ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
P37349 | MVNLVIVSHSSRLGEGVGELARQMLMSDSCKIAIAAGIDDPQNPIGTDAVKVMEAIESVADADHVLVMMDMGSALLSAETALELLAPEIAAKVRLCAAPLVEGTLAATVSAASGADIDKVIFDAMHALEAKREQLGLPSSDTEISDTCPAYDEEARSLAVVIKNRNGLHVRPASRLVYTLSTFNADMLLEKNGKCVTPESINQIALLQVRYNDTLRLIAKGPEAEEALIAFRQLAEDNFGETEEVAPPTLRPVPPVSGKAFYYQPVLCTVQAKSTLTVEEEQDRLRQAIDFTLLDLMTLTAKAEASGLDDIAAIFSGHHT... | Function: Component of the dihydroxyacetone kinase complex, which is responsible for the phosphoenolpyruvate (PEP)-dependent phosphorylation of dihydroxyacetone. DhaM serves as the phosphoryl donor. Is phosphorylated by phosphoenolpyruvate in an EI- and HPr-dependent reaction, and a phosphorelay system on histidine res... |
Q9CIV6 | MTYGIVIVSHSPEIASGLKKLIREVAKNISLTAIGGLENGEIGTSFDRVMNAIEENEADNLLTFFDLGSARMNLDLVSEMTDKELTIFNVPLIEGAYTASALLEAGATFEAIKEQLEKMLIEK | Function: Component of the dihydroxyacetone kinase complex, which is responsible for the phosphoenolpyruvate (PEP)-dependent phosphorylation of dihydroxyacetone. DhaM serves as the phosphoryl donor. Is phosphorylated by phosphoenolpyruvate in an EI- and HPr-dependent reaction, and a phosphorelay system on histidine res... |
P0DN88 | MIGLIIVSHSKLLADGLHQLAAQMQNKQKCHIITAAGVDDETHPIGTDAVKVMEAIESLSDAEHIILLMDLGSALLSAETALDLIDPDLAEKVHLCSAPLVEGAIAITAAASGGASIDEILNEAQQALQAKQQQLNDTVTTTENEKDKHTHFSEQALTTQWVVKNPSGLHIRPAAKLATLLSGFTATLELRHGEKRADAKSMNQIALLQVRQGDKITLVAEGVDSQNAINAFNQLAQHNFGDNIATTDSKTFVGKTAYVPTVAGLAHHHAPNTELCISSYQTSENETRRATKAIEQLKTHLDSLANTLNEQYGEEIANIF... | Function: Component of the dihydroxyacetone kinase complex, which is responsible for the phosphoenolpyruvate (PEP)-dependent phosphorylation of dihydroxyacetone. DhaM serves as the phosphoryl donor. Is phosphorylated by phosphoenolpyruvate in an EI- and HPr-dependent reaction, and a phosphorelay system on histidine res... |
P28997 | MTDTLNPLVAAQEKVRIACEKLGCDPAVYELLKEPQRVIEISIPVKMDDGTVKVFKGWRSAHSSAVGPSKGGVRFHPNVNMDEVKALSLWMTFKGGALGLPYGGGKGGICVDPAELSERELEQLSRGWVRGLYKYLGDRIDIPAPDVNTNGQIMSWFVDEYVKLNGERMDIGTFTGKPVAFGGSEGRNEATGFGVAVVVRESAKRFGIKMEDAKIAVQGFGNVGTFTVKNIERQGGKVCAIAEWDRNEGNYALYNENGIDFKELLAYKEANKTLIGFPGAERITDEEFWTKEYDIIVPAALENVITGERAKTINAKLVCE... | Catalytic Activity: H2O + L-glutamate + NAD(+) = 2-oxoglutarate + H(+) + NADH + NH4(+)
Sequence Mass (Da): 46514
Sequence Length: 421
Pathway: Amino-acid degradation; L-glutamate degradation via hydroxyglutarate pathway; crotonoyl-CoA from L-glutamate: step 1/5.
EC: 1.4.1.2
|
B2RKJ1 | MKTQEIMTMLEAKHPGESEFLQAVKEVLLSVEEVYNQHPEFEKNGIIERIVEPDRVFTFRVPWVDDQGKVQVNIGYRVQFNNAIGPYKGGIRFHPSVNLSILKFLGFEQMFKNALTTLPMGGGKGGADFSPKGKSEAEIMRFCQSFMTELWRNIGPDTDIPAGDIGVGGREVGYMFGMYKKLAREHTGTLTGKGFEFGGSRLRPESTGFGAVYFVQNMCKQNGVDYKGKTLAISGFGNVAWGVAQKATELGIKVVTISGPDGYVYDPDGINTPEKFRCMLDLRDSGNDVVSDYVKRFPNAQFFPGKKPWEQKVDFAMPCA... | Function: Probably involved in degradation rather than biosynthesis of glutamate.
Catalytic Activity: H2O + L-glutamate + NAD(+) = 2-oxoglutarate + H(+) + NADH + NH4(+)
Sequence Mass (Da): 49199
Sequence Length: 445
Subcellular Location: Cell surface
EC: 1.4.1.2
|
A3MUY9 | MSTTYIVSDFLINTLLTIKRGVELAGLPPEFYEALEKPKRILVVNIPVKMDDGKIKYFEGYRVQHNDALGPFKGGIRFHPEVTLADDIALAMLMTLKNSLAGLPYGGAKGAVRVDPRRLSRRELEELARGYARAVAPLIGEQLDIPAPDVGTDSQVMAWMVDEYSRLVGRNAPAVFTSKPPELWGNPVREYSTGFGVAVAAREVAKRLWGGIVGKTAAVQGLGNVGRWAAYWLEKMGAKVVAVSDVNGVVYRERGLDVDLIRETKAKGPQLLEMISQKNGVEIVKNPDQIFSLDVDILVPAAIENVVREDNVDGVRARLV... | Function: Catalyzes the reversible oxidative deamination of L-glutamate to 2-oxoglutarate and ammonia, thereby playing a key role at the intersection of the carbon and nitrogen metabolic pathways. Is strictly specific for NAD(+)/NADH as the acceptor/donor, since it cannot use NADP(+)/NADPH. May function in vivo in the ... |
P80053 | MMEEVLSSSLYTQQVKKLYKVGELLGLDNETLETLSQPERIIQVKIQIRGSDGKLKTFMGWRSQHNSALGPYKGGVRYHPNVTQDEVEALSMIMTWKNSLLLLPYGGGKGGVRVDPKKLTREELEQLSRKYIQAIYKYLGSELDIPAPDVNTDSQTMAWFLDEYIKITGKVDFAVFTGKPVELGGIGVRLYSTGLGVATIAKEAANKFIGGVEEARVIIQGFGNVGYYAGKFLSEMGAKIVGVSDSKGGVINEKGIDVGKAIEIKEKTGSVINYPEGRKVTNEELLISDCDILIPAALENVINKFNAPKVKAKLIVEGAN... | PTM: Methylation of lysine residues may play a role in the thermal stability of this enzyme.
Catalytic Activity: H2O + L-glutamate + NAD(+) = 2-oxoglutarate + H(+) + NADH + NH4(+)
Sequence Mass (Da): 46031
Sequence Length: 420
EC: 1.4.1.3
|
P16027 | MSRFVTSVSALAMLALAPAALSSGAYANDKLVELSKSDDNWVMPGKNYDSNNFSDLKQINKGNVKQLRPAWTFSTGLLNGHEGAPLVVDGKMYIHTSFPNNTFALGLDDPGTILWQDKPKQNPAARAVACCDLVNRGLAYWPGDGKTPALILKTQLDGNVAALNAETGETVWKVENSDIKVGSTLTIAPYVVKDKVIIGSSGAELGVRGYLTAYDVKTGEQVWRAYATGPDKDLLLASDFNIKNPHYGQKGLGTGTWEGDAWKIGGGTNWGWYAYDPGTNLIYFGTGNPAPWNETMRPGDNKWTMTIFGRDADTGEAKFG... | Cofactor: Binds 1 PQQ group per subunit. PQQ is inserted between disulfide Cys-130-Cys-131 and the indole ring of Trp-270.
Function: Catalyzes the oxidation of primary alcohols including methanol.
Catalytic Activity: a primary alcohol + 2 Fe(III)-[cytochrome cL] = an aldehyde + 2 Fe(II)-[cytochrome cL] + 2 H(+)
Locatio... |
P14775 | MKTTLIAAAIVALSGLAAPALAYDGTKCKAAGNCWEPKPGFPEKIAGSKYDPKHDPKELNKQADSIKQMEERNKKRVENFKKTGKFEYDVAKISAN | Function: Catalyzes the oxidation of primary alcohols including methanol.
Catalytic Activity: a primary alcohol + 2 Fe(III)-[cytochrome cL] = an aldehyde + 2 Fe(II)-[cytochrome cL] + 2 H(+)
Sequence Mass (Da): 10512
Sequence Length: 96
Subcellular Location: Periplasm
EC: 1.1.2.7
|
P38540 | MKHVLTLLALASVFAVSNQALAYDGQNCKEPGNCWENKPGYPEKIAGSKYDPKHDPVELNKQEESIKAMDARNAKRIANAKSSGNFVFDVK | Function: Catalyzes the oxidation of primary alcohols including methanol.
Catalytic Activity: a primary alcohol + 2 Fe(III)-[cytochrome cL] = an aldehyde + 2 Fe(II)-[cytochrome cL] + 2 H(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 10037
Sequence Length: 91
Subcellular Location: Cell inner memb... |
Q09053 | YDGTNCKPGVCWEPKPGY | Function: Catalyzes the oxidation of primary alcohols including methanol.
Catalytic Activity: a primary alcohol + 2 Fe(III)-[cytochrome cL] = an aldehyde + 2 Fe(II)-[cytochrome cL] + 2 H(+)
Sequence Mass (Da): 2014
Sequence Length: 18
Subcellular Location: Periplasm
EC: 1.1.2.7
|
P64302 | MDVLRTPDSRFEHLVGYPFAPHYVDVTAGDTQPLRMHYVDEGPGDGPPIVLLHGEPTWSYLYRTMIPPLSAAGHRVLAPDLIGFGRSDKPTRIEDYTYLRHVEWVTSWFENLDLHDVTLFVQDWGSLIGLRIAAEHGDRIARLVVANGFLPAAQGRTPLPFYVWRAFARYSPVLPAGRLVNFGTVHRVPAGVRAGYDAPFPDKTYQAGARAFPRLVPTSPDDPAVPANRAAWEALGRWDKPFLAIFGYRDPILGQADGPLIKHIPGAAGQPHARIKASHFIQEDSGTELAERMLSWQQAT | Function: Catalyzes hydrolytic cleavage of carbon-halogen bonds in halogenated aliphatic compounds, leading to the formation of the corresponding primary alcohols, halide ions and protons.
Catalytic Activity: 1-haloalkane + H2O = a halide anion + a primary alcohol + H(+)
Sequence Mass (Da): 33358
Sequence Length: 300
E... |
P64304 | MSIDFTPDPQLYPFESRWFDSSRGRIHYVDEGTGPPILLCHGNPTWSFLYRDIIVALRDRFRCVAPDYLGFGLSERPSGFGYQIDEHARVIGEFVDHLGLDRYLSMGQDWGGPISMAVAVERADRVRGVVLGNTWFWPADTLAMKAFSRVMSSPPVQYAILRRNFFVERLIPAGTEHRPSSAVMAHYRAVQPNAAARRGVAEMPKQILAARPLLARLAREVPATLGTKPTLLIWGMKDVAFRPKTIIPRLSATFPDHVLVELPNAKHFIQEDAPDRIAAAIIERFG | Function: Catalyzes hydrolytic cleavage of carbon-halogen bonds in halogenated aliphatic compounds, leading to the formation of the corresponding primary alcohols, halide ions and protons.
Catalytic Activity: 1-haloalkane + H2O = a halide anion + a primary alcohol + H(+)
Sequence Mass (Da): 32151
Sequence Length: 286
E... |
Q9A919 | MDVLRTPDERFEGLADWSFAPHYTEVTDADGTALRIHHVDEGPKDQRPILLMHGEPSWAYLYRKVIAELVAKGHRVVAPDLVGFGRSDKPAKRTDYTYERHVAWMSAWLEQNDLKDIVLFCQDWGGLIGLRLVAAFPERFSAVVVSNTGLPIGVGKSEGFEAWLNFSQNTPELPVGFILNGGTARDLSDAERSAYDAPFPDESYKEGARIFPALVPITPEHASVEENKAAWAVLETFDKPFVTAFSDADPITRGGEAMFLARVPGTKNVAHTTLKGGHFVQEDSPVEIAALLDGLVAGLPQA | Function: Catalyzes hydrolytic cleavage of carbon-halogen bonds in halogenated aliphatic compounds, leading to the formation of the corresponding primary alcohols, halide ions and protons.
Catalytic Activity: 1-haloalkane + H2O = a halide anion + a primary alcohol + H(+)
Sequence Mass (Da): 33155
Sequence Length: 302
E... |
O30010 | MKEIWLLAESESWDEAKEMLKDAIEIGFDGALVRRDFLERAEKLGRMKIVPIEDAVVKISSAEDQERALQREVVVLKFEDWKVIPLENIVAMKKSGKVIAAVDTIEDAKLALTTLERGADGIAVSGDRETLRKFYEVVKEEGERVELVRARVKEIRPLGVGERVCIDTVTLMTPGEGMLVGNQASFMFLVASESEESEYVASRPFRVNAGSVNAYLKVGDKTRYLAELKAGDEVEVVKFDGAVRKSYVGRVKIERRPLILIRAEVDGVEGSVILQNAETIKLVAPDGKHVSVAELKPGDEILVWLGKKARHFGVEVDEFI... | Function: Catalyzes the oxidative deamination and cyclization of 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid (ADH) to yield 3-dehydroquinate (DHQ), which is fed into the canonical shikimic pathway of aromatic amino acid biosynthesis.
Catalytic Activity: 2-amino-2,3,7-trideoxy-D-lyxo-hept-6-ulosonate + H2O + NAD(+)... |
A0RU27 | MPRAQLQRFLSGISAEGIRTVYLDPKDAAKAKLDAMHSSPSSRYVVLEGRAAKPRGKKVGRRFKILSNKDIDGVLQEAQKGLDFVITEVQDWKIIPLENMIAKLHKIHTRLYAVARSPAEVRKMFSILDVGVDGVIFTASTVGDVREALVHLGTKSFRLQPARITEIREVGDGERVCVDTASMLERGEGMLVGSRSNFMFLVHNESVGSSFTSPRPFRVNAGAVHSYTLGTDGNTLYLSEVETGTEVLVLDSHGRARRAAVGRSKIERRPMLMIKAEADGEIGGIIAQDAETIRFVRPGGGLVSVTHLKKGDKVLVHSKP... | Function: Catalyzes the oxidative deamination and cyclization of 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid (ADH) to yield 3-dehydroquinate (DHQ), which is fed into the canonical shikimic pathway of aromatic amino acid biosynthesis.
Catalytic Activity: 2-amino-2,3,7-trideoxy-D-lyxo-hept-6-ulosonate + H2O + NAD(+)... |
B1L5W7 | MRSKELIILADSSPDSVVEKAIKMGLKVAAVDQSVKERLKGYLDPSLIVEVSEWPSEGELTLFKIRGPEDVEILRREANERKFLIESESWKIIPLENIIAEVGGERIYAIADDLEEARSLLGVLEIGVKGVVIPIKDSAQLERALRLSEEVNPLNLREARVTEVKQVGMGDRVCVDTTSILSKGEGMLVGGSASFLFLVHSENIESPFTSPREFRVNAGAVSNYLLAPGGKTLYLSEVRAGSEVLAVSVDGRRRAVSVGRAKVERRPMVLVRASSDGEEGWTVLQLAETIPLVKPDGSTVAVTDLKPGDRVLVYVSERKA... | Function: Catalyzes the oxidative deamination and cyclization of 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid (ADH) to yield 3-dehydroquinate (DHQ), which is fed into the canonical shikimic pathway of aromatic amino acid biosynthesis.
Catalytic Activity: 2-amino-2,3,7-trideoxy-D-lyxo-hept-6-ulosonate + H2O + NAD(+)... |
A6UW69 | MKFGWIMANDEDWEERKETVKDSLESSIPAVMVYEEDIEKVKELGNIKTISKNPNSDIVVIDKGDDLTILFDAKKEGKETGVFISIECKEDEEYASEVSRYDYVDYIILEGKDWNIIPLENLIADLFDENIKIVSLAKDINDARTAYEILERGVDGVLYVPKDINDVKDFATLIEKMNSEKLDLDCATITKVEAIGSGDRVCIDTCSMMEMGEGMLIGSYSRALFLVHAETVENPYVATRPFRVNAGPVHAYVLCTGNKTRYLSELKAGDGILIVDKDGMTREGIVGRVKIEKRPLMLIEAEYVGGEIVRTIVQNAETIR... | Function: Catalyzes the oxidative deamination and cyclization of 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid (ADH) to yield 3-dehydroquinate (DHQ), which is fed into the canonical shikimic pathway of aromatic amino acid biosynthesis.
Catalytic Activity: 2-amino-2,3,7-trideoxy-D-lyxo-hept-6-ulosonate + H2O + NAD(+)... |
Q0W131 | MSDKLVWIDAQGSWNGAKEKVTGALESGANAVLVSPENVERVRELGKMTVAAAEGNPDIRVIGIGSEGDGTLFLPHDLNSSEDMATAKALKAQGTTTAAYVRLAGKEYEQFAARMGKLCDYLIIEGDDWKVIPLENLIAELGGSGTKILAKARDIDEASVALQTLEKGADGVLVDVDDPLKVREIARAVSTKQAGLGLTPVTITAVRDAGTGDRVCIDTCSLMTPGEGMLIGNQSSGLFLVQSEAEESPYVASRPFRVNAGAVHEYVLVGEKTRYLSELASGDPALIVTRDGDARKATIGRVKIERRPLLYVEAETGDRK... | Function: Catalyzes the oxidative deamination and cyclization of 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid (ADH) to yield 3-dehydroquinate (DHQ), which is fed into the canonical shikimic pathway of aromatic amino acid biosynthesis.
Catalytic Activity: 2-amino-2,3,7-trideoxy-D-lyxo-hept-6-ulosonate + H2O + NAD(+)... |
Q12UJ7 | MDKTIWIKADKGHWEAHKDRITTGLESGANCVLVNSDEVEKVRELGDIQVAAFTYDDKSGADIVVVGKGGEGDGTKPLSPDPVGSLDMITAIRLKEKGLTVGAYVVIQNKKYEEFAAEIGKECDFLIIVGTDWKVIPLENLIAALQDSDVKIIAGVRDQDEAKLALETMEHGSEGVLLDSDDPNTIKATVAVAERSGIEDLKLVPGKVTKVEAVGMGDRVCVDTCNMMTKGEGMLVGSQASGMFLVHSESEESPYVASRPFRVNAGAVHAYVKVGDRTRYLSELSSGDEVTIVNAGGKQRTGIVGRVKIERRPLMLVEAE... | Function: Catalyzes the oxidative deamination and cyclization of 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid (ADH) to yield 3-dehydroquinate (DHQ), which is fed into the canonical shikimic pathway of aromatic amino acid biosynthesis.
Catalytic Activity: 2-amino-2,3,7-trideoxy-D-lyxo-hept-6-ulosonate + H2O + NAD(+)... |
Q2FQ51 | MKQVFVDLRPWDKELAIAALESGAAGVIADSAGPVRELGRILVIAPDGDLIPGQDIHEITIGNTEDQARAMEAARTCRIIVHTPDWTIIPLENLVACGDNVIAVVSDIKEAEQALTVLEKGVSGVLVKTDDPDLVRSICRMVQSGISGQQLHRLTVTTVKPAGMGERVCVDTCSLMVDGEGMLVGNTSSGFFLVHAETLVNPYVAPRPFRVNAGGVHAYLQVPEGKTAYLADLKAGDRVMIVHGNGSCREATVGRVKIERRPLFLVEAESECQKVSIILQNAETIRLVRPDNSAVSVTSLKPGDVVLGRVESGGRHFGMA... | Function: Catalyzes the oxidative deamination and cyclization of 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid (ADH) to yield 3-dehydroquinate (DHQ), which is fed into the canonical shikimic pathway of aromatic amino acid biosynthesis.
Catalytic Activity: 2-amino-2,3,7-trideoxy-D-lyxo-hept-6-ulosonate + H2O + NAD(+)... |
Q58646 | MKFGWVNVIGDNWEEKKKIVTTALESSIPVVVAEPEDIEKIKELGNIKVASHSLDADIVLVNKNDNIEFLKEAKNLGKETAIYIPIESKEDEEFASEVARFGFVDNIILEGRDWTIIPLENLIADLFHRDVKIVASVNSVDEAKVAYEILEKGTDGVLLNPKNLEDIKELSKLIEEMNKEKVALDVATVTKVEPIGSGDRVCIDTCSLMKIGEGMLIGSYSRALFLVHSETVENPYVATRPFRVNAGPVHAYILCPGNKTKYLSELKAGDKVLIVDKDGNTREAIVGRVKIERRPLVLIEAEYKGDIIRTILQNAETIRL... | Function: Catalyzes the oxidative deamination and cyclization of 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid (ADH) to yield 3-dehydroquinate (DHQ), which is fed into the canonical shikimic pathway of aromatic amino acid biosynthesis.
Catalytic Activity: 2-amino-2,3,7-trideoxy-D-lyxo-hept-6-ulosonate + H2O + NAD(+)... |
A2SU08 | MTIQLPPILIRADHLQTYDERKAIVASALESGYTHIILRPEDEALRHLGRYTAILADGKNLMYSGERIGVLLNLTGAEEMEEAYSLKNAVPNLIISPENWKVIPLENLISRFQNAETSVYICVKTPEEARLAFQTMEVGCDGIVITPDGPADLAAFSGIRNDEYPIVDLETAVVTKISTLSLGDRVCIDTCSLLERGEGMLIGSQSSCLFLVCSESFESEYVNSRPFRVNAGAVHSYILCPDGTTKYLSEIASGNELLSRMPDGNLRTVNVGRVKIEIRPMLYIEAKAGGKTYSVVLQNAETIRLGTPSGAVSVSDLAIG... | Function: Catalyzes the oxidative deamination and cyclization of 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid (ADH) to yield 3-dehydroquinate (DHQ), which is fed into the canonical shikimic pathway of aromatic amino acid biosynthesis.
Catalytic Activity: 2-amino-2,3,7-trideoxy-D-lyxo-hept-6-ulosonate + H2O + NAD(+)... |
Q68FN7 | MAALVRISSLCHRGVSPLLFRPSSLIRPLAVQQKDHDCSYLISARIHATPSNYAGSGSKAATMHWTGERILSIALLSLAPVAYFCPSPAVDYSLAAALTLHGHWGLGQVVTDYVHGDAKIKMANAGLFVLSTVTFAGLCYFNYHDVGICKAVALLWSK | Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 16973
Sequence Le... |
O29573 | MVEMESAKSVLEPLAWLMQMITGLLMILLVTAHFYVTHMTTHDALRYAEVVERVAQPEFKALYALLLLAVSFHAFNGLRAILLDTNAGMRKKGAVSALTTLAFLLAFFYGLYLLFSI | Cofactor: The heme is bound between the two transmembrane subunits.
Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13100
Sequence Length: 117
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle.
Subcellular Location: Cell ... |
Q750S6 | MQGIKMASPVIRAACKRSLHQSAVRAITIPFLPTLPQNPGGVKGDVNEANPVPPANKMHGSLHWNIERAFAVAAVPLVGLPLVAGSGVSTLMDSLLASVMLGHCYIGFQACIIDYIPQRVYGKFHQYAMYLLAFGSLLSGVGIYKMESEGYGICGAVAAVWSGKAAREEKA | Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 18143
Sequence Le... |
O62215 | MAASLRHMAHFQKALLVARSAPRISTIVRATSTLNDGASKVPDHSMHFKLERLWAVGMLPILPASYFIHGPVMDAVLTVALTLHIHWGIHGVVYDYARPYVIGEAAAKAAHVGVYLITGLLLGALLHFNTNDVGITKAFELVFSL | Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 15765
Sequence Le... |
Q5ZIS0 | MAALVLLRAGLARPRGVPTALLRGTLLRHSAVLTAAADRSAPARQSHGGAPQGHGSSKAASLHWTSERAVSALLLGLLPAAYLYPGPAVDYSLAAALTLHGHWGLGQVITDYVHGDTPIKVANTGLYVLSAITFTGLCYFNYYDVGICKAVAMLWSI | Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 16435
Sequence Le... |
P54323 | MITFQWLIVRVVALFISLTILIDIEMFVVMLSFLIIHISIGLKAIIHDYIHFQKIKLMLLILLRVSAIEISRSFRTFYIIIKNT | Cofactor: The heme is bound between the two transmembrane subunits.
Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 9906
Sequence Length: 84
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle.
Subcellular Location: Mitocho... |
P51057 | MDMVDRTSRRGYRDWFVQRITALLSGIYAVFVIVFLLVHHPISYPQWHALFSHLIMKIFTLIVIFSILWHAWIGMWTIFTDYVKNKPIRLALETLVCLLLVGYFVWAIEFLWIAR | Cofactor: The heme is bound between the two transmembrane subunits.
Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13774
Sequence Length: 115
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle.
Subcellular Location: Cell ... |
Q9VCI5 | MSLSLLLRGAVRCNAANLVKSARITPLKSYSTLVANVQRKAVVQPLAVAKIVAPVVREISVSAPRMASAGSSHTLLWTVERIVSAGLLAVIPAAFIAPSQVLDALMAISVVIHTHWGVEAMVVDYMRPSVVGNVLPKVAHIALIIISVATLGGLFYFIQNDVGLANGIKRFWAIKGKDAEKA | Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 19300
Sequence Le... |
Q8X9A9 | MVSNASALGRNGVHDFILVRATAIVLTLYIIYMVGFFATSGELTYEVWIGFCASAFTKVFTLLALFSILIHAWIGMWQVLTDYVKPLALRLMLQLVIVVALVVYVIYGFVVVWGV | Cofactor: The heme is bound between the two transmembrane subunits.
Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 12824
Sequence Length: 115
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle.
Subcellular Location: Cell ... |
Q9HQ63 | MSESYDRGLVADFGRWTEFSAGMWAWVFHKFTGWVLVGYLFTHISVLSTSLQGAQVYNSTLSGLESLAIVRLLEVGLLAVAVFHILNGIRLLFVDLGVGLEAQDKSFYASLVLTGVIVVASVPTFLTGAF | Cofactor: The heme is bound between the two transmembrane subunits.
Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 14149
Sequence Length: 130
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle.
Subcellular Location: Cell ... |
O14521 | MAVLWRLSAVCGALGGRALLLRTPVVRPAHISAFLQDRPIPEWCGVQHIHLSPSHHSGSKAASLHWTSERVVSVLLLGLLPAAYLNPCSAMDYSLAAALTLHGHWGLGQVVTDYVHGDALQKAAKAGLLALSALTFAGLCYFNYHDVGICKAVAMLWKL | Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 17043
Sequence Le... |
Q9CXV1 | MAVLLKLGVLCSGQGARALLLRSRVVRPAYVSAFLQDQPTQGRCGTQHIHLSPSHHSGSKAASLHWTSERVVSVLLLGLIPAGYLNPCSVVDYSLAAALTLHSHWGLGQVVTDYVHGDTLPKAARAGLLALSALTFAGLCYFNYHDVGICRAVAMLWKL | Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 17014
Sequence Le... |
Q7SGY6 | MASVARSSALLKQVAAQQSVAANGLRVAAFHTTSRKSLLPPPPQRIEGTVNDPVEVPPPSPSHGSYHWTFDRVVAAGLIPLTVAPFAAGSLNPTMDAVLAATILIHSHTGFGNIIVDYVPSKRVPKARKVFTWGLNAATVLVGLALYEFETTDVGLTETIKRVWKA | Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 17675
Sequence Le... |
O94337 | MDESLAKDAVFVASSKPSDLTTEVVGPDFNKYDERKKAGGPGITVEELVESYGKIGFQATNLHDAVTIINEMRNWRDPNPPEEKSDRATIFLGYTSNLISSGVREVLRYLVQHKCVDVIVTTAGGVEEDIIKCLGPTYVGDFHLDGKNLRAKGLNRIGNLIVPNDNYCRFEEWIFPILNKMVEEQETLGTHWTPSSFIRRLGKEINDESSVLYWAYKNNIPIYSPALTDGSIGDMLYFHTYKATPRPLVLDIVADIRNMNTHAVRANKSGIIILGGGVVKHHICNANLMRNGAEWSVYINSANEFDGSDAGARPDEAVSW... | Function: Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue.
Catalytic Activity: [eIF5A protein]-L-lysine +... |
Q9HL74 | MDRKELLSRPVRDLSITADTRLGDLMDQFSSIGGFTAAKIHEAYEIIKDMFSEDNTTFLSFPADIISTGLRGLINEVVKRKLVDVIITTSGTLDHDIARTYRNYYCGSFSYSDIELRDLGINRLGNVLVPDESYGEIIEEKVMESLEKLYAKKKEWATVDLIHEVGLDINSESSIIYNAAKNNIPVFVPGITDGSFGSQLWSFYEQHHDFKINLLEDEHRLSDIIFDAKKTGAIMIGGGISKHHTIWWNQFRDGLDYAVYVTTAQEYDGSLSGAKLEEAISWKKVRPDARYVNVYGDATVIMPVLLAPFL | Function: Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue.
Catalytic Activity: [eIF5A protein]-L-lysine +... |
Q97BN6 | MDRKELLSKPVQDLRIDGNTTLSNLMAQFSNIGGFTAAKLYEAHSIISDMFLEDNTTFLSFPADIISTGLRGLINDVVKRKLVDVIITTSGTLDHDIARTFGKYYCGSFNYSDVELREININRLGNVLVPDESYGELIEEKVMEQLEKLYSIKKEWATVDLIKEIGLSINNESSILYNAAKNDIPIFVPGITDGSFGSQLWSFYEQHHDFKINLLEDEHRLSDIIFDAKKTGAIMVGGGISKHHTIWWNQFRDGLDYAVYITTAQEYDGSLSGAKLEEAISWKKVRPNARFVNIYGDATVIMPILMAPFL | Function: Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue.
Catalytic Activity: [eIF5A protein]-L-lysine +... |
P38791 | MSDINEKLPELLQDAVLKASVPIPDDFVKVQGIDYSKPEATNMRATDLIEAMKTMGFQASSVGTACEIIDSMRSWRGKHIDELDDHEKKGCFDEEGYQKTTIFMGYTSNLISSGVRETLRYLVQHKMVDAVVTSAGGVEEDLIKCLAPTYLGEFALKGKSLRDQGMNRIGNLLVPNDNYCKFEEWIVPILDKMLEEQDEYVKKHGADCLEANQDVDSPIWTPSKMIDRFGKEINDESSVLYWAHKNKIPIFCPSLTDGSIGDMLFFHTFKASPKQLRVDIVGDIRKINSMSMAAYRAGMIILGGGLIKHHIANACLMRNG... | Function: Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue.
Catalytic Activity: [eIF5A protein]-L-lysine +... |
Q39083 | MDADSKRFLATLRSRSEMLMGFEEIDGDDDFQEEFACPFCAESYDIIGLCCHIDDEHTLESKNAVCPVCSLKVGVDIVAHITLHHGSLFKLQRKRKSRKSGTNSTLSLLRKELREGDLQRLLGFTSRNGSVASSVTPDPLLSSFISPTRSQSSPAPRQTKNVSEDKQIERKRQVFISPVSLKDREERRHKSEFVQRLLSSAIFDEV | PTM: Phosphorylated within the NLS/NES region.
Sequence Mass (Da): 23275
Sequence Length: 206
Domain: The NLS/NES region (98-121) is necessary and sufficient for interaction with CPK11.
Subcellular Location: Nucleus
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Q01460 | MALSDLLELTLLLLLPLLERLSAEDCPCSEASLCRPIRHHRDFEVFVFDVGQKTWKSYDWSQITTVAVFGKYDSELMCYAHSKGARVVLKGDVALKDIINPTFRASWIAQKVALAKAQHMDGINIDIEQEVDCSSPEYEALTALVRETTEGFHREIEGSQVTFDVAWSPKGIDKRCYNYTGIADACDFLFVMSYDEQSQIWSECIAAANAPYNQTLTGYGDYLRMGISPRKLVMGIPWYGYDYICLNLSKDDVCAIAKVPFRGAPCSDAAGHQVPYRVIMKQVNSSVSGSQWNQDQQAPYYNYKDPTGRLHQVWYDNPRS... | Function: Involved in the degradation of asparagine-linked glycoproteins. Hydrolyze of N-acetyl-beta-D-glucosamine (1-4)N-acetylglucosamine chitobiose core from the reducing end of the bond, it requires prior cleavage by glycosylasparaginase.
Sequence Mass (Da): 41531
Sequence Length: 367
Subcellular Location: Lysosome... |
Q2FWX9 | MNIIEQKFYDSKAFFNTQQTKDISFRKEQLKKLSKAIKSYESDILEALYTDLGKNKVEAYATEIGITLKSIKIARKELKNWTKTKNVDTPLYLFPTKSYIKKEPYGTVLIIAPFNYPFQLVFEPLIGAIAAGNTAIIKPSELTPNVARVIKRLINETFDANYIEVIEGGIEETQTLIHLPFDYVFFTGSENVGKIVYQAASENLVPVTLEMGGKSPVIVDETANIKVASERICFGKFTNAGQTCVAPDYILVHESVKDDLITALSKTLREFYGQNIQQSPDYGRIVNLKHYHRLTSLLNSAQMNIVFGGHSDEDERYIEP... | Function: Involved in the biosynthesis of the yellow-orange carotenoid staphyloxanthin, which plays a role in the virulence via its protective function against oxidative stress. Catalyzes the oxidation of 4,4'-diaponeurosporen-4-al to yield 4,4'-diaponeurosporenoic acid.
Catalytic Activity: 4,4'-diaponeurosporenal + H2... |
Q24306 | MASVVADLPSYGPIAFDQVDNNTNATQLFKNNINKTRMNDLNREETRLKTFTDWPLDWLDKRQLAQTGMYFTHAGDKVKCFFCGVEIGCWEQEDQPVPEHQRWSPNCPLLRRRTTNNVPINAEALDRILPPISYDICGANDSTLEMREHAYAEGVIPMSQLIQSIGMNAVNAAGSVTGTAAPQPRVTVATHASTATQATGDVQPETCRPSAASGNYFPQYPEYAIETARLRTFEAWPRNLKQKPHQLAEAGFFYTGVGDRVRCFSCGGGLMDWNDNDEPWEQHALWLSQCRFVKLMKGQLYIDTVAAKPVLAEEKEESSS... | Function: Anti-apoptotic protein which functions as a caspase regulator, using its E3 ubiquitin-protein ligase activity to smother caspase activity. Binds, ubiquitinates and inactivates initiator caspase Dronc, and effector caspases Drice and Dcp-1. Acts as a Nedd8-E3 ubiquitin-protein ligase for Drice. Suppresses apop... |
Q24307 | MTELGMELESVRLATFGEWPLNAPVSAEDLVANGFFATGNWLEAECHFCHVRIDRWEYGDQVAERHRRSSPICSMVLAPNHCGNVPRSQESDNEGNSVVDSPESCSCPDLLLEANRLVTFKDWPNPNITPQALAKAGFYYLNRLDHVKCVWCNGVIAKWEKNDNAFEEHKRFFPQCPRVQMGPLIEFATGKNLDELGIQPTTLPLRPKYACVDARLRTFTDWPISNIQPASALAQAGLYYQKIGDQVRCFHCNIGLRSWQKEDEPWFEHAKWSPKCQFVLLAKGPAYVSEVLATTAANASSQPATAPAPTLQADVLMDEA... | Function: Required for activation of NF-kappaB transcription factors in the immune deficiency (Imd) signaling cascade which is essential for innate immune responses upon infection by Gram-negative bacteria . Promotes cytoplasmic cleavage of Rel and its translocation to the nucleus where it drives expression of antimicr... |
F8DNI1 | MLDDRSAIEHHKYSQRLTELERRSAAAQQRQQKKKPPKMHVGNKIRGIKIKRYVSNGERVLKLVVLFSAILLFMLYIISPLSKITTLHVTGNHDLTKEQVEKNANIYPGRFIWGVYLARHQLTKQAIRKNPQIKDLRIKVTGPQSLQISVKENALLGIAVMNNDTYAVLADGQLQRTKNADNGIAYKRFDGHKKVLATTAAQLGKLKLAIRNGISSVSYQPTKEYPDRVIIYMRDGNTVYGDLNTIGDKMGYYPAIAASMKNKGIIDLQVGAYSYDYGSKDK | Function: Cell division protein that may be involved in stabilizing or promoting the assembly of the division complex.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 31819
Sequence Length: 282
Subcellular Location: Cell membrane
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Q8Y5M3 | MAENKRVISIENRIPELKKYRKKKLVRHLAILIGIFVILIAITLYFLSPLSKLDKIAVSGNKQLTENEVRKESGLEIGEFVIGISNGKTEDALKKNTLIKDATVSKEGLNDVQINITEFKTIGYQQQDGKYYDVLESGIMLTDQPRQFPIGNDLLFQNFKNGKTLEKMVDQINKLPKDVVSSISEVIYSPTKSDKNHIKLYMNDGNQVSADISTFAEKMQHYPAIVAQLAKGQKGVIDIEVGSYFQSYYQQNAEKKATEEAAKEKKETNE | Function: Cell division protein that may be involved in stabilizing or promoting the assembly of the division complex.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 30497
Sequence Length: 270
Subcellular Location: Cell membrane
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B9EB52 | MMEDKIIHTPRFDEQRRMRRKKRQRLQLFIFLSIVAIVSLILIYMFTSISYVKKISVNDTSINSTKTIKEKSGIQSNMRIYSLDTKQIVSNIEYLDGVKSVTVRRHFPNTVSINVEEYDVLGVVKDGEHYHPALENGQILHKHNYAEPSEVPLINNFSSKALNQLVKVLRASDTAIINQISEINFIPKVEASHRVQFYMKNGLEVIGDMRTIDNKLNYFPAMASKLKKDSNGRILKPGIIDLEIGAVFIPYESKQAEERRIELEAAMEERSEKDKAELEKSVEKLKKELNQVKKNS | Function: Cell division protein that may be involved in stabilizing or promoting the assembly of the division complex.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 34112
Sequence Length: 296
Subcellular Location: Cell membrane
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Q04ET1 | MRLSSHGKKTVSTSNNPVFNRIGLFFTAAILFALFLQMLFFLRPWQDIKETKVYTFQMDYRQVLKKVDLKVGDPYWRWAGQGQTINRRIKNDSMIRSLSLRLSKNGTAIIRVNENLTAGFVQIKQKWYRMDQNAHLSSKSIQPDGKTPVYTDFKNGSKILKKTITAYLSMDKVMRLAVAQIIYSPVKSSPNRLALVMNDGNLVYANPSSLAKRMDLYPKMVATMEEKGIKNGVIDLQYGGYARKFENSDDNLLSSLSSDKSKSSSKSSNSSK | Function: Cell division protein that may be involved in stabilizing or promoting the assembly of the division complex.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 30881
Sequence Length: 272
Subcellular Location: Cell membrane
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E0RGM4 | MPNAQIPVLKKNRTKKRTSRKIAILLILLFIVLLAVLFFRSSLSRVSEIRFDGNVFSTRDQLLNRSGLAVGDQYFGVSSSDISEKLREIQSIQQVTVDKQFPGIIAIHIKEFATVAYELQSDGSLRAILANGTSVSVGSSGIAVEKPILTKWRSDDPYKAKLCDALSRIPGEWTADISEIIPAPIPSFPDRIKMYTRSQFEVITTVSLLNSKISYLNQVLETEDPGLITMLEADSYVPFKPDTSEEGQEKDTTQ | Function: Cell division protein that may be involved in stabilizing or promoting the assembly of the division complex.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 28271
Sequence Length: 254
Subcellular Location: Cell membrane
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Q03EY3 | MKKKKDEELTPWAKYQKEHNANSRSRFKRKRKATSKNPREPQASFRRNNRNKVKKSNKKGTKRIVKEQRLSRQKLGILIGSTLIVIALFFGYFYSSISRVQKFSVSGNKRVSTAKILKNVSIKKNDVILTSIFKEGKFENNLLKKNTDIKDATVSISWSGKVKIKVKENAVMGYVIRNKTYYTVKQDGSVVRKSVSQPSSDYPIFRNFQENSTLKKFLKEYAQMPNSVQNDVAEVDFSPTKNVKDRLHFFMNDGNQVYAIMSTFAKKMKYYPEISASMKERGMVDLQVGAFSRPSGWTDEAKAASESSKSAESSSKAKKQ... | Function: Cell division protein that may be involved in stabilizing or promoting the assembly of the division complex.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 41836
Sequence Length: 370
Subcellular Location: Cell membrane
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F2F702 | MEKVIDITERVPAMKKRRRRRTNFKFLALVTIFLFIIIILLYFQLPYSDIKKIDIKGAALKEDTYYIDQSNLKINDSLWGFKISEVEQAIAQHEWVKSVTVERKFLNEVQITVEEWQKVAYISQDGEFYPMLDNGIVFEESNEIVPIDAPIFRDFENEALRKKLLKELANLKPEVLSLISQINANPTEADPYSITLFMNDGYEVRADANTLAEKLNYYPSIIAQIESEDVSEKGIVDIEVGSYYRPFSDEYTLIKENTEKTEEPAEETENADTEEGGQLEEQNEEEPE | Function: Cell division protein that may be involved in stabilizing or promoting the assembly of the division complex.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 33418
Sequence Length: 288
Subcellular Location: Cell membrane
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Q2FZ91 | MDDKTKNDQQESNEDKDELELFTRNTSKKRRQRKRSKATHFSNQNKDDTSQQADFDEEIYLINKDFKKEESNDKNNDSASSHANDNNIDDSTDSNIENEDYRYNQEIDDQNESNVISVDNEQPQSAPKEQNSDSIDEETVTKKERKSKVTQLKPLTLEEKRKLRRKRQKRIQYSVITILVLLIAVILIYMFSPLSKIAHVNINGNNHVSTSKINKVLGVKNDSRMYTFSKKNAINDLEENPLIKSVEIHKQLPNTLNVDITENEIIALVKYKGKYLPLLENGKLLKGSNDVKINDAPVMDGFKGTKEDDMIKALSEMTPE... | Function: Cell division protein that may be involved in stabilizing or promoting the assembly of the division complex.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 50212
Sequence Length: 439
Subcellular Location: Cell membrane
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E8SFP1 | MTKEIPKINNEYLKEKRKKQRIQQRRVQRMIVGILVVIVLLILVYMFTPISHIKSADIKGNHYVSKQDILKELDIQNHPRIYAYSSDDAETRLKQNELIDEVTIEKGLFNPIEVNVKEHTIIAITTEKSRVVPMIENGKVLKDYKQEVPNEAPYIEGFKGAEKRNLIDALQKMDRTTRAQISEIVSAPQKDQPHLIKLFMRDGIEVVGNTNTIAEKLKYYPSMSQALEKDETGKLKKSGFIDLSVGATFIPYDNVNNGQTSSASAKEVQSGTASEDKAKDDLQKALNKIKDEESSE | Function: Cell division protein that may be involved in stabilizing or promoting the assembly of the division complex.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 33617
Sequence Length: 296
Subcellular Location: Cell membrane
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A8AW16 | MTTKDKGDQKELQKYLSEWQKRHQEYLEKKSQEKASETDEEERNAEPLETSESAGTKETDNSEDEKEDQTQDQASDDDETNESEESEDVEEPEEENIEESSDVSEDRTEKFIGQADVGIEKEAKRDKPRIERIHLYRALPVLVISSLLILLSLYFITPLGSLKNLVVTGNERVTQDEIIKATQIDSRDYTLTTFLNRNQYANNLKKANSWIEKAEISYQFPITFKIQVTEYKILAYEASTGNIYPVISNGTVINQPVKKEALPENYMRLNLSDKAKVKKLVQELSDVPDSIKNEIQTVDLTPSKATKDLLTLTMRDEHKI... | Function: Cell division protein that may be involved in stabilizing or promoting the assembly of the division complex.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 45335
Sequence Length: 397
Subcellular Location: Cell membrane
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D5AGC8 | MTEKDSNVEESVLEVEQASQVELDSEQISPAEKESVLAEEKEFSTDVDIPEMTAPDDEKSAFFEQWKARHQAYLAHKDEADIQAVDEGQTEQEIPEAKKSKRVLFQGIERKTESLKSKKETGEKVQTLKVDIPSKVVWKAIPVLVTSLLLAALALYFISPTSKKKQIEVVGNERLTAEQVENYSLISPDDYNVTIALHADAYAKNIKKNSSSVETATIKFQFPATFTIHIKEYAIIGYIQQQSQWYPVLSSGEIGGEPISQDSLPEDYTTINLSDKELIKELAIELGKIDAGIRSAIQTINLPPSKVTADLLTFNMRDGN... | Function: Cell division protein that may be involved in stabilizing or promoting the assembly of the division complex.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 40128
Sequence Length: 360
Subcellular Location: Cell membrane
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Q1JG12 | MAKDKEKQSDDKLVLTEWQKRNIEFLKKKKQQAEEEKKLKEKLLSDKKAQQQAQNASEAVELKTDEKTDSQEIESETTSKPKKTKKVRQPKEKSATQIAFQKSLPVLLGALLLMAVSIFMITPYSKKKEFSVRGNHQTNLDELIKASKVKASDYWLTLLISPGQYERPILRTIPWVKSVHLSYHFPNHFLFNVIEFEIIAYAQVENGFQPILENGKRVDKVRASELPKSFLILNLKDEKAIQQLVKQLTTLPKKLVKNIKSVSLANSKTTADLLLIEMHDGNVVRVPQSQLTLKLPYYQKLKKNLENDSIVDMEVGIYTT... | Function: Cell division protein that may be involved in stabilizing or promoting the assembly of the division complex.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 43477
Sequence Length: 382
Subcellular Location: Cell membrane
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Q8DQM0 | MSKDKKNEDKETLEELKELSEWQKRNQEYLKKKAEEEVALAEEKEKERQARMGEESEKSEDKQDQESETDQEDSESAKEESEEKVASSEADKEKEEPESKEKEEQDKKLAKKATKEKPAKAKIPGIHILRAFTILFPSLLLLIVSAYLLSPYATMKDIRVEGTVQTTADDIRQASGIQDSDYTINLLLDKAKYEKQIKSNYWVESAQLVYQFPTKFTIKVKEYDIVAYYISGENHYPILSSGQLETSSVSLNSLPETYLSVLFNDSEQIKVFVSELAQISPELKAAIQKVELAPSKVTSDLIRLTMNDSDEVLVPLSEMS... | Function: Cell division protein that may be involved in stabilizing or promoting the assembly of the division complex.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 45400
Sequence Length: 396
Subcellular Location: Cell membrane
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F8HZP7 | MNEKNKNDESKHQEDKLQDQKMWNRINKFFSRSIGQSAKRAPKPKAISKSQSFRILNRFNAMERNSIHMIVILSIISLLLILLLSPLMRFQKVEITGNHDLTKAEVLAASGINKKIPAWQLLSEQHYFIQRAEKNSQIKKVKISYLNMQVAQIKIEENSKVGLVTKKDKNYYILADGKFIPAQSVGEKPQRLPNYEKFPNDKTIKRVAMQFNGISKALQNSVSEVIWSPDHEDDEKVILIMDDGNKVLIKASDIKNKLKYYPGMVAQIDKNGTFNFQVGTYFQQY | Function: Cell division protein that may be involved in stabilizing or promoting the assembly of the division complex.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 32878
Sequence Length: 285
Subcellular Location: Cell membrane
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Q03228 | MILPTALKSRLALEFETLPDPFRRPAARAAGLDPAHAWRLGWLAAVCLAAAAALFTADSGGWPVWAALGAGALPALVSLIFTREDERTQSWLLVLWAVGGSLAAVLTGGVGGAMAAWCLAPVAAASTQDQPKRLAEGAALALIGACVAALTQLSGLAPAAPTGPLAFVLGFLALVTTGLGLAAGLLIGRRRQGARDDRYASEIIGLETLLDGLPHLAIAVRGQGQVTAVRGAAPPGVTRADLVNRGLTGAAAPGDRQRLTAAIAQAHREGSASLTFNPALGVERVVALDMHRVAPNQLVGVLRDITVERHREHALDQARI... | Function: Kinase required for the regulation of cell division and differentiation. Is part of a signal transduction pathway, activating PleD by phosphorylation.
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 62373
S... |
Q74Q30 | MRYWGKLLGLVLGVMYAPGVVGALLGLLVGHMVDRALGAKRRGFFADQQTRQSLFFRTTFQVMGHLTKAKGRVTEVDIQLASQLMDRMQLHGAARTAAQQAFREGKESHFPLRKALQEFRRVCFGRFDLIRIFLEIQLQAAFADGSLHPNERQVLYVIAEELGISRGQFDQFLRMFDGGRQFGGHGGWQGQQGGYSQSGYQRASQGPTLEDACKVLGVNSSDDSVAIKRAYRKLMGEHHPDKLVAKGLPPEMMEMAKQKAQEIQAAYDLIKREKGFK | Function: Regulatory DnaK co-chaperone. Direct interaction between DnaK and DjlA is needed for the induction of the wcaABCDE operon, involved in the synthesis of a colanic acid polysaccharide capsule, possibly through activation of the RcsB/RcsC phosphotransfer signaling pathway. The colanic acid capsule may help the b... |
O17919 | MGKKDKRSKLEGDDLAEAQQKGSFQLPSSNETAKLDASQWPLLLKNYDKLNVRTNHYTPHVEGVSPLKRDIKNYISSGFFNLDKPSNPSSHEVVSWIKRILRCEKTGHSGTLDPKVSGCLIVCIDRTTRLAKSQQGAGKEYICIFKLHEEVEDDRKVKQALEKLTGALFQRPPLISAVKRQLRIRTVYENKFIEYDPAQQMGIFNCICESGTYVRTICVHLGLILGCGGQMQELRRNRSGICDENENMVTMHDVLDAQYLLDTQKDESYMRHIVRPLEALLTQHKRVVVKDSCINAICYGAKILIPGILRYDDDIEVGKE... | Function: Plays a central role in ribosomal RNA processing. Probable catalytic subunit of H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. P... |
Q5ZJH9 | MADGDGSSVKKRRKKDKRSLPDEDVADIQHTEEFLIKPESRVAQLDTSQWPLLLKNFDKLNVLTTHYTPLPSGANPLKREISDYVRSGFINLDKPSNPSSHEVVAWIRRILRVEKTGHSGTLDPKVTGCLIVCIERATRLVKSQQSAGKEYVGIVRLHNAIESEAQLARAIETLTGALFQRPPLIAAVKRQLRVRTIYESKLVEYDPERRLGIFWVSCEAGTYIRTLCVHLGLLLGVGGQMQELRRVRSGILGEMDNMVTMHDVLDAQWQYDNNKDDSYLRRVILPLEKLLTSHKRLVMKDSAVNAICYGAKIMLPGVLR... | Function: Catalytic subunit of H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Each rRNA can contain up to 100 pseudouridine ('psi') residu... |
O60832 | MADAEVIILPKKHKKKKERKSLPEEDVAEIQHAEEFLIKPESKVAKLDTSQWPLLLKNFDKLNVRTTHYTPLACGSNPLKREIGDYIRTGFINLDKPSNPSSHEVVAWIRRILRVEKTGHSGTLDPKVTGCLIVCIERATRLVKSQQSAGKEYVGIVRLHNAIEGGTQLSRALETLTGALFQRPPLIAAVKRQLRVRTIYESKMIEYDPERRLGIFWVSCEAGTYIRTLCVHLGLLLGVGGQMQELRRVRSGVMSEKDHMVTMHDVLDAQWLYDNHKDESYLRRVVYPLEKLLTSHKRLVMKDSAVNAICYGAKIMLPGV... | Function: Catalytic subunit of H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA . This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1 . Each rRNA can contain up to 100 pseudouridine ('psi') resi... |
Q9ESX5 | MADAEVITFPKKHKKKKDRKPLQEDDVAEIQHAEEFLIKPESKVAQLDTSQWPLLLKNFDKLNVRTAHYTPLPCGSNPLKREIGDYIRTGFINLDKPSNPSSHEVVAWIRRILRVEKTGHSGTLDPKVTGCLIVCIERATRLVKSQQSAGKEYVGIVRLHNAIEGGTQLSRALETLTGALFQRPPLIAAVKRQLRVRTIYESKMIEYDPERRLGIFWVSCEAGTYIRTLCVHLGLLLGVGGQMQELRRVRSGVMSEKDHMVTMHDVLDAQWLYDNHKDESYLRRVVYPLEKLLTSHKRLVMKDSAVNAICYGAKIMLPGL... | Function: Catalytic subunit of H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA . This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Each rRNA can contain up to 100 pseudouridine ('psi') resid... |
P40615 | MADAEAAMTFPKKHKKKKERKPLPEADVAEIQHAEDFLIKPESKAAQLDTSQWPLLLKNFDRLNVRTTHYTPIPCGSNPLKREIGEYVRTGFINLDKPSNPSSHEVVAWIRRILRVEKTGHSGTLDPKVTGCLIVCIERATRLVKSQQSAGKEYVGVVRLHNAIEGTAQLSRALETLTGALFQRPPLIAAVKRQLRVRTIYESRVVEYDPERRLGVFWVSCEAGTYIRTLCVHLGLLLGVGGQMQELRRVRSGVVGERDHMVTMHDVLDAQYLYDHHRDESYLRRVVFPLEKLLTSHKRLVMKDSAVNAICYGAKIMLPG... | Function: Catalytic subunit of H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA . This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1 (By similarity). Each rRNA can contain up to 100 pseudouridi... |
Q8GNT2 | MDYCNKKHTAEEYVKISDNNYVPFPEAFSDGGITWQLLHSSPETSSWTAIFNCPAGSSFASHIHAGPGEYFLTKGKMEVRGGEQEGGSTAYAPSYGFESSGALHGKTFFPVESQFYMTFLGPLNFIDDNGKVIASIGWAEAQGAWLATKNEAA | Cofactor: Binds 1 Fe cation per subunit.
Function: Cleaves acetylacetone to equimolar amounts of methylglyoxal and acetate, consuming one equivalent of molecular oxygen.
Catalytic Activity: acetylacetone + O2 = acetate + H(+) + methylglyoxal
Sequence Mass (Da): 16607
Sequence Length: 153
Pathway: Xenobiotic degradation... |
P97838 | MRGYHGDRGSHPRPARFADQQHMDVGPAARAPYLLGSREAFSTEPRFCAPRAGLGHLSPEGPLSLSEGPSSVGPEGGPGGVGAGGSSSTFPRMYPGQGPFDTCEDCVGHPQGKGATRLLPTFLDQFEKQLPVQQDGFHTLPYQRGPAGPGPGPGSGAAPEARSESPSRIRHLVHSVQKLFAKSHSLEAPGKRDYNGPKAEGRSSSGGDSYSGPGSGGPPTSHHHHHHHHHHHHQSRHGKRSKSKDRKGDGRHQTKATGWWSSDDNLDSDSGFLGGRPPGEPGGPFCLDAPDGSYRDLSFKGRSGGSEGRCLACTGMSMSL... | Function: May play a role in the molecular organization of synapses and neuronal cell signaling. Could be an adapter protein linking ion channel to the subsynaptic cytoskeleton. May induce enrichment of PSD-95/SAP90 at the plasma membrane.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 105990
Sequen... |
Q9Y2H0 | MKGLGDSRPRHLSDSLDPPHEPLFAGTDRNPYLLSPTEAFAREARFPGQNTLPGDGLFPLNNQLPPPSSTFPRIHYNSHFEVPEESPFPSHAQATKINRLPANLLDQFEKQLPIHRDGFSTLQFPRGEAKARGESPGRIRHLVHSVQRLFFTKAPSLEGTAGKVGGNGSKKGGMEDGKGRRAKSKERAKAGEPKRRSRSNISGWWSSDDNLDGEAGAFRSSGPASGLMTLGRQAERSQPRYFMHAYNTISGHMLKTTKNNTTELTAPPPPPAPPATCPSLGVGTDTNYVKRGSWSTLTLSHAHEVCQKTSATLDKSLLKS... | Function: May play a role in the molecular organization of synapses and neuronal cell signaling. Could be an adapter protein linking ion channel to the subsynaptic cytoskeleton. May induce enrichment of PSD-95/SAP90 at the plasma membrane.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 108012
Sequen... |
Q15398 | MSSSHFASRHRKDISTEMIRTKIAHRKSLSQKENRHKEYERNRHFGLKDVNIPTLEGRILVELDETSQGLVPEKTNVKPRAMKTILGDQRKQMLQKYKEEKQLQKLKEQREKAKRGIFKVGRYRPDMPCFLLSNQNAVKAEPKKAIPSSVRITRSKAKDQMEQTKIDNESDVRAIRPGPRQTSEKKVSDKEKKVVQPVMPTSLRMTRSATQAAKQVPRTVSSTTARKPVTRAANENEPEGKVPSKGRPAKNVETKPDKGISCKVDSEENTLNSQTNATSGMNPDGVLSKMENLPEINTAKIKGKNSFAPKDFMFQPLDGL... | Function: Potential cell cycle regulator that may play a role in carcinogenesis of cancer cells. Mitotic phosphoprotein regulated by the ubiquitin-proteasome pathway. Key regulator of adherens junction integrity and differentiation that may be involved in CDH1-mediated adhesion and signaling in epithelial cells.
PTM: U... |
W7MAD3 | MADINDPVLAKPADLCCLKGDFHRGEPTGSIIQIEGVDTYVAKPDPKFTNGNVLLFFPDAFGLHINSKLMMDAYAACGYLTLGVDYFLGDAVTKYSASPLNDPNFDLAAWSAKHLLPSEEIAREWVKNIKAKYGNDGKVKFGCIGYCWGARIVLQQLSDGGICSAGAIAHPSFVNESHVQKSKAPVAFSVPATDKLFSNEARTRVIEICTEKQQRFNMQVFSHVGHGFASRTRLTDPYELWAKEQHFKGFIEWLDFWLARE | Function: Dienlactone hydrolase; part of the Fusarium detoxification of benzoxazolinone cluster 1 (FDB1) involved in the degradation of benzoxazolinones produced by the host plant . Maize, wheat, and rye produce the 2 benzoxazinone phytoanticipins 2,4-dihy-droxy-7-methoxy-1,4-benzoxazin-3-one (DIMBOA) and 2,4-dihydroxy... |
P39580 | MTPYSSFLFFILLGILLLPTIILGLNGKRFQAYNMFISIIILALIFSHDLHGVIALCLFTIWQVLLISGYLAYRQKANSGFVFCGAVIASILPLFLSKIWPFLSHPQPHHPPHNLISFLGISYLTFKGVQLIMEARDGLLKEQLPLHRLLYFILFFPTISSGPIDRYRRFVKDEQKAWTKEEYADLLYTGIHKIFIGFLYKFIIGYAINTYFIMNLPAITHNKILGNLLYMYGYSMYLFFDFAGYTMFAVGVSYIMGIKSPENFNKPFISKNIKDFWNRWHMSLSFWFRDYVFMRFVFWMTKKKWIKNRMAVSNIGYFLL... | Function: O-acyltransferase that catalyzes D-alanylation of both teichoic acid and lipoteichoic acid (LTA) . D-alanylation of LTA plays an important role in modulating the properties of the cell wall in Gram-positive bacteria, influencing the net charge of the cell wall . Catalyzes D-alanylation from DltC carrier prote... |
P35855 | MLNLQPYENPQYFVYLIIALLPVIIGMFKGFRMHWYESIFSLVFLVLIFDADKWPQGKALLGYVVFNLLLVYAYFKYRTREGSKNSTAVFYLSVALGIAHVAVVKFTPLFQHHGSILGFLGISYLTFRVVGTIMEIRDGSIKDLNMWKFIQFLLFFPTISSGPIDRYRRFVKDYDRVPDPEHYAQLVTKAIHYLMLGFLYKFILGYIFGTLWLPSVEHMAMASRGGAFLGLSWPVVGVMYAYSGYLFFDFAGYSLFAVAISYLMGIETPMNFNKPWSHITSRLLNRWQLSLSFWFRDYIYMRFVFFMMKHKWIKSRVWTA... | Function: O-acyltransferase that catalyzes D-alanylation of both teichoic acid and lipoteichoic acid (LTA). D-alanylation of LTA plays an important role in modulating the properties of the cell wall in Gram-positive bacteria, influencing the net charge of the cell wall. Catalyzes D-alanylation from DltC carrier protein... |
Q5M4V4 | MIDFLKQLPHLEPYGNPFYFIYLGIALLPIFIGLFFKKRFAIYECLVSITFIVLALTGTHASQILALLFYIVWQIIWVYSYKRYRSQRDNKWVFYLHSFLVVLPLILVKVEPTINGTQSLLNFLGISYLTFRAVGMIIEMRDGVLKEFTLGEFLRFMLFMPTFTSGPIDRFKRFNEDYQSIPNRDELLNMLEQAVKYIMLGFLYKFVLAQIFGSMLLPPLKAQALSQGGIFNLPTLGVMYVYGFDLFFDFAGYSMFALAVSNLMGIKSPINFDKPFISRDMKEFWNRWHMSLSFWFRDFVFMRLVIVLMRNKVFKNRNTT... | Function: O-acyltransferase that catalyzes D-alanylation of both teichoic acid and lipoteichoic acid (LTA) . D-alanylation of LTA plays an important role in modulating the properties of the cell wall in Gram-positive bacteria, influencing the net charge of the cell wall . Catalyzes D-alanylation from DltC carrier prote... |
Q88VM8 | MTMDDTKATVLSILADLTGEDVSSNMDVNLFDEGILDSMGSVQLLLELQNQLGIEVPVSEFQRSEWDTPAKIVAKVENLQ | Function: Carrier protein involved in the D-alanylation of lipoteichoic acid (LTA). The loading of thioester-linked D-alanine onto DltC is catalyzed by D-alanine--D-alanyl carrier protein ligase DltA. The DltC-carried D-alanyl group is further transferred to cell membrane phosphatidylglycerol (PG) by forming an ester b... |
Q8GR69 | MEEQVLSLLEELCEDEVVREDLDINLRDEGLLDSLGFVEMLVRMEEVFGFATAPTEVTYEEIDTPRRVMAYVKKRVAAL | Function: Carrier protein involved in the D-alanylation of lipoteichoic acid (LTA). The loading of thioester-linked D-alanine onto DltC is catalyzed by D-alanine--D-alanyl carrier protein ligase DltA. The DltC-carried D-alanyl group is further transferred to cell membrane phosphatidylglycerol (PG) by forming an ester b... |
B4F9A4 | MSATGRAPCGLPRIGLGTAVQGPRPDPVRAAVLRAIQLGYRHFDTAAHYATEAPIGEAAAEAVRTGLVASREDLFVTSKVWCADAHRDRVLPALRRTLSNLQMEYVDLYMVHWPVTMKAGRFTAPFTPEDFEPFDMRAVWEAMEECHRLGLAKAIGVCNFSCKKLETLLSFATIPPVVNQVEINPVWQQRKLREFCRAKGIQLCAYSPLGAKGTHWGSDSVMDSGVLHEIAKSKGKTVAQVCLRWVYEQGDCLIVKSFDEGRMKENLDIVDWELSEEERQRISKIPQRKINQGRRYVSEHGPYKSFEELWDGEI | Function: Catalyzes the reduction of a 3''-keto intermediate during the biosynthesis of 2'-deoxymugineic acid (DMA) from L-Met. Involved in the formation of phytosiderophores (MAs) belonging to the mugineic acid family and required to acquire iron.
Catalytic Activity: 2'-deoxymugineate + NAD(+) = 3''-deamino-3''-oxonic... |
Q10PE7 | MSDGGAGAKGAGFGMPRVGMGTAVQGPRPEPIRRAVLKAIEAGYRHFDTAAHYETEAPIGEAAAEAVRSGAIASRADLFITSKLWCSDAHRDRVLPALRQTLWNLQMEYVDLYLVHWPVSMKPGRYKAPFTADDFVPFDMRAVWEAMEECHRLGLAKAIGVCNFSCKKLDTLLSFATIPPAVNQVEVNPVWQQRKLRELCREKGVQICAYSPLGASGTHWGSDSVMASAVLRDIAQSKGKTVAQVCLRWVYEQGDCLIVKSFDEARMRENLDIVGWELTEEERQRIAGIPQRKINRALRFVSDHGPYKSLDDLWDGEI | Function: Catalyzes the reduction of a 3''-keto intermediate during the biosynthesis of 2'-deoxymugineic acid (DMA) from L-Met. Involved in the formation of phytosiderophores (MAs) belonging to the mugineic acid family and required to acquire iron.
Catalytic Activity: 2'-deoxymugineate + NAD(+) = 3''-deamino-3''-oxonic... |
D4AK48 | MGSIEIPNCSGSIVYKTISDFIDFPNHEQKLWWHSTAPMFAEMLRVAGYDLHSQYKILGIFLNHVIPFLGVYPTRINNRWLSILTRYGTPFELSLNCSQSLVRYTYEPINSATGTVKDPFNTHSIWDALDRLMPLQKGIDLEFFKHLKQDLTVDDQDSAYLLENNLVGGQIRTQNKLALDLKGGNFVLKTYIYPALKALATGKSIKTLMFDSVYRLCRQNPSLEAPLRALEEYVDSKGPNSTASPRLLSCDLIDPSKSRVKIYILELNVTLEAMEDLWTMGGRLNDASTLAGLEMLRELWDLIKLPPGMREYPEPFLQLG... | Function: Tryptophan dimethylallyltransferase; part of the gene cluster that mediates the biosynthesis of fungal ergot alkaloid . DmaW catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan . The second step is catalyzed... |
Q50EL0 | MKAANASSAEAYRVLSRAFRFDNEDQKLWWHSTAPMFAKMLETANYTTPCQYQYLITYKECVIPSLGCYPTNSAPRWLSILTRYGTPFELSLNCSNSIVRYTFEPINQHTGTDKDPFNTHAIWESLQHLLPLEKSIDLEWFRHFKHDLTLNSEESAFLAHNDRLVGGTIRTQNKLALDLKDGRFALKTYIYPALKAVVTGKTIHELVFGSVRRLAVREPRILPPLNMLEEYIRSRGSKSTASPRLVSCDLTSPAKSRIKIYLLEQMVSLEAMEDLWTLGGRRRDASTLEGLSLVRELWDLIQLSPGLKSYPAPYLPLGVI... | Function: Tryptophan dimethylallyltransferase; part of the gene cluster that mediates the biosynthesis of fumiclavanine C, a fungal ergot alkaloid . DmaW catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan . The secon... |
Q12594 | MMTKAPATAVYDTLSLLFDFPNQEQRLWWHSIAPMFAAMLDTAGHNVHDQYRHLGIFKKHIIPFLGVYPAQGKHTWPSVLTRYGIPFELSLNCLDSVVRYTFEPTTEHTGTGDDSYNAFAILECIQKLVRIQPGIDMEWFSYFRNELVLNATESARLGRNDSVNQQPIRTQNKLALDLKGDRFALKVYLYPHLKSIATGVSSHDLIFNSVRKLSQKHTSIQPSFNVLCDYVASRNDPDSNAAEAEAGVPASALRARLLSCDLVDPSKSRIKIYLLEQTVSLTAMEDLWTLGGRRTDSSTLNGLDMMRELWHLLQIPSGFM... | Function: Tryptophan dimethylallyltransferase; part of the gene cluster that mediates the biosynthesis of fungal ergot alkaloid . DmaW catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan . The second step is catalyzed... |
P04392 | MLGAIAYTGNKQSLLPELKSHFPKYNRFVDLFCGGLSVSLNVNGPVLANDIQEPIIEMYKRLINVSWDDVLKVIKQYKLSKTSKEEFLKLREDYNKTRDPLLLYVLHFHGFSNMIRINDKGNFTTPFGKRTINKNSEKQYNHFKQNCDKIIFSSLHFKDVKILDGDFVYVDPPYLITVADYNKFWSEDEEKDLLNLLDSLNDRGIKFGQSNVLEHHGKENTLLKEWSKKYNVKHLNKKYVFNIYHSKEKNGTDEVYIFN | Function: An alpha subtype methylase, recognizes the double-stranded sequence 5'-GATC-3' and methylates A-2. Also acts on 5-hydroxymethylcytosine (hmC)-containing DNA, the normal base in this virus . May prevent degradation of viral DNA by the host restriction-modification antiviral defense system (Probable).
Catalytic... |
P0AEE9 | MKKNRAFLKWAGGKYPLLDDIKRHLPKGECLVEPFVGAGSVFLNTDFSRYILADINSDLISLYNIVKMRTDEYVQAARELFVPETNCAEVYYQFREEFNKSQDPFRRAVLFLYLNRYGYNGLCRYNLRGEFNVPFGRYKKPYFPEAELYHFAEKAQNAFFYCESYADSMARADDASVVYCDPPYAPLSATANFTAYHTNSFTLEQQAHLAEIAEGLVERHIPVLISNHDTMLTREWYQRAKLHVVKVRRSISSNGGTRKKVDELLALYKPGVVSPAKK | Function: An alpha subtype methylase, recognizes the double-stranded sequence 5'-GATC-3' and methylates A-2 (By similarity) . May be involved in methyl-directed DNA mismatch repair, initiation of chromosome replication and gene expression (By similarity).
Catalytic Activity: a 2'-deoxyadenosine in DNA + S-adenosyl-L-me... |
Q2NEM0 | MVKDEITTTKYLIHSQINAKGFVEKPDVVGAIFGQTEGLLSDSLDLRELQKTGRIGRIKVDMTNRSGRTKGEIIIPSSLDRIETTILAASLETINRVGPCEANLRVTKIEDVRAVKRRTIVERAKELYQNMMEEFTPESSRMIDEVKESIRRPEIIEYGEDNLPAGPNTPTSDAILIVEGRSDVLNLLKYGIKNTIAVEGVNVPKTVADLTKKRTVTAFLDGDRGGDLILKELLQIGDIDYVTRAPRGLEVEYLDKDQVIYALKNKTSVDKITSHANYNHNQHRYHNKPKSHDKFESKLHEVTSSVNKTDKYSQKNESKQ... | Cofactor: Binds two Mg(2+) per subunit.
Function: RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. Also part of the exosome, which is a complex involved in RNA degradation. Acts as a poly(A)-binding protein that enhances the interaction betwee... |
P47492 | MVNKSNSLDELLKQIKITEIIQHYGVKIQTKGNSLLALCPFHDDKNPSMSISSSKNIFKCWACNAAGNGIAFIQKHDQLDWKTALKKAIEICGIKLENWNSNLLTKVDPKQKRYWEINNALITYYQTRLKRETNPNGMNYLVEKRKLNKTLIEQFQLGLAFHNEDKYLCESMERYPFINPKIKPSELYLFSKTNQQGLGFFDFNTKKATFQNQIMIPIHDFNGNPVGFSARSVDNINKLKYKNSADHEFFKKGELLFNFHRLNKNLNQLFIVEGYFDVFTLTNSKFEAVALMGLALNDVQIKAIKAHFKELQTLVLALDN... | Cofactor: Binds 1 zinc ion per monomer.
Function: RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.
Catalytic Activity: ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.
Sequence Mass (Da): 71062
Sequence Length: 607
Domain: Contain... |
Q9CCG2 | MVGRIPDRDIAAIRERVCIEEVVGDYVQLRRAGADSLKGLCPFHNEKSPSFHVRPNHGHFHCFGCSEGGDVYAFIQKIEHVSFVEAVEMLADRIGHTINYFGTATSVQRDRGSRSRLIAANAAAAAFYAAALESDEAAPARQYLMERNFDANAARHFGCGFAPSGWDSLTKYLISKGFEFTELEAAGLSRQGRRGPMDRFHRRLLWPILTLAGEVIGFGARRLFDDDPMEAKYVNTPETLLYKKSSVMFGIDLAKRDIVKGHQAVVVEGYTDVMAMHLAGVTTAVASCGTAFGDEHLAMLRRLIMDDNWYRGELIFVFDG... | Cofactor: Binds 1 zinc ion per monomer.
Function: RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.
Catalytic Activity: ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.
Sequence Mass (Da): 70761
Sequence Length: 642
Domain: Contain... |
P75426 | MTSPTSLDQLKQQIKIAPIVEHYAIKLKKKGKDFVALCPFHADQNPSMTVSVAKNIFKCFSCQVGGDGIAFIQKIDQVDWKTALNKALSILNLDSQYAVNFYLKEVDPKLKRYWDLHSALVDYYQTRLKLEPKEQGLTYLTETRKLSPQVIERFQLGLAFTLEDQYFLPSLLNYPWISPAIEKAELCFATEKFPEALGFFNQQTHYATFKSRIMIPIHDLKGNPVGFSGRALQKTEKIKYKNSAEHQWFKKSELLFNFHRIDKNTLKLYLVEGYFDVFALTSAGIGDVVGLMGLALSESHIIAFQQQLKALETVVLALDN... | Cofactor: Binds 1 zinc ion per monomer.
Function: RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.
Catalytic Activity: ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.
Sequence Mass (Da): 71537
Sequence Length: 620
Domain: Contain... |
Q98QB3 | MNNLWEIEKKILEKTTLSNLIGKLISIKPKGKSFWALCPFHDDKNASLSISDQKAMFSCFSCNVRGGLFVFYSKFLNKSYVEVANMLAKEFDLDFHFDQQEKEKYNENEQLFIDVTSIANHYFKVSLKSQVHSNSKLVDFLKSRGISRETASEFEIGYDDGNFWKIPNKEKKNFSFFLSNNLIVKKETNQYYDFFYKRVVFPIHNSFGDVVGFSGRALDENNIKYLNSPESLVFKKHKILYNWAKAKEKAIQEKKLYITEGFMDTIALYKIGIKNAIAIMGTNLSNEQLELIPKDIELIFFLDGDQAGKNAVYNILKKII... | Cofactor: Binds 1 zinc ion per monomer.
Function: RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.
Catalytic Activity: ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.
Sequence Mass (Da): 70907
Sequence Length: 602
Domain: Contain... |
O52200 | MPVAGGRIPDRDIAAIREKVRIEDVVGDYVQLRRAGADSLKGLCPFHDEKTPSFHVRPNHGHFHCFGCGEGGDVYAFIQKIEHVSFVEAVELLADKVGYTVTYTGSSTTNVQRDRGSRSRLLAANAAAAEFYAEALQSEEAAPARQYLTERNFDAAAAAKFGCGYAPSGWDKLTKHLLRKGFEFKELEAAGLSREGKRGPMDRFHRRLLWPIRVSSGETIGFGARRLFDDDPNQAKYVNTPETVLYKKSQVLFGLDLAKRDIAKGHQAVVVEGYTDVMAMHLAGVTTAVASCGTAFGEQHLSMLRRLMMDDNFFRGELIY... | Cofactor: Binds 1 zinc ion per monomer.
Function: RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.
Catalytic Activity: ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.
Sequence Mass (Da): 69816
Sequence Length: 636
Domain: Contain... |
P50070 | MGVVIPEHKIQEVLERVDLVGLISRHVDLKKAGREWKACCPFHQEKTPSFYVVPEKRFYFCHGCRASGDAVSFVQRYLGKTFLDAVRDLARELGVDLEAEQDPSMRERQQIKEATDQAAEHFRAMLWQQDEGRSARAYIASRGVSDETAMAFGLGWAPLEWASLTERFQKLGMLEWAAKAGLVLKRNSGDGYYDFFRSRVMVPIRAPEGRPIAFGGRLIGADEGPKYLNSRESRLYNKSETLFGMDQSRDEIRKRKAAVLVEGYFDALGLHQVGVRHAVALCSTNLTAGHMQVLKRAEARELILLLDGDSAGLAAVERLS... | Cofactor: Binds 1 zinc ion per monomer.
Function: RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.
Catalytic Activity: ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.
Sequence Mass (Da): 66847
Sequence Length: 606
Domain: Contain... |
Q74MB1 | MAKFAPVQYKYIIKAEFEIDGIVDREDIIGAIFGQTEGLLGMELDLRELQKQGKLGRIEVEYKRVGNKTIGTITIPTSLKAVETSLIAAAIETVDRVGPAKARFRVKEIVDVRSSKREYIRNRAKELFVQLLSKTAPDIEELRRELEEAYYSKQLIEYGEEKLPAGPLVEKSDEIILVEGRADVVNLVKHGILNVLGMNGINIPKSVVELSKRKKVTLFIDGDRGGELVLRNLLAAGADIDYVAVAPPGREVEELTNKEILKALKSKIPLEQYIKNLRISINNDENKEKYKELLSKVFDTKKAIVFDEQFNIIDEKPLEE... | Cofactor: Binds two Mg(2+) per subunit.
Function: RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. Also part of the exosome, which is a complex involved in RNA degradation. Acts as a poly(A)-binding protein that enhances the interaction betwee... |
P17631 | MSKRDYYEVLGVSKSASKDEIKKAYRKLSKKYHPDINKEAGSDEKFKEVKEAYETLSDDQKRAHYDQFGHTDPNQGFGGGGFGGGDFGGFGFDDIFSSIFGGGTRRRDPNAPRQGADLQYTMTLSFEDAAFGKETTIEIPREETCETCKGSGAKPGTNPETCSHCGGSGQLNVEQNTPFGKVVNRRVCHHCEGTGKIIKNKCADCGGKGKIKKRKKINVTIPAGVDDGQQLRLSGQGEPGINGGPAGDLFVVFHVRAHEFFERDGDDIYCEMPLTFAQAALGDEVEVPTLHGKVKLKIPAGTQTGTKFRLRGKGVQNVRG... | Cofactor: Binds 2 Zn(2+) ions per monomer.
Function: Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction... |
Q8A8C3 | MAEKRDYYEVLEVTKTATVEEIKKAYRKKAIQYHPDKNPGDKEAEEKFKEAAEAYDVLSNPDKRSRYDQFGHAGVSGAAGNGGPFGGFGGEGMSMDDIFSMFGDIFGGRGGGFSGGFGGFSGFGGGGGGSQQRRYRGSDLRVKVKMTLKEISTGVEKKFKLKKYVPCNHCHGTGAEGDGGSETCPTCKGSGSVIRNQQTILGTMQTRTTCPTCNGEGKIIKNKCKECGGDGIVYGEEVVTVKIPAGVAEGMQLSMGGKGNAGKHNGVPGDLLILVEEEPHPDLIRDENDLIYNLLLSFPTAALGGAVEIPTIDGKVKVKI... | Cofactor: Binds 2 Zn(2+) ions per monomer.
Function: Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction... |
Q8G6C6 | MADYYETLGVERGASDDEIKKAYRKLSRKYHPDIAGPEFEDKFKEVNNAYDVLSNPDKRRMYDSGVDPNNPNAGAGGFSGAGFGDMSDVFSTFFGSAFGGGSQGPVPRTQPGRDALASASIDLKTAVFGGTAHVKINTFSLCQECGGSGAQGGAQPVTCPDCHGQGFMQKVVRTMLGQMMTSAPCERCEGHGTIIQNPCPSCMGHGRVRTTRTVGVTVPAGINDNARLRLANQGEVGEGGGAAGDLYIDIRIKADKQFTRDGDDLHCWIQVPMSWAVLGHDLSIDTFDGEKTVSIPAGCQTEDTVTLKGLGVTNIRNKDE... | Cofactor: Binds 2 Zn(2+) ions per monomer.
Function: Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction... |
P28616 | MKKDYYEILGLSKGASKDEIKKAYRKIAIKYHPDRNQGNEEAASIFKEATQAYEILIDDNKKAKYDRFGHSAFEGGGFEGFSGGFSGFSDIFEDFGDIFDSFFTGNKGQERNRKHAKGEDLGYNIEISLENAYFGYKNNINITRQMLCDSCLGKKSEKGTSPSICNMCNGSGRVVQGGGFFRVTTTCSKCYGEGKIISNPCKSCKGKGSLTKQETIQLNIPPGIDNNQQIKMKGKGNVNPDNQEYGDLYVKILIRSHKVFKRNGKDLYAMLPISFTQAALGKEVKIKTIASKEIKIHIPKGINNEEQILIKNAGMPILQT... | Cofactor: Binds 2 Zn(2+) ions per monomer.
Function: Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction... |
P94319 | MSTSTKRCYYETLEVERDADESKLKSSFRKLAMKFHPDRNPGDDTSEVKFKEINEAYEVLKDKDKRAAYDRFGHAAFEQGGPGGGAGFGAGFASSFSDIFEDLFGMAGQRGRGGRERGADLRYNMEITLEEAFGGKTAQIEIPVSVTCEACSGIGAKAGTKPKTCSTCGGAGRVRQSQGFFTLERTCPGCQGRGQMIEDACPSCSGQGRVTRERTLSVNIPQGVEDGTRIRLAGEGEAGVRGGPPGDLYIFLSLAQHQFFQRDGADLHCRVPISMVTAALGGEFEVPTIEKGKAKVKVPAGTQSNRRFRIASKGMPVLRS... | Cofactor: Binds 2 Zn(2+) ions per monomer.
Function: Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction... |
C0ZB49 | MKRDLYEVLGVAKDADADEIKKAYRKLARQYHPDVNKEADAEEKFKEVKDAYDILSEPQKRAQYDRFGHQDPNQGFGGGGFDGSGMGGFGDIFDMFFGGNGRRANPNAPRKGSDLQFGLSIDFIDAIFGKETDVEIPKEAECDTCLGSGAKPGSGVDTCKTCSGTGQQEVVANTPFGRIVNRRVCSTCEGKGKVVKEKCSTCRGSGRVKVRRKIHLNIPAGVDDGAQLRVTGEGEPGANGGPPGDLYVVLRVKSHEFFEREGNDIYCEVPLTYAQAALGDEIEVPTVDGRVKLKIPAGTQTETFFRLRGKGVPHLRGNGR... | Cofactor: Binds 2 Zn(2+) ions per monomer.
Function: Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction... |
A6T225 | MAKRDFYEILGVGKSASDEEIKKAYRKLAMKHHPDRNPDSKGAEDKFKEAKEAYEMLSDPQKRDAYDRYGHAGVDPNMGGGGGGGGFADAFGDIFGDIFGQAGGGRGGRGGPQVYRGADLRYNLEITLEQAAHGYDTTIRVPSWDNCETCDGSGAKPGTSPVNCTTCGGHGQVRMQQGFFSVLQTCPKCHGSGKINPSPCGTCSGAGKIKRNKTLEVKIPSGIDDGMRIRSSGNGEPGMNGGPPGDLYVEIRIKQHPMFQRDGDDLHCEIPISFAKAALGGEIEVPTLNGKASFTIPEGTQSGKTFRLRSKGIKGVRSGY... | Cofactor: Binds 2 Zn(2+) ions per monomer.
Function: Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction... |
Q1G9R3 | MAANRDYYDVLGVSRDASDAEISKAYRKLAKKYHPDLNHEAGAEEKYKEVNEAYEVLHDPQKRQQYDQFGQAGMNGQGGFGGQYGGQGFGGADFGDFGDIFSSFFGGARQQVDPTAPQRGADLDYTMTIDFMDAIKGKTSEISYSRSTTCEVCKGSGAEKGTHPITCDKCGGSGMMTITQRSVLGMIQRQTTCDKCTGSGVIIQHPCHNCHGKGVKTQKQTLQVKVPAGIDNGQQIRLAGQGEAGKNGGPYGDLYIVFRVRPSKDFTRRGQTIYTTVPISFAQATLGDEINVKTVYGDTKLKIPAGTQPNQKFTLKEKGV... | Cofactor: Binds 2 Zn(2+) ions per monomer.
Function: Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction... |
C4Z1J3 | MADKRDYYEVLGVPKDADDAAIKKAYRQLAKKYHPDMNPGDKEAEIKFKEASEAYAVLSDAEKRRQYDQFGHAAFEGGAGGAGAGGFDFDFGDMGDIFGDLFGGMFGGGGSRRNSNGPRRGADVRVNVRITFDESVRGTTKKIDVTLKDECSSCHGTGAKPGTSPETCSKCGGRGQVTFTQQSFLGMVRSQQPCPDCHGTGKIIKEKCPDCYGTGYISSKKTIEVNIPAGIDNGQCVRIQGKGEPGVNGGPRGDLLVAVIISASTEFERDGYNIFSNVVISYPTAVLGGEIKVKTVDGEVLYEVKPGTASGTRVRLKGKG... | Cofactor: Binds 2 Zn(2+) ions per monomer.
Function: Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction... |
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