ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
B7LQD7 | MSAIAPGMILFAYLCGSISSAILVCRLCGLPDPRTSGSGNPGATNVLRMGGKGAALAVLIFDVLKGMLPVWGAYELGVSPFWLGLIAIAACLGHIWPIFFGFKGGKGVATAFGAIAPIGWDLTGVMAGTWLLTVLLSGYSSLGAIVSALIAPFYVWWFKPQFTFPVSMLSCLILLRHHDNIQRLWRRQETKIWTKLKRKREKDPE | Function: Catalyzes the transfer of an acyl group from acyl-ACP to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme can also utilize acyl-CoA as fatty acyl donor, but not acyl-PO(4).
Catalytic Activity: an acyl-CoA + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-phosphate + CoA
Location Top... |
Q2S2H7 | MWSLTVILLISYFLGSIPGALWSSKALHGVDIRNHGSHNCGATNAFRVVGWQAGALATVVDFGKGFLAAGVVASVIRIDPIPSGLSLFGGDPFVVLGLLAGVGAVIGHMYPIFARFEGGKGVNTAAGMLFALTPLTMAITLAVFVAVLLSSRYVSLSSITAAVAFPTIVALRRFGFGADLDPSLLVFGGLLALSIVVAHRSNIQRLLNGTESQISSFEPAQGMLGRGEL | Function: Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
Catalytic Activity: an acyl phosphate + sn-glycerol 3-phosphate = a 1-acyl-sn-glyce... |
A8GJV0 | MSATALGMIIFAYLCGSISSAILVCRIARLPDPRENGSGNPGATNVLRIGGRVAAAAVLVFDILKGMLPVWLAYKLDVPPLYLGLTAIAACLGHIYPVFFHFRGGKGVATAFGAIAPIGWDLTGLMTGTWLLTVLLSGYSSLGAIISALIAPFYVWWFKPQFTFPVAMLSCLILMRHHDNIQRLWRGQEGKIWGVFRKKKNDAAEQEEKKEE | Function: Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
Catalytic Activity: an acyl phosphate + sn-glycerol 3-phosphate = a 1-acyl-sn-glyce... |
Q940Q1 | MAVLPTWLLAMMCLLFFVGAMENTTHDNISSLPRSDETEWNQHAVTNPDEVADEVLALTEMSVRNHTERRKLGYFTCGTGNPIDDCWRCDPNWHKNRKRLADCGIGFGRNAIGGRDGRFYVVTDPRDDNPVNPRPGTLRHAVIQDRPLWIVFKRDMVIQLKQELIVNSFKTIDGRGANVHIANGGCITIQFVTNVIVHGLHIHDCKPTGNAMVRSSETHFGWRTMADGDAISIFGSSHVWIDHNSLSHCADGLVDAVMGSTAITISNNHLTHHNEVMLLGHSDSYMRDKAMQVTIAYNHFGVGLIQRMPRCRHGYFHVVN... | Cofactor: Binds 1 Ca(2+) ion. Required for its activity.
Catalytic Activity: Eliminative cleavage of (1->4)-alpha-D-galacturonan to give oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at their non-reducing ends.
Sequence Mass (Da): 47771
Sequence Length: 431
Pathway: Glycan metabolism; pectin degradat... |
P81294 | MASPCLIAVLVFLCAIVSCYSDNPIDSCWRGDSNWDQNRMKLADCAVGFGSSTMGGKGGDFYTVTSTDDNPVNPTPGTLRYGATREKALWIIFSQNMNIKLKMPLYVAGHKTIDGRGADVHLGNGGPCLFMRKVSHVILHSLHIHGCNTSVLGDVLVSESIGVEPVHAQDGDAITMRNVTNAWIDHNSLSDCSDGLIDVTLGSTGITISNNHFFNHHKVMLLGHDDTYDDDKSMKVTVAFNQFGPNAGQRMPRARYGLVHVANNNYDPWNIYAIGGSSNPTILSEGNSFTAPSESYKKEVTKRIGCESPSACANWVWRST... | Cofactor: Binds 1 Ca(2+) ion.
Function: Has low pectate lyase activity.
PTM: N-glycosylated; consists of complex-type N-glycans containing the Lewis a antigen (Galbeta1-3(Fucalpha1-4)GlcNAcbeta1-).
Catalytic Activity: Eliminative cleavage of (1->4)-alpha-D-galacturonan to give oligosaccharides with 4-deoxy-alpha-D-gala... |
Q6CZT4 | MKYLLPSAAAGLLLLAAQPTMAANTGGYATTDGGDVSGAVKKTARSLQEIVDIIEAAKKDSSGKVVKGGAFPLVITYNGNEDALIKAAEANICGQWSKDPRGVEIKEFTKGITILGTNGSSANFGIWVVNSSNVVVRNMRFGYMPGGAKDGDAIRIDNSPNVWIDHNEIFAKNFECAGTPDNDTTFESAVDIKKASTNVTVSYNFIHGVKKVGLSGSSNTDTGRNLTYHHNIYSDVNSRLPLQRGGQVHAYNNLYDGIKSSGFNVRQKGIALIESNWFENALNPVTARNDDSNFGTWELRNNNITSPSDFAKYKITWGKP... | Cofactor: Binds 1 Ca(2+) ion per subunit.
Function: Involved in maceration and soft-rotting of plant tissue.
Catalytic Activity: Eliminative cleavage of (1->4)-alpha-D-galacturonan to give oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at their non-reducing ends.
Sequence Mass (Da): 40178
Sequence Len... |
Q93WF1 | MAVTQILVVFASALLLSMFFTGVDSTRSNETWHEHAVENPEEVAAMVDMSIRNSTARRRLGYFSCSTGNPIDDCWRCDRRWQSRRKHLANCAIGFGRNAIGGRDGRYYVVSDPNDDNPVNPKPGTLRHAVIQEEPLWIVFKRDMVITLKEELIMNSFKTIDGRGVNVHIANGACITIQFVTNIIIHGIHIHDCRPTGNAMVRSSPSHYGWRTMADGDGISIFGSSHIWIDHNSLSNCADGLIDAVMASTAITISNNYFTHHNEVMLLGHSDTYTRDKVMQVTIAYNHFGEGLIQRMPRCRHGYFHVVNNDYTHWEMYAIG... | Cofactor: Binds 1 Ca(2+) ion. Required for its activity.
Catalytic Activity: Eliminative cleavage of (1->4)-alpha-D-galacturonan to give oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at their non-reducing ends.
Sequence Mass (Da): 46728
Sequence Length: 417
Pathway: Glycan metabolism; pectin degradat... |
Q9FM66 | MSIVCTFFLFLLNTSFAFAFAIPKPPIVRRLSTTVTSNSTASSCSANGNPIDECWRCDENWKDNRKNLADCAVGFGRDSIGGRAGEFYTVTDSGDDNPLNPTPGTLRYAATQDQPLWIIFDRDMVIQLKQDLQVASYKTIDGRGNNVQIAYGPCLTLYKVSNIIINNLYIHDCVPVKRNALSSLGGYSDGDGISIFESRDIWIDHCTLEKCYDGLIDAVNGSTDITISNSYMLNHNEVMLLGHSDEYSGDRDMRVTIAFNYFGEGLVQRMPRCRHGYFHIVNNIYRDWKMYAIGGSANPTIFSQGNVFIASNNQFTKEVT... | Cofactor: Binds 1 Ca(2+) ion. Required for its activity.
Catalytic Activity: Eliminative cleavage of (1->4)-alpha-D-galacturonan to give oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at their non-reducing ends.
Sequence Mass (Da): 43682
Sequence Length: 392
Pathway: Glycan metabolism; pectin degradat... |
Q93Z25 | MFRPNSLLIPSNLSTTKSQRNTMLNSSYLSFALIFFCCILFSALASSLPVSDPELVVEEVHRKINESISRRKLGFFSCGSGNPIDDCWRCDKDWEKNRKRLADCGIGFGKNAIGGRDGEIYVVTDPGNDDPVNPRPGTLRYAVIQDEPLWIIFKRDMTIQLKEELIMNSFKTLDGRGASVHISGGPCITIQYVTNIIIHGLHIHDCKQGGNTYVRDSPEHYGYRTVSDGDGVSIFGGSHVWVDHCSLSNCNDGLIDAIRGSTAITISNNYLTHHNKVMLLGHSDTYEQDKNMQVTIAFNHFGEGLVQRMPRCRHGYFHVV... | Cofactor: Binds 1 Ca(2+) ion. Required for its activity.
Catalytic Activity: Eliminative cleavage of (1->4)-alpha-D-galacturonan to give oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at their non-reducing ends.
Sequence Mass (Da): 47895
Sequence Length: 432
Pathway: Glycan metabolism; pectin degradat... |
O65388 | MASLFLTIISLLFAAFSSSVVEAAYSNGYTIPKLLPNPIDSCWRRNPYWASNRRALADCAVGFGKSAVGGKYGSIYVVTNPSDDPENPRPGTLRYAVIQSKPLWITFARDMVIVLRNELIMNSYKTIDGRGAKVEIAYGPCITIQHVSHVIIHGISIHDCKPGKSGRVRSSPTHVGSRKGSDGDAIAIFDSSHIWIDHCFFSRCQDGLIDVLHASTAVTISNNYFTQHDKVMLLGHNDNNVEDKIMRVTIAFNHFGPGLIERMPRVRRGYAHVANNRYEKWQMYAIGGSADPTIFSEGNYFVASDDPSKKQVTKRIDSGY... | Cofactor: Binds 1 Ca(2+) ion. Required for its activity.
Catalytic Activity: Eliminative cleavage of (1->4)-alpha-D-galacturonan to give oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at their non-reducing ends.
Sequence Mass (Da): 42693
Sequence Length: 384
Pathway: Glycan metabolism; pectin degradat... |
Q9M9S2 | MAAAFLNLGGYVFVFFSSFLAIVAPQVRGNVAVFDSYWTQRQSDALKQTIGSYDPHPLNVTNHFNYHVNIAVDASESRNDTRRELTQVRSGRKTHKSSGKCLAYNPIDNCWRCDRNWANNRKKLADCVLGFGRRTTGGKDGPIYVVKDASDNDLINPKPGTLRHAVTRDGPLWIIFARSMIIKLQQELMITSDKTIDGRGARVYIMEGAGLTLQFVNNVIIHNIYVKHIVPGNGGLIRDSEAHIGLRTKSDGDGISLFGATNIWIDHVSMTRCADGMIDAIDGSTAVTISNSHFTDHQEVMLFGARDEHVIDKKMQITVA... | Cofactor: Binds 1 Ca(2+) ion. Required for its activity.
Catalytic Activity: Eliminative cleavage of (1->4)-alpha-D-galacturonan to give oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at their non-reducing ends.
Sequence Mass (Da): 51455
Sequence Length: 459
Pathway: Glycan metabolism; pectin degradat... |
P19456 | MSSLEDIKNETVDLEKIPIEEVFQQLKCSREGLTTQEGEDRIQIFGPNKLEEKKESKLLKFLGFMWNPLSWVMEMAAIMAIALANGDGRPPDWQDFVGIICLLVINSTISFIEENNAGNAAAALMAGLAPKTKVLRDGKWSEQEAAILVPGDIVSIKLGDIIPADARLLEGDPLKVDQSALTGESLPVTKHPGQEVFSGSTCKQGEIEAVVIATGVHTFFGKAAHLVDSTNQVGHFQKVLTAIGNFCICSIAIGMVIEIIVMYPIQRRKYRDGIDNLLVLLIGGIPIAMPTVLSVTMAIGSHRLSQQGAITKRMTAIEEM... | Function: The plasma membrane H(+) ATPase of plants and fungi generates a proton gradient that drives the active transport of nutrients by H(+)-symport . The resulting external acidification and/or internal alkinization may mediate growth responses . Involved in maintaining the membrane potential and delta-pH, together... |
P19657 | MSSTEAKQYKEKPSKEYLHASDGDDPANNSAASSSSSSSTSTSASSSAAAVPRKAAAASAADDSDSDEDIDQLIDELQSNYGEGDESGEEEVRTDGVHAGQRVVPEKDLSTDPAYGLTSDEVARRRKKYGLNQMAEENESLIVKFLMFFVGPIQFVMEAAAILAAGLSDWVDVGVICALLLLNASVGFIQEFQAGSIVDELKKTLANTATVIRDGQLIEIPANEVVPGEILQLESGTIAPADGRIVTEDCFLQIDQSAITGESLAAEKHYGDEVFSSSTVKTGEAFMVVTATGDNTFVGRAAALVGQASGVEGHFTEVLN... | Function: The plasma membrane ATPase of plants and fungi is a hydrogen ion pump. The proton gradient it generates drives the active transport of nutrients by H(+)-symport. The resulting external acidification and/or internal alkinization may mediate growth responses.
Catalytic Activity: ATP + H(+)(in) + H2O = ADP + 2 H... |
P20431 | MASGLEDIVNENVDLEKIPIEEVFQQLKCSREGLSGAEGENRLQIFGPNKLEEKKESKLLKFLGFMWNPLSWVMEAAAIMAIALANGGGKPPDWQDFVGIVCLLVINSTISFVEENNAGNAAAALMAGLAPKTKVLRDGKWSEQEASILVPGDIVSIKLGDIIPADARLLEGDPLKVDQSALTGESLPATKGPGEEVFSGSTCKQGEIEAVVIATGVHTFFGKAAHLVDSTNQVGHFQKVLTAIGNFCICSIAVGIAIEIVVMYPIQRRHYRDGIDNLLVLLIGGIPIAMPTVLSVTMAIGSHKLSQQGAITKRMTAIEE... | Function: The plasma membrane H(+) ATPase of plants and fungi generates a proton gradient that drives the active transport of nutrients by H(+)-symport. The resulting external acidification and/or internal alkinization may mediate growth responses.
PTM: Phosphorylation level varies significantly during early response t... |
Q03194 | MAKAISLEEIKNETVDLEKIPIEEVFEQLKCTREGLSADEGASRLQIFGPNKLEEKNESKILKFLGFMWNPLSWVMEAAAVMAIALANGDGKPPDWQDFIGIICLLVINSTISFIEENNAGNAAAALMAGLAPKTKVLRDGRWSEQEAAILVPGDIISVKLGDIIPADARLLEGDPLKIDQSALTGESLPVTKNPGDEVFSGSTCKQGELEAVVIATGVHTFFGKAAHLVDSTNNVGHFQKVLTAIGNFCICSIAIGMLVEIIVMYPIQHRKYRDGIDNLLVLLIGGIPIAMPTVLSVTMAIGSHRLSQQGAITKRMTAI... | Function: The plasma membrane ATPase of plants and fungi is a hydrogen ion pump. The proton gradient it generates drives the active transport of nutrients by H(+)-symport. The resulting external acidification and/or internal alkinization may mediate growth responses.
Catalytic Activity: ATP + H(+)(in) + H2O = ADP + 2 H... |
Q9SJB3 | MSELDHIKNESVDLVRIPMEEVFEELKCTKQGLTANEASHRLDVFGPNKLEEKKESKLLKFLGFMWNPLSWVMEVAALMAIALANGGGRPPDWQDFVGIVCLLLINSTISFIEENNAGNAAAALMAGLAPKTKVLRDNQWSEQEASILVPGDVISIKLGDIIPADARLLDGDPLKIDQSSLTGESIPVTKNPSDEVFSGSICKQGEIEAIVIATGVHTFFGKAAHLVDNTNQIGHFQKVLTSIGNFCICSIALGIIVELLVMYPIQRRRYRDGIDNLLVLLIGGIPIAMPSVLSVTMATGSHRLFQQGAITKRMTAIEEM... | Function: The plasma membrane H(+) ATPase of plants and fungi generates a proton gradient that drives the active transport of nutrients by H(+)-symport. The resulting external acidification and/or internal alkinization may mediate growth responses (By similarity).
Catalytic Activity: ATP + H(+)(in) + H2O = ADP + 2 H(+)... |
Q9LY32 | MTDIEALKAITTESIDLENVPVEEVFQHLKCTKEGLTSNEVQERLTLFGYNKLEEKKESKILKFLGFMWNPLSWVMEAAALMAIGLAHGGGKPADYHDFVGIVVLLLINSTISFVEENNAGNAAAALMAQLAPKAKAVRDGKWNEIDAAELVPGDIVSIKLGDIIPADARLLEGDPLKIDQATLTGESLPVTKNPGASVYSGSTCKQGEIEAVVIATGVHTFFGKAAHLVDSTTHVGHFQKVLTAIGNFCICSIAVGMAIEIVVIYGLQKRGYRVGIDNLLVLLIGGIPIAMPTVLSVTMAIGAHRLAQQGAITKRMTAI... | Function: The plasma membrane H(+) ATPase of plants and fungi generates a proton gradient that drives the active transport of nutrients by H(+)-symport. The resulting external acidification and/or internal alkinization may mediate growth responses (By similarity).
Catalytic Activity: ATP + H(+)(in) + H2O = ADP + 2 H(+)... |
Q9M2A0 | MATEFSWDEIKKENVDLERIPVEEVFEQLKCSKEGLSSDEGAKRLEIFGANKLEEKSENKFLKFLGFMWNPLSWVMESAAIMAIVLANGGGKAPDWQDFIGIMVLLIINSTISFIEENNAGNAAAALMANLAPKTKVLRDGKWGEQEASILVPGDLISIKLGDIVPADARLLEGDPLKIDQSALTGESLPTTKHPGDEVFSGSTCKQGEIEAVVIATGVHTFFGKAAHLVDSTNNVGHFQKVLTSIGNFCICSIGLGMLIEILIMYPIQHRTYRDGIDNLLVLLIGGIPIAMPTVLSVTMAIGSHRLSQQGAITKRMTAI... | Function: The plasma membrane H(+) ATPase of plants and fungi generates a proton gradient that drives the active transport of nutrients by H(+)-symport. The resulting external acidification and/or internal alkinization may mediate growth responses (By similarity).
Catalytic Activity: ATP + H(+)(in) + H2O = ADP + 2 H(+)... |
Q940Z5 | MVNEEMESSLKVIDVARVTPSNSDSSESLTLPLTFFDLLWYKLHAVERVIFYKLTDASRPFFDSVIVPNLKTSLSSSLSHYLPLAGKLVWEPLDPKPKIVYTPNDAVSFTVAESNADFSRLTGKEPFPTTELYPLVPELHVSDDSASAVSFQVTLFPNQGFCISVNAHHAVLDGKTTTNFLKSWARTCKNQDSFLPQDLIPVYDRTVIKDPMDLDTKILNAWHRVAKVFTGGKEPENPKSLKLLWSPEIGPDVFRYTLNLTREDIQKLRERLKKESSSSSVSSSPKELRLSTFVIVYSYALTCLIKARGGDPSRPVGYGF... | Function: Malonyltransferase acting on xenobiotic glucosides. Has activity toward 2-Naphthol glucoside (2NAG), 1-Naphthol glucoside (1NAG), kaempferol 7-O-glucoside, kaempferol 3-O-glucoside, hydroxycoumarin glucosides, phenol-glucosides and isoflavone glucoside (daidzin), but not toward 4-coumaroyl glucoside, kaempfer... |
Q9LRQ8 | MTLHVIETARVTPTDYSVINSANLHKLPLTFFDLPWLLFQPVKRVFFYELTESTRDHFHSIILPKLKDSLSLILRNYLPLTGHITWEPNEPKPSIIVSENGVVLVTIAESDADFSHLSGYGQRPLSELHALVPKLPVSDDSATAFSIQITLFPNQGFSIGVAAHHAVLDGKTSSTFIKAWAQICKQELQSMPENLTPSYDRSLIKYPTYLDEKMIELVRSLKEDQTNIRSLTSLPSSKLGDDVVLATLVLSRADIERLREQVKNVSPSLHLSTFVIAYAYAWTCFVKARGGNKDRSVSLLFVGDFRDRLDPKLPGTYFGN... | Function: Malonyltransferase acting on xenobiotic glucosides. Has activity toward 2-Naphthol glucoside (2NAG), 1-Naphthol glucoside (1NAG), kaempferol 7-O-glucoside, hydroxycoumarin glucosides and phenol-glucosides, but not toward kaempferol 3-O-glucoside or daidzin. Prefers phenol glucosides rather than naphtol glucos... |
Q7M290 | WGEQEASILVPGDIVSIKLGDIVPADARIDQSGLTGESLPVTKNPGDEVFSGSTCKTGTLTLNKGIVGMTGDGVNDAPALKTLHGLQAPESTSLNLPNDKELSEIAEQAK | Function: The plasma membrane ATPase of plants and fungi is a hydrogen ion pump. The proton gradient it generates drives the active transport of nutrients by H(+)-symport. The resulting external acidification and/or internal alkinization may mediate growth responses (By similarity).
PTM: The N-terminus is blocked.
Loca... |
A7E7L8 | MLKAVMPRPWVCSRCVKRQIQSSRGLATASTQYREPRPVPTDHSAPGAKHDDRTLRQIFDSPDFWADFSQSSKQSYYRPGVGLFQNRYLVNPQGFEVFANTSLRKAQRIVDKVLKASTVEEYRHVARDLDRLSDLLCRVIDLSDFVRATHPNAAIQAAASRAYAKMFEYMNILNTTTGLDKQLEVAMGTPEIVAGWTEEEVVVADILKKDFAKSAIDLPRAQREKFVALSQEISEIGPDFVDYMTPAKSYLTFESSKLKGMDPVLVREHTTWGQTKIPTIGGAAAAAIRTVQNEEVRREIFMATRTASRNTVHKLEELMR... | Cofactor: Binds 1 zinc ion.
Function: Cleaves proteins, imported into the mitochondrion, to their mature size. While most mitochondrial precursor proteins are processed to the mature form in one step by mitochondrial processing peptidase (MPP), the sequential cleavage by MIP of an octapeptide after initial processing b... |
Q4PBS8 | MASTSKNAQRAAASVAHSYHVCLARRMSRLPTLLSNISAPAASKALDRYESKRIHSRSFSSSLAAQRVQRPTSAGPILTNPISDHEKDNDELRSLFDAPPTSSSANHLRSSGPSTGLFEIPSLTSPQNFLVLAQQTLARAQLLVDRIDRAGSADASTAQGIKELKEVVRNLDRLSDLLCGVIDMAELVRNAHPDPEWAEAANAAYEYLCGYMNVLNTHTGLYSVLKNILSIKEVAETLSKEATAVAQVFLRDFEKSGIHLPPAERERFVQLSDEILVLGRGFLQDIAGNDASDDFARIASAQADADKSDMVGLPTHWLED... | Cofactor: Binds 1 zinc ion.
Function: Cleaves proteins, imported into the mitochondrion, to their mature size. While most mitochondrial precursor proteins are processed to the mature form in one step by mitochondrial processing peptidase (MPP), the sequential cleavage by MIP of an octapeptide after initial processing b... |
Q6CHD6 | MRRFSTLSRRLQRVVPASSASTANTSPSPALYTGLEPKIKESQDSLIRAVFDNGDVWQDFSQKSVAKPKQSRSITGFINYLTNESDYETGLFMNDFLKTPAGFQKYTAASIEEAGQLIQQLLGALTQRDKLRHAITTFDRLSDVLCQVIDLAEFIRAAHPEQHFVQAAQEAHEQMYEYMNVLNTSVELYTVLDMVFKDSEIVNQLTHEEKVVGTLLLEDFKKSGVTLDDAGRENFVSLTTKISLLGRDFISSNHPKEDYITLTQGEAQGLDPQLAQQLSQGNSVYVPTGGVPGQLALRGMKNENSRKLLWSKMRESSDKS... | Cofactor: Binds 1 zinc ion.
Function: Cleaves proteins, imported into the mitochondrion, to their mature size. While most mitochondrial precursor proteins are processed to the mature form in one step by mitochondrial processing peptidase (MPP), the sequential cleavage by MIP of an octapeptide after initial processing b... |
P35999 | MLRTIILKAGSNASIPSPSRQNKLLRFFATAGAVSRTSPGSIKKIFDDNSYWRNINGQDANNSKISQYLFKKNKTGLFKNPYLTSPDGLRKFSQVSLQQAQELLDKMRNDFSESGKLTYIMNLDRLSDTLCRVIDLCEFIRSTHPDDAFVRAAQDCHEQMFEFMNVLNTDVSLCNILKSVLNNPEVSSKLSAEELKVGKILLDDFEKSGIYMNPDVREKFIQLSQEISLVGQEFINHTDYPGSNSVKIPCKDLDNSKVSTFLLKQLNKDVKGQNYKVPTFGYAAYALLKSCENEMVRKKLWTALHSCSDKQVKRLSHLIK... | Cofactor: Binds 1 zinc ion.
Function: Cleaves proteins, imported into the mitochondrion, to their mature size. While most mitochondrial precursor proteins are processed to the mature form in one step by mitochondrial processing peptidase (MPP), the sequential cleavage by MIP of an octapeptide after initial processing b... |
A0A1W2PS18 | MALKPPSATQPAPNAPATPDAPPTTGDPGASAAPGSPTTTGGPGAPAEVPQEPQEPTQTPEELAFYAPNYLCLTIFAILLFPPFGLAALYFSYEGSWTQKPTSMLPPLQTMKANQNSEWEEAYINSGRTGWFGAFVVMIGLGIIYGLVLY | Function: May play a role in spermatozoa mobility.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 15819
Sequence Length: 150
Subcellular Location: Membrane
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Q8CES1 | MDTDEQGAPGRKPLDRPQTPDELKFYARNYVMLALLAMILFLPFGILAIYFSIQTNEANKCSNWEDAYRNSSRTMWFNMLAIVAFVGIIYILVLVL | Function: May play a role in spermatozoa mobility.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 11040
Sequence Length: 96
Subcellular Location: Membrane
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Q17446 | MFPQTTMDHILHPTPREGYYVVELNRSVWVVPNYYINLTPIGTGAYGTVCAAECTRSGTRVAIKKFNRPFQSIIHARRTYRELRLLRCMCHENIIDLLDVFTPNENVNDIEDVYFVSMLMGADLSNILKIQRLNDDHIQFLVYQILRGLKYIHSADIIHRDLKPSNIAVNEDCELKILDFGLARQTDSEMTGYVATRWYRAPEIMLNWMHYTQTVDVWSVGCILAELITGKTLFPGSDHIDQLTRIMSVTGTPDEEFLKKISSEEARNYIRNLPKMTRRDFKRLFAQATPQAIDLLEKMLHLDPDRRPTAKEAMEHEYLA... | Cofactor: Divalent cations such as magnesium or manganese.
Function: Serine/threonine kinase which responds to activation by environmental stress and pro-inflammatory cytokines by phosphorylating downstream targets . As part of a MAP kinase signaling pathway, plays a role in modulation of lifespan and immunity . Phosph... |
G4N0Z0 | MSRANPPSNSSGSRKISFNVSEQYDIQDVVGEGAYGVVCSAIHKPSGQKVAIKKITPFDHSMFCLRTLREMKLLRYFNHENIISILDIQKPRSYETFNEVYLIQELMETDMHRVIRTQDLSDDHCQYFIYQTLRALKAMHSANVLHRDLKPSNLLLNANCDLKVCDFGLARSAASQEDNSGFMTEYVATRWYRAPEIMLTFKEYTKAIDVWSVGCILAEMLSGKPLFPGKDYHHQLTLILDVLGTPTMEDYYGIKSRRAREYIRSLPFKKKVPFRTLFPKTSDLALDLLEKLLAFNPVKRITVEEALKHPYLEPYHDPDD... | Function: Mitogen-activated protein kinase; part of the MST11-MST7-PMK1 MAP kinase (MAPK) cascade that is essential for appressorium formation, penetration and invasive growth . Central regulator of appressorium development that acts downstream of the cAMP signal . The MST11-MST7-PMK1 MAP kinase cascade transduces sign... |
Q8MXI4 | MGMSATMGDSASIPGVFFADFGPAPPEITPEGYHEVELNKTKWVLPQWYNSLKPLGEGAYGVVCTAEYEPTGDRVAIKKFFRPFQSTIHAKRTYRELKLLRTLQHDNVLEMIDVFTPDPDASSLNNVYFVSVLMGSDLQNIMKIQRLTDEQIQLLIYQVLRGLKYIHSAGIIHRDLKPSNIAVNERCEVKVFLSFSQLSFLILSFFKILDFGLARAQDAEMTGYVATRWYRAPEIMLNWMHYTQTVDVWSVGCILAELVSGRPLFPGDDHIDQLTKIMSVVGTPKEEFWSKIQSEEARNYIKNRSPIIRQDFVTLFPMAS... | Function: Responds to activation by environmental stress and pro-inflammatory cytokines by phosphorylating downstream targets.
PTM: Dually phosphorylated on Thr-222 and Tyr-224, which activates the enzyme.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 48026
S... |
O44514 | MASVPSSSSLPVSHVRRHEDVSTPSAPPTKRSNNQSQPPESYEPNTWLQQQREQEQQKKLAAENIKKQSIEATGNNEMVGEEEEDILSKPCGPHKRRFQFVMIRNITFAIPEGYDVEPNSIEYLGGGSFGNVIKTSAVCRDGLRRYVAIKKMREPFFDPHHARRIFRETKLLQLMRHDNIICALDIYTPDEENDFRDVYVVTEFAGRSLYQILKQQRDYGRRVLTDEHIKFIIYQIIRALKYIHSANIIHRDLKPGNLALTDDSDLMILDFGLARSLEKKDTSLTQYVQTRWYRSPEVIYWKIDSYTNLADMWSLGCIAA... | Function: Responds to activation by environmental stress and pro-inflammatory cytokines by phosphorylating downstream targets . Involved in axon regeneration after injury, probably downstream of dlk-1 and mkk-4 and upstream of mak-2 . May phosphorylate mak-2 . Plays a role in cilium length regulation, possibly by reduc... |
Q9C6T1 | MAVVASAPGKVLMTGGYLVLEKPNAGLVLSTNARFYAIVKPINEEVKPESWAWKWTDVKLTSPQLSRESMYKLSLNHLTLQSVSASDSRNPFVEHAIQYAIAAAHLATEKDKESLHKLLLQGLDITILGSNDFYSYRNQIESAGLPLTPESLGTLAPFASITFNAAESNGANSKPEVAKTGLGSSAAMTTAVVAALLHYLGVVDLSDPCKEGKFGCSDLDVIHMIAQTSHCLAQGKVGSGFDVSCAVYGSQRYVRFSPEVLSFAQVAVTGLPLNEVIGTILKGKWDNKRTEFSLPPLMNLFLGEPGSGGSSTPSMVGAVK... | Catalytic Activity: (R)-5-phosphomevalonate + ATP = (R)-5-diphosphomevalonate + ADP
Sequence Mass (Da): 54409
Sequence Length: 505
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via mevalonate pathway; isopentenyl diphosphate from (R)-mevalonate: step 2/3.
Subcellular Location: Peroxisome
EC: 2.... |
Q97UL6 | MIKVSAPGKILWIGSYSVVFGGISHVIAVNKRVSCSLREIKEKDSLIFHTSYGHFKNSGNELINSVLDTFRERLSQLPQGYEIDLYNDKEFIIDGKKTGLGSSSAATVSLTACLYYAIHGKLDLFEIHKLAQIANYKRQKGIGSGFDIASAVFGSIVYKRFTDLDKMDFYFEKLNLGNYDMMLGFTGKSSETVGLVRKFVEKSNLDDFKEIMRLIDEENYMAIKLIKLNKLDEAVEHIKLGRKYLNYIAERIVGVKLVSKMEEELIKIAEEEGALVALSPGAGGGDSIFALGNDLNRVREAWSKRGIFIIDVKEDEGLRL... | Function: Catalyzes the phosphorylation of (R)-mevalonate 5-phosphate (MVAP) to (R)-mevalonate 5-diphosphate (MVAPP). Functions in the mevalonate (MVA) pathway leading to isopentenyl diphosphate (IPP), a key precursor for the biosynthesis of isoprenoid compounds such as archaeal membrane lipids.
Catalytic Activity: (R)... |
Q9KWG3 | MTTGQRTIVRHAPGKLFVAGEYAVVDPGNPAILVAVDRHISVTVSDADADTGAADVVISSDLGPQAVGWRWHDGRLVVRDPDDGQQARSALAHVVSAIETVGRLLGERGQKVPALTLSVSSRLHEDGRKFGLGSSGAVTVATVAAVAAFCGLELSTDERFRLAMLATAELDPKGSGGDLAASTWGGWIAYQAPDRAFVLDLARRVGVDRTLKAPWPGHSVRRLPAPKGLTLEVGWTGEPASTASLVSDLHRRTWRGSASHQRFVETTTDCVRSAVTALESGDDTSLLHEIRRARQELARLDDEVGLGIFTPKLTALCDAA... | Function: Catalyzes the phosphorylation of (R)-mevalonate 5-phosphate (MVAP) to (R)-mevalonate 5-diphosphate (MVAPP). Functions in the mevalonate (MVA) pathway leading to isopentenyl diphosphate (IPP), a key precursor for the biosynthesis of isoprenoid compounds.
Catalytic Activity: (R)-5-phosphomevalonate + ATP = (R)-... |
Q03760 | MEKDALEVRLKSIRHSLDKNTKLLPGKYRNTLGERLITKWRYKKKSHNGSSMLPEKCKSHVQLYDDLVQESSKHFVGFRLHDLRALLKRICSIQNYTRHVLIEWDVRWVNPLTLASKGWEPYQSASQSQVPFKCCCCHAIMTIPLLKNGDDVADYTMKLNEKIWNSNIIGNHLQKCPWRENQVDLNKEYYLSSQNLIREIERIHTEIDRIVSGSNEFSLKRNSSRIFHYLSEKEIQKLAFFFDCKDYSLVGLLLLGYTKFQKDDLVQCTACFHRASLKKLEYTEFNGHALWCRYYNKELLPTMLLELIGKEDKLITKLGV... | Function: Involved in the nuclear retention of improperly spliced pre-mRNAs.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 39207
Sequence Length: 334
Subcellular Location: Nucleus membrane
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Q9SD39 | MAFGRGRGNKRTSTSSYASTITMVIFVALCVFGVWMLSSNSVIPPQITQGSTRAAVAETERSDVSASSNGNDEPEPTKQESDEQQAFEDNPGKLPDDAVKSEDEQRKSAKEKSETTSSKTQTQETQQNNDDKISEEKEKDNGKENQTVQESEEGQMKKVVKEFEKEQKQQRDEDAGTQPKGTQGQEQGQGKEQPDVEQGNKQGQEQDSNTDVTFTDATKQEQPMETGQGETSETSKNEENGQPEEQNSGNEETGQQNEEKTTASEENGKGEKSMKDENGQQEEHTTAEEESGNKEEESTSKDENMEQQEERKDEKKHEQG... | Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 101444
Sequence Length: 895
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.1.1.-
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Q9LN50 | MMERKREMGIAYFARRIKQPRGIWVKMTFIVVLGLCFVFFWSFLSSSASTFNVQRESFDDIAEPVSSRTKSAHEVSESSKLHERGKVESGSKSKEGKKVGGSSVHKHETKKKKEHAVSHPHKKKDVPKPVVEEVVVKEDQEHEEAESDDSDQSNKEDGEEGTESDGNEGESDGNGDGSVDDSSASVDEEVEEKNEEVTVNEISKKRKRKGPVFDPKAEYSWRLCNTRSKHNYMPCIDNDGLIGRLQSYRHRERSCPKKPVMCLVPLPHDGYDPPVSWPESKSKILYKNVAHPKLAAYIKKHNWVNETGEYLSFPQNQTTF... | Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 82662
Sequence Length: 724
Subcellular Location: Golgi apparatus membrane
EC: 2.1.1.-
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Q9C9Q8 | MSMPLQRGISGVRVSDSSDDLRDSQMKDKTERARSTENNNLTLRFPFGFLFSNQSSSKHGGGGENGFSADPYSARSRHRLMLLFLKISLVLIVVIALAGSFWWTISISTSSRGHVYHNYRRLQEQLVSDLWDIGEISLGPNRWKELEYCNIESENFVPCFNVSENLALGYSNGDENDRFCGPGSKQECLELPPVKYRVPLRWPTGKDIIWHSNVKITAQEVVSSGSITKRMMMMEDDQISFRSASPMSDEVEDYSHQIAEMIGIKKDNFIEAGVRTILDIGCGYGSFGAHLLSKQILTMCIANYEASGSQVQLTLERGLP... | Function: May be involved in the synthesis of homogalacturonan. Required for normal cell adhesion and plant development.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 77897
Sequence Length: 684
Pathway: Glycan metabolism; pectin biosynthesis.
Subcellular Location: Golgi apparatus membrane
... |
Q8NRZ6 | MSQALPVRDQGRDQGIFAGTLPPAPPKFKWTRLDTYTWAIIAVFALVTRFTGLSSATASGTPVFDEKHYVPQAWDMVRSWINPITGGIESNPGYGLVVHPPLAKQLEALGEWVFGYTPLGWRIMVAIFGTLTIFAIMAIARRLSGSTMVTFIAGILALADGVLLVSSRFGMLDIFLVFFITAAAWALIRDHQQMHQRLNDLLLTNGQITKDFGPRFGFRWWRFTTGVFLGLALSVKWSGLYYIAFFGLTSVFLDLWLRKRYGVRRYVTGTLKNDVIPALGSLVIIPALLYIWSWRAWFASETSVYRHAKTDGTITEDSIL... | Function: Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins.
Catalytic Activity: a dolichyl beta-D-mannosyl phosphate + L-seryl-[protein] = 3-O-(alpha-D-mannosyl)-L-seryl-[protein] + a dolichyl phosphate + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 58734
Sequence Lengt... |
L8F4Z2 | MTALDTDTPTAGRSAPLISPGPVIPPPDFGPLDRAQGWAMTAIITALAAITRFLNLGSPTDAGTPIFDEKHYAPQAWQVLHNDGVEDNPGYGLVVHPPVGKQLIAIGEWLFGYNGLGWRFSGAVCGVIIVMLVTRIARRISRSTLVGAIAGLLIIADGVSFVSSRTALLDVFLVMFAVAAFACLMVDRDQVRERMYHAFLDGRIAETRWGPRLGVRWWRFGAGVLLGLACATKWSGLYFVLFFGVMTLVFDAIARKQYHVPHPWRGMLRRDLGPAAYVFGLIPFAVYLASYAPWFASETAVNRYEVGRSIGPDSILPIPD... | Function: Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins (By similarity). Involved in DNA conjugation, in at least the recipient strain .
Catalytic Activity: a dolichyl beta-D-mannosyl phosphate + L-seryl-[protein] = 3-O-(alpha-D-mannosyl)-L-seryl-[protein] + a dolichyl phosphate + H(+)
Locatio... |
D4B4V1 | MAGRILLGLTLLATSLPLLAMGDAAVVPCISYSTVPGYFLQDDPAVDPKTFDYAKEGFGLIDQAYDTDETLDAELKKLPWRRFEHKVRSLNKHAASNVRFAVLFLGRHGQGFHNVAEAYYGTKAWDDYWSKLDGDGTITWSDAHLTEEGISQAKVARDTWAGQMKNSIPLPEVYYTSPLDRCLATAKFTFSKLELPPSKPFIPTVKELLRETLGVHTCDRRSSRNYIESTYPTYKIEPGFTQKDMLWDPEVRESDSDRDARLKKLLDDIFSHDKSTFMSLTAHGGAIRSILNVIGHREFGLQTGAVIPVLIRIETSTDAP... | Function: Probable phosphomutase that may have a function related to the manipulation of phosphate groups on carbohydrates.
Sequence Mass (Da): 37547
Sequence Length: 335
Subcellular Location: Secreted
EC: 5.4.-.-
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P36069 | MSLRAVPGYFAAYPSEGFQGLDSTKYDHLELINHKNWKELYHAIPRNTKNRHYKLLILARHGQGYHNAAILRYGMEKWDAYWSLLSGDEHGEWLDSKLTPLGKDQVRRTGSNVLLPMAKQLGMLPHVFFSSPMRRCLETFIESWTPVLAETQELPAGTKISTRIIEGLRETLGSHTCDKRVAHSMAVDEYQDFSTESGHTVHWQYVPDYPEDDELWLPDHRETCAEMDKRTLNGLFELFNQLSSEEKFISLTCHSGVIQSVLRNLQHPPIYNLDTGKVVAVVVEVPVNTADRGRL | Function: Probable phosphomutase that may have a function related to the manipulation of phosphate groups on carbohydrates. Reduces trehalose-6-phosphate levels when overexpressed in TPS2-deleted cells. Reduces 5'-Phosphoribosyl-4-carboxamide-5-aminoimidazole (AICAR) levels, a metabolic intermediate at the crossroads b... |
Q9VIT2 | MMKIVLISGKRKCGKDYISERLQRRLGSRSCIVRISEPIKSEWARKLQLDLDALLGDGPYKEKYRRDMIVWSDEVRAQDYGYFCRVAMEEALSRQQTPYILVSDVRRKNDIRWFRETYGPERVITLRLTSRPETRSARGWTFTAGIDDVPSECDLDDLADGFDVVLANDEELDQEAIDILLDRLQLQYR | Catalytic Activity: (R)-5-phosphomevalonate + ATP = (R)-5-diphosphomevalonate + ADP
Sequence Mass (Da): 22144
Sequence Length: 189
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via mevalonate pathway; isopentenyl diphosphate from (R)-mevalonate: step 2/3.
Subcellular Location: Cytoplasm
EC: 2.7... |
Q15126 | MAPLGGAPRLVLLFSGKRKSGKDFVTEALQSRLGADVCAVLRLSGPLKEQYAQEHGLNFQRLLDTSTYKEAFRKDMIRWGEEKRQADPGFFCRKIVEGISQPIWLVSDTRRVSDIQWFREAYGAVTQTVRVVALEQSRQQRGWVFTPGVDDAESECGLDNFGDFDWVIENHGVEQRLEEQLENLIEFIRSRL | Function: Catalyzes the reversible ATP-dependent phosphorylation of mevalonate 5-phosphate to produce mevalonate diphosphate and ADP, a key step in the mevalonic acid mediated biosynthesis of isopentenyl diphosphate and other polyisoprenoid metabolites.
Catalytic Activity: (R)-5-phosphomevalonate + ATP = (R)-5-diphosph... |
Q9D1G2 | MAPLGASPRLVLLFSGKRKSGKDFVTERLKSRLGGNICALLRLSGPLKEEYAREHGLDFQRLLDASTYKETYRRDMICWGEQKRQADPGFFCRKIVEGVSQPIWLVSDTRRTSDIQWFQEAYGAVIQTVRVVASEQSRQQRGWVFTPGVDDAESECGLDNFGNFDWVIENHGDEQCLEDQLEHLLGFIQAKL | Function: Catalyzes the reversible ATP-dependent phosphorylation of mevalonate 5-phosphate to produce mevalonate diphosphate and ADP, a key step in the mevalonic acid mediated biosynthesis of isopentenyl diphosphate and other polyisoprenoid metabolites.
Catalytic Activity: (R)-5-phosphomevalonate + ATP = (R)-5-diphosph... |
Q29081 | MAPLGSVPRLVLLFSGKRKSGKDFVTEALQSRLGADVCAILRLSGPLKEQYAQEHGLDFQRLLDASTYKESYRKDMIRWGQEKRQADPGFFCRKIVEGVSQPIWLVSDTRRLSDIQWFQETYGAVTQTVRVVATEQSRQQRGWVFIPGVDDAESECGLDDFGAFDWVIENHGDEQHLEEQLGHLIEFVHSRL | Function: Catalyzes the reversible ATP-dependent phosphorylation of mevalonate 5-phosphate to produce mevalonate diphosphate and ADP, a key step in the mevalonic acid mediated biosynthesis of isopentenyl diphosphate and other polyisoprenoid metabolites.
Catalytic Activity: (R)-5-phosphomevalonate + ATP = (R)-5-diphosph... |
Q20085 | MNSVLSNIEKLDTYILRRNEYVAESKDEPNKLNTSRKLEVTTKKNQSNNKKRPPPINKARKSLPSIFRRAEENKDSAQIITPTGSKIIGSPLYKRSKSDSFFDHAFNFDKNLGKGSFGEVVAATCRSTSKKFAIKKIPFSKLSKDQYREAYGHMNIPCHPNIVRFHQAWIDKQILHIQLEMCDKSLAAYCHGIDWLEDKELWNVFLDILQGLGHLHNNFMLHNDIKPDNIFMTKNKVCKLGDFGLISDMRSEPINNSSNKHYQSEGDGKYCSKEAINGTLSIFSDIFSFGISILEVGTNIHLPSYGTGWEPIRKWEIPEE... | Function: Acts as a negative regulator of entry into mitosis (G2 to M transition) by phosphorylation of the CDK1 kinase.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 54046
Sequence Length: 468
Subcellular Location: Nucleus
EC: 2.7.11.1
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O18209 | MDDTEGNSSMDSIRNGQSSPLPQVTPRLPQIPMMMRETPLSTKRERQAITPRFRRPAPKMIKTMPPTRSIWSVRKESVPLLVTPQGPKPLESPKYDHTNAQSFFEQVFQIDEIIGRGSFGEVFAARCREDSQLYAVKVSLAPIRQHSISKYREAESHMIIPPHKNLVKFYRAWEETGRLYIQTELCDQSLLKYCTEKHALPEDEIWNIFVDLLQAVHHLHSNDMIHDDIKPENIFLTKDMICKLGDFGLVINLKNPNDVKSAEEGDSKYLAPEVLNGRPTKSSDIFSLGMTILEATTDLDVPSNGDSWHQIRNGQIPDRF... | Function: Acts as a negative regulator of entry into mitosis (G2 to M transition) by phosphorylation of the CDK1 kinase during oocyte maturation . Required for oocyte maturation, embryonic development, germline proliferation and initiation of meiosis during spermatogenesis . Required for chromosome structure during mit... |
Q9NI63 | MEKHHRLPLPELHDDKHRHKQCNGENSNRFRPPKYKTRGYVAVDNNNLNRSQSLGSCSTNSSQIAHAISFRDAGCSDSSTLPSSPVQAELSTLSLSHFEQCFERLAKLGEGSFGEVFQVRDRSDGQLYAVKISKQLFRGEQYRAERLEEVRRYEEFSGHENCIRFIRAWEQYDRLYMQMELCRESLEQYLLRCQRIPEERIWHILLDLLRGLKSLHDRNLIHLDIKLDNVLIGEDDETCKLADFGLVIDVDRANSHHATEGDSRYMAPEILQGHFSKAADIFSLGIAMLELACYMDLPSNGPLWHELRHGILPEEFINKI... | Function: Acts as a negative regulator of entry into mitosis (G2 to M transition) by phosphorylation of Cdk1 specifically when Cdk1 is complexed to cyclins . Mediates phosphorylation of Cdk1 predominantly on 'Thr-14' . Also involved in Golgi fragmentation . May be involved in phosphorylation of Cdk1 on 'Tyr-15' to a le... |
P22253 | MTQFASPVLHSLLDTDAYKLHMQQAVFHHYYDVQVAAEFRCRGDDLLGIYADAIREQVDAMQHLRLLEDEFQWLSGLPFFKPDYLNWLREFRYNPAQVCVTNDNGKLNIRLTGPWREVIMWEVPLLAVISELVHHYRSPNAGVDQALDALESKLVDFTALTANLDMSRFHLMDFGTRRRFSREVQQAIVKRLQQESWFVGTSNYDLARRLALTPMGTQAHEWFQAHQQISPDLATSQRAALAAWLNEYPDQLGIALTDCITMDAFLRDFGIEFASRYQGLRHDSGDPVAWGEKAIAHYEKLGIDPLTKTLVFSDNLDLPK... | Function: Catalyzes the synthesis of beta-nicotinate D-ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate at the expense of ATP.
PTM: Transiently phosphorylated on a His residue during the reaction cycle . Phosphorylation strongly increases the affinity for substrates and increases the rate of nicotinate... |
Q9AJD6 | MAQYDVAIIGAGSAGALIAARLSEDPARNVLLIEAGGRPSDPDILKPSMWPAIQHRSYDWDYKTTPQEGAAGRSFAWARGKGLGGSSLLHAMGYMRGHPADFAAWAEATGDERWSWEGLLPSFMANEDHVSGGDGIHGKDGPMPVWIPDDEVSPLTQAFMTAGNALGLPRIPDHNTGQMIGVTPNSLMIRDGRRVTVAEAWLTPEVCARPNLTIMTGTLTRRLKLEKSHVSAIELAGPEGLATVTASEIILSAGSLESPALLMRSGIGRENVLREAGVTCRVKAPELGLNLMDHLLGAGNLYATKKHLPPSRLQHSESMA... | Catalytic Activity: O2 + pyridoxine = H2O2 + pyridoxal
Sequence Mass (Da): 54196
Sequence Length: 507
Pathway: Cofactor degradation; B6 vitamer degradation; pyridoxal from pyridoxine (oxidase route): step 1/1.
EC: 1.1.3.12
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Q8GZQ3 | MLTSPSNALHSSTPQFWPLRRSKLCRSRNFPRFHSGERSSGGGGKLCSLSLLSGSGAGKFSVRALVRPDDTDDADSVGDGSLAFPNHVSVKIPFGNREILVETGLMGRQASSAVTVTDGETIVYTSVCLADVPSEPSDFLPLYVHYQERFSAVGRTSGGFFKREGRTKDHEVLICRLIDRPLRPTMPKGFYNETQILSWVLSYDGLHAPDALAVTSAGIAVALSEVPNAKAIAGVRVGLIGGEFIVNPTVKEMEESQLDLFLAGTDTAILTIEGYSNFLPEEMLLQAVKVGQDAVQATCIAIEVLAKKYGKPKMLDAIRL... | Function: Involved in the metabolism of all major classes of plastid RNAs. Required for efficient 3'-end processing of mRNAs and 3'-end maturation of rRNA transcripts, but is not sufficient to mediate their degradation. Mediates tRNA degradation. May function as a poly(A) mRNA 3'-5' degrading phosphorylase. May be requ... |
Q69LE7 | MLATPGALHHLLLLPPPPHTQLAFHHAVGGVPAALLPLPRPRRVAASASTSRRGGARRRAAGARVRASVGEEAPPVVTEEASTSGGPTKFSTKIPVGDRHILVETGHIGRQASASVMVTDGETIVYSSVCLADTPNDPSDFFPMSVHYQERLSAAGRTSGGFFKREGRAKDHEVLVCRLIDRPLRPTMPKGFYYETQILSWVFSYDGIHSPDSLAITAAGVAMALSEVPNKQTIAGVRVGMINDQFVVNPTTEQMDDSELDLVMAGTDSAILMIEGYCDFLTEEKLLQAVETGQGAIREICKAIDGLVQKCGKKKMFDAI... | Function: Involved in the metabolism of all major classes of plastid RNAs. Required for efficient 3'-end processing of mRNAs and 3'-end maturation of rRNA transcripts, but is not sufficient to mediate their degradation. Mediates tRNA degradation. May function as a poly(A) mRNA 3'-5' degrading phosphorylase (By similari... |
Q9S7G6 | MSSIVNRASSASLPNFLAWRALGFRTICSGRLGFAPSVPDSPVSAGTKILESFKEEFEVGSRVVSFETGKIARFANGSVVLGMDETKVLSTVTCAKTDSPRDFLPLTVDYQEKQYAQGLIPNTYMRREGAPKERELLCGRLIDRPIRPLFPTGFYHEVQIMASVLSSDGKQDPDILAANASSAALMLSDVPWGGPIGVIRIGRICGQFVVNPTMDELSSSDLNLIYACTRDKTMMIDVQSREISEKDLAAALRLAHPEAVKYLDPQIRLAEKAGKQKKEYKLSMLSDKTLEKVADLAATRIESVFTDPSYGKFERGEALD... | Function: Involved in the 3'-end maturation of mitochondrial mRNAs, rRNAs and tRNAs. Functions as a poly(A) mRNA 3'-5' degrading phosphorylase and is required for the degradation of highly expressed transcripts of non-coding regions.
Catalytic Activity: phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + RNA(n)
Se... |
Q6KAI0 | MSMAVASLRLLARGGRRRARFPAPLSVPGGRAAFLSGAAEEVAQADAPPPPPPGRKVLESFREEFEIGGRVISFETGKMARFANGSVVISMDDTHVLSTVAAAKSSEPVRDFLPLTVDYQEKQYAQGVIPTTYMRREGAPKERELLCGRIIDRPIRPLFPPGFYHEVQVMNATIIMVNVISSDGKQDPDVMAANASSAALMLSDIPWNGPIGVIRVGRIDGNFVLNPTVDELGLSDLNLVYACSRDKTLMIDVQAREITERDLQAGMKLAHAEAVKCINPQLRLAKRAGKKKKEYKISLISDKSYEKIRTLSEAPIEEVF... | Function: Involved in the 3'-end maturation of mitochondrial mRNAs, rRNAs and tRNAs. Functions as a poly(A) mRNA 3'-5' degrading phosphorylase (By similarity).
Catalytic Activity: phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + RNA(n)
Sequence Mass (Da): 107028
Sequence Length: 982
Subcellular Location: Mitoch... |
C1I201 | METLDGVVVVGGGPVGLLTALKLGKAGIKVVVLEAEPGVSPSPRAVAYMPPTAAALDRFGLLQDIRKRAVMCPDFAYRHGNGELIAKMDWSVLSQDTQYPYMLLLGQNHVSNVIFQHLRELPNVEIRWNHRVEEVDQDDAYVTIETSSPGGTSRLRARWLAATDGARSTVRQKIGLTFDGITWDERLVATNVFYDFSLHGYSRANFVHDPVDWAVVVQLDKTGLWRVCYGEDASLSDAEVRRRLPERFKRLLPGAPTPDQYRVDHLNPYRVHQRCAAEFRRGRVVLAGDAAHATNPMGGLGLSGGVLDAEHLAEALIAVI... | Function: Involved in the degradation of para-nitrophenol (4-NP). Catalyzes oxidation of 4-nitrophenol (4-NP) at position 4 with concomitant removal of the nitro group as nitrite and production of para-benzoquinone.
Catalytic Activity: 4-nitrophenol + H(+) + NADPH + O2 = 1,4-benzoquinone + H2O + NADP(+) + nitrite
Seque... |
C1I202 | MPTKIQIVFYSSYGHIYKMAEAIAAGAREVGDVEVTLLQVPELMPEEVQVKSGIKGYRAAFGSIPYATPEVLAEADAIIFGTPTRFGNMCSQMRNFLDQTGGLWMSGGLIGKVGSVFTSTASQHGGQETTITSFHTTLLHHGMVIVGVPYSEPGLTNMTEISGGTPYGASTLAGADGSRQPSENELQIARFQGKHVATIAKRLANNK | Cofactor: Binds 1 FMN per monomer.
Function: Involved in the degradation of para-nitrophenol (PNP). Catalyzes the reduction of p-benzoquinone to hydroquinone.
Catalytic Activity: 1,4-benzoquinone + H(+) + NADPH = hydroquinone + NADP(+)
Sequence Mass (Da): 22040
Sequence Length: 207
Pathway: Xenobiotic degradation; 4-ni... |
A4Q998 | MSKFSYLQNGKASTNGVPHANGHHQQHQNGHSNGVARNGGTATDTLPVAYQQKAATSGPFHMPRTEHVGYTYDTLQEIATYLLERTELRPKVGIICGSGLGTLAEQLTDVDSFDYETIPHFPVSTVAGHVGRLVFGYLAGVPVMCMQGRFHHYEGYPLAKCAMPVRVMHLIGCTHLIATNAAGGANPKYRVGDIMLIKDHINLMGFAGNNPLQGPNDERFGPRFFGMANTYDPKLNQQAKVIARQIGIENELREGVYTCLGGPNFETVAEVKMLSMLGVDAIGMSTVHEIITARHCGMTCFAFSLITNMCTMSYEEEEEH... | Function: As part of the purine salvage pathway, catalyzes the phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate . Preferentially acts on 2'-deoxyinosine and inosine, and to a lesser extent on ... |
O66839 | MLGIIGGSGLYNLPGIKVKEEVQVKTPFGEPSSPVVIAEVEGKKVAFLARHGRGHEYPPHLVPYRANLWALREVGVKRVLGISAVGGINELLMPGDFVVIHDYLDFTKTRRSTYYEGKFSVKVEGEDKVAKLLREGKVVHVDMSEAYCPEMRKVLIQILKEKNFRFHPKGVYACTEGPRFETPSEIKMLKLLGADVVGMTGYPEVALARELTMCYASLCVVANPAAGIAGYRLTSNEVIQLMKRKEEEIKEVVLKFIKELPEIRSCDCEKSLEGAEV | Function: Purine nucleoside phosphorylase which is highly specific for 6-oxopurine nucleosides. Cleaves guanosine or inosine to respective bases and sugar-1-phosphate molecules. Involved in purine salvage.
Catalytic Activity: a purine D-ribonucleoside + phosphate = a purine nucleobase + alpha-D-ribose 1-phosphate
Seque... |
O28486 | MIGIIGGTHILEIKVLKDVEETRIETPYGTAEIDVGRVDGIDVAIIQRHGKRKDKPPHRINHAANFYALKSLGVKYVIGMGSVGALREEYSLPSLIIPHDYIDFFSGVTIYNDSLVHVTPGFDEYLREVLVEVARKISSFPVIDKGVYFQTRGPRLETKAEIAMIKSFADCVGMTAGSEATIARELGLSYAIVCTMDNYAHGIKNQSIDYREIVEKAKENARECLKIVEEAVKKVWEEKIQRT | Function: Purine nucleoside phosphorylase which is highly specific for 6-oxopurine nucleosides. Cleaves guanosine or inosine to respective bases and sugar-1-phosphate molecules. Involved in purine salvage.
Catalytic Activity: a purine D-ribonucleoside + phosphate = a purine nucleobase + alpha-D-ribose 1-phosphate
Seque... |
Q8IMU4 | MEADLEVQSELEKDTIPIKIGIIGEANLDKPIYLAERMEYAVCTPFGKPSDVIIDGQIEGVNVCLLSRNGRNHDIMPSNINYRANVWAMRKMGCTHILVTNTFSSLRDTFQPGHLVVPNDVIDYTSRRAQTFYDGAVGSPLGVCHVPMNPTFCERTRQHLLSAAEELGFPTGSSGTVLTLEGPRYSTVAENNMFRKWGADLLSMTLCPEAILAKEAGIPYASLGLVTNMECWCAKQPNATTHEIIYIFKKQSENLQKVLITAIRNMAAEDWAEDILKAKILVCSNFANSK | Function: Purine nucleoside phosphorylase involved in purine salvage.
Catalytic Activity: a purine D-ribonucleoside + phosphate = a purine nucleobase + alpha-D-ribose 1-phosphate
Sequence Mass (Da): 32132
Sequence Length: 290
Pathway: Purine metabolism; purine nucleoside salvage.
Subcellular Location: Cytoplasm
EC: 2.4... |
Q8RA43 | MEERTFEMELAGRKLVVQTGKVAQQANGAAWVKYGDTVVLVTACASKEPREGIDFFPLTVEYEERLYSIGKIPGGFIKREGKPSEKAILSARLIDRPIRPLFPEGYRNDVQVIATVLSVDPDAQPEIVAMIGSSVALSISDIPFNGPTGSVAVGLVDGKFVINPTYEQREKSLMHLVVSGTKDAIVMVEAGAKEVPEETILDAIVYAHQYIKQIVEFIEGIVKEVGVPKAEVVLHEIDKELEEKVRAYATEKIYNALRTPEKKERNDNLDKVEQEVLEHFKDEYPDNLADIDEVLYKIMKEQMRKMIKEEKIRVDGRGLD... | Function: Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Catalytic Activity: phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + RNA(n)
Sequence Mass (Da): 78520
Sequence Length: 707
Subcellular Location: Cytoplasm
EC: 2.7.... |
A7GX79 | MQYSIEVNNQVEIFDLNKVAKQAAGAVMLRVKNTVVLATVARDDVQVEEDFLPLTVQYIEKAYAAGRIPGGYVKRETKPGDFETLTARIIDRSLRPLFPKGYAYPTQIVVMVLSADPEVDLQVVGLNAASVALYLSDIPVNRPVCGVRVGYIDDKFVINPSNSELKSSALDLYVAGTKDELLMIEMRSIAQQSSQIIPIIAIDPMMDPSLNDSITQKQDMNEFSEDRIVEAIDFAGKAILRASNAYEEAFKEHKKEDAILELKPEIENENIAIYIDKFYKNDVKNAINQMAKSERASELGKIAKQIASDEVAQKEGWEEG... | Function: Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Catalytic Activity: phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + RNA(n)
Sequence Mass (Da): 80567
Sequence Length: 735
Subcellular Location: Cytoplasm
EC: 2.7.... |
Q7VIL0 | MQHIKLEFENLSEQYSFNYVAQAANGGILYQNGGSVLLASVCTQENEKYDDEFLPLSVQYIEKTYANNKFPSGFIKREGKPSEFEILTSRLIDRTLRPLFPKGYTYITSIVVMVLSYDGKSDLQLNALNAAACALYVSDLPLESLQDKAVSGVRIGRKDGHFIINPTMEQLSESELNLFVSGRDDELLMIEMKSIRTAQGANELSEENFLEALECAKNYIKNATQTYHQQFAPYKKSPFAFESANDELDEQLLNIIQTHYHTPITEAIKHMAKSERHTQLKALIKQVVRECEIEDEKKVQEHIMAYKRKLVREMILQSHI... | Function: Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Catalytic Activity: phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + RNA(n)
Sequence Mass (Da): 78828
Sequence Length: 709
Subcellular Location: Cytoplasm
EC: 2.7.... |
Q2S1P1 | MKPEAHIEDIEFVPDRSLSLETGRIAKQADGSVVARLGDTMVLSTATLSDSVNESNFFPLTVDYREKFAAGGKVPGGFIKREGRPTDKETLTSRLIDRAIRPLFPDGFYHDVHVVNFVISAGQDFDADVIAGVGSSAALMLSGAPFAGPFAEVRVGRVDGDYIVNPTMQQTEESDIDLVVAGKEDALVMVEGEAEEISEESMIEALDVAHRSIRRLCEGQHRLVEQAGEPDPFEWEADRVPEQLVQRMREEYGPKVADHIHGPYSKETFHGGIGDLKDQAVDDVLGDASETPEGYTASDIRDAIGEVEKGEMRNMIVEEG... | Function: Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Catalytic Activity: phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + RNA(n)
Sequence Mass (Da): 78371
Sequence Length: 712
Subcellular Location: Cytoplasm
EC: 2.7.... |
Q12QG9 | MNPIVKSFEYGQHTVTLETGVIARQADAAVLASMGDTTVLVTVVGKKVADLSRDFFPLTVNYQEKTYAAGKIPGGFFKREGRPSEDETLIARLIDRPIRPLFPNGFKNEVQVIITVVSVDPQIEPDIISMIGTSAALAISGIPFSGPLGAARVGYINGEYLLNPTVDQLATSSLNLVVAGTKAAVLMVESEAKALAEEIMLGAVTYGHDQQQVVVDAIAEFKAEAGKPTWDWTAPVQDQALVAKIKELAEAGMTDAYQIEVKQDRYVQVGVVKAAAKAALVAENPDVDTREVDNLLGSLEKNVVRSRIIAGKPRIDGREP... | Function: Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Catalytic Activity: phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + RNA(n)
Sequence Mass (Da): 75278
Sequence Length: 698
Subcellular Location: Cytoplasm
EC: 2.7.... |
Q9PGQ9 | MAKITKTFQYGKHTVTLETGEVARQANGAVIVKMDDTVLLVTVVAAKTAREGQDFFPLTVDYQEKFYAGGRIPGSFFKREGRATEKETLISRLIDRPIRPLFPEDYKNEVQIIAMVMSLDPEIDGDIPAMIGASAALSLAGIPFKGPIGAAKIGYNDGQYILNPTVSELKKSQLELVVAGTANAVLMVESEAALLSEEVMLGAVIFGHREMQKVIQVIDSLTAEAGTQPSDWVPPAKNDALVIALKEVIGGRLSDAFHIRDKLQRRDAIAAVKDDVIQQLAGRLEVEGWNLAELLKEFGELEYRTMRDALLDTKVRIDGR... | Function: Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
Catalytic Activity: phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + RNA(n)
Sequence Mass (Da): 75961
Sequence Length: 700
Subcellular Location: Cytoplasm
EC: 2.7.... |
Q12796 | MTVVSVPQREPLVLGGRLAPLGFSSRGYFGALPMVTTAPPPLPRIPDPRALPPTLFLPHFLGGDGPCLTPQPRAPAALPNRSLAVAGGTPRAAPKKRRKKKVRASPAGQLPSRFHQYQQHRPSLEGGRSPATGPSGAQEVPGPAAALAPSPAAAAGTEGASPDLAPLRPAAPGQTPLRKEVLKSKMGKSEKIALPHGQLVHGIHLYEQPKINRQKSKYNLPLTKITSAKRNENNFWQDSVSSDRIQKQEKKPFKNTENIKNSHLKKSAFLTEVSQKENYAGAKFSDPPSPSVLPKPPSHWMGSTVENSNQNRELMAVHLK... | Function: Nuclear receptor coactivator. May play a role in signal transduction.
Sequence Mass (Da): 35225
Sequence Length: 327
Domain: The interaction between PNRC1 and nuclear receptors is dependent on the SH3 binding motif.
Subcellular Location: Nucleus
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Q63647 | MTVVSVPQRDLALGGRLAPLGSLGALPMVSPAPPPLPRLPDPRALPPTLFLPHFLGGDGPCLARASHRCTVQLQLGPGRCPTAAPKKRRKKKVRASPAGQLPSRFHQFQQHRPSLEGGRSPVPGPIAAQEERGPGATALLYRQPPLAKEVLKSKMGKSEKISPPHSQLVHGIHLCEQPKISRQKSKFNLPLTKITSAKRNENDFWQDSASSDRMQKQEKKPLKNTENIKNNHLKKSAFLTEGSQKENYAGAKFSDPPSPSVLPKPPSHWMGSTTENPSQSRELMAVHLKTLLKVQT | Function: Nuclear receptor coactivator. May play a role in signal transduction (By similarity).
Sequence Mass (Da): 32374
Sequence Length: 296
Domain: The interaction between PNRC1 and nuclear receptors is dependent on the SH3 binding motif.
Subcellular Location: Nucleus
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Q0VCW6 | MGGGERYNIPAPQTRNVSKNQQQLSRQKTKDQNSQMKIVHKKKERGHTYNSSSAAWQAMQNGGKNKNFPNNQNWNSSLSSPTLLFKSQTNQNYAGAKFSEPPSPSVLPKPPSHWVPVSFNPSDKEIMTFQLKTLLKVQV | Function: Involved in nonsense-mediated mRNA decay (NMD) by acting as a bridge between the mRNA decapping complex and the NMD machinery. May act by targeting the NMD machinery to the P-body and recruiting the decapping machinery to aberrant mRNAs. Required for UPF1/RENT1 localization to the P-body. Plays a role in gluc... |
Q8TC44 | MASATEDPVLERYFKGHKAAITSLDLSPNGKQLATASWDTFLMLWNFKPHARAYRYVGHKDVVTSVQFSPHGNLLASASRDRTVRLWIPDKRGKFSEFKAHTAPVRSVDFSADGQFLATASEDKSIKVWSMYRQRFLYSLYRHTHWVRCAKFSPDGRLIVSCSEDKTIKIWDTTNKQCVNNFSDSVGFANFVDFNPSGTCIASAGSDQTVKVWDVRVNKLLQHYQVHSGGVNCISFHPSGNYLITASSDGTLKILDLLEGRLIYTLQGHTGPVFTVSFSKGGELFASGGADTQVLLWRTNFDELHCKGLTKRNLKRLHFD... | Function: Plays an important role in centriole assembly and/or stability and ciliogenesis . Involved in early steps of centriole duplication, as well as in the later steps of centriole length control . Acts in concert with POC1A to ensure centriole integrity and proper mitotic spindle formation . Required for primary c... |
Q5RD06 | MASATEDPVLERYFKGHKAAITSLDLSPNGKQLATASWDTFLMLWNFKPHARAYRYVGHKDVVTSVQFSPHGNLLASASRDRTVRLWIPDKRGKFSEFKAHTAPVRSVDFSADGQFLATASEDKSIKVWSMYRQRFLYSLYRHTHWVRCAKFSPDGRLIVSCSEDKTIKIWDTTNKQCVNNFSDSVGFANFVDFNPSGTCIASAGSDQTVKVWDVRVNKLLQHYQVHSGGVNCISFHPSDNYLVTASSDGTLKILDLLEGRLIYTLQGHTGPVFTVSFSKGGELFASGGADTQVLLWRTNFDELHCKGLNKRNLKRLHFD... | Function: Plays an important role in centriole assembly and/or stability and ciliogenesis. Involved in early steps of centriole duplication, as well as in the later steps of centriole length control. Acts in concert with POC1A to ensure centriole integrity and proper mitotic spindle formation. Required for primary cili... |
Q65729 | ETEITPYGENEELLWRHRITTEVGDCGATMVALSDQKIVGFHSLGGISMNYFVPVTQELLDFLNSKTEKPLVPWRFSEDQVDVGGLYIHNDFDKFPFVKTIQKLVGFQNGHMIKYCGEGFTPVARSENRLSRQHVISGQRESFIHFVEASAKWRPIVTPMLGRLQPSALNREAYYKDVLKYDKPIRLGTVHEEAFQSAVINVIRILENAGFERGGVKACFDYGKIFNDLNLDAAMGALYAGKKKDYFVEATDEEIEEMFLRSAGKICANGHGVWSALLKAELRPAEKVAANKTRTFTSAPIDILFGAKAVVDDFNKQFYK... | Function: Has RNA-binding and proteolytic activities.
PTM: Genome polyprotein of potyviruses undergoes post-translational proteolytic processing by the main proteinase NIa-pro resulting in the production of at least ten individual proteins. The P1 proteinase and the HC-pro cleave only their respective C-termini autocat... |
P07993 | YVPKLEEERIVIYSTMDRADLAEHRLEAICAAMIESWGYSELTHQIRRFYSWLLQQQPFASIAQEGKAPYIASMALRKLYMDRAVDEEELRVFTEMMVALDDEFECDSYEVHHQANDTIDTGGNSKKDVKPEQGSIQPSSNKGKEKDVNAGTSGTHTVPRIKAITAKMRMPKSKGAAVLKLDHLLEYAPQQIDISNTRATQSQFDTWYEAVRVAYDIGETEMPTVMNGLMVWCIENGTSPNINGVWVMMDGSEQVEYPLKPIVENAKPTLRQIMAHFSDVAEAYIEMRNKKEPYMPRYGLVRNLRDASLARYAFDFYEVT... | Function: An RNA-dependent RNA polymerase that plays an essential role in the virus replication.
PTM: Genome polyprotein of potyviruses undergoes post-translational proteolytic processing by the main proteinase NIa-pro resulting in the production of at least ten individual proteins. The P1 proteinase and the HC-pro cle... |
Q703G9 | MNTNKATATYLKSIMLPETGPASIPDDITERHILKQETSSYNLEVSESGSGVLVCFPGAPGSRIGAHYRWNANQTGLEFDQWLETSQDLKKAFNYGRLISRKYDIQSSTLPAGLYALNGTLNAATFEGSLSEVESLTYNSLMSLTTNPQDKVNNQLVTKGVTVLNLPTGFDKPYVRLEDETPQGLQSMNGAKMRCTAAIAPRRYEIDLPSQRLPPVPATGTLTTLYEGNADIVNSTTVTGDINFSLAEQPADETKFDFQLDFMGLDNDVPVVTVVSSVLATNDNYRGVSAKMTQSIPTENITKPITRVKLSYKINQQTAI... | Function: Capsid protein VP2 self assembles to form an icosahedral capsid with a T=13 symmetry, about 70 nm in diameter, and consisting of 260 VP2 trimers. The capsid encapsulates the genomic dsRNA. VP2 is also involved in attachment and entry into the host cell (By similarity).
PTM: Specific enzymatic cleavages yield ... |
P17517 | SVTEHFNVYKATRPYXXXCADCGDGYFCYSPVAIEKIRDEASDGMLKIQVSAQIGLDKAGTHAHTKLRYMAGHDVQESKRDSLRVYTSAACSIHGTMGHFIVAHCPPGDYLKVSFEDADSHVKACKVQYKHNPLPVGREKFVVRPHFGVELPCTSYQLTTAPTDEEIDMHTPPDIPDRTLLSQTAGNVKITAGGRTIRYNCTWGRDNVGTTSTDKTINACKIDQCHAAVTSHDKWQFTSPFVPRADQTARKGKVHVPFPLTNVTCRVPLARAPDVTYGKKEVTLRLHPDHPTLFSYRSLGAEPHPYEEWVDKFSERIIPV... | Function: Spike glycoprotein E2: Plays a role in viral attachment to target host cell, by binding to the cell receptor. Synthesized as a p62 precursor which is processed by furin at the cell membrane just before virion budding, giving rise to E2-E1 heterodimer. The p62-E1 heterodimer is stable, whereas E2-E1 is unstabl... |
P15629 | MNTEIVQKHRVLTKGNPNVTFIKVSIGKRNFLAYIDTGATLCFGKRKISNNWEILKQPKEIIIADKSKHYIREAISNVFLKIENKEFLIPIIYLHDSGLDLIIGNNFLKLYQPFIQRLETIELRWKNLNNPKESQMISTKILTKNEVLKLSFEKIHICLEKYLFFKTIEEQLEEVCSEHPLDETKNKNGLLIEIRLKDPLQEINVTNRIPYTIRDVQEFKEECEDLLKKGLIRESQSPHSAPAFYVENHNEIKRGKRRMVINYKKMNEATIGDSYKLPRKDFILEKIKGSLWFSSLDAKSGYYQLRLHENTKPLTAFSCP... | Function: Encodes for at least two polypeptides: protease (PR) and reverse transcriptase (RT). The protease processes the polyprotein in cis. Reverse transcriptase is multifunctional enzyme that converts the viral RNA genome into dsDNA in viral cytoplasmic capsids. This enzyme displays a DNA polymerase activity that ca... |
G0S6T0 | MAPPPPSADVPLAERLQRLASTLQFAWFSGHALLLLCVFRYAFSWIRFNYYSGMARFCYRFAFIAAAATYGIVVYKTWRARQKTGVKTSGIKDYLRDENIQYLVLALVWLFMPQYPLALLPYGIYSVFHVATYVRANLIPTLVPPQRINAPAGASPNAKPQYTQHPASEAIGVFVKKYYDSSMSMVARLEIMLWLRLILSVILFQRRSWILFAIYTTFLRTRFSQSIHVQNAFALLEARIDNLIGAQGTPPQARQVWDNVKTAARQFYAVTDLNKYESGVAAPKKSS | Function: Contributes to proper distribution and/or efficient assembly of nuclear pores.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32671
Sequence Length: 287
Subcellular Location: Nucleus membrane
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Q12164 | MSSRPANNQGPPNLPARDKSLVQRFMAVAKSLQFAWFTGHSVVLISSILYLLKMSEFYYRSAYLGVIESFGIIIYQQFFTRNEPLQTQDAAATKASIKSRVAGLLKSEDVLYLVLANFWLFTPRFSFSLIPFFAFAVFHVLIYVEKVLLPKVFHLSSKDSSKILSFIDKFVVQYNDLCMHWVGTAELLIFILVLFRAILCFQRSWIILVVYAIFIKLRYENSKYMKAAFAQWRVRMDGIISHPSIPPFVKRAYNAIKMSLIRLSEYRLSGAPQVTKKQN | Function: Contributes to proper distribution and/or efficient assembly of nuclear pores. Required for normal pore density in the daughter nucleus during telophase.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32186
Sequence Length: 279
Subcellular Location: Endoplasmic reticulum membrane
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G0S7R3 | MSSTLSVAKAASTPVKQITSAVGPVKESPGNWKHPRLAEITRRQSRNIFGEKNVRQIVYNVAAIVLLEIFRVFASPSIPSQLILPSLRPYSLWIHAVFLVIPLTNIVIALLPLFRPVDDLSDIPLTPAQRKLLGLPPSSKPATPNSVYSTPPRYSRTPSLAGSPASIKSYTSSTLPTASSPTPGAAGIGAGSPAAPIYLSPSKFTTSTSSQQFSPSPSGASPLLHRAISNTSTASGVSPYGSPNSPSKFGASTNSTLAASTISTSTFSVSTTSSIAHVLNNSRLRESVIEGVPATPTPVGKGASVKANSKWLYQRGRRTS... | Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors.
Location Topology: Multi-pass membrane p... |
P03710 | MKTPTIPTLLGPDGMTSLREYAGYHGGGSGFGGQLRSWNPPSESVDAALLPNFTRGNARADDLVRNNGYAANAIQLHQDHIVGSFFRLSHRPSWRYLGIGEEEARAFSREVEAAWKEFAEDDCCCIDVERKRTFTMMIREGVAMHAFNGELFVQATWDTSSSRLFRTQFRMVSPKRISNPNNTGDSRNCRAGVQINDSGAALGYYVSEDGYPGWMPQKWTWIPRELPGGRASFIHVFEPVEDGQTRGANVFYSVMEQMKMLDTLQNTQLQSAIVKAMYAATIESELDTQSAMDFILGANSQEQRERLTGWIGEIAAYYAA... | Function: Forms the portal vertex of the capsid . This portal plays critical roles in head assembly, genome packaging, neck/tail attachment, and genome ejection (Probable). The portal protein multimerizes as a single ring-shaped homododecamer arranged around a central channel . Binds to the terminase subunits to form t... |
P22009 | MSVEVDGFNASPLFKELNDGLADKAKAQEAVKAVNAIIVITLKNKEGKEQSWVLDLKKDGTLAKVDGAAPKGDVQLILKDVDFVKLANNKVNGQKLFMNGKLKVKGNMMKATAIEAVFKKLDPRPKL | Function: Is involved in beta-oxidation of long-chain fatty acids. Its exact function is unknown, but possesses a nonspecific lipid-transfer activity, despite the absence of a cysteine residue thought to be essential for the activity of its mammalian counterparts.
Sequence Mass (Da): 13806
Sequence Length: 127
Pathway:... |
Q6TMK4 | MRLNLISFFIIFTILVSISNSQEFRSYTGEGNNKQNPKQGSIFTPFIRLANPIKFNKNGFPNITNQPSRAISNIIFDQQTHIGSKEHLTDMFNMWGQFLIHNMALSKPEPNSWPIKVPKCDQYFDPACIGNKTMNYFRTRATEVPCDVGKTVVDEDGKCYEQINSLGSYIDGNVLYGNSEEICKNLRSLSGGEMKMTVTDVGDLPPKNVPGVPMDNDANLFPIDQLYSVGERRGNENPGLLSIHTLLLRDHNRLARKFARLHPEWDDERVFQQSRSCIIEQIQKITYDEYLPTTLGSFPSYTGYDANVNAQVSNEFTTTA... | Catalytic Activity: 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O
Sequence Mass (Da): 60797
Sequence Length: 531
Subcellular Location: Secreted
EC: 1.11.1.7
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S7ZK48 | MPASDRTSETGDVEKVTAAETPKEVPASNAAESTALTGLPLYTVLVGLGLALFLGAMDMAMLGTAVPSITSTFHTTADIGWYGAAYPLTMSSIQLLAGKIYAQFPQKLVFLVFFGLFMLGSLLCGVAVNSPMFIVGRATAGAGAAGVLSGTLAIVSAVVPLDKQSLILGLMMSLVGTAVVLGPVISGLLTDHSTWRWCFYLNLPCGGVTLLALILFFRPPKRPTRTTPLSIPELIKKLDLAGCLGFIPAVVMLLLALQWGGDGSKEHAWNSATIIGLFCGAGVSLILFLIWEHYQGDDAMLPLKFFRDLTIIASCLYGFA... | Function: MFS-type transporter; part of the gene cluster that mediates the biosynthesis of oxaleimides, cytotoxic compounds containing an unusual disubstituted succinimide moiety.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 60410
Sequence Length: 567
Subcellular Location: Cell membrane
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P07003 | MKQTVAAYIAKTLESAGVKRIWGVTGDSLNGLSDSLNRMGTIEWMSTRHEEVAAFAAGAEAQLSGELAVCAGSCGPGNLHLINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQELFRECSHYCELVSSPEQIPQVLAIAMRKAVLNRGVSVVVLPGDVALKPAPEGATMHWYHAPQPVVTPEEEELRKLAQLLRYSSNIALMCGSGCAGAHKELVEFAGKIKAPIVHALRGKEHVEYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYRAFYPTDAKIIQIDINPASIGAHSKVDMALVGDIKSTLRALL... | Cofactor: Binds 1 FAD per subunit.
Function: A peripheral cell membrane enzyme that catalyzes the oxidative decarboxylation of pyruvate to form acetate and CO(2). It channels electrons from the cytoplasm to the respiratory chain at the cell membrane via ubiquinone (By similarity) . The main pathway for acetate producti... |
P37063 | MVMKQTKQTNILAGAAVIKVLEAWGVDHLYGIPGGSINSIMDALSAERDRIHYIQVRHEEVGAMAAAADAKLTGKIGVCFGSAGPGGTHLMNGLYDAREDHVPVLALIGQFGTTGMNMDTFQEMNENPIYADVADYNVTAVNAATLPHVIDEAIRRAYAHQGVAVVQIPVDLPWQQIPAEDWYASANSYQTPLLPEPDVQAVTRLTQTLLAAERPLIYYGIGARKAGKELEQLSKTLKIPLMSTYPAKGIVADRYPAYLGSANRVAQKPANEALAQADVVLFVGNNYPFAEVSKAFKNTRYFLQIDIDPAKLGKRHKTDI... | Cofactor: Binds 1 FAD per subunit.
Function: Important for the aerobic growth. Decarboxylates pyruvate in four steps. The energy released is partially stored in acetyl phosphate.
Catalytic Activity: H(+) + O2 + phosphate + pyruvate = acetyl phosphate + CO2 + H2O2
Sequence Mass (Da): 66111
Sequence Length: 603
Domain: E... |
S8B3I0 | MSEIIESTVAFLIGLLKASWTRTAWHFAVLSFVYVIARSIYRVWFHPLSSYPGPKLAALTQLWYARHWMGGRYPFAIEEAHRRYGEVVRIAPNELSFNTAQSFNEIYGHTTKDHKPFIKGTFYEHYQPEPGIVAERNPEKHRETRKLLAHGFSARALKAQESIIAQYSDLFLAQVKKLAKSHFWIDTIHDAGILVTLFEIGRRLPLLWPLILFSLPNGIKKKFDLFLKYSRDLVRTRVARQNTLTREDFFARLLADKSHSQSEEWLLAQANVLVIAGSDTTATALTTLIYYLAAHQDKLWHLQQELRETFDEASDMTSEK... | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of oxaleimides, cytotoxic compounds containing an unusual disubstituted succinimide moiety . The first step of the pathway is provided by the HR-PKS poxF that serves in a new mode of collaborative biosynthesis with the PKS-... |
S8ASK3 | MVSPVVLATTAMIVVFLLAQRYLSLPVLPNEPLLIPHWMPFFGHAFRFARSKRSFFRWANAKTGGQPFSVPMGGRRHYIFSDPADIAGIHKNGKTLSIRGFVRFIYISIWGFKPADADAMWEIKPEWHRMDIEWLLSDKNDQIAVQYLRRIEEQLRALDAEVEGAPDKAIVRPGLKTVVDVQGKATCQVLYGATTLEKHPGLLDDLTIMVRDGFWGLLFRAPRFLFRNAYEARDRIINTYADLVENIETRKDVSQYLYERTVYLTQQGISPQAQGADMLRTMFASLLNSMPTGYLALLHILAEPGLADEVRKELIDCGYL... | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of oxaleimides, ccytotoxic compounds containing an unusual disubstituted succinimide moiety . The first step of the pathway is provided by the HR-PKS poxF that serves in a new mode of collaborative biosynthesis with the PKS... |
S7ZEI0 | MVSLSCLISYGECLLETVQTHPWSTIGVVVFLSSVKNAPLMWHARLIIAVFYHSVTRKNDVVTIERYGRQGLFGYIVTSSRSPLYECDINGHKSDSTYFSDLDINRIHLITRLFKGAGDLSLRPDRPNVAPEDRPKKMRVLLGGTCCSFRREIKPYAAYEIHSRVLAWDEKWLYVVSYFVKPGSARKMASLQTEVGDKCEMTDLARSMVFTSAITKFVFKDGRKTVRPADALEEMGLLSASEEVVETSEAGEDLWTRSRVEERRKTGIKIAQHFIALDELHDQFEHVSEHPFLGKFGVLGTMF | Function: Thioesterase; part of the gene cluster that mediates the biosynthesis of oxaleimides, cytotoxic compounds containing an unusual disubstituted succinimide moiety . The first step of the pathway is provided by the HR-PKS poxF that serves in a new mode of collaborative biosynthesis with the PKS-NRPS poxE, by pro... |
Q6MFY6 | MAEAGAGGLSETVTETTVTVTTEPENRSLTIKLRKRKPEKKVEWSSDTVDNEHMGRRSSKCCCIYEKPRAFGESSTESDEDEEEGCGHTHCVRGHRKGRRPTTPGPTPTTPPQPPDPSQPPPGPMQH | Function: Atypical E3 ubiquitin-protein ligase which ubiquitinates TLR2 at 'Lys-754' leading to its degradation by the proteasome. Plays a role in regulating inflammatory cytokine release and gram-positive bacterial clearance by functioning, in part, through the ubiquitination and degradation of TLR2. Inhibitor of prot... |
Q6GLB0 | MAESSGPTAGGGATSSTVTTESDTQPEHRSLTLKLRKRKPDKKVEWTCDTVDNENLGRRSSKCCCIYEKPRPFGESSSESEDEDDCCESAHCIRGHKKATSGSKETPSSHHDKTGSMQH | Function: Atypical E3 ubiquitin-protein ligase which ubiquitinates TLR2 at 'Lys-754' leading to its degradation by the proteasome. Inhibitor of protein phosphatase 1.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cystei... |
P20654 | MADQDVDLDSIIDRLLEVRGSRPGKQVQLLESEIRYLCTKAREIFISQPILLELEAPIKICGDIHGQYYDLLRLFEYGGFPPEANYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFVLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIIDEKIFTMHGGLSPDLNSMEQIRRVMRPTDIPDCGLLCDLLWSDPDKDITGWSENDRGVSFTFGPDVVSRFLQKHDMDLICRAHQVVEDGYEFFSKRQLVTLFSAPNYCGEFDNAGAMMSVDESLLCSFQILKPAEKKQKYVYGAMSSGRPITPPRK... | Cofactor: Binds 2 manganese ions per subunit.
Function: Plays an important role in the control of mitosis by reversing the action of the nimA kinase.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 37176
Sequence Length: 323
EC: 3.1.3.16
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P22198 | MDPALLDDVIRRLLEVKNLKPGKNAQLSESEIKQLCAAAKEIFLQQPNLLELEAPIKICGDVHGQYSDLLRLFDYGGYPPQANYLFLGDYVDRGKQSLETICLLLAYKVKYPENFFLLRGNHECASVNRIYGFYDECKRRFSVKLWKTFTDCFNCLPVSALIDEKILCMHGGLSPELNKLEQILNLNRPTDVPDTGLLCDLLWSDPSNEATGWAINDRGVSFTFGPDKVSEFLEKHDLDLICRAHQVVEDGYEFFASRQLVTIFSAPNYCGEFDNAGAMMSVDDTLMCSFQILKPARKMMGGSTNNKSGFKSFRGW | Cofactor: Binds 2 manganese ions per subunit.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 35763
Sequence Length: 316
EC: 3.1.3.16
|
P48488 | MDDTVLDDIIKKLVSAKNGRTTKQVHLTEADIRQLCTSAKEIFLSQPNLLELEAPIKICGDVHGQFSDLLRLFEYGGYPPEANYLFLGDYVDRGKQSIETICLLLAYKIKYKENFFLLRGNHECASINRIYGFYDECKRRYNVRLWKTFTDCFNCLPVAALVDEKILCMHGGLSPELKNLDQIRNIARPIDVPDHGLLCDLLWADPDKDLEGWGENDRGVSFTFGADKVVEFLEHHDLDLICRAHQVVEDGYEFFAKRKLVTVFSAPNYCGEFDNAGAMMSVDDSLTCSFQILKSSDKKGKVGFGNNSSRPGTPPHKGGK... | Cofactor: Binds 2 manganese ions per subunit.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 36248
Sequence Length: 321
EC: 3.1.3.16
|
O04951 | MPPATGDIDRQIEQLMECKALSETEVKMLCEHAKTILVEEYNVQPVKCPVTVCGDIHGQFYDLIELFRIGGSSPDTNYLFMGDYVDRGYYSVETVSLLVALKVRYRDRLTILRGNHESRQITQVYGFYDECLRKYGNANVWKHFTDLFDYLPLTALIESQVFCLHGGLSPSLDTLDNIRSLDRIQEVPHEGPMCDLLWSDPDDRCGWGISPRGAGYTFGQDIATQFNHTNGLSLISRAHQLVMEGFNWCQEKNVVTVFSAPNYCYRCGNMAAILEIGENMDQNFLQFDPAPRQVEPETTRKTPDYFL | Cofactor: Binds 2 manganese ions per subunit.
Function: Associates with the serine/threonine-protein phosphatase PP2A regulatory subunits A and B' to positively regulates beta-oxidation of fatty acids and protoauxins in peroxisomes by dephosphorylating peroxisomal beta-oxidation-related proteins . Involved in the posit... |
O04860 | MSSSDLVAASIQGNLDEQISQLMQCKPLSEPDVRALCEKAKEILAEESNVQPVKSPVTICGDIHGQFHDLAELFRIGGQCPDTNYLFMGDYVDRGYYSVETVTLLVALKVRYPQRLTILRGNHESRQITQVYGFYDECLRKYGNANVWKTFTDLFDYFPLTALVESEIFCLHGGLSPSIETLDNVRSFDRVQEVPHEGAMCDLLWSDPDDCCGWGMSPRGAGYTFGQDISEQFHQTNNLKLIARAHQLVMEGYNWSHEQKVVTIFSAPNYCYRCGNMASILEVDDCRGHTFIQFDPAPRRGEPDVTRRTPDYFL | Cofactor: Binds 2 manganese ions per subunit.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 35640
Sequence Length: 314
Subcellular Location: Cytoplasm
EC: 3.1.3.16
|
P67775 | MDEKVFTKELDQWIEQLNECKQLSESQVKSLCEKAKEILTKESNVQEVRCPVTVCGDVHGQFHDLMELFRIGGKSPDTNYLFMGDYVDRGYYSVETVTLLVALKVRYRERITILRGNHESRQITQVYGFYDECLRKYGNANVWKYFTDLFDYLPLTALVDGQIFCLHGGLSPSIDTLDHIRALDRLQEVPHEGPMCDLLWSDPDDRGGWGISPRGAGYTFGQDISETFNHANGLTLVSRAHQLVMEGYNWCHDRNVVTIFSAPNYCYRCGNQAAIMELDDTLKYSFLQFDPAPRRGEPHVTRRTPDYFL | Cofactor: Binds 2 manganese ions per subunit.
Function: PP2A is the major phosphatase for microtubule-associated proteins (MAPs) . PP2A can modulate the activity of phosphorylase B kinase casein kinase 2, mitogen-stimulated S6 kinase, and MAP-2 kinase . Cooperates with SGO2 to protect centromeric cohesin from separase-... |
P63330 | MDEKLFTKELDQWIEQLNECKQLSESQVKSLCEKAKEILTKESNVQEVRCPVTVCGDVHGQFHDLMELFRIGGKSPDTNYLFMGDYVDRGYYSVETVTLLVALKVRYRERITILRGNHESRQITQVYGFYDECLRKYGNANVWKYFTDLFDYLPLTALVDGQIFCLHGGLSPSIDTLDHIRALDRLQEVPHEGPMCDLLWSDPDDRGGWGISPRGAGYTFGQDISETFNHANGLTLVSRAHQLVMEGYNWCHDRNVVTIFSAPNYCYRCGNQAAIMELDDTLKYSFLQFDPAPRRGEPHVTRRTPDYFL | Cofactor: Binds 2 manganese ions per subunit.
Function: PP2A is the major phosphatase for microtubule-associated proteins (MAPs) (By similarity). PP2A can modulate the activity of phosphorylase B kinase casein kinase 2, mitogen-stimulated S6 kinase, and MAP-2 kinase (By similarity). Cooperates with SGO2 to protect cent... |
Q0P594 | MDDKAFTKDLDQWVEQLNECKQLNENQVRTLCEKAKEILTKESNVQEVRCPVTVCGDVHGQFHDLMELFRIGGKSPDTNYLFMGDYVDRGYYSVETVTLLVALKVRYPERITILRGNHESRQITQVYGFYDECLRKYGNANVWKYFTDLFDYLPLTALVDGQIFCLHGGLSPSIDTLDHIRALDRLQEVPHEGPMCDLLWSDPDDRGGWGISPRGAGYTFGQDISETFNHANGLTLVSRAHQLVMEGYNWCHDRNVVTIFSAPNYCYRCGNQAAIMELDDTLKYSFLQFDPAPRRGEPHVTRRTPDYFL | Cofactor: Binds 2 manganese ions per subunit.
Function: Catalytic subunit of protein phosphatase 2A (PP2A), a serine/threonine phosphatase involved in the regulation of a wide variety of enzymes, signal transduction pathways, and cellular events. PP2A can modulate the activity of phosphorylase B kinase, casein kinase 2... |
G5EGK8 | MAAAPPSADPLDKALIVDVDQWIEQLYECKPLSENQVKTLCEKAKEILEKEPNVQEVRCPVTVCGDVHGQFHDLMELFKMGGKSPDTNYLFMGDYVDRGYYSVETVSLLVCLKIRYKDRVTLLRGNHESRQITQVYGFYDECLRKYGNSNVWKYFTDLFDCFPLTALVDGQIFCLHGGLSPSIDTLDHIRALDRIQEVPHEGPMCDLLWSDPDDRGGWGISPRGAGYTFGQDISETFNHSNGLTLISRAHQLVMEGYNWSHDRNVVTVFSAPNYCYRCGNQAAMVELDDDLKYSFLQFDPAPRRGEPHVTRRTPDYFL | Cofactor: Binds 2 manganese ions per subunit.
Function: Protein phosphatase which plays an essential role in early embryonic cell division . Probably together with constant regulatory subunit paa-1 and regulatory subunit sur-6, positively regulates centriole duplication by preventing the degradation of sas-5 and kinase... |
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