNNINADSIMNTLVTWVQRNDSMLYDPSLHYHVHNLTSKALLQLISEFKRMGAQVIFANRNKMLIQTSKISVENSYAYGQYILKAARSKPLFNFLDLRIVKYWDILIWMDEFNYGGRSCTEIVNEEMQNLVPENHWHLQKFLPIIFQNEFEDWLVIFLDALTKYKNENLLGKGAQANTPRVTQIVHILKGQKKLQAQEVEEEDDDHGVIETFKKPILRRMEKLYRRQLEAILNPEFKQEYEFPTLAGSYLHMKNPALELVKFLCHVFALSEKRSKEVRILKKELLLIFDVRDFSKDATFRDPCTSLKLPHVICDYCNHIRDIDLCREEEINIWNCLNCHKAYNKIALEEEIINQFNKLFVKFYGQDLKCNKCNQIRQNNMDLHCKCSGNWIETVDYHTIEKQFQTFVNVAKFYNLQLLNGLVEEII

Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)

FUNCTION: DNA polymerase II participates in chromosomal DNA replication. {ECO:0000256|RuleBase:RU365029}.

2.7.7.7

CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.7; Evidence={ECO:0000256|RuleBase:RU365029};

COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000256|ARBA:ARBA00001966, ECO:0000256|RuleBase:RU365029};

4Fe-4S;DNA replication;DNA-binding;DNA-directed DNA polymerase;Iron;Iron-sulfur;Metal-binding;Nucleotidyltransferase;Nucleus;Reference proteome;Transferase;Zinc;Zinc-finger

base-excision repair, gap-filling [GO:0006287]; CENP-A containing chromatin assembly [GO:0034080]; CMG complex assembly [GO:0140529]; DNA replication proofreading [GO:0045004]; double-strand break repair via nonhomologous end joining [GO:0006303]; error-prone translesion synthesis [GO:0042276]; gene conversion [GO:0035822]; leading strand elongation [GO:0006272]; mitotic cell cycle [GO:0000278]; mitotic DNA replication checkpoint signaling [GO:0033314]; mitotic DNA replication initiation [GO:1902975]; mitotic DNA replication leading strand elongation [GO:1903460]; mitotic intra-S DNA damage checkpoint signaling [GO:0031573]; mitotic sister chromatid cohesion [GO:0007064]; nucleotide-excision repair, DNA gap filling [GO:0006297]; premeiotic DNA replication [GO:0006279]; regulatory ncRNA-mediated heterochromatin formation [GO:0031048]

chromosome, telomeric repeat region [GO:0140445]; epsilon DNA polymerase complex [GO:0008622]; nuclear replication fork [GO:0043596]

4 iron, 4 sulfur cluster binding [GO:0051539]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; double-stranded DNA binding [GO:0003690]; nucleotide binding [GO:0000166]; single-stranded DNA 3'-5' DNA exonuclease activity [GO:0008310]; single-stranded DNA binding [GO:0003697]; SUMO binding [GO:0032183]; zinc ion binding [GO:0008270]

SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU365029}.

IPR006172;IPR006133;IPR006134;IPR043502;IPR042087;IPR013697;IPR023211;IPR029703;IPR012337;IPR036397;

1.10.132.60;3.30.342.10;3.90.1600.10;3.30.420.10;

A0A1E1FFL0

MAPMIPPRLQRFPATASADEIFAAFQEDGCVVIEGFISPEQVARFSQEVDPAMEKIPVEVTNNGNSNDRTKRFSKCVIASPTFRNEIIESDLMHELCDRVFSKPGEGMGYHFNDNMVIEVQPGAPAQRLHRDQELYPWWNSMGPAGPECVINFFCAVTPFTEENGATRLVPGSHLWPEFTQINERDCPQFGKIETVPAIMQPGDCYLMSGKVIHGAGHNATTTDRRRALALAIIRRELRPMQAFSLSVPMKLAREMSERSQTMFGFRSSVQHCDVDMVHFWGNDGKDIAHHLGLEAPSVHV

Penicillium brasilianum

FUNCTION: Multifunctional dioxygenase; part of the gene cluster that mediates the biosynthesis of paraherquonin, a meroterpenoid with a unique, highly congested hexacyclic molecular architecture (PubMed:27602587). The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid (DMOA) by the polyketide synthase prhL (By similarity). Synthesis of DMOA is followed by farnesylation by the prenyltransferase prhE, methylesterification by the methyl-transferase prhM, epoxidation of the prenyl chain by the flavin-dependent monooxygenase prhF, and cyclization of the farnesyl moiety by the terpene cyclase prhH, to yield the tetracyclic intermediate, protoaustinoid A (By similarity). The short chain dehydrogenase prhI then oxidizes the C-3 alcohol group of the terpene cyclase product to transform protoaustinoid A into protoaustinoid B (PubMed:27602587). The FAD-binding monooxygenase prhJ catalyzes the oxidation of protoaustinoid B into preaustinoid A which is further oxidized into preaustinoid A1 by FAD-binding monooxygenase phrK (PubMed:27602587). Finally, prhA leads to berkeleydione via the berkeleyone B intermediate (PubMed:27602587, PubMed:29317628). PrhA is a multifunctional dioxygenase that first desaturates at C5-C6 to form berkeleyone B, followed by rearrangement of the A/B-ring to form the cycloheptadiene moiety in berkeleydione (PubMed:27602587, PubMed:29317628). Berkeleydione serves as the key intermediate for the biosynthesis of paraherquonin as well as many other meroterpenoids (Probable). The cytochrome P450 monooxygenases prhB, prhD, and prhN, as well as the isomerase prhC, are probably involved in the late stage of paraherquonin biosynthesis, after the production of berkeleydione (Probable). Especially prhC might be a multifunctional enzyme that catalyzes the D-ring expansion via intramolecular methoxy rearrangement, as well as the hydrolysis of the expanded D-ring (Probable). {ECO:0000250|UniProtKB:Q5ATJ7, ECO:0000269|PubMed:27602587, ECO:0000269|PubMed:29317628, ECO:0000305|PubMed:27602587, ECO:0000305|PubMed:28759016, ECO:0000305|PubMed:29317628}.

1.14.11.-

CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + O2 + preaustinoid A1 = berkeleyone B + CO2 + H2O + succinate; Xref=Rhea:RHEA:65184, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:69025, ChEBI:CHEBI:69026; Evidence={ECO:0000269|PubMed:27602587, ECO:0000269|PubMed:29317628}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65185; Evidence={ECO:0000269|PubMed:27602587, ECO:0000269|PubMed:29317628}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + berkeleyone B + O2 = berkeleydione + CO2 + H2O + succinate; Xref=Rhea:RHEA:65188, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:69021, ChEBI:CHEBI:69025; Evidence={ECO:0000269|PubMed:27602587}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65189; Evidence={ECO:0000269|PubMed:27602587}; CATALYTIC ACTIVITY: Reaction=2 2-oxoglutarate + 2 O2 + preaustinoid A = berkeleytrione + 2 CO2 + H2O + 2 succinate; Xref=Rhea:RHEA:65192, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:69022, ChEBI:CHEBI:69023; Evidence={ECO:0000269|PubMed:27602587}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65193; Evidence={ECO:0000269|PubMed:27602587};

COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250|UniProtKB:Q4WAW9};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=48.3 uM for preaustinoid A1 {ECO:0000269|PubMed:29317628};

PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:27602587, ECO:0000269|PubMed:29317628}.

3D-structure;Dioxygenase;Iron;Metal-binding;Oxidoreductase

paraherquonin biosynthetic process [GO:0140874]

dioxygenase activity [GO:0051213]; metal ion binding [GO:0046872]

DOMAIN: Residues at positions 150 and 232 are important for type of reaction catalyzed, using identical substrate (PubMed:29317628). Both ausE and prhA accept preaustinoid A1 as a substrate to form divergent products through dynamic skeletal rearrangement. AusE (containing Leu-150 and Ser-232) first desaturates at C1-C2 to form preaustinoid A2,followed by rearrangement leading to the formation of the spiro-lactone in preaustinoid A3 (PubMed:29317628). In contrast, prhA (containing Val-150 and Ala-232) first desaturates at C5-C6 to form berkeleyone B, followed by rearrangement of the A/B-ring to form the cycloheptadiene moiety in berkeleydione (PubMed:29317628). {ECO:0000269|PubMed:29317628}.

IPR008775;

2.60.120.620;

A0A1I9LN01

MTGWYEFPVMIGFVSAAVFLLISVAYLPLLNDLYWSTLKSLTPPAGIVADLLVTNGTIFTSDSSLPFADSMAIRNGRILKVGSFATLKGFIGDGTMEVNLEGKIVVPGLIDSHVHLISGGLQMAQVGLRGVSQKDEFCKMVKDAVQNAKEGSWILGGGWNNDFWGGELPSASWIDEISPRNPVWLIRMDGHMALANSLALKIAGVISLTEDPVGGTIMRMPSGEPTGLLIDAAMELVTPWVKEISVDERREALFRASKYALTRGVTTVIDLGRYFPGTTDELSWKDFQDVYLYADSSKKMMIRTCLFFPITTWSRLLDLKLQKGSVLSEWLYLGGVKAFIDGSLGSNSALFYEEYIDTPNNYGLEVMDPEKLSNFTMAADKSGLQVAIHAIGDKANDMILDMYESVAAANGDRDRRFRIEHAQHLAPGSANRFGQLHIVASVQPDHLLDDADSVAKKLGSERAVKESYLFQSLLNGNALLALGSDWPVADINPLHSIRTAVKRIPPKWDHAWIPSERISFTDALIAQTISAARAAFLDHHLGSLSPGKLADFVILSTNSWDEFSKDVSASVLATYVGGKQLYP

Arabidopsis thaliana (Mouse-ear cress)

FUNCTION: Required for phyA-controlled responses to continuous far-red light (FRc) conditions, including the inhibition of hypocotyl elongation and the regulation of XTH15/XTR7 expression. {ECO:0000269|PubMed:14645728}.

3.5.-.-

Alternative splicing;Cytoplasm;Glycoprotein;Hydrolase;Membrane;Reference proteome;Transmembrane;Transmembrane helix

de-etiolation [GO:0009704]; response to far red light [GO:0010218]; seed germination [GO:0009845]

membrane [GO:0016020]; perinuclear region of cytoplasm [GO:0048471]

hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds [GO:0016810]

SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:14645728}.

IPR013108;IPR011059;IPR032466;IPR033932;

3.10.310.70;3.20.20.140;2.30.40.10;

A0A1J1DL12

MSPKRIISTPLAPQPIGPYSQAVQVGNTVYLSGQIGMNVRTNEMVTGPIRDEAQQAFTNMKAVVEASGAKMSDVVKVNIFIRNFNDFPAINDVMKEFFQSPFPARSTVGVAELPKNARVEIESIVVIE

Dermatophagoides farinae (American house dust mite)

FUNCTION: Catalyzes the hydrolytic deamination of enamine/imine intermediates that form during the course of normal metabolism (PubMed:27539850). May facilitate the release of ammonia from these potentially toxic reactive metabolites, reducing their impact on cellular components. It may act on enamine/imine intermediates formed by several types of pyridoxal-5'-phosphate-dependent dehydratases including L-threonine dehydratase (By similarity). Preferentially digests Leu and Met in cooperation with L-amino acid oxidase, but digests Phe poorly (PubMed:27539850). {ECO:0000250|UniProtKB:P52758, ECO:0000269|PubMed:27539850}.

3.5.99.10

CATALYTIC ACTIVITY: Reaction=2-iminobutanoate + H2O = 2-oxobutanoate + NH4(+); Xref=Rhea:RHEA:39975, ChEBI:CHEBI:15377, ChEBI:CHEBI:16763, ChEBI:CHEBI:28938, ChEBI:CHEBI:76545; EC=3.5.99.10; Evidence={ECO:0000305|PubMed:27539850}; CATALYTIC ACTIVITY: Reaction=2-iminopropanoate + H2O = NH4(+) + pyruvate; Xref=Rhea:RHEA:40671, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:44400; EC=3.5.99.10; Evidence={ECO:0000305|PubMed:27539850};

Allergen;Cytoplasm;Direct protein sequencing;Hydrolase

organonitrogen compound catabolic process [GO:1901565]

cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]

2-iminobutanoate deaminase activity [GO:0120242]; 2-iminopropanoate deaminase activity [GO:0120243]; deaminase activity [GO:0019239]

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P52758}.

IPR006056;IPR019897;IPR035959;IPR006175;

3.30.1330.40;

A0A1L1RKB7

MENAHTKTVEEVLAYFGVNESTGLSLEQVKKLKEKWGSNELPAEEGKTLLELVIEQFEDLLVRILLLAACISFVLAWFEEGEETITAFVEPFVILLILVANAIVGVWQERNAENAIEALKEYEPEMGKVYRQDRKSVQRIKARDIVPGDIVEVAVGDKVPADIRITSIKSTTLRVDQSILTGESVSVIKHTDPVPDPRAVNQDKKNMLFSGTNIAAGKAMGVVIATGVNTEIGKIRDEMVATEQERTPLQQKLDEFGEQLSKVISLICIAVWIINIGHFNDPVHGGSWIRGAIYYFKIAVALAVAAIPEGLPAVITTCLALGTRRMAKKNAIVRSLPSVETLGCTSVICSDKTGTLTTNQMSVCRMFILDKVEGDSCSLNEFTVTGSTYAPMGEVHKDDKLIKCSQYDGLVELATICALCNDSSLDYNEAKGVYEKVGEATETALTCLVEKMNVFDTDLKGLSRIERANACNSVIKQLMKKEFTLEFSRDRKSMSVYCTPNKPSRTSMSKMFVKGAPEGVIDRCTHVRVGNAKIPLSSGIKQKIMSVIREWGTGRDTLRCLALATHDNPPRKEEMNLEDSSNFINYETNLTFVGCVGMLDPPRIEVASSIKLCKQAGIRVIMITGDNKGTAVAICRRIGIFVEDEDVSTKAFTGREFDELSLAAQRDACHHARCFARVEPSHKSKIVEFLQSFDEITAMTGDGVNDAPALKKAEIGIAMGSGTAVAKTASEMVLADDNFSTIVAAVEEGRAIYNNMKQFIRYLISSNVGEVVCIFLTAALGFPEALIPVQLLWVNLVTDGLPATALGFNPPDLDIMNKPPRNPKEPLISGWLFFRYLAIGCYVGAATVGAAAWWFIAADGGPRVTFYQLSHFLQCKEDNPDFSGVDCVVFESPYPMTMALSVLVTIEMCNALNSLSENQSLMRMPPWENIWLVGAICLSMSLHFLILYVEPLPIIFQITPLNVTQWLMVLKISLPVILLDETLKYVARNYLEPGKDSVQPATKPCSLSACTEGVSWPFVFITLPLVIWLYSTDTNFSDMFWS

Gallus gallus (Chicken)

FUNCTION: Catalyzes the hydrolysis of ATP coupled with the transport of calcium. {ECO:0000256|RuleBase:RU361146}.

7.2.2.10

CATALYTIC ACTIVITY: Reaction=ATP + Ca(2+)(in) + H2O = ADP + Ca(2+)(out) + H(+) + phosphate; Xref=Rhea:RHEA:18105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29108, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.10; Evidence={ECO:0000256|RuleBase:RU361146};

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|ARBA:ARBA00001946};

ATP-binding;Calcium;Calcium transport;Disulfide bond;Ion transport;Membrane;Nucleotide-binding;Reference proteome;Sarcoplasmic reticulum;Translocase;Transmembrane;Transmembrane helix;Transport

autophagosome assembly [GO:0000045]; autophagosome membrane docking [GO:0016240]; calcium ion import into sarcoplasmic reticulum [GO:1990036]; calcium ion transmembrane transport [GO:0070588]; calcium ion transport from cytosol to endoplasmic reticulum [GO:1903515]; cardiac muscle hypertrophy in response to stress [GO:0014898]; cellular response to oxidative stress [GO:0034599]; ER-nucleus signaling pathway [GO:0006984]; intracellular calcium ion homeostasis [GO:0006874]; mitochondrion-endoplasmic reticulum membrane tethering [GO:1990456]; negative regulation of heart contraction [GO:0045822]; neuron cellular homeostasis [GO:0070050]; positive regulation of cardiac muscle cell apoptotic process [GO:0010666]; positive regulation of endoplasmic reticulum calcium ion concentration [GO:0032470]; regulation of calcium ion-dependent exocytosis of neurotransmitter [GO:1903233]; regulation of cardiac muscle contraction by calcium ion signaling [GO:0010882]; regulation of the force of heart contraction [GO:0002026]; T-tubule organization [GO:0033292]; transition between fast and slow fiber [GO:0014883]

ribbon synapse [GO:0097470]; sarcoplasmic reticulum membrane [GO:0033017]

ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; calcium ion binding [GO:0005509]; enzyme binding [GO:0019899]; lncRNA binding [GO:0106222]; P-type calcium transporter activity [GO:0005388]; P-type calcium transporter activity involved in regulation of cardiac muscle cell membrane potential [GO:0086039]; S100 protein binding [GO:0044548]; transmembrane transporter binding [GO:0044325]

SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477}. Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361146}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361146}. Sarcoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004326}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004326}.

IPR006068;IPR004014;IPR023299;IPR018303;IPR023298;IPR008250;IPR036412;IPR023214;IPR005782;IPR001757;IPR044492;

3.40.1110.10;2.70.150.10;1.20.1110.10;3.40.50.1000;

A0A1L3THR9

MLAPLFAALLAGAATASPIQERQSSVPVGTIITACTVPNTFALTFDDGPFAYTSELLDLLSSNGVKATFFLNGQNWGSIYDYTSVVTRMDAEGHQIGSHTWSHADLATLDAAGITSQMTQLETALTSILGKVPTYMRPPYFSTNALALSTLGGLGYHVINANIDTLDYEHDDDTIGVAFTNFQNGLASGGTVSLMHDVHAQTVHVLVQEAINAIKAKGLTPVTVGTCLGDASANWYKSGGGSGTTPPPATGGPSPDDTCGGSNGYVCQNSQCCSQWGWCGTTSEYCAAGCQAAYGPCT

Pestalotiopsis sp

FUNCTION: Hydrolyzes the N-acetamido groups of N-acetyl-D-glucosamine polymers in chitin to form chitosan and acetate (PubMed:27901067). May play a role in evasion of the host immune response; plant chitinases liberate chitin molecules from the fungal cell wall which act as elicitors of the plant immune response, deacetylation of the liberated chitin neutralizes elicitor activity (PubMed:27901067). {ECO:0000269|PubMed:27901067}.

3.5.1.41

CATALYTIC ACTIVITY: Reaction=[(1->4)-N-acetyl-beta-D-glucosaminyl](n) + n H2O = n acetate + chitosan; Xref=Rhea:RHEA:10464, Rhea:RHEA-COMP:9593, Rhea:RHEA-COMP:9597, ChEBI:CHEBI:15377, ChEBI:CHEBI:17029, ChEBI:CHEBI:30089, ChEBI:CHEBI:57704; EC=3.5.1.41; Evidence={ECO:0000269|PubMed:27901067}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10465; Evidence={ECO:0000305|PubMed:27901067};

COFACTOR: Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250|UniProtKB:Q6DWK3};

BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8. {ECO:0000269|PubMed:27901067};

BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 55 degrees Celsius. {ECO:0000269|PubMed:27901067};

Carbohydrate metabolism;Cell wall biogenesis/degradation;Chitin degradation;Chitin-binding;Cobalt;Disulfide bond;Hydrolase;Metal-binding;Polysaccharide degradation;Secreted;Signal;Virulence

cell wall organization [GO:0071555]; chitin catabolic process [GO:0006032]; evasion of host immune response [GO:0042783]; polysaccharide catabolic process [GO:0000272]

extracellular region [GO:0005576]

chitin binding [GO:0008061]; chitin deacetylase activity [GO:0004099]; metal ion binding [GO:0046872]

SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:27901067}.

IPR001002;IPR018371;IPR036861;IPR011330;IPR002509;

3.30.60.10;3.20.20.370;

A0A1L5YRA2

MANQRKFFVGGNWKMNGDKAAIDGIISFMKGPLNADTEVVVGCPQCYLMYTREHMPANIGVAAQNCYKTAKGAFTGEISPAMIKDCGCEWVILGHSERRNVFGEPDQLISEKVGHALEAGLKVIPCIGEKLEERESNRTEEVVFAQMKALVPNISDWSRVVIAYEPVWAIGTGKTATPEQAQDVHAKLRQWLRDNVSPQVAESTRIIYGGSVSAGNCKELAKTGDIDGFLVGGASLKPDFVTIINARA

Scylla paramamosain (Mud crab)

FUNCTION: Triosephosphate isomerase is an extremely efficient metabolic enzyme that catalyzes the interconversion between dihydroxyacetone phosphate (DHAP) and D-glyceraldehyde-3-phosphate (G3P) in glycolysis and gluconeogenesis. {ECO:0000250|UniProtKB:P00939}.; FUNCTION: It is also responsible for the non-negligible production of methylglyoxal a reactive cytotoxic side-product that modifies and can alter proteins, DNA and lipids. {ECO:0000250|UniProtKB:P00939}.

4.2.3.3; 5.3.1.1

CATALYTIC ACTIVITY: Reaction=D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate; Xref=Rhea:RHEA:18585, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=5.3.1.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10127, ECO:0000255|RuleBase:RU363013}; CATALYTIC ACTIVITY: Reaction=dihydroxyacetone phosphate = methylglyoxal + phosphate; Xref=Rhea:RHEA:17937, ChEBI:CHEBI:17158, ChEBI:CHEBI:43474, ChEBI:CHEBI:57642; EC=4.2.3.3; Evidence={ECO:0000250|UniProtKB:P00939};

PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. {ECO:0000255|PROSITE-ProRule:PRU10127, ECO:0000255|RuleBase:RU363013}.; PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate from glycerone phosphate: step 1/1. {ECO:0000255|PROSITE-ProRule:PRU10127, ECO:0000255|RuleBase:RU363013}.

3D-structure;Allergen;Cytoplasm;Gluconeogenesis;Glycolysis;IgE-binding protein;Isomerase;Lyase

gluconeogenesis [GO:0006094]; glyceraldehyde-3-phosphate biosynthetic process [GO:0046166]; glycerol catabolic process [GO:0019563]; glycolytic process [GO:0006096]; methylglyoxal biosynthetic process [GO:0019242]

cytoplasm [GO:0005737]; cytosol [GO:0005829]

IgE binding [GO:0019863]; methylglyoxal synthase activity [GO:0008929]; protein homodimerization activity [GO:0042803]; triose-phosphate isomerase activity [GO:0004807]

SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU10127}.

IPR013785;IPR035990;IPR022896;IPR000652;IPR020861;

3.20.20.70;

A0A1L7NQ96

MKIGCHGLVWTGHFDAEGIRYSVQKTREAGFDLVEFPLMDPFSFDVQTAKSALAEHGLAASASLGLSDATDVSSEDPAVVKAGEELLNRAVDVLAELGATDFCGVIYSAMKKYMEPATAAGLANSKAAVGRVADRASDLGINVSLEVVNRYETNVLNTGRQALAYLEELNRPNLGIHLDTYHMNIEESDMFSPILDTAEALRYVHIGESHRGYLGTGSVDFDTFFKALGRIGYDGPVVFESFSSSVVAPDLSRMLGIWRNLWADNEELGAHANAFIRDKLTAIKTIELH

Arthrobacter globiformis

FUNCTION: Catalyzes the reversible C-3 epimerization of several ketoses. Shows the highest enzymatic activity for the epimerization of L-ribulose to L-xylulose. Is also able to convert D-allulose (also known as D-psicose) to D-fructose and, to a lesser extent, L-tagatose to L-sorbose, D-ribulose to D-xylulose, L-allulose to L-fructose and D-tagatose to D-sorbose. {ECO:0000269|PubMed:27713017, ECO:0000269|PubMed:30279320}.

5.1.3.-

CATALYTIC ACTIVITY: Reaction=L-ribulose = L-xylulose; Xref=Rhea:RHEA:53268, ChEBI:CHEBI:16880, ChEBI:CHEBI:17399; Evidence={ECO:0000269|PubMed:30279320}; CATALYTIC ACTIVITY: Reaction=D-allulose = keto-D-fructose; Xref=Rhea:RHEA:42360, ChEBI:CHEBI:27605, ChEBI:CHEBI:48095; Evidence={ECO:0000269|PubMed:27713017, ECO:0000269|PubMed:30279320}; CATALYTIC ACTIVITY: Reaction=keto-L-tagatose = keto-L-sorbose; Xref=Rhea:RHEA:61780, ChEBI:CHEBI:13172, ChEBI:CHEBI:134275; Evidence={ECO:0000269|PubMed:27713017}; CATALYTIC ACTIVITY: Reaction=D-ribulose = D-xylulose; Xref=Rhea:RHEA:51544, ChEBI:CHEBI:17140, ChEBI:CHEBI:17173; Evidence={ECO:0000269|PubMed:30279320}; CATALYTIC ACTIVITY: Reaction=L-allulose = keto-L-fructose; Xref=Rhea:RHEA:61784, ChEBI:CHEBI:37724, ChEBI:CHEBI:145026; Evidence={ECO:0000269|PubMed:27713017}; CATALYTIC ACTIVITY: Reaction=keto-D-tagatose = keto-D-sorbose; Xref=Rhea:RHEA:43048, ChEBI:CHEBI:13022, ChEBI:CHEBI:47693; Evidence={ECO:0000269|PubMed:27713017};

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:27713017}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:27713017, ECO:0000269|PubMed:30279320}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000269|PubMed:27713017}; Note=Binds 1 divalent metal cation per subunit. Seems able to use Mg(2+), Mn(2+) or Co(2+). {ECO:0000269|PubMed:27713017, ECO:0000269|PubMed:30279320};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=31 mM for D-allulose {ECO:0000269|PubMed:27713017}; KM=37.5 mM for D-fructose {ECO:0000269|PubMed:27713017}; Vmax=177 umol/min/mg enzyme for the epimerization of D-allulose {ECO:0000269|PubMed:27713017}; Vmax=78.4 umol/min/mg enzyme for the epimerization of D-fructose {ECO:0000269|PubMed:27713017}; Note=kcat is 5664 min(-1) for the epimerization of D-allulose. kcat is 2509 min(-1) for the epimerization of D-fructose. {ECO:0000269|PubMed:27713017};

BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5-8.0. Is stable from pH 6.0-11.0. {ECO:0000269|PubMed:27713017};

BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 70 degrees Celsius. Is highly stable at 55 degrees Celsius. {ECO:0000269|PubMed:27713017};

3D-structure;Carbohydrate metabolism;Cobalt;Isomerase;Magnesium;Manganese;Metal-binding

carbohydrate metabolic process [GO:0005975]

manganese ion binding [GO:0030145]; racemase and epimerase activity, acting on carbohydrates and derivatives [GO:0016857]

IPR036237;IPR013022;

3.20.20.150;

A0A1L8G2K9

MGDMQMSVVDPTWELLDPNPDIRALFLEFNDTFFWGQLSGVEVKWSARMTLCAGVCSYEGRGGLCSIRLSEPLLKLRPRKDLVETLLHEMIHALLFVTHNNKDHDSHGPEFCKHMERINGRTGANISVYHNFHDEVDEYRKHWWLCNGPCQKRKPYFGYVKRAMNRAPSSLDPWWADHQRTCGGSFVKVKEPENYPQKRKRKNDPTISEVNSSSHVKGKSNGVDIRTVIPFSGTGYKLFEPNKSDAPLKILNINPTKDKAAVPLLNHTPPSTNINGTFLTNKIGSAKSTPAQSILTKVSVANTKVFINLNGSPIKLPSGSKNKSHQISSKQKSVLPFFKMQKDNSFDLTLPSPSIQSTSQKPQKDISFGFTLPSQSFPSTSPGSNSENKEPLYKKLQMNDRESFIIHSGNKTNVNDNKSCTGPAATTASGLNHTIKVSCPVCGTEVLECKINDHLDTCTSSGPQKDILLDVSLPLQSFPSTSQGSNSAIKEPLYKKLQINDKDSFIIHSGNKTNVNDNKSCTRPAATTASGFNHTIKVCCPVCGTDVLQDKINDHLDTCLQNCNT

Xenopus laevis (African clawed frog)

FUNCTION: DNA-dependent metalloendopeptidase that mediates the proteolytic cleavage of covalent DNA-protein cross-links (DPCs) during DNA synthesis, thereby playing a key role in maintaining genomic integrity (PubMed:30595436, PubMed:35534579, PubMed:36608669). DPCs are highly toxic DNA lesions that interfere with essential chromatin transactions, such as replication and transcription, and which are induced by reactive agents, such as UV light or formaldehyde (By similarity). Associates with the DNA replication machinery and specifically removes DPCs during DNA synthesis (By similarity). Catalyzes proteolytic cleavage of the hmces DNA-protein cross-link following unfolding by the brip1/fancj helicase (PubMed:35534579, PubMed:36608669). Acts as a pleiotropic protease for DNA-binding proteins cross-linked with DNA, such as top1, top2a, histones H3 and H4 (By similarity). Mediates degradation of DPCs that are not ubiquitinated, while it is not able to degrade ubiquitinated DPCs (PubMed:30595436). SPRTN activation requires polymerase collision with DPCs followed by helicase bypass of DPCs (PubMed:30595436). May also act as a 'reader' of ubiquitinated pcna: facilitates chromatin association of rad18 and is required for efficient pcna monoubiquitination, promoting a feed-forward loop to enhance pcna ubiquitination and translesion DNA synthesis (By similarity). Acts as a regulator of translesion DNA synthesis by recruiting vcp/p97 to sites of DNA damage (By similarity). {ECO:0000250|UniProtKB:Q9H040, ECO:0000269|PubMed:30595436, ECO:0000269|PubMed:35534579, ECO:0000269|PubMed:36608669}.

3.4.24.-

COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q9H040};

Autocatalytic cleavage;Chromosome;DNA damage;DNA repair;Hydrolase;Isopeptide bond;Metal-binding;Metalloprotease;Nucleus;Protease;Reference proteome;Repeat;Zinc;Zinc-finger

DNA damage response [GO:0006974]; protein autoprocessing [GO:0016540]; protein-DNA covalent cross-linking repair [GO:0106300]; proteolysis [GO:0006508]

chromatin [GO:0000785]; nucleus [GO:0005634]

double-stranded DNA binding [GO:0003690]; metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; polyubiquitin modification-dependent protein binding [GO:0031593]; single-stranded DNA binding [GO:0003697]

SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H040}. Chromosome {ECO:0000269|PubMed:30595436}. Note=Localizes to sites of UV damage via the PIP-box (By similarity). Recruited to stalled replication forks at sites of replication stress (By similarity). {ECO:0000250|UniProtKB:Q9H040}.

PTM: Autocatalytically cleaved in response to double-stranded DNA-binding: autocatalytic cleavage takes place in trans and leads to inactivation. {ECO:0000250|UniProtKB:Q9H040}.

DOMAIN: The UBZ4-type zinc fingers mediate binding to 'Lys-48'- and 'Lys-63'-linked polyubiquitin. {ECO:0000250|UniProtKB:Q9H040}.

IPR006642;IPR044245;IPR006640;

3.30.160.60;

A0A1L8GSA2

MMETQPTSLPHVLPQDVYEFCDDRKSLGRLRVSEMPAESNGDGGGSKGDGAAVVAKEVPEQSNKKRKRCGVCVPCLRKEPCGACYNCVNRSTSHQICKMRKCEQLKKKRVVPLKGVEAVNKDDSKNQAKEQVPNVKNCSESILVDGPKTDQMEAGPVNHVQEGRLKKECDSTLPSKACEDLANQLLMEANSWLSNTAAPQDPCNKLNWDKPTIPNHTAATNNSNLEDAKNLVAFSAVAEAMSNYGMPASGTPSSVSMQLYEKFNYETNRDSSGHPEGNAPSCPEDLNTLKTALALAKHGVKPPNCNCDGPECPDYLEWLENKIKSSQKDSQESSFPGLGQVSKELVQKSYPKEEVLNLENKNLCPSGNLPFSQNALSLAKEKNISLQTAIAIEALTQLSSALPQTNNECPNSSSQPLINTCDQLTHFPTAKGNQLPIFPMACNELFQNQQSQLYTGKNALPVPQSPRQTSWEQNKKPSYQEGQYIPENLSQSSSVLPSDASTPQKTEFLQQWIQNADLLKSPSDPMTGLKQLLGNTDEYIKSVFKGPEALPNKIKHVKTKRTIKSIKKKSSDFLKMSPDQQLSQLLQENDFHHNAQAALQQHLHHKRNLFVDPNTMEACAQEQQNWWVPKSQKLPVSKTTENPVKERKKRRQRSPSQKQVEPKPKPPRKQVQIKKPRMKEGNAVFMPVSQISLDAFRGAEKEENQLKEMNLEKSLSNNIQPDLLESQSILVTGSQANIENRKTVNTQETCNENQASNGKASNFALCVNQANSLGAKDSCPTPSTDDASSSSGQGDSANQHTNVGDVPGQNDLSCLDDKFEDLLRQFEAEFGEDFSLPGSEAPSQNGVGPPKQQISGDPQFKMPFPSQLLPSENSTRPDAHSNPALSNNPISHNVSHNLDSLFSSKSPKKIKIESSGAITVVSTTCFYSEENQHLDGTPTKSDLPFNPTLSGFLESPLKYLTSPTKSLIDTPAKMAQAEFPTCDCVEQINEKDEGPYYTHLGSGPTVASIRELMEDRFGEKGEAIRIEKVIYTGKEGKSSRGCPIAKWVIRRQSEDEKLMCLVRQRAGHHCENAVIIILIMAWEGIPRALGDSLYSDITETITKYGNPTSRRCGLNDDRTCACQGKDPNTCGASFSFGCSWSMYFNGCKYARSKTPRKFRLIGDNPKEEEFLNDNFQDLATKVAPVYQMLAPQSYENQVNNEEVAIDCRLGLKEGRPFSGVTACMDFCAHAHKDQHNLYNGCTVVCTLTKEDNRTIGRIPEDEQLHVLPLYKVSSTDEFGSEDGQAEKIRKGGIQVLASFPREVRKLSEPAKSCRQRQLDAKKAAAEKKKLQKEKLVSPDKTKQEPADTKMCQQNPGVPQQQTKPCVKVEPSNHYNTYKYNGNGVVESYSVLGSCRPSDPYSMNSVYSYHSFYAQPNLPSVNGFHSKFALPPFGFYGFPNNPVVPNQFMNYGTSDARNSGWMNNSFEKKPDVQSLADGMNQSYGSELPEQSYRRSSEVPHHYSLQNPNSQKSFNISHRTTPSPMETTPYSNLPCYNKVIKKEPVCDPLVDPFQRANSVHSQSPGVNHSLQTSDLPFKANGALPSSGRSNAEGPCSMSLPNDKSGLEKRDYFGVHSNVPALKDKQWTPYGTDVPVGQRDSLDAQSPGKVWSSCKLSDSPAVLPSFASTQTKNWNGRQASLNQGLKEPMPFQEKLWNSVAASDRCSVTPSDRSSVTPCAELQDKNWASFPNPVGNSLKTESSQNHWDPYSLDDNMDDGQSKSVKEEEDEEEIWSDSEHNFLDKNIGGVAVAPGHGSILIECARRELHATTPLKKPNRCHPARISLVFYQHKNLNQPNHGLALWEAKMKLLAERARVKEEEAARLGIKQEVKSLGKKRKWGGAATTETPPVEKKDFIPTRQATTILTDSATTAFSYAYTKVTGPYSRFI

Xenopus laevis (African clawed frog)

FUNCTION: Dioxygenase that catalyzes the conversion of the modified genomic base 5-methylcytosine (5mC) into 5-hydroxymethylcytosine (5hmC) and plays a key role in epigenetic chromatin reprogramming during embryonic development. Conversion of 5mC into 5hmC probably constitutes the first step in cytosine demethylation. Selectively binds to the promoter region of target genes and contributes to regulate the expression of numerous developmental genes, including pax6, rax, sox9 and six3. May also contribute to the regulation of target genes in ways that do not require its enzyme activity. {ECO:0000269|PubMed:23217707}.

1.14.11.80

CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + a 5-methyl-2'-deoxycytidine in DNA + O2 = a 5-hydroxymethyl-2'-deoxycytidine in DNA + CO2 + succinate; Xref=Rhea:RHEA:52636, Rhea:RHEA-COMP:11370, Rhea:RHEA-COMP:13315, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:85454, ChEBI:CHEBI:136731; EC=1.14.11.80; Evidence={ECO:0000269|PubMed:23217707}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + a 5-hydroxymethyl-2'-deoxycytidine in DNA + O2 = a 5-formyl-2'-deoxycytidine in DNA + CO2 + H2O + succinate; Xref=Rhea:RHEA:53828, Rhea:RHEA-COMP:13315, Rhea:RHEA-COMP:13656, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:136731, ChEBI:CHEBI:137731; EC=1.14.11.80; Evidence={ECO:0000250|UniProtKB:Q6N021}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + a 5-formyl-2'-deoxycytidine in DNA + O2 = a 5-carboxyl-2'-deoxycytidine in DNA + CO2 + H(+) + succinate; Xref=Rhea:RHEA:53832, Rhea:RHEA-COMP:13656, Rhea:RHEA-COMP:13657, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:137731, ChEBI:CHEBI:137732; EC=1.14.11.80; Evidence={ECO:0000250|UniProtKB:Q6N021};

COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250|UniProtKB:Q6N021}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:Q6N021}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q6N021}; Note=The zinc ions have a structural role. {ECO:0000250|UniProtKB:Q6N021};

Chromatin regulator;Chromosome;Coiled coil;Developmental protein;Dioxygenase;DNA-binding;Iron;Metal-binding;Nucleus;Oxidoreductase;Reference proteome;Zinc;Zinc-finger

5-methylcytosine catabolic process [GO:0006211]; DNA demethylation [GO:0080111]; eye development [GO:0001654]; nervous system development [GO:0007399]; positive regulation of gene expression via CpG island demethylation [GO:0044029]; positive regulation of transcription by RNA polymerase II [GO:0045944]

chromosome [GO:0005694]; nucleus [GO:0005634]

5-methylcytosine dioxygenase activity [GO:0070579]; methyl-CpG binding [GO:0008327]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; zinc ion binding [GO:0008270]

SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:A0JP82}. Chromosome {ECO:0000250|UniProtKB:A0JP82}. Note=Detected on chromatin, where it binds to target gene promoters. {ECO:0000250|UniProtKB:A0JP82}.

DOMAIN: Binds target DNA that contains at least one unmethylated cytosine via the CXXC-type zinc-finger domain. {ECO:0000250|UniProtKB:A0JP82}.

IPR024779;IPR040175;IPR046942;IPR002857;

A0A1L8GVF0

MSKIEKMSIQGVRSFGINDKNKQVIQFFTPLTILVGPNGAGKTTIIECLKYMTTGDFPSGSKGNTFVYHPKLAHETDVRAQICLQLKDVNGEPVAVQRSIICRQKGKSTECKTVDCVITRIKHGGPVSLRPKCEEMNKEMISALGVSSAVLNNVIFCHQEDSNWPLSEGKRLKGKFDEIFSITRYSKALETLRDVRMKEDQNVSNYQEEIKYLKENKEKAREIQDNLQSKEKQLTVSKENVKSIESQLEPLKDRLADIQRNLFKVIRLENEIKALESRKRTMEQDNQDLMEKMEKVFQGTDEELNEMYQNQCFVREKERKLNDHQREMDRACKESQRLNREKGELLVQQGHLQLEADNHQRYIKTRDSLIKSLAVQLELDGFELTPFNQRQTSNFQMLVKERQEEVEAHANQILREFSEREAMQQRQIDEIRDKKTGLERTIELKSSTESKKHTDLKKVKYDLQQLEGTSDRLHELDEELQKTAHALENVEKSCNLEALKGEVVQLQTQKSELDRNVRELDQEMEQLNKHTMTRTQMDMLKNDKADKDEQIRKMKSRHNDELISLYEYFPNKKQLEDWLYSKREDINQTRDKLARLTKELVAAEQNSNHLSNELCQKEKQSASFEEKVFDVCGSQDFNSDLSQLLEDIEKTSKQRAMLAGATAVYTQFITTLTEENQPCCPVCQRTFPSEAEVQDVINDMQSKLCLVPDKLKAAEDELKRKEKRKDEMMELKPMRQMLSDLKEKEIPEIRNKLEAINREIKRLQNDVEEQESLIVTFVSEEARAEACLQDISLMEQYQMELRDVDQKIAHYATKLLGVDLNRTVQQVNQEKLEKHHSLDNVSRRIELLQNHLQNQQEQVQQLKSRVNELTAEKLHISSNLQQRQQLEEQNVELTTELHCLSIEIKESREQVFPLESTLQKLQQEKQALLQRKESSYREAQEKVNDIKEKVKKINLHTKDIEKYIQDGKEEFKEQKESELQELTVRLNECEELKEKINREMVTIRQDIDTQKIQERCLQDNLTLRKRIEELKQVEEERDQLLKEMGQMKVTQMEKEYQELENKRETLKTNHSLTLGRQKGFEDEILRFKNELNEPKYKDAEEEYREKMIVMRTTELAIKDLDIYFKTMDQAIMKFHSIKMEEINKIIRDLWCSTYRGQDIEYIEIQSEPDEGISAADNRRTYNYRVVMIKGDTELDMRGHCSAGQKVLASLIIRLALAEIFCSNCGVLALDEPTTNLDHENIDSLAHALVEIIKSRSRQRNFQLIVITHNEDFVELLGRSEYVEHFYRIKKNIDQCSEIIRCSVSSLASYLH

Xenopus laevis (African clawed frog)

FUNCTION: Component of the MRN complex, which plays a central role in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity and meiosis (PubMed:19892829, PubMed:23434370). The MRN complex is involved in the repair of DNA double-strand breaks (DSBs) via homologous recombination (HR), an error-free mechanism which primarily occurs during S and G2 phases (PubMed:19892829). The complex (1) mediates the end resection of damaged DNA, which generates proper single-stranded DNA, a key initial steps in HR, and is (2) required for the recruitment of other repair factors and efficient activation of ATM and ATR upon DNA damage (By similarity). The MRN complex possesses single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity, which are provided by mre11, to initiate end resection, which is required for single-strand invasion and recombination (By similarity). Within the complex, rad50 is both required to bind DNA ends and hold them in close proximity and regulate the activity of MRE11 (By similarity). Rad50 provides an ATP-dependent control of MRE11 by positioning DNA ends into the mre11 active site: ATP-binding induces a large structural change from an open form with accessible MRE11 nuclease sites into a closed form (By similarity). The MRN complex is also required for DNA damage signaling via activation of the atm and atr kinases: the nuclease activity of mre11 is not required to activate ATM and ATR (By similarity). The MRN complex promotes recruitment of topbp1 to DNA damage sites (PubMed:23582259). The MRN complex and rbbp8/CtIP are also required for chromosome alignment during metaphase (PubMed:23434370). {ECO:0000250|UniProtKB:Q92878, ECO:0000250|UniProtKB:Q9X1X1, ECO:0000269|PubMed:19892829, ECO:0000269|PubMed:23434370, ECO:0000269|PubMed:23582259}.

3.6.-.-

CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q92878};

COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q92878}; Note=Binds 1 zinc ion per homodimer. {ECO:0000250|UniProtKB:Q92878};

ATP-binding;Chromosome;Coiled coil;DNA damage;DNA repair;Hydrolase;Magnesium;Meiosis;Metal-binding;Nucleotide-binding;Nucleus;Reference proteome;Telomere;Zinc

chromosome organization involved in meiotic cell cycle [GO:0070192]; DNA double-strand break processing [GO:0000729]; DNA duplex unwinding [GO:0032508]; DNA strand resection involved in replication fork processing [GO:0110025]; metaphase chromosome alignment [GO:0051310]; R-loop processing [GO:0062176]; telomere maintenance via recombination [GO:0000722]; telomere maintenance via telomerase [GO:0007004]

chromosome, telomeric region [GO:0000781]; condensed nuclear chromosome [GO:0000794]; Mre11 complex [GO:0030870]; site of double-strand break [GO:0035861]

ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; double-stranded telomeric DNA binding [GO:0003691]; G-quadruplex DNA binding [GO:0051880]; metal ion binding [GO:0046872]; protein serine/threonine kinase activator activity [GO:0043539]; single-stranded telomeric DNA binding [GO:0043047]

SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q92878}. Chromosome, telomere {ECO:0000250|UniProtKB:Q92878}. Chromosome {ECO:0000250|UniProtKB:Q92878}. Note=Localizes to discrete nuclear foci after treatment with genotoxic agents. Localizes to DNA double-strand breaks (DSBs). {ECO:0000250|UniProtKB:Q92878}.

DOMAIN: The zinc-hook, which separates the large intramolecular coiled coil regions, contains 2 Cys residues that coordinate one molecule of zinc with the help of the 2 Cys residues of the zinc-hook of another RAD50 molecule, thereby forming a V-shaped homodimer. The two heads of the homodimer, which constitute the ATP-binding domain, interact with the MRE11 homodimer. {ECO:0000250|UniProtKB:P58301}.

IPR027417;IPR038729;IPR004584;IPR013134;

3.40.50.300;

A0A1L8GXM0

MSKIEKMSIQGVRSFGIEDKNKQVIQFFTPLTVLVGPNGAGKTTIIECLKYITTGDFPPGSKGKTFVHDPKVAHETDVRAQIRLQLKDVNGELVAVQRSMICTQKGKSTEFKTLEGVITRIKHGEKVSLSTKCAEMDKEMISALGVSAAVLNNVIFCHQEDSNWPLSEGRQLKVKFDEIFSATRYIKALETLKKVRTQQAHNVREYQVEIKYLKQNKEKAREIQDNLQSKEKQLAVSKENVKSIESQLEPLKDRLADIQRNLSKVMRLDNEIKALESRKRTMEQDNQDLEEKMEKVFQGTDEELNGMYQNHQRSVREKERKLNDQQREMDRACKESQRLNREKGELLVQQGRLQLEADHHQQYIKTRDSLIKSLAAQLELDGFERTPFNQRQTSNFQMLVKERQEKDEAHANQILREFSEREAMKQRQLDEMRDKKTGLERTIELKSSTQSKKHTDLKNVKYELQQLEGSSDRLQELDEELQKTERELENVEKSCNLEALRGEVLQLQNQKSELDRNVRKLDQEMEQMNTHTMTRTQMDMLKKDKADKDEQIRKIKSRHNDELSLLLGYFPNKKQLEDWLYSKRKDINQTRDKLARLTKELVAAEQNKNHLSNELRRKEEQSASFEEKVFDVCGSQDFDSDLSRLQDDIEKTSKQRAMLAGATAVYTQFITTLTEENQPCCPVCQRIFPSEAELQDVINDMQSKLRLVPDKLKSAEGELKRKEKRKDDMMELKPMRQMLADLKEKEIPEIRNKLVTINREIQRLKNDVDEQETLIATFASEEESAKACLQDISLMERYQMELRDVERKIAQYATKLQGVDLNRTVQQVSQEKQEKQHNLDNVSGKIELLRKRIQDQQEQVQQLKSAVNELTAEKLHISSNLQRRQQLEDQNVELTTELQCLAREIKEAREQLFPLESTLQKLQQEKQELLQRKESSYREAQEKVNDIKEKVKKINLLTKDIEKYSQDGKEEFKEQKESELQELIGRLNECEKLKEKVNREMVTIRQDIDTQKIQERCLQDNLTLRKRIEELKRVEEERHQLLKEMGQMKVVQMKNEYQELENKSESLKTNHSLALGRQKGFEDEILRFKKELRESQYKEAEEKYREKMIVMRTTELAIKDLDIYYKTLDQAIMKYHSIKMEEINKIVRDLWRSTYRSQDIEYIEIQSDADESVTAADKRRTYNYRVVMIKGDTALDMRGRCSAGQKVLASLIIRLALAETFCLNCGILALDEPTTNLDRENIESLAHALVEIIKSRSRQRNFQLIVITHDEDFVELLGRSEYVEHFYRIKKNIDQCSEIIRCSVNSLASYVH

Xenopus laevis (African clawed frog)

FUNCTION: Component of the MRN complex, which plays a central role in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity and meiosis (PubMed:19892829, PubMed:23434370). The MRN complex is involved in the repair of DNA double-strand breaks (DSBs) via homologous recombination (HR), an error-free mechanism which primarily occurs during S and G2 phases (PubMed:19892829). The complex (1) mediates the end resection of damaged DNA, which generates proper single-stranded DNA, a key initial steps in HR, and is (2) required for the recruitment of other repair factors and efficient activation of ATM and ATR upon DNA damage (By similarity). The MRN complex possesses single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity, which are provided by mre11, to initiate end resection, which is required for single-strand invasion and recombination (By similarity). Within the complex, rad50 is both required to bind DNA ends and hold them in close proximity and regulate the activity of MRE11 (By similarity). Rad50 provides an ATP-dependent control of MRE11 by positioning DNA ends into the mre11 active site: ATP-binding induces a large structural change from an open form with accessible MRE11 nuclease sites into a closed form (By similarity). The MRN complex is also required for DNA damage signaling via activation of the atm and atr kinases: the nuclease activity of mre11 is not required to activate ATM and ATR (By similarity). The MRN complex promotes recruitment of topbp1 to DNA damage sites (PubMed:19279141, PubMed:23582259). The MRN complex and rbbp8/CtIP are also required for chromosome alignment during metaphase (PubMed:23434370). {ECO:0000250|UniProtKB:Q92878, ECO:0000250|UniProtKB:Q9X1X1, ECO:0000269|PubMed:19279141, ECO:0000269|PubMed:19892829, ECO:0000269|PubMed:23434370, ECO:0000269|PubMed:23582259}.

3.6.-.-

CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q92878};

COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q92878}; Note=Binds 1 zinc ion per homodimer. {ECO:0000250|UniProtKB:Q92878};

ATP-binding;Chromosome;Coiled coil;DNA damage;DNA repair;Hydrolase;Magnesium;Meiosis;Metal-binding;Nucleotide-binding;Nucleus;Reference proteome;Telomere;Zinc

chromosome organization involved in meiotic cell cycle [GO:0070192]; DNA double-strand break processing [GO:0000729]; DNA duplex unwinding [GO:0032508]; DNA strand resection involved in replication fork processing [GO:0110025]; metaphase chromosome alignment [GO:0051310]; R-loop processing [GO:0062176]; telomere maintenance via recombination [GO:0000722]; telomere maintenance via telomerase [GO:0007004]

chromosome, telomeric region [GO:0000781]; condensed nuclear chromosome [GO:0000794]; Mre11 complex [GO:0030870]; site of double-strand break [GO:0035861]

ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; double-stranded telomeric DNA binding [GO:0003691]; G-quadruplex DNA binding [GO:0051880]; metal ion binding [GO:0046872]; protein serine/threonine kinase activator activity [GO:0043539]; single-stranded telomeric DNA binding [GO:0043047]

SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q92878}. Chromosome, telomere {ECO:0000250|UniProtKB:Q92878}. Chromosome {ECO:0000250|UniProtKB:Q92878}. Note=Localizes to discrete nuclear foci after treatment with genotoxic agents. Localizes to DNA double-strand breaks (DSBs). {ECO:0000250|UniProtKB:Q92878}.

DOMAIN: The zinc-hook, which separates the large intramolecular coiled coil regions, contains 2 Cys residues that coordinate one molecule of zinc with the help of the 2 Cys residues of the zinc-hook of another RAD50 molecule, thereby forming a V-shaped homodimer. The two heads of the homodimer, which constitute the ATP-binding domain, interact with the MRE11 homodimer. {ECO:0000250|UniProtKB:P58301}.

IPR027417;IPR038729;IPR004584;IPR013134;

1.10.287.1490;3.40.50.300;

A0A1L8HU22

MEALPPQVLKPLDCMSIYSRHREPENRHNELSTGRCGRGHVIFSSMKALQPQVLKPTGSHANLQQVLYAPAATIITAPASSHNDLSSLTGCSYAGVETLGKELFIYFGLKAMRVHFGMNGSMRINQPMKKGQENGRPIPIAVLEVQLTKDLICFYESTVDVRNASECQEKIRFFEELDVCSSKFSFPRAECEIKKQRTRMLCDILLDQMILPGVGNIIKNEALFDSGLHPGVQAGLLTDEQVSHLVKMTRDFTLLFYKCRKSGSALYKHYKVYKRPNCGQCGTKITVCRLGEHNRMTYFCPKCQKDKPQHVDVSKLPTRNSLIGWVQRTASNANEHVATSKEEHWACAVCTLINKPSDKQCDACLTLRPEVSSLAVSDEAAELNTDLVKYPCNNFAKVLPELKLNRRTAFGNTTLVLTDFGAKEGLADKNSQQNILNRSTFDVPLNNKYYHTKTPSNKRSNENEHWTNTLNAVNGHSAASNNVFNHPQKKLKTGHTTSNTIHLSSTISSPQSKMTGDAAAKTGNPQCSAHNVPCALQVVRKEGENKGRSFYTCSLPRERRCQYFEWADLHFPFCNHGKRCIVRTVLKIGPNNGKNFYVCPMGKDKQCNFFEWAKTE

Xenopus laevis (African clawed frog)

FUNCTION: DNA glycosylase which prefers single-stranded DNA (ssDNA), or partially ssDNA structures such as bubble and fork structures, to double-stranded DNA (dsDNA) (PubMed:30842657). Mediates interstrand cross-link repair in response to replication stress: recruited to replication stress sites via interaction with ubiquitinated CMG helicase and acts by mediating DNA glycosylase activity (PubMed:30842657). Cleaves one of the two N-glycosyl bonds comprising the interstrand cross-link, which avoids the formation of a double-strand break but generates an abasic site that is bypassed by translesion synthesis polymerases (PubMed:30842657). {ECO:0000269|PubMed:30842657}.

3.2.2.-; 4.2.99.18

CATALYTIC ACTIVITY: Reaction=2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-phospho-2'-deoxyribonucleoside-DNA + H(+); Xref=Rhea:RHEA:66592, Rhea:RHEA-COMP:13180, Rhea:RHEA-COMP:16897, Rhea:RHEA-COMP:17067, ChEBI:CHEBI:15378, ChEBI:CHEBI:136412, ChEBI:CHEBI:157695, ChEBI:CHEBI:167181; EC=4.2.99.18; Evidence={ECO:0000255|PROSITE-ProRule:PRU00392, ECO:0000269|PubMed:30842657};

Chromosome;DNA damage;DNA repair;DNA-binding;Glycosidase;Hydrolase;Lyase;Metal-binding;Multifunctional enzyme;Nucleus;Reference proteome;Repeat;Zinc;Zinc-finger

base-excision repair [GO:0006284]; interstrand cross-link repair [GO:0036297]

chromosome [GO:0005694]; nucleoplasm [GO:0005654]

class I DNA-(apurinic or apyrimidinic site) endonuclease activity [GO:0140078]; damaged DNA binding [GO:0003684]; DNA N-glycosylase activity [GO:0019104]; DNA-(apurinic or apyrimidinic site) endonuclease activity [GO:0003906]; MCM complex binding [GO:1904931]; zinc ion binding [GO:0008270]

SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8TAT5}. Chromosome {ECO:0000269|PubMed:30842657}. Note=Recruited to replication stress sites via interaction with ubiquitinated CMG helicase. {ECO:0000269|PubMed:30842657}.

DOMAIN: The RanBP2-type zinc-finger, also named NZF zinc finger, recognizes and binds ubiquitinated CMG helicase complex (PubMed:30842657). The GRF-type zinc-fingers recognize single-stranded DNA (ssDNA), possibly on the lagging strand template (PubMed:30842657). {ECO:0000269|PubMed:30842657}.

IPR015886;IPR015887;IPR035937;IPR010979;IPR000214;IPR010666;IPR001876;IPR036443;

1.10.8.50;3.20.190.10;2.30.30.380;

A0A1L8HV70

MATPPKRICIDVPASPSGNKCKVKRISIEGNIAAGKSTFVNILKKANEEWDVVPEPIARWCNIQSCKDEFEELTTSQKSGGNLLQMMYEKPERWSFTFQSYACLSRIRAQLKALGGKLKEAENPVLFFERSVYSDRYIFASNLYEAECMNETEWTVYQDWHDWMNSQFGADLELDGIIYLRAIPEKCLNRVYTRGREEEQGIPMEYLEKLHYKHETWLHHRTLRTDFEYLQEIPILTLDVNEDFRDNKQKQESLIEKVKEFLSTL

Xenopus laevis (African clawed frog)

FUNCTION: Phosphorylates the deoxyribonucleosides deoxyadenosine, deoxycytidine and deoxyguanosine with highest activity against deoxycytidine followed by deadenosine and deoxyguanosine (PubMed:27906638). Shows only very minor activity against deoxyuridine and deoxythymidine (PubMed:27906638). {ECO:0000269|PubMed:27906638}.

2.7.1.113; 2.7.1.74; 2.7.1.76

CATALYTIC ACTIVITY: Reaction=2'-deoxycytidine + a ribonucleoside 5'-triphosphate = a ribonucleoside 5'-diphosphate + dCMP + H(+); Xref=Rhea:RHEA:20061, ChEBI:CHEBI:15378, ChEBI:CHEBI:15698, ChEBI:CHEBI:57566, ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=2.7.1.74; Evidence={ECO:0000269|PubMed:27906638}; CATALYTIC ACTIVITY: Reaction=2'-deoxyguanosine + ATP = ADP + dGMP + H(+); Xref=Rhea:RHEA:19201, ChEBI:CHEBI:15378, ChEBI:CHEBI:17172, ChEBI:CHEBI:30616, ChEBI:CHEBI:57673, ChEBI:CHEBI:456216; EC=2.7.1.113; Evidence={ECO:0000269|PubMed:27906638}; CATALYTIC ACTIVITY: Reaction=2'-deoxyadenosine + ATP = ADP + dAMP + H(+); Xref=Rhea:RHEA:23452, ChEBI:CHEBI:15378, ChEBI:CHEBI:17256, ChEBI:CHEBI:30616, ChEBI:CHEBI:58245, ChEBI:CHEBI:456216; EC=2.7.1.76; Evidence={ECO:0000269|PubMed:27906638};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.34 uM for deoxycytidine {ECO:0000269|PubMed:27906638}; KM=527 uM for deoxyguanosine {ECO:0000269|PubMed:27906638}; KM=533 uM for deoxyadenosine {ECO:0000269|PubMed:27906638}; KM=12457 uM for deoxythymidine {ECO:0000269|PubMed:27906638}; KM=15081 uM for deoxyuridine {ECO:0000269|PubMed:27906638}; Vmax=0.1 umol/min/mg enzyme toward deoxycytidine {ECO:0000269|PubMed:27906638}; Vmax=6.6 umol/min/mg enzyme toward deoxyguanosine {ECO:0000269|PubMed:27906638}; Vmax=5.2 umol/min/mg enzyme toward deoxyadenosine {ECO:0000269|PubMed:27906638}; Vmax=0.6 umol/min/mg enzyme toward deoxythymidine {ECO:0000269|PubMed:27906638}; Vmax=2.5 umol/min/mg enzyme toward deoxyuridine {ECO:0000269|PubMed:27906638}; Note=kcat is 0.09 sec(-1) with deoxycytodine as substrate. kcat is 3.40 sec(-1) with deoxyguanosine as substrate. kcat is 2.73 sec(-1) with deoxyadenosine as substrate. kcat is 0.29 sec(-1) with deoxythymidine as substrate. kcat is 1.27 sec(-1) with deoxyuridine as substrate. {ECO:0000269|PubMed:27906638};

ATP-binding;Kinase;Nucleotide-binding;Nucleus;Reference proteome;Transferase

deoxyribonucleoside monophosphate biosynthetic process [GO:0009157]; phosphorylation [GO:0016310]

cytoplasm [GO:0005737]; nucleus [GO:0005634]

ATP binding [GO:0005524]; deoxyadenosine kinase activity [GO:0004136]; deoxycytidine kinase activity [GO:0004137]; deoxyguanosine kinase activity [GO:0004138]

SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P27707}.

IPR002624;IPR031314;IPR027417;

3.40.50.300;

A0A1P8ASY1

MPPRKKPKSSALKSNKQSSANHSSQPSTFGIQQLFLRHIQNSQSTSNSHTSTADPVDQQNVNGLASDTAVLTPQNPLGTSNEKPDESKDMDQQLTEASPKISKNLKRFSPGMLIKQSQDDCGGEITWKISPVNERLRAAAKNIPKMMDLTENSLGVKSSTIRPCSLNKLVQKQCPTSGITSKVEQWLSSPSKKASKRPAFATNRVMERVNPSPDAEFEIVNTSSSGNSPFQTPPSLSCPHNKLPCTVTCSGACGSMGAGQHKKALLELLDQVEDVIAVDDKTTDDVGIVMPQARVKDDIISSVVDCAVDEGPVSLPKMQNSINPDSYFLVLEVSEKRGSGSSSKGQCPYKVLRLLDEHTGVECALYLWDEWFYSTVSPGDSINVIGEFDGDGKCDVDRQNNFLIVHPDTLVAGTRVAASFGCPRRTVLDERLRSNEHATVALLGTLQHQVFQAGLSQESPSVDGLQEYASTVIEKSIESLYACGVHEGDVRSTLFKAIPKMLNWIEHFRYSKDSEVSKVDFGSTIGKKAVKVSEVIDIEEMSWAPKYGLKGMIDASVRVIVESDMNTVNEKIMPLEFKSGKAPSGQSSIEHSAQVILYTLLMSERYLKHIDNGLLYYLQSDQTQGISVQRSDLVGLIIRRNELANDILVASTTQQLPPMLRNPNICRNCRHLDVCTIYHKADGGNTESSGLGDVFDTHVSHLSTLHFNFLRHWDRLIDLEGREMQLLRKDIAHPHGSKGSHSASYLSSMVLDVTNGFQHHNSHKETRFIYRFVRQKSSESRERVTSEDMIRTGNLATDDLDCKLRTGDRVILRTEVSHLTVANGIIADISRTHISVSLSKRLRLPWSEPSSEVSNLSHELWRIYKDEFMTSFSVMRFNLMQLFVQNGHNIRKMIVDLEPPRFDNGSILSQDPAISYIWSEKSLNNDQRQAILKILTAKDYALILGMPGTGKTSTMVHAVKALLIRGSSILLASYTNSAVDNLLIKLKAQGIEFLRIGRDEAVHEEVRESCFSAMNMCSVEDIKKKLDQVKVVASTCLGINSPLLVNRRFDVCIIDEAGQIALPVSIGPLLFASTFVLVGDHYQLPPLVQSTEARENGMGISLFRRLSEAHPQAISVLQNQYRMCRGIMELSNALIYGDRLCCGSAEVADATLVLSTSSSTSPWLKKVLEPTRTVVFVNTDMLRAFEARDQNAINNPVEASIIAEIVEELVNNGVDSKDIGIITPYNSQASLIQHAIPTTPVEIHTIDKYQGRDKDCILVSFVRSREKPRSSASSLLGDWHRINVALTRAKKKLIMVGSQRTLSRVPLLMLLLNKVKEQSGILNLLPGDLKP

Arabidopsis thaliana (Mouse-ear cress)

FUNCTION: Essential protein required during embryogenesis (PubMed:15266054). Key enzyme involved in DNA replication and damage repair, shoot apical meristem (SAM) maintenance, and development (PubMed:26951435). Involved in Okazaki fragments processing. Possesses different enzymatic activities, such as single-stranded DNA (ssDNA)-dependent ATPase, 5'-3' helicase and endonuclease activities. While the ATPase and endonuclease activities are well-defined and play a key role in Okazaki fragments processing and DSB repair, the 5'-3' DNA helicase activity is atypical: it cannot load onto its tracking strand internally and has an absolute free 5'-end requirement (By similarity). {ECO:0000250|UniProtKB:Q9URU2, ECO:0000269|PubMed:15266054, ECO:0000269|PubMed:26951435}.

3.1.-.-; 3.6.4.12

CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; Evidence={ECO:0000250|UniProtKB:P51530};

COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250|UniProtKB:P38859}; Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250|UniProtKB:P38859};

4Fe-4S;Alternative splicing;ATP-binding;Chromosome;DNA damage;DNA repair;DNA replication;DNA-binding;Helicase;Hydrolase;Iron;Iron-sulfur;Metal-binding;Multifunctional enzyme;Nuclease;Nucleotide-binding;Nucleus;Reference proteome

DNA damage response [GO:0006974]; DNA repair [GO:0006281]; DNA replication [GO:0006260]; meristem maintenance [GO:0010073]; replication fork reversal [GO:0071932]

chromosome [GO:0005694]; cytoplasm [GO:0005737]; nucleus [GO:0005634]

4 iron, 4 sulfur cluster binding [GO:0051539]; 5'-flap endonuclease activity [GO:0017108]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677]; metal ion binding [GO:0046872]; single-stranded DNA helicase activity [GO:0017116]

SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26951435}. Chromosome {ECO:0000250|UniProtKB:P51530}. Note=Localized to nuclear foci in response to DNA damage. {ECO:0000269|PubMed:26951435}.

IPR026851;IPR045055;IPR041679;IPR041677;IPR014808;IPR027417;IPR011604;IPR047187;

3.90.320.10;3.40.50.300;

A0A1R3RGK0

MTFTSHPQSEPLAIIGLACKYANDINSPLDLYQQVMAARSMHGPMPPSRMDAAFYYHPSSEATGTTYAKGGYFLQSDLNAFDSPFFQLSEIDVLAMDPQQKMLLENVYHALENAGIPLKDAVSSSTSVFVGCSNNDHLALANADLLLALKGKGTGTSPSILANRISWFYDFQGTSQTIDTACSSSLVAFHQGCMDVRAGKSTMSIISGVNLMEHPAPTMYLSSLGVLSPDGRSMSFDARANGYGRGEGLGTVIIKPLTAALRDGNRIRAIVRSTGSNQDGRTPGITVPSPTAQERLIREVYKAADLDPSRTGYVEAHGTGTPVGDPLEVQAISAALGMSRDSPLYVGSVKSVVGHLEGGAGMAGLISATMAVESKTIPPVAGLQTLNPRIPQRPDLKFAKEATPWPREDVRRASINSFGFGGTNAHVVLEDVEGFFSDLFGQQLPGALQLSEVTSKALVPSAMKSAVNGIPADQPPKESSVNRLFVISAFDEAGIQRNAASLASHLESMRAITGSDGEERLLNDLCHTLNEKRTRFDWRSYHVADSIDSLRNSLQNPRPIRQSPAEKVVRFIFTGQGANWAGMAYDLLVYPLFRRRIQEAAIFLKELGSDWDLYERIASQSGELDEPTFAQSSCVAVQVALVDLLASWNVTPQTVVGHSSGEIAAAYCAGQISRQAAWKVAFCRGQVCARRTDGQGRMLAAAMPVTQLEQLVARVNKGQSTAVKVGCYNSPKNLTLTGRAEDILRAKLELDDVGALNRLLPVKVAYHSDYMRDAAPEYLDLLGDLDFGDSIHADAGIKMVSSVTGRAVSAGEAQQPSYWVDNLVSPVRFSTALLASMDDPSATGAREDALIEIGPHSTLRTAIKETFADVREFQSIQYGSLLKRYETDGSTILRTFGMLVCSGHKISLAAINDRRVGAKKTPRLLTGLPSYAFDHSRSMRGTSRRIEQAKFPAYKRHELLGVPVEDTNPVEQRWRNILRPDDLPWLRMNRMNGQIHFPGVAYLLMATEAAIQRVGNTVAISGVRLGNVSMLAPLPIPDSAAGVEIQFSIYPMKIHANSGTDWSTFRIVSYDSAEKTWTEHCVGSVRVETGPHESHEPHPGNATREECTESVDIAQMYSRFTTAGMDFGEYLRNIQEMKLSPDHQACTATITAPDIPCQAHDHYSLHPCTFESILHALLHLCKSSQGPMVTTYIEEVLVLSPQDTGVCGFEACAQTQRASATTWRSDVTITANTGRQQIRVTGLDLVQLPPSEDASDAESFYVVKWKPDVKLLTSVDALRDSASMYVAQHLPTLDEHEGFQLASGIFLLDTMDYVTRTGLPALPQHHQAFMQWMEKECRSIADGTVPLLDTALFEGIRASPDRRRELLARVAQLSARGELLVRVGTQMVPILEQKIDCLEVMFGPDNLMDRTYEEGLPGQIAPSVAGYLHCLAHAQTGIKVLEVGAGTGSATKVILDSLKPTERQDGGGLVSSVSTYHFTDISAAFFEKARARFPDWADILRPKVLNIELDPADQGFEMGSYDLVIATHVLHATADLSVSLKNIRGLLKEGGDLIVIENIQPDLMCSPLAFGLLPGWWRSVEPYRKTNPLITKDQWDQELRNAGLQSRLLIDDTDEGVNEMTAFVASRVREPPATQHVCSIIYSSRYGGQYELASQVARDLPPSCTASLVDLADISPEHTSTIGIVLVGYQGLDLSELSAHEYDRVNFLLTAFHRLLWVTCDEDEVPKSAMASGLVRTARWERDHDGVNFILLGISHRVPSASAAVSQMIRVCDHAFFSHELVPRNAEFRLEGSVLLTNRLFPATGINECIASSSRPRSKQVALEAVQHPVKLTSIGPHQPNGFHFVEDPQVDEPLLPDEVKIQIRAVGLDESDVEEMNRLIPGESAGSQGTGVVVEVGPAVHDIHVGDRVMALRTGHSGSLQTVLRTHSSAVTQVPEGLSLADAAAVPLPFTTAYHGLVNVARLEPQDTILIHNAGGATGQAAVQFACMLGATVYATVESDAQRQALLDYGVDRSRLLDGPSFAQQLARRGAKGSVDVLFNLSRESLEDRDLACLSQFGRLVGVHGQGSLPAGPTNRSYATVSIRELVQVRPKALHGTLRTISDLLTSRAIRPITPVRAGYSELQTVLSQIRQGNAGPWVLEPRANDTIPVAMKPLGDYQFDPCASYLLIGGFGGIGRSVVRWMLTRGAKNFIFLSRSGASSVPAKQLCADLLDAGCGVSDTVCDVTDATAVENALQQCGKSMPPIRGCLQCSMVLEDSMLSNMSHAQFLNAITPKVQGTIHVASALSSVKSNLDFFVLLSSSAGIIGNRGQANYSAANAFLDAFAAHLVSRGYPATSISLGSVLSVGWVAENQDRLPIALSYGAISEDLLLAILEYHMDPSWGAAQSPGTCHTVAGVRSARDFQRQSIPLPGFMAYPLFSPLRAIAGASQTAEEVAEAPIAQGLRGATSMEDAVELVTRAIVYKLARIMALSAKEIDAQRSLASYGVDSLVTVDLKAWFQREVGATVASGDLLGDSTIVQLAQQAAGGSRLVSVAMKGTE

Aspergillus carbonarius (strain ITEM 5010)

FUNCTION: Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of ochratoxin A (OTA), a mycotoxin composed of a chlorinated type I polyketide dihydroisocoumarin moiety linked to L-phenylalanine, and demonstrated to have nephrotoxic, immunotoxic, genotoxic, neurotoxic, and teratogenic properties (PubMed:24699234, PubMed:30054361). OtaA catalyzes the condensation of one acetate and 4 malonate units to form the isocoumarin group (PubMed:24699234). The pathway begins with the highly reducing polyketide synthase otaA that catalyzes the formation of the isocoumarin group during the initial stages of biosynthesis, starting from one acetate and 4 malonate units, to originate the characteristic pentaketide skeleton 7-methylmellein (7-MM) of the OTA molecule. The newly identified cyclase otaY might be involved in the polyketide cyclization reaction during the initial steps of the OTA biosynthesis. 7-MM is then oxidized into 7-carboxymellein (also called ochratoxin beta) by the cytochrome P450 monooxygenase otaC. The NRPS encoded by the otaB gene is involved in the linking of phenylalanine to the dihydroisocoumarin ring. The reaction catalyzed by NRPS results in the production of ochratoxin B (OTB), which is the non-chlorinated analog of OTA and which subsequently serves as the substrate of the halogenase otaD for chlorination activity to form the final molecular structure of OTA, containing a chlorine atom in the C-5 position of the molecule (Probable) (PubMed:33391201). {ECO:0000269|PubMed:24699234, ECO:0000269|PubMed:30054361, ECO:0000305|PubMed:33391201}.

2.3.1.-

CATALYTIC ACTIVITY: Reaction=acetyl-CoA + 9 H(+) + 4 malonyl-CoA + 5 NADPH = 7-methylmellein + 3 CO2 + 5 CoA + 4 H2O + 5 NADP(+); Xref=Rhea:RHEA:72767, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:192524; Evidence={ECO:0000305|PubMed:24699234}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72768; Evidence={ECO:0000305|PubMed:24699234};

COFACTOR: Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942; Evidence={ECO:0000255|PROSITE-ProRule:PRU00258};

PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:24699234, ECO:0000269|PubMed:30054361}.

Acyltransferase;Methyltransferase;Multifunctional enzyme;NADP;Oxidoreductase;Phosphopantetheine;Phosphoprotein;Reference proteome;S-adenosyl-L-methionine;Transferase

fatty acid biosynthetic process [GO:0006633]; methylation [GO:0032259]; ochratoxin A biosynthetic process [GO:1900818]

3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315]; fatty acid synthase activity [GO:0004312]; methyltransferase activity [GO:0008168]; oxidoreductase activity [GO:0016491]; phosphopantetheine binding [GO:0031177]; polyketide synthase activity [GO:0016218]

DOMAIN: Multidomain protein; including a ketosynthase (KS) that catalyzes repeated decarboxylative condensation to elongate the polyketide backbone; a malonyl-CoA:ACP transacylase (MAT) that selects and transfers the extender unit malonyl-CoA; a dehydratase (DH) domain that reduces hydroxyl groups to enoyl groups; a methyltransferase (CMeT) domain responsible for the incorporation of methyl groups; an enoylreductase (ER) domain that reduces enoyl groups to alkyl group; a ketoreductase (KR) domain that catalyzes beta-ketoreduction steps; and an acyl-carrier protein (ACP) that serves as the tether of the growing and completed polyketide via its phosphopantetheinyl arm. {ECO:0000305|PubMed:24699234}.

IPR001227;IPR036736;IPR014043;IPR016035;IPR013154;IPR011032;IPR018201;IPR014031;IPR014030;IPR016036;IPR013217;IPR036291;IPR032821;IPR020841;IPR042104;IPR020807;IPR049551;IPR049552;IPR020843;IPR013968;IPR049900;IPR020806;IPR009081;IPR029063;IPR016039;

3.30.70.3290;3.40.47.10;1.10.1200.10;3.40.366.10;3.90.180.10;3.40.50.720;3.10.129.110;3.40.50.150;

A0A1S3XSG2

MATTKQKVTAPSSSTAPCCPSTSILRREATAAVAGVGDGLQNWNNVPSVDDKQKKTASSALASLASTEPLSSNTSTKGIQIMTRAQTCHPLDPLSAAEISVAVATVRAAGETPEVRDGMRFIEVVLLEPDKSVVALADAYFFPPFQSSLMPRTKGGSLIPTKLPPRRARLIVYNKKTNETSIWIVELNEVHAAARGGHHRGKVISSNVVPDVQPPIDAQEYAECEAVVKSYPPFRDAMRRRGIDDLDLVMVDPWCVGYHSEADAPSRRLAKPLVFCRTESDCPMENGYARPVEGIYVLVDVQNMQIIEFEDRKLVPLPPADPLRNYTAGETRGGVDRSDVKPLHIIQPEGPSFRISGNYIEWQKWNFRIGFTPREGLVIHSVAYLDGSRGRRPIAHRLSFVEMVVPYGDPNDPHYRKNAFDAGEDGLGKNAHSLKRGCDCLGYIKYFDAHFTNFTGGVETTENCVCLHEEDHGMLWKHQDWRTGLAEVRRSRRLTVSFVCTVANYEYAFYWHFYQDGKIEAEVKLTGILSLGALQPGEYRKYGTTILPGLYAPVHQHFFVARMNMAVDCKPGEAHNQVVEVNVKVEEPGKENVHNNAFYAEETLLRSELQAMRDCDPFSARHWIVRNTRTVNRTGQLTGYKLVPGPNCLPLAGPEAKFLRRAAFLKHNLWVTQYAPGEEFPGGEFPNQNPRVGEGLASWVKQDRPLEESDIVLWYIFGITHVPRLEDWPVMPVEHIGFVLQPHGFFNCSPAVDVPPPSACDSESRDSDVTETSVAKSTATSLLAKL

Nicotiana tabacum (Common tobacco)

FUNCTION: Involved in putrescine catabolism in peroxisomes (PubMed:24287136). May also be involved in the biosynthesis of pyridine alkaloid natural products, leading mainly to the production of anabasine, anatabine, nicotine and nornicotine, effective deterrents against herbivores with antiparasitic and pesticide properties (neurotoxins); nornicotine serves as the precursor in the synthesis of the carcinogen compound N'-nitrosonornicotine (NNN) (PubMed:16656744). Oxidizes preferentially non-N-methylated amines (PubMed:24287136). {ECO:0000269|PubMed:16656744, ECO:0000269|PubMed:24287136}.

1.4.3.-; 1.4.3.21

CATALYTIC ACTIVITY: Reaction=a primary methyl amine + H2O + O2 = an aldehyde + H2O2 + NH4(+); Xref=Rhea:RHEA:16153, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17478, ChEBI:CHEBI:28938, ChEBI:CHEBI:228804; EC=1.4.3.21; Evidence={ECO:0000269|PubMed:24287136}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16154; Evidence={ECO:0000269|PubMed:24287136}; CATALYTIC ACTIVITY: Reaction=H2O + N-methylputrescine + O2 = 4-methylaminobutanal + H2O2 + NH4(+); Xref=Rhea:RHEA:71015, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:58039, ChEBI:CHEBI:190141; Evidence={ECO:0000250|UniProtKB:A0A1S4BDC4}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71016; Evidence={ECO:0000250|UniProtKB:A0A1S4BDC4};

COFACTOR: Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250|UniProtKB:P46883}; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P12807}; Note=Binds 1 copper ion per subunit (By similarity). Can also use zinc ion as cofactor (By similarity). {ECO:0000250|UniProtKB:P12807, ECO:0000250|UniProtKB:P46883}; COFACTOR: Name=L-topaquinone; Xref=ChEBI:CHEBI:79027; Evidence={ECO:0000250|UniProtKB:P46883}; Note=Contains 1 topaquinone per subunit. {ECO:0000250|UniProtKB:P46883};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=163 uM for putrescine {ECO:0000269|PubMed:24287136}; KM=478 uM for N-methylputrescine {ECO:0000269|PubMed:24287136}; KM=492 uM for cadaverine {ECO:0000269|PubMed:24287136}; Vmax=561 pmol/sec/mg enzyme with putrescine as substrate {ECO:0000269|PubMed:24287136}; Vmax=928 pmol/sec/mg enzyme with N-methylputrescine as substrate {ECO:0000269|PubMed:24287136}; Vmax=840 pmol/sec/mg enzyme with cadaverine as substrate {ECO:0000269|PubMed:24287136};

PATHWAY: Alkaloid biosynthesis; nicotine biosynthesis. {ECO:0000269|PubMed:16656744}.; PATHWAY: Amine and polyamine degradation; putrescine degradation. {ECO:0000269|PubMed:24287136}.

Alkaloid metabolism;Copper;Disulfide bond;Manganese;Metal-binding;Oxidoreductase;Peroxisome;Reference proteome;TPQ

alkaloid metabolic process [GO:0009820]; amine metabolic process [GO:0009308]; nicotine biosynthetic process [GO:0042179]; putrescine catabolic process [GO:0009447]

peroxisome [GO:0005777]

aliphatic amine oxidase activity [GO:0052595]; copper ion binding [GO:0005507]; primary amine oxidase activity [GO:0008131]; putrescine oxidase activity [GO:0050232]; quinone binding [GO:0048038]

SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:24287136}.

PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue. {ECO:0000250|UniProtKB:P46883}.

IPR000269;IPR015798;IPR036460;IPR016182;IPR015800;IPR015802;

3.10.450.40;2.70.98.20;

A0A1S3YCW2

MPALGCCVDAAVSPPPGYSFLWDSSLPAPEIFPSGVPPSTNTAVATTTTTHWSPAHSSALYSIDGWGAPYFTVNSSGDISVKPHGTDTLPHQEIDLLKVVKKASDPKNLGGLGLQFPLVVRFPDILKNRLESLQSVFDYAVQSQGYEAHYQGVYPVKCNQDRFVVEDIVKFGSGFRFGLEAGSKPELLLAMSCLCKGSHEGLLVCNGFKDAEYISLALVARKLMLNTVIVLEQEEELDLVIDISKKMAVRPVIGLRAKLRTKHSGHFGSTSGEKGKFGLTTTQIVRVVKKLEESGMLDCLQLLHFHIGSQIPSTALLADGVGEAAQIYCELVRLGAGMKYIDCGGGLGIDYDGTKSCDSDCSVGYGLQEYASTVVQAVRFVCDRKNVKHPVICSESGRAIVSHHSVLIFEAVSSTTTRSQELSSVDLQSFVEKLNDDARADYRNLSAAAIRGEYDTCVLYADQLKQRCVEQFKDGDLDIEQLAAVDGICDFVSKAIGASDPVRTYHVNLSIFTSVPDFWAIDQLFPIVPIHKLDERPVVRGILSDLTCDSDGKIDKFIGGESSLPLHELGSNGGGGGDGGKYYLGMFLGGAYEEALGGLHNLFGGPSVLRVSQSDSPHSFAVTCAVPGPSCADVLRAMQHEPELMFETLKHRAEEFVHNDDEQEEDKGLAFASLASSLAQSFNNMPYLVTNSSCCLTAAANNGGYYYCNDENIVGVGAESAAAEEELWPYCVA

Nicotiana tabacum (Common tobacco)

FUNCTION: Involved in the biosynthesis of pyridine alkaloid natural products, leading mainly to the production of anabasine, anatabine, nicotine and nornicotine, effective deterrents against herbivores with antiparasitic and pesticide properties (neurotoxins); nornicotine serves as the precursor in the synthesis of the carcinogen compound N'-nitrosonornicotine (NNN) (PubMed:32242247). Required for the biosynthesis of putrescine (By similarity). Catalyzes the first step of polyamine (PA) biosynthesis to produce putrescine from arginine (By similarity). {ECO:0000250|UniProtKB:Q9SI64, ECO:0000269|PubMed:32242247}.

4.1.1.19

CATALYTIC ACTIVITY: Reaction=H(+) + L-arginine = agmatine + CO2; Xref=Rhea:RHEA:17641, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:32682, ChEBI:CHEBI:58145; EC=4.1.1.19; Evidence={ECO:0000250|UniProtKB:Q9SI64};

COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P21170}; COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250|UniProtKB:P11926};

PATHWAY: Alkaloid biosynthesis; nicotine biosynthesis. {ECO:0000269|PubMed:32242247}.; PATHWAY: Amine and polyamine biosynthesis; agmatine biosynthesis; agmatine from L-arginine: step 1/1. {ECO:0000250|UniProtKB:Q9SI64}.

Alkaloid metabolism;Chloroplast;Decarboxylase;Lyase;Magnesium;Plastid;Pyridoxal phosphate;Reference proteome;Spermidine biosynthesis;Transit peptide

alkaloid metabolic process [GO:0009820]; arginine catabolic process [GO:0006527]; nicotine biosynthetic process [GO:0042179]; spermidine biosynthetic process [GO:0008295]

chloroplast [GO:0009507]

arginine decarboxylase activity [GO:0008792]

SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.

IPR009006;IPR002985;IPR022657;IPR022644;IPR022653;IPR000183;IPR029066;

1.20.58.930;3.20.20.10;

A0A1S3Z5Y0

MDGSGQQTDTMMSDAGAEQPPPAPQPVAGMDNIPATLSYGGRFIQYNIFGNIFEVTAKYKPPILPIGKGAYGIVCSALNSETIENVAIKKIANAFDNKIDAKRTLREIKLLRHMDHENIVAIRDIIPPPQREAFNDVYIAYELMDTDLHQIIRSNQGLSEEHCQYFLYQILRGLKYIHSANVLHRDLKPSNLLLNANCDLKICDFGLARVTSETDFMTEYVVTRWYRPPELLLNSSDYTAAIDIWSVGCIFTELMDRKPLFPGRDHVHQLRLIMELIGTPSEAEMEFLNENAKRYIRQLPLYRRQSFTEKFPHVHPAAIDLVEKMLTFDPRRRITVEGALAHPYLNSLHDISDEPICMTPFSFDFEQHALTEEQMKELIYRESLAFNPEYQHM

Nicotiana tabacum (Common tobacco)

FUNCTION: Phosphorylates myelin basic protein (MBP) in vitro (PubMed:9618567). May be involved in disease resistance (Probable). {ECO:0000269|PubMed:9618567, ECO:0000305|PubMed:9618567}.

2.7.12.2

CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.12.2; Evidence={ECO:0000305|PubMed:9618567}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10597; Evidence={ECO:0000305|PubMed:9618567}; CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.12.2; Evidence={ECO:0000305|PubMed:9618567}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990; Evidence={ECO:0000305|PubMed:9618567}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.12.2; Evidence={ECO:0000305|PubMed:9618567}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609; Evidence={ECO:0000305|PubMed:9618567};

ATP-binding;Kinase;Nucleotide-binding;Plant defense;Reference proteome;Serine/threonine-protein kinase;Transferase

defense response [GO:0006952]; intracellular signal transduction [GO:0035556]; phosphorylation [GO:0016310]

cytoplasm [GO:0005737]; nucleus [GO:0005634]

ATP binding [GO:0005524]; MAP kinase activity [GO:0004707]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein tyrosine kinase activity [GO:0004713]

IPR011009;IPR003527;IPR000719;IPR017441;IPR008271;

1.10.510.10;

A0A1S4AUX8

MAGQTIIVSGLNPAAILQSTIGGGASPTAAAAENGTRKVIPLSRDALQDFMLSIITQKLQDEKQPFYVLDLGEVVSLIDQWKSALPNIRPFYAVKCNPEPSFLSILSAMGSNFDCASRAEIEYVLSLGISPDRIVFANPCKPESDIIFAAKVGVNLTTYDSEDEVYKIRKHHPKSELLLRIKPMFDGNARCPMGPKYGALPEEVEPLLRAAQAARLTVSGVSFHIGSGDADSNAYLGAIAAAKEVFETAAKLGMSKMTVLDVGGGFTSGHQFTTAAVAVRSALKQHFDDQPELTIIAEPGRFFAETAFTLATTIIGKRVRGELREYWINDGLYGSMNCVLYDHATVNATPLAVLSNRTNVTCGGSKTFPTTVFGPTCDALDTVLRDYQLPELQVNDWLVFPNMGAYTKAAGSNFNGFNTSAIVTHLAYAYPS

Nicotiana tabacum (Common tobacco)

FUNCTION: Involved in the biosynthesis of pyridine alkaloid natural products, leading mainly to the production of anabasine, anatabine, nicotine and nornicotine, effective deterrents against herbivores with antiparasitic and pesticide properties (neurotoxins); nornicotine serves as the precursor in the synthesis of the carcinogen compound N'-nitrosonornicotine (NNN) (PubMed:27126795, PubMed:32242247). Catalyzes the first and rate-limiting step of polyamine biosynthesis that converts ornithine into putrescine, which is the precursor for the polyamines, spermidine and spermine (By similarity). Polyamines are essential for cell proliferation and are implicated in cellular processes, ranging from DNA replication to apoptosis (By similarity). {ECO:0000250|UniProtKB:P11926, ECO:0000269|PubMed:27126795, ECO:0000269|PubMed:32242247}.

4.1.1.17

CATALYTIC ACTIVITY: Reaction=H(+) + L-ornithine = CO2 + putrescine; Xref=Rhea:RHEA:22964, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:46911, ChEBI:CHEBI:326268; EC=4.1.1.17; Evidence={ECO:0000250|UniProtKB:P11926};

COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250|UniProtKB:P11926};

PATHWAY: Alkaloid biosynthesis; nicotine biosynthesis. {ECO:0000269|PubMed:32242247}.; PATHWAY: Amine and polyamine biosynthesis; putrescine biosynthesis via L-ornithine pathway; putrescine from L-ornithine: step 1/1. {ECO:0000250|UniProtKB:O22616}.

Alkaloid metabolism;Chloroplast;Lyase;Plastid;Pyridoxal phosphate;Reference proteome;Transit peptide

alkaloid metabolic process [GO:0009820]; nicotine biosynthetic process [GO:0042179]; polyamine biosynthetic process [GO:0006596]; putrescine biosynthetic process from ornithine [GO:0033387]; response to wounding [GO:0009611]; tyramine biosynthetic process [GO:1901695]

chloroplast [GO:0009507]; cytoplasm [GO:0005737]

ornithine decarboxylase activity [GO:0004586]

SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.

IPR009006;IPR022643;IPR022657;IPR022644;IPR022653;IPR000183;IPR002433;IPR029066;

3.20.20.10;

A0A1S4BDC4

MATTKQKVTAPSPSPSSSTASCCPSTSILRREATAAIAVVGDGLQNWTNIPSVDEKQKKTASSALASLPTTEPLSTNTSTKGIQIMTRAQTCHPLDPLSAAEISVAVATVRAAGETPEVRDGMRFIEVVLVEPDKSVVALADAYFFPPFQSSLMPRTKGGSQIPTKLPPRRARLIVYNKKTNETSIWIVELNEVHAAARGGHHRGKVIASNVVPDVQPPIDAQEYAECEAVVKSYPPFRDAMRRRGIDDLDLVMVDPWCVGYHSEADAPSRRLAKPLVFCRTESDCPMENGYARPVEGIYVLVDVQNMQIIEFEDRKLVPLPPVDPLRNYTAGETRGGVDRSDVKPLHIIQPEGPSFRISGNYVEWQKWNFRIGFTPREGLVIHSVAYLDGSRGRRPIAHRLSFVEMVVPYGDPNDPHYRKNAFDAGEDGLGKNAHSLKRGCDCLGYIKYFDAHFTNFTGGVETTENCVCLHEEDHGMLWKHQDWRTGLAEVRRSRRLTVSFVCTVANYEYAFYWHFYQDGKIEAEVKLTGILSLGALQPGEYRKYGTTILPGLYAPVHQHFFVARMNMAVDCKPGEAHNQVVEVNVKVEEPGKENVHNNAFYAEETLLRSELQAMRDCDPFSARHWIVRNTRTVNRTGQLTGYKLVPGPNCLPLAGPEAKFLRRAAFLKHNLWVTQYAPGEDFPGGEFPNQNPRVGEGLASWVKQDRPLEESDIVLWYIFGITHVPRLEDWPVMPVEHIGFVLQPHGYFNCSPAVDVPPPFACDSESRDSDVTETSVAKSTATSLLAKL

Nicotiana tabacum (Common tobacco)

FUNCTION: Involved in the biosynthesis of pyridine alkaloid natural products, leading mainly to the production of anabasine, anatabine, nicotine and nornicotine, effective deterrents against herbivores with antiparasitic and pesticide properties (neurotoxins); nornicotine serves as the precursor in the synthesis of the carcinogen compound N'-nitrosonornicotine (NNN) (PubMed:16656744, PubMed:17174363, PubMed:17283012). Amine oxidase which mediates the deamination of N-methylputrescine to produce 4-methylaminobutanal (PubMed:17174363, PubMed:17283012). Oxidizes preferentially N-methylated amines (PubMed:24287136). {ECO:0000269|PubMed:16656744, ECO:0000269|PubMed:17174363, ECO:0000269|PubMed:17283012, ECO:0000269|PubMed:24287136}.

1.4.3.-; 1.4.3.21

CATALYTIC ACTIVITY: Reaction=a primary methyl amine + H2O + O2 = an aldehyde + H2O2 + NH4(+); Xref=Rhea:RHEA:16153, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17478, ChEBI:CHEBI:28938, ChEBI:CHEBI:228804; EC=1.4.3.21; Evidence={ECO:0000269|PubMed:17174363, ECO:0000269|PubMed:17283012, ECO:0000269|PubMed:24287136}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16154; Evidence={ECO:0000269|PubMed:17174363, ECO:0000269|PubMed:17283012, ECO:0000269|PubMed:24287136}; CATALYTIC ACTIVITY: Reaction=H2O + N-methylputrescine + O2 = 4-methylaminobutanal + H2O2 + NH4(+); Xref=Rhea:RHEA:71015, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:58039, ChEBI:CHEBI:190141; Evidence={ECO:0000269|PubMed:17174363, ECO:0000269|PubMed:17283012, ECO:0000269|PubMed:24287136}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71016; Evidence={ECO:0000269|PubMed:17174363, ECO:0000269|PubMed:17283012, ECO:0000269|PubMed:24287136};

COFACTOR: Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250|UniProtKB:P46883}; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P12807}; Note=Binds 1 copper ion per subunit (By similarity). Can also use zinc ion as cofactor (By similarity). {ECO:0000250|UniProtKB:P12807, ECO:0000250|UniProtKB:P46883}; COFACTOR: Name=L-topaquinone; Xref=ChEBI:CHEBI:79027; Evidence={ECO:0000250|UniProtKB:P46883}; Note=Contains 1 topaquinone per subunit. {ECO:0000250|UniProtKB:P46883};

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=309 uM for putrescine {ECO:0000269|PubMed:24287136}; KM=57 uM for N-methylputrescine {ECO:0000269|PubMed:24287136}; KM=215 uM for cadaverine {ECO:0000269|PubMed:24287136}; KM=0.19 mM for N-methylputrescine {ECO:0000269|PubMed:17174363}; KM=0.76 mM for putrescine {ECO:0000269|PubMed:17174363}; KM=1.79 mM for cadaverine {ECO:0000269|PubMed:17174363}; KM=0.35 mM for 1,3-diaminopropane {ECO:0000269|PubMed:17174363}; KM=36 uM for N-methylputrescine {ECO:0000269|PubMed:17283012}; KM=247 uM for putrescine {ECO:0000269|PubMed:17283012}; KM=362 uM for cadaverine {ECO:0000269|PubMed:17283012}; KM=158 uM for 1,3-diaminopropane {ECO:0000269|PubMed:17283012}; KM=96 uM for N-methyl-1,3-diaminopropane {ECO:0000269|PubMed:17283012}; KM=249 uM for n-butylamine {ECO:0000269|PubMed:17283012}; Vmax=28.8 nmol/sec/mg enzyme with N-methylputrescine as substrate {ECO:0000269|PubMed:17174363}; Vmax=11.1 nmol/sec/mg enzyme with putrescine as substrate {ECO:0000269|PubMed:17174363}; Vmax=5.2 nmol/sec/mg enzyme with cadaverine as substrate {ECO:0000269|PubMed:17174363}; Vmax=11.3 nmol/sec/mg enzyme with 1,3-diaminopropane as substrate {ECO:0000269|PubMed:17174363}; Vmax=926 pmol/sec/mg enzyme with N-methylputrescine as substrate {ECO:0000269|PubMed:17283012}; Vmax=902 pmol/sec/mg enzyme with putrescine as substrate {ECO:0000269|PubMed:17283012}; Vmax=715 pmol/sec/mg enzyme with cadaverine as substrate {ECO:0000269|PubMed:17283012}; Vmax=666 pmol/sec/mg enzyme with 1,3-diaminopropane as substrate {ECO:0000269|PubMed:17283012}; Vmax=1270 pmol/sec/mg enzyme with N-methyl-1,3-diaminopropane as substrate {ECO:0000269|PubMed:17283012}; Vmax=862 pmol/sec/mg enzyme with n-butylamine as substrate {ECO:0000269|PubMed:17283012}; Vmax=750 pmol/sec/mg enzyme with putrescine as substrate {ECO:0000269|PubMed:24287136}; Vmax=512 pmol/sec/mg enzyme with N-methylputrescine as substrate {ECO:0000269|PubMed:24287136}; Vmax=920 pmol/sec/mg enzyme with cadaverine as substrate {ECO:0000269|PubMed:24287136};

PATHWAY: Alkaloid biosynthesis; nicotine biosynthesis. {ECO:0000269|PubMed:16656744, ECO:0000269|PubMed:17174363, ECO:0000269|PubMed:17283012}.

Alkaloid metabolism;Copper;Disulfide bond;Manganese;Metal-binding;Oxidoreductase;Peroxisome;Reference proteome;TPQ

alkaloid metabolic process [GO:0009820]; amine metabolic process [GO:0009308]; nicotine biosynthetic process [GO:0042179]; response to auxin [GO:0009733]; response to jasmonic acid [GO:0009753]

peroxisome [GO:0005777]

aliphatic amine oxidase activity [GO:0052595]; copper ion binding [GO:0005507]; identical protein binding [GO:0042802]; methylputrescine oxidase activity [GO:0052599]; primary amine oxidase activity [GO:0008131]; protein homodimerization activity [GO:0042803]; quinone binding [GO:0048038]

SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:24287136}.

PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue. {ECO:0000250|UniProtKB:P46883}.

IPR000269;IPR015798;IPR036460;IPR016182;IPR015800;IPR015802;

3.10.450.40;2.70.98.20;

A0A1S4F020

MIPRIVVVLLSVLAVVTARRSYEGYKVYGIVPESPDEAEILYQIRQSNPDLDFWHLTKQPGDEARVLVAPKDQRSFLIKLIRHGLHYQEVISDVEGTLAPYNEPRTRGMSLDRDVSTSYLRHNEINEYLQTLSQKYPSLVSVEEAGTSYEGRSIKTITINKKPGNAVVFLDAGIHAREWIAPATALYAIEQLVEHSSENQEVLSNLTWVIMPVVNPDGYEFSHETDRFWRKTRKPTGKTCKGTDGNRNFDYHWGEVGASTQACADTFRGETAFSEPETRAVRDAVMKLKGSCKFYLSLHSYGNYILYPWGWTSKLPETWEAIDEVAQAGAEAIKQSTGSRYTVGSSTNVLYAAAGGSDDWAFAVAEVPISITMELPGGGNGGFNPPPSSIEKIVNESWVGIKAMALKVAQMF

Aedes aegypti (Yellowfever mosquito) (Culex aegypti)

FUNCTION: Carboxypeptidase that preferentially hydrolyzes arginine and lysine residues at the C-terminus (PubMed:34750241). During infection by dengue virus, may play a role in preventing viral packaging, maturation, and release from the midgut (PubMed:25521592). {ECO:0000269|PubMed:25521592, ECO:0000269|PubMed:34750241}.

3.4.17.2

CATALYTIC ACTIVITY: Reaction=Preferential release of a C-terminal lysine or arginine amino acid.; EC=3.4.17.2; Evidence={ECO:0000269|PubMed:34658092, ECO:0000269|PubMed:34750241};

COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P15086}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:34658092, ECO:0000269|PubMed:34750241};

3D-structure;Carboxypeptidase;Disulfide bond;Endoplasmic reticulum;Glycoprotein;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Signal;Zinc;Zymogen

proteolysis [GO:0006508]

endoplasmic reticulum [GO:0005783]; extracellular space [GO:0005615]

metallocarboxypeptidase activity [GO:0004181]; zinc ion binding [GO:0008270]

SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:25521592}.

IPR036990;IPR003146;IPR000834;

3.30.70.340;3.40.630.10;