ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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Q9KSG1 | MTIWVLSLAMKNTIYHAPLTFGLYALAGVLFALYTSRVCPFLATLSTREIATQVGAVFILAWLIRHTLLRQHIWARKQQFIQLDTALLFAMSLPLALYYNLQYQFTLDSNLKVLFGMTLFGFFTGALLQLSSKLRTLRQMPQSQNLALSSDERRSLVKQLIGLIVLLISTLTVMLSMVAIKDIHWLENNPARLLDGSGKISIVKEFAFLSLVLGGYITAILVLWSRMMKEILDHQERSLQAVTQGNLQVRLPVYSNDELGNVAMLTNQMLDSLEATQNEVKTTRDVAIVSLSALAESRDNETGAHILRTQEYVKALAEYLAAFPQYSTLLTPAYIELLYKSAPLHDVGKVGIPDSVLLKPGKLTDEEFTVMKEHPRIGAQALAIAERHLGTSSFLAIAKEIALTHHEKWDGTGYPAQLQGEAIPLSGRLMALADVYDALISARVYKPAFSHDKAKAIIVEGSGHHFDPAVVEAFLAVEEKFVAIAAHFKDAA | 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 Length: 492
Subcellular Location: Cell inner membrane
EC: 3.1.4.-
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Q9HV27 | MESMLDRPEQELVLVVDDTPDNLLLMRELLEEQYRVRTAGSGPAGLRAAVEEPRPDLILLDVNMPGMDGYEVCRRLKADPLTRDIPLMFLTARADRDDEQQGLALGAVDYLGKPVSPPIVLARVRTHLQLKANADFLRDKSEYLELEVRRRTRQLQQLQDAVIEALATLGDLRDNPRSRHLPRIERYVRLLAEHLAAQRAFADELTPEAVDLLSKSALLHDIGKVAVPDRVLLNPGQLDAADTALLQGHTRAGRDALASAERRLGQPSGFLRFARQIAYSHHERWDGRGFPEGLAGERIPLAARIVALADRYDELTSRHAYRPPLAHAEAVLLIQAGAGSEFDPRLVEAFVAVADAFAEVARRYADSAEALDVEMQRLEQAVAESIELTAPPA | 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 regulation of motility, synthesis of virulence determinants and biofilm architecture . May act preferentially as a pGpG binding protein .
PTM: Phosphorylated.
Catalytic Activity: 3',3'-c-di-GMP + 2 H2O = 2 GMP + 2 H(+)
Sequence Mass (Da): 43629
Sequence Length: 393
Domain: Contains an unselective bimetallic binding site, with a high-affinity site (H-site) and a low-affinity site (L-site). Metal binding to the H-site triggers the binding to the L-site. This bimetallic center may play a structural more than a catalytic role.
EC: 3.1.4.-
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Q9KSB1 | MATANIAIKQNSSTNIAFIERMPSPSLHRILYNLFSKFSYSLSNSCHFNLKCLNFVMNRMFHMSMEDLSQCTILIVDDSPDNIAFMSQGLAQYYRIKAARSGKVALEILAQYPIDLVLLDIVMPEMSGYEVINQIKHNPHTEHIPVIFLTGKSNPEDEQLGFELGAVDYVFKPVSIPLLKSRVHTHLQNKRSKDILLNQNDYLETEVLRRSGELDRMQDAVVFALASLAETRDPETGNHLLRTQHYVKVLAQRLATTDKYRDVLSPTVIDTYFKAAPLHDIGKVGIPDNILLKPGKLTPDEFTTMRNHALLGKLALEKAEKLSGACTALINVAKEIAMGHHEKWDGSGYPLGLKGDDIPLSARLMALADVYDALICRRVYKEPMSHEEAKAIILQGRGSHFDPMVIDAFLIEEQNFIDIAQKFADEESAMVPIQLGQQASG | 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 | MATPPYPEDEHSRQAYVDQLGLLEEGADEVFEEILAAATSYFQTPIALISILDHQRQWFRASIGLDIRQTPRRDSFCAYAILGKGVFEVADATLDPRFRDNPYVQGEPRIRFYAGAPLATAEGLNLGSLCVIDREPRGPLAERDVAMLEHFARLVMARIHTLRSTNYIDEPTGLYNRLRLQEDVSLRLQRDGALTVIAADLLPLALLNTIIRTLGYPFSNDLMLEARDRIRAELPDFTLYKISPTRFGLLLPRQQQEETESVCLRLLRAFESPVVCRGIPIKANVGLGVLPLADDTLDGDQDWLRLVVSAADDARDRGVGWARYNPPLDQAQQRAFTLLTSLSQAIGTEEGFHLVYQPKIDLPTGRCTGVEALLRWRHPQLGFVSPAEFVPLAEKTALMRPLSDWVLRHAMAQLAQWNARNIPLRLAINVSASDMEDSSFLEEAVRLAKTYDIDLSALELEFTESVLIRDASAVGSVLLRARELGMGIAVDDFGTGYSNWTYLRDLPITAIKLDQSFTRDLAGSPKAQSVTQAVIGLASQLGYRVVAEGIETHDTFHLLQAWGCHEGQGYLIAQPMLPEQLEDWLRR | 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 plays crucial roles in stabilizing the overall protein structure and participating in catalysis, and also controls c-di-GMP and Mg(2+) ion binding.
EC: 3.1.4.52
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Q9WY30 | MTVLIVEDDDITREAMGQYLKLSGFNVIEAENGEKAVELSENVDVALVDVMLPGMSGIEVVNKIKAKNPSCVVFVVTAYDDTEIVKKCVEAGADDFIKKPVNLELLRLKITHALRNRVFHMYRNSYLKSLKKKLFLLEKTAEEFFTEYEDFLFEVLEILNMLSEYRDMETHRHTERVGWLSGRIAEEMGMSEVFVTEIQFAAPLHDIGKIGIPDRILLKPGILTPEEFEIMKQHTTIGFRILSRSNSPILQLGAEIALTHHERWDGSGYPRGLKEREIPISGLIVAVADSFDAMVSRRPYKNPKPLEEAFREIESLSGKLYSPEVVEAFLKLEKEITDVYRREKDEDTSHNGGRSHQSSPGEGVEGIR | 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
Sequence Length: 368
EC: 3.1.4.-
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Q06850 | MGNTCVGPSRNGFLQSVSAAMWRPRDGDDSASMSNGDIASEAVSGELRSRLSDEVQNKPPEQVTMPKPGTDVETKDREIRTESKPETLEEISLESKPETKQETKSETKPESKPDPPAKPKKPKHMKRVSSAGLRTESVLQRKTENFKEFYSLGRKLGQGQFGTTFLCVEKTTGKEFACKSIAKRKLLTDEDVEDVRREIQIMHHLAGHPNVISIKGAYEDVVAVHLVMECCAGGELFDRIIQRGHYTERKAAELTRTIVGVVEACHSLGVMHRDLKPENFLFVSKHEDSLLKTIDFGLSMFFKPDDVFTDVVGSPYYVAPEVLRKRYGPEADVWSAGVIVYILLSGVPPFWAETEQGIFEQVLHGDLDFSSDPWPSISESAKDLVRKMLVRDPKKRLTAHQVLCHPWVQVDGVAPDKPLDSAVLSRMKQFSAMNKFKKMALRVIAESLSEEEIAGLKEMFNMIDADKSGQITFEELKAGLKRVGANLKESEILDLMQAADVDNSGTIDYKEFIAATLHLNKIEREDHLFAAFTYFDKDGSGYITPDELQQACEEFGVEDVRIEELMRDVDQDNDGRIDYNEFVAMMQKGSITGGPVKMGLEKSFSIALKL | 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
Sequence Mass (Da): 68254
Sequence Length: 610
Domain: There are 3 contiguous domains conserved in the CDPK subfamily: a kinase domain, an autoinhibitory (junction) domain and a calmodulin-like domain. The autoinhibitory domain (414-444) inactivates kinase activity under calcium-free conditions.
Subcellular Location: Peroxisome membrane
EC: 2.7.11.1
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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-phosphate: step 3/3.
Subcellular Location: Cell inner membrane
EC: 2.7.7.41
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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-phosphate: step 3/3.
Subcellular Location: Cell inner membrane
EC: 2.7.7.41
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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-phosphate: step 3/3.
Subcellular Location: Cell inner membrane
EC: 2.7.7.41
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Q49433 | MNEKAKQFIKKRTSVFIALLVVFCFFLLISAFADGFNFWSPWSADFNSRTLKVEQASGVTSVISTEINENFKAVRFSFSIIIILIVGVIGSLMIWELFTNILKNKPKLSLSLTLLNAGIIIFGMIGTFVVVYFYKWNATVNGIWTLSFTLSVVLLWIIYIACMSKTRIKFSLQLSYSLGAIACFIASIGTIYFSVIRGWTTIFLLMSLAVSVDTFSFLFGKRFGKNPLIKISPSKTWEGAFFGIISTIVVVALLCVLYSIPFFVAKPTFNQTNGIALNTPQNYDSHNLITNIFLIAFISGGSSFYIYWWVSTLALIFTGSVFAIGGDLFFSYIKRLISIKDFSKVLGKHGGVLDRFDSSSFLISFFFVYHLIAGTISNQRLLMEPNTYFSAITSIQS | 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-phosphate: step 3/3.
Subcellular Location: Cell membrane
EC: 2.7.7.41
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P9WPF6 | MSWLNTKKASCWRSSGRSATKSVTTNDAGTGNPAEQPARGAKQQPATETSRAGRDLRAAIVVGLSIGLVLIAVLVFVPRVWVAIVAVATLVATHEVVRRLREAGYLIPVIPLLIGGQAAVWLTWPFGAVGALAGFGGMVVVCMIWRLFMQDSVTRPTTGGAPSPGNYLSDVSATVFLAVWVPLFCSFGAMLVYPENGSGWVFCMMIAVIASDVGGYAVGVLFGKHPMVPTISPKKSWEGFAGSLVCGITATIITATFLVGKTPWIGALLGVLFVLTTALGDLVESQVKRDLGIKDMGRLLPGHGGLMDRLDGILPSAVAAWIVLTLLP | 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-phosphate: step 3/3.
Subcellular Location: Cell membrane
EC: 2.7.7.41
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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-phosphate: step 3/3.
Subcellular Location: Cell inner membrane
EC: 2.7.7.41
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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-phosphate: step 3/3.
Subcellular Location: Cell membrane
EC: 2.7.7.41
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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 transcription . Binds to and activates transcription of LPH (By similarity). Activates transcription of CLDN2 and intestinal mucin MUC2 . Binds to the 5'-AATTTTTTACAACACCT-3' DNA sequence in the promoter region of CA1 and activates CA1 transcription . Important in broad range of functions from early differentiation to maintenance of the intestinal epithelial lining of both the small and large intestine. Binds preferentially to methylated DNA (By similarity).
PTM: Ubiquitinated, leading to its degradation by the proteasome.
Sequence Mass (Da): 33476
Sequence Length: 311
Subcellular Location: Nucleus
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Q9Y232 | MTFQASHRSAWGKSRKKNWQYEGPTQKLFLKRNNVSAPDGPSDPSISVSSEQSGAQQPPALQVERIVDKRKNKKGKTEYLVRWKGYDSEDDTWEPEQHLVNCEEYIHDFNRRHTEKQKESTLTRTNRTSPNNARKQISRSTNSNFSKTSPKALVIGKDHESKNSQLFAASQKFRKNTAPSLSSRKNMDLAKSGIKILVPKSPVKSRTAVDGFQSESPEKLDPVEQGQEDTVAPEVAAEKPVGALLGPGAERARMGSRPRIHPLVPQVPGPVTAAMATGLAVNGKGTSPFMDALTANGTTNIQTSVTGVTASKRKFIDDRRDQPFDKRLRFSVRQTESAYRYRDIVVRKQDGFTHILLSTKSSENNSLNPEVMREVQSALSTAAADDSKLVLLSAVGSVFCCGLDFIYFIRRLTDDRKRESTKMAEAIRNFVNTFIQFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSTVMFPKIMGGASANEMLLSGRKLTAQEACGKGLVSQVFWPGTFTQEVMVRIKELASCNPVVLEESKALVRCNMKMELEQANERECEVLKKIWGSAQGMDSMLKYLQRKIDEF | 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 histone marks, thereby preserving the epigenetic landscape . Required for chromatin targeting and maximal enzymatic activity of Polycomb repressive complex 2 (PRC2); acts as a positive regulator of PRC2 activity by bridging the pre-existing histone H3K27me3 and newly recruited PRC2 on neighboring nucleosomes . Acts as a corepressor for REST by facilitating histone-lysine N-methyltransferase EHMT2 recruitment and H3K9 dimethylation at REST target genes for repression . Involved in X chromosome inactivation in females: recruited to Xist RNA-coated X chromosome and facilitates propagation of H3K9me2 by anchoring EHMT2 (By similarity). Promotes EZH2 accumulation and H3K27me3 methylation at DNA double strand breaks (DSBs), thereby facilitating transcriptional repression at sites of DNA damage and homology-directed repair of DSBs . Required for neuronal migration during brain development by repressing expression of RHOA (By similarity). By repressing the expression of SCN8A, contributes to the inhibition of intrinsic neuronal excitability and epileptogenesis (By similarity). In addition to acting as a chromatin reader, acts as a hydro-lyase . Shows crotonyl-coA hydratase activity by mediating the conversion of crotonyl-CoA ((2E)-butenoyl-CoA) to beta-hydroxybutyryl-CoA (3-hydroxybutanoyl-CoA), thereby acting as a negative regulator of histone crotonylation . Histone crotonylation is required during spermatogenesis; down-regulation of histone crotonylation by CDYL regulates the reactivation of sex chromosome-linked genes in round spermatids and histone replacement in elongating spermatids (By similarity). By regulating histone crotonylation and trimethylation of H3K27, may be involved in stress-induced depression-like behaviors, possibly by regulating VGF expression (By similarity).
Catalytic Activity: 3-hydroxybutanoyl-CoA = (2E)-butenoyl-CoA + H2O
Sequence Mass (Da): 66482
Sequence Length: 598
Domain: The chromo domain recognizes and binds histone H3K9me3, histone H3K27me2 and histone H3K27me3.
Subcellular Location: Nucleus
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Q9WTK2 | MGIGNSQPNSQEAQLCTLPEKAEQPTDDNTCQQNNVVPATVSEPDQASPAIQDAETQVESIVDKRKNKKGKTEYLVRWKGYDSEDDTWEPEQHLVNCEEYIHDFNRRHNERQKEGSLARASRASPSNARKQISRSTHSTLSKTNSKALVVGKDHESKSSQLLAASQKFRKNPAPSLANRKNMDLAKSGIKILVPKSPVKGRTSVDGFQGESPEKLDPVDQGAEDTVAPEVTAEKPTGALLGPGAERARMGSRPRIHPLVPQVSGPVTAAMATGLAVNGKGTSPFMDALAANGTVTIQTSVTGVTAGKRKFIDDRRDQPFDKRLRFSVRQTESAYRYRDIVVRKQDGFTHILLSTKSSENNSLNPEVMKEVQSALSTAAADDSKLVLLSAVGSVFCCGLDFIYFIRRLTDDRKRESTKMADAIRNFVNTFIQFKKPIIVAVNGPAIGLGASILPLCDVVWANEKAWFQTPYTTFGQSPDGCSTVMFPKIMGGASANEMLFSGRKLTAQEACGKGLVSQVFWPGTFTQEVMVRIKELASCNPVVLEESKALVRCNMKMELEQANERECEVLKKIWGSAQGMDSMLKYLQRKIDEF | 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 histone marks, thereby preserving the epigenetic landscape . Required for chromatin targeting and maximal enzymatic activity of Polycomb repressive complex 2 (PRC2); acts as a positive regulator of PRC2 activity by bridging the pre-existing histone H3K27me3 and newly recruited PRC2 on neighboring nucleosomes (By similarity). Acts as a corepressor for REST by facilitating histone-lysine N-methyltransferase EHMT2 recruitment and H3K9 dimethylation at REST target genes for repression (By similarity). Involved in X chromosome inactivation in females: recruited to Xist RNA-coated X chromosome and facilitates propagation of H3K9me2 by anchoring EHMT2 . Promotes EZH2 accumulation and H3K27me3 methylation at DNA double strand breaks (DSBs), thereby facilitating transcriptional repression at sites of DNA damage and homology-directed repair of DSBs (By similarity). Required for neuronal migration during brain development by repressing expression of RHOA . By repressing the expression of SCN8A, contributes to the inhibition of intrinsic neuronal excitability and epileptogenesis . In addition to acting as a chromatin reader, acts as a hydro-lyase (By similarity). Shows crotonyl-coA hydratase activity by mediating the conversion of crotonyl-CoA ((2E)-butenoyl-CoA) to beta-hydroxybutyryl-CoA (3-hydroxybutanoyl-CoA), thereby acting as a negative regulator of histone crotonylation (By similarity). Histone crotonylation is required during spermatogenesis; down-regulation of histone crotonylation by CDYL regulates the reactivation of sex chromosome-linked genes in round spermatids and histone replacement in elongating spermatids . By regulating histone crotonylation and trimethylation of H3K27, may be involved in stress-induced depression-like behaviors, possibly by regulating VGF expression . May have histone acetyltransferase activity; such activity is however unsure in vivo .
Catalytic Activity: acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-lysyl-[protein]
Sequence Mass (Da): 65211
Sequence Length: 593
Domain: The chromo domain recognizes and binds histone H3K9me3, histone H3K27me2 and histone H3K27me3.
Subcellular Location: Nucleus
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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 protein
Sequence Mass (Da): 28878
Sequence Length: 271
Domain: The N-terminal alpha-helix of peptide ECE1-III allows insertion of the toxin into host epithelial cells membranes .
Subcellular Location: Secreted
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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 cells membranes.
Subcellular Location: Secreted
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Q5B7R2 | MALLLSLSLLATTISAQQIGTPEIRPRLTTYHCTSANGCTEQNTSVVLDAATHPIHDASNPSVSCTTSNGLNPALCPDKQTCADNCVIDGITDYAAHGVETHGSRLTLTQYRNVNGALSSVSPRVYLVDESDPDEQEYRALSLLAQEFTFTVNVSALPCGMNGALYLSEMSPSGGRSALNPAGASYGTGYCDAQCYVNPWINGEGNINGYGACCNEMDIWEANSRSTGFTPHACLYEPEETEGRGVYECASEDECDSAGENDGICDKWGCGFNPYALGNTEYYGRGQGFEVDTKEPFTVVTQFLTDDGTSTGALTEIRRLYIQNGQVIENAVVSSGADSLTDSLCASTASWFDSYGGMEGMGRALGRGMVLAMSIWNDAGGYMQWLDGGDAGPCNATEGAPEFIEEHTPWTRVVFEDLKWGDIGSTFQAS | 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 cellulose, lichenin and cereal beta-D-glucans.
Sequence Mass (Da): 45929
Sequence Length: 430
Subcellular Location: Secreted
EC: 3.2.1.4
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Q9CJ32 | MNGITAWMEKYLVPVAAKIGSQKHLVALRDSFIGMLPATLAGALAAMISAIVTTFPSAIQQMMLGATAFSKLAPEKVWTLANTPIIGDLNNISALVNQGTLTVIGLIFAFSWGYNLARAYGVNDLAGGIVSLATLFAGLPNQMGKFTAALGTGKAGVAATDKLNGVLGDQGLAAWKPLFASAHLDAGAYFTVIIMGALAVIIYAKLMLADITIKMPESVPPAVAKAFLAIIPTIAALYIVGLIYYIIGKLTNDSVINLITHYIAEPFQILSQNIFSVLIVTLFVSVFWFFGLHGPNVLAPVLDGIWGPLGLNNQALYFQVHSQGIRDLIAKGAVDKAHAINGDYVNLWVRGSWDAFAWFGGSGGTITLVIAIILFSKRKDYKIVGRLGLAPGIFNINEPVLFGLPVVLNAIFFIPFAVAPLISVIIAYTATALHLVDPVVNAVPWVTPPIMNAFMATGFDWRAIVLTIINLIITFVIWVPFVIAANKLEETELD | 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. This system can also transport lactose .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 52780
Sequence Length: 494
Domain: The EIIC type-3 domain forms the PTS system translocation channel and contains the specific substrate-binding site.
Subcellular Location: Cell membrane
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A0A0U4EBH5 | MNKWHINKWYFFVGMLVIFAVIISLILKDTSLTFSSYDREKFPHLIGNSMVKKPSLAGRLKIIEIDGRKTLGDQHGNPIQLRGMSTHGLQWFPQIINNNAFSALSKDWEANVIRLAMYVGEGGYSTDPSVKEKVIEGINLAIKNDMYVIVDWHILNPGDPNAKIYSGAKEFFKEIASKYPNDLHIIYELANEPNPTESDITNDIAGWEKVKKYAEPIIKMLRDMGNENIIIVGNPEWSTRPDLAVNDPIDDKNVMYSAHFYTGSASVWENGNKGHIARNIEKALENGLTVFVTEWGTSEASGDGGPYLNEADEWLEFLNSNNISWVNWSLANKNEASAAFLPTTSLDPGNGKVWAVNQLSLSGEYVRARIKGIPYKPISRETMGK | 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 glycans, such as laminarin. Likewise, lacks activity with xylan, galactomannan and pectin.
Catalytic Activity: Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 43215
Sequence Length: 385
Subcellular Location: Cell membrane
EC: 3.2.1.4
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P10477 | MKKIVSLVCVLVMLVSILGSFSVVAASPVKGFQVSGTKLLDASGNELVMRGMRDISAIDLVKEIKIGWNLGNTLDAPTETAWGNPRTTKAMIEKVREMGFNAVRVPVTWDTHIGPAPDYKIDEAWLNRVEEVVNYVLDCGMYAIINVHHDNTWIIPTYANEQRSKEKLVKVWEQIATRFKDYDDHLLFETMNEPREVGSPMEWMGGTYENRDVINRFNLAVVNTIRASGGNNDKRFILVPTNAATGLDVALNDLVIPNNDSRVIVSIHAYSPYFFAMDVNGTSYWGSDYDKASLTSELDAIYNRFVKNGRAVIIGEFGTIDKNNLSSRVAHAEHYAREAVSRGIAVFWWDNGYYNPGDAETYALLNRKTLSWYYPEIVQALMRGAGVEPLVSPTPTPTLMPTPSPTVTANILYGDVNGDGKINSTDCTMLKRYILRGIEEFPSPSGIIAADVNADLKINSTDLVLMKKYLLRSIDKFPAEDSQTPDEDNPGILYNGRFDFSDPNGPKCAWSGSNVELNFYGTEASVTIKSGGENWFQAIVDGNPLPPFSVNATTSTVKLVSGLAEGAHHLVLWKRTEASLGEVQFLGFDFGSGKLLAAPKPLERKIEFIGDSITCAYGNEGTSKEQSFTPKNENSYMSYAAITARNLNASANMIAWSGIGLTMNYGGAPGPLIMDRYPYTLPYSGVRWDFSKYVPQVVVINLGTNDFSTSFADKTKFVTAYKNLISEVRRNYPDAHIFCCVGPMLWGTGLDLCRSYVTEVVNDCNRSGDLKVYFVEFPQQDGSTGYGEDWHPSIATHQLMAERLTAEIKNKLGW | 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 synthetic substrate 4-nitrophenyl acetate (4-NPAc) .
Catalytic Activity: Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
Sequence Mass (Da): 90230
Sequence Length: 814
Domain: Contains an N-terminal module that displays cellulase activity (CtCel5C), a central type I dockerin module (Doc) that facilitates the integration of the enzyme into the cellulosome, and a C-terminal module, CtCE2, which displays dual activities: it catalyzes the deacetylation of plant polysaccharides and also potentiates the activity of its appended cellulase catalytic module through its non-catalytic cellulose binding function.
Pathway: Glycan metabolism; cellulose degradation.
Subcellular Location: Secreted
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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 | MNGTLDHPDQPDLDAIKMFVGQVPRTWSEKDLRELFEQYGAVYEINVLRDRSQNPPQSKGCCFVTFYTRKAALEAQNALHNMKVLPGMHHPIQMKPADSEKNNAVEDRKLFIGMISKKCTENDIRVMFSSFGQIEECRILRGPDGLSRGCAFVTFTTRAMAQTAIKAMHQAQTMEGCSSPMVVKFADTQKDKEQKRMAQQLQQQMQQISAASVWGNLAGLNTLGPQYLALYLQLLQQTASSGNLNTLSSLHPMGGLNAMQLQNLAALAAAASAAQNTPSGTNALTTSSSPLSVLTSSGSSPSSSSSNSVNPIASLGALQTLAGATAGLNVGSLAGMAALNGGLGSSGLSNGTGSTMEALTQAYSGIQQYAAAALPTLYNQNLLTQQSIGAAGSQKEGPEGANLFIYHLPQEFGDQDLLQMFMPFGNVVSAKVFIDKQTNLSKCFGFVSYDNPVSAQAAIQSMNGFQIGMKRLKVQLKRSKNDSKPY | 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. Specifically activates exon 5 inclusion of cardiac isoforms of TNNT2 during heart remodeling at the juvenile to adult transition. Acts as both an activator and repressor of a pair of coregulated exons: promotes inclusion of the smooth muscle (SM) exon but exclusion of the non-muscle (NM) exon in actinin pre-mRNAs. Activates SM exon 5 inclusion by antagonizing the repressive effect of PTB. Promotes exclusion of exon 11 of the INSR pre-mRNA. Inhibits, together with HNRNPH1, insulin receptor (IR) pre-mRNA exon 11 inclusion in myoblast. Increases translation and controls the choice of translation initiation codon of CEBPB mRNA. Increases mRNA translation of CEBPB in aging liver (By similarity). Increases translation of CDKN1A mRNA by antagonizing the repressive effect of CALR3. Mediates rapid cytoplasmic mRNA deadenylation. Recruits the deadenylase PARN to the poly(A) tail of EDEN-containing mRNAs to promote their deadenylation. Required for completion of spermatogenesis (By similarity). Binds to (CUG)n triplet repeats in the 3'-UTR of transcripts such as DMPK and to Bruno response elements (BREs). Binds to muscle-specific splicing enhancer (MSE) intronic sites flanking the alternative exon 5 of TNNT2 pre-mRNA. Binds to AU-rich sequences (AREs or EDEN-like) localized in the 3'-UTR of JUN and FOS mRNAs. Binds to the IR RNA. Binds to the 5'-region of CDKN1A and CEBPB mRNAs. Binds with the 5'-region of CEBPB mRNA in aging liver. May be a specific regulator of miRNA biogenesis. Binds to primary microRNA pri-MIR140 and, with CELF2, negatively regulates the processing to mature miRNA .
PTM: Phosphorylated. Its phosphorylation status increases in senescent cells.
Sequence Mass (Da): 52063
Sequence Length: 486
Domain: RRM1 and RRM2 domains preferentially target UGU(U/G)-rich mRNA elements.
Subcellular Location: Nucleus
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P28659 | MNGTLDHPDQPDLDAIKMFVGQVPRTWSEKDLRELFEQYGAVYEINILRDRSQNPPQSKGCCFVTFYTRKAALEAQNALHNMKVLPGMHHPIQMKPADSEKNNAVEDRKLFIGMISKKCTENDIRVMFSSFGQIEECRILRGPDGLSRGCAFVTFTTRTMAQTAIKAMHQAQTMEGCSSPMVVKFADTQKDKEQKRMAQQLQQQMQQISAASVWGNLAGLNTLGPQYLALYLQLLQQTASSGNLNTLSSLHPMGGLNAMQLQNLAALAAAASAAQNTPSGTNALTTSSSPLSVLTSSGSSPSSSSSNSVNPIASLGALQTLAGATAGLNVGSLAGMAALNGGLGSSGLSNGTGSTMEALTQAYSGIQQYAAAALPTLYNQNLLTQQSIGAAGSQKEGPEGANLFIYHLPQEFGDQDLLQMFMPFGNVVSAKVFIDKQTNLSKCFGFVSYDNPVSAQAAIQSMNGFQIGMKRLKVQLKRSKNDSKPY | 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 similarity). Specifically activates exon 5 inclusion of cardiac isoforms of TNNT2 during heart remodeling at the juvenile to adult transition (By similarity). Acts as both an activator and repressor of a pair of coregulated exons: promotes inclusion of the smooth muscle (SM) exon but exclusion of the non-muscle (NM) exon in actinin pre-mRNAs (By similarity). Activates SM exon 5 inclusion by antagonizing the repressive effect of PTB (By similarity). Promotes exclusion of exon 11 of the INSR pre-mRNA (By similarity). Inhibits, together with HNRNPH1, insulin receptor (IR) pre-mRNA exon 11 inclusion in myoblast (By similarity). Increases translation and controls the choice of translation initiation codon of CEBPB mRNA (By similarity). Increases mRNA translation of CEBPB in aging liver. Increases translation of CDKN1A mRNA by antagonizing the repressive effect of CALR3 (By similarity). Mediates rapid cytoplasmic mRNA deadenylation (By similarity). Recruits the deadenylase PARN to the poly(A) tail of EDEN-containing mRNAs to promote their deadenylation (By similarity). Required for completion of spermatogenesis. Binds to (CUG)n triplet repeats in the 3'-UTR of transcripts such as DMPK and to Bruno response elements (BREs) (By similarity). Binds to muscle-specific splicing enhancer (MSE) intronic sites flanking the alternative exon 5 of TNNT2 pre-mRNA (By similarity). Binds to AU-rich sequences (AREs or EDEN-like) localized in the 3'-UTR of JUN and FOS mRNAs. Binds to the IR RNA (By similarity). Binds to the 5'-region of CDKN1A and CEBPB mRNAs (By similarity). Binds with the 5'-region of CEBPB mRNA in aging liver. May be a specific regulator of miRNA biogenesis. Binds to primary microRNA pri-MIR140 and, with CELF2, negatively regulates the processing to mature miRNA (By similarity).
PTM: Phosphorylated. Phosphorylated by CDK4 on Ser-302. Its phosphorylation status increases in aging liver and is important for the formation of the EIF2 complex and activation of CEBPB mRNA translation. Hyperphosphorylated in the EIF2 complex. EGFR signaling regulates its phosphorylation status in epithelial cells.
Sequence Mass (Da): 52107
Sequence Length: 486
Domain: RRM1 and RRM2 domains preferentially target UGU(U/G)-rich mRNA elements.
Subcellular Location: Nucleus
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Q28HE9 | MNGTMDHPDHPDPDSIKMFVGQVPRSWSEKELRELFEQYGAVYEINVLRDRSQNPPQSKGCCFITFYTRKAALEAQNALHNMKVLPGMHHPIQMKPADSEKNNAVEDRKLFVGMVSKKCNENDIRAMFSQFGQIEESRILRGPDGMSRGCAFVTFTTRSMAQMAIKAMHQAQTMEGCSSPIVVKFADTQKDKEQKRMTQQLQQQMQQLNAASMWGNLAGLSSLAPQYLALLQQTASSGNLNSLSGLHPMGGEYATGMTSGLNAMQLQNLAALAAAASAAQNTPSAGSALTTSSSPLSILTSSGSSPSSNNNSAVNPMASLGALQTLAGATAGLNVGSLAGMAALNGGLGSSLSNGTGSTMEALSQAYSGIQQYAAAALPSLYNQSLLSQQGLGAAGSQKEGPEGANLFIYHLPQEFGDQDLLQMFMPFGNVVSAKVFIDKQTNLSKCFGFVSYDNPVSAQAAIQSMNGFQIGMKRLKVQLKRSKNDSKPY | 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 fertilization. Binds to AU-rich sequences (AREs) of jun mRNA. Binds to the embryonic deadenylation element (EDEN) motif localized in the 3'-UTR of maternal mRNAs. Binds to RNA containing several repeats of the consensus sequence 5'-UGU-3'. EDEN-dependent deadenylation is enhanced by the presence of an additional cis element composed of three AUU repeats (By similarity).
PTM: Phosphorylated during oocyte maturation and dephosphorylated following egg activation. Dephosphorylation is calcium dependent and correlates with the increase in the activity of EDEN-dependent deadenylation (By similarity).
Sequence Mass (Da): 52387
Sequence Length: 490
Domain: The 2 N-terminal RRMs and a part of the linker region (between RRM2 and RRM3) are necessary for binding to EDEN of mos mRNA.
Subcellular Location: Nucleus
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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 | MDGESPEIMPVECPDPEPASSESGDDHDIPEPLSSRLSVPSGELNLYRAAVALRLVLLAAFFRYRVTRPVADAHALWVTSVACELWLAASWLIAQLPKLSPANRVTYLDRLASRYEKGGEASRLAGVDVFVAAADAAREPPLATANTVLSVLAADYPAGGVACYVHDDGADMLVFESLFEAAGFARRWIPFCRRHGVEPRAPELYFARGVDYLRDRAAPSFVKDRRAMKREYEEFKVRMNHLAARARKVPEEGWIMSDGTPWPGNNSRDHPAMIQVLLGHPGDRDVDGGELPRLFYVSREKRPGFRHHGKAGAMNALLRVSAVLTNGAYVLNLDCDHCVNNSSALREAMCFMMDPVAGNRTCFVQFALRDSGGGDSVFFDIEMKCLDGIQGPVYVGSGCCFSRKALYGFEPAAAADDGDDMDTAADWRRMCCFGRGKRMNAMRRSMSAVPLLDSEDDSDEQEEEEAAGRRRRLRAYRAALERHFGQSPAFIASAFEEQGRRRGGDGGSPDATVAPARSLLKEAIHVVSCAFEERTRWGKEIGWMYGGGVATGFRMHARGWSSAYCSPARPAFRRYARASPADVLAGASRRAVAAMGILLSRRHSPVWAGRRLGLLQRLGYVARASYPLASLPLTVYCALPAVCLLTGKSTFPSDVSYYDGVLLILLLFSVAASVALELRWSRVPLRAWWRDEKLWMVTATSASLAAVFQGILSACTGIDVAFSTETAASPPKRPAAGNDDGEEEAALASEITMRWTNLLVAPTSVVVANLAGVVAAVAYGVDHGYYQSWGALGAKLALAGWVVAHLQGFLRGLLAPRDRAPPTIAVLWSVVFVSVASLLWVHAASFSAPTAAPTTEQPIL | 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-glucosyl](n+1) + H(+) + UDP
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 93472
Sequence Length: 860
Pathway: Glycan metabolism; plant cellulose biosynthesis.
Subcellular Location: Cell membrane
EC: 2.4.1.12
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Q9RLB8 | MKKHFVVGETIKRFLRIGTSLALSISTLSLLPSAPRLSSAAGTIKIMPLGDSITYGMADEGGYRKYLSYFLQQKGYTNVDLVGPEGKDSASFNYNGQSVKYDDNHAGYSGYTITNLPGGWFGQLNGILETMQGGDYIKKYSPDIILLQIGTNDVSNGHLDGSEERLHKLLDYLRENMPSNGKVFLTTIPDLGNSGWGGNSNGDIAKYNELIKKVANDYSSKNVIYADIHSVIDASKDLADGVHPNAGGYEKMGKYWLEQIEGYLKASDGPQQTQPTQPSQGDSGPELIYGDLDGDKTITSFDAVIMRKGLINDFKDNNVKKAADIDQNGKAEVADLVQLQSFIIGKIKEFTVAEKTVTEKPVFEKSYNFPAVNQLKSSKDIPDPFIFMDGSKVESTDDWWKRQSEISCMYEYYMYGKWIDGSDDETTYSISGNSMTINVKRKSTGKTASFKAVINLPKNVRHEGGAPVILGMHKGISESTATSNGYAVITYDSDGMFSAPGTAQDNNQHKGAFYDLYPYGRNWDEQTGDLMAWSWGISRILDALYNGAAKELNINPDSSIVTGVSRYGKAASVCGAFDTRIKMCAPSCSGAGGLALYRYSSVGKTYDFSSKGGSSSYTYKENEPLGSLQASGEQGWFNGRFMEFRNAEQFPMDQHMLGALCCDPDRYLFIIGSCESEDWVNAPSVWMAYLGMKHVWDYVGISDHLAINIHKSGHAVIAEDIEKMVQYFDYHVYGIQPKMNLEELQTSVFALPKNKDSFADTFASKWLY | 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 4-O-methyl-D-glucuronic acid (MeGlcA) side residues in synthetic glucuronoxylan methyl ester, suggesting that it may be able to cleave ester linkages between MeGlcA carboxyl and more complex alcohols, including linkages between hemicellulose and lignin alcohols in plant cell walls .
Catalytic Activity: Deacetylation of xylans and xylo-oligosaccharides.
Sequence Mass (Da): 84835
Sequence Length: 768
Domain: Contains a dockerin-like region in addition to its catalytic domains, suggesting that this enzyme forms part of a cellulosome-like multienzyme complex.
Pathway: Glycan degradation; xylan degradation.
Subcellular Location: Secreted
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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), V2R (EC(50)=299.2 nM) and oxytocin receptor (EC(50)=353.73 nM, partial agonist). Shows a weaker activity on human receptors AVPR1B (EC(50)=51.92 nM), AVPR1A (EC(50)=123.78 nM), AVPR2 (EC(50)=299.2 nM) and oxytocin (OXTR) receptor (EC(50)=455.66 nM, partial agonist). In vivo, exhibits grooming and scratching behavior in mice, following intracerebral injection.
Sequence Mass (Da): 10873
Sequence Length: 101
Domain: The cysteine framework of the conopressin is C-C.
Subcellular Location: Secreted
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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), V2R (EC(50)=299.2 nM) and oxytocin receptor (EC(50)=353.73 nM, partial agonist) . Shows a weaker activity on human receptors AVPR1B (EC(50)=51.92 nM), AVPR1A (EC(50)=123.78 nM), AVPR2 (EC(50)=299.2 nM) and oxytocin (OXTR) receptor (EC(50)=455.66 nM, partial agonist). In vivo, exhibits grooming and scratching behavior in mice, following intracerebral injection .
Sequence Mass (Da): 13875
Sequence Length: 128
Domain: The cysteine framework of the conopressin is C-C.
Subcellular Location: Secreted
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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: Plastid
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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: 227
Pathway: Secondary metabolite biosynthesis; flavonoid biosynthesis.
EC: 5.5.1.6
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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: Secondary metabolite biosynthesis; flavonoid biosynthesis.
EC: 5.5.1.6
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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: Secondary metabolite biosynthesis; flavonoid biosynthesis.
EC: 5.5.1.6
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O80842 | MATSSAHLSFLAGRISPFSSERIGLFPLRGEFRPRMTRFRCSAGPSGFFTRLGRLIKEKAKSDVEKVFSGFSKTRENLAVIDELLLFWNLAETDRVLDELEEALLVSDFGPKITVRIVERLREDIMSGKLKSGSEIKDALKESVLEMLAKKNSKTELQLGFRKPAVIMIVGVNGGGKTTSLGKLAHRLKNEGTKVLMAAGDTFRAAASDQLEIWAERTGCEIVVAEGDKAKAATVLSKAVKRGKEEGYDVVLCDTSGRLHTNYSLMEELIACKKAVGKIVSGAPNEILLVLDGNTGLNMLPQAREFNEVVGITGLILTKLDGSARGGCVVSVVEELGIPVKFIGVGEAVEDLQPFDPEAFVNAIFS | 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 protein (LHCP) integration into thylakoids. Might be also functionally linked to the Sec translocation machinery.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 39679
Sequence Length: 366
Domain: The N-terminal domain (39-56) is necessary and sufficient for thylakoid binding.
Subcellular Location: Plastid
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A0QSS4 | MSKQIEFNETARRAMEAGVDKLADAVKVTLGPRGRHVVLAKSFGGPQVTNDGVTIAREIDLEDPYENLGAQLVKSVATKTNDVAGDGTTTATVLAQALVRAGLRNVAAGANPIALGSGISKAADAVSEALLASATPVDDKKAIAQVATVSSRDEQVGELVGEAMTKVGHDGVVTVEESSTLETYLEVTEGVGFDKGFLSAYFVTDFDSQEAVLEDALVLLHRDKISSLPDLLPLLEKVAEAGKPLLIVAEDVEGEALSTLVVNAIRKTLKAVAVKAPFFGDRRKAFLDDLAIVTGGQVVNPDVGLLLREVGLEVLGSARRVVVNKDSTVIVDGGGTAEAIADRVKQIKSEIETTDSDWDREKLQERLAKLAGGVAVIKVGAATETDLKKRKEAVEDAVAAAKAAVEEGIVTGGGAALVQARSAVEKLRGELSGDEALGVDVFASALSAPLYWIATNAGLDGSVVVNKVSELPKGQGFNAATLEFGDLVSAGVVDPAKVTRSAVLNAASVARMILTTETAVVDKPADEDEHGHGHHHGHAH | 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 + H2O + a folded polypeptide = ADP + phosphate + an unfolded polypeptide.
Sequence Mass (Da): 56153
Sequence Length: 540
Subcellular Location: Cytoplasm
EC: 5.6.1.7
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P0C923 | MAKDIYFNEDARKSLLSGVEKLSNAVKVTLGPKGRNVLIDKKFGSPTVTKDGVSVAREIELENPFENMGAQLLKEVAIKTNDVAGDGTTTATVLAYAIAREGLKNVSSGINPIGIKKGIDHAVNLAAEKIRQSAKKITTKEEIAQVASISANNDSYIGEKIAEAMDKVGKDGVITVEESKTFDTTISYVEGMQFDRGYLSPYFSTNKENMSVNFDDAFILIYEKKISSIKELLPVLEKVLGTNKPLLIIAEDIEGDALAALVLNSVRGALKVCAIKSPGFGDRRKAMLEDIAVLTGGVLISEELGLTLETVEIEQLGQAKTIKVDKDNTTIINTGNKEQIKERSELIKKQIEDSTSEYDKEKLQERLAKLVGGVAVINVGAVTEVELKEKKHRVEDALSATRAAVEEGVVPGGGSTLIEVAMYLDTIDTSKLSYEEKQGFEIVKRSLEEPMRQIISNAGFEGSIYIHQIKTEKKGLGFDASSFKWVNMIESGIIDPAKVTRSALQNAASIAGLLLTTECAITDIKEEKNTSGGGGYPMDPGMGMM | 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 + H2O + a folded polypeptide = ADP + phosphate + an unfolded polypeptide.
Sequence Mass (Da): 58952
Sequence Length: 545
Subcellular Location: Cytoplasm
EC: 5.6.1.7
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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 + H2O + a folded polypeptide = ADP + phosphate + an unfolded polypeptide.
Sequence Mass (Da): 11783
Sequence Length: 114
Subcellular Location: Cytoplasm
EC: 5.6.1.7
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H2L0H3 | MPPRDAVPTSTQVSGIGADGVQTEKVLKNRPKASALRQQKLPAWQPILTATTVIPTVFVIGAIFLPIGVFLFIASDAVSEFTVEYTNCLSPCQLQINLPNAFDGDVFLYYNLENYYQNHRRYVKSRNDQQYLGDLTNVKDCAPFDIDPATKKPIAPCGAIANSIFNDTFTLAHRADTGIVTMVPVTTQGVIWNVDKDRKFKNPPLNDGNLCDAFNNTTKPPNWSKNPCEVGGFENVDFIVWMRTAALPYFKKLWRIVDRTTNPLFSNGLPQGTYILTVENNYPVQSFGGKKEFVISTTSWAGGKNSFLGIAYLVVGSLAIVLGVVFIVIHMKFGHSMNELSNVSEIHH | 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 the recycling and degradation of endocytic cargo and this is likely with the phospholipid-transporting ATPase tat-1.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 38572
Sequence Length: 348
Subcellular Location: Cell membrane
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Q9SRQ2 | MDHQVSLPQSTTTGLSFKVHRQQRELVTPAKPTPRELKPLSDIDDQQGLRFQIPVIFFYRPNLSSDLDPVQVIKKALADALVYYYPFAGRLRELSNRKLAVDCTGEGVLFIEAEADVALAELEEADALLPPFPFLEELLFDVEGSSDVLNTPLLLVQVTRLKCCGFIFALRFNHTMTDGAGLSLFLKSLCELACGLHAPSVPPVWNRHLLTVSASEARVTHTHREYDDQVGIDVVATGHPLVSRSFFFRAEEISAIRKLLPPDLHNTSFEALSSFLWRCRTIALNPDPNTEMRLTCIINSRSKLRNPPLEPGYYGNVFVIPAAIATARDLIEKPLEFALRLIQETKSSVTEDYVRSVTALMATRGRPMFVASGNYIISDLRHFDLGKIDFGPWGKPVYGGTAKAGIALFPGVSFYVPFKNKKGETGTVVAISLPVRAMETFVAELNGVLNVSKG | 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): 50290
Sequence Length: 454
EC: 2.3.1.195
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P17411 | MSQKLKVVTIGGGSSYTPELLEGFIKRYHELPVSELWLVDVEGGKPKLDIIFDLCQRMIDNAGVPMKLYKTLDRREALKDADFVTTQLRVGQLPARELDERIPLSHGYLGQETNGAGGLFKGLRTIPVIFDIVKDVEELCPNAWVINFTNPAGMVTEAVYRHTGFKRFIGVCNIPIGMKMFIRDVLMLKDSDDLSIDLFGLNHMVFIKDVLINGKSRFAELLDGVASGQLKASSVKNIFDLPFSEGLIRSLNLLPCSYLLYYFKQKEMLAIEMGEYYKGGARAQVVQKVEKQLFELYKNPELKVKPKELEQRGGAYYSDAACEVINAIYNDKQAEHYVNIPHHGQIDNIPADWAVEMTCKLGRDGATPHPRITHFDDKVMGLIHTIKGFEIAASNAALSGEFNDVLLALNLSPLVHSDRDAELLAREMILAHEKWLPNFADCIAELKKAH | 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-glucopyranoside-6P. Is also able to hydrolyze phospho-N,N'-diacetylchitobiose.
Catalytic Activity: 6-phospho-beta-D-glucosyl-(1->4)-D-glucose + H2O = D-glucose + D-glucose 6-phosphate
Sequence Mass (Da): 50513
Sequence Length: 450
EC: 3.2.1.86
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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-propionate intermediate.
Catalytic Activity: Fe-coproporphyrin III + 2 H(+) + 2 H2O2 = 2 CO2 + 4 H2O + heme b
Sequence Mass (Da): 29585
Sequence Length: 249
Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis.
EC: 1.3.98.5
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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-propionate intermediate.
Catalytic Activity: Fe-coproporphyrin III + 2 H(+) + 2 H2O2 = 2 CO2 + 4 H2O + heme b
Sequence Mass (Da): 28132
Sequence Length: 243
Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis.
EC: 1.3.98.5
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P0CH62 | MAIKRGADLIVEALEEYGTEQVVGFIGHTSHFVADAFSKSHLGKRVINPATELGGAWMVNGYNYVKDRSAAVGAWHCVGNLLLHAAMQEARTGRIPAVHIGLNSDGRLAGRSEAAQQVPWQSFTPIARSTQRVERLDKVGEAIHEAFRVAEGHPAGPAYVDIPFDLTADQIDDKALVPRGATRAKSVLHAPNEDVREAAAQLVAAKNPVILAGGGVARSGGSEALLKLAEMVGVPVVTTSTGAGVFPETHALAMGSAGFCGWKSANDMMAAADFVLVLGSRLSDWGIAQGYITKMPKFVHVDTDPAVLGTFYFPLLSVVADAKTFMEQLIEVLPGTSGFKAVRYQERENFRQATEFRAAWDGWVREQESGDGMPASMFRAMAEVRKVQRPEDIIVTDIGNHTLPMFGGAILQRPRRLVTSMAEGILGCGFPMALGAQLAEPNSRVFLGTGDGALYYHFNEFRVAVEHKLPVITMVFTNESYGANWTLMNHQFGQNNWTEFMNPDWVGIAKAFGAYGESVRETGDIAGALQRAIDSGKPALIEIPVSKTQGLASDPVGGVGPNLLLKGREIPVDTGGSMYPGENLLHLKS | 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 | MWCLLRGLGRPGALARGALGQQQSLGARALASAGSESRDEYSYVVVGAGSAGCVLAGRLTEDPAERVLLLEAGPKDVLAGSKRLSWKIHMPAALVANLCDDRYNWCYHTEVQRGLDGRVLYWPRGRVWGGSSSLNAMVYVRGHAEDYERWQRQGARGWDYAHCLPYFRKAQGHELGASRYRGADGPLRVSRGKTNHPLHCAFLEATQQAGYPLTEDMNGFQQEGFGWMDMTIHEGKRWSAACAYLHPALSRTNLKAEAETLVSRVLFEGTRAVGVEYVKNGQSHRAYASKEVILSGGAINSPQLLMLSGIGNADDLKKLGIPVVCHLPGVGQNLQDHLEIYIQQACTRPITLHSAQKPLRKVCIGLEWLWKFTGEGATAHLETGGFIRSQPGVPHPDIQFHFLPSQVIDHGRVPTQQEAYQVHVGPMRGTSVGWLKLRSANPQDHPVIQPNYLSTETDIEDFRLCVKLTREIFAQEALAPFRGKELQPGSHIQSDKEIDAFVRAKADSAYHPSCTCKMGQPSDPTAVVDPQTRVLGVENLRVVDASIMPSMVSGNLNAPTIMIAEKAADIIKGQPALWDKDVPVYKPRTLATQR | 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: 1.1.99.1
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Q2T8Y5 | MTEFSSKERYTMIRVLVIDDSATMRILLKKLIDKNEHMECVGVAPNPVAAQELLRETRPDVITLDIEMPKMNGLDFLDRIMRLMPVAVIMISTLTEAGSESALRALELGAIDFIAKPKLDFAEGVQAYAEEIYRKIETAGRAKVKKLTRDVPPVRMDAEPPAKPLLAEAGKDGRVVAVGASTGGTEAVKELLLSLPADCPPLLIAQHMPEPFMRSLAKRLDLLCAMRVKMAEDGETLRRGCVYIAPGHSNLTIDATAAGYVCRIVRNAGEAQSDSSVDELFRSVAAAAGARGVGIVLTGSGSDGAAGARAMMAAGAFNIAQDAETSVVYSMPDAAIAACGINEVLPLEKIAGKLMELDGA | 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 irreversible deamidation of specific glutamine residues to glutamic acid.
PTM: Phosphorylated by CheA. Phosphorylation of the N-terminal regulatory domain activates the methylesterase activity.
Catalytic Activity: [protein]-L-glutamate 5-O-methyl ester + H2O = H(+) + L-glutamyl-[protein] + methanol
Sequence Mass (Da): 38354
Sequence Length: 360
Domain: Contains a C-terminal catalytic domain, and an N-terminal region which modulates catalytic activity.
Subcellular Location: Cytoplasm
EC: 3.1.1.61
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O33558 | MTTHAAAPSTRVLIVDDSAAARAMFKVIVESDPALQVMAAVPDAFAAARAMRTELPDVILLDLELPSMDGLTFLRKIMQQHPIPVVVCSSHVGAGTEAMVSALELGAREVISKPAARNDLERQEASIRICDAIRAATETTRRRSQPEPRPLAPGPKLTADEILPARPPRPVPETMPVVCIGASTGGTEALRDVLTALPASAPPIVIVQHMPRGFTAAFARRLDSLCAIEVLEAEDEMQVMPGRAIIAQGDRHLLLRRRNQGYRVSVLDGAYVCRHRPSVDVLFRSAAQEAGGNALGVIMTGMGDDGARCMAEMRAAGAETIAQNEESCVVYGMPREAVAHGGVGKVEPLDRLAARIMEFGRRHTERTVR | 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 irreversible deamidation of specific glutamine residues to glutamic acid.
PTM: Phosphorylated in vitro by CheA2, but not by CheA1. Phosphorylation of the N-terminal regulatory domain activates the methylesterase activity.
Catalytic Activity: [protein]-L-glutamate 5-O-methyl ester + H2O = H(+) + L-glutamyl-[protein] + methanol
Sequence Mass (Da): 39635
Sequence Length: 369
Domain: Contains a C-terminal catalytic domain, and an N-terminal region which modulates catalytic activity.
Subcellular Location: Cytoplasm
EC: 3.1.1.61
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P62640 | MRKIRVVVIDDSAYSRRAITKMLESMPEVEVIGYATDGEEGIRKIIDLKPDLVTLDLEMPRMDGFTLLRIVMEYSPTAVIVISSRSEDEKVFRALELGAVDFVAKPTKGVSEEILTIREDLHRKVRGVIHLNLAGIVRREREQERASVAAGRRTSGSAPYAKAAVRTESTAPRPAGRLEVVAIGASTGGPPALQRILCALPGAFPQAVVVSQHMPAGFTRTFAERLNRLSPLEICEAADGDEVRAGRVLIAPGGHNMVFERQGSEVRARIVKPGTDDRYVPSVDAMLLSCAEVFGPRTLGVVLTGMGNDGSKGVAAINRAGGQTLAEAEETAVVFGMPKEAIATGVVDKIVSLDRMSREIIQRCGLLSDVD | 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 irreversible deamidation of specific glutamine residues to glutamic acid.
PTM: Phosphorylated by CheA. Phosphorylation of the N-terminal regulatory domain activates the methylesterase activity.
Catalytic Activity: [protein]-L-glutamate 5-O-methyl ester + H2O = H(+) + L-glutamyl-[protein] + methanol
Sequence Mass (Da): 39996
Sequence Length: 371
Domain: Contains a C-terminal catalytic domain, and an N-terminal region which modulates catalytic activity.
Subcellular Location: Cytoplasm
EC: 3.1.1.61
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Q2SFK0 | MDVLIVDDSPVIRQLLRHIIEEGGMRVIGEASNGVEALRCIARRRPDVITMDIHMPVMDGLEASRRIMEEYPTPIVVVTASYSLGDAVTAMQVLEAGAITVTPKPQGPSHPDFERDVESLLRTIRLISEVKVVRRFRRRQGKREEVQPPPPVNHEHEGFQPGVIAIGASTGGPVALKELLQGISRKTPCPVLVVQHISPGFLTSFCEWLNQVSALPVSIGEYGERAERGRVYLAPDGCHMEVDRSCRISLVNGNRDETLCPSVSRLFSSVAKNFGRNAVVVLLSGMGRDGAAEMAELHRLGALTIAQDPATVVVNGMPGEAVKLGAARHVLSPPRIAALLNELPVQSCV | 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 irreversible deamidation of specific glutamine residues to glutamic acid.
PTM: Phosphorylated by CheA. Phosphorylation of the N-terminal regulatory domain activates the methylesterase activity.
Catalytic Activity: [protein]-L-glutamate 5-O-methyl ester + H2O = H(+) + L-glutamyl-[protein] + methanol
Sequence Mass (Da): 37866
Sequence Length: 349
Domain: Contains a C-terminal catalytic domain, and an N-terminal region which modulates catalytic activity.
Subcellular Location: Cytoplasm
EC: 3.1.1.61
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Q2W2W9 | MPARGKISVLIVDDSGMARAMLRSIFEDEDDFDVVAEAVNGREAIEMVRHLRPGLVTMDLEMPEMGGLEAIEEIMCSKAVPILVVSGVADAQKAFGAMSRGAVDVVAKPNVTSAREVEDFVDKARLVAKIPVITVPRTRSAPAAGPTPVPQAPPPPAAPPAGDGGIIAIAASTGGPQALAALLAAIGRPLSCPMVVAQHISDGFASGMADWLNSISAMPVRLAAEGERLTAGTVYLSPSEWNMSVTESRHIALALRPERQVYRPSCDALLTSVAQVAGRRAVGVILTGMGSDGVAGMEAISKAGGTTLGQDEGSSVIFGMNAIAIERGWVQRVLPLAELAASLLEITGASVGAAP | 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 irreversible deamidation of specific glutamine residues to glutamic acid.
PTM: Phosphorylated by CheA. Phosphorylation of the N-terminal regulatory domain activates the methylesterase activity.
Catalytic Activity: [protein]-L-glutamate 5-O-methyl ester + H2O = H(+) + L-glutamyl-[protein] + methanol
Sequence Mass (Da): 36570
Sequence Length: 355
Domain: Contains a C-terminal catalytic domain, and an N-terminal region which modulates catalytic activity.
Subcellular Location: Cytoplasm
EC: 3.1.1.61
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Q1CZL0 | MSVQRPIRVLVVDDSPTMANMLTALLTEEPRIEVVGRAGDGNRAVQLARLLRPDVITMDLLLPGLDGPGAIAAIMSQSPARILVVSAVAEQRGVDLGFQAMSAGALELIGKPNVTNAEELRRWGKELAHSVCLMAEVPVISRRPRAATAPPPPTGARVDIFGVVASTGGPPALADVLSKLPRSLPVPLLIAQHITVGFTQGMVRWLSQVTPLPVSIAKDGERLEPGRVYFPLDGHDLLVDAAGLARLQPSQGGPCPSGDVMLTSLAAAFGRRSGGVVLTGMGEDGARGLLAIRRAGGVTFSQDEASSVVFGMPRAALDVKATDQGVPLASMPELILQSCTFAPFRGGRPEGGPTR | 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 irreversible deamidation of specific glutamine residues to glutamic acid.
PTM: Phosphorylated by CheA. Phosphorylation of the N-terminal regulatory domain activates the methylesterase activity.
Catalytic Activity: [protein]-L-glutamate 5-O-methyl ester + H2O = H(+) + L-glutamyl-[protein] + methanol
Sequence Mass (Da): 37049
Sequence Length: 355
Domain: Contains a C-terminal catalytic domain, and an N-terminal region which modulates catalytic activity.
Subcellular Location: Cytoplasm
EC: 3.1.1.61
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Q9HXT8 | MRIGIVNDMPLAVEALRRALAFEPQHQIVWVASNGAEAVTQCAADTPDVVLMDLLMPVMDGVEATRRIMAESPCAIVIVTVDIEQNVHRVFEAMGYGALDAVNTPALGIGNPQTAAAPLLRKIQNVGWLIGQRDNRGKVQVVPPKAGGARQRLVAIGASAGGPASLAVLLKQLPASFNAAVVLVQHVDEVFAAGMAEWLASESKLPVRLARDGEPPIPGQILLAGTNNHIRLLRNGSLVYTAEPRSFVYRPSIDVFFESVANYWRGDAVGVLLTGMGRDGAQGLKQMRERGFLTIAQDQASCAVYGMPKAAAAIDAAVQILSLEKIAPRLAEVFD | 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 irreversible deamidation of specific glutamine residues to glutamic acid.
PTM: Phosphorylated by CheA. Phosphorylation of the N-terminal regulatory domain activates the methylesterase activity.
Catalytic Activity: [protein]-L-glutamate 5-O-methyl ester + H2O = H(+) + L-glutamyl-[protein] + methanol
Sequence Mass (Da): 35697
Sequence Length: 335
Domain: Contains a C-terminal catalytic domain, and an N-terminal region which modulates catalytic activity.
Subcellular Location: Cytoplasm
EC: 3.1.1.61
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Q88MS5 | MKIAIVNDMPLAVEALRRAVALEPAHQVVWVASNGAEAVQRCTEQLPDLILMDLIMPVMDGVEATRRIMAETPCAIVIVTVDRKQNVHRVFEAMGHGALDVVDTPALGAGDAREAAAPLLRKILNIGWLVGQQRAPAARSVAAPLREASQRRGLVAIGSSAGGPAALEVLLKGLPAAFPAAIVLVQHVDQVFAAGMAEWLSSAAGLPVRLAREGEPPQPGQVLLAGTNHHIRLLQNGQLAYTAEPVNEIYRPSIDVFFESVARYWNGDAVGVLLTGMGRDGAQGLKLMRQQGFLTIAQDQASSAVYGMPKAAAAIDAAVEIRPLERIAGRLTEFFAK | 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 irreversible deamidation of specific glutamine residues to glutamic acid.
PTM: Phosphorylated by CheA. Phosphorylation of the N-terminal regulatory domain activates the methylesterase activity.
Catalytic Activity: [protein]-L-glutamate 5-O-methyl ester + H2O = H(+) + L-glutamyl-[protein] + methanol
Sequence Mass (Da): 35824
Sequence Length: 337
Domain: Contains a C-terminal catalytic domain, and an N-terminal region which modulates catalytic activity.
Subcellular Location: Cytoplasm
EC: 3.1.1.61
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Q92YM4 | MVRILLATSTVELEDLVKRAIEGDASAELVLIARSGREAVRMTGELLPDIVAVELCPSGDDSAETVREIMIAAPTPVVMLSHRDGSQLGTISARALEAGALAVIPAPAAHGMQLEQPAIEKFLSTIKAMSQVKVVRQWRQKVRGDRAAKDQPPTARTPIGIVGIAASTGGPAAIRAILKDISADLPVPILIVQHMSNGFIDGVAASLNATVPLTVKVARNGELLKPGTVYLAPDNCQLGVSGRSRLRVSDDAPVNGFKPSGSYLFGSIARAFKGESLAVVLTGMGDDGTEGLRALRMAGGKAIAQDEKSSVVFGMPKSAIGAGLVDLVLPLESIAENITAIARGRSEPEGETRT | 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 irreversible deamidation of specific glutamine residues to glutamic acid.
Catalytic Activity: [protein]-L-glutamate 5-O-methyl ester + H2O = H(+) + L-glutamyl-[protein] + methanol
Sequence Mass (Da): 36888
Sequence Length: 354
Domain: Contains a C-terminal catalytic domain, and an N-terminal region which modulates catalytic activity.
Subcellular Location: Cytoplasm
EC: 3.1.1.61
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P62645 | MAKQKIRVLIVDDSASVRQVLGTILAEDPEIEVIGTASDPFVAAKRLQNELPDVILLDIEMPRMDGITFLRKIMAQHPIPVVICSSLTPEGSDLMFEALEAGAVDIVPKPRVDTRQALMESSGRLREAIKSAARARVRPRAARKVIEQKLTADAIIPPPVAGRSRPTTERIVCIGVSTGGTEALYDVLEVLPPNCPGILIVQHMPQGFTAAFAKRLNAGCQINVKEAEDGDPVLPGWAYIAPGARHMLLVRSGLRYQIAIKDGPPVSRHRPSADVLFRSAAQYAGANALGIIMTGMGDDGARGLLEMRKLGAYTCAQDEESCVVFGMPKEAIACGAVEKVVSLNQIPREIMAWQQAKQPASAD | 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 irreversible deamidation of specific glutamine residues to glutamic acid.
PTM: Phosphorylated by CheA. Phosphorylation of the N-terminal regulatory domain activates the methylesterase activity.
Catalytic Activity: [protein]-L-glutamate 5-O-methyl ester + H2O = H(+) + L-glutamyl-[protein] + methanol
Sequence Mass (Da): 39080
Sequence Length: 363
Domain: Contains a C-terminal catalytic domain, and an N-terminal region which modulates catalytic activity.
Subcellular Location: Cytoplasm
EC: 3.1.1.61
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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 | MKLCALFAGAVISTSAVAASWEYAWPEEWHQEWPLDEQGPDAWSSSECTVSRLDAFEMEKGRKPVFFSTDPLDDPEAPKMLPLNSTGGEQWEFDGVSEDGQMAFCFGFYRDPNYAILGTGNLRLSAEFSRPNKTRFVRVDYPSSSTVTSCPWGTRGVWKGADYSYTFEVTRDIKVARIGVDAPDLKGSVVMRSVMPPRYPDGSTYPNKEASTEVVPYFRWLEAIPAADVRVDVVMDGQPYRWSGLGGHERLWTAFSWFTCLQAMTAVRVKAGPFAAVHGSFVSAIDKGLYRPSTVLAENDEVIFSTTLHEPSDTEDYAVFTKTYGGRVSGNLKEKATGYELVMVSPSAKKQWSFSITNEAIGFEYMLGEGVGGTGFSGRAVGGSIGLKQYFGPSFAETLEFPKRSYLFKSNYVDAVPEEKGEL | 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 pathway is the synthesis of prochaetoglobosin I via condensation of one acetyl-CoA, 8 malonyl-CoA, and a L-tryptophan molecule by the PKS-NRPS hybrid synthetase cheA, followed by reduction of backbone double bond to install desired geometry by the enoyl reductase cheB . Further multiple oxidation steps performed by the cytochrome P450 monooxygenases cheE and cheG, as well as by the FAD-linked oxidoreductase cheF, lead to the formation of chaetoglobosin A . Depending on the order of action of these reductases, distinct intermediates can be identified . Within the pathway, the cytochrome P450 monooxygenase cheE catalyzes a stereospecific epoxidation on prochaetoglobosin I, cytoglobosin D, and chaetoglobosin J intermediates . The FAD-linked oxidoreductase cheF performs dehydrogenation of the C-20 hydroxyl groups in the 20-dihyrochaetoglobosin A and cytoglobosin D intermediates . Finally, the cytochrome P450 monooxygenase cheG can catalyze the stereospecific dihydroxylation of prochaetoglobosin I and prochaetoglobosin IV at C-19 and C-20, respectively . The Diels-Alderase cheD may play a role in the post-PKS-NRPS biosynthetic steps catalyzing Diels-Alder cyclization (Probable).
Sequence Mass (Da): 46809
Sequence Length: 423
Pathway: Secondary metabolite biosynthesis.
EC: 5.5.1.-
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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 signaling proteins .
Sequence Mass (Da): 28622
Sequence Length: 253
Subcellular Location: Cytoplasm
EC: 3.1.3.-
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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 | MTNQDSDQAWGKLVKVDASPGSEIVLINSECTVGRKKDCDLSFPANKLVSGNHCKITHDQNSGKVWLEDMSTNGTVINMSKVVKKQTHLLQNGDVIYFVYRKNEPEQNIAYVYQSITPQESASHDVEDAGREEDSDLTETESEPAPVEPVIVKPLPQSGHEDPQPSTSSSSLHFYNMPLSTCSDVSARKNPVSSSAVCKGDSTSSGSPAQTRLKWTCWTDGEPEEEMQRKRRKTDRDDPGFGSAHSDASADIPLRGASGKEKTEGATTDKMEESLTCIICQDLLYDCISVQPCMHTFCAACYSGWMERSSFCPTCRCPVERIRKNHILNNLVEAYLLQHPEKCRTEDDLRSMDARNKITQDMLQPKVERSFSDEEASSDYLFELSDNDSDISDMSQPYMMCRQCPGYRKELSSALWICESAQSESLAKTAGDGPSTSSDSTTAAPQEFRCPPQASHLICTCCLQPMPDRRFEHLPPQVSPQHCLVCQKPFCHVYWGCPRIGCHGCLARFSELNLNDKCLDGVFNGNQYESEVLQNYLSCRGMSWRHLLQDSLQALQQGLYHLSDYRITANSFLCYCCGLRTFRELAYKYRERIPPSELPDAVTNRPNCYWGRNCRTQVKAHHALKFNHICEQTRFKN | 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 signaling the presence of mitotic stress caused by microtubule poisons by mediating the 'Lys-48'-linked ubiquitination of target proteins, leading to their degradation by the proteasome. May also promote the formation of 'Lys-63'-linked polyubiquitin chains and functions with the specific ubiquitin-conjugating ubc13-mms2 (ube2n-ube2v2) heterodimer. Substrates that are polyubiquitinated at 'Lys-63' are usually not targeted for degradation, but are rather involved in signaling cellular stress.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 71730
Sequence Length: 637
Domain: The PBZ-type zinc finger (also named CYR) mediates non-covalent poly(ADP-ribose)-binding. Poly(ADP-ribose)-binding is dependent on the presence of zinc and is required for its function in antephase checkpoint.
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Nucleus
EC: 2.3.2.27
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Q96EP1 | MERPEEGKQSPPPQPWGRLLRLGAEEGEPHVLLRKREWTIGRRRGCDLSFPSNKLVSGDHCRIVVDEKSGQVTLEDTSTSGTVINKLKVVKKQTCPLQTGDVIYLVYRKNEPEHNVAYLYESLSEKQGMTQESFEANKENVFHGTKDTSGAGAGRGADPRVPPSSPATQVCFEEPQPSTSTSDLFPTASASSTEPSPAGRERSSSCGSGGGGISPKGSGPSVASDEVSSFASALPDRKTASFSSLEPQDQEDLEPVKKKMRGDGDLDLNGQLLVAQPRRNAQTVHEDVRAAAGKPDKMEETLTCIICQDLLHDCVSLQPCMHTFCAACYSGWMERSSLCPTCRCPVERICKNHILNNLVEAYLIQHPDKSRSEEDVQSMDARNKITQDMLQPKVRRSFSDEEGSSEDLLELSDVDSESSDISQPYVVCRQCPEYRRQAAQPPHCPAPEGEPGAPQALGDAPSTSVSLTTAVQDYVCPLQGSHALCTCCFQPMPDRRAEREQDPRVAPQQCAVCLQPFCHLYWGCTRTGCYGCLAPFCELNLGDKCLDGVLNNNSYESDILKNYLATRGLTWKNMLTESLVALQRGVFLLSDYRVTGDTVLCYCCGLRSFRELTYQYRQNIPASELPVAVTSRPDCYWGRNCRTQVKAHHAMKFNHICEQTRFKN | 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 signaling the presence of mitotic stress caused by microtubule poisons by mediating the 'Lys-48'-linked ubiquitination of target proteins, leading to their degradation by the proteasome. Promotes the ubiquitination and subsequent degradation of AURKA and PLK1. Probably acts as a tumor suppressor, possibly by mediating the polyubiquitination of HDAC1, leading to its degradation. May also promote the formation of 'Lys-63'-linked polyubiquitin chains and functions with the specific ubiquitin-conjugating UBC13-MMS2 (UBE2N-UBE2V2) heterodimer. Substrates that are polyubiquitinated at 'Lys-63' are usually not targeted for degradation, but are rather involved in signaling cellular stress.
PTM: Poly-ADP-ribosylated. In addition to binding non covalently poly(ADP-ribose) via its PBZ-type zinc finger, the protein is also covalently poly-ADP-ribosylated by PARP1.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 73386
Sequence Length: 664
Domain: The PBZ-type zinc finger (also named CYR) mediates non-covalent poly(ADP-ribose)-binding. Poly(ADP-ribose)-binding is dependent on the presence of zinc and is required for its function in antephase checkpoint.
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Nucleus
EC: 2.3.2.27
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Q5FWP4 | MEGLDEKKPWGKLSRLLGAETDSSSELFLYKKEWTIGRKKACDLSFPGNKLVSGEHCKITVNEESGEVSLEDTSTNGTVINKLKVIRKQTYPLKNGDVIYVVYRKNEPEQNVAYLYKSLNQGQDSLHDPADTSGSEEAETQTLSSQDDQLSYEEPQPSTSTSSLFSTPTTSAIPGVQLESAEKSGESLGGHSSTSDASPAIRASIPKSNLSTQEQGSLGPPKKRIRTEDHWTTNKNFVPASCPIGASDESKTPSMKPDKMEETLTCIICQELLHDCVSLQPCMHTFCAACYSGWMERSSLCPTCRCPVERICKNHILNNLVEAYLIQHPEKCRSEEDRCSMDARNKITQDMLQPKVRRSFSDEEGSSEDLLELSDVDSESSDISQPYTVCRQCPGFVRHSMQPPPYPPPSDTETSRTQGDAPSTSTNFPTATQEYVCPSHGSHVICTCCFQPMPDRRAEREHNSHVAPQQCTICLEPFCHMYWGCNRMGCFGCLAPFCELNLGDKCLDGVLNNNNYESDILKNYLASRGLTWKDMLNESLAAVQRGVFMLPDYRINGTTVLCYFCGLRNFRILTYQYRQNIPASELPVTVTSRPNCYWGRNCRTQVKAHHAMKFNHICEQTRFKN | 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 signaling the presence of mitotic stress caused by microtubule poisons by mediating the 'Lys-48'-linked ubiquitination of target proteins, leading to their degradation by the proteasome. May also promote the formation of 'Lys-63'-linked polyubiquitin chains and functions with the specific ubiquitin-conjugating ubc13-mms2 (ube2n-ube2v2) heterodimer. Substrates that are polyubiquitinated at 'Lys-63' are usually not targeted for degradation, but are rather involved in signaling cellular stress.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 70019
Sequence Length: 625
Domain: The PBZ-type zinc finger (also named CYR) mediates non-covalent poly(ADP-ribose)-binding. Poly(ADP-ribose)-binding is dependent on the presence of zinc and is required for its function in antephase checkpoint.
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Nucleus
EC: 2.3.2.27
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Q750G3 | MGRCEFYHPFTPYRIQLELMQQIYGLLESGKKMGIFESPTGTGKTLSLICSTFTWLREHKAGYLQGSTGAQDSEEDSEDEPAWVKENYEQSVLADVTASMRAYEQRLAAVDTDLLVKGAAKRQRVEVAVERPDDGAEFLPDAYHSDVEERPSHAGGRGQLRKQLDADIKRLLRKLDEPDAADKSRLAANPLKVYFASRTHTQLGQFAAQLRLPQFPPSLAGLEQERVKFLPLGSRKQLCIHKKVSKVKSDGINEACMDAVSKSECSFFSAAREPDIIRQFQDQAFSTIQDIEDLVGIGNTLHACPYYSSRELIEGAEVITLPYQHLLLENARKTMGIDLRDSIIVIDEAHNLIDTINSIHSASISLTELRQCKLALQAYLAKFKTRLNSGNRVNLLKLIKMVDVLSQFIETQYKNGKRINDPNDIFMGTSMDVVNIHKLEKYMKTSKVAYKIDKYIQATTSNDLQDRGSRDIKQPILFKVASFLKTLANPSEEGQFFFENGHVLKYMLLEPSEVLKSIVTEAKCVILAGGTMEPVNDFFTQLVPYLAPTDVTTYSCGHVIPDDNLNAFIVSENFEFTFANREDIALIERLFHFIYQLASRVPFGMVVFFSSYKYIDFVVKTWTDRGLLSRLDAIKRIYHETSDGADVLKGYSETIQSEKKGAILLAVVGGRLSEGINFENELARAVVLVGLPFPNMFSGEMIVKQQHIKEKVIRNGGTQEDVNKAVREFYENICMKAVNQSVGRAIRHASDFANVYLIDKRYSGPRIQQKLSDWVRKRIQSASNIPKILSDTEAFFSGKGL | 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 specific role in chromosome segregation during meiosis II (By similarity).
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 90288
Sequence Length: 801
Subcellular Location: Nucleus
EC: 3.6.4.12
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A1CJ34 | MCQKYDTLSGDRDVEHDEHFVLEDYDSESEDQNISSKSLGHSSELSMSTLALLERFKKQYSAPTEEEETVGDDEPKIFYCSRTHSQLAQFASELRRVEMPPSLPKELSEKLTDSEALEERVKHLSLGSRKNLCINPRVMKLENATAINERCMDLQQPGMAVEHRCPYLPSKDDEPQVLQFRDHTLATVKDIEDMGKLGKHIGVCPYYASRSVIKHSEIVTLPYPLLLQRSAREALGLSIKNHIVIIDEAHNLMDAISNIHSVTITLSQLQTAIFQLTTYARKFKTRLKGKNRTYIAQVIRLVSSVADHLRSIQGSNQPPDGAVKTSDLMAGKGVDQINPYKLSHYLQESKLARKVDGYVEYSKDTANRQSHGKPSTPVLFHVQSFLLPLMNPSAEGRLFYMKDQNDIQLKYLLLDPTNHFREIVEDARAVILAGGTMSPMSDYMNHLFPYVPASRLDTFSYGHVIPPENLVAHTLAQGVMGCAFDFTYESRDSEKMIIDLGRTVATLCQAIPDGVVAFFPSYDYLSRILHIWKKPLGADKNQTILGLIERKKPILYESRDMTTKSDDILQEYTRTIDSGSGALLLSVIGGKLSEGINFSDRLGRGVLIIGLPFPNIRSAVWQAKLQYVEQKAYSGSSGSETDRQMIAKAAGRDFYENACMRAVNQCIGRAIRHRNDYAAIVMIDRRYDKPNIQGKLPAWIKQSMVRSPTQRPAGATVQNLIKFFAARGSLD | 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 specific role in chromosome segregation during meiosis II (By similarity).
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 82217
Sequence Length: 731
Subcellular Location: Nucleus
EC: 3.6.4.12
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Q4WWE9 | MLEFAKRESARAVTEKRRALEARLEKIKVEEEKQRHATDHPKEARKRRRVDTSSGDPGPEQDDQFILDDYDSDADERMASSKKLSDISGLSTSTLELLERFKEQFSAPVEDEIGHEDDDVKIFYCSRTHSQLSQFSSELRRVKMPSSMPAELSTSDANTDEVQERVKHLTLGSRKNLCINPKVMSLGNAAAINERCLELQQPGIAAEKRCPYLPSKEDEGQILQFRDHTLATIKDIEDMGKLGKRMGICPYYASRSVLKHSENVLLKAQKIVTLPYPLLLQRSARDALDLSIKNHVVIIDEAHNLMDAICNIHSVTIRLSQLQTALLQLTTYAHKHKARLKGKNRSYIAQIIRLVSSIRDHLRSILGQNLPAEGTVDPSDLMAGKGVDQINPYKLSRYLQESKLARKVDGYVEFLKNKNQQSDDKPSSPVLFLVQSFLLSLMNPSAEGRFFYLKCHDDIQLRYMLLDPTNQFREIVEDARAVILAGGTMSPMSDYRNHLFSYIAPSRLDTFSYGHVIPPENLIAHTLVNGVLGSEFDFTYDSRDSEKMILDLGRTVATLCQAIPDGVVAFFPSYDYLSRIVAIWRKPLEGEKGETILSLIEREKSILYEGRDMGPKTDDLLQEYTRTIDSGQGALLLSVVGGKLSEGINFSDKLGRGVLIIGLPFPNIRSAVWQAKIQYVEQKTYNSSSGSEKDRQSIAKAAGKDFYENACMRAVNQCIGRAIRHRNDYAAIVMIDRRYEKANIQGKLPAWIKESMLRRSVRRPASALAADLSNFFSGRSPR | 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 specific role in chromosome segregation during meiosis II (By similarity).
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 88226
Sequence Length: 782
Subcellular Location: Nucleus
EC: 3.6.4.12
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Q21489 | MDEFSFPFQPYDIQLNLMREIRQCIEQRKIGIFESPTGTGKSLSVLCSTMTWLEAEELRISTDLSTRLGEVHTKITECDKITTADNWETAVREKMRAQDVETEILEQIQSRERLQSRIDQARRGMVEVSRKRKAPARDTDQFLEPQDEAAPSEEYNNDEKSEKQRDSDFFDDVDEEEEKPLKCLKIFYASRTHSQLEQLAEELAKTRFQPRIVTCASRGTLCVNEEVKKLKLNHLINEKCMELRKNGMSEKEKVQKLEKGTTKKTKTCATSCEFYNSTQIEDVVNGVLSNKLKSTLEVSKQGKLSNGCPYFATRKSVPQCQLVLLPYQVLLHDGTRKAWGIELKDNVIVLDEAHNVLNTISSLYSAEISTKSLTLALRLIREYNAHYKLKLLAHNLLYMKQLESLTSKMLIFLNSQSKEDVMTMAQLARNLNILEINLFKLAEYMEKTDLCKKFHGFYMRLQKEEIKKENEKPKLTGIQKLMAAKEAEPEPEAEPLPPPKPVPSPLFSLKSFIDALTNKCEDGRIIVEKSATEAKFRFMLLNPADRLSEVVTSARATILVGGTMEPAQLLVETLSRGSIGADSIRRFSCCHVIDDSQLLAVTVERTVDGKPFQLTYQTRGADTTLRSLATSIQALIPHIPNGVVIFVPSYDFLFNFQKKMKEFGILKRIEEKKAVFTESRQPTSDVWDRFSRAAKTSKGAILFAVVGGKMSEGINFCDELGRAVIVIGLPYPNKTSVELRERMKFLDTQMPNGGNLLYESLCMHAVNQAIGRAIRHRRDYAAVYLFDDRYAKESTRRKLSTWIGDRTQVKLGFGEIIRKTRSFFEANSKK | 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 | MVSESCSRNYNHPYTPYDIQIQLMDAIYNTIENGYKIGLFESPTGTGKTLSIICSSMTWLRTFKRNNTFLETNNEVEDVYESESEEDEPEWVKKAYQSSIVNRSKNKLIEYEHYLDKIEKEHAQNKRKEEELEIKVHKRRKAMTAAGTDLSEESYLPMDYYSDSEVGKIEDQNLAITKEINRLLKKVENKEEVSYINECPIKIFFSSRTHSQLNQFSSQLRLTNFQASFEDLEERTKYIPLGSRKQLCINEKVRSKGNDQSVNDACLDLQRETNGCQYLPKNYMMSSVTKEFADLSLAKIRDIEDLNELGIELNICPYYSVRKGIEMTEIISLPYQMIFQDTTRKILNLDIKDSIIIIDEAHNIIDVITSMYSIKITSDQLNKVIKSLKIYLNKFLKRLNSGNRINLMKLIKICQILLKFLNTNSEKVKSGDEVQIQDIFKDSTGDLVNIHKLDQFLTKSKIAYKIESYIEKTEMETDNGEKKGRITNSGGSSSSSSSSNPLLFTIIKFLRTLTNLSKEGKFFWDNENGTISLNYMLLDPSAVFKEIVDQAKCVLLCGGTMEPMSDYMDYLFPSVPTNKINTFACGHVIPKENLQVFPISQWNDTNFEFSYQKRNDSKQLMALGEFLIEITKRVPYGVVIFFPSYKYLDQVLQFWRDTKILTSIESEKTIFREPKDPSNVEKVLNEYGYLIQTERKGAILFSVVGGKMSEGINFSDDLARAVIMVGLPYPNAYSGEMVTKRKYIETSELSNGGTTTDAKEKSRNYYENLCMRAVNQSIGRSIRHINDYSIIYLVDRRFSTPRIQNKLSQWVKERISITTTNNNNNNSIYIMESTTDFFNIIR | 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 specific role in chromosome segregation during meiosis II (By similarity).
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 97275
Sequence Length: 842
Subcellular Location: Nucleus
EC: 3.6.4.12
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Q6FKT4 | MDNATKFHHPYSPYDIQLDLMQCVYDTLANPVKKVAIVESPTGTGKTLSLICSTLTWLRDNKADILSSVDTLHSNEDDSHDSEPEWVKDTYKESILKDKLELLDEYEKYLEELHLKENKIIKFGTSIEDKSKVKRRKVTSSSKAKIEVSIEDEDEFVAKPYESDGEETTDLEKKEALSKEVQELLAKFDSSKKNTDNVELGRFASASQNQVRIFFSSRTHSQLNQFAEQLKLTNFPSSFPDKVAHERVKYMPLGSKKQLCINPDVKKWKTLEGINDACSEVRRSKEGCPFYQNTPKWHNSKETNHFRDQVFSDIHDIEDIAKVGESLAVCPYYAARDFIPSSEIVTLPYQYLLSESTRSQLRLDLKGSIVVIDEAHNLVDTINSIHSAEISLSELKQSYNSIILYMKKFKSRLNPGNRVNLLKLSKLITVLINFITTHYKKPGLEVDAFSILESNNTDMLNVHRVLKYIKTSHIAYKLDTYIQKLQEKESPSNQKPSSQPLLYKISKFLECLNNTSSEGSFFFERGPSLRYMLLEPSRIFQDIIDSARCVILAGGTMEPVSQLLQYLVPKLDDSSITKFSCNHVIPDSHLRTYIVNEPQFEFTFEKRNSVNLVQNHLFNFYLELSTTIPKTGGIIGFFPSYKYLDEIIVSWRKAGLFEKLDKERKVFYEMKDGPDPLPDYTSAVANSEGAILFAIVGGKLSEGINFGGNLCRAIVMTGLPYPNVFSGELIISRKHLEEKVLNGGGSKTDANMAAKEFFENICMKAVNQSVGRSIRSINDYSLIYLLDKRYANANIQSKLSQWVRSRIQSVSTVRDVMASSKEFFDQIADT | 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 specific role in chromosome segregation during meiosis II (By similarity).
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 94515
Sequence Length: 830
Subcellular Location: Nucleus
EC: 3.6.4.12
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A5DNW6 | MNRDDPRLTYNHPYKPYDIQVQLMDAIYDTIQNKYKVGLFESPTGTGKTLSIICSSMTWLRNYKKTQDHSTMGSNSSNDNDPNQTSDSDEEPDWVKEAHIKNIRSRTSGLAIDYERHLEELSQTPHAGHTVELGQRTHKRKKRATNDDDFLPDDYNSDTDSNSVETKNAKLQQEINQIMKRVDGSDGKTPGFVNTCPVTIFFSSRTHSQLSQFAHQLSITSFESSLGEIAERIKFMPLSSRKQLCIHPKVSSLSSVSAVNDACVELQQKSDKRCEFMPRVNNPESDQLVQRFADYSFAVIKDIEELHELGADLKVCPYYASRRNIENSEIIALPYQMLLQQATRKSLGLSIKDSIVIIDEAHNLLDVISSINSVSITRKELSSVIASLKLYYNKFTKRLNSGNRIHLMKLIKLCSLVETYIKNCEIQNKCVPGSDVLIDELFQGSTGDLLNIHRIEKYLDKSKIAYKIQTYIEQSREESDEKQASSPLLFKVTAFLKSLVNPSKEGRFFWDKINDDTEIKYLLLDPSEMFRDVVESARCVLLCGGTMEPVEDYYRYLFPYVPGEKIKKFTCGHIVPQENIEVLTVSSRKTTVFDFSYHKRNDPSMLRELALSLQDICERVPNGIIVFAPSYKYLNQLISTWRKDGNLAKISTLKQVFLESSDSTSIESILRDYGAAARGSGAILFSVVGGKMSEGVNFSDELARAVIMLGLPYPNAFSGELIAKRKFIEETTLSKGGTQAMAKKNSREYYENICMRAVNQSVGRSIRHANDYSVIVLFDTRYNSSHIQSKLSGWMRSSIRPERESFDMTLERIADFFAAKTLTKR | 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 specific role in chromosome segregation during meiosis II (By similarity).
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 93770
Sequence Length: 825
Subcellular Location: Nucleus
EC: 3.6.4.12
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O14147 | MCHSKEVKFKTNFHHPYTPYDIQLEFMRSLYSSISDGKIGIFESPTGTGKSLSLICASLTWLDEHGGVLLEDNEKSNDNKSNTSSKIPDWVLEQDLKIQKDLVKETHARLEQRLEEIRKRNQSRKNQMSNNSTTYHRETKRRNINAEASTSDNCNNSNTSVDPMDEYLVTAEYTMPSTSEQSEDLFNNGYSSKVSELLRKLSPDNEKPPIVQKIYFTSRTHSQLQQLVQEIKKLNNQTFSTPIRVVSLASRKNLCINNEVRKLRPTSALNEKCIELQGSAHKCPFLQDNTQLWDFRDEALAEIMDIEELVELGQRLKVCPYYGTREAVDSAQIVTLPYPLLLQESARNALNLTLKDNICIIDEAHNLIDAICSMHSSSISFRQVCIAETQLQQYFLRFEKRLNGNNRMHIKQLIKVVYNLKSFFLNCLETNTNSKVINVDSLLVSNGADQINLHHLSEYLNVSKLARKVDGYTKYMHSLGTQELESLNDLRSERFSNGNGYEEDPYTPVLMQLESFLLNIANPAPEGKLFYEKQTGDNPYLKYLLLDPSKHVEILTEQCRSVNLAGGTMSPIDDFITLLFSDEQSRILPFSCDHIVPPENITTILVSQGPAGVPFEFTHKRKDDENLLKDLGRTFQNFISIIPDGVVVFFPSFAFLQQAVKVWEMNGITNRLNAKKPLFIESKDFGDNPLDTFEHYKQSVDAGLSGMLFSVIGGRLSEGINFSDKLGRAVMVVGMPFPNSQDVEWQAKVSYVEEKAKEKGINAKQASQEFYENTCMRAVNQSIGRAIRHRDDYASIILLDSRYNRSSIQRKLPNWLSKNIHSSPNFGPAIRQLATFFRAKKMCD | 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 specific role in chromosome segregation during meiosis II (By similarity).
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 96204
Sequence Length: 844
Subcellular Location: Cytoplasm
EC: 3.6.4.12
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Q32742 | MTEEKKINPPIFPFTAIVGQEEMKLALQLNVIDPKIGGVMIMGDRGTGKSTTIRAIADLLPEIEVVKDNQFNTAPSEDLNEEIVKIKTPMIDLPLGATEDRVCGTIDIEKALTDGVKAFEPGLLAKANRGILYVDEVNLLDDHLVDILLDSAASGLNTVEREGISIRHAARFVLVGSGNPEEGELRPQLLDRFGMHAVIKTVKDPKLRVRVVEERTLFDLNPEEWINKYREQQEALKTRIIAAQNLISSVTISDDFKLKISQVCSELDVDGLRGDIVTNRAAKAYAAFNNRTEVEIGDIEKVITLCLRHRLRKDPLETIDSGDKVQKLFEEIFD | 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 compound metabolism; chlorophyll biosynthesis.
Subcellular Location: Plastid
EC: 6.6.1.1
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Q53RM0 | MASAFSPATAAPAASPALFSASTSRPLSLTAAAAAVSARIPSRRGFRRGRFTVCNVAAPSATQQEAKAAGAKESQRPVYPFAAIVGQDEMKLCLLLNVIDPKIGGVMIMGDRGTGKSTTVRSLVDLLPDIRVVVGDPFNSDPDDPEVMGPEVRERVLEGEKLPVVTAKITMVDLPLGATEDRVCGTIDIEKALTDGVKAFEPGLLAKANRGILYVDEVNLLDDHLVDVLLDSAASGWNTVEREGISISHPARFILIGSGNPEEGELRPQLLDRFGMHAQVGTVRDAELRVKIVEERARFDRDPKAFRESYLEEQDKLQQQISSARSNLGAVQIDHDLRVKISKVCAELNVDGLRGDIVTNRAAKALAALKGRDTVTVEDIATVIPNCLRHRLRKDPLESIDSGLLVVEKFYEVFT | 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 = ADP + 3 H(+) + Mg-protoporphyrin IX + phosphate
Sequence Mass (Da): 44865
Sequence Length: 415
Pathway: Porphyrin-containing compound metabolism; chlorophyll biosynthesis.
Subcellular Location: Plastid
EC: 6.6.1.1
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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 electron donor to the NB-component of the complex, and binds Mg-ATP.
Catalytic Activity: 2 ADP + chlorophyllide a + oxidized 2[4Fe-4S]-[ferredoxin] + 2 phosphate = 2 ATP + 2 H2O + protochlorophyllide a + reduced 2[4Fe-4S]-[ferredoxin]
Sequence Mass (Da): 32230
Sequence Length: 293
Pathway: Porphyrin-containing compound metabolism; chlorophyll biosynthesis (light-independent).
Subcellular Location: Plastid
EC: 1.3.7.7
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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 electron donor to the NB-component of the complex, and binds Mg-ATP.
Catalytic Activity: 2 ADP + chlorophyllide a + oxidized 2[4Fe-4S]-[ferredoxin] + 2 phosphate = 2 ATP + 2 H2O + protochlorophyllide a + reduced 2[4Fe-4S]-[ferredoxin]
Sequence Mass (Da): 32064
Sequence Length: 290
Pathway: Porphyrin-containing compound metabolism; chlorophyll biosynthesis (light-independent).
Subcellular Location: Plastid
EC: 1.3.7.7
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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 electron donor to the NB-component of the complex, and binds Mg-ATP.
Catalytic Activity: 2 ADP + chlorophyllide a + oxidized 2[4Fe-4S]-[ferredoxin] + 2 phosphate = 2 ATP + 2 H2O + protochlorophyllide a + reduced 2[4Fe-4S]-[ferredoxin]
Sequence Mass (Da): 31945
Sequence Length: 293
Pathway: Porphyrin-containing compound metabolism; chlorophyll biosynthesis (light-independent).
Subcellular Location: Plastid
EC: 1.3.7.7
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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 limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and the budding of enveloped viruses (lentiviruses). ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4 (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 23951
Sequence Length: 213
Subcellular Location: Cytoplasm
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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 limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 24017
Sequence Length: 214
Subcellular Location: Cytoplasm
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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 limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and the budding of enveloped viruses (HIV-1 and other lentiviruses). ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 23907
Sequence Length: 213
Domain: The acidic C-terminus and the basic N-termminus are thought to render the protein in a closed, soluble and inactive conformation through an autoinhibitory intramolecular interaction. The open and active conformation, which enables membrane binding and oligomerization, is achieved by interaction with other cellular binding partners, probably including other ESCRT components (By similarity).
Subcellular Location: Cytoplasm
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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 limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis. ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4 (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 23935
Sequence Length: 213
Subcellular Location: Cytoplasm
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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 limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and the budding of enveloped viruses (lentiviruses). ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. When overexpressed, membrane-assembled circular arrays of CHMP4A filaments can promote or stabilize negative curvature and outward budding. CHMP4A/B/C are required for the exosomal release of SDCBP, CD63 and syndecan (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 24948
Sequence Length: 222
Domain: The acidic C-terminus and the basic N-termminus are thought to render the protein in a closed, soluble and inactive conformation through an autoinhibitory intramolecular interaction. The open and active conformation, which enables membrane binding and oligomerization, is achieved by interaction with other cellular binding partners, probably including other ESCRT components (By similarity).
Subcellular Location: Cytoplasmic vesicle membrane
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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 limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and the budding of enveloped viruses (HIV-1 and other lentiviruses). ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. When overexpressed, membrane-assembled circular arrays of CHMP4A filaments can promote or stabilize negative curvature and outward budding. Via its interaction with PDCD6IP involved in HIV-1 p6- and p9-dependent virus release. CHMP4A/B/C are required for the exosomal release of SDCBP, CD63 and syndecan .
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 25098
Sequence Length: 222
Domain: The acidic C-terminus and the basic N-termminus are thought to render the protein in a closed, soluble and inactive conformation through an autoinhibitory intramolecular interaction. The open and active conformation, which enables membrane binding and oligomerization, is achieved by interaction with other cellular binding partners, probably including other ESCRT components (By similarity).
Subcellular Location: Cytoplasmic vesicle membrane
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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 limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 25155
Sequence Length: 227
Subcellular Location: Cytoplasm
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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 limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 24796
Sequence Length: 220
Subcellular Location: Cytoplasm
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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 limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released . The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis . Together with SPAST, the ESCRT-III complex promotes nuclear envelope sealing and mitotic spindle disassembly during late anaphase . Plays a role in the endosomal sorting pathway. ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. When overexpressed, membrane-assembled circular arrays of CHMP4B filaments can promote or stabilize negative curvature and outward budding. CHMP4A/B/C are required for the exosomal release of SDCBP, CD63 and syndecan .
PTM: ISGylated. Isgylation weakens its interaction with VPS4A.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 24950
Sequence Length: 224
Domain: The acidic C-terminus and the basic N-termminus are thought to render the protein in a closed, soluble and inactive conformation through an autoinhibitory intramolecular interaction. The open and active conformation, which enables membrane binding and oligomerization, is achieved by interaction with other cellular binding partners, probably including other ESCRT components.
Subcellular Location: Cytoplasm
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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 limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 24849
Sequence Length: 222
Subcellular Location: Cytoplasm
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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 limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and the budding of enveloped viruses (HIV-1 and other lentiviruses). Key component of the cytokinesis checkpoint, a process required to delay abscission to prevent both premature resolution of intercellular chromosome bridges and accumulation of DNA damage: upon phosphorylation by AURKB, together with ZFYVE19/ANCHR, retains abscission-competent VPS4 (VPS4A and/or VPS4B) at the midbody ring until abscission checkpoint signaling is terminated at late cytokinesis. Deactivation of AURKB results in dephosphorylation of CHMP4C followed by its dissociation from ANCHR and VPS4 and subsequent abscission . ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. Involved in HIV-1 p6- and p9-dependent virus release. CHMP4A/B/C are required for the exosomal release of SDCBP, CD63 and syndecan .
PTM: Phosphorylated at Ser-210 by AURKB during cytokinesis: together with ZFYVE19/ANCHR, phosphorylated CHMP4C retains abscission-competent VPS4 (VPS4A and/or VPS4B) at the midbody ring until abscission checkpoint signaling is terminated at late cytokinesis.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 26411
Sequence Length: 233
Domain: The acidic C-terminus and the basic N-terminus are thought to render the protein in a closed, soluble and inactive conformation through an autoinhibitory intramolecular interaction. The open and active conformation, which enables membrane binding and oligomerization, is achieved by interaction with other cellular binding partners, probably including other ESCRT components (By similarity).
Subcellular Location: Cytoplasm
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