ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
A0A8X6G5T0 | MHFFNFQPSSPNRNRKSPSLPSGKMSCTEKLSTGSSGKMKVPHRFEIHSYTRPTVCCYCKKLLKGLIRQGMQCKDCKLNVHKRKCLECIPMDCTGEAPKENCEIPKIHQMKMIPDLQDDESKIPVHEASSNNIPLQRIVQSIKHTKGKNYKVLKEGWLVHHTNREGMRKRHFWRLDTKSVTLFQNDTTSKYYKEIPLSEILSVELSKQNLCTEQNQSYYLELRTANVDYYITEDTNTLKAWETAIRQALMPVDTPKTTNPSTQGNKESSNGANTKKENPEQSLDISLQYQIFPDEVLGSGQFGIVYGGVHRTSGRGVAIK... | Catalytic Activity: ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]
EC: 2.7.11.13
Subcellular Location: Membrane
Sequence Length: 622
Sequence Mass (Da): 71552
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A0A357IKD4 | MPVKKGILIIVLIFGLLVLSACKKPVAFTFNFYEYMDTFINVSLYAESESDAENMKQEIEDIYAMYHELTNNYEDLSFGSTYKENIFTINQKINENIEIDRELYEVLEEAIRLNILTDGYFDISIGKMVDVWKDVISNDVDGYMHNEVPESVFQGILDDLVDIEVVEEPFILTETDGKYYVRLTHEDVKLDLGALSKGYATQVVYDYLIEQGVEYFSITAGSSSISIGKKIDRKTEMFHISLANPVESGQTYGMIYVQNKAINTSGNFEQYFLYEGLRYHHVISPKTKMPAQYYHTVTLVGEDAGLLDALSTALFSMNEE... | Cofactor: Magnesium. Can also use manganese.
Function: Flavin transferase that catalyzes the transfer of the FMN moiety of FAD and its covalent binding to the hydroxyl group of a threonine residue in a target flavoprotein.
EC: 2.7.1.180
Catalytic Activity: FAD + L-threonyl-[protein] = AMP + FMN-L-threonyl-[protein] + H... |
A0A8J5HWL3 | MIGRLSNTPNVVFAYEVSGVVDYLTSHGVNALPGRRYSTSQLQGMNWVIKLTQINFPMQPTEIQVKKLTPTTIIPRRYSDEVAGYDLSSDETITIELRDRSLIFTGIAIMIPKGFYDQIVAISSIARRLGVHVGDGVIDSDYQGDVETCKYCKNPTQKRHRRHCTLCDIAMCEMCSIYYYNKRTPVAISSPIRMDRGAAGSSRPLGRGDSGSLGPTQQQSSERVPTNDSSCPNFVEQYQAYLTQY | Pathway: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2.
Function: This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA... |
A0A932XUW1 | MLALMPSRRVLALVGSWEITWYGALYVASFGLAWWLLPRLTRWRGVEITPDAQLAIVAWGAVGAVIGGRLGYVLLYEPAYFITHPLQAFALWDGGMASHGGFLGAAVVLYLAARRFSLDPLALGDAVVVPAALGLMLGRLGNWINQELFVSTAAHAAVIGKDLLIAGMCYAHLRFTARREKGQTLALFLILYSLLRWLAEYVREPLYPSMLGMTYGQVLTWPILAAGVSLMVWLRQSARRNV | Pathway: Protein modification; lipoprotein biosynthesis (diacylglyceryl transfer).
Function: Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins.
Catalytic Activity: 1,... |
C0GG56 | MKKTIVVGSRDSELALTQTHFVIGELQKHFPDVDFTVKHIKTEGDKILDVALSKIGDKGLFVKEIENALLSKEIDFAVHSMKDVPTAVPDGLQITTITEREDPRDCYIAKDGKTRLFDTPQGAVIGTSSLRRSAQLLHQRSDFEIVPIRGNLNTRFRKLSEQDMHGIILAYAGVYRLGWADKITEIIDFEKSLPAVGQGALGIETRSDDDFTINIVSALNHDTTASAILAERAFLRQLEGGCQVPIGAYGRLEAEELVLDGVVAGLDGSTVLRDQVRGSADESDALGKKLAQKMVERGADEILKQVRQEFDANA | Cofactor: Binds 1 dipyrromethane group covalently.
Function: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
EC: 2.5.1.61
Catalytic Activity: H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+)
Sequence Length: 314
Sequence Mass (Da): 34471
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A0A7S3D2B6 | QRKEESKALSFSRQKREREREATSKVQRETDASEFEFSTEKINQNFSNYSAWHHRSAVITRKENRDNAEGDDKHDFHDDEFSLISNAFFTEPEDSSSWMYHRWLLSRSAPLSTSFTWPSQGERLPSPPKALLVEFTEEVEGVEGGVTVKVRKTGKSGEGEKEGEEGGGEGAVISSVQLLFSPAVVMENASTFVDLKPAAKAWTAVEAVVEGSKVQVEELFQPNSEDGVVTVTIKIGGENSSINATRTKKKLQAEQVLTFTVGKEGQAHTKGQEGEGEGEGEGVSSTLSLLKRTHMYGKKRMTQALRKQVIEERAEEEERA... | Function: Catalyzes the transfer of a geranyl-geranyl moiety from geranyl-geranyl pyrophosphate to cysteines occuring in specific C-terminal amino acid sequences.
EC: 2.5.1.60
Catalytic Activity: geranylgeranyl diphosphate + L-cysteinyl-[protein] = diphosphate + S-geranylgeranyl-L-cysteinyl-[protein]
Sequence Length: 8... |
A0A7Y1X6D1 | MSDTKLPCLILCGGASRRFEGEHKAFAPLGEKTVLQHVIDRVEPQCREICLNAPEHDGFELFELPLCPDGPDAGKGPLAGVLTAMNWADKAGAAQVLTCSNDTPFIPLDWAQILNKDSNDKIRVPAFEGNSHFVCALWPVQLKIELANYLASGDRSVQGFVQSQAVEFIEFSGVNDFDPFFNVNTPDDLRTAAEILQSVNRR | Function: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
Catalytic Activity: GTP + H(+) + Mo-molybdopterin = diphosphate + Mo-molybdopterin guanine dinucleotide
EC: 2.7.7.77
Subcellular Location: Cytopl... |
K2N009 | MELQDDDGDRRTLESHWLQRHARDEWMAPIGGTGCCTELTLAALAALGCLMVKCEMVEPMGWCGNSGCGLLYKKYSALKMSEYPQMFCEAGVPARRCTSDRYSGGYCLGSINEGPAKHTMYSCLIIDPALVVRDAEAVVWSGEYLSVVPGDEPFLWCLDTLPTNTT | Cofactor: Binds 1 zinc ion per subunit.
EC: 3.4.24.-
Catalytic Activity: Preference for hydrophobic residues at P1 and P1' and basic residues at P2' and P3'. A model nonapeptide is cleaved at -Ala-Tyr-|-Leu-Lys-Lys-.
Sequence Length: 166
Sequence Mass (Da): 18273
|
K2MYL8 | MVLWLSVGVFYAGMRCAVASGCRSVGEVASNRNMAALLITTRGIIVPQQLKAYGGTFSRSIGERSDHLVGNFVLQSLSPSRTAHSPLLAKNVKTKTVTSFEDMLLAPELRKALMQSLHIFTPSPIQQMAIEVIVQGKDTVVAAPHGEGKTLAYLLPLYQNMMKDRDVYKIPLRERRPRMILLAPTK | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 186
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence Mass (Da): 20507
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A0A8J5FKT1 | MNIAKNHARRIFSRRPGTQRCLIKKPEKKCSTSVFKSRTKLLNLALNTVLGKNSRITVMLEFLAHECGSWEQRSAVLRMQSGRQPLDLGLNRVSRGRMKRSNSETYDITLSIFGGVWAHGDISPEVPLWLRRTGVKGNGLVLSWCSLAGRRACFDKVLSTTDSSGDQQILEASNDISADGAEGTLDSVTRCCHLRSCWVNFVSRAWRLADISLRRWRVMEDTVEAMLIQSVVRVLFICMVVWLGLCPRSCIHVMMVDVCVRQPTIVILMPSLVRHCISRRLYGFLVPIWHWSGYDERGPMPHRHCELKEERQEVTRSTSG... | Pathway: Protein modification; protein ubiquitination.
Function: Functions as an E3 ubiquitin ligase.
EC: 2.3.2.27
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
S... |
A0A420WJI6 | MKAFLSLFLRDITLAWRSGGGWIMGAVFMSAFLALCSIALGGQISELRRLGTALIWLSVLFSMLLSFNTIFQSDFRQGTLSQILLSGISPLTLCLAKWASFLVTGFLPLFITIPFASLLFGLEGRLIAAILFALALTAPALAAYVTLAGAILCGRVGAGFLAILLVMPFLIPLLIFGIAATESFVTDGWAASEIRILSGLSLLSIAVGIPASSAALRLNLEPS | Function: Required for the export of heme to the periplasm for the biogenesis of c-type cytochromes.
Subcellular Location: Cell inner membrane
Sequence Length: 223
Sequence Mass (Da): 23573
Location Topology: Multi-pass membrane protein
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R6DGQ8 | MKERQKKRSIFSWKFFWIAFVFGIIVLGVEYVGLTGYDNRTAQNVSEKSISIVKKTLRRYDNMILNDQTKSLIRLLDKTSELSRVYNQEKGFDHNRLNEYVQEQRLDGAMILDHKGRIVMQSSIGSKGCYTLWKDVINDENVNDVLKYSKKSYISRIRRKNAEYDFVATSTKRAHGMVVSYKKAGTSSESSSEITLASLFEECNLKLDGTVVITNGKKVLSTNNRRLKKQTMKFCKALHENSHNKNEISMTKLVAKTKVWYGSGSRLKNYHIYVFFPGRSMYKNRRTVIAYSMAVLGVFLLIVLLLYQHFLKGNFDEIQK... | Function: May play the central regulatory role in sporulation. It may be an element of the effector pathway responsible for the activation of sporulation genes in response to nutritional stress. Spo0A may act in concert with spo0H (a sigma factor) to control the expression of some genes that are critical to the sporula... |
A0A8J5L8J3 | MFYRDCDVNGSVDFIFGNAATIFQNCNLYTCLPLHDQSNVVTTQGCTMPNSPQGSPSTTARCAAPPWKAYMCTVVMHSFINDAVDPMEWLEWSGAFALCTLYYDEFQKLWCRC | Pathway: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5.
EC: 3.1.1.11
Catalytic Activity: [(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O = [(1->4)-alpha-D-galacturonosyl](n) + n H(+) + n methanol
Sequence Length: 113
Sequence Mass (Da): 12775
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A0A8J5LJL6 | MAASPLMAEAKPPSAPRSSSSSPPPILAVAILGILTTAILLLSYYLFVTKCRTGRRLRSPLANQARGLHPSLIRSIPVVNFTVASNDIELRSQCAVCLNEFQNMERLKLLPGCFHTFHIDCIETWLQFNANCPLCRSDVTASAAAVPAQFILVVEQSRSSGPIDPPAIERPNFRHRALASSRRRTEQRHPLLCRLSSVLDQSFFVVELAKLEFQQ | Pathway: Protein modification; protein ubiquitination.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
EC: 2.3.2.27
Subcellular Location: Membrane
Sequence Length: ... |
A0A8J5GX85 | MLSYFLNCTSASMAWGALHLLAFFLLCFIVVGLDVVVPVNQSVRVAQDNTDNFNTIGEAITFALNNTLLHHLHQRRGVPGERDHAQEENEPYFDCSSIAALINGVGLRQCYGMESGTDNFNTIGEAIAFAPNDTTVEEGGYFAIYVNEGAYRENVFVPEIKKNLILIGAGADRTVITSNRNVEDGWETYDIATFGSVHCPQDMTFENTAGSAKQQVVAMRNNADLSIFYRCKFLGYQDTLYVHSNNQFYRDCEVHGTIDFIFGDATAVFQNCHIYARLSLQGQVNVVTAQGRTLYNESIGFSIHNCTIGAASELVAANYS... | Pathway: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5.
EC: 3.1.1.11
Catalytic Activity: [(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O = [(1->4)-alpha-D-galacturonosyl](n) + n H(+) + n methanol
Sequence Length: 398
Sequence Mass (Da): 44325
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A0A8J5H535 | MSSQVFHMSQMKFSPSSSSPTPPPIAGLPIVTISIAGILATFFLLLSYYVFVIKCWLNAHHSSRRRHSVSLSSAYEQRGLAESAIRAIPAFRYRQLSVGAAECAVCLSEFQEQERIRLLPSCLHVFHIDCIDTWLQFNANCPLCRASITAPPVPINPLAMALAPQFSHPHDAFLEIRDEEIKMEFLGSRGDECIDARKEEEEKLCLQRMRRSFSVDSSGDMQLHVALQRILQQSSHEGSSSVGGGGRFRRSLLSFSRSSRSSVLPLQMEL | Pathway: Protein modification; protein ubiquitination.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
EC: 2.3.2.27
Subcellular Location: Membrane
Sequence Length: ... |
A0A1I7N0U1 | MIVVWLKFFHVASIALWSAGLIALPFLYRERPGLRDGELYRLHSFTRAFYIRFVSPSAFVAIGTGTALILLQETYANWFSAKLLAVAAMTGIHIFSGLAILRIFERTGRFHTERFFVMLPATTAVVTAILVLVLGKPELQWPEPLTQLLAPGALREIASSLTDGWIS | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; protoporphyrin-IX from protoporphyrinogen-IX: step 1/1.
Function: Catalyzes the oxidation of protoporphyrinogen IX to protoporphyrin IX.
EC: 1.3.99.-
Subcellular Lo... |
A0A453KSI9 | MEKGTPAIGWAARDDSGLLSPYSFSRRVPKDDDVTIKVLFCGICHTDLHIAKNEWGNALYPIVPGHEIVGIVTDVGPGVKSFKAGDTVGVGYFLDSCRSCDTCSKGYENYCPTLVLTSNGVDYDGATTQGGFSDVLVVNQDYVLRVPESLSLAGAAPLLCAGVTVYSPMMQYGLNAPGKHLGVVGLGGLGHMAVKFGKAFGMTVTVISSSPRKREEALERLGADAFLVSRDAEQMKVTFLCPLH | Pathway: Aromatic compound metabolism; phenylpropanoid biosynthesis.
EC: 1.1.1.195
Catalytic Activity: (E)-cinnamyl alcohol + NADP(+) = (E)-cinnamaldehyde + H(+) + NADPH
Sequence Length: 244
Sequence Mass (Da): 25941
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A0A453K2J9 | MAAPASRHRGSSWGRSWPLLFVAILALHSLAIYLFTRGFLLTRTELDLHSHRDDRTGVSPGCSSWPQPAVDRLVIVVLDALRFDFVAPSTFFEEKQPWMDKLQVLQKLAADEKNSARIFKALADPPTTSLQRLKALTTGGLPTFIDVGNSFGAPAIVEDNIMHQLVKSGKRVVMMGDDTWIQLYPEHFNKSFPYPSFNVKDLDTVDNGVIDHLLPSLHENDWDVLIAHFLGVDHAGHIFGVDSTPMIQKLEQYNQILEDVIDTLKSLSTPGGPHENTLLLVMGDHGQTLNGDHGGGTAEEVETSLFAWSPKTPPDAVLSV... | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 365
Sequence Mass (Da): 40474
Location Topology: Multi-pass membrane protein
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A0A8J5EST4 | MWHFFLLIIGIFPMAFFILLPSTTTVPVIDVDPPIKPLKHASGADTEVGGDHTVIASAYISYARRLNLECSKQMRVFSELVRNLSLLLSVSFFRLNHLSFYLPEMYIKLHKILFLDDDIVLQRDLTALWKIDMDGKVNEAIEICFGSFHRYAQYMNFSHPLIKEKFELDAWRKGKCIEAESLVAIRENIMTIPRKEKKRKARREEKAENVAVLDMVFRRCTGCLEDAQVEKI | Pathway: Glycan metabolism; pectin biosynthesis.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 232
Sequence Mass (Da): 26914
Location Topology: Single-pass type II membrane protein
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A0A8X6KEQ4 | MPVLAPTVPSSSNHREQVIWTRLCLGHTRLTHRHLLFGEPPPYCEICNVLLSGEYDYPEPEKWTDAELGVVDIDD | Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
... |
A0A7U3RWI1 | MMSLFLMWNFLMSILFMFMKHPMSMGFILLLQTTVIAMMTGMLTYSYWMSYILFLIMVGGMLILFIYMTSLASNEMIQYSNKLFLLIFINMMIFFIIYLLMDYSQLIPFMNN | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity and assembly of complex I.
Catalytic Activity: a ubiquinone + 5 ... |
A0A7X7NW08 | MKIIAVGKIKKKYFLDGIDFYKKQISKLDIIEVRQSNIEKEGKDILAKISERDYVIALDIKGMKYDSESFSKKLEELKLNGNDIVFLIGGSLGLSDEVKNRANERLSFSDFTFPHELFRLILVEQIYRAESILLNKPYHK | Function: Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA.
Catalytic Activity: pseudouridine(1915) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(3)-methylpseudouridine(1915) in 23S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.177
Subcellular Location: Cytoplasm
Sequence Length: 140
S... |
A0A1I7XTV8 | MWRRMTVEYSNVVNTSSFHVFTRILLRWKGSLWKAVYIDLLLWLSAYAVIAVIYNYALDDNSQRIFEGVCEFFVKYEHHLPLTFMLGFYVSLVITRWWSMYLNIGWIDSSALLISYLIDGSDEAARLMRRNIIRHMLLYQFLLKILVRSDKTGSSLKQILNMSGYLTTEEYHKFRNFNSQFPQYWIPIRWALSGIKRARREGRIPTDRLQQDLSKV | Function: Forms chloride channels.
Subcellular Location: Cell membrane
Sequence Length: 216
Sequence Mass (Da): 25770
Location Topology: Multi-pass membrane protein
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A0A453LCA9 | ASSSILMVGYAMKPSREEDFAKRGAFPLYPSQNGLIFVPLSFELHLASQLQEVDIILHKMTDEIISIDPNCSISFPRGISFSAGMSEVISRFMEEYPDFCIIDPFKNISPLLDRLQIQEILVRLQELGSEGRPKLRAPHSLKVINFSGSELQKQLAEANLSFPLIVKPQVACGVADAHNMALVFQIEEFSNLSVPLPAILQEYIDHGSKIYKFYVIGDKVFHAVKTSMPNANLLKSSSGDEPLTFNSLKTLPVATKEQLLLNRAQDNKSLNIGVVEEAAKLLKESLGLTIFGFDVVVQEGSGDHVIVDLNYLPSFKEVPD... | Cofactor: Binds 2 magnesium ions per subunit.
Function: Kinase that can phosphorylate various inositol polyphosphate such as Ins(3,4,5,6)P4 or Ins(1,3,4)P3.
EC: 2.7.1.134
Catalytic Activity: 1D-myo-inositol 1,3,4-trisphosphate + ATP = 1D-myo-inositol 1,3,4,5-tetrakisphosphate + ADP + H(+)
Sequence Length: 344
Sequence ... |
A0A453K1U1 | MLIFCIITLVQAIDDAGHDKAVKLKVRGLEAVDRAIGQLARLLWEAEKSGHYQYFFCVTGDHSTPVEYGDHSFEPVPFAICRLRDFVGAIGEGNVMNTPLDDFPLPSVKSGEDLTDDSEPAEHKPEERKAFSGDTVCEYTEIAAARGCLGRFPGSEMMGIIKKFMKAKND | Pathway: Carbohydrate degradation.
Function: Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
Catalytic Activity: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
Sequence Length: 170
Sequence Mass (Da): 18771
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A0A7G7NC95 | LSSGIAHAGGSVDLAIFSLHVAGASSIVASINFITTVINMRSPGVTFDRLPLFVWSAFITAFLLLLSLPVLAGAITMLLTDRNVNTTFXXPAGGGDPILFQHL | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A4R2MAZ4 | MKILLLPSSWSLGARLLTLALVPACAMALVVSVVLYVVTSTEVSEALEERGRFLSVTLAEAVQYGVVSGNTSAVEATLHGVAEADPVVAAARVLDADRRPVVEVRSRAGQAAEWRFEAPISLKPLDVDLYDTAPGARGTAHWLGWVQVDLSPQPLLAGSRRRLLLGVALVLVAAALGAAAGLLMARRLRRPLENAMGALRSIRDGDYAVTLAPRVSGELGELQDSIATMARAVKLSRQYLEEQVRERTRELQQAVERLTAADAEKRRLIARGNRLVEEERRRIAVEIHDELNAALVSIRLIASSLADDTRGQGMHTAADA... | Function: Member of the two-component regulatory system NreB/NreC involved in the control of dissimilatory nitrate/nitrite reduction in response to oxygen. NreB functions as a direct oxygen sensor histidine kinase which is autophosphorylated, in the absence of oxygen, probably at the conserved histidine residue, and tr... |
K2FLJ1 | MQTYDMKVVNHREIAECTYEITLQTDVFFPAEPGQFVHILVDPPHQLRRPLSLASSSGREITVVYKTFGEGTRTLANKKRGETVNVLGPLGNGFTLPEQKKVMLVGGGVGVPPLLWLAKELHKNGKKVSAVLGFKSVNQVFYRRKMEEYAEVTVVTDDGSSGEKGLVTKWLDPEADVYYACGPNPMLKALEAQLTIPGYNSMEERMGCAIGACFACTVETKDGGYVNVCKDGPVFPKGRVKLP | Cofactor: Binds 1 FAD per subunit.
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (NAD(+) route): step 1/1.
Function: Responsible for channeling the electrons from the oxidation of dihydroorotate from the FMN redox center in the PyrD type B subunit to the ultimate ... |
A0A847YHD9 | MNEERIVNGELTSSPETLLQDMRALRDQAEFAFNRLLDVTAVDRGDAFELLYRLNSWTTNRDLVVRLRVPMTEPRLPSVSGLWAAALFGEREVQDMFGIEFMGHPDPRPLLVLEEGFGFFPLRKSYQLPGRPGQSNRR | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain.
EC: 7.1.1.-
Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
Sequence Length: 138
Sequence Mass (Da): 15852
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A0A7S9VKZ6 | MPGRGQNKRFEDPYDRVLGFGDPHARKRGQQLNALAKDKVKDLIPDGPYVYDFTDLVVPKIVGGVVVPATTIVRTVRVSGVTADNTYVSYVFTPGPNTWVEVDPVIHQPTALVGVLRAEYKKVSTERDDLKQELSNLKLELSLLRHDYERVKPKEIRARRWSYTALFTLFFLLGLLLADVTQASQPVCTIVNEEAKTCEQWEWEEATPTYLESIVQQFRGYWEVSRVSDALRYCVPYLYDWHVMAAVLAVVYSLWADRSIPMLVTLVLATVTRMQVLVLAITPLLDAAATFSLWAVMVLYTIDQPAAIVLSFVLLTMASI... | Function: Protein covalently attached to the 5' extremity of the genomic and subgenomic RNAs.
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Subcellular Location: Host membrane
Sequence Length: 832
Sequence Mass (Da): 93136
Location Topology: Multi-pass membrane protein
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O47439 | HSFIDLPXPSNISSWWNFGSLLGICLMLQIITGLFLAMHYTSDTTTAFSSVTHICRDVNYGWLIRYMHANGASMFFICLFLHVGRGMYYGSYTFLETWNIGVALLFAVMATAFMGYVLP | Function: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membra... |
A0A4P7JD71 | MRNVRLIARLDIKLNWLIKGVQMEGWRKVGPPAEFARTYAEGGADELFLMDAVASLYERNSLLDIVRTVATEVFVPMTVGGGVRSVEDANVLLSSGADKVAINTAATRDPSLISALSDRFGAQATVVSIEAIRSGTNWLAMTDNGRNHTGRDVLEWASEAEKCGAGEIVLTSIDKDGLGSGFDVDLVRQVSDRVSIPVVASGGLGTGDHLVELIDKTEVSGVAVAQALHWRELDLSDLRQCLRDEGIFVRPLPEERARYSLSS | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9.
Function: IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ... |
A0A453Q5Y6 | MFLLIQWAWGLLKLLLRYNSNISWYHMNCTFIWFIAFFESILIRKWTIRVIVFCTTAMVTEFMYIMLRDLKLNVREIHSRKPQLYRTRISEEFRDSNRLILVTSDVSTRGVNYPDVTLVIQIRLVFLLVESIIFIVLEGLEGKVNPGKEFC | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 151
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence Mass (Da): 18031
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A0A7S3G4G1 | MEKWPTFSSLSPALSQSTLNVLERDLGFSTATPVQCATIPLLLTHKDVAVEACTGSGKTLSFVLPMVDILRKRAALETPKPFQLGGLVLAPTRELALQIFDVALPFVESIPGYSLYLLVGGTDTSSEVETMRDRERGREDEAAEYTIIDEASWTEEKEEVDNTEVEANGGKRERGKGMVWVGTPGRVLDLMQRMYEVNLKKIEVLILDEADRLLELGFQATLNSILKKMPKQRRTGLFSATQTDDVKSLIRAGLRNPVSVEVAVSDKNGRLLQELKVPSTLLNEVMFCSSKERIGELFSLLHDYKGRKVMVFAMTCAMTE... | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 629
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence Mass (Da): 71488
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A0A453DHL7 | MINVSPIGRNCSQEERDDFEKYDKAHNVRPKMVSVLREKFAHLNLTFSIGGQISFDVFPQGWDKTYCLRYLEEFKEIHFFGDKTYKVRDIYFSCAVLPSKEISFSFREVPLCTQDVV | Pathway: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 2/2.
Function: Catalyzes the interconversion of mannose-6-phosphate to mannose-1-phosphate, the precursor for the synthesis of GDP-mannose. GDP-mannose is an essential sugar nucleotide... |
A0A453EGS9 | CLCKFRIQEKHQPVQVLEALLPEGIIIPAGFETVGHIAHLNLRDEHLPYKTLIAQVVLDKNKPKIQTVVNKIDAIQNDYRTMQLEILAGHDSLVTTVIESGLRFQVDLATVYWNSRLSTERQRLVNNIFQNSDVVCDVFSGVGPIAISAAKKVKYVYANDLNPAAVEYLEQNIVLNKLERKIEVYNMDARRFVNAMYSSQHVHPVTQVVMNLPKDAAEFLDVFRGILRNRQTGHIAMPKIHVYGFSKAEDPEYDFHERINLALCDSVMGVEMHRVRLVAPGKWMLCASFTLPESVAYAKANYITC | Function: Specifically methylates the N1 position of guanosine-37 in various cytoplasmic and mitochondrial tRNAs. Methylation is not dependent on the nature of the nucleoside 5' of the target nucleoside. This is the first step in the biosynthesis of wybutosine (yW), a modified base adjacent to the anticodon of tRNAs an... |
A0A453NHY3 | LPLSPHPTRRRAMDAGGGEQLSLAAVRDQLIREEDSIVFALIERAKRPRNTPAYSAAAAGGSLAEFFVREAQVLHAKAGHYQKPEDVPFFSQDLPPPVFPTKGHPKVLHPFASSVCVNDAIWKMYFNELLPLFTADGDDGNYAETVALDFACLQALSRRIHCGKYVAEVKFKDAPQDYSPPIRAKVNLVGALYFTSSNYLSRLISWLIWLTSYTLLPQLIFHLLYRLTRFLLHFS | Pathway: Metabolic intermediate biosynthesis; prephenate biosynthesis; prephenate from chorismate: step 1/1.
EC: 5.4.99.5
Catalytic Activity: chorismate = prephenate
Sequence Length: 235
Sequence Mass (Da): 26419
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A0A357ALM4 | MNKTIKKLRISLAIAMTKLTVFGLRLLNRGGTSLPGKIALKIYPNLLSELSGKFRIIMITGTNGKTTTSRIVAGMLDQSGIKYITNKAGANLASGITTTLISALSLTGKPLVRTALLETDEAAFRTIAPKLRPETAIITNFFRDQLDRFGELYTTLNGVREGVSGTPDTTLILNADDSLCASLGQNVPNPVLYFGFAEGAYPEADESGKTDAAFCIHCSSRYTYSSTTFGHLGHFLCPSCQYTRPAAQIECTQVLAYDNLSSTIEIQMPEEKFSVKLALPGLYNIYNALAGAALGHILNLKEKELVHVLEGFECGFGRME... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: The lipid II isoglutaminyl synthase complex catalyzes the formation of alpha-D-isoglutamine in the cell wall lipid II stem peptide. The MurT subunit catalyzes the ATP-dependent amidation of D-glutamate residue of lipid II, converting it to an isogluta... |
A0A453CX64 | MTPISLVGPTPADHESSSRLEVLLREAGLYETSDELAAREDVLRDLQAIVDRWVKRVTAQRGFPDGMAEQATALLIPFGSYRLGVHGRGSDIDALVVGPSYIDRDHDFFAVLGGVLAETEAVTELQPVPRAHVPVIKMRFRGVQVDLLYAGLCLPVVPRDLDLRDRSVFRGMDLASARSLNGVRVADELLRLVPDAGAFRTTLRCIKHWAKARGVYSNVMGFLGGVGWAILVARVCQLYPNASPSMLVPRFFKIFTQWKWPNPVLLRDIEHDDGGELALRLPVWDPRRNPRDKSHLMPVITPAYPCMNSCYNVSHATLRT... | Cofactor: Binds 2 magnesium ions. Also active with manganese.
Function: Polymerase that creates the 3'-poly(A) tail of mRNA's.
EC: 2.7.7.19
Catalytic Activity: ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide
Subcellular Location: Nucleus
Sequence Length: 388
Sequence Mass (Da): 42970
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A0A453DS99 | MRTRLILPSPQCSVGHFVCSSCRPKLVRNKCHLCSAETTFKRCLGMERLMESVTVACSNANYGCAQKLTYYQREEHEDACPSAPCFCPASSCSFAGPIDALLEHSASQHKWPCTTIKYSEDVKFCLEPGLHFLRIKDREIFLLNVALEPFGHAISVVCIQPKATNSKFKCRMSYGSFLTDYYQISVYKIRSSSLSDGLPKGYNLILPKDEIANNGKVTLLTFSIDDPNPKVKVREPICLKPVRGV | Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Length: 245
Sequence Mass (Da): 27414
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A0A837IH35 | MDENQNLDPEQENTTSIPVPDEQTQWGLIRTTPIIEEMERSYLDYAMSVIVARALPDVRDGLKPVHRRILFAMKEMGLTHKSAYKKSARIVGEVLGKYHPHGDQAVYQTMVRLAQTFSMRYPLIDGQGNFGSIDGDSAAAMRYTEARLSKIAGEALEDIDKRTVDLIDNFDGSQQEPTVLPAKLPNLLLMGSDGIAVGMATKIPPHNLLEVVDAIKALIDKSTATVTKHYPDEELVSAPYRDLIGNLESGVEIEELCKHIKGPDFPTAGIIYDTNEIKKLYATGKASIIVRGVAEIVEKKSGRFQILITELPYQVNKAKL... | Function: A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of ... |
A0A8X6IXM4 | MGILFSRFRAKPSTKELLEDLEKEIETLEEYKRSTEVQQKAVIGSLIFYSVLLYVIVAAVFLFYSYPVTTKDRIVYAVPFLIFPLLLYVLKKFLQWYFLQKIRHNEENLLELKKRKKSLLEFAMETETYKVVKELLEKYDPAYHRKIFDSKPAIEAPPPQPIKGSFSEMELRRRNVSPRGSSPIPLGSSGQTLTINSAAGSPNFQFFPGKSPTNPPYPTQFFQRGGQRFVRPPVPPMPRPVLPRERTFMDRLVDYLVGDGPSNRYALICRQCQSHNGMALKEEFDYVAFRCCYCFQFNPPRNQQPPPPRLTLPAPPPSAP... | Function: Plays a role in determining ER morphology.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 408
Domain: The C4-type zinc finger motif is necessary both for its ER three-way tubular junction localization and formation.
Sequence Mass (Da): 46252
Location Topology: Multi-pass membrane protei... |
A0A7C6CED7 | MTVKKIILSYGNAGADEGVFEGAKKLLKKGELSNYCLLEPILVAKETKNNLKNLNEVLLNIDLVAKKTKEALIEGAFPLFIGGDHSLSLGTVSAVSSHYDNLGLIWFDAHGDMNTNKTSPSGNIHGMILAALQGYGDESLTDFYFQGIKVKTSNVLIFGVRDLDSKEKELIKEKGVTYITYDEIKQMGLKAALKKVKNYFKNKTNNIHLSFDLDVLDPQLSPGVSVPVRKGFNFQESKEIIEGIFKDFNVTSMDIVEYNPQLDQNNQTLTYLLKTIKEVENLISSEK | Pathway: Nitrogen metabolism; urea cycle; L-ornithine and urea from L-arginine: step 1/1.
EC: 3.5.3.1
Catalytic Activity: H2O + L-arginine = L-ornithine + urea
Sequence Length: 287
Sequence Mass (Da): 31933
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A0A453DJP2 | GVQSSSGRPGRPGHGLRRAVVPLGGGGRRRSVPRLPRGDVPAAGANRGVARAGGLQERLRRGAGLHPHPLPRLLPAGLRRVGAHRGPRQRAEGEAQHDAPQRSAGPHRPHPCRGPPRLQGHGVVRRHHRARHPRIPLPGRRAPLRRHPRPARLLLPRVAGTSQTAAGALPQCGQAHRVLRQTWPRRGRPGVPLRCAHLRRRPLPGLRDRFKNGFDTNPAIDHAFATTLKKNCDKDFPRGTVEQNLDRRTPDIFDNKYYFDLIAKQGLFKSDQGLIDHPATKSKATHFSLNQGAFFDQFAKSMAKMVKMDLLTGNKGEIRA... | Cofactor: Binds 2 calcium ions per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress.
EC: 1.11.1.7
Catalytic Activity: 2 a phenolic donor... |
S6CEU9 | MNDKRQTRSCQVLAGDRERALALLRVALAAGVSRSCLWFGEAAPDGVRRLGRHDYLDALGCECDLLVYDAHAGLYPDVLAALLGTLRGGGVLVLLSPSWAQWAAFDDPALAGLAPWPLGSTDVGRRFLQRLQDQFAASPVVRILDVDGTESLVLPPAAAPVHSPELNEDQHRVVEALLRVVTGHARRPLLLTADRGRGKSTALGAGLARLLRERSCRVAVLAPTRRAVEALFARLHRDLPDAGGEVRYWRPADFLAEAPDCDLLVIDEAAALGVPLLQTLAERYNRVVFSTTVQGYEGSGRGFVQRFLAWLNERFRACRH... | Function: Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of tRNA(Met), by using acetyl-CoA as an acetyl donor and ATP (or GTP).
Catalytic Activity: acetyl-CoA + ATP + cytidine(34) in elongator tRNA(Met) + H2O = ADP + CoA + H(+) + N(4)-acetylcytidine(34) in elongator tRNA(Met) + phosphate... |
A0A453NSU1 | PQGKFMSWLVLTPGSLFLSTFHNSICEWVIGYMFAYEATVSTRSRSLAKELTTAAVASVFLGFGSLFVLLASGVFV | Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in ... |
A0A453DM04 | GVAAFVGLCLVAVWMASSALVTPADFSPFQAPLWRRAAAPAEANAPPAAVREEETAADDQEPPVADRQQAGSTEKAKGADEQQSAAEKPEEKPDEKPKVKKVEAEVFPDAKDAELLNQTAAEPGSWRTQAAESNKETNERTNPSSTVPAASHSWKLCDVDAGADYIPCLDNVEAIRKLRSDKHYEHRERHCPEEAPTCLVPLPSGYRSPIRWPESRDQIWYSNVPHTKLVEYKGHQNWVNVSGEHLVFPGGGTQFKRGALHYIDFIQEAKKDVAWGKRTRVVLDVGCGVASFGGYLFDRDVLTMSFAPKDEHEAQVQFAL... | EC: 2.1.1.-
Subcellular Location: Membrane
Sequence Length: 563
Sequence Mass (Da): 62864
Location Topology: Single-pass type II membrane protein
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A0A2T2XE93 | MTKKTRSWYGHDYGLSFRMFFTMLLLAALYLGFIAVLVALHVGIPLLIVIIGALALSQYFFSDQLVLLSTGARRVTAQQAPELHKTIERLAQMADLPKPGIAIMPTRMPNAFTTGRNPKTAVITVTQGLLDRLDGPELEAVLAHELTHIKNRDVAVITIASFFAMIASFIVQQFFFFGFAMEEDRGRGRGNSGQAIMLIWLASIVVWAVSYVLIRTLSRYREYAADRGSAILTGHPGYLASALQKIHASMARSTQRDLRKAESFNAFFIFPAVRKNSFMEMFSTHPSLEHRIRYLEKLQSEIDNK | Cofactor: Binds 1 zinc ion per subunit.
EC: 3.4.24.-
Subcellular Location: Cell membrane
Sequence Length: 305
Sequence Mass (Da): 34278
Location Topology: Multi-pass membrane protein
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A0A345RBZ1 | MACSQQGFFCCLVAQISSKVSNVRQKIPIAATWFSLSPSVNLLMLQKTLLERPRMLRRALCILSLILIGLLVLNGPPVFAQSTDGSDQTRSPADEKLPSEDPTPSLTNAGEIDIDALAKEFNLPSHILDPRIESERLELLLLPLTETQLAAASEAWQRIVQEQTQDVVDATLRVNELDGETADVFRERVAELADERRHMFDNFVLVLNDWQKKGGSADEIAKYRAYRSAIIIDEIRNADVETLHQRVLKWLTARDGGIKVAIDSIVVVVSLLGLLFVARMIRSVTRRWMGRISGLSSLLSTFLGGLFYWLTLIIGLIIVL... | Function: Mechanosensitive channel that participates in the regulation of osmotic pressure changes within the cell, opening in response to stretch forces in the membrane lipid bilayer, without the need for other proteins. Contributes to normal resistance to hypoosmotic shock. Forms an ion channel of 1.0 nanosiemens con... |
A0A3C1FE28 | IVATQMLESMINSYRPTRAEVSDVANAILDGADAVMLSGETAVGDHAIDAVSVMSRIISRTEHGGLDKIRALDWNPHTTAGVISKAAVEVAERVNAKYLAAFTISGDTPHRLARLRSEVPIMAFTPLPKTAAELTLCWGVQSYVTPEYTDTDSMVASVQEALTSTGFLKRGDRVVIVAGNPGRTIYQTNSLRVYEMS | Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5.
EC: 2.7.1.40
Catalytic Activity: ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate
Sequence Length: 197
Sequence Mass (Da): 21241
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A0A7S3DAW5 | CRLKQTMAESAEAAHTSLGEGEERKEQPLSSNSVLDGDAVAKEKAETFINRIHKKPVVAIVIGMAGSGKSSLMQRINAYTNEHGTPSYFINLDPAVANLHYNANIDIRDTVKFKDVMKEYHLGPNGAIMTSLNLFATRFDQVVGILEQRKSEFSNVFIDTPGQIEVFNWSASGTIITETLANTFTTVVIYVVDTPRSNNPVTFMSNMLYACSILYKTRLPFVLAFNKCDIISDDTLREWMTDFEALHEALSEEETYAGSLTRSMSLVLEEFYRNLKGVGVSALTGEGMEDLFTAIGDAAEEYEQTYLADLKERIILKEKK... | Function: Small GTPase required for proper nuclear import of RNA polymerase II (RNAPII). May act at an RNAP assembly step prior to nuclear import.
EC: 3.6.5.-
Subcellular Location: Cytoplasm
Sequence Length: 395
Sequence Mass (Da): 44408
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A0A8J5GMY3 | MAAIFHLAFPSITGRQDHGRPSPGGRRSGASPIAELQQHSSSGGIARRSSISAHGTEPVPFHAFRTQECGPMGITAHQNSLRWLIWTTMGLFDSSYSSLLELQAMIRKFIQLVCGNASCEIQLAAKRSDLVNKMPEVQLGQKSEYLEEDGDRDSDGDGKGDKDGDSEGGGEEHSEEDNVGRENPNDANSNEAAGGDEDDDGGKPDGEDENEGEEPEDQDPNDNNEQDDDDDDDDDSGNAEDEGEEEEEDDEEEISDEGGGIPRSGLPKIFTYLYSTAKNPLEENDEGSSDGDQIAKICVSKVVADSMLPCRPDAESTGRN... | Function: May be involved in modulation of pathogen defense and leaf cell death.
Subcellular Location: Membrane
Sequence Length: 469
Domain: The C-terminus contains a calmodulin-binding domain, which binds calmodulin in a calcium-dependent fashion.
Sequence Mass (Da): 51819
Location Topology: Multi-pass membrane protei... |
A0A1B2PQZ6 | TLYFIFGIWAGMVGTSLSLLIRAELGNPGSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAXDMAFPRMNNMSFWLLPPSLTLLISSSIVENGAGTGWTVYPPLSSNIAHGGSSVDLAIFSLHLAGISSILGAINFITTIINMRINGLSFDQMPLFVWAVGITALLLLLSLPVLAG | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A8J5G9T7 | MNQEAREIPVLHDTEFILQQQNRNWSFLKCILFYIANSGVSQNAICSTPLWRNGPPEKPILCNACGSRWRTKGSLTNYVPLHAREAFNVSEVKAPSKITVFFKEKKLQKKKESNYILEGDREVQYPDQYCHKFAEGDTSNRSSSGSAISGSDSCVNFGINDASEITGSVQSNIWDSLMPSKKRTFLPRPKSSSIEKLTKDLHSILHEEQASNMSRTTEEDNLLYESGTPFDSSEIGYGGILIKHPYAKSVEEESEASSFSVDKLKTIKEGYSSSTSFPVNSKDKGASCTRSGMDTMKSTSQVSRDTDNSLKTMFSSSQFL... | Function: May be involved in both secretory and endocytic intracellular trafficking in the endosomal/prevacuolar compartments.
Subcellular Location: Membrane
Sequence Length: 768
Sequence Mass (Da): 86306
Location Topology: Multi-pass membrane protein
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A0A453IHJ5 | VCLFSSYHCPLYPQEKKDLSTVGDPFDAPTYNIPEKPVTFAEGASYSVVILAGLGVAALAGYSVFKELIFEPKEYKIFGKALARVQSDSQVTARIGYPITGYGNESRNRAARQRIPNRVWTDEDGVEHVEVNFYIRGPHGAGKVYSEMFKDNSDRTWKFMYLLVEFTASLQGQVMLESYIPA | Function: Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane.
Subcellular Location: Membrane
Sequence Length: 182
Sequence Mass (Da): 20408
Location Topology: Single-pass membrane protein
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A0A452YUK3 | MQMPFCPKLWDRSPVPPANAIAVNGTVVVANTFGLSAPGKSTTLRLFSGTQIDHETGKGKLSPEAPLRGGKKSKHGKTSTTTYHVTFVVDADFGTPGAVSVRNGNRADRFFLRHVRLELAEDRSIHFECNSWVYPYKKTAADRLFFVNTSYLPSKTPEALVLLRDEELRSLRGDGKGERKDWERIYDYDRYNDLGNPDNPEHVRPVVGGTRTHPYPRRCRTGRAISNTDGVTETRKHVINLDFYIPPDERFSPGKLEEVLKLGVQAVTHFVIPEARTLVHGNDFKSMEQLRKDLYSRPVQPAVDGEVMERLKSSVPSHKT... | Pathway: Lipid metabolism; oxylipin biosynthesis.
Function: Plant lipoxygenase may be involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence or responses to wounding.
EC: 1.13.11.-
Sequence Length: 611
Sequence Mass (Da): 69081
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A0A2Y9JXT3 | MGRENQTWMSEFILLGLSSCWDTQLSLFVLFLVMYLVTVLGNFLIILLIRLDSKLHTPMYFFLSVLSFVDICYTNSTVPQMLVHFLSAWKSIPFHSCVLQLLISLAMGSSEFFLLGAMAYDRYVAVCHPLHYTVIMHGGLCLGLAAGCVGAGFMNSMMQTIIIFQLPLCRNVINHFACEMLAVLRLTCVDISFNKVMVAISGFLVIMLPCFLVLFSYGRIVTAILHIRSAQGRCKAFETCASHLTVVSMCFGTAIFTYLRPTAGSSAEQEKMVALFYAVVTPMLNPLIYSLRNKEVMSALRRLLGKFSEKRPPAFSPKKC... | Function: Putative odorant or sperm cell receptor.
Subcellular Location: Cell membrane
Sequence Length: 360
Sequence Mass (Da): 40330
Location Topology: Multi-pass membrane protein
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A0A453D6G0 | YFLSLCWDRGGAMLIAAVYIAGAQYKNISHRPESTREISSSDDMAAGAAGGGSDELKLLGVWVSPFVHRVQVALHLKGLTGYEYAEEDLTNKSDLLLASNPVHTKVPVLLHAGKPVCESMLIVQYLDEAFPGSGPALLPADPHDRAVARFWAAYADDQFFASWIKAFVGTTDEERAAATEAAVA | Function: Is involved in the conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.
Catalytic Activity: glutathione + RX = a halide anion + an S-substituted glutathione + H(+)
EC: 2.5.1.18
Subcellular Location: Cytoplasm
Sequence Length: 184
Sequence Mass (Da): 19795
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A0A1I7XKP4 | MLFLYHLSLLIISSSALGSGLFRMRLSSKEGAMVKFCYTEWPANAPLRSDKKCFFNQYNFTIHANGHRVISRPFDNAINEFVAFTAIVMNSRGLFIGQVNERIAIDGLGLTRMVTVGGDVEITIGVECAKNLYGPKCMRYCNPKSGDHLQNYICSPLGEKQCNKGWTGIECETQHVQVSHTAAIIFESVTSRRFIIEMGSFILVILVGFLLVLLILNRRVNRLMNDPKTQNAINSRRNISRVAEIDSQDLNKVYIIGTKTFGSSNSFHYNSHYTAEPTDYSVPSCHSSSISTDMSIYDEIDSTGSNSLPLGKASDCKLSV... | Function: Putative Notch ligand involved in the mediation of Notch signaling.
Subcellular Location: Membrane
Sequence Length: 327
Sequence Mass (Da): 36390
Location Topology: Single-pass type I membrane protein
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A0A453FKN9 | MEFKVVSKTAALPAAWHGTSQGAQGRSSVAFGSAWRKASSRPARALFAATNNSAPVARVEKQRIDQSQILTLDSIRTSLIRLEDSIIFGLLERAQYCYNADTYDSDSFHVDGFGGSLVEFMVRETEKLHAKVEHPCN | Pathway: Metabolic intermediate biosynthesis; prephenate biosynthesis; prephenate from chorismate: step 1/1.
EC: 5.4.99.5
Catalytic Activity: chorismate = prephenate
Sequence Length: 137
Sequence Mass (Da): 15092
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A0A3N4UKK7 | MNLIAIVLALLLEQVRPVSEGNPMDRWIDRWFEWARCNFDAGQHHHGWLAWGAAVAVPALFVLSVHLGAQAVAGWPLALLWHVAVLYTTLGFRRFSHRFAEVREALEADDLARARQVLAQWRGEPSPEDTTELIRALIRQALIDGHRHMFGVLFWYVVVAALGGGPAGAVFYRLSDRLRDGLKRRGGEVVVESASLMRVAGQAWIWLDAVPSRVTALWFAMVGSFEDAIEVWRGLSEDWGEGSSDRLIVAAGSGALNLDLGAAKKEEGPEQSPAQGAGEFPRGWAMPEVGHLPQVVGLLWRSVVLWLLVLALLALGRLFG | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
Subcellular Location: Cell membrane
Sequence Length: 320
Sequence Mass (Da): 35271
Location Topology: Multi-pass membrane protein
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A0A1I7XBU8 | MQLILKQQFSFTFRLLTQIVIERKPKRRLVMRTEILLKNFDEKASTRTVHVYEPPVAPQKLMEAIEWMDDDMITLITPKLLGKRPNTYTLTKALAETLLVEDARQLPVVVIRPSIVGAMWGAPLPGWTDNINGPTGIFAAVGKGVLTNMCGSVVSKADIIPVDIVANMIIVGAAHRATTAYEEIPVMHCASGDLNPLKWEKVVNFLEQFYHKYPMDQCYAVPSTQFHTSRRLFELNYYLKHHIPAATMDMLNGLVGRKKSNVRLYGKVWKMIETLHYFTTHGWTFQSKALPRLWETLHPEDKKGSAIQWYAACKIFRVRL... | Function: Catalyzes the reduction of fatty acyl-CoA to fatty alcohols.
EC: 1.2.1.84
Catalytic Activity: a long-chain fatty acyl-CoA + 2 H(+) + 2 NADPH = a long-chain primary fatty alcohol + CoA + 2 NADP(+)
Sequence Length: 400
Sequence Mass (Da): 46084
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A0A378I812 | MKFLYEIFPIVLFFLAFKFYDIYLATYVGIIATAIQVIMTRLIQKKWDKVQLFTLLTFVVFGGLTLYLRDPIFIKWKPSIIFWTFALLILVSHFILKKSLLQFLISSMLKDGDNLPASIWNKLNNIWIIFFVLIGFLNLIFAYYFSTNAWVNFKFYGISLGVILISIIQTIYIRKWRKKLSQADAN | Function: Plays a role in cell envelope biogenesis, maintenance of cell envelope integrity and membrane homeostasis.
Subcellular Location: Cell inner membrane
Sequence Length: 186
Sequence Mass (Da): 21955
Location Topology: Multi-pass membrane protein
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A0A8J5HZF7 | MSKFAALFVVALLLLNGTLSRAARPAPADPSSNGRQLQPEAKEEEECGGGEEECLMRRTLAAHTDYIYTQNKQP | PTM: PSK-alpha is produced by endopeptidase digestion. PSK-beta is produced from PSK-alpha by exopeptidase digestion.
Function: Promotes plant cell differentiation, organogenesis and somatic embryogenesis as well as cell proliferation.
Subcellular Location: Secreted
Sequence Length: 74
Sequence Mass (Da): 8092
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D1A713 | MVTDKARDKARDATGIPDAAPSPSGGPPPWTLPAVTFALTVLLAWAAWAKVAQQWAGIAGGAALIALLGWAAATGRAADQMTTAAARAGLAVVLGWAGLAKATEPPALQELAVESYQLLPEGLITPVGVGLPILEIVLAALLLAGFATRFSGALSGLLMVVFIVGIASAWARGLKIDCGCFGGGGQIDDPPYLGEIMRDLGFLALAAWVAAWPPGRFALDRKIGLYQD | Pathway: One-carbon metabolism; methylamine degradation.
Function: May be specifically involved in the processing, transport, and/or maturation of the MADH beta-subunit.
Subcellular Location: Cell membrane
Sequence Length: 228
Sequence Mass (Da): 23366
Location Topology: Multi-pass membrane protein
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K2NVZ6 | MTTPVCYLCAAIGGEACRVAEGDTPLLAAADHTPLRPKAIDILWHLDGVCVCVNNWVQTCCTRLWSAKRSATDLRCARLLLLLRACLLLLVPFCFPCFLFLLYCRLVCTFAVHVGIVLNARNKLLTMLRQLRLLCSALLLLLCTGGGLVIAVPHHCVFDRLPRNVGEVTGREEPASPVTVSVGSDWAPLRIKVFADDLEGLGGFCTSAGEHINMFFGKEMVCQEEDILTEEKVDILENVILPEAAKMHGERLLVQPLDGPLVVP | Cofactor: Binds 1 zinc ion per subunit.
EC: 3.4.24.-
Catalytic Activity: Preference for hydrophobic residues at P1 and P1' and basic residues at P2' and P3'. A model nonapeptide is cleaved at -Ala-Tyr-|-Leu-Lys-Lys-.
Sequence Length: 264
Sequence Mass (Da): 28932
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D5JGH4 | HCGKIXIDESNPQFKEALRYREPKKRFDAIHRLCKPKLICEADAPDEDGEGDPDKAAKKPKHGGCGNIQPDIRKEGLRLIGSWKVPKGEDDEVDTKEKDKRPITPQQALNVFRSISTEDIRKIGLSNDYARPDWMIITVLPVPPPPVRPSIVMDGSSSGPRGEDDLTYKLGDIIRANANVRRCEVEGSPQHVVSEFEALLQFHVATYMDNNIAGQPQALQKSGRPVKSIRARLKGKEGRLRGNLMGNR | Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
EC: 2.7.7.6
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Length: 248
Sequence Mass (Da): 27686
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A0A7V6GN47 | MKKDYKDTLLLPKTDFPMRGNLGVKEVEIQAFWDEINLYEKVLKKNEGNTEFVFHDGPPYANGDIHAGTALNKILKDFIIRYKTMSGMYCDYVPGWDTHGLPIEVAVTKQGVDRKKLGKVEFREKCAAFAHAQVARQREQFMRLGILGRWFNPYLTLTPDYEARQIRLFAKMVERGLIYRGLKPIYWSPSSESALAEAEIEYHEVTSDSIYVAFPLVNVVGELKDAKLIIWTTTPWTLPANLATSVHPKLEYVLISTNKNKYIVAKSRLKDLTEILSFENVKILKTYLGEQLENLEYVHPIYQRTSPVILGEHVTADDGT... | Function: Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves ... |
A0A651DNQ7 | MKLKIVNQSTKVGDVDIVVIDNQKGLRVRLTSYGAAIHRIQMKNGNGHHDDVVVAPIDVNDFLVSDFYYGKLVGRTSGRLHAPSYQIADKQYPVTPFGGKTSKLHGGEKGFSFQHFTIEEQVVESDHASVTFRYFSQHLEEGYPGNLEVLATYTLDVHDRLTLDIKAKSDRDTLCNITNHAYFNMGLPKNKIYDHELMIKASRFLDIKPDFTLKAVRPVEGTPWDFRTPVRLGTAMEKMLDTPFGGFDHNWLFDDHGPETPVIDLYEPETDRGLQMFTTYPSVVVYTHNRLSSAYLRQVPGESHHASLAIECQYEPGGIH... | Pathway: Carbohydrate metabolism; hexose metabolism.
EC: 5.1.3.3
Catalytic Activity: alpha-D-glucose = beta-D-glucose
Sequence Length: 351
Sequence Mass (Da): 39950
|
A0A1F7JBW3 | MIKRMRLTTAIAFAKSAGYVSQLLNTGAGTTWAGKTSLTIFPKTISSLSQQLTHRIVVVGTNGKTTTTAMIAHILSTTGMRVVHNATGANLRNGIAGCLVRYSLATGHMNADVGVFEVDEAELKHVIHELDPTIIVMLNLFRDQLDRYGELDAIAREWNNAFSRVSKKTKLVANADDPLIAHIGEVSNRSVAYFGLSRGKKRHIADLTADSSYCISCGSKLTYEWISYAHLGKWSCGLCGRKRPHISVPHVTNPLAGTYNMYNSLAAFLACIQTGISVHSAQEALESFTPVFGRQESLRVKGRTVQILLSKNPAGFNESM... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: The lipid II isoglutaminyl synthase complex catalyzes the formation of alpha-D-isoglutamine in the cell wall lipid II stem peptide. The MurT subunit catalyzes the ATP-dependent amidation of D-glutamate residue of lipid II, converting it to an isogluta... |
A0A7X8V9V3 | TVDSFIRGADAMIKGEVILPITQHLLLKKIIPLEEIEEVLSHPQALYQCRGFLKEKMPYARLKEVSSTAEAAKFVSESENNIAAIGSISLSKIYDLKIAAESIQDSENNMTRFYILSTEDEMVTGRDKTALVFSTENKPGSLFRALKIFAEKGLNLTKIESRPSRRVLGEYIFLIEVEGHRLQEPLKSALKELELSASLFKILGSFPTFELS | Pathway: Amino-acid biosynthesis; L-phenylalanine biosynthesis; phenylpyruvate from prephenate: step 1/1.
EC: 4.2.1.51
Catalytic Activity: H(+) + prephenate = 3-phenylpyruvate + CO2 + H2O
Sequence Length: 212
Sequence Mass (Da): 23770
|
A0A8H5CZX6 | MLTTGTGGESIYGEKFEDEAFPVKHTKPFLLSMANAGSNTNGSQFFITVAPTPHLDGKHVVYGEVIKGKSIVRRIENNPTSSGDVPQAAVTITDCGELSPDDPSLTEQGVVTEGDPYEDYPDDEDRDLSKPETVIEIAKVVREVGNKLYKEGNVDQALEKYQKSIRYLDTFREIPEDSPEELKQAYNALLAPLLLNSSLAAIRSVPPSTSNAMIAIANATRALDTLELNTADKAKALYRRAMAHSIMKSEDDQEADLVEANKLAPQDALIPGELAKIKQRRAEQKEKEKKAYKKFFS | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
EC: 5.2.1.8
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Length: 297
Sequence Mass (Da): 32690
|
A0A1H8PTK2 | MTEHCRVDYDADGIAWLTLDVAGAATNTVHMAVLAELAELLDDIAAWSGLRGVVLRSAKPAGFVAGASNDELAAMGDLERVASLIDLGQAVTSRLYGLKVPTVAAIHGHCLGSGLELALGCRYRVADQGATTSLGLPDVRLGLHPCYGATARLPSVVGSWRALELMTSGRSLDAAAAKQLGLIDAAVPAESLADTALDFIARDPGRHRPRIWSQLVRLAPARWVTYRYLDAQLQRQARPENFPATYAILRLWRRAAGRRLRERFRAERESLLELIRKPSALNLVRTYLLQDRLRREARELDVAVPQVVHVIGCGAIGAGL... | Pathway: Lipid metabolism; fatty acid beta-oxidation.
EC: 1.1.1.35
Catalytic Activity: a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) + NADH
Sequence Length: 658
Sequence Mass (Da): 70954
|
A0A453CUI8 | AAMRPATFTAAQYQELEQQALIYKYLVAGVPVPPDLLLPIRRGFDSLASRFYHHHARTFRYLGRVFLLQSTRTLLHSPVRFARVVYWDREIQVYSTS | Function: Transcription activator.
Subcellular Location: Nucleus
Sequence Length: 97
Domain: The QLQ domain and WRC domain may be involved in protein-protein interaction and DNA-binding, respectively.
Sequence Mass (Da): 11341
|
A0A8X6J647 | MWYDRDIDLLMKRTKNRPIPSGRVLAESALEFGITLGILSVFIMAIAVNYISAALLAVSILFYVFIYTIWLKRRTPQNIVIGGAAGAFPPMIGWAAVTNSVSWESFILFLVIFMWTPPHFWALSLK | Function: Converts protoheme IX and farnesyl diphosphate to heme O.
Subcellular Location: Membrane
Sequence Length: 126
Sequence Mass (Da): 14240
Location Topology: Multi-pass membrane protein
|
Q5YLA4 | MNTDTIRAIFLYWISLALSMAAVVQLETKVDLSNHQSLVMMIAILLPALSVLFGLRVWRRWKVVIVKEVNPREVINLVGEPFLDPVRGVLMNGISTSGGTFEVLIEPKWWHLFPRSAISKDGEKECAIFNAGYSSVLPGTEPTSLVMLKAKDLAVGFGARVRFNGCSDYLLTAYHVIKPHEKLNLCKGGYMVEDVDLAVTCGSDHDAVDFALIKVPPAVWSKLKVGVGKLEPMTKKTHITVYGGSDSTRLLSSSGPAYKGKAGYAIIHEASTTKGWSGTPLYSGNTIVGVHTGSGQVGYSNRAVNVKLLLTAVSKFETIF... | Function: Covalently attached to the 5' extremity of the genomic and subgenomic RNAs. It may serve as a primer for the replicase.
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Subcellular Location: Host membrane
Sequence Length: 966
Sequence Mass (Da): 107623
Location Topology: ... |
A0A453PTF8 | MAAAMGSGFIAKGLTIINNAGPRKGQAVALRVGGDLSVVYQCDIEAYQDTLHTHSNRQFYTEDIISGTVDFIFGNSAVVIQNCDIRPRKHPFGQKDMITAQGRTDRNQNTGISIHKCRIAAASDLGDTKVYLGRPWKKYSRTVVMESSLDRSIAAAGWLEWSGQFALNTLYYGEYGNTGPGAGTSGRVKWAGVHTSLSTVDATRFTVRDFILGDSWLGDTGVSYTSGL | Pathway: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5.
EC: 3.1.1.11
Catalytic Activity: [(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O = [(1->4)-alpha-D-galacturonosyl](n) + n H(+) + n methanol
Sequence Length: 228
Sequence Mass (Da): 24712
|
H0BN67 | MTAPARLPDPAAPRPDELPLTETFGPTLQGEGPATGRTAWFIRFGGCNLSCSWCDSAYTWDSSRYQLREEIRHTPVGEIDAAVPDGALVVLTGGEPLLQQASTAWSRLLGGLRRRGCTLHVETNGTIAPNDRTRELVETFIVSPKLPNAGRHRGQQNPALHRGWSAAARDGQAHLKIVCASPEDVDTAVGIAHDHGWPDRQVWVMPEGTTASTLNARWPALADAAARYGINATHRLHVLAWGDKRGH | Cofactor: Binds 1 S-adenosyl-L-methionine per subunit.
Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
Function: Catalyzes the complex heterocyclic radical-mediated conversion of 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) to 7-carboxy-7-deazaguanine (CDG), a step common to the biosynthetic pathways of a... |
A0A436SGT0 | MIIVLGSINADQIGVVDRLPMPGETVLGSSFRTEPGGKGANQALAARRAGSEVALFAAVGNDPFAEIALTLLRRDRVDLAGVRMARVNTGIAMIVVDAAGENQIAVLSGANATVGEREIRQALDKCSDEDLLLLQLEIPVDAARHALELAKERSLRSILNVAPYVPETGSLAKLASIVVANQSEFELLLGLKPVNLDDEVLKLAAQNGQVVVVTLGNMGAVVSAGDKVVRVSAPSVQVVDTVGAGDTFCGYLAAGICEGESLDLAVRRAVVAASIACTSAGAQPAIPQAAEVECMMR | Cofactor: Requires a divalent cation, most likely magnesium in vivo, as an electrophilic catalyst to aid phosphoryl group transfer. It is the chelate of the metal and the nucleotide that is the actual substrate.
Pathway: Carbohydrate metabolism; D-ribose degradation; D-ribose 5-phosphate from beta-D-ribopyranose: step ... |
A0A8J5BBZ0 | MLEVLDNLPHDLLYSPNQVSPWMEVWLEKAKESLQISEVYKPIQDLLIAKCIKIIGLDEDHASGTNRLVSASRRIWSKAFPRPRRSWMPTGCLKLMEVLHSALPKMSLIASDFSYLPEVRIPGDRAPLVSSMVVSSIAVKVRMMDSSVYLILLATFVQWASCILPFGLLVVFSQELTMLASNLFVNLYKLMNRHGSGTNIAPNSKPWSVLQKGGRTTDYDSYLDAKGNADIFFPTDFWLLERIDHYTSVWSSEQKVSTPQKPLKKRRTIIVSSALAYISSAKALILIHPLSWMNLVCHQRRGQKMDTIHWSMTLRTLNFT... | Function: Arginine methyltransferase involved in the assembly or stability of mitochondrial NADH:ubiquinone oxidoreductase complex (complex I).
Catalytic Activity: L-arginyl-[protein] + 2 S-adenosyl-L-methionine = 2 H(+) + N(omega),N(omega)'-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-homocysteine
EC: 2.1.1.320
Subce... |
A0A1I7WJ27 | MLFDVVMLCSGILLSEACRFIEDIREKNIDFEIIGSGLHLHLLISAHIASINRFSECRILYELDIPKGAYIDSDSINSTLLEHSFFSDAQFNVEAPAGKSEDHKVYLLLSTSIRKKFVLEDRLKLPVHLRYHACRNTDGITEVATVVFNTPVIALDCPHDYQSLQLESCPGKREYKIAGLESKSPYWITVEPLEKRTATAIIPIGNCLLLPYIFCGTILTLLMGLYCICSAQKGSKLIHKAE | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Function: Essential component of glycosylphosphatidylinositol-mannosyltransferase 1 which transfers the first of the 4 mannoses in the GPI-anchor precursors during GPI-anchor biosynthesis.
Subcellular Location: Endoplasmic reticulum mem... |
A0A1I7WNX4 | MANKRGISALEQLRALSIRNSMDINRAEMVKPMTMVFDAYKDALRSLEDLVYVKVHRPLSVRQREGLAKETATTAAVKMLPSYVRAVPNGKESGDFLALDLGGTNFRVLLIRLHGREAEMSGKIFRVPENIMRGTGEAVSQSITLFDSIILHSICDCYCVITYCFTSL | Pathway: Carbohydrate metabolism; hexose metabolism.
EC: 2.7.1.-
Catalytic Activity: ATP + D-glucose = ADP + D-glucose 6-phosphate + H(+)
Sequence Length: 168
Sequence Mass (Da): 18747
|
S5ZYB3 | MNIDIYTDGACSGNPGKGGWAYVIINKDEDSELLRGSGADPLTTNNRMELSAVINALKKAQTEYGTNGLCFSVYTDSQYVQQGISSWIFNWKKNNWKTASKQPVKNQDLWQELDKLSASLMPKWFWVKGHAGNKYNEICDNLAVSAMKTV | Cofactor: Binds 1 Mg(2+) ion per subunit. May bind a second metal ion at a regulatory site, or after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
EC: 3.1.26.4
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Subcellular Location: Cytoplasm
Sequence... |
A0A8J5FCM9 | MRDVTVENSAGPSKHQAVALRVGADLSAFHRCSFVGNQDTLYVHSLRQFFYDCDVYGTIDFIFGNSAVVLQKCRLYARRPLPGQQNFFTAQAREDPNQNTGISVHRCQVKAAADLLPVQSSFLTYLGRPWREYSRTVFMKSFLDSLIDPAGWSEWDGSFALSTLFYGEYKNSGPGATTTGRVKWPGYRIINSSTEAKAFTLKPIAFGIVSSQFNMHILFAYIKKAACIGLRSNRNDDLENGVVEGRPISQGKEIFLEEHLLQAAHRYVLFNTVEIDPYIQMHIEELKQTDRRFSNRIQWLAHGPRKHVISYTGYIINGHR... | Pathway: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5.
EC: 3.1.1.11
Catalytic Activity: [(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O = [(1->4)-alpha-D-galacturonosyl](n) + n H(+) + n methanol
Sequence Length: 489
Sequence Mass (Da): 55636
|
A0A8X6IIJ1 | MKYYKDAYEQIFNATLKSNSTTSDNLINPTNSMENISIPLKLVHATIWNSETVDELFAESSMCIRGLYLLILVASAPHSIEQRSIIRKTWANPMNNRIYGFHVKTIFMVGRASSHFNKMLLQAESEISKDILVGDNYYSYHNLTLKTIEGLTWAYTNCEPTYILKTNDDCFINVQLLVNFLSTQNPIKKKLYVGHVRWASHIARKLNRQRYLSVKNFPKSRYVPYVEGSGYIMSYDVLEKFVQYSELFEPFPNEDAFVGTVLHMAGVEPTFSARFISHSDSWQKCNFLYVFVIHHVWLLRQFELDKMASDAWDECPRDQM... | EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 324
Sequence Mass (Da): 37744
Location Topology: Single-pass type II membrane protein
|
A0A7S3G6P3 | KKRHRGKLDHYVNAETLKPLDNNFEYPFHLSIVVKWRNQLKSNSHVWLAEFFVKDSFENTTSIPRAVLLTDCGILYDRGCIKNLYNEFSRDGWVMAVCGRQRVMTIREQEQLDNIDENYNPIAMASGFCDQLRLLISPMKTLKSPWQALLRGVQSYDFDYGHAISKSAWNLVGWQPVLPGPCGMYSIKAFQMGEKGQSSVFDQYIDILLIKEKEDAMRRVGLLYWHLLLAEDRIPSFLAVFGDMPKGMKTIWVRNAAFAYEAEVKLRQFVLQRKRWILGTLVGFLYLFNGREGRSFIFRKHLNCFRKFMLLIYMILQVVD... | Catalytic Activity: [(1->4)-N-acetyl-beta-D-glucosaminyl](n) + UDP-N-acetyl-alpha-D-glucosamine = [(1->4)-N-acetyl-beta-D-glucosaminyl](n+1) + H(+) + UDP
EC: 2.4.1.16
Subcellular Location: Membrane
Sequence Length: 354
Sequence Mass (Da): 41284
Location Topology: Multi-pass membrane protein
|
M9V7Z1 | YYTPEYXTKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYGIEPVPGEEXQFIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPTSYIKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNS | Cofactor: Binds 1 Mg(2+) ion per subunit.
Catalytic Activity: 2 (2R)-3-phosphoglycerate + 2 H(+) = CO2 + D-ribulose 1,5-bisphosphate + H2O
EC: 4.1.1.39
Subcellular Location: Plastid
Sequence Length: 185
Sequence Mass (Da): 20467
|
A0A1H8RPU8 | MAVEIPAFELQLPFEIGVEPPVIGEEPAWWFVFQDSNLVLERIDERRVRPLFQRQDPRPDSPPPDTAHFLGRLDGIPCFAADLHGGLPDTTLIARGLFVLHHRMDTDLFLLAGRAFQILEWDRKHRYCGRCGTPTERATTQRARICPNCEFTQFPRLTPAMMVLVRRGRQLLLAHAPRYPDGFYSVLAGFTEPGETLEACVRREVREEVGLEVRNIRYFASQSWPFPHSLMVAYVADWASGEIRIDDEEITHADWFDPDNLPDIPGEMSIAGHLIRWFVEEQRAGNTEPGPS | Cofactor: Divalent metal cations. Mg(2+) or Mn(2+).
Function: mRNA decapping enzyme that specifically removes the nicotinamide adenine dinucleotide (NAD) cap from a subset of mRNAs by hydrolyzing the diphosphate linkage to produce nicotinamide mononucleotide (NMN) and 5' monophosphate mRNA. The NAD-cap is present at th... |
A0A7V7C340 | MAYGGWARFLRKVLEPFRILRRLPEAFRKGKARGRGALLAGTAFLGGGRFFTGEIGRGLLLLLLETGAVLYYVFFGIPLLQGKISYPKLGLEAVSVILVPVLLYFYLRELALILLTVEREEYRETRIPWFFAELRSKLLGYFRIWKEASPKERFELASPFFLMGYFQFRKRAYVKGAMLFLVEVGFIFYLAATGIYDLVDFVRLETDFRPSTFNLVYGFVAFAVILVFLNIYIKNIKSVTKAVKGELAFKPFKEEIREFLDNKLYATFLAFPVLGVILFTIVPLVFMISIAFTGYEGASQNFVWTGFQSFKNLVLVRDNL... | Function: Part of the ABC transporter complex MalEFGK involved in maltose/maltodextrin import. Probably responsible for the translocation of the substrate across the membrane.
Subcellular Location: Cell membrane
Sequence Length: 562
Sequence Mass (Da): 64203
Location Topology: Multi-pass membrane protein
|
A0A453QHE8 | SSTISTLRANHCPGGNKQIRAESLAAMALKVSFPGELAGAAILESPRSGAFRHLRQAVDFTFRKRDKRAAFLRMTCCSMQQGPLPAWPGRAVAEPERRSWDSPKPISIIGSTGSVGTQTLAIVAENPDKFRVVALAAGSNVTLLADQVKMFKPNLVAIGNESLLNELKEALADCEYMPEIIPGEQGVIEVARHPDAVTVVTGIVGCAGLEPTVAAIEAGKDIALANKETLIAGGPFVLPLAHKHNVKILPADSEHSAIFQCIQGLSEGSLRRVILTASGGAFRDWPIERLKDVQVADALKHPNWKMGKKITVDSATLFNK... | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 1/6.
EC: 1.1.1.267
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + NADP(+) = 1-deoxy-D-xylulose 5-phosphate + H(+) + NADPH
Sequence Length: 328
Sequence Mas... |
A0A453MMN8 | TDNLKVRDSIRLYAWLSHGCIFDCVTTFYRKTLGKREGDCVRACVRKYQL | Function: Mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer me... |
A0A8J5HQW8 | MASMEPDSNSKQPKSWTFSAWFPARDAAAGEIEDPREPLIHGDGSGDSYSVAAAILPFLFPAIGGLLYGYDIGATSGAKISLQISASHAAVIEPYDRDLIHTGLRIEILYGYYGRLASRSGLAWKTGIEVGADVIDSDYRGEVQVLLFNRTNLPQQQKIAQLILEKIAIPEVYEVPHLSYT | Pathway: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2.
Function: This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA... |
A0A453A0F5 | VQIKEAIISHGCFLRECKIEHSIIGVRSRLNSGSELKNAMMMGADSYETEDEISRLMSEGKVPIGVGENTKISNCIIDMNARIGRDVVISNKEGVQEADRPEEGYYIRSGIVVIQKNATIKDGTVV | Pathway: Glycan biosynthesis; starch biosynthesis.
EC: 2.7.7.27
Catalytic Activity: alpha-D-glucose 1-phosphate + ATP + H(+) = ADP-alpha-D-glucose + diphosphate
Sequence Length: 126
Sequence Mass (Da): 13856
|
A0A8J5LE32 | MNMKHILKILALLVVVAATWITLLETSVVPHHYTWLLPVYLVVSLGCYGLLMVGVGLMLFPTCPQEAVLLQKDIVEAKEFFGRRGVDVGSD | Pathway: Protein modification; protein glycosylation.
Function: Stabilizer subunit of the dolichol-phosphate mannose (DPM) synthase complex; tethers catalytic subunit to the ER.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 91
Sequence Mass (Da): 10082
Location Topology: Multi-pass membrane prot... |
A0A453BZQ9 | SSHADISIDIRPEFNSFDHLRSTGYISTDRPWLKLYGIRVPPVSPFNSLTSTPDLALIHQCLPDELLIEIFGRMSPYTLGRAACVCRKWKYTTRNPTLWRNACLKTWQRNGIEANFRMVQSLYDSSWRKMWVQRPRIRIDGLYVSRNTYIHTGITEWQFKKTVNVVCYYRYLRFFPTGKFLYKIEMALLYPGHRYTLVRMRLRVRGTTIGANNRLDVLKILTTGVNGTELGNWKGNILELVEDWEENETHDPDVPAVSHSRGLTPFVFVPFEEADTSVLNLPVEKMDYFVPG | Pathway: Protein modification; protein ubiquitination.
Function: Acts as a component of a SCF E3 ubiquitin ligase complexes.
Subcellular Location: Nucleus
Sequence Length: 292
Sequence Mass (Da): 34019
|
A0A8J5HEM6 | MTTSTSIDLNLDRKEMVILGTQYAGEMKKGLFGVMHYLVPKRNILSLHSSNNMGKDGDVALFFGLSGKCWLDEILAHHLPIACVFAIWLLCSYDFCFVSENGISNIEGGCYAKCIGLTKEKEPDIWNAIKFGIGKCPIKLDMHFELEPFIFFCPNVCKFLAVLENIIFDEHTREVDYSDNSITENTRASYPIEYIPNAKIPCVGLQPKNVILLACDAFGVLTLVSKLTLPQTMYHFISGYTALIAAAALDDDKKDDSSNERTSGWLGRWRSGCCGSAGEDGQRPRRAGQPRGDRVAEALEAEPEIVRAVRQSPVGGGGQG... | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
EC: 4.1.1.49
Catalytic Activity: ATP + oxaloacetate = ADP + CO2 + phosphoenolpyruvate
Sequence Length: 386
Sequence Mass (Da): 41827
|
A0A1I7XRF4 | MRKFIKNMEQRRVGELNDERITHESLTLFNYRYRIDLFRVCFDEDEKRKLPGCLWTRPFPYFQPFPVVRFTFQQDNATITPVEVPRLGLRTIKRGHWANPRTLQTDPMENFCAILVHRINADNHLFEIVKGLKSVISKVDKSYELSRIEGILGTPEKPLSDLGLASYRSYWAYGIVEYLRGMMDMSSVSVSELSNTLGINRSDVADTLEWLHLVEAGMAESTPFCVTLKQVDALRTTVARAPRLMLNSRLIRWKPGET | Catalytic Activity: acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-lysyl-[protein]
EC: 2.3.1.48
Subcellular Location: Nucleus
Sequence Length: 258
Sequence Mass (Da): 29903
|
Q0CCD4 | MFTDTISFSPSTLPSNYSPPPRAQQIPPRDADIIIVGGGVAGCSAAVAFGKQGRRVLLFEKSLKEPDRVSGELLQPGGVKALNRLGLGTCLEGIDAVPCYGYWVSYKGESAQIPYPERADRPGTREEGRSFRHGKFVQKLRQEAMNTANVTVIESKVKDVIRDWTGARVLGVITEAASGERKYRHFFASLVLISDGYASTFRKRFLPNKPSIRSKFWALKLERAELPCSNYGHVVLSNHPPILLYKIDDTTTRIFIDVPTGLPSASPKAGGIRAHMLNVVLPVLPPRCQQSFREAVDRGKFLSMPNCYLADSEQTTPALL... | Function: Catalyzes the stereospecific oxidation of squalene to (S)-2,3-epoxysqualene, and is considered to be a rate-limiting enzyme in steroid biosynthesis.
Catalytic Activity: O2 + reduced [NADPH--hemoprotein reductase] + squalene = (S)-2,3-epoxysqualene + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]
EC: 1.1... |
A0A7S3DGF3 | SFSFPFAHAQHTQHAFSRSQWVKQQSKPRCAAVMVENTSAQPKQDLVSAQHTADRFSLSKPIDAILSKLFPIICFQTPVHTFLAWFALSYVMPRTYYWSSLAVFFSYPHINLKLAELGILKREWPAMKGLAPYFLRHCVRYFPLTPFKSAELDPEKRYMFAYHPHGVYCFGMYTMIFREVSGWDSLFPRMRPVHPFVASSLLSLPLLGDILSWWGYKSATRANIVKNFKRDRNSIIIPGGIAEMMMQVKAKNNEEVVILKKRYGFIKVALLTGAHIVPVYGFGENETFKRVHFMQETLTWLSRKLRVTLQPFLGRYGTFM... | EC: 2.3.1.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 379
Sequence Mass (Da): 43866
Location Topology: Multi-pass membrane protein
|
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