ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
B1HVP6 | MFEKPLGMRDTFPQIFEKVEAVRQTGRDFLTKRGYEFIKTPAVEYFDTVGKASAIADTHLFKLVDSQGNTLVLRPDMTTPIARVATSKLLKEMIPQRLAYFASVFRAQEAEGGRPAEFDQMGIELIGDQSVFADAEVIVTAMELLKHLKLEAFKVTIGHAGILNCILQDYTESIEQQTTLRTLLVHRNYVGFEEAVDSFNLPKAKADALLQFIEEAMDVKDIRDIEKYVRKNDALVYMQQLAQLLEMADLAAYVTFDFTLSSHMSYYTGMLFEVFALGSGFPLGNGGRYDGLLEVFGSKAGATGFSIRVDRLLETLHGQS... | Function: Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine.
Sequence Mass (Da): 42992
Sequence Length: 385
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: s... |
Q2W2D0 | MTESANRALLPAGLRDMLPPDAEFEASVVHSLMSMFARHGYDRVKPPLIEFEESLLDGAGGGTSSQTFRVMDPMSQKMMGLRADMTPQVARIAATRLGSQPRPLRLSYAGQVLRVKGTQLRPERQFGQAGIELIGSDDAGADAEVLVMTAEALDDLGVPGVSADLALPTLVPAVFAAYGINGETADRLRAALDHKDSATVAAQGGAAAPLLQALIAAAGPAARALAELCALDLPPAAAAERDRLARVVELAGADLPSLTLTVDPVENRGFEYHTGLSFTLFARNMGAELGRGGRYQGGGGEPATGATLFMDSVLAALPGP... | Function: Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine.
Sequence Mass (Da): 39612
Sequence Length: 379
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: s... |
A6VYL1 | MTLADRWLLPEGVDEALPEQAAKIEHLRRTLLNLHESWGYHLVIPPLLEYLDSLLTGAGSDLEIETFKVIDQLSGRLLGIRADFTSQVARIDAHCLKDDGVQRLSYCGSVLRTMPAGLDGTRSPIQLGAEIYGHGGVESDVEVLSLMLQTLSTAGLSNLVLDLGHVDIVSGVLAACNLNADQESKLIELYKAKDLPELDRYAEELGCLTDIQKQWLVGLPRLCGGKEVLKHATDLLGDVNESIRDAIVLLQKVSDSICQRFPKVGLHFDLSDLVSYSYHTGVIFAAYVPGHGNAIARGGRYNNIGQVFGRSRPATGFSTD... | Function: Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine.
Sequence Mass (Da): 42886
Sequence Length: 392
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: s... |
Q2RGV6 | MASNLPLQLPAGVSDLLPPEAAALRQLEQRLLNCFRSWGYQEVMTPTFEFATTFQAGSPAGEEGALYKFIDRQGRVLALRPEMTAPIARLVATSLRRRELPLRLGYSARVFRYEEPQAGRRREFHQAGVELIGAGGVAGDVEIIALAVESLAQAGLEDFRLGLGQVAVTKGVLQDLALPPEAVAGIKSALASKDLVALERIYDEYHLEGERRRRLELLATIHGGREALEEARACFGRTAAAASLAELSRVWEALGAAGLEKWLFIDLGILRDFDYYTGIVFEGYVPGLGAPVCGGGRYDGLLAQFGYPCPATGFALGLER... | Function: Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine.
Sequence Mass (Da): 41904
Sequence Length: 389
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: s... |
Q9K013 | MQTWQLPEHIADVLPTNARQLESAREQLLALFRVHGYELVQPPLMEYAHSLLTHIDAGLSLKTILVTDRLSGRQLGIRADITPQVARIDAHLLSANQGINRLCYAGPVLHAQPDGLLNMREPLQAGAEMYGFADIRGDIELIDLMLKSMKIADMGKVLLSLGHIGIFRALSDAAHLDAGQSATLLALMQDKDTGAVEAQVKAWKLDGMWAKAFSLLPRLYGGREVLSDARGRLPDLSAVGGALGELQAVCDAFPDCEIHIDLSELRVDNYHTGLLYAAYAADFHDAVARGGRYDGLGGYFGRARPATGFSFDLRSFIGRL... | Function: Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine (By similarity).
Sequence Mass (Da): 41746
Sequence Length: 383
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose ... |
Q82V28 | MRNWLLPEYIEDVLPRDAYRIEKIRRLIMDMLFAHGYQFVMPPLLEYVESLLAGSGSGMNLRMFKVVDQLSGRMMGLRADMTPQAARIDAHLLNISGVTRLCYASSVVHTVPDEITRTREPFQVGAELYGHSGIESDLEIQCLLLECLSVSGIHSIHLDLGHIRVFRSLIRDSGIKPEFEMELYAALWAKDISSLKELVRTGLNKRLTRSVQNALLLLPELYGDGTVLLSARQHLPDFPEIGEALDQLEHVARILQPYVDRITFDLADLRGYHYHTGMVFAVYTPGCPAPIALGGRYDEIGKSFGRARPATGFSLDLKQL... | Function: Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine.
Sequence Mass (Da): 43900
Sequence Length: 391
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: s... |
Q2YBX1 | MNMSAWALPEYIEDILPAEALKIEMMRRRVLDWLFVNGYELVGPPLLEYVESLLTGSGGQMNLRVLKVVDQLSGRMMGLRADMTPQVARIDAHLLNRKGITRLCYAGSVLHARPSGLTRTREPLQIGAELYGHQGLESDLEIQRLMLQSLAIAGVGNIHLDLGHVAVFRGLIRSTGISPDLEMELSGALQGKDKAALKELCAGLKKQVDASVREALQLLPELYGDENVLTLARSALPSYPGIMKALDELEMVASELSPLVDTLAFDLADLRGYHYHSGMVFAAYTDNCPNAIAVGGRYDEVGKAFGRARPATGFSMDLRE... | Function: Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine.
Sequence Mass (Da): 42932
Sequence Length: 393
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: s... |
Q97YX6 | MNRDIGKNAERELVSILRGEGFNAVRIPTSNSSPNPLPDIFATKGNTLLSIECKSTWENKVKVKEHQVRKLLDFLSMFTMKGVPLIAIKFKQVHEWRVLVPEKAEDIIVTIDNSIPIEDLFKILEKRIEEKILTP | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: A structure-specific endonuclease that resolves Holliday junction (HJ) intermediates during genetic recombination. Acts only on 4-way DNA junctions in a sequence non-specific manner; introduces paired nicks in opposing strands 2 bases 3' of the point of strand exchang... |
O07778 | MPITPLLHESVARFAATGADITTRAEPDLFVSIDPDHLRRILTAVLDNAITHGDGEIAVTAHARDGAVDIGVRDHGPGFADHFLPVAFDRFTRADTARGGRGSGLGLAIVAALTTTHGGHANATNHPDGGAELRITLPTPRPPFHEELPRITSSDTKDPNREHDTSDQ | Function: Member of the three-protein two-component system HK1/HK2/TcrA. Kinase that binds ATP and catalyzes the transfer of a phosphoryl group from ATP to HK2.
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Sequence Mass (Da): 17854
Sequence Length: 168
EC: 2.7.13.3
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O07777 | MALVLAAAGAVTVVQFRDAAHEADPDGALRGLTDDITADLVRELVTILPIVLVIAAVAAYLLSRAALRPVDRIRAAAQTLTTTPHPDTDAPLPVPPTDDEIAWLATTLNTMLTRLQRALAHEQQFVADASHELRTPLALLTTELELRCAGPDPPTS | Function: Member of the three-protein two-component system HK1/HK2/TcrA. HK2 transfers its phosphoryl group to TcrA.
PTM: Phosphorylated by HK1.
Location Topology: Single-pass membrane protein
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Sequence Mass (Da): 16595
Sequence Length:... |
Q91W97 | MFAVHLVAFYFTKLKEDQIKKVDRFLYHMRLSDETLVDIMARFQAEMEKGLGKDTNPTASVKMLPTFVRAIPDGSENGEFLSLDLGGSKFRVLKVQVSQEGQQNVQMESQFYPMPNEITRGNGTELFDYVADCLADFMKTKNLTHKKLPLGFTFSFPCRQNKLEEGVLLSWTKKFKARGVQDTDVVNRLATAMKKHKDLDVDILALVNDTVGTMMTCAYDDPNCEVGVIIGTGTNACYMEDMSNIDLVEGDEGRMCINTEWGAFGDDGALEDIRTEFDRELDLGSLNPGKQLFEKMISGLYMGELVRLILLKMAKVGLLF... | Function: Catalyzes the phosphorylation of hexose to hexose 6-phosphate, although at very low level compared to other hexokinases (By similarity). Has low glucose phosphorylating activity compared to other hexokinases (By similarity). Involved in glucose homeostasis and hepatic lipid accumulation . Required to maintain... |
P0DUM0 | MLSKYQPSAHIAVTRAHWEDLHQAISSGKVTIDGNSLTLADVVAVSKFGCYARLSENRETIDAINESVSTLQECLDEGHHIYGVNTGFGGSADSRTDHLASLQRALLQLLQSGILTKADIGSGDTPSQSHAMPPEWVKAIMVVRSNSVARGHSAVSIGSIEAILRLLQRDITPVVPLRGTISASGDLMPLAYIVGAIEGNPGVFARAGKSPHGQALPAQQVLEQLGIPRITLGPKEALGLVNGTAASAALSSLVLYEAHRLALLSQVTTALTVEALRGSAESFHPFISQARPHDGQMEAASNILTVMRGSRLAMGTSEVQ... | Function: Phenylalanine ammonia-lyase; part of the gene cluster that mediates the biosynthesis of hancockiamides, an unusual new family of N-cinnamoylated piperazines . The NRPS hkm10 and the NmrA-like reductase hkm9 are proposed to convert two molecules of L-Phe to the intermediary piperazine called xenocockiamide A (... |
P0DUL1 | MTKLDSPQFEPFELTAADYAFPMFYAGCTLSFRLKSPEMGIPVLQTAVERITAHLPFLTGIVIPSAVKDGVMEVHPAACGQSGLEDPQCRVRRLPHLCLPPKTASASANKKHGSGMTYDRNECLIVAPLEAATAAQQHPVIRFQINVLADGIIFTLFANHMVIDGTGLGIITEMLASCCQTADNTGSVPELAGAIDREARTRAMLGTIGRREREKVQFEPVAAESAAPDGHQEVHDASLVDCNFRLSADKIRRIRERAQELGIASASEDDIVTAVLWLCMSEFRSHSGAGKEISACTLLRMVNVRRRFHPAVPDNYLGNC... | Function: O-acetyltransferase; part of the gene cluster that mediates the biosynthesis of hancockiamides, an unusual new family of N-cinnamoylated piperazines . The NRPS hkm10 and the NmrA-like reductase hkm9 are proposed to convert two molecules of L-Phe to the intermediary piperazine called xenocockiamide A (Probable... |
P0DUL3 | METPTPPLPSKDQLFPPLIQLVRALLWVLVITIGGAIVQRLFFHPLRKIPGPLTAAISGWDEFYHNIWRDGEWCKTYPKLHKEYNSPVIRIGPNHVHLNDIDAYETVFRVGTNFYKDKTFYTCADNDGSIFSLCDRDEHSERRKVLSSLFSKQAAEMTAPKVMSKLNELLDFMITQSKEGKACNITDLFRALAINWVADTLLGDCGDVVTYAETKPDLLEDIDGLSKLIPTLRFFPYLIPTLNSLAPSTSPAGVAKFKKICENYTRPRINDPIKNISQRSRASVVELLIAHRHEVYHKPPTVDYLAEEAFTFIDAGVDTT... | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of hancockiamides, an unusual new family of N-cinnamoylated piperazines . The NRPS hkm10 and the NmrA-like reductase hkm9 are proposed to convert two molecules of L-Phe to the intermediary piperazine called xenocockiamide A... |
P0DUQ0 | MDDFSATHINYTLSIHLSGIFFAWHRHFVWLWERTLREECGYNGYQPYWDWALSANNISASPIFDGSPTSLSGNGDPINQEPFLQLEPTNITIPTGTGGGCVTNGPFANMTLNLPDLSMAGDEEFPSNAFDYKPHCFTRNLNSHMSSAFTSQADVDRLLNSPSITDLQANIDFSAWPELREARILGPHAAAHMSLGRTMDDFWTAPQDPSFMLHHAQVDRIWSLWQARGPESRRWALNGTSTINNRPTSPEVTLDTELVWGSLSESKTMREVMSTEAYHFCYEYGA | Cofactor: Binds 2 copper ions per subunit.
Function: Oxidase; part of the gene cluster that mediates the biosynthesis of hancockiamides, an unusual new family of N-cinnamoylated piperazines . The NRPS hkm10 and the NmrA-like reductase hkm9 are proposed to convert two molecules of L-Phe to the intermediary piperazine ca... |
P0DUL5 | MEIFESFGIEGEVTKQWEPATDEILWCRNESGTLSRMERFRNEPPVGVKWTHGTLQQGRVEEIMKKRITEISGVEVEYSTELSDLTINTRESSNSKASACSVTIRSVADDQEAHRSSETIRARYIIGADGGRSSIRDLMGVAMEGTKGTAIWGVMDILGGSDFPDFGATSVVRSDSDGAVDFVRREEGLTRIYVELNKCAAGWEALERDTITPELILEKCRYIIRPYKLEVDYVEWWSSFTVWQRLSKSMIVHDRVFLVGDAVHTHSPLCGMGMNTGIQDSFNLGWKLAGVVQGQLNYDILQTYETERRPVAEALLDTDR... | Function: FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of hancockiamides, an unusual new family of N-cinnamoylated piperazines . The NRPS hkm10 and the NmrA-like reductase hkm9 are proposed to convert two molecules of L-Phe to the intermediary piperazine called xenocockiamide A (... |
P0DUL6 | MRDRCMLSFTKEQLTSVGEYCTLHSSPLPKSVEEQCRVTDERSQDEVVMAPSPAQCAWLMSFALASRPRRILELGTFTGVSTLAFYEGTRKTKAEIITVDMSEEYLQIAETAFRRHGATDRIQTIRGPCLEILPTITGEFDLIYIDAAEEEYEAYTRFVLDHKLLSAEGVMLVDDGTYIRWFYFFQANWWSVLLEGLVVDRSIVKEFPEEIQEPYLGIADQMNDFNRYARSDPRVEVTMIPLFNGVTQITWK | Function: O-methyltransferase; part of the gene cluster that mediates the biosynthesis of hancockiamides, an unusual new family of N-cinnamoylated piperazines . The NRPS hkm10 and the NmrA-like reductase hkm9 are proposed to convert two molecules of L-Phe to the intermediary piperazine called xenocockiamide A (Probable... |
A5FVE7 | MAEHDDGDLIAAIRGLARANVLVVGDLMLDRYAYGRVERISPEAPVPILTVTREIAMPGGAGNVVRNLTALDAAAAFVSVVGDDQEGSDLTALIGGQPNVEPWLLVETGRATTVKTRYIAAGQHLIRADRELVMPLTDKLGERLLKIASDAMAATSVTVLSDYRKGVLAPTIARNLIASARSIGRTVIVDPKGADWSHYAEADVITPNRRELAEAVGRDLPDEAAIVGAAREVIGRFGFGAVLCTRSEDGMSLVTVDTVRHYPAEAAEVYDVSGAGDTVVAVLAAGLASGLPLEIAARLSNIAGGLVVGKVGTAVARPDD... | Function: Catalyzes the phosphorylation of D-glycero-D-manno-heptose 7-phosphate at the C-1 position to selectively form D-glycero-beta-D-manno-heptose-1,7-bisphosphate.
Catalytic Activity: ATP + D-glycero-beta-D-manno-heptose 7-phosphate = ADP + D-glycero-beta-D-manno-heptose 1,7-bisphosphate + H(+)
Sequence Mass (Da)... |
Q9Z5B5 | MTGPMAVRTDRTPLVVVGDALLDRDLTGTADRLAPDAPVPVVQECAERIRPGGAALAAYLAARDGREVTLIAGVGEDPAGLALRELLAPWLKLIPLPLTGTVPEKTRVLAQDRPVVRLDRGGGRVREATDEARDALGCARAVLVSDYGRGAADALRDVLAARPPLVWDPHPRGGPPVPGTRLVTPAEKEAHGFAPSEGRPGGGLRAAALNAAALVRDWRVAAVTVTLGSRGALLSYGEHPLLVPAPAAHHGDSCGAGDRFAATAAGLLADGALVGEAVEGAVGAATAFVAAGGAAAVPPAGSERALAALPDTDDPGALAA... | Function: Catalyzes the phosphorylation of D-glycero-D-manno-heptose 7-phosphate at the C-1 position to selectively form D-glycero-beta-D-manno-heptose-1,7-bisphosphate.
Catalytic Activity: ATP + D-glycero-beta-D-manno-heptose 7-phosphate = ADP + D-glycero-beta-D-manno-heptose 1,7-bisphosphate + H(+)
Sequence Mass (Da)... |
P41936 | MFNVSALRAATPSIASVSSVASPSEQHGLSTSVGVGVNDTTSRTGDGGAASSASSASAAPQQQSQSALHNKLEAKWDTLLPTDTNLQCSTWPDSIPLLAGYSATPTFSFDPCTYGSYDPSAYFASNGIAGSMYTLPDQFPRSENDMLDNSNTSNGNKSDKDGIKLEDEDEILEDEENDEEDDGTGKRKKRKRRVLFTKAQTYELERRFRSQKYLSAPEREALAMQIRLTPTQVKIWFQNHRYKTKKSHTDKPINAALLTTMPNAFSSQSTAASFPTRAMPIPMLVRDSSARSSDISSTSPYTVAFGSANSGYLPTPSAYL... | Function: Involved in combinatorial activation of gene expression in pharyngeal muscle. Specifically binds a site necessary for activity of the B subelement of myo-2 enhancer.
Sequence Mass (Da): 37511
Sequence Length: 346
Domain: The homeobox domain is required for the induction of distal tip cell fate.
Subcellular Lo... |
P02836 | MALEDRCSPQSAPSPITLQMQHLHHQQQQQQQQQQQMQHLHQLQQLQQLHQQQLAAGVFHHPAMAFDAAAAAAAAAAAAAAHAHAAALQQRLSGSGSPASCSTPASSTPLTIKEEESDSVIGDMSFHNQTHTTNEEEEAEEDDDIDVDVDDTSAGGRLPPPAHQQQSTAKPSLAFSISNILSDRFGDVQKPGKSMENQASIFRPFEASRSQTATPSAFTRVDLLEFSRQQQAAAAAATAAMMLERANFLNCFNPAAYPRIHEEIVQSRLRRSAANAVIPPPMSSKMSDANPEKSALGSLCKAVSQIGQPAAPTMTQPPLS... | Function: This protein specifies the body segmentation pattern. It is required for the development of the central nervous system. Transcriptional regulator that represses activated promoters. Wg signaling operates by inactivating the SGG repression of EN autoactivation.
PTM: Phosphorylated. Phosphorylation may directly... |
P23397 | QDEKRPRTAFTGDQLARLKREFSENKYLTEQRRTCLAKELNLNESQIKIWFQNKRAKMKKASGVKNQLALQLMAQGLYNHSSSSSSSSSSSSSIFLLA | Function: This protein specifies the body segmentation pattern.
PTM: Phosphorylated in the Ser-rich domain.
Sequence Mass (Da): 11143
Sequence Length: 98
Subcellular Location: Nucleus
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E4QP00 | MTDTIFDYVIVGGGTAGSVLANRLSARPENRVLLIEAGIDTPENNIPPEIHDGLRPWLPRLSGDKFFWPNLTIHRAAEHPGITREPQFYEQGRLLGGGSSVNMVVSNRGLPRDYDEWQALGADGWDWQGVLPYFIKTERDADYGDDPLHGNAGPIPIGRVDSRHWSDFTVAATQALEAAGLPNIHDQNARFDDGYFPPAFTLKGEERFSAARGYLDASVRVRPNLSLWTESRVLKLLTTGNAITGVSVLRGRETLQVQAREVILTAGALQSPAILLRTGIGPAADLHALGIPVLADRPGVGRNLWEHSSIGVVAPLTEQA... | Function: Involved in the degradation and detoxification of 5-(hydroxymethyl)furfural (HMF) by mediating its oxidation to furan-2,5-dicarboxylate (FDCA), a biobased platform chemical for the production of polymers. Active with a wide range of aromatic and aliphatic primary alcohols and aldehydes: acts on alcohol groups... |
P30519 | MSAEVETSEGVDESEKKNSGALEKENQMRMADLSELLKEGTKEAHDRAENTQFVKDFLKGNIKKELFKLATTALYFTYSALEEEMERNKDHPAFAPLYFPMELHRKEALTKDMEYFFGENWEEQVQCPKAAQKYVERIHYIGQNEPELLVAHAYTRYMGDLSGGQVLKKVAQRALKLPSTGEGTQFYLFENVDNAQQFKQLYRARMNALDLNMKTKERIVEEANKAFEYNMQIFNELDQAGSTLARETLEDGFPVHDGKGDMRKCPFYAAEQDKGALEGSSCPFRTAMAVLRKPSLQFILAAGVALAAGLLAWYYM | Function: Catalyzes the oxidative cleavage of heme at the alpha-methene bridge carbon, released as carbon monoxide (CO), to generate biliverdin IXalpha, while releasing the central heme iron chelate as ferrous iron.
PTM: A soluble form arises by proteolytic removal of the membrane anchor.
Location Topology: Single-pass... |
P43242 | MSAEVETSEGVDEPEEKNFGENHIRMADLSELLKEGTKEAHDRAENTKFVKDFLKGNIKKEIFKLATTALYFTYSALEEEMDRNKDHPAFAPLYFPMELHRKEALTKDMEYFFGENWEEQVQCSEAAQKYVERIHYIGQNEPELLVAHAYTRYMGDLSGGQVLKKVAQRALKLPSTGEGTQFYLFENVDNAQQFKQFYRARMNALDLNLKTKERIVEEANKAFEYNMQIFSELDQAGSAPASETVEDRIPVHDGKGDVRKCPYYAAGQVNGALEGSSCPFRAAMAVLRKPSLQLVLAAAVALAAGLLAWYYM | Function: Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed. ... |
P23711 | MSSEVETSEGVDESENNSTAPEKENHTKMADLSELLKEGTKEAHDRAENTQFVKDFLKGNIKKELFKLATTALYFTYSALEEEMDRNKDHPAFAPLYFPTELHRKEALIKDMEYFFGENWEEQVKCSEAAQKYVDRIHYVGQNEPELLVAHAYTRYMGDLSGGQVLKKVAQRALKLPSTGEGTQFYLFEHVDNAQQFKQFYRARMNALDLSMKTKERIVEEANKAFEYNMQIFSELDQAGSMLTKETLEDGLPVHDGKGDVRKCPFYAAQPDKGTLGGSNCPFRTAMAVLRKPSLQLILAASVALVAGLLAWYYM | Function: Catalyzes the oxidative cleavage of heme at the alpha-methene bridge carbon, released as carbon monoxide (CO), to generate biliverdin IXalpha, while releasing the central heme iron chelate as ferrous iron.
PTM: A soluble form arises by proteolytic removal of the membrane anchor.
Location Topology: Single-pass... |
Q9C9L4 | MATTRLNPSCHFPASTRLSCESYLGLRTTGRISYARTLTAPRGYLAVKANGGQASVVTAAAITEKQQKKYPGESKGFVEEMRFVAMRLHTKDQAREGEKESRSPEEGPVAKWEPTVEGYLHFLVDSKLVYDTLEGIIDGSNFPTYAGFKNTGLERAESLRKDLEWFKEQGYEIPEPMAPGKTYSEYLKDLAENDPQAFICHFYNIYFAHSAGGQMIGTKVSKKILDNKELEFYKWDGQLSQLLQNVRQKLNKVAEWWTREEKSHCLEETEKSFKFSGEILRLILS | Function: Catalyzes the opening of the heme ring to form the open-chain tetrapyrrole biliverdin IX with the release of iron and carbon monoxide (CO). Produces specifically the biliverdin IX-alpha isomer. Plays a minor role in phytochrome assembly and photomorphogenesis.
Catalytic Activity: heme b + 3 O2 + 3 reduced [NA... |
O70453 | MSSEVETAEAVDESEKNSMASEKENHSKIADFSDLLKEGTKEADDRAENTQFVKDFLKGNIKKELFKLATTALSYSAPEEEMDSLTKDMEYFFGENWEEKVKCSEAAQTYVDQIHYVGQNEPEHLVAHTYSTYMGGNLSGDQVLKKETQPVPFTREGTQFYLFEHVDNAKQFKLFYCARLNALDLNLKTKERIVEEATKAFEYNMQIFSELDQAGSIPVRETLKNGLSILDGKGGVCKCPFNAAQPDKGTLGGSNCPFQMSMALLRKPNLQLILVASMALVAGLLAWYYM | Function: Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Heme oxygenase 3 could be implicated in some heme-dependent regulatory role in the cell.
Catalytic Activity: heme b + 3 O2 + 3 reduced [NADPH--hemopro... |
Q9LQC0 | MATSRLNASCRFPASRRLDCESYVSLRAKTVTIRYVRTIAAPRRHLVRRANEDQTLVVNVVAAAGEKPERRYPREPNGFVEEMRFVVMKIHPRDQVKEGKSDSNDLVSTWNFTIEGYLKFLVDSKLVFETLERIINESAIQAYAGLKNTGLERAENLSRDLEWFKEQGYEIPESMVPGKAYSQYLKNIAEKDPPAFICHFYNINFAHSAGGRMIGTKVAEKILDNKELEFYKWDGQLSELLQNVSEELNKVAELWTREEKNHCLEETEKSFKFYWEIFRYLLS | Function: Catalyzes the opening of the heme ring to form the open-chain tetrapyrrole biliverdin IX with the release of iron and carbon monoxide (CO). Produces specifically the biliverdin IX-alpha isomer. Plays a minor role in phytochrome assembly and photomorphogenesis.
Catalytic Activity: heme b + 3 O2 + 3 reduced [NA... |
O73688 | MEADKKTTAQTESNRDLSEQIKKVTKDVHVRAESTELMLSFQRGQVTLQQYKLLLCSLYEIYLALEEEMDRNCDHPSVAPIYFPAELARLATIEKDLEFFFGPDWREKIVVPAATERYCHRIRQIGQENPEYLIAHAYTRYLGDLSGGQVLGRIAQKSMKLGGSEGLSFFAFPGVSSPNLFKRLYRSRMNSVELTEEQRSAVLQEALGAFEFNIQVFEDLQKMLNVTENEPGVGTPRSRPATTLQVGGSMIQTNPLFRMVLGLCLALATVSIGLYAL | Function: Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed.
... |
O52792 | MTYVSLADLERAARDVLPGEIFDFLAGGSGTEASLVANRTALERVFVIPRMLRDLTDVTTEIDIFGRRAALPMAVAPVAYQRLFHPEGELAVARAARDAGVPYTICTLSSVSLEEIAAVGGRPWFQLYWLRDEKRSLDLVRRAEDAGCEAIVFTVDVPWMGRRLRDMRNGFALPEWVTAANFDAGTAAHRRTQGVSAVADHTAREFAPATWESVEAVRAHTDLPVVLKGILAVEDARRAVDAGAGGIVVSNHGGRQLDGAVPGIEMLGEIVAAVSGGCEVLVDGGIRSGGDVLKATALGASAVLVGRPVMWALAAAGQDG... | Function: Catalyzes the oxidation of p-hydroxymandelate to p-hydroxybenzoylformate in the biosynthesis of L-(4-hydroxyphenyl)glycine and L-(3,5-dihydroxyphenyl)glycine, 2 non-proteinogenic amino acids occurring in the vancomycin group of antibiotics.
Catalytic Activity: (S)-4-hydroxymandelate + O2 = 4-hydroxyphenylglyo... |
Q8Y563 | MKKVFITTGTEHYLRQLMANYTGGNVTLLQNFSQSLLYQESTGEKLFQEGAEYRVLQSSGSIKGFGVVVFEYIHLRDEEIPIFLQMYQRASLHFSETPGLQSTKLTKAMNMNKFLIISFWDSEVFFHDWKKSPLSKEITNIMRKNNTQSGFSHEDIYHYPEFSHDAK | Function: Catalyzes the degradation of heme to biliverdin in the presence of a suitable electron donor such as ascorbate, with the subsequent release of iron. Hardly any CO is released by the heme degradation reaction. Binds heme . Allows bacterial pathogens to use the host heme as an iron source. Release of iron from ... |
Q988D0 | MRRKVFEELVTATKILLNEGIMDTFGHISARDPEDPASFFLAQKLAPSLITVDDIQRFNLDGETSDNRPSYLERYIHSEIYKTRPDVQCVLHTHSPAVLPYCFVDTPLRPVTHMGAFIGESVPVYEIRDKHGDETDLFGGSPDVCADIAESLGSQTVVLMARHGVVNVGKSVREVVFRAFYLEQEAAALTAGLKIGNVKYLSPGEIKTAGKLVGAQIDRGWNHWSQRLRQAGLA | Cofactor: Binds 1 manganese ion per subunit.
Function: Involved in the catabolism of pyridoxal 5-phosphate (Vitamin B6). Catalyzes the decarboxylation of 3-hydroxy-2-methylpyridine-4,5-dicarboxylate to yield 3-hydroxy-2-methylpyridine-5-carboxylate. The decarboxylation proceeds by an aldolase-like mechanism in which th... |
Q88DY1 | MLQVEGLYLCRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARRLAVLPQVSSLGFSFRVEEVVGMGRMPHGTGQRRDAEIVEAALRAADAWHLVARSYLALSGGERQRVHLARVLAQLWPGEEGSTLLLDEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQGRCHAFATPEAALTPAALKAVYGIDVLVQAHPERGHPLIITR | Function: Part of the ABC transporter complex HmuTUV involved in hemin import. Responsible for energy coupling to the transport system.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 27656
Sequence Length: 255
Subcellular Location: Cell inner membrane
EC: 7.6.2.-
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Q3ICT8 | MLCANNVSAQIGQKKLLKHINFYVKPNELVVIIGPNGAGKSSLLKALCGDIKINNGDITLNDRLLSDYSIASLATLRAVLTQNYELDFPFSVAEVVDMAHFAHQADYSKQQLMHFSEQVMQALSVTHLKTHTFTQLSGGEKQRVQLARVLCQIQPSLVANKTPYLLIDEPTSSLDIFHQYDVMAQAKSIASQGAGVVAVIHDLSLAASFADRIYMLNNGEVAACGIPKEVLTPALLKRVYNINARLENNTSEAMPHIQMCY | Function: Part of the ABC transporter complex HmuTUV involved in hemin import. Responsible for energy coupling to the transport system.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 28686
Sequence Length: 261
Subcellular Location: Cell inner membrane
EC: 7.6.2.-
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Q1MCZ1 | MIEVSGVSVRLSGKTIISDVAFTARAGELTAIAGPNGSGKTTTMKAISGELAYGGSVRIGGGEVKGLKPWQLAAIRGVLPQASTISFPFTVREIVRMGLTSGLNLHPDKAEQTAAAALASVDLTGFEGRFYQELSGGEQQRVQLARVLCQIAEPIVDGKPCWLLLDEPVSSLDISHQLTIMTLARNFCERGGGVIAVMHDLNLTALFADRIVLMKSGRLAAAGSIGEVLTNETMLAVFGCALRINQVPSDGTPFVLAHSAISRP | Function: Part of the ABC transporter complex HmuTUV involved in hemin import. Responsible for energy coupling to the transport system.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 27743
Sequence Length: 264
Subcellular Location: Cell inner membrane
EC: 7.6.2.-
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Q98L75 | MIEARDVSVDIAGKRIVGGVDFDARPGEVAAIVGPNGSGKTTFLKALSGEFAYTGRIALNGHNLSSMRPAEMAVHRAVLPQATTLSFPFTVREVVKLGLVGGRSGALPGEDARLPERALARVDLDGFAGRFYQELSGGEQQRVQLARVLCQVWAPVLDGKPRYLFLDEPVSSLDIKHQLIIMNIARDFAKRGGGVVAILHDLNLTSMYADRIFVMHRGRLAATGSPQDVLSDDLIEKVFDCRLRVGVLPAGNMPFVLPQSSVY | Function: Part of the ABC transporter complex HmuTUV involved in hemin import. Responsible for energy coupling to the transport system.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 28452
Sequence Length: 263
Subcellular Location: Cell inner membrane
EC: 7.6.2.-
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Q0SIB7 | MSPAFHPLRTRVGEAIEQSLFRRTDPVPPPRPSGAVTLRADGIAVTRGGRPVLDDVSVDVRIGEVLVLVGPNGAGKSTLLAALSGDQDVHTGTVHLDDRDLGEWTALEMAQRRAVLPQQNTVGFSFTARQVITMGRSPWARTPRSDDDAVAIAEAMRICDVVAFADRPFTALSGGERARVALARVLAQRTETILLDEPTAALDLGHQETVMRLARSRAEQGTAVVVVLHDLALAAAYADRIVVLEQGRVAANGPPADVLSEELLTRVYGHPVEVIEHPVTGATLVLPRRDQR | Function: Part of the ABC transporter complex HmuTUV involved in hemin import. Responsible for energy coupling to the transport system.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 31376
Sequence Length: 292
Subcellular Location: Cell membrane
EC: 7.6.2.-
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Q160G4 | MSLDAADITVKLGRTPILHGIGFCAKPGEVSAIVGPNGSGKTTLLRAITGDLPFDGTVRLNGKDTSRMKPWELSAIRAVLPQSAVLAFPFTVAEVVRLGVQAGVCARDCDAPMAALSQVRLAHYADRFYHELSGGEQQRVQLARVLAQVWRPVVGGAPRWLLLDEPVASLDIANQLEVMEITRAYASAGGGVVAVMHDLNLTAMFADHLAILSGGQCLAAGPPEQVMTDAILSQAYGCALRVNTPPPHSATYVLPHAANRL | Function: Part of the ABC transporter complex HmuTUV involved in hemin import. Responsible for energy coupling to the transport system.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 27606
Sequence Length: 261
Subcellular Location: Cell inner membrane
EC: 7.6.2.-
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Q8EB59 | MDRLSYAIGDKAVLNNIRVQFQPGSVTALLGPNGAGKSTLLKALCQEIPSAQGSIKLGHCQLVDWPRAELAKSLAVLPQHASLTFPFTVDEVVAMGLYPLTLSQKEGQQLVTKWLAEVGVLHLARRSYPTLSGGEKQRVQLARVLTQLSQSPFPPILLLDEPTSALDLAQQHKVLALAKNLAHKHAYTVIVVLHDLNQAARYSDRVIVLKQGEIVSEGTPNDALSIDIIRQVWDYEPEFIPAPQGDYPLIF | Function: Part of the ABC transporter complex HmuTUV involved in hemin import. Responsible for energy coupling to the transport system.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 27509
Sequence Length: 251
Subcellular Location: Cell inner membrane
EC: 7.6.2.-
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O60506 | MATEHVNGNGTEEPMDTTSAVIHSENFQTLLDAGLPQKVAEKLDEIYVAGLVAHSDLDERAIEALKEFNEDGALAVLQQFKDSDLSHVQNKSAFLCGVMKTYRQREKQGTKVADSSKGPDEAKIKALLERTGYTLDVTTGQRKYGGPPPDSVYSGQQPSVGTEIFVGKIPRDLFEDELVPLFEKAGPIWDLRLMMDPLTGLNRGYAFVTFCTKEAAQEAVKLYNNHEIRSGKHIGVCISVANNRLFVGSIPKSKTKEQILEEFSKVTEGLTDVILYHQPDDKKKNRGFCFLEYEDHKTAAQARRRLMSGKVKVWGNVGTV... | Function: Heterogenous nuclear ribonucleoprotein (hnRNP) implicated in mRNA processing mechanisms. Component of the CRD-mediated complex that promotes MYC mRNA stability. Isoform 1, isoform 2 and isoform 3 are associated in vitro with pre-mRNA, splicing intermediates and mature mRNA protein complexes. Isoform 1 binds t... |
Q7TMK9 | MATEHVNGNGTEEPMDTTSAVIHSENFQTLLDAGLPQKVAEKLDEIYVAGLVAHSDLDERAIEALKEFNEDGALAVLQQFKDSDLSHVQNKSAFLCGVMKTYRQREKQGTKVADSSKGPDEAKIKALLERTGYTLDVTTGQRKYGGPPPDSVYSGQQPSVGTEIFVGKIPRDLFEDELVPLFEKAGPIWDLRLMMDPLTGLNRGYAFVTFCTKEAAQEAVKLYNNHEIRSGKHIGVCISVANNRLFVGSIPKSKTKEQILEEFSKVTEGLTDVILYHQPDDKKKNRGFCFLEYEDHKTAAQARRRLMSGKVKVWGNVGTV... | Function: Heterogeneous nuclear ribonucleoprotein (hnRNP) implicated in mRNA processing mechanisms. Component of the CRD-mediated complex that promotes MYC mRNA stability. Isoform 1 and isoform 2 are associated in vitro with pre-mRNA, splicing intermediates and mature mRNA protein complexes. Isoform 1 binds to apoB mRN... |
Q7TP47 | MATEHVNGNGTEEPMDTTSAVIHSENFQTLLDAGLPQKVAEKLDEIYVAGQRKYGGPPPDSVYSGQQPSVGTEIFVGKIPRDLFEDELVPLFEKAGPIWDLRLMMDPLTGLNRGYAFVTFCTKEAAQEAVKLYNNHEIRSGKHIGVCISVANNRLFVGSIPKSKTKEQILEEFSKVTEGLTDVILYHQPDDKKKNRGFCFLEYEDHKTAAQARRRLMSGKVKVWGNVGTVEWADPIEDPDPEVMAKVKVLFVRNLANTVTEEILEKSFSQFGKLERVKKLKDYAFIHFDERDGAVKAMEEMNGKDLEGENIEIVFAKPPD... | Function: Heterogenous nuclear ribonucleoprotein (hnRNP) implicated in mRNA processing mechanisms. Component of the CRD-mediated complex that promotes MYC mRNA stability. Is associated in vitro with pre-mRNA, splicing intermediates and mature mRNA protein complexes. Binds to apoB mRNA AU-rich sequences. Part of the APO... |
Q00839 | MSSSPVNVKKLKVSELKEELKKRRLSDKGLKAELMERLQAALDDEEAGGRPAMEPGNGSLDLGGDSAGRSGAGLEQEAAAGGDEEEEEEEEEEEGISALDGDQMELGEENGAAGAADSGPMEEEEAASEDENGDDQGFQEGEDELGDEEEGAGDENGHGEQQPQPPATQQQQPQQQRGAAKEAAGKSSGPTSLFAVTVAPPGARQGQQQAGGKKKAEGGGGGGRPGAPAAGDGKTEQKGGDKKRGVKRPREDHGRGYFEYIEENKYSRAKSPQPPVEEEDEHFDDTVVCLDTYNCDLHFKISRDRLSASSLTMESFAFLW... | Function: DNA- and RNA-binding protein involved in several cellular processes such as nuclear chromatin organization, telomere-length regulation, transcription, mRNA alternative splicing and stability, Xist-mediated transcriptional silencing and mitotic cell progression . Plays a role in the regulation of interphase la... |
Q0QLF7 | MFKIDEEKCKKCRMCVKECPVHAVYYEKKDKGAIVEITEKCVECGICKRVCKFGAIENDAPLESVITCSSCPIQCKVPLGETGACTRYRNVGGKLVRDRELVVEALEQKEAADNIKKPIITAVGAGTNYPCSKPAPHIVSECRDGVDVVTVVTEAPLSYSGLVIKLDTNTYIGEEGDPVYRDGKVVGMVNTEEYGSKMIAIGGANRLTGDNGFATARTIVELANGEEVELKVNKKIVLKLKAGVAPVIDGVEESIMRIGCGSATVGLFAKRMKDAVDECIVIDHHVIGLCSEHLAGEAVGMTWSGIIPNATKSSRGRYFG... | Cofactor: Binds 1 flavin covalently per subunit.
Function: Catalyzes the reversible reduction of 6-hydroxynicotinate to 6-oxo-1,4,5,6-tetrahydronicotinate.
Catalytic Activity: 1,4,5,6-tetrahydro-6-oxonicotinate + oxidized 2[4Fe-4S]-[ferredoxin] = 6-hydroxynicotinate + 2 H(+) + reduced 2[4Fe-4S]-[ferredoxin]
Sequence Ma... |
D8LQS7 | MQRVGAASPTCSSLQAPAAAPPILTISPHHRVKTAETAAEPDLLEPTGVHHPFHSLSPLTEARAWAAREGQYFNGLIEANGGASVSKGHPDLAVTFLTDHASCEWFFSQRQEVLDRQDGAYFGPLKCKKQYIGESLPTLASNQKESHQVLREHKLRVFRSRVPFAQSAMTNATDTFYKNLRDNGTGDYTVVYDFFLQQTIHFLHEWIYGLGVEGGQPLPPFKDFMNANPLDVSVLLELEMDTPVANLAAKLAQRSKKPSAEQLASVESIAEAIRSSDVWAGFVEMLEDSNVNTKDLERSFMFTTNFQSAGAIAKGMMPVV... | Function: Cytochrome P450 hydroperoxide bicyclase involved in the metabolism of oxylipins 'ectocarpins' natural products, such as hybridalactone, ecklonilactones and derivatives . Isomerizes the hydroperoxides into epoxyalcohols via epoxyallylic radical . Can use alpha-linolenic acid 13(S)-hydroperoxide (13-HPOTE) and ... |
Q8GZ99 | MSSRTGASLLLILFFFQICSVSALTNGLDASALNALKSEWTTPPDGWEGSDPCGTNWVGITCQNDRVVSISLGNLDLEGKLPADISFLSELRILDLSYNPKLSGPLPPNIGNLGKLRNLILVGCSFSGQIPESIGTLKELIYLSLNLNKFSGTIPPSIGLLSKLYWFDIADNQIEGELPVSNGTSAPGLDMLLQTKHFHFGKNKLSGNIPKELFSSNMSLIHVLFDGNQFTGEIPETLSLVKTLTVLRLDRNKLIGDIPSYLNNLTNLNELYLANNRFTGTLPNLTSLTSLYTLDVSNNTLDFSPIPSWISSLPSLSTLR... | Function: Leucine-rich repeat receptor protein kinase that acts as sensor of extracellular hydrogen peroxide . Required for intracellular calcium influx in response to extracellular hydrogen peroxide . Mediates hydrogen peroxide-induced activation of calcium channels in guard cells and is required for stomatal closure ... |
A9A2G6 | MAAVKKIFDEIIETDHKVITEESSKSILKNYGVKVPPYALVTSAEEAAKEAKKIGFPLVMKVVSPQILHKTDVGGVKVGLDNVADVKKTFTDMYGRLSKKKGVNVKGILLEKMVPKGVELIVGIQNDSQFGPIIMVGMGGIMTEVMKDVAFRMLPITTSDAKSMLNELKGSKLLKGFRGSEPIDTNLVAKMLVNIGKLGVENADYINSIDFNPVIVYPKSHYVVDAKIILNKEKKKNSISKAKPSITDMETFFTPKSVALVGASASPGKIGNSILDSLVNYDFKGKVYPINPKADKIFGQKCYPSVADIPGKVDLVVVSV... | Cofactor: No activity with Ni(2+), Co(2+) and Ca(2+).
Function: Involved in thaumarchaeal hydroxypropionate/hydroxybutyrate (HP/HB) cycle, a modified version of the autotrophic HP/HB cycle of Crenarchaeota. Catalyzes the formation of 3-hydroxypropionyl-CoA, ADP and phosphate from 3-hydroxypropionate, coenzyme A (CoA) a... |
A4YGR1 | MFMRYIMVEEQTLKTGSQELEEKADYNMRYYAHLMKLSKEKPAEFWGSLAQDLLDWYEPWKETMRQEDPMTRWFIGGKINASYNAVDRHLNGPRKFKAAVIWESELGERKIVTYQDMFYEVNRWANALRSLGVGKGDRVTIYMPLTPEGIAAMLASARIGAIHSVIFAGFGSQAIADRVEDAKAKVVITADAYPRRGKVVELKKTVDEALNSLGERSPVQHVLVYRRMKTDVNMKEGRDVFFDEVGKYRYVEPERMDSNDPLFILYTSGTTGKPKGIMHSTGGYLTGTAVMLLWSYGLSQENDVLFNTSDIGWIVGHSYI... | Function: Plays a role in the autotrophic CO(2) fixation pathway. Activates 3-hydroxypropionate to its CoA ester. Can also activate propionate, and to a lesser extent acrylate, acetate and butyrate.
Catalytic Activity: 3-hydroxypropanoate + ATP + CoA = 3-hydroxypropanoyl-CoA + AMP + diphosphate
Sequence Mass (Da): 7440... |
P84074 | MGKQNSKLRPEMLQDLRENTEFSELELQEWYKGFLKDCPTGILNVDEFKKIYANFFPYGDASKFAEHVFRTFDTNSDGTIDFREFIIALSVTSRGRLEQKLMWAFSMYDLDGNGYISREEMLEIVQAIYKMVSSVMKMPEDESTPEKRTEKIFRQMDTNNDGKLSLEEFIRGAKSDPSIVRLLQCDPSSASQF | Function: Calcium-binding protein that may play a role in the regulation of voltage-dependent calcium channels . May also play a role in cyclic-nucleotide-mediated signaling through the regulation of adenylate and guanylate cyclases (By similarity).
PTM: Myristoylation facilitates association with membranes.
Location T... |
Q05353 | MGKLALAAKITHVPSMYLSELPGKNHGCRQGAIDGHKEISKRCREMGVDTIIVFDTHWLVNSAYHINCADHFEGVYTSNELPHFIRDMTYNYEGNPELGQLIADEALKLGVRAKAHNIPSLKLEYGSVVPMRYMNEDKRFKVVSISAFCTVHDFADSRKLGERIVKAIEQYDGTVAVLASGSLSHRFIDDQRAEEGMNSYTREFDRQMDERVVKLWREGQFKEFCNMLPEYADYCYGEGNMHDTVMLLGMLGWDKYDGKVWSLSPSYSQASWHRSG | Function: Transforms homoprotocatechuic acid (HPC) into 5-carboxymethyl-2-hydroxy-muconic semialdehyde (CHMS).
Catalytic Activity: 3,4-dihydroxyphenylacetate + O2 = 2-hydroxy-5-carboxymethylmuconate semialdehyde + H(+)
Sequence Mass (Da): 31495
Sequence Length: 276
Pathway: Aromatic compound metabolism; 4-hydroxyphenyl... |
P42269 | MKKVNHWINGKNVAGNDYFLTTNPATGEVLADVASGGEAEINQAVATAKEAFPKWANLPMKERARLMRRLGDLIDQNVPEIAAMETADTGLPIHQTKNVLIPRASHNFEFFAEVCQQMNGKTYPVDDKMLNYTLVQPVGVCALVSPWNVPFMTATWKVAPCLALGITAVLKMSELSPLTADRLGELALEAGIPAGVLNVVQGYGATAGDALVRHHDVRAVSFTGGTATGRNIMKNAGLKKYSMELGGKSPVLIFEDADIERALDAALFTIFSINGERCTAGSRIFIQQSIYPEFVKFAERANRVRVGDPTDPNTQVGALI... | Function: Transforms 5-carboxymethyl-2-hydroxy-muconic semialdehyde (CHMS) into 5-carboxymethyl-2-hydroxy-muconic acid (CHM).
Sequence Mass (Da): 50827
Sequence Length: 468
Pathway: Aromatic compound metabolism; 4-hydroxyphenylacetate degradation; pyruvate and succinate semialdehyde from 4-hydroxyphenylacetate: step 3/... |
Q05354 | MPHFIVECSDNIREEADLPGLFAKVNPTLAATGIFPLAGIRSRVHWVDTWQMADGQHDYASVHMTLKIGAGRSLESRQQAGEMLFELIKTHFAALMESRLLALSFEIEELHPTLNFKQNNVHALFK | Function: Transforms 5-carboxymethyl-2-hydroxy-muconic acid (CHM) into 5-oxo-pent-3-ene-1,2,5-tricarboxylic acid (OPET).
Catalytic Activity: (2E,4Z)-5-hydroxypenta-2,4-diene-1,2,5-tricarboxylate = (3E,5R)-5-carboxy-2-oxohept-3-enedioate
Sequence Mass (Da): 14215
Sequence Length: 126
Pathway: Aromatic compound metabolis... |
A4YI89 | MEFETIETKKEGNLFWITLNRPDKLNALNAKLLEELDRAVSQAESDPEIRVIIITGKGKAFCAGADITQFNQLTPAEAWKFSKKGREIMDKIEALSKPTIAMINGYALGGGLELALACDIRIAAEEAQLGLPEINLGIYPGYGGTQRLTRVIGKGRALEMMMTGDRIPGKDAEKYGLVNRVVPLANLEQETRKLAEKIAKKSPISLALIKEVVNRGLDSPLLSGLALESVGWGVVFSTEDKKEGVSAFLEKREPTFKGK | Function: Plays a role in autotrophic carbon fixation via the 3-hydroxypropionate/4-hydroxybutyrate cycle. Catalyzes the reversible dehydration of 3-hydroxypropionyl-CoA to form acryloyl-CoA, and the reversible dehydration of (S)-3-hydroxybutyryl-CoA to form crotonyl-CoA. Inactive towards (R)-3-hydroxybutyryl-CoA.
Cata... |
P32755 | MTTYSNKGPKPERGRFLHFHSVTFWVGNAKQAASFYCNKMGFEPLAYKGLETGSREVVSHVIKQGKIVFVLCSALNPWNKEMGDHLVKHGDGVKDIAFEVEDCEHIVQKARERGAKIVREPWVEEDKFGKVKFAVLQTYGDTTHTLVEKINYTGRFLPGFEAPTYKDTLLPKLPSCNLEIIDHIVGNQPDQEMESASEWYLKNLQFHRFWSVDDTQVHTEYSSLRSIVVANYEESIKMPINEPAPGRKKSQIQEYVDYNGGAGVQHIALRTEDIITTIRHLRERGMEFLAVPSSYYRLLRENLKTSKIQVKENMDVLEEL... | Cofactor: Binds 1 Fe cation per subunit.
Function: Catalyzes the conversion of 4-hydroxyphenylpyruvic acid to homogentisic acid, one of the steps in tyrosine catabolism.
Catalytic Activity: 3-(4-hydroxyphenyl)pyruvate + O2 = CO2 + homogentisate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 45112
Se... |
Q53586 | MTQTTHHTPDTARQADPFPVKGMDAVVFAVGNAKQAAHYYSTAFGMQLVAYSGPENGSRETASYVLTNGSARFVLTSVIKPATPWGHFLADHVAEHGDGVVDLAIEVPDARAAHAYAIEHGARSVAEPYELKDEHGTVVLAAIATYGKTRHTLVDRTGYDGPYLPGYVAAAPIVEPPAHRTFQAIDHCVGNVELGRMNEWVGFYNKVMGFTNMKEFVGDDIATEYSALMSKVVADGTLKVKFPINEPALAKKKSQIDEYLEFYGGAGVQHIALNTGDIVETVRTMRAAGVQFLDTPDSYYDTLGEWVGDTRVPVDTLREL... | Cofactor: Binds 1 Fe cation per subunit.
Catalytic Activity: 3-(4-hydroxyphenyl)pyruvate + O2 = CO2 + homogentisate
Sequence Mass (Da): 41863
Sequence Length: 381
Pathway: Amino-acid degradation; L-phenylalanine degradation; acetoacetate and fumarate from L-phenylalanine: step 3/6.
EC: 1.13.11.27
|
Q27203 | MSENKDHVVVGYTEKPVGERPTGGKFLGYDHLHFWVGNAKQAAGWYTSRFGFEYYAYKGLETGSREVATHVVRNKQGVTLAFSTPYGNDKDNQREMNQHQSLHGDGVKDVAFAVEDCHSIYNKAIQRGAKCAYPPQDLKDEHGSVTIAAVHTYGEVIHTFIQRNDYKGFFMPGFVAHPLKDPLNNVLPDISYNYVDHIVGNQPDNMMTSAADWYEKTLDFHRFWSVDDSMIHTEFSSLRSIVMTDYDQKIKMPINEPADGKRKSQIQEYIDFYAGPGVQHIALNTSDVINTVEGLRARGVEFLSIPTSYYDNLRKALTAQ... | Cofactor: Binds 1 Fe cation per subunit.
Function: Key enzyme in the degradation of tyrosine.
Catalytic Activity: 3-(4-hydroxyphenyl)pyruvate + O2 = CO2 + homogentisate
Sequence Mass (Da): 46046
Sequence Length: 404
Pathway: Amino-acid degradation; L-phenylalanine degradation; acetoacetate and fumarate from L-phenylala... |
O42764 | MAPGALLVTSQNGRTSPLYDSDGYVPAPAALVVGGEVNYRGYHHAEWWVGNAKQVAQFYITRMGFEPVAHKGLETGSRFFASHVVQNNGVRFVFTSPVRSSARQTLKAAPLADQARLDEMYDHLDKHGDGVKDVAFEVDDVLAVYENAVANGAESVSSPHTDSCDEGDVISAAIKTYGDTTHTFIQRTTYTGPFLPGYRSCTTVDSANKFLPPVNLEAIDHCVGNQDWDEMSDACDFYERCLGFHRFWSVDDKDICTEFSALKSIVMSSPNQVVKMPINEPAHGKKKSQIEEYVDFYNGPGVQHIALRTPNIIEAVSNLR... | Cofactor: Binds 1 Fe cation per subunit.
Catalytic Activity: 3-(4-hydroxyphenyl)pyruvate + O2 = CO2 + homogentisate
Sequence Mass (Da): 46740
Sequence Length: 419
Pathway: Amino-acid degradation; L-phenylalanine degradation; acetoacetate and fumarate from L-phenylalanine: step 3/6.
EC: 1.13.11.27
|
Q9JN69 | MDVRTLAVGKAHLEALLATRKMTLEHLQDVRHDATQVYFDGLEHLQNVAQYLAIPLSEFFVGQTQSDLDDGVKIARRNGGFKREEIRGGVHYYTYEHLVTTNQDPGLMALRLDLHSDDEQPLRLNGGHGSREIVYVTRGAVRVRWVGDNDELKEDVLNEGDSIFILPNVPHSFTNHVGGAKSEIIAINYG | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Non-heme-dependent dioxygenase that catalyzes the oxidative epoxidation of (S)-2-hydroxypropylphosphonate into (1R,2S)-epoxypropylphosphonate, the final step in the biosynthesis of fosfomycin antibiotic.
Catalytic Activity: (S)-2-hydroxypropylphosphonate + H2O2 = (1R,... |
Q56185 | MSNTKTASTGFAELLKDRREQVKMDHAALASLLGETPETVAAWENGEGGELTLTQLGRIAHVLGTSIGALTPPAGNDLDDGVIIQMPDERPILKGVRDNVDYYVYNCLVRTKRAPSLVPLVVDVLTDNPDDAKFNSGHAGNEFLFVLEGEIHMKWGDKENPKEALLPTGASMFVEEHVPHAFTAAKGTGSAKLIAVNF | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Non-heme-dependent dioxygenase that catalyzes the oxidative epoxidation of (S)-2-hydroxypropylphosphonate into (1R,2S)-epoxypropylphosphonate, the final step in the biosynthesis of fosfomycin antibiotic.
Catalytic Activity: (S)-2-hydroxypropylphosphonate + H2O2 = (1R,... |
O66550 | MATVYLGLGSNVGDRISYILKAIEKLEEFLEIEKISTVYESKAWGFENQGNFLNFVLKAKTSLLPQELLLKIKKVEKEVGRKERFKWGPREIDIDILLYKDEVIRTKLLKVPHPFLEKRDFFVYPLLEIEPNVIHPIYRKPLKEFKPENTLKPFCCILKV | Function: Catalyzes the transfer of pyrophosphate from adenosine triphosphate (ATP) to 6-hydroxymethyl-7,8-dihydropterin, an enzymatic step in folate biosynthesis pathway.
Catalytic Activity: 6-hydroxymethyl-7,8-dihydropterin + ATP = (7,8-dihydropterin-6-yl)methyl diphosphate + AMP + H(+)
Sequence Mass (Da): 18838
Sequ... |
P29252 | MNNIAYIALGSNIGDRETYLRQAVALLHQHAAVTVTKVSSIYETDPVGYEDQAQFLNMAVEIKTSLNPFELLELTQQIENELGRTREVRWGPRTADLDILLFNRENIETEQLIVPHPRMYERLFVLAPLAEICQQVEKEATSAETDQEGVRVWKQKSGVDEFVHSES | Function: Catalyzes the transfer of pyrophosphate from adenosine triphosphate (ATP) to 6-hydroxymethyl-7,8-dihydropterin, an enzymatic step in folate biosynthesis pathway.
Catalytic Activity: 6-hydroxymethyl-7,8-dihydropterin + ATP = (7,8-dihydropterin-6-yl)methyl diphosphate + AMP + H(+)
Sequence Mass (Da): 19058
Sequ... |
Q9PJ54 | MLKIQGVKHFEKSRFFPFFSQNIRSFKYLALIGLGSNIEPEKKRFDMLFRVMMDDKRFKILSTSPMLINEAFGFKEQKDFTNAVMLIQTNLHARALLKVLLYYEVKFKRKRTFKNAPRTLDLDLLYFSQKVKRDKWCEVPHKGAKERVSVILPLGMI | Function: Catalyzes the transfer of pyrophosphate from adenosine triphosphate (ATP) to 6-hydroxymethyl-7,8-dihydropterin, an enzymatic step in folate biosynthesis pathway.
Catalytic Activity: 6-hydroxymethyl-7,8-dihydropterin + ATP = (7,8-dihydropterin-6-yl)methyl diphosphate + AMP + H(+)
Sequence Mass (Da): 18628
Sequ... |
P26281 | MTVAYIAIGSNLASPLEQVNAALKALGDIPESHILTVSSFYRTPPLGPQDQPDYLNAAVALETSLAPEELLNHTQRIELQQGRVRKAERWGPRTLDLDIMLFGNEVINTERLTVPHYDMKNRGFMLWPLFEIAPELVFPDGEMLRQILHTRAFDKLNKW | Function: Catalyzes the transfer of pyrophosphate from adenosine triphosphate (ATP) to 6-hydroxymethyl-7,8-dihydropterin, an enzymatic step in folate biosynthesis pathway.
Catalytic Activity: 6-hydroxymethyl-7,8-dihydropterin + ATP = (7,8-dihydropterin-6-yl)methyl diphosphate + AMP + H(+)
Sequence Mass (Da): 18079
Sequ... |
P43777 | MITAYIALGSNLNTPVEQLHAALKAISQLSNTHLVTTSSFYKSKPLGPQDQPDYVNAVAKIETELSPLKLLDELQRIENEQGRVRLRRWGERTLDLDILLYGNEIIQNERLTIPHYDMHNREFVIVPLFEIASDLVLPNSQIITELVKQFADHKMIKLNP | Function: Catalyzes the transfer of pyrophosphate from adenosine triphosphate (ATP) to 6-hydroxymethyl-7,8-dihydropterin, an enzymatic step in folate biosynthesis pathway.
Catalytic Activity: 6-hydroxymethyl-7,8-dihydropterin + ATP = (7,8-dihydropterin-6-yl)methyl diphosphate + AMP + H(+)
Sequence Mass (Da): 18299
Sequ... |
O25680 | MMREILTSRFFPSLFKKRLDFSNRVVLGLGSNLKNPLKILKNCFLYFKNHSKIGKIFSSPIYINPPFGYTKQPNFYNATIILKTSLSLRHFFALVFYIERRFGRQRKRDFKDAPRTLDIDIIAFNQVILRQNDLALPHPKWSERDSVLVPLALQQILFKKGEW | Function: Catalyzes the transfer of pyrophosphate from adenosine triphosphate (ATP) to 6-hydroxymethyl-7,8-dihydropterin, an enzymatic step in folate biosynthesis pathway.
Catalytic Activity: 6-hydroxymethyl-7,8-dihydropterin + ATP = (7,8-dihydropterin-6-yl)methyl diphosphate + AMP + H(+)
Sequence Mass (Da): 19282
Sequ... |
P71512 | MTRAYLGLGSNIGDKAAMLAGAVEHLAATPGIRVVARSADYRTPPWGDTDQDWFLNAAVAIDTELTPHGLLEVCLSIEAALGRVRERRWGPRVIDIDVLAYEGAQVSDERLVLPHRFVRERAFVLVPLAEIAPDLVIGGETVREALAKLDPSGIERVE | Function: Catalyzes the transfer of pyrophosphate from adenosine triphosphate (ATP) to 6-hydroxymethyl-7,8-dihydropterin, an enzymatic step in folate biosynthesis pathway.
Catalytic Activity: 6-hydroxymethyl-7,8-dihydropterin + ATP = (7,8-dihydropterin-6-yl)methyl diphosphate + AMP + H(+)
Sequence Mass (Da): 17206
Sequ... |
O69528 | MTRVVLSIGSNLGDRLAWLQSAVDGLGDAVVAVSPVYDTVPWGAVEQRSFLNAVVIADGPAYDTKAWLCRAQELERNAGRVRGQRWGARTLDVDLISCYQTSGATTGAVEVITCESNLTLPHPRAHLRAFVLVPWLAVDSDAELTVAGRAQRVDRLLAEMEPTEREGVRLTNLTLKLKRSSPARPVSPKSD | Function: Catalyzes the transfer of pyrophosphate from adenosine triphosphate (ATP) to 6-hydroxymethyl-7,8-dihydropterin, an enzymatic step in folate biosynthesis pathway.
Catalytic Activity: 6-hydroxymethyl-7,8-dihydropterin + ATP = (7,8-dihydropterin-6-yl)methyl diphosphate + AMP + H(+)
Sequence Mass (Da): 20761
Sequ... |
P61325 | MEKFTIKDLTDNLKFEIISGQDKLDTEIKSYGINRAGLELADYFKPFKDQSEWRATLMSTKESGYMLQFDEETKIKKYTQLMKCGIPVLIITNKFKDKTLIKVAKRLNFPLLRSDYPITIQLVQKIQDIYDIYFSPTAEEHAALMNIFGTGVLIKGKSGIGKSELCLDLIKHNHLFIGDDRIILTNKSNKIIGRVHPILKNLIEIRGIGIFDIVKSNGYQVIMNESPVELVVELVEYKEQNIDNSDRLGNDWSKFKILGVEIEHIQIPVSAGRSLVNIIESAVAQFKINKSKQFENVFDVIHKRTKEFLSSKK | Function: Catalyzes the ATP- as well as the pyrophosphate-dependent phosphorylation of a specific serine residue in HPr, a phosphocarrier protein of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS). HprK/P also catalyzes the pyrophosphate-producing, inorganic phosphate-dependent dephosphorylation... |
P75548 | MKKLLVKELIEQFQDCVNLIDGHTNTSNVIRVPGLKRVVFEMLGLFSSQIGSVAILGKREFGFLSQKTLVEQQQILHNLLKLNPPAIILTKSFTDPTVLLQVNQTYQVPILKTDFFSTELSFTVETYINEQFATVAQIHGVLLEVFGVGVLLTGRSGIGKSECALDLINKNHLFVGDDAIEIYRLGNRLFGRAQEVAKKFMEIRGLGIINVERFYGLQITKQRTEIQLMVNLLSLEKQTTVTFERLGTELKKQRLLGVDLSFYEIPISPGRKTSEIIESAVIDFKLKHSGYNSALDFIENQKAILKRKKDES | Function: Is a metabolite-sensitive enzyme that catalyzes the ATP-as well as probably the pyrophosphate-dependent phosphorylation of Ser-47 in HPr, a phosphocarrier protein of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS). HprK/P also catalyzes the pyrophosphate-producing, inorganic phosphate-... |
Q98PL1 | MKKKLFVSELIKHFDLEVLNHDFPEIEDREILTPSIKRLGLELSGHFIYDAISGVIVGWGTNESKFFEKIGSEKAKSSIEEIFSRKIPMLVLSKGFDKNYYSTIIEIANKHKTPVIFYKASLSEINTILGIYLLQYFAKKVQVHGTLVSVFGMGILIVGDSGLGKSEAALELVQKGHVLISDDAVLVSHYGNKYFGKAPYITKNLIEVRGLGLIDILSVHGLKSVLPECEINFVVELKDYEQNKSNFDRLGNKVLKYQIGEWKIPKIEIPIRQGRSVASLIEASANMFLSKLNGHDVLAMIQERSLNDE | Function: Catalyzes the ATP- as well as the pyrophosphate-dependent phosphorylation of a specific serine residue in HPr, a phosphocarrier protein of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS). HprK/P also catalyzes the pyrophosphate-producing, inorganic phosphate-dependent dephosphorylation... |
Q9K081 | MPSISVRRLFDDNQYKLQLAWAAGNSGADNRIGVEADKPVLALVGHLNFIHPNQIQVVGLAESEYLNRLESGETGYQFGDLFDISMSLVIVANGLPVSPGLRDYCHKNDIPLLTSKLESPYLMDVLRIYLQRTLAASSVKHGVFLDVFEIGVLITGHSGLGKSELALELISRGHSLIADDAVELFRIGPETLEGRCSPMLRDFLEVRGLGILNIRHIFGETSIRPKKILQLIINLVEADDEYMKQLDRLSIRTETESILNVNVRSVTLPVAVGRNLAVLVEAAVRNYILQLRGKDSTREFLERHQTQLKENEQHNEDRPD | Function: Catalyzes the ATP- as well as the pyrophosphate-dependent phosphorylation of a specific serine residue in HPr, a phosphocarrier protein of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS). HprK/P also catalyzes the pyrophosphate-producing, inorganic phosphate-dependent dephosphorylation... |
Q82Y30 | MSQVSITQLFEENQEKLNLQWGEPSAVIDRQLENHQINNSTQELIGHLNFVHPNWIQVLNQTSVNYLDQLDDVSLKKRLNQLAKSQLACLIVADDAPIPNAIRQFVNEQSVPLIQSATASLEIIWRLQSYLARMLAPAITRHGVLLDVLGMGVMITGESGVGKSELALELISRGHGLVADDVVELHRIGPETLEGQCPPLLRDFLEVRGLGMLNIRTIFGETAVRRRKNMKLIVHLEKTVGSSINAYERLPLSNLNEIILNVGIRKVIIPVAAGRNLAVLVEAAVRNYILQLRGIDSTQEFIRRHESEMAGNTAEHFDDS... | Function: Catalyzes the ATP- as well as the pyrophosphate-dependent phosphorylation of a specific serine residue in HPr, a phosphocarrier protein of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS). HprK/P also catalyzes the pyrophosphate-producing, inorganic phosphate-dependent dephosphorylation... |
Q8Y2D1 | MELTGVTAQSIFDDNAADLKLSWVAGLEGADRAFDVDFAKEATSAADLVGHLNLIHPNRIQVLGKPEITYYQRLSEENRKRQMGELILLEPPFLVVADGVDPPPDLELRCTRSSTPLFTSPISSAAVIDHLRLYLSRISAPRVTMHGVFLDILGMGVLIMGDSGLGKSELGLELISRGHGLVADDAVDFVRLGPDFIEGRCPPLLQNLLEVRGLGLLDIKTIFGETAVRRKMKIKLIVQLVRRNDGEFERLPLDSQYMDVLGLPIHMVKIQVAAGRNLAVLVEAAVRNTILRLRGIDTLRDFMDRQRAAMQAEAASHSPQ... | Function: Catalyzes the ATP- as well as the pyrophosphate-dependent phosphorylation of a specific serine residue in HPr, a phosphocarrier protein of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS). HprK/P also catalyzes the pyrophosphate-producing, inorganic phosphate-dependent dephosphorylation... |
O85093 | MSALRLRKVDALLAQATRELGAGQSLGFSAAGQDAELTLLPLLADAGEPAGAVWLSTAIGPLLLSDAEALLSLLGDIPLTLGGEQQAWYWQLFNQRLSPTVARLLAPVEPLHNKPQAPTLGCRVQIRRGGEQLHAHMHATPDTLLRLLRSASWQARTRTVDESWSVASPLIIGEMSLTREQIASLRPGDVVLPAHCQFDSAGQGFLSLAGRQWAAQTDQHAQRLFLRLSHEEHRHHEY | Function: Component of the type III secretion system, which is required for effector protein delivery, parasitism, and pathogenicity. Probably participates in the formation of a C-ring-like assembly along with hrcQb.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 25998
Sequence Length: 238
Domain: T... |
Q4L8L8 | MNLAWKEIKFYRFRYTLIMLIIFLLGSMVLFISGLAQGLARENISYLNNMPAEHYIVEDNKEPKLESSQLNQSQQNKIEKIIHENATQMGTQTLKINQQDQDVITLNTPKHLTPKLVSGNYPKKQNEIAISEKLTGNDLKVGDTVTFKGHHHNYKISGIMNESMYSHSSMILMNKEAFKSLNKQVSTFYPVDKINKDNKESLKQIKGIKVVNEKALTDNIASYQAEQMPLNLMIISLFVITAIVLSAFFYVMTIQKIPQIGILKAIGIKTKHLLTALLLQIILTTMVGVILAFSVILILNAFMPVTMPFYLSYSQVLLMI... | Function: Part of the ABC transporter complex hrt involved in hemin import. Responsible for the translocation of the substrate across the membrane (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 39569
Sequence Length: 351
Subcellular Location: Cell membrane
|
Q49ZT7 | MKLAWQEIKYYKFRYILIMLIILLLGIMVLFISGLAQGLARENISMLDNMKSEKYVLQDNKQPQIEKSIIKPEQQNKIEDITGQEPLKMAPQTLKIDKNEEDVLMINTVKNEKPELKAGHYPTKDNEVAINNKLTADGINVGDKIKLKDGKALKVSGVLNDTMYSHSSVVMMSDNGFNTLNKQASTIYPVKDLSKSEQEKVNDISGVKVFTENDITSEIPSYQAEQAPLNMMIVSLFVISAIVLSAFFYVMTIQKIPEIGILKAIGMKTKHLLSALIIQILITTMIGVIISVAIITGLSFLMPVSMPFHVTTSNLLLVVG... | Function: Part of the ABC transporter complex hrt involved in hemin import. Responsible for the translocation of the substrate across the membrane (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 38790
Sequence Length: 350
Subcellular Location: Cell membrane
|
O94641 | MADYPFTDKAAKTLSDAYSIAQSYGHSQLTPIHIAAALLSDSDSNGTTLLRTIVDKAGGDGQKFERSVTSRLVRLPAQDPPPEQVTLSPESAKLLRNAHELQKTQKDSYIAQDHFIAVFTKDDTLKSLLAEAGVTPKAFEFAVNNVRGNKRIDSKNAEEGFDALNKFTVDLTELARNGQLDPVIGREDEIRRTIRVLSRRTKNNPVLIGEPGVGKTSIAEGLARRIIDDDVPANLSNCKLLSLDVGSLVAGSKFRGEFEERIKSVLKEVEESETPIILFVDEMHLLMGAGSGGEGGMDAANLLKPMLARGKLHCIGATTL... | Function: Required, in concert with Hsp40 and Hsp70 and small Hsps, for the dissociation, resolubilization and refolding of aggregates of damaged proteins after heat or other environmental stresses. Extracts proteins from aggregates by unfolding and threading them in an ATP-dependent process through the axial channel o... |
P31539 | MNDQTQFTERALTILTLAQKLASDHQHPQLQPIHILAAFIETPEDGSVPYLQNLIEKGRYDYDLFKKVVNRNLVRIPQQQPAPAEITPSYALGKVLQDAAKIQKQQKDSFIAQDHILFALFNDSSIQQIFKEAQVDIEAIKQQALELRGNTRIDSRGADTNTPLEYLSKYAIDMTEQARQGKLDPVIGREEEIRSTIRVLARRIKSNPCLIGEPGIGKTAIIEGVAQRIIDDDVPTILQGAKLFSLDLAALTAGAKYKGDFEERFKGVLKEIEESKTLIVLFIDEIHMLMGNGKDDAANILKPALSRGQLKVIGATTNNE... | Function: Required, in concert with Hsp40 (YDJ1) and Hsp70 (SSA1) and small Hsps (HSP26), for the dissociation, resolubilization and refolding of aggregates of damaged proteins after heat or other environmental stresses. Extracts proteins from aggregates by unfolding and threading them in an ATP-dependent process throu... |
Q92598 | MSVVGLDVGSQSCYIAVARAGGIETIANEFSDRCTPSVISFGSKNRTIGVAAKNQQITHANNTVSNFKRFHGRAFNDPFIQKEKENLSYDLVPLKNGGVGIKVMYMGEEHLFSVEQITAMLLTKLKETAENSLKKPVTDCVISVPSFFTDAERRSVLDAAQIVGLNCLRLMNDMTAVALNYGIYKQDLPSLDEKPRIVVFVDMGHSAFQVSACAFNKGKLKVLGTAFDPFLGGKNFDEKLVEHFCAEFKTKYKLDAKSKIRALLRLYQECEKLKKLMSSNSTDLPLNIECFMNDKDVSGKMNRSQFEELCAELLQKIEVP... | Function: Acts as a nucleotide-exchange factor (NEF) for chaperone proteins HSPA1A and HSPA1B, promoting the release of ADP from HSPA1A/B thereby triggering client/substrate protein release . Prevents the aggregation of denatured proteins in cells under severe stress, on which the ATP levels decrease markedly. Inhibits... |
Q61699 | MSVVGLDVGSQSCYIAVARAGGIETIANEFSDRCTPSVISFGSKNRTIGVAAKNQQITHANNTVSSFKRFHGRAFNDPFIQKEKENLSYDLVPMKNGGVGIKVMYMDEEHFFSVEQITAMLLTKLKETAENNLKKPVTDCVISVPSFFTDAERRSVLDAAQIVGLNCLRLMNDMTAVALNYGIYKQDLPNAEEKPRVVVFVDMGHSSFQVSACAFNKGKLKVLGTAFDPFLGGKNFDEKLVEHFCAEFKTKYKLDAKSKIRALLRLHQECEKLKKLMSSNSTDLPLNIECFMNDKDVSGKMNRSQFEELCAELLQKIEVP... | Function: Acts as a nucleotide-exchange factor (NEF) for chaperone proteins HSPA1A and HSPA1B, promoting the release of ADP from HSPA1A/B thereby triggering client/substrate protein release (By similarity). Prevents the aggregation of denatured proteins in cells under severe stress, on which the ATP levels decrease mar... |
Q9S7U5 | MVKSTDGGGGSSSSSSVAPFLRKCYDMVDDSTTDSIISWSPSADNSFVILDTTVFSVQLLPKYFKHSNFSSFIRQLNIYGFRKVDADRWEFANDGFVRGQKDLLKNVIRRKNVQSSEQSKHESTSTTYAQEKSGLWKEVDILKGDKQVLAQELIKVRQYQEVTDTKMLHLEDRVQGMEESQQEMLSFLVMVMKNPSLLVQLLQPKEKNTWRKAGEGAKIVEEVTDEGESNSYGLPLVTYQPPSDNNGTAKSNSNDVNDFLRNADMLKFCLDENHVPLIIPDLYDDGAWEKLLLLSPSRKKTKKQENIVKKGKDDLTLEEE... | Function: Transcriptional activator that specifically binds DNA sequence 5'-AGAAnnTTCT-3' known as heat shock promoter elements (HSE).
PTM: Exhibits temperature-dependent phosphorylation.
Sequence Mass (Da): 42630
Sequence Length: 374
Domain: The hydrophobic-rich region (HR-A/B) corresponds to the oligomerization domai... |
Q9LVW2 | MTAIPNVVDIESSSSSLCQETATETVTVERGSSDSSSKPDDVVLLIKEEEDDAVNLSLGFWKLHEIGLITPFLRKTFEIVDDKVTDPVVSWSPTRKSFIIWDSYEFSENLLPKYFKHKNFSSFIRQLNSYGFKKVDSDRWEFANEGFQGGKKHLLKNIKRRSKNTKCCNKEASTTTTETEVESLKEEQSPMRLEMLKLKQQQEESQHQMVTVQEKIHGVDTEQQHMLSFFAKLAKDQRFVERLVKKRKMKIQRELEAAEFVKKLKLLQDQETQKNLLDVEREFMAMAATEHNPEPDILVNNQSGNTRCQLNSEDLLVDGG... | Function: Seed-specific transcriptional regulator that specifically binds DNA sequence 5'-AGAAnnTTCT-3' known as heat shock promoter elements (HSE). Seems to be specialized for the developmental expression of heat shock protein (HSP) genes during seed maturation. Activated by ABI3.
PTM: Exhibits temperature-dependent p... |
Q10PR4 | MGSKKRSPQHPAAAAPPPAVGGGGGGEVSGDGGASTANGPVVPKPSEVAPFLTKVYDMVSDPATDNVISWAEGGGSFVIWDSHAFERDLHRHFKHSNFTSFIRQLNTYGFRKVHPDRWEWANEGFIMGQKHLLKTIKRRKKSSQESPSEIQKAPVKTAPGTENIEIGKYGGLEKEVETLKRDKALLMQQLVDLRHYQQTSNLEVQNLIERLQVMEQNQQQMMALLAIVVQNPSFLNQLVQQQQQQRRSNWWSPDGSKKRRFHALEQGPVTDQETSGRGAHIVEYLPPVPETSGQVNPVEGAICSANSQPVPSPAVATPMD... | Function: Transcriptional regulator that specifically binds DNA of heat shock promoter elements (HSE).
PTM: Exhibits temperature-dependent phosphorylation.
Sequence Mass (Da): 45466
Sequence Length: 410
Domain: The hydrophobic-rich region (HR-A/B) corresponds to the oligomerization domain.
Subcellular Location: Cytopla... |
Q96320 | MTAVTAAQRSVPAPFLSKTYQLVDDHSTDDVVSWNEEGTAFVVWKTAEFAKDLLPQYFKHNNFSSFIRQLNTYGFRKTVPDKWEFANDYFRRGGEDLLTDIRRRKSVIASTAGKCVVVGSPSESNSGGGDDHGSSSTSSPGSSKNPGSVENMVADLSGENEKLKRENNNLSSELAAAKKQRDELVTFLTGHLKVRPEQIDKMIKGGKFKPVESDEESECEGCDGGGGAEEGVGEGLKLFGVWLKGERKKRDRDEKNYVVSGSRMTEIKNVDFHAPLWKSSKVCN | Function: Transcriptional regulator that specifically binds DNA sequence 5'-AGAAnnTTCT-3' known as heat shock promoter elements (HSE).
PTM: Exhibits temperature-dependent phosphorylation.
Sequence Mass (Da): 31328
Sequence Length: 284
Domain: The hydrophobic-rich region (HR-A/B) corresponds to the oligomerization domai... |
Q67TP9 | MAAAEAAAAVGKQQQKGGGGRGGGGGGPAPFLTKTNQMVEESATDEVISWGKEGRSFVVWKPVEFARDLLPLHFKHCNFSSFVRQLNTYGFRKVVPDRWEFANGNFRRGEQGLLSGIRRRKATTPQSSKSCGSGVNVAFPPPLPPLPPEPSATTSSGNDRSSSSASSPPRADITSENEQLRKDNQTLTMELARARRHCEELLGFLSRFLDVRQLDLRLLMQEDMRAAAGGVGGEQRVQEHAREEKCVKLFGVLLDDTHGAATRKRARCEEAAASERPIKMIRIGEPWVSVPSSGPARCGGDN | Function: Transcriptional regulator that specifically binds DNA of heat shock promoter elements (HSE).
PTM: Exhibits temperature-dependent phosphorylation.
Sequence Mass (Da): 32799
Sequence Length: 302
Domain: The hydrophobic-rich region (HR-A/B) corresponds to the oligomerization domain.
Subcellular Location: Cytopla... |
O22230 | MEDAGEHLRCNDNVNDEERLPLEFMIGNSTSTAELQPPPPFLVKTYKVVEDPTTDGVISWNEYGTGFVVWQPAEFARDLLPTLFKHCNFSSFVRQLNTYGFRKVTTIRWEFSNEMFRKGQRELMSNIRRRKSQHWSHNKSNHQVVPTTTMVNQEGHQRIGIDHHHEDQQSSATSSSFVYTALLDENKCLKNENELLSCELGKTKKKCKQLMELVERYRGEDEDATDESDDEEDEGLKLFGVKLE | Function: Transcriptional regulator that specifically binds DNA sequence 5'-AGAAnnTTCT-3' known as heat shock promoter elements (HSE).
PTM: Exhibits temperature-dependent phosphorylation.
Sequence Mass (Da): 28308
Sequence Length: 244
Domain: The hydrophobic-rich region (HR-A/B) corresponds to the oligomerization domai... |
Q9C635 | MAMMVENSYGGYGGGGGERIQLMVEGQGKAVPAPFLTKTYQLVDDPATDHVVSWGDDDTTFVVWRPPEFARDLLPNYFKHNNFSSFVRQLNTYGFRKIVPDRWEFANEFFKRGEKHLLCEIHRRKTSQMIPQQHSPFMSHHHAPPQIPFSGGSFFPLPPPRVTTPEEDHYWCDDSPPSRPRVIPQQIDTAAQVTALSEDNERLRRSNTVLMSELAHMKKLYNDIIYFVQNHVKPVAPSNNSSYLSSFLQKQQQQQPPTLDYYNTATVNATNLNALNSSPPTSQSSITVLEDDHTNHHDQSNMRKTKLFGVSLPSSKKRSH... | Function: Transcriptional regulator that specifically binds DNA sequence 5'-AGAAnnTTCT-3' known as heat shock promoter elements (HSE).
PTM: Exhibits temperature-dependent phosphorylation.
Sequence Mass (Da): 39615
Sequence Length: 348
Domain: The hydrophobic-rich region (HR-A/B) corresponds to the oligomerization domai... |
Q9LV52 | MEDDNSNNNNNNNVIAPFIVKTYQMVNDPSTDWLITWGPAHNSFIVVDPLDFSQRILPAYFKHNNFSSFVRQLNTYGFRKVDPDRWEFANEHFLRGQKHLLNNIARRKHARGMYGQDLEDGEIVREIERLKEEQRELEAEIQRMNRRIEATEKRPEQMMAFLYKVVEDPDLLPRMMLEKERTKQQQQVSDKKKRRVTMSTVKSEEEEVEEDEGRVFRVMSSSTPSPSSTENLYRNHSPDGWIVPMTQGQFGSYETGLVAKSMLSNSTSSTSSSLTSTFSLPESVNGGGGGGCGSIQGERRYKETATFGGVVESNPPTTPP... | Function: Transcriptional regulator that specifically binds DNA sequence 5'-AGAAnnTTCT-3' known as heat shock promoter elements (HSE).
PTM: Exhibits temperature-dependent phosphorylation.
Sequence Mass (Da): 37714
Sequence Length: 330
Domain: The hydrophobic-rich region (HR-A/B) corresponds to the oligomerization domai... |
Q5AQ33 | MIMNMTTDYRDPLLDLFGTESNSGNETSSPSDIPVINRSGTFNQQQFSPLLTQQSLYNTPNSGSTPNIFDPNYTQMQEEQTSPSSNKLQPEDPPRKKRNTRSQTKIHQQSEGDEYNSNDYKDSIDLDKPPVVEPSPPFFVESDTTPEFVIPTPTSEQQQQQHHELIAQDYQRSNNSNQFGNLTHYEPNLPPLPPLSESILPQTNTFHPLVLPHDPRHAITAGPANNSQQQQQQQQQDSSIPSDGISSKIQQLHAPSLSNNQSASQRKKKESSGPKTRPAFVMKIWSMVNDPANHEYIRWNDDGKTFQVFHREDFMKVILP... | Function: DNA-binding transcription factor that specifically binds heat shock promoter elements (HSE) and activates transcription. With HSP90, is required for the modulation of the chaperone levels in response to growth temperature, rather than the activation of acute responses to sudden thermal transitions. Activated ... |
J9VHZ9 | MTTNLYAIAGPSKPTTPTSTPSPRSEPPSPLKSLTSLPTNPLNPQGTSTSNALTNQSSSTGIGISKPGLSVDENGEVMKVPAFLNKLYTMVSDPEVDDLIYWGENGDSFFVPNAELFGRELLPRWFKHSNFSSFVRQLNMYGFHKVPHLQSGALKNETPIELWEFANPYFKRGQPQLLTKVTRKNNRLSNSGVGSSSSLGGSGAGGGMNTRSASAAAASGSGSGQIQQAISQGHEAGNHSTSGKYLITDGTTPGSAPPSHTSAGPLIAPQTLDLSAINSGIAAIRQTQASIATDLRKLQASNEALWRQAYETQEKQRKHE... | Function: DNA-binding transcription factor that specifically binds heat shock promoter elements (HSE) and activates transcription . Promotes thermotolerance by transiently regulating a subset of genes . Induces expression of STI, SSA1, SSA2, HSP78 and KAR2 during the heat response .
PTM: Phosphorylated at high temperat... |
P22813 | MSRSRSSAKAVQFKHESEEEEEDEEEQLPSRRMHSYGDAAAIGSGVPAFLAKLWRLVDDADTNRLICWTKDGQSFVIQNQAQFAKELLPLNYKHNNMASFIRQLNMYGFHKITSIDNGGLRFDRDEIEFSHPFFKRNSPFLLDQIKRKISNNKNGDDKGVLKPEAMSKILTDVKVMRGRQDNLDSRFSAMKQENEVLWREIASLRQKHAKQQQIVNKLIQFLITIVQPSRNMSGVKRHVQLMINNTPEIDRARTTSETESESGGGPVIHELREELLDEVMNPSPAGYTAASHYDQESVSPPAVERPRSNMSISSHNVDYS... | Function: DNA-binding protein that specifically binds heat shock promoter elements (HSE) and activates transcription. In higher eukaryotes, HSF is unable to bind to the HSE unless the cells are heat shocked.
PTM: Exhibits temperature-dependent phosphorylation.
Sequence Mass (Da): 76933
Sequence Length: 691
Subcellular ... |
P22121 | MGHNDSVETMDEISNPNNILLPHDGTGLDATGISGSQEPYGMVDVLNPDSLKDDSNVDEPLIEDIVNPSLDPEGVVSAEPSNEVGTPLLQQPISLDHVITRPASAGGVYSIGNSSTSSAAKLSDGDLTNATDPLLNNAHGHGQPSSESQSHSNGYHKQGQSQQPLLSLNKRKLLAKAHVDKHHSKKKLSTTRARPAFVNKLWSMVNDKSNEKFIHWSTSGESIVVPNRERFVQEVLPKYFKHSNFASFVRQLNMYGWHKVQDVKSGSMLSNNDSRWEFENENFKRGKEYLLENIVRQKSNTNILGGTTNAEVDIHILLNE... | Function: DNA-binding transcription factor that specifically binds heat shock promoter elements (HSE) and activates transcription.
PTM: Exhibits temperature-dependent phosphorylation.
Sequence Mass (Da): 75420
Sequence Length: 677
Subcellular Location: Nucleus
|
Q8YAC4 | MSDYLVKALAYDGMARVYAAVTTETIKEAQRRHDTWSVSSAALGRTMTGTLFLGAMQKEDQKITVKIEGDGPIGPIVADSNAQGQIRGYVTNPHVHFSELNEAGKLDVRRGVGTSGMLSVVKDLGFGENFTGQTPIVSGEIGEDFTYYLATSEQINSSVGVGVLVNPDDTIEAAGGFMLQLLPGATDEIIDEIEKNLMALPTVSRMIEAGETPESILAKLAGGEDKLQILEKIPVSFECNCSKERFGSAIISLGKEEIRSMIEEDHGAEAECHFCRNTYDFSEEELKTLYEEAK | Function: Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress.
PTM: Under oxidizing conditions two disulfide bonds are formed involving the reactive cysteine... |
Q1H2B1 | MQISDHLHRFLFENTPVRGSIVHLDDSFQQSLQHHDFPQILRQALGELMAASALLAATLKLKGGALVLQVQGKGPLKLLVVECTSDLGIRATAKWSGELDGMSFSDMVSNGHFVITLDPRDGGQPYQGIVPVEGGSIAEILQSYMQRSEQIDTRMWLACDGKRAAGMLVQKMPDQPDAADPDAWNRIIMLADTVRDEELLDLSAVSLIKRLFNEEDVRLFKEQPIKFHCGCSRESVGNMLRMLGEEEVADILAEQHTIDINCDFCNAEYHFDEVDAEQLFTTEIVMPGNDVRH | Function: Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress.
PTM: Under oxidizing conditions two disulfide bonds are formed involving the reactive cysteine... |
Q9JWC8 | MNQTAINRADVRTRFIFDDMPVRGLHVRLENVWQHIVKQKNYPAAIRRALGELLAAGVLLSGNLKNEGTLIVQVQGQGRLKMLVAEATSDRTVRATARWDETAEIADDESLGDLLGEGGVFVLTLQPKDGEPWQGVVPLEGDGIAQMLVNYMKRSEQLDTHIVLSASDEAAGGLLVQRLPEEVLDEEAWEHVSTLARTLTAEELAGLDAQHVLYRLFHETPPRVFEPETFEFSCTCSRGKVSDMLLMLGGEEVGGVVVEQGSIEVDCDFCHSKYVFDETDVNALFGEDVVGVAKGLPRHTVQ | Function: Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress.
PTM: Under oxidizing conditions two disulfide bonds are formed involving the reactive cysteine... |
Q3J9G2 | MNNRDNLHRFLFEEAKIRGELVQLDASWRAVLACHDYPAVVQSQLGQALAATILLSATIKFKGSLILQTQSEGPLQTLVAQATHHRTLRGLARWDGDVPHGSLSETYGSGRLALTIQTEGKNPYQGIVSLEGVNLAEALQTYFSRSEQLRTRLWLVADEQQAVGLFLQELPSQQGHKTDWERIALLASTVTTQEMLSLPSTELLYRLFNEEQVRLFEPEPVSFRCGCSRGRIEQTLAALGREEMESILKEQGIIEVDCEFCNRHYNFDRVDMEQLFTEQVKAPVTSTRH | Function: Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress.
PTM: Under oxidizing conditions two disulfide bonds are formed involving the reactive cysteine... |
P57115 | MTTILSVRLKNKVVIGGDGQATLGNTIMKSNVKKIRSLYHEKVIAGFAGGTADAFTLFEMFDKKLAMYQGQLQRAAIELAKDWRSDRMLRKLEALLAVADKKTSLIITGNGDVIQPEDDLIAIGSGGSYAQSSARALIENTHLDANQIVRKSLNIAANICIYTNHNFTIKELFSEK | Function: Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
Catalytic Activity: ATP-dependent cleavage of peptide bonds with broad specificity.
Sequence Mass (Da): 19317
Sequence Length: 176
Subcellular Location: Cytoplasm
EC: 3.4.25.2
|
Q9ZDK9 | MSDNFALHGTTILCLKKKEEIIIAADGQVSHGNTVLKSTARKLRTIANNKIIVGFAGSTADGLALFEKLEIKIEQYNSNLLRSAVELAKDWRNDKYLRRLEAMMIVADRSHILILTGNGDVIEPENNVAAIGSGGLFALSAARALMSYENNLTAEEIALKSMNIAADLCVFSNHNIIMEKVV | Function: Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
Catalytic Activity: ATP-dependent cleavage of peptide bonds with broad specificity.
Sequence Mass (Da): 19873
Sequence Length: 182
Subcellular Location: Cytoplasm
EC: 3.4.25.2
|
Q28222 | MAKAAAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDPVVQSDMKHWPFQVINDGDKPKVQVSYKGETKAFYPEEISSMVLTKMKEIAEADLGYPVTNAVITVPAYFNDSQRQATKDAGVIAGLNVLRIINEPTRTIAYALDRTGKGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTTWVEDFDNRLVNHFVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQASLEIDSLFEGIDFYTSITRARFEELCSDLFRSTLEPVEKALR... | Function: Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in th... |
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