ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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Q9KSG1 | MTIWVLSLAMKNTIYHAPLTFGLYALAGVLFALYTSRVCPFLATLSTREIATQVGAVFILAWLIRHTLLRQHIWARKQQFIQLDTALLFAMSLPLALYYNLQYQFTLDSNLKVLFGMTLFGFFTGALLQLSSKLRTLRQMPQSQNLALSSDERRSLVKQLIGLIVLLISTLTVMLSMVAIKDIHWLENNPARLLDGSGKISIVKEFAFLSLVLGGYITAILVLWSRMMKEILDHQERSLQAVTQGNLQVRLPVYSNDELGNVAMLTNQMLDSLEATQNEVKTTRDVAIVSLSALAESRDNETGAHILRTQEYVKALAEYL... | Function: Phosphodiesterase (PDE) that catalyzes the hydrolysis of cyclic diguanylate (c-di-GMP) to GMP in vitro. Increases motility and decreases biofilm formation in vivo.
Catalytic Activity: 3',3'-c-di-GMP + 2 H2O = 2 GMP + 2 H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 54566
Sequence Leng... |
Q9HV27 | MESMLDRPEQELVLVVDDTPDNLLLMRELLEEQYRVRTAGSGPAGLRAAVEEPRPDLILLDVNMPGMDGYEVCRRLKADPLTRDIPLMFLTARADRDDEQQGLALGAVDYLGKPVSPPIVLARVRTHLQLKANADFLRDKSEYLELEVRRRTRQLQQLQDAVIEALATLGDLRDNPRSRHLPRIERYVRLLAEHLAAQRAFADELTPEAVDLLSKSALLHDIGKVAVPDRVLLNPGQLDAADTALLQGHTRAGRDALASAERRLGQPSGFLRFARQIAYSHHERWDGRGFPEGLAGERIPLAARIVALADRYDELTSRHA... | Function: Phosphodiesterase (PDE) that catalyzes the hydrolysis of cyclic diguanylate (c-di-GMP) to GMP . Hydrolyzes c-di-GMP to GMP in a two-step reaction, via the linear intermediate 5'-phosphoguanylyl(3'->5')guanosine (pGpG). In vitro, can use pGpG as an alternative substrate and hydrolyze it into GMP . Acts in regu... |
Q9KSB1 | MATANIAIKQNSSTNIAFIERMPSPSLHRILYNLFSKFSYSLSNSCHFNLKCLNFVMNRMFHMSMEDLSQCTILIVDDSPDNIAFMSQGLAQYYRIKAARSGKVALEILAQYPIDLVLLDIVMPEMSGYEVINQIKHNPHTEHIPVIFLTGKSNPEDEQLGFELGAVDYVFKPVSIPLLKSRVHTHLQNKRSKDILLNQNDYLETEVLRRSGELDRMQDAVVFALASLAETRDPETGNHLLRTQHYVKVLAQRLATTDKYRDVLSPTVIDTYFKAAPLHDIGKVGIPDNILLKPGKLTPDEFTTMRNHALLGKLALEKAE... | Function: Probable phosphodiesterase (PDE) that catalyzes the hydrolysis of cyclic diguanylate (c-di-GMP). Increases motility and decreases biofilm formation in vivo.
Catalytic Activity: 3',3'-c-di-GMP + 2 H2O = 2 GMP + 2 H(+)
Sequence Mass (Da): 49422
Sequence Length: 441
EC: 3.1.4.-
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Q9I0R8 | MATPPYPEDEHSRQAYVDQLGLLEEGADEVFEEILAAATSYFQTPIALISILDHQRQWFRASIGLDIRQTPRRDSFCAYAILGKGVFEVADATLDPRFRDNPYVQGEPRIRFYAGAPLATAEGLNLGSLCVIDREPRGPLAERDVAMLEHFARLVMARIHTLRSTNYIDEPTGLYNRLRLQEDVSLRLQRDGALTVIAADLLPLALLNTIIRTLGYPFSNDLMLEARDRIRAELPDFTLYKISPTRFGLLLPRQQQEETESVCLRLLRAFESPVVCRGIPIKANVGLGVLPLADDTLDGDQDWLRLVVSAADDARDRGVG... | Function: Phosphodiesterase (PDE) that catalyzes the hydrolysis of cyclic diguanylate (c-di-GMP) to 5'-pGpG.
Catalytic Activity: 3',3'-c-di-GMP + H2O = 5'-phosphoguanylyl(3'->5')guanosine + H(+)
Sequence Mass (Da): 65618
Sequence Length: 587
Domain: The EAL domain contains a functional active site loop (loop 6), which ... |
Q9WY30 | MTVLIVEDDDITREAMGQYLKLSGFNVIEAENGEKAVELSENVDVALVDVMLPGMSGIEVVNKIKAKNPSCVVFVVTAYDDTEIVKKCVEAGADDFIKKPVNLELLRLKITHALRNRVFHMYRNSYLKSLKKKLFLLEKTAEEFFTEYEDFLFEVLEILNMLSEYRDMETHRHTERVGWLSGRIAEEMGMSEVFVTEIQFAAPLHDIGKIGIPDRILLKPGILTPEEFEIMKQHTTIGFRILSRSNSPILQLGAEIALTHHERWDGSGYPRGLKEREIPISGLIVAVADSFDAMVSRRPYKNPKPLEEAFREIESLSGKL... | Function: Phosphodiesterase (PDE) that catalyzes the hydrolysis of cyclic diguanylate (c-di-GMP) to GMP. Hydrolyzes c-di-GMP to GMP in a two-step reaction, via the linear intermediate 5'-phosphoguanylyl(3'->5')guanosine (pGpG).
Catalytic Activity: 3',3'-c-di-GMP + 2 H2O = 2 GMP + 2 H(+)
Sequence Mass (Da): 41788
Sequen... |
Q06850 | MGNTCVGPSRNGFLQSVSAAMWRPRDGDDSASMSNGDIASEAVSGELRSRLSDEVQNKPPEQVTMPKPGTDVETKDREIRTESKPETLEEISLESKPETKQETKSETKPESKPDPPAKPKKPKHMKRVSSAGLRTESVLQRKTENFKEFYSLGRKLGQGQFGTTFLCVEKTTGKEFACKSIAKRKLLTDEDVEDVRREIQIMHHLAGHPNVISIKGAYEDVVAVHLVMECCAGGELFDRIIQRGHYTERKAAELTRTIVGVVEACHSLGVMHRDLKPENFLFVSKHEDSLLKTIDFGLSMFFKPDDVFTDVVGSPYYVAP... | Function: May play a role in signal transduction pathways that involve calcium as a second messenger. Phosphorylates the Ca(2+)-ATPase ACA2 resulting in the inhibition of its calcium activation.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Lipid-anchor
Sequen... |
P0ABG2 | MLKYRLISAFVLIPVVIAALFLLPPVGFAIVTLVVCMLAAWEWGQLSGFTTRSQRVWLAVLCGLLLALMLFLLPEYHRNIHQPLVEISLWASLGWWIVALLLVLFYPGSAAIWRNSKTLRLIFGVLTIVPFFWGMLALRAWHYDENHYSGAIWLLYVMILVWGADSGAYMFGKLFGKHKLAPKVSPGKTWQGFIGGLATAAVISWGYGMWANLDVAPVTLLICSIVAALASVLGDLTESMFKREAGIKDSGHLIPGHGGILDRIDSLTAAVPVFACLLLLVFRTL | Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphate + CTP + H(+) = a CDP-1,2-diacyl-sn-glycerol + diphosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31454
Sequence Length: 285
Pathway: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phospha... |
P44937 | MLKQRVLSAIVLIAAVLCALFLFTPFYFALALGAVAILGIWEWTQFARLKQPLIRFFVTTFLGVFIFLWLYTEGNYLDAGRVFEQHLQLLLINAVSWWGLALLLVISYPKSAKFWSKNPLLQLLFAFSTLIPFVAGVLRLRLEHYTHDPYHGLFLLLYVFILVWAADSGAYFSGRAFGKRKLAPKVSPGKSWEGVIGGLITALVLAFIFIHFSNNTLVGDRNITGFIILSVATVAISVLGDLTESMFKRESGVKDSSQLIPGHGGVLDRIDSLTAAVPFFSYFYFFVL | Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphate + CTP + H(+) = a CDP-1,2-diacyl-sn-glycerol + diphosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32247
Sequence Length: 288
Pathway: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phospha... |
O25004 | MKEELFKEKSRYITGFVLIIVADLILYADNLLLFWAVLGGIYAVGFSEALRLFQVKASFSLYLILVLSWVAAYFNGRPIECALISAMVMASVIAYQKAHHSEAILPFLYPGVGFFALFGVYKDFGAVAIIWLLVVVVASDVGAFFGGKLLGKTPFTPTSPNKTLEGALIGVVLASVLGSFVGMGKLSGGFFMALFFSFLIALVAVFGDLYESYLKRKVGIKDSGKILPGHGGVLDRLDSMLFGALGLHALLYFLEIWKETAVFLGD | Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphate + CTP + H(+) = a CDP-1,2-diacyl-sn-glycerol + diphosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28899
Sequence Length: 266
Pathway: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phospha... |
Q49433 | MNEKAKQFIKKRTSVFIALLVVFCFFLLISAFADGFNFWSPWSADFNSRTLKVEQASGVTSVISTEINENFKAVRFSFSIIIILIVGVIGSLMIWELFTNILKNKPKLSLSLTLLNAGIIIFGMIGTFVVVYFYKWNATVNGIWTLSFTLSVVLLWIIYIACMSKTRIKFSLQLSYSLGAIACFIASIGTIYFSVIRGWTTIFLLMSLAVSVDTFSFLFGKRFGKNPLIKISPSKTWEGAFFGIISTIVVVALLCVLYSIPFFVAKPTFNQTNGIALNTPQNYDSHNLITNIFLIAFISGGSSFYIYWWVSTLALIFTGS... | Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphate + CTP + H(+) = a CDP-1,2-diacyl-sn-glycerol + diphosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 44484
Sequence Length: 397
Pathway: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phospha... |
P9WPF6 | MSWLNTKKASCWRSSGRSATKSVTTNDAGTGNPAEQPARGAKQQPATETSRAGRDLRAAIVVGLSIGLVLIAVLVFVPRVWVAIVAVATLVATHEVVRRLREAGYLIPVIPLLIGGQAAVWLTWPFGAVGALAGFGGMVVVCMIWRLFMQDSVTRPTTGGAPSPGNYLSDVSATVFLAVWVPLFCSFGAMLVYPENGSGWVFCMMIAVIASDVGGYAVGVLFGKHPMVPTISPKKSWEGFAGSLVCGITATIITATFLVGKTPWIGALLGVLFVLTTALGDLVESQVKRDLGIKDMGRLLPGHGGLMDRLDGILPSAVAA... | Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphate + CTP + H(+) = a CDP-1,2-diacyl-sn-glycerol + diphosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34458
Sequence Length: 328
Pathway: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phospha... |
Q59640 | MLKQRIITALVLLPIALGGFFLLEGAFFALFIGAVVSLGAWEWARLAGYEQQFGRVAYAATVAVLMVALYHLPQLAGAVLLLALVWWTLATVLVLTYPESVGYWGGRWRRLGMGLLILLPAWQGLVLLKQWPLANGLIIAVMVLVWGADIGAYFSGKAFGKRKLAPRVSPGKSWEGVYGGLAASLAITLAVGLYRGWSLGALLLALLGAALVVFVSIVGDLTESMFKRQSGIKDSSNLLPGHGGVLDRIDSLTAAIPVFAALLWAAGWGAP | Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphate + CTP + H(+) = a CDP-1,2-diacyl-sn-glycerol + diphosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28856
Sequence Length: 271
Pathway: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phospha... |
Q9ZDA8 | MITQKEKEHLAKDKQNIYLRIISGIALVSLFVIAILCLKTLFYILMILVGLGMLSEWYNMTYPSINYLLIGLIIIPIPISLLIFLSMEESNRLVIMLYFCILWSVDTFAMIGGKTFKGIKLAPKISPKKTWTGLITGTVSAGLVSVLVSLIPNYHIEHYYFSNKIYLFIISCILALIAQSSDLFISYFKRKFNIKDSGHIIPGHGGVLDRFDSIILTAPVFFCINIYL | Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphate + CTP + H(+) = a CDP-1,2-diacyl-sn-glycerol + diphosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 25814
Sequence Length: 228
Pathway: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phospha... |
P43241 | MYVSYLLDKDVSMYPSSVRHSGGLNLAPQNFVSPPQYPDYGGYHVAAAAAATANLDSAQSPGPSWPTAYGAPLREDWNGYAPGGAAAANAVAHGLNGGSPAAAMGYSSPAEYHAHHHPHHHPHHPAASPSCASGLLQTLNLGPPGPAATAAAEQLSPSGQRRNLCEWMRKPAQQSLGSQVKTRTKDKYRVVYTDHQRLELEKEFHFSRYITIRRKSELAATLGLSERQVKIWFQNRRAKERKIKKKQQQQQQQQQQQPPQPPPQPSQPQPGALRSVPEPLSPVTSLQGSVPGSVPGVLGPAGGVLNSTVTQ | Function: Transcription factor which regulates the transcription of multiple genes expressed in the intestinal epithelium . Binds to the promoter of the intestinal sucrase-isomaltase SI and activates SI transcription . Binds to the DNA sequence 5'-ATAAAAACTTAT-3' in the promoter region of VDR and activates VDR transcri... |
Q9Y232 | MTFQASHRSAWGKSRKKNWQYEGPTQKLFLKRNNVSAPDGPSDPSISVSSEQSGAQQPPALQVERIVDKRKNKKGKTEYLVRWKGYDSEDDTWEPEQHLVNCEEYIHDFNRRHTEKQKESTLTRTNRTSPNNARKQISRSTNSNFSKTSPKALVIGKDHESKNSQLFAASQKFRKNTAPSLSSRKNMDLAKSGIKILVPKSPVKSRTAVDGFQSESPEKLDPVEQGQEDTVAPEVAAEKPVGALLGPGAERARMGSRPRIHPLVPQVPGPVTAAMATGLAVNGKGTSPFMDALTANGTTNIQTSVTGVTASKRKFIDDRR... | Function: Chromatin reader protein that recognizes and binds histone H3 trimethylated at 'Lys-9', dimethylated at 'Lys-27' and trimethylated at 'Lys-27' (H3K9me3, H3K27me2 and H3K27me3, respectively) . Part of multimeric repressive chromatin complexes, where it is required for transmission and restoration of repressive... |
Q9WTK2 | MGIGNSQPNSQEAQLCTLPEKAEQPTDDNTCQQNNVVPATVSEPDQASPAIQDAETQVESIVDKRKNKKGKTEYLVRWKGYDSEDDTWEPEQHLVNCEEYIHDFNRRHNERQKEGSLARASRASPSNARKQISRSTHSTLSKTNSKALVVGKDHESKSSQLLAASQKFRKNPAPSLANRKNMDLAKSGIKILVPKSPVKGRTSVDGFQGESPEKLDPVDQGAEDTVAPEVTAEKPTGALLGPGAERARMGSRPRIHPLVPQVSGPVTAAMATGLAVNGKGTSPFMDALAANGTVTIQTSVTGVTAGKRKFIDDRRDQPFD... | Function: Chromatin reader protein that recognizes and binds histone H3 trimethylated at 'Lys-9', dimethylated at 'Lys-27' and trimethylated at 'Lys-27' (H3K9me3, H3K27me2 and H3K27me3, respectively) . Part of multimeric repressive chromatin complexes, where it is required for transmission and restoration of repressive... |
Q07730 | MKFSKIACATVFALSSQAAIIHHAPEFNMKRDVAPAAPAAPADQAPTVPAPQEFNTAITKRSIIGIIMGILGNIPQVIQIIMSIVKAFKGNKREDIDSVVAGIIADMPFVVRAVDTAMTSVASTKRDGANDDVANAVVRLPEIVARVATGVQQSIENAKRDGVPDVGLNLVANAPRLISNVFDGVSETVQQAKRDGLEDFLDELLQRLPQLITRSAESALKDSQPVKRDAGSVALSNLIKKSIETVGIENAAQIVSERDISSLIEEYFGKA | Function: Secreted protein cleaved by KEX2 in 8 similar peptides (ECE1-I to ECE1-VIII) . Stimulates biofilm formation .
PTM: Cleavage by KEX2 generates 8 peptides ECE1-I to ECE1-VIII, all terminating in Lys-Arg . Only peptide ECE1-III, called candidalysin, shows toxin activity .
Location Topology: Single-pass membrane ... |
C5M337 | MKFSKVASFAFLALSSQAALIQHDVIIENIKRDAVLAGSAENNIASSAFTKRESEVDSSEDVQLEKRISFAGIVSSIINQLPSIIQIIGNIIKAGLVKRDDIDDAFALVLAEYPHIVSVFEDAFGDFTEAKRDEAASVGTQILGSFPSILTQVVNGFSKVLDFANSDTFSTGLSILSNFTSIASSFASSLSSVVQNGKRDGVEDIVSMVVRQIPDLIVEASTPFVTNAEKMKRDADVAASLVDNLVKKGLSTAIDTFGAATVASVVSKRQVSSFLSKVLSKA | Function: Secreted protein cleaved by KEX2 in 8 similar peptides (ECE1-I to ECE1-VIII). Stimulates biofilm formation.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 29977
Sequence Length: 282
Domain: The N-terminal alpha-helix of peptide ECE1-III allows insertion of the toxin into host epithelial c... |
Q5B7R2 | MALLLSLSLLATTISAQQIGTPEIRPRLTTYHCTSANGCTEQNTSVVLDAATHPIHDASNPSVSCTTSNGLNPALCPDKQTCADNCVIDGITDYAAHGVETHGSRLTLTQYRNVNGALSSVSPRVYLVDESDPDEQEYRALSLLAQEFTFTVNVSALPCGMNGALYLSEMSPSGGRSALNPAGASYGTGYCDAQCYVNPWINGEGNINGYGACCNEMDIWEANSRSTGFTPHACLYEPEETEGRGVYECASEDECDSAGENDGICDKWGCGFNPYALGNTEYYGRGQGFEVDTKEPFTVVTQFLTDDGTSTGALTEIRRL... | Function: Has endoglucanase activity on substrates containing beta-1,4 glycosidic bonds, like in carboxymethylcellulose (CMC), hydroxyethylcellulose (HEC) and beta-glucan. Involved in the degradation of complex natural cellulosic substrates.
Catalytic Activity: Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cel... |
Q9CJ32 | MNGITAWMEKYLVPVAAKIGSQKHLVALRDSFIGMLPATLAGALAAMISAIVTTFPSAIQQMMLGATAFSKLAPEKVWTLANTPIIGDLNNISALVNQGTLTVIGLIFAFSWGYNLARAYGVNDLAGGIVSLATLFAGLPNQMGKFTAALGTGKAGVAATDKLNGVLGDQGLAAWKPLFASAHLDAGAYFTVIIMGALAVIIYAKLMLADITIKMPESVPPAVAKAFLAIIPTIAALYIVGLIYYIIGKLTNDSVINLITHYIAEPFQILSQNIFSVLIVTLFVSVFWFFGLHGPNVLAPVLDGIWGPLGLNNQALYFQV... | Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitant with their translocation across the cell membrane (By similarity). Involved in cellobiose transport with PtcA and PtcB. ... |
A0A0U4EBH5 | MNKWHINKWYFFVGMLVIFAVIISLILKDTSLTFSSYDREKFPHLIGNSMVKKPSLAGRLKIIEIDGRKTLGDQHGNPIQLRGMSTHGLQWFPQIINNNAFSALSKDWEANVIRLAMYVGEGGYSTDPSVKEKVIEGINLAIKNDMYVIVDWHILNPGDPNAKIYSGAKEFFKEIASKYPNDLHIIYELANEPNPTESDITNDIAGWEKVKKYAEPIIKMLRDMGNENIIIVGNPEWSTRPDLAVNDPIDDKNVMYSAHFYTGSASVWENGNKGHIARNIEKALENGLTVFVTEWGTSEASGDGGPYLNEADEWLEFLNS... | Function: Thermostable endoglucanase that has high activity with soluble polymeric substrates containing beta-1,4-glycosidic bonds, such as carboxymethyl cellulose (CMC) and barley beta-D-glucan (in vitro). Has no activity with cellobiose and filter paper. Has no activity with substrates containing beta-1,3-linked glyc... |
P10477 | MKKIVSLVCVLVMLVSILGSFSVVAASPVKGFQVSGTKLLDASGNELVMRGMRDISAIDLVKEIKIGWNLGNTLDAPTETAWGNPRTTKAMIEKVREMGFNAVRVPVTWDTHIGPAPDYKIDEAWLNRVEEVVNYVLDCGMYAIINVHHDNTWIIPTYANEQRSKEKLVKVWEQIATRFKDYDDHLLFETMNEPREVGSPMEWMGGTYENRDVINRFNLAVVNTIRASGGNNDKRFILVPTNAATGLDVALNDLVIPNNDSRVIVSIHAYSPYFFAMDVNGTSYWGSDYDKASLTSELDAIYNRFVKNGRAVIIGEFGTI... | Function: Multifunctional enzyme involved in the degradation of plant cell wall polysaccharides. Displays endoglucanase activity against carboxymethyl cellulose (CMC) and barley beta-glucan . Also catalyzes the deacetylation of acetylated birchwood xylan and glucomannan, with a preference for the latter, and of the syn... |
P0DQY9 | MAPSQKALLVLVLSMLLTASDSRARRIDCTRFVYAPICRGVAAKRGGDSLSVGASTELDDALTDPFLRSEEPREEDTEKKWRELSRLSRVLQILLSHPTGETEQLDRLLTL | Function: May mimic the function of prey elevenin neuropeptide. In vivo, intracranial injection in mice induces hyperactivity.
Sequence Mass (Da): 12383
Sequence Length: 111
Domain: The cysteine framework is C-C.
Subcellular Location: Secreted
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A0A0F7YZQ7 | MAPSQKALLVLVLSMLLTASDSWARRIDCKVFVFAPICRGVAAKRGGDSLSVGGSAELDDALTDPFLRSEEPREWRELTRLSRVLQTFLSHPTGETEQHD | Function: May mimic the function of prey elevenin neuropeptide. In vivo, intracranial injection in mice induces hyperactivity (tested at 5 and 10 nM).
Sequence Mass (Da): 11056
Sequence Length: 100
Domain: The cysteine framework is C-C.
Subcellular Location: Secreted
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Q92879 | MNGTLDHPDQPDLDAIKMFVGQVPRTWSEKDLRELFEQYGAVYEINVLRDRSQNPPQSKGCCFVTFYTRKAALEAQNALHNMKVLPGMHHPIQMKPADSEKNNAVEDRKLFIGMISKKCTENDIRVMFSSFGQIEECRILRGPDGLSRGCAFVTFTTRAMAQTAIKAMHQAQTMEGCSSPMVVKFADTQKDKEQKRMAQQLQQQMQQISAASVWGNLAGLNTLGPQYLALYLQLLQQTASSGNLNTLSSLHPMGGLNAMQLQNLAALAAAASAAQNTPSGTNALTTSSSPLSVLTSSGSSPSSSSSNSVNPIASLGALQT... | Function: RNA-binding protein implicated in the regulation of several post-transcriptional events. Involved in pre-mRNA alternative splicing, mRNA translation and stability. Mediates exon inclusion and/or exclusion in pre-mRNA that are subject to tissue-specific and developmentally regulated alternative splicing. Speci... |
P28659 | MNGTLDHPDQPDLDAIKMFVGQVPRTWSEKDLRELFEQYGAVYEINILRDRSQNPPQSKGCCFVTFYTRKAALEAQNALHNMKVLPGMHHPIQMKPADSEKNNAVEDRKLFIGMISKKCTENDIRVMFSSFGQIEECRILRGPDGLSRGCAFVTFTTRTMAQTAIKAMHQAQTMEGCSSPMVVKFADTQKDKEQKRMAQQLQQQMQQISAASVWGNLAGLNTLGPQYLALYLQLLQQTASSGNLNTLSSLHPMGGLNAMQLQNLAALAAAASAAQNTPSGTNALTTSSSPLSVLTSSGSSPSSSSSNSVNPIASLGALQT... | Function: RNA-binding protein implicated in the regulation of several post-transcriptional events. Involved in pre-mRNA alternative splicing, mRNA translation and stability. Mediates exon inclusion and/or exclusion in pre-mRNA that are subject to tissue-specific and developmentally regulated alternative splicing (By si... |
Q28HE9 | MNGTMDHPDHPDPDSIKMFVGQVPRSWSEKELRELFEQYGAVYEINVLRDRSQNPPQSKGCCFITFYTRKAALEAQNALHNMKVLPGMHHPIQMKPADSEKNNAVEDRKLFVGMVSKKCNENDIRAMFSQFGQIEESRILRGPDGMSRGCAFVTFTTRSMAQMAIKAMHQAQTMEGCSSPIVVKFADTQKDKEQKRMTQQLQQQMQQLNAASMWGNLAGLSSLAPQYLALLQQTASSGNLNSLSGLHPMGGEYATGMTSGLNAMQLQNLAALAAAASAAQNTPSAGSALTTSSSPLSILTSSGSSPSSNNNSAVNPMASL... | Function: RNA-binding protein implicated in the regulation of several post-transcriptional events. May be involved in pre-mRNA alternative splicing, mRNA translation activation and stability (By similarity). Mediates the rapid and sequence-specific cytoplasmic deadenylation of EDEN-containing maternal mRNAs following f... |
Q7Z7K6 | MRRSRSSAAAKLRGQKRSGASGASAAPAASAAAALAPSATRTRRSASQAGSKSQAVEKPPSEKPRLRRSSPRAQEEGPGEPPPPELALLPPPPPPPPTPATPTSSASNLDLGEQRERWETFQKRQKLTSEGAAKLLLDTFEYQGLVKHTGGCHCGAVRFEVWASADLHIFDCNCSICKKKQNRHFIVPASRFKLLKGAEHITTYTFNTHKAQHTFCKRCGVQSFYTPRSNPGGFGIAPHCLDEGTVRSMVTEEFNGSDWEKAMKEHKTIKNMSKE | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Required for distribution of pericentromeric heterochromatin in interphase nuclei and for centromere formation and organization, chromosome alignment and cytokinesis.
Sequence Mass (Da): 29946
Sequence Length: 275
Subcellular Location: Chromosome
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Q9CXS4 | MRRTRSAVATGPREQRRSGATGGLSGGESRAQRSRSRTRAGAGGGGGAVGPQPSAKPRPKPPPRAQEAAAEEPPPAVTPAASVSALDLGEQRERWETFQKRQRLSFEGAAKLLLDTFEYQGLVKHTGGCHCGAVRFEVWASADLHIFDCNCSICKKKQNRHFIVPASRFKLLKGAESITTYTFNTHKAQHTFCKRCGVQSFYTPRSNPGGFGIAPHCLDEGTVRSVVTEEFNGSDWERAMKEHKTIKNMSKE | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Required for distribution of pericentromeric heterochromatin in interphase nuclei and for centromere formation and organization, chromosome alignment and cytokinesis.
Sequence Mass (Da): 27541
Sequence Length: 252
Subcellular Location: Chromosome
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Q69XK5 | MDGESPEIMPVECPDPEPASSESGDDHDIPEPLSSRLSVPSGELNLYRAAVALRLVLLAAFFRYRVTRPVADAHALWVTSVACELWLAASWLIAQLPKLSPANRVTYLDRLASRYEKGGEASRLAGVDVFVAAADAAREPPLATANTVLSVLAADYPAGGVACYVHDDGADMLVFESLFEAAGFARRWIPFCRRHGVEPRAPELYFARGVDYLRDRAAPSFVKDRRAMKREYEEFKVRMNHLAARARKVPEEGWIMSDGTPWPGNNSRDHPAMIQVLLGHPGDRDVDGGELPRLFYVSREKRPGFRHHGKAGAMNALLRV... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Catalytic subunit of cellulose synthase terminal complexes ('rosettes'), required for beta-1,4-glucan microfibril crystallization, a major mechanism of the cell wall formation.
Catalytic Activity: [(1->4)-beta-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->4)-beta-D-glu... |
Q9RLB8 | MKKHFVVGETIKRFLRIGTSLALSISTLSLLPSAPRLSSAAGTIKIMPLGDSITYGMADEGGYRKYLSYFLQQKGYTNVDLVGPEGKDSASFNYNGQSVKYDDNHAGYSGYTITNLPGGWFGQLNGILETMQGGDYIKKYSPDIILLQIGTNDVSNGHLDGSEERLHKLLDYLRENMPSNGKVFLTTIPDLGNSGWGGNSNGDIAKYNELIKKVANDYSSKNVIYADIHSVIDASKDLADGVHPNAGGYEKMGKYWLEQIEGYLKASDGPQQTQPTQPSQGDSGPELIYGDLDGDKTITSFDAVIMRKGLINDFKDNNVK... | Function: Esterase involved in the degradation of plant cell wall polysaccharides. Catalyzes the deacetylation of chemically acetylated xylan and native, steam-extracted xylan . Seems to act in synergy with the xylanase XynD which produces xylo-oligosaccharides . Also catalyzes the deesterification of methyl esters of ... |
A0A4Y5X186 | MKCSVLQMSRLSWAMCLMLLMLLLLGTAQGCFIRNCPRGGKRAVDALQPTRQCMSCGPDGVGQCVGPSVCCGLGLGCLMGTPETEVCQKENESSVPCAISGRHCGMDNTGNCVADGICCVEDACSFNSLCRVDTDQEDSVSARQELLTLIRRLLVNRQYD | Function: Targets vasopressin-oxytocin related receptors.
Sequence Mass (Da): 17194
Sequence Length: 160
Domain: The cysteine framework of the conopressin is C-C.
Subcellular Location: Secreted
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A0A4Y5X1A7 | ACFIRNCPKGGKRNVDEGPTKPCMFCSFGQCVAPHTCCGEKGCEMGTVDANMCQEENESPIPCHVFGKRCLLNHPGNSHGNCVTYGICCSHDTCTVHLACM | Function: Targets vasopressin-oxytocin related receptors. Is more active on fish receptors than on their human counterparts, supporting an evolved role of this conopressin in the envenomation process. Acts as an agonist on zebrafish vasopressin receptors V1a1R (EC(50)=10.6 nM), V1a2R (EC(50)=44.06 nM, partial agonist),... |
P05486 | MTRSAMQMGRLTLVLCLLLLLLLTTQACFIRNCPKGGKRDVDERYLFKACMSCSFGQCVGPRICCGPRGCEMGTAEANRCIEEDEDPIPCQVVGQHCDLNNPGNIHGNCVANGICCVDDTCTIHTGCL | Function: Targets vasopressin-oxytocin related receptors . Is more active on fish receptors than on their human counterparts, supporting an evolved role of this conopressin in the envenomation process . Acts as an agonist on zebrafish vasopressin receptors V1a1R (EC(50)=10.6 nM), V1a2R (EC(50)=44.06 nM, partial agonist... |
Q5VQK9 | MALLSPPSPPPPLPPLRRRPASPTLLAVATRPSSLLSLPHCHCGLPLPSTANARAYSRSSRRRRRVAASLGQDEPGVSDTAVAPEGEGDSEPPASSDGAAGDIAASAEQPEASPEDLEDIRQVKRVLELLQKNRDMTFGEVKLTIMIEDPRDIERKRLLGIEDPDEITRDDLADALVEVNEGRIPENRVALQLLAKEMTEWPDLEMEAPKKKSKPGKSVYAKATDTGIDPETAAKRLNIDWDSAADLDDEEEEDDETEVPSAVGYSALYLLTAFPVIIGISVVLILFYNSLQ | Function: Involved in light-induced chloroplast development and growth. Involved in the plant response to abiotic and photooxidative stresses. May be involved in the suppression of photooxidative damage.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 31747
Sequence Length: 292
Subcellular Location:... |
Q5VTT2 | MDSLDRSCQDWCDRKQHWLEIGPPDLVERKGSLTLRSHHKKYSKPVLVYSWHRDREAFPKGYDIEGPEKVKKLCNSTYRRLGTDESPIWTSETHEKLSQMCLNTEWVEMKSKALLNEETVSSGIIERVTGLPATGFGAVFPRHPPDWSKMCALTTYSEDYVPPYDYQPHAYPCQDDYSIVHRKCRSQFTDLNGSKRFGINTWHDESGIYANSDVKQKLYPLTSGPIVPI | Function: Microtubule inner protein (MIP) part of the dynein-decorated doublet microtubules (DMTs) in cilia axoneme, which is required for motile cilia beating.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 26445
Sequence Length: 229
Subcellular Location: Cytoplasm
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A2IBF8 | MSTSLSVTELQVENFTFPPTVKPPGSTKTLFLGGAGERGLEIQGKFIKFTAIGVYLEDSAVNCLGVKWKGKSAVELTESVEFFRDVVTGDFEKFIRVTMILPLTGQQYSEKVSENCVAIWKSLGIYTDAEAKAIEKFIEVFKDENFPPGSSILFTISGQGSLTIGFSKDSSVPEGGKVVIENKLLANSVLESVIGKNGVSPAAKESLASRLSPLFNDCGADSEKPQS | Function: Catalyzes the intramolecular cyclization of bicyclic chalcones into tricyclic (S)-flavanones. Responsible for the isomerization of 4,2',4',6'-tetrahydroxychalcone (also termed chalcone) into naringenin (By similarity).
Catalytic Activity: a chalcone = a flavanone.
Sequence Mass (Da): 24404
Sequence Length: 22... |
Q8S3X0 | MAVSELEVDGVVFPPLARPPGSAHAHFLAGAGVRGMEIGGHFIKFTAIGVYLQADAAVSALAAKWAGKPAADLASDAAFFRDVVTGEFEKFTRVTMILPLTGAQYSDKVTENCVAYWKAAGVYTDAEAAAVDKFKEAFGPHSFAPGASILFTHSPAGVLTVAFSKDSSVPESGGVAIENARLCEAVLESIIGEHGVSPAAKLSLANRVAELLKGAAHAGGEPAAEPVPVSV | Function: Catalyzes the intramolecular cyclization of bicyclic chalcones into tricyclic (S)-flavanones. Responsible for the isomerization of 4,2',4',6'-tetrahydroxychalcone (also termed chalcone) into naringenin.
Catalytic Activity: a chalcone = a flavanone.
Sequence Mass (Da): 23704
Sequence Length: 231
Pathway: Secon... |
Q8LKP9 | MAPPPSSTSIQVESIVFPPSVKPPGATTTLFLGGAGVRGMEIQGNFVKFTGIGVYLEDKAIPSLAVKWKGKTAAELTDSVQFYRDIVTGPFEKFSQVTMILPLTGKQYSEKVSEMCIGVWKAQGTYTDADTATIEKFLEVFKDENFLPGSSILFTTSPTGSLTISFSKDGNIPEAATVVLENRKLAQTVIESVIGEHGVSPEAKQSLASRLSDFMTQFDEKATANVESQIGL | Function: Catalyzes the intramolecular cyclization of bicyclic chalcones into tricyclic (S)-flavanones. Responsible for the isomerization of 4,2',4',6'-tetrahydroxychalcone (also termed chalcone) into naringenin.
Catalytic Activity: a chalcone = a flavanone.
Sequence Mass (Da): 24941
Sequence Length: 232
Pathway: Secon... |
O80842 | MATSSAHLSFLAGRISPFSSERIGLFPLRGEFRPRMTRFRCSAGPSGFFTRLGRLIKEKAKSDVEKVFSGFSKTRENLAVIDELLLFWNLAETDRVLDELEEALLVSDFGPKITVRIVERLREDIMSGKLKSGSEIKDALKESVLEMLAKKNSKTELQLGFRKPAVIMIVGVNGGGKTTSLGKLAHRLKNEGTKVLMAAGDTFRAAASDQLEIWAERTGCEIVVAEGDKAKAATVLSKAVKRGKEEGYDVVLCDTSGRLHTNYSLMEELIACKKAVGKIVSGAPNEILLVLDGNTGLNMLPQAREFNEVVGITGLILTKL... | Function: Signal recognition particle receptor protein. Binds GTP specifically. The GTPase activity is inhibited by the N-terminus of the protein until binding to the thylakoid membrane. Activates the GTPase activity of FFC/cpSRP54 when bound to the cpSRP complex. Required for light-harvesting chlorophyll a/b-binding p... |
A0QSS4 | MSKQIEFNETARRAMEAGVDKLADAVKVTLGPRGRHVVLAKSFGGPQVTNDGVTIAREIDLEDPYENLGAQLVKSVATKTNDVAGDGTTTATVLAQALVRAGLRNVAAGANPIALGSGISKAADAVSEALLASATPVDDKKAIAQVATVSSRDEQVGELVGEAMTKVGHDGVVTVEESSTLETYLEVTEGVGFDKGFLSAYFVTDFDSQEAVLEDALVLLHRDKISSLPDLLPLLEKVAEAGKPLLIVAEDVEGEALSTLVVNAIRKTLKAVAVKAPFFGDRRKAFLDDLAIVTGGQVVNPDVGLLLREVGLEVLGSARR... | Function: Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding.
Catalytic Activity: ATP ... |
P0C923 | MAKDIYFNEDARKSLLSGVEKLSNAVKVTLGPKGRNVLIDKKFGSPTVTKDGVSVAREIELENPFENMGAQLLKEVAIKTNDVAGDGTTTATVLAYAIAREGLKNVSSGINPIGIKKGIDHAVNLAAEKIRQSAKKITTKEEIAQVASISANNDSYIGEKIAEAMDKVGKDGVITVEESKTFDTTISYVEGMQFDRGYLSPYFSTNKENMSVNFDDAFILIYEKKISSIKELLPVLEKVLGTNKPLLIIAEDIEGDALAALVLNSVRGALKVCAIKSPGFGDRRKAMLEDIAVLTGGVLISEELGLTLETVEIEQLGQAK... | Function: Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding.
Catalytic Activity: ATP ... |
Q50826 | YEKIGAEMVKEVAKKTDDVAGDGTTTATVLAQALVKEGLRNVAAGANPLGLKRGIEKAVEKVTETLLKSAKEVETKEQIAATAAISAGEQSIGDLIAEAMDKVGNEGVITVEES | Function: Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding.
Catalytic Activity: ATP ... |
H2L0H3 | MPPRDAVPTSTQVSGIGADGVQTEKVLKNRPKASALRQQKLPAWQPILTATTVIPTVFVIGAIFLPIGVFLFIASDAVSEFTVEYTNCLSPCQLQINLPNAFDGDVFLYYNLENYYQNHRRYVKSRNDQQYLGDLTNVKDCAPFDIDPATKKPIAPCGAIANSIFNDTFTLAHRADTGIVTMVPVTTQGVIWNVDKDRKFKNPPLNDGNLCDAFNNTTKPPNWSKNPCEVGGFENVDFIVWMRTAALPYFKKLWRIVDRTTNPLFSNGLPQGTYILTVENNYPVQSFGGKKEFVISTTSWAGGKNSFLGIAYLVVGSLAI... | Function: Probable chaperone protein for the phospholipid-transporting ATPase tat-1. Regulates cell membrane structure and function. Plays a role in maintaining the membrane phosphatidylserine asymmetry and the formation of the tubular membrane structure. Involved in membrane trafficking and is specifically involved in... |
Q9SRQ2 | MDHQVSLPQSTTTGLSFKVHRQQRELVTPAKPTPRELKPLSDIDDQQGLRFQIPVIFFYRPNLSSDLDPVQVIKKALADALVYYYPFAGRLRELSNRKLAVDCTGEGVLFIEAEADVALAELEEADALLPPFPFLEELLFDVEGSSDVLNTPLLLVQVTRLKCCGFIFALRFNHTMTDGAGLSLFLKSLCELACGLHAPSVPPVWNRHLLTVSASEARVTHTHREYDDQVGIDVVATGHPLVSRSFFFRAEEISAIRKLLPPDLHNTSFEALSSFLWRCRTIALNPDPNTEMRLTCIINSRSKLRNPPLEPGYYGNVFVI... | Function: Acyltransferase involved in the production of green leaf volatiles (GLVs). Uses acetyl-CoA as substrate, but not malonyl-CoA or benzoyl-CoA. Prefers primary, medium-chain-length, aliphatic alcohols.
Catalytic Activity: (3Z)-hex-3-en-1-ol + acetyl-CoA = (3Z)-hex-3-en-1-yl acetate + CoA
Sequence Mass (Da): 5029... |
P17411 | MSQKLKVVTIGGGSSYTPELLEGFIKRYHELPVSELWLVDVEGGKPKLDIIFDLCQRMIDNAGVPMKLYKTLDRREALKDADFVTTQLRVGQLPARELDERIPLSHGYLGQETNGAGGLFKGLRTIPVIFDIVKDVEELCPNAWVINFTNPAGMVTEAVYRHTGFKRFIGVCNIPIGMKMFIRDVLMLKDSDDLSIDLFGLNHMVFIKDVLINGKSRFAELLDGVASGQLKASSVKNIFDLPFSEGLIRSLNLLPCSYLLYYFKQKEMLAIEMGEYYKGGARAQVVQKVEKQLFELYKNPELKVKPKELEQRGGAYYSDA... | Cofactor: Divalent metal ion. Manganese, cobalt and nickel ions enhance activity whereas magnesium, calcium, strontium and zinc ions do not.
Function: Hydrolyzes a wide variety of P-beta-glucosides including cellobiose-6P, salicin-6P, arbutin-6P, gentiobiose-6P, methyl-beta-glucoside-6P and p-nitrophenyl-beta-D-glucopy... |
Q8CTQ2 | MSEAAETLDGWYSLHLFYAVDWTTFRLIAEDDREAMITELETFIKDKTVARESHQGDHAIYNITGQKADLLLWFLRPEMKELNQIENEFNKLRIADYLIPTYSYVSVIELSNYLAGKSDEDPYENPHVKARLYPELPHSEYICFYPMDKRRNETYNWYMLPIEDRKTLMYNHGMIGRKYAGKIKQFITGSVGFDDYEWGVTLFSNDVLQFKKIVYEMRFDETTARYGEFGSFYIGHILNIEDFKQFFSI | Cofactor: Fe-coproporphyrin III acts as both substrate and redox cofactor.
Function: Involved in coproporphyrin-dependent heme b biosynthesis. Catalyzes the decarboxylation of Fe-coproporphyrin III (coproheme) to heme b (protoheme IX), the last step of the pathway. The reaction occurs in a stepwise manner with a three-... |
O69830 | MSDDASTPAAERIPNKGKLAKDLNEVIRYTLWSVFKLKDTLPEDRAGYADEVQELFDQLAAKDVTIRGTYDLSGLRADADLMIWWHAETADQLQEAYNLFRRTKLGRALEPVWSNMALHRPAEFNRSHIPAFLADETPRNYISVYPFVRSYDWYLLPDEDRRRMLADHGKMARGYPDVRANTVASFSLGDYEWILAFEADELHRIVDLMRHLRGSEARRHVREEIPFYTGRRKDIGELVAGLA | Cofactor: Fe-coproporphyrin III acts as both substrate and redox cofactor.
Function: Involved in coproporphyrin-dependent heme b biosynthesis. Catalyzes the decarboxylation of Fe-coproporphyrin III (coproheme) to heme b (protoheme IX), the last step of the pathway. The reaction occurs in a stepwise manner with a three-... |
P0CH62 | MAIKRGADLIVEALEEYGTEQVVGFIGHTSHFVADAFSKSHLGKRVINPATELGGAWMVNGYNYVKDRSAAVGAWHCVGNLLLHAAMQEARTGRIPAVHIGLNSDGRLAGRSEAAQQVPWQSFTPIARSTQRVERLDKVGEAIHEAFRVAEGHPAGPAYVDIPFDLTADQIDDKALVPRGATRAKSVLHAPNEDVREAAAQLVAAKNPVILAGGGVARSGGSEALLKLAEMVGVPVVTTSTGAGVFPETHALAMGSAGFCGWKSANDMMAAADFVLVLGSRLSDWGIAQGYITKMPKFVHVDTDPAVLGTFYFPLLSVVA... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the ring-opening cleavage of the alicyclic alcohol cyclohexane-1,2-dione.
Catalytic Activity: cyclohexan-1,2-dione + H2O = 6-oxohexanoate + H(+)
Sequence Mass (Da): 63294
Sequence Length: 589
EC: 3.7.1.11
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Q8NE62 | MWCLLRGLGRPGALARGALGQQQSLGARALASAGSESRDEYSYVVVGAGSAGCVLAGRLTEDPAERVLLLEAGPKDVLAGSKRLSWKIHMPAALVANLCDDRYNWCYHTEVQRGLDGRVLYWPRGRVWGGSSSLNAMVYVRGHAEDYERWQRQGARGWDYAHCLPYFRKAQGHELGASRYRGADGPLRVSRGKTNHPLHCAFLEATQQAGYPLTEDMNGFQQEGFGWMDMTIHEGKRWSAACAYLHPALSRTNLKAEAETLVSRVLFEGTRAVGVEYVKNGQSHRAYASKEVILSGGAINSPQLLMLSGIGNADDLKKLG... | Catalytic Activity: A + choline = AH2 + betaine aldehyde
Sequence Mass (Da): 65358
Sequence Length: 594
Pathway: Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine aldehyde from choline (cytochrome c reductase route): step 1/1.
Subcellular Location: Mitochondrion inner membrane
EC: 1.1.... |
Q2T8Y5 | MTEFSSKERYTMIRVLVIDDSATMRILLKKLIDKNEHMECVGVAPNPVAAQELLRETRPDVITLDIEMPKMNGLDFLDRIMRLMPVAVIMISTLTEAGSESALRALELGAIDFIAKPKLDFAEGVQAYAEEIYRKIETAGRAKVKKLTRDVPPVRMDAEPPAKPLLAEAGKDGRVVAVGASTGGTEAVKELLLSLPADCPPLLIAQHMPEPFMRSLAKRLDLLCAMRVKMAEDGETLRRGCVYIAPGHSNLTIDATAAGYVCRIVRNAGEAQSDSSVDELFRSVAAAAGARGVGIVLTGSGSDGAAGARAMMAAGAFNIA... | Function: Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irrever... |
O33558 | MTTHAAAPSTRVLIVDDSAAARAMFKVIVESDPALQVMAAVPDAFAAARAMRTELPDVILLDLELPSMDGLTFLRKIMQQHPIPVVVCSSHVGAGTEAMVSALELGAREVISKPAARNDLERQEASIRICDAIRAATETTRRRSQPEPRPLAPGPKLTADEILPARPPRPVPETMPVVCIGASTGGTEALRDVLTALPASAPPIVIVQHMPRGFTAAFARRLDSLCAIEVLEAEDEMQVMPGRAIIAQGDRHLLLRRRNQGYRVSVLDGAYVCRHRPSVDVLFRSAAQEAGGNALGVIMTGMGDDGARCMAEMRAAGAET... | Function: Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irrever... |
P62640 | MRKIRVVVIDDSAYSRRAITKMLESMPEVEVIGYATDGEEGIRKIIDLKPDLVTLDLEMPRMDGFTLLRIVMEYSPTAVIVISSRSEDEKVFRALELGAVDFVAKPTKGVSEEILTIREDLHRKVRGVIHLNLAGIVRREREQERASVAAGRRTSGSAPYAKAAVRTESTAPRPAGRLEVVAIGASTGGPPALQRILCALPGAFPQAVVVSQHMPAGFTRTFAERLNRLSPLEICEAADGDEVRAGRVLIAPGGHNMVFERQGSEVRARIVKPGTDDRYVPSVDAMLLSCAEVFGPRTLGVVLTGMGNDGSKGVAAINRA... | Function: Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irrever... |
Q2SFK0 | MDVLIVDDSPVIRQLLRHIIEEGGMRVIGEASNGVEALRCIARRRPDVITMDIHMPVMDGLEASRRIMEEYPTPIVVVTASYSLGDAVTAMQVLEAGAITVTPKPQGPSHPDFERDVESLLRTIRLISEVKVVRRFRRRQGKREEVQPPPPVNHEHEGFQPGVIAIGASTGGPVALKELLQGISRKTPCPVLVVQHISPGFLTSFCEWLNQVSALPVSIGEYGERAERGRVYLAPDGCHMEVDRSCRISLVNGNRDETLCPSVSRLFSSVAKNFGRNAVVVLLSGMGRDGAAEMAELHRLGALTIAQDPATVVVNGMPGE... | Function: Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irrever... |
Q2W2W9 | MPARGKISVLIVDDSGMARAMLRSIFEDEDDFDVVAEAVNGREAIEMVRHLRPGLVTMDLEMPEMGGLEAIEEIMCSKAVPILVVSGVADAQKAFGAMSRGAVDVVAKPNVTSAREVEDFVDKARLVAKIPVITVPRTRSAPAAGPTPVPQAPPPPAAPPAGDGGIIAIAASTGGPQALAALLAAIGRPLSCPMVVAQHISDGFASGMADWLNSISAMPVRLAAEGERLTAGTVYLSPSEWNMSVTESRHIALALRPERQVYRPSCDALLTSVAQVAGRRAVGVILTGMGSDGVAGMEAISKAGGTTLGQDEGSSVIFGM... | Function: Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irrever... |
Q1CZL0 | MSVQRPIRVLVVDDSPTMANMLTALLTEEPRIEVVGRAGDGNRAVQLARLLRPDVITMDLLLPGLDGPGAIAAIMSQSPARILVVSAVAEQRGVDLGFQAMSAGALELIGKPNVTNAEELRRWGKELAHSVCLMAEVPVISRRPRAATAPPPPTGARVDIFGVVASTGGPPALADVLSKLPRSLPVPLLIAQHITVGFTQGMVRWLSQVTPLPVSIAKDGERLEPGRVYFPLDGHDLLVDAAGLARLQPSQGGPCPSGDVMLTSLAAAFGRRSGGVVLTGMGEDGARGLLAIRRAGGVTFSQDEASSVVFGMPRAALDVK... | Function: Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irrever... |
Q9HXT8 | MRIGIVNDMPLAVEALRRALAFEPQHQIVWVASNGAEAVTQCAADTPDVVLMDLLMPVMDGVEATRRIMAESPCAIVIVTVDIEQNVHRVFEAMGYGALDAVNTPALGIGNPQTAAAPLLRKIQNVGWLIGQRDNRGKVQVVPPKAGGARQRLVAIGASAGGPASLAVLLKQLPASFNAAVVLVQHVDEVFAAGMAEWLASESKLPVRLARDGEPPIPGQILLAGTNNHIRLLRNGSLVYTAEPRSFVYRPSIDVFFESVANYWRGDAVGVLLTGMGRDGAQGLKQMRERGFLTIAQDQASCAVYGMPKAAAAIDAAVQI... | Function: Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irrever... |
Q88MS5 | MKIAIVNDMPLAVEALRRAVALEPAHQVVWVASNGAEAVQRCTEQLPDLILMDLIMPVMDGVEATRRIMAETPCAIVIVTVDRKQNVHRVFEAMGHGALDVVDTPALGAGDAREAAAPLLRKILNIGWLVGQQRAPAARSVAAPLREASQRRGLVAIGSSAGGPAALEVLLKGLPAAFPAAIVLVQHVDQVFAAGMAEWLSSAAGLPVRLAREGEPPQPGQVLLAGTNHHIRLLQNGQLAYTAEPVNEIYRPSIDVFFESVARYWNGDAVGVLLTGMGRDGAQGLKLMRQQGFLTIAQDQASSAVYGMPKAAAAIDAAVE... | Function: Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irrever... |
Q92YM4 | MVRILLATSTVELEDLVKRAIEGDASAELVLIARSGREAVRMTGELLPDIVAVELCPSGDDSAETVREIMIAAPTPVVMLSHRDGSQLGTISARALEAGALAVIPAPAAHGMQLEQPAIEKFLSTIKAMSQVKVVRQWRQKVRGDRAAKDQPPTARTPIGIVGIAASTGGPAAIRAILKDISADLPVPILIVQHMSNGFIDGVAASLNATVPLTVKVARNGELLKPGTVYLAPDNCQLGVSGRSRLRVSDDAPVNGFKPSGSYLFGSIARAFKGESLAVVLTGMGDDGTEGLRALRMAGGKAIAQDEKSSVVFGMPKSAI... | Function: Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irrever... |
P62645 | MAKQKIRVLIVDDSASVRQVLGTILAEDPEIEVIGTASDPFVAAKRLQNELPDVILLDIEMPRMDGITFLRKIMAQHPIPVVICSSLTPEGSDLMFEALEAGAVDIVPKPRVDTRQALMESSGRLREAIKSAARARVRPRAARKVIEQKLTADAIIPPPVAGRSRPTTERIVCIGVSTGGTEALYDVLEVLPPNCPGILIVQHMPQGFTAAFAKRLNAGCQINVKEAEDGDPVLPGWAYIAPGARHMLLVRSGLRYQIAIKDGPPVSRHRPSADVLFRSAAQYAGANALGIIMTGMGDDGARGLLEMRKLGAYTCAQDEE... | Function: Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irrever... |
O87719 | MTSFHHDDPERAVKVHVTQGESHVTADPNVVMTTVLGSCIAACIRDPQSGVGGMNHFLLPDSGDGRRDGDAVRYGAYAMEVLINDLLKRGARRERLEAKIFGGAKLFDGLSDVGASNAAFAERFLRDEGIPIVSSSTGGVSARRVEFWPASGRVRQRLVAVDNAPQDVRRPTPPPMPAVASGDVDLF | Function: Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis.
Catalytic Activity: H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)
Sequence Mass (Da): 20068
Sequence Length: 187
EC: 3.5.1.44
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Q3J3N4 | MTRCDDSPSASQISITHVTQGSCVASSSPNEVYATILGSCICTCMCDPVAGVGGMNHFLLPSADVEDAQHLRYGSHAMELLINALLKLGAARQRIEAKIFGGAMMTPQLGAIGQANAAFARRYLKDEGIRCTAHSLGGNRARRIRFWPKTGRVQQMFLGSEDVVPNEQPQFRLQGGAGDVTFFDRHNNAEMPDPIKEPR | Function: Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis.
Catalytic Activity: H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)
Sequence Mass (Da): 21592
Sequence Length: 199
EC: 3.5.1.44
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Q2HEW3 | MKLCALFAGAVISTSAVAASWEYAWPEEWHQEWPLDEQGPDAWSSSECTVSRLDAFEMEKGRKPVFFSTDPLDDPEAPKMLPLNSTGGEQWEFDGVSEDGQMAFCFGFYRDPNYAILGTGNLRLSAEFSRPNKTRFVRVDYPSSSTVTSCPWGTRGVWKGADYSYTFEVTRDIKVARIGVDAPDLKGSVVMRSVMPPRYPDGSTYPNKEASTEVVPYFRWLEAIPAADVRVDVVMDGQPYRWSGLGGHERLWTAFSWFTCLQAMTAVRVKAGPFAAVHGSFVSAIDKGLYRPSTVLAENDEVIFSTTLHEPSDTEDYAVF... | Function: Diels-Alderase; part of the gene cluster that mediates the biosynthesis of chaetoglobosin A which has a unique inhibitory activity against actin polymerization in mammalian cells . Chaetoglobosin A and its intermediates are involved in the morphological differentiation of C.globosum . The first step of the pa... |
Q3B327 | MKKTAKTDTEDAFKFRSTFGEHYYDGYGARHETPHIVAYTGEVTAAGPGRVLISSPLGSCIAVCAYDPGTRVGGLAHVMLPGVPPAHAETGKDRYAAHALETLFSVMQNEGADPGNLLICLIGGANVLRREHDTIHIDNLRSLTSLILQRNLPICRTMTGGSERMMARMETKTGRIFQTTGNNPEEMLFDYFTHNIENPDN | Function: Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis.
Catalytic Activity: H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)
Sequence Mass (Da): 22024
Sequence Length: 201
EC: 3.5.1.44
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Q97GZ2 | MEERENIKEIRVGIADLNTAFSPNRIITVGLGSCIGIAIYDSKNKLGGLSHIMLPDSTQFSKVTNPYKFADLAIPILIKKMEGMGANIRNMKAKIAGGASMFNFSDKNMNMDIGNRNGISVKKVLKELNVPLLSQDIGGNKGRTMIFNTLDGSVDIRTVGMGIRKI | Function: Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis.
Catalytic Activity: H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)
Sequence Mass (Da): 18075
Sequence Length: 166
EC: 3.5.1.44
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A0PZY2 | MNKDEIRIGIADLNVALPPKKLITVGLGSCIGIALYDSIKKIGGLAHIMLPDSTQFSNVSNPMKFADLAIPMLLEKMEKQGAVKRHLKAKIAGGASMFNFSDKSMIMDIGNRNSKSVKKVLGEYGIPIISEDTGGNKGRTMIFSTEDGMVEIRTVGMGIRAI | Function: Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis.
Catalytic Activity: H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)
Sequence Mass (Da): 17455
Sequence Length: 162
EC: 3.5.1.44
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B7LP17 | MMQPSIKPADEHSAADIIARIGSLTRMLRDSLRELGLDRAIAEAAEAIPDARDRLDYVVQMTAQAAERALNSVEASQPHQEEMEKGAKSLSQRWDAWFDDPIELAQARELVTDTRRFLAEVPDHTRFTNAQLLDIMMAQDFQDLTGQVIKRMMDVIQEIERQLLMVLLENIPEQDARPKRENESLLNGPQVDTSKAGVVASQDQVDDLLDSLGF | Function: Plays an important role in bacterial chemotaxis signal transduction pathway by accelerating the dephosphorylation of phosphorylated CheY (CheY-P).
Sequence Mass (Da): 24096
Sequence Length: 214
Subcellular Location: Cytoplasm
EC: 3.1.3.-
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O24976 | MTQEELDALMNGGDLENLEALETKEETKEEAKEEAKEEAKEEAKEKEEIKEESSSQKMTVKKEDAEKYGKISPNEWPPPPPTEEHKVVHQLDDVTRDSEVKATQIFDQLDLIGASAEKIAKMVKKIQEPLQKHQEIFDNLHGHFPHVESFKTALNEQQEILNALKSIEEEAANCSDSSMQAMDIMQFQDIHRQKIERVVNVMRALSQYMNSLFEGKIDDSKRVSSATFITGDDDKDLASADDIEALIASFGAK | Function: Plays an important role in bacterial chemotaxis signal transduction pathway by accelerating the dephosphorylation of phosphorylated CheY (CheY-P). Dephosphorylates also CheV2 but not CheV1 or CheV3 . In addition, forms a distinct chemotaxis regulatory complex with ChePep independently of the core chemotaxis s... |
Q51434 | MQLIQELSQARDRGLYQEVGKLTRELHNAIVDFQIDPHSPHAQEMSQIADATDRLSYVVEMTEKAANRTMDLVEQSAPLVNQLGDDSRELHQEWQRFMRREIDADGFRELAKRIEQFLVRSGENAGQLSSQLNDILLAQDYQDLTGQVIKRVTKLVTEVESNLVKLVWMAGQVDRYAGIEHDHVSMRHQAALERSAKGEGPQVAAEKREDVVSGQDDVDDLLSSLGF | Function: Plays an important role in bacterial chemotaxis signal transduction pathway by accelerating the dephosphorylation of phosphorylated CheY (CheY-P).
Sequence Mass (Da): 25710
Sequence Length: 227
Subcellular Location: Cytoplasm
EC: 3.1.3.-
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P07800 | MMQPSIKPADEGSAGDIIARIGSLTRMLRDSLRELGLDQAIAEAAEAIPDARDRLDYVVQMTAQAAERALNSVEASQPHQDAMEKEAKALTQRWDEWFDNPIELSDARELVTDTRQFLRDVPGHTSFTNAQLLDIMMAQDFQDLTGQVIKRMMDVIQEIERQLLMVLLENIPEQSARPKRENESLLNGPQVDTSKAGVVASQDQVDDLLDSLGF | Function: Plays an important role in bacterial chemotaxis signal transduction pathway by accelerating the dephosphorylation of phosphorylated CheY (CheY-P). Acts on free CheY-P.
Sequence Mass (Da): 23920
Sequence Length: 214
Subcellular Location: Cytoplasm
EC: 3.1.3.-
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A3QCQ6 | MQAETSGLINLAQAKQLVDLLEAGQQEMADELIRDIASPIQKELFDEVGRLTRQLHSAIVDFQVDGRLVELANSEIPDAKERLNYVIDMTEQAANKTMDAVEESLPLADALTMNVQAVKPSWDRLMRRDIQLHEFKALCHDVQQFIERSESDSNRLKELLNNILLAQDFQDLTGQMIRRVIELVREVESNLVSMLTVFGEQPATDKPRASEKCVEAEGPIMNADQRDDVVTGQDEVDDLLSSLGF | Function: Plays an important role in bacterial chemotaxis signal transduction pathway by accelerating the dephosphorylation of phosphorylated CheY (CheY-P).
Sequence Mass (Da): 27578
Sequence Length: 245
Subcellular Location: Cytoplasm
EC: 3.1.3.-
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A5F6J8 | MISLEQAKELVQLLEQGRQDDANRLFTYVYESANNPMFKEIGMLTRDLHEALKNFQIDERFSEIATDEIPDARERLHYVIQKTEVAANKTMDAVDRCMPIADKLHESLLLIRPEWNGLMNGRIELMHFKSLCHRIDDLLSQVEGDSSELRGELTEILMAQDFQDLTGQIIKRVINLVNEVEKRLVEILTVFGAAQKEQKADKATVASIEPEGPILNPHERIDAVSSQDEVDDLLSSLGF | Function: Plays an important role in bacterial chemotaxis signal transduction pathway by accelerating the dephosphorylation of phosphorylated CheY (CheY-P).
Sequence Mass (Da): 27232
Sequence Length: 239
Subcellular Location: Cytoplasm
EC: 3.1.3.-
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Q9LB13 | MISLEQAKSLVQMLENGEQDQANMLVASLYEGTENPVLQEIGTLTRDLHDSLKQFNLDQRMTEIAKDEIPNARDRLHYVIEKTELAANKTMDAVDCCLPIADNLHDCLQQVRPQWNELMYGRIELSEFKALCHRIDKLLVQVEGDSTELRGQLTEILMAQDFQDLTGQIIRRVITLVNEVEGRLVEILTVFSGQKPAEQVQVLSEPADKKIKQSSEAEGPILHPELREDAVSSQDEVDDLLSSLGF | Function: Plays an important role in bacterial chemotaxis signal transduction pathway by accelerating the dephosphorylation of phosphorylated CheY (CheY-P).
Sequence Mass (Da): 27782
Sequence Length: 246
Subcellular Location: Cytoplasm
EC: 3.1.3.-
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A5WW08 | MTNQDSDQAWGKLVKVDASPGSEIVLINSECTVGRKKDCDLSFPANKLVSGNHCKITHDQNSGKVWLEDMSTNGTVINMSKVVKKQTHLLQNGDVIYFVYRKNEPEQNIAYVYQSITPQESASHDVEDAGREEDSDLTETESEPAPVEPVIVKPLPQSGHEDPQPSTSSSSLHFYNMPLSTCSDVSARKNPVSSSAVCKGDSTSSGSPAQTRLKWTCWTDGEPEEEMQRKRRKTDRDDPGFGSAHSDASADIPLRGASGKEKTEGATTDKMEESLTCIICQDLLYDCISVQPCMHTFCAACYSGWMERSSFCPTCRCPVE... | Function: E3 ubiquitin-protein ligase that functions in the antephase checkpoint by actively delaying passage into mitosis in response to microtubule poisons. Acts in early prophase before chromosome condensation, when the centrosome move apart from each other along the periphery of the nucleus. Probably involved in si... |
Q96EP1 | MERPEEGKQSPPPQPWGRLLRLGAEEGEPHVLLRKREWTIGRRRGCDLSFPSNKLVSGDHCRIVVDEKSGQVTLEDTSTSGTVINKLKVVKKQTCPLQTGDVIYLVYRKNEPEHNVAYLYESLSEKQGMTQESFEANKENVFHGTKDTSGAGAGRGADPRVPPSSPATQVCFEEPQPSTSTSDLFPTASASSTEPSPAGRERSSSCGSGGGGISPKGSGPSVASDEVSSFASALPDRKTASFSSLEPQDQEDLEPVKKKMRGDGDLDLNGQLLVAQPRRNAQTVHEDVRAAAGKPDKMEETLTCIICQDLLHDCVSLQPC... | Function: E3 ubiquitin-protein ligase that functions in the antephase checkpoint by actively delaying passage into mitosis in response to microtubule poisons. Acts in early prophase before chromosome condensation, when the centrosome move apart from each other along the periphery of the nucleus. Probably involved in si... |
Q5FWP4 | MEGLDEKKPWGKLSRLLGAETDSSSELFLYKKEWTIGRKKACDLSFPGNKLVSGEHCKITVNEESGEVSLEDTSTNGTVINKLKVIRKQTYPLKNGDVIYVVYRKNEPEQNVAYLYKSLNQGQDSLHDPADTSGSEEAETQTLSSQDDQLSYEEPQPSTSTSSLFSTPTTSAIPGVQLESAEKSGESLGGHSSTSDASPAIRASIPKSNLSTQEQGSLGPPKKRIRTEDHWTTNKNFVPASCPIGASDESKTPSMKPDKMEETLTCIICQELLHDCVSLQPCMHTFCAACYSGWMERSSLCPTCRCPVERICKNHILNNL... | Function: E3 ubiquitin-protein ligase that functions in the antephase checkpoint by actively delaying passage into mitosis in response to microtubule poisons. Acts in early prophase before chromosome condensation, when the centrosome move apart from each other along the periphery of the nucleus. Probably involved in si... |
Q750G3 | MGRCEFYHPFTPYRIQLELMQQIYGLLESGKKMGIFESPTGTGKTLSLICSTFTWLREHKAGYLQGSTGAQDSEEDSEDEPAWVKENYEQSVLADVTASMRAYEQRLAAVDTDLLVKGAAKRQRVEVAVERPDDGAEFLPDAYHSDVEERPSHAGGRGQLRKQLDADIKRLLRKLDEPDAADKSRLAANPLKVYFASRTHTQLGQFAAQLRLPQFPPSLAGLEQERVKFLPLGSRKQLCIHKKVSKVKSDGINEACMDAVSKSECSFFSAAREPDIIRQFQDQAFSTIQDIEDLVGIGNTLHACPYYSSRELIEGAEVIT... | Function: ATP-dependent DNA helicase important for chromosome transmission and normal cell cycle progression in G(2)/M (By similarity). May have a role in changing DNA topology to allow the loading of proteins involved in maintaining sister chromatid cohesion in the vicinity of the centromeres (By similarity). Has a sp... |
A1CJ34 | MCQKYDTLSGDRDVEHDEHFVLEDYDSESEDQNISSKSLGHSSELSMSTLALLERFKKQYSAPTEEEETVGDDEPKIFYCSRTHSQLAQFASELRRVEMPPSLPKELSEKLTDSEALEERVKHLSLGSRKNLCINPRVMKLENATAINERCMDLQQPGMAVEHRCPYLPSKDDEPQVLQFRDHTLATVKDIEDMGKLGKHIGVCPYYASRSVIKHSEIVTLPYPLLLQRSAREALGLSIKNHIVIIDEAHNLMDAISNIHSVTITLSQLQTAIFQLTTYARKFKTRLKGKNRTYIAQVIRLVSSVADHLRSIQGSNQPPD... | Function: ATP-dependent DNA helicase important for chromosome transmission and normal cell cycle progression in G(2)/M (By similarity). May have a role in changing DNA topology to allow the loading of proteins involved in maintaining sister chromatid cohesion in the vicinity of the centromeres (By similarity). Has a sp... |
Q4WWE9 | MLEFAKRESARAVTEKRRALEARLEKIKVEEEKQRHATDHPKEARKRRRVDTSSGDPGPEQDDQFILDDYDSDADERMASSKKLSDISGLSTSTLELLERFKEQFSAPVEDEIGHEDDDVKIFYCSRTHSQLSQFSSELRRVKMPSSMPAELSTSDANTDEVQERVKHLTLGSRKNLCINPKVMSLGNAAAINERCLELQQPGIAAEKRCPYLPSKEDEGQILQFRDHTLATIKDIEDMGKLGKRMGICPYYASRSVLKHSENVLLKAQKIVTLPYPLLLQRSARDALDLSIKNHVVIIDEAHNLMDAICNIHSVTIRLS... | Function: ATP-dependent DNA helicase important for chromosome transmission and normal cell cycle progression in G(2)/M (By similarity). May have a role in changing DNA topology to allow the loading of proteins involved in maintaining sister chromatid cohesion in the vicinity of the centromeres (By similarity). Has a sp... |
Q21489 | MDEFSFPFQPYDIQLNLMREIRQCIEQRKIGIFESPTGTGKSLSVLCSTMTWLEAEELRISTDLSTRLGEVHTKITECDKITTADNWETAVREKMRAQDVETEILEQIQSRERLQSRIDQARRGMVEVSRKRKAPARDTDQFLEPQDEAAPSEEYNNDEKSEKQRDSDFFDDVDEEEEKPLKCLKIFYASRTHSQLEQLAEELAKTRFQPRIVTCASRGTLCVNEEVKKLKLNHLINEKCMELRKNGMSEKEKVQKLEKGTTKKTKTCATSCEFYNSTQIEDVVNGVLSNKLKSTLEVSKQGKLSNGCPYFATRKSVPQC... | Function: Required for normal cell proliferation and chromosome stability. Plays a role in DNA repair during replication.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 94650
Sequence Length: 830
Subcellular Location: Nucleus
EC: 3.6.4.12
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Q5AD67 | MVSESCSRNYNHPYTPYDIQIQLMDAIYNTIENGYKIGLFESPTGTGKTLSIICSSMTWLRTFKRNNTFLETNNEVEDVYESESEEDEPEWVKKAYQSSIVNRSKNKLIEYEHYLDKIEKEHAQNKRKEEELEIKVHKRRKAMTAAGTDLSEESYLPMDYYSDSEVGKIEDQNLAITKEINRLLKKVENKEEVSYINECPIKIFFSSRTHSQLNQFSSQLRLTNFQASFEDLEERTKYIPLGSRKQLCINEKVRSKGNDQSVNDACLDLQRETNGCQYLPKNYMMSSVTKEFADLSLAKIRDIEDLNELGIELNICPYYS... | Function: ATP-dependent DNA helicase important for chromosome transmission and normal cell cycle progression in G(2)/M (By similarity). May have a role in changing DNA topology to allow the loading of proteins involved in maintaining sister chromatid cohesion in the vicinity of the centromeres (By similarity). Has a sp... |
Q6FKT4 | MDNATKFHHPYSPYDIQLDLMQCVYDTLANPVKKVAIVESPTGTGKTLSLICSTLTWLRDNKADILSSVDTLHSNEDDSHDSEPEWVKDTYKESILKDKLELLDEYEKYLEELHLKENKIIKFGTSIEDKSKVKRRKVTSSSKAKIEVSIEDEDEFVAKPYESDGEETTDLEKKEALSKEVQELLAKFDSSKKNTDNVELGRFASASQNQVRIFFSSRTHSQLNQFAEQLKLTNFPSSFPDKVAHERVKYMPLGSKKQLCINPDVKKWKTLEGINDACSEVRRSKEGCPFYQNTPKWHNSKETNHFRDQVFSDIHDIEDI... | Function: ATP-dependent DNA helicase important for chromosome transmission and normal cell cycle progression in G(2)/M (By similarity). May have a role in changing DNA topology to allow the loading of proteins involved in maintaining sister chromatid cohesion in the vicinity of the centromeres (By similarity). Has a sp... |
A5DNW6 | MNRDDPRLTYNHPYKPYDIQVQLMDAIYDTIQNKYKVGLFESPTGTGKTLSIICSSMTWLRNYKKTQDHSTMGSNSSNDNDPNQTSDSDEEPDWVKEAHIKNIRSRTSGLAIDYERHLEELSQTPHAGHTVELGQRTHKRKKRATNDDDFLPDDYNSDTDSNSVETKNAKLQQEINQIMKRVDGSDGKTPGFVNTCPVTIFFSSRTHSQLSQFAHQLSITSFESSLGEIAERIKFMPLSSRKQLCIHPKVSSLSSVSAVNDACVELQQKSDKRCEFMPRVNNPESDQLVQRFADYSFAVIKDIEELHELGADLKVCPYYA... | Function: ATP-dependent DNA helicase important for chromosome transmission and normal cell cycle progression in G(2)/M (By similarity). May have a role in changing DNA topology to allow the loading of proteins involved in maintaining sister chromatid cohesion in the vicinity of the centromeres (By similarity). Has a sp... |
O14147 | MCHSKEVKFKTNFHHPYTPYDIQLEFMRSLYSSISDGKIGIFESPTGTGKSLSLICASLTWLDEHGGVLLEDNEKSNDNKSNTSSKIPDWVLEQDLKIQKDLVKETHARLEQRLEEIRKRNQSRKNQMSNNSTTYHRETKRRNINAEASTSDNCNNSNTSVDPMDEYLVTAEYTMPSTSEQSEDLFNNGYSSKVSELLRKLSPDNEKPPIVQKIYFTSRTHSQLQQLVQEIKKLNNQTFSTPIRVVSLASRKNLCINNEVRKLRPTSALNEKCIELQGSAHKCPFLQDNTQLWDFRDEALAEIMDIEELVELGQRLKVCP... | Function: ATP-dependent DNA helicase important for chromosome transmission and normal cell cycle progression in G(2)/M (By similarity). May have a role in changing DNA topology to allow the loading of proteins involved in maintaining sister chromatid cohesion in the vicinity of the centromeres (By similarity). Has a sp... |
Q32742 | MTEEKKINPPIFPFTAIVGQEEMKLALQLNVIDPKIGGVMIMGDRGTGKSTTIRAIADLLPEIEVVKDNQFNTAPSEDLNEEIVKIKTPMIDLPLGATEDRVCGTIDIEKALTDGVKAFEPGLLAKANRGILYVDEVNLLDDHLVDILLDSAASGLNTVEREGISIRHAARFVLVGSGNPEEGELRPQLLDRFGMHAVIKTVKDPKLRVRVVEERTLFDLNPEEWINKYREQQEALKTRIIAAQNLISSVTISDDFKLKISQVCSELDVDGLRGDIVTNRAAKAYAAFNNRTEVEIGDIEKVITLCLRHRLRKDPLETID... | Function: Involved in chlorophyll biosynthesis; introduces a magnesium ion into protoporphyrin IX to yield Mg-protoporphyrin IX.
Catalytic Activity: ATP + H2O + Mg(2+) + protoporphyrin IX = ADP + 3 H(+) + Mg-protoporphyrin IX + phosphate
Sequence Mass (Da): 37209
Sequence Length: 334
Pathway: Porphyrin-containing compo... |
Q53RM0 | MASAFSPATAAPAASPALFSASTSRPLSLTAAAAAVSARIPSRRGFRRGRFTVCNVAAPSATQQEAKAAGAKESQRPVYPFAAIVGQDEMKLCLLLNVIDPKIGGVMIMGDRGTGKSTTVRSLVDLLPDIRVVVGDPFNSDPDDPEVMGPEVRERVLEGEKLPVVTAKITMVDLPLGATEDRVCGTIDIEKALTDGVKAFEPGLLAKANRGILYVDEVNLLDDHLVDVLLDSAASGWNTVEREGISISHPARFILIGSGNPEEGELRPQLLDRFGMHAQVGTVRDAELRVKIVEERARFDRDPKAFRESYLEEQDKLQQQ... | Function: Involved in chlorophyll biosynthesis. Catalyzes the insertion of magnesium ion into protoporphyrin IX to yield Mg-protoporphyrin IX. The reaction takes place in two steps, with an ATP-dependent activation followed by an ATP-dependent chelation step.
Catalytic Activity: ATP + H2O + Mg(2+) + protoporphyrin IX =... |
Q85FG5 | MKVAVYGKGGIGKSTTSCNISIALARRGRKVLQIGCDPKHDSTFTLTGFLIPTIIDTLQVKDYHYEDVWPEDVIYRGYGGVDCVEAGGPPAGAGCGGYVVGETVKLLKELNAFYEYDIILFDVLGDVVCGGFAAPLNYADYCIIITDNGFDALFAANRIAASVREKSHTHPLRLAGLVGNRTSGRDLIDKYVEACPMPVLEVLPLVEDIRVSRVKGKTLFEMAEYQPNLNYVCDFYLNIADQILSEPEGVVPREIPDRELFSLLSDFYLNSTFTNESDGGYDHQDVPLDFTII | Cofactor: Binds 1 [4Fe-4S] cluster per dimer.
Function: Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The L component serves as a unique... |
Q85A82 | MKIAVYGKGGIGKSTTSCNTSIASARRGKRVLQIGCDPKHDSTFTLTGSLIPTIIDTSQSKDYHYEDVWPEDVIYKGYGGVDCVEVGGPPAGAGCGGYVVGETVKLLKELNAFYEYDIILFDVSGDVVCGGFVVLLNYADYCIIITDNGFDALFAVNCIAASVREKARTHSLRLAGSVGNRTSKRDLINRYVEACPMPVLEVSLLIEDIRVSRVKGKTSFEMVEFQPFLNYVCEFYLNIADQILSQPEGVIPKEIPDRELFSLLSDFYLNPTNNERENKNQETLLDFMII | Cofactor: Binds 1 [4Fe-4S] cluster per dimer.
Function: Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The L component serves as a unique... |
Q00469 | MKLAVYGKGGIGKSTTSCNISIALRKRGKKVLQIGCDPKHDSTFTLTGFLIPTIIDTLSSKDYHYEDIWPEDVIYGGYGGVDCVEAGGPPAGAGCGGYVVGETVKLLKELNAFFEYDVILFDVLGDVVCGGFAAPLNYADYCIIVTDNGFDALFAANRIAASVREKARTHPLRLAGLIGNRTSKRDLIDKYVEACPMPVLEVLPLIEEIRISRVKGKTLFEMSNKNNMTSAHMDGSKGDNSTVGVSETPSEDYICNFYLNIADQLLTEPEGVIPRELADKELFTLLSDFYLKI | Cofactor: Binds 1 [4Fe-4S] cluster per dimer.
Function: Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The L component serves as a unique... |
Q3SX42 | MASLFKKKTVDDVIKEQNRELRGTQRAIIRDRAALEKQEKQLELEIKKMAKIGNKEACRVLAKQLVHLRKQKTRTFAVSSKVTSMSTQTKVMNSQMKMAGAMSTTAKTMQAVNKKMDPQKTLQTMQNFQKENMKMEMTEEMINDTLDDIFDGSDDEEESQDIVNQVLDEIGIEISGKMAKAPSAARSLPSASTSKSTISDEEIERQLKALGVD | Function: Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limi... |
Q6NXD2 | MTSLFKKKTVDDVIKEQNKELRGTQRQIARDRTALEKQEKQLEMEIKKMAKTGNRDACKVLAKQLVQVRKQKTRTYAVSSKVTSMSTQTKLMNSQMKMAGAMATTTKTMQAVNKKMDPKKTMQTLQNFQKETAKMDMTEEMMNDTLDEIFEDSGDEEESQDIVNQVLDEIGIEISGKMAHAPSAARKTPSAATAKADGISDEDIERQLKALGVD | Function: Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limi... |
Q9UQN3 | MASLFKKKTVDDVIKEQNRELRGTQRAIIRDRAALEKQEKQLELEIKKMAKIGNKEACKVLAKQLVHLRKQKTRTFAVSSKVTSMSTQTKVMNSQMKMAGAMSTTAKTMQAVNKKMDPQKTLQTMQNFQKENMKMEMTEEMINDTLDDIFDGSDDEEESQDIVNQVLDEIGIEISGKMAKAPSAARSLPSASTSKATISDEEIERQLKALGVD | Function: Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limi... |
Q8BJF9 | MASLFKKKTVDDVIKEQNRELRGTQRAIIRDRAALEKQEKQLELEIKKMAKIGNKEACRVLAKQLVHLRKQKTRTFAVSSKVTSMSTQTKVMNSQMKMAGAMSTTAKTMQAVNKKMDPQKTLQTMQNFQKENMKMEMTEEMINDTLDDIFDGSDDEEESQDIVNQVLDEIGIEISGKMAKAPSAARSLPSASTSKATISDEEIERQLKALGVD | Function: Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limi... |
A2VDY3 | MSGLGRLFGRGKKEKGPTPEEAIQKLKETEKILIKKQEFLEQKIEQELQAAKKHGTKNKRAALQALRRKKRLEQQLAQTDGTLSTLEFQREAIENATTNAEVLRTMELAAQGLKKAYQDMDIDKVDELMADITEQQEVAQQISDAISRPVGFGDDVDEDELLEELEELEQEELARELLHVGDEEEEPPVALPSAPSTHLPAEPAPKADEDEAELKQLAEWVS | Function: Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limi... |
Q9BY43 | MSGLGRLFGKGKKEKGPTPEEAIQKLKETEKILIKKQEFLEQKIQQELQTAKKYGTKNKRAALQALRRKKRFEQQLAQTDGTLSTLEFQREAIENATTNAEVLRTMELAAQSMKKAYQDMDIDKVDELMTDITEQQEVAQQISDAISRPMGFGDDVDEDELLEELEELEQEELAQELLNVGDKEEEPSVKLPSVPSTHLPAGPAPKVDEDEEALKQLAEWVS | Function: Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limi... |
Q5ZHP5 | MSGILGKLFGAGAGGKGAGKGPSPQEAIQRLRDTEEMLSKKQEFLEKKIEQELAAARKHGTKNKRAALQALKRKKRYEKQLAQIDGTLSTIEFQREALENANTNTEVLKNMGFAAKAMKAAHDNMDIDKVDELMQDIAEQQELADEISTAISKPVGFGEEFDEDELMAELEELEQEELDKNLLEISGPETVPLPNVPSISIPSKPAKKKEEEEDDDMKELEAWAGNM | Function: Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limi... |
Q7ZVC4 | MSLFGKMFGSGGKGGKSASPQEAIQRLRETEEMLTKKQEFLEKKIEQELVTAKKNGTKNKRAALQALKRKKRYEKQLAQIDGTLSTIEFQREALENAHTNTEVIKNMGYAAKAMKAAHDNMDIDKVDELMQDIIEQQELAQEISDAISKPVGFGEEFDEDELLAELEELEQEELDKNLLEIGDNVPLPNVPSTSLPSRPAKKKEEEDEDDMKDLEAWAAN | Function: Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limi... |
Q9H444 | MSVFGKLFGAGGGKAGKGGPTPQEAIQRLRDTEEMLSKKQEFLEKKIEQELTAAKKHGTKNKRAALQALKRKKRYEKQLAQIDGTLSTIEFQREALENANTNTEVLKNMGYAAKAMKAAHDNMDIDKVDELMQDIADQQELAEEISTAISKPVGFGEEFDEDELMAELEELEQEELDKNLLEISGPETVPLPNVPSIALPSKPAKKKEEEDDDMKELENWAGSM | Function: Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limi... |
Q5XGW6 | MSLIGKLFGTGGKGAKGPSPQEAIQKLRDTEEMLAKKQEFLEKKIEQELVTAKKHGTKNKRAALQALKRKKRYEKQLAQIDGTLSTIEFQREALENANTNTEVLKNMGFAAKAMKAAHDNMDIEKVDELMQDIADQQELAQEISDAISKPVGFGEDFDEDELMAELEELEQEELDKNLLEVQGPETVPLPNVPAASLPAKPVKKKQEEDDDDMRELENWATA | Function: Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limi... |
Q96CF2 | MSKLGKFFKGGGSSKSRAAPSPQEALVRLRETEEMLGKKQEYLENRIQREIALAKKHGTQNKRAALQALKRKKRFEKQLTQIDGTLSTIEFQREALENSHTNTEVLRNMGFAAKAMKSVHENMDLNKIDDLMQEITEQQDIAQEISEAFSQRVGFGDDFDEDELMAELEELEQEELNKKMTNIRLPNVPSSSLPAQPNRKPGMSSTARRSRAASSQRAEEEDDDIKQLAAWAT | Function: Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limi... |
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