ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
I1L3N3 | MLCKPPLKCLKIVIMANLLTMFFVMEMIIVSGLSFGASGLNMNYYLLSCPFVEPVVKNTVNRALQDDPTLAAGLVRMHFHDCFIEGCDGSVLIDSTKDNTAEKDSPANLSLRGYEVIDDIKEELENQCPGVVSCADIVAMAARDAVFFAGGPVYDIPKGRKDGTRSKIEDTINLPAPFFNASELIKMFGQRGFSARDMVALSGAHTLGVARCSSFKHRLTQVDPTLDSEFAKTLSKTCSAGDTAEQPFDSTRNDFDNEYFNDLVSNNGVLTSDQTLYNSPQTRNIVNAYAMNQALFFLDFQQAMVKMSMLDVKEGFKGEV... | 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. These functions might be dependent on each isozyme/... |
A0A0R4J2Q8 | MAMALPLRRLSSTLNKPLASATSIYHRMSSSLSAQEKDKSRADWIKQLNDPLETIDPEIADIIELEKARQWKGFELIPSENFTSLSVMQAVGSVMTNKYSEGYPGARYYGGNEYIDMAETLCQKRALEAFRLDPAKWGVNVQSLSGSPSNFQVYTALLKPHERIMALDLPHGGHLSHGYQTDTKKISAVSIFFETMPYRLNESTGYIDYDQLEKSAVLFRPKLIVAGASAYARLYDYARVRKVCDKQKAVLLADMAHISGLVAAGVIPSPFDYADVVTTTTHKSLRGPRGAMIFFRKGVKEINKQGKEVLYDYEDRINQA... | Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
Function: Interconversion of serine and glycine.
EC: 2.1.2.1
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine + H2O = (6S)-5,6,7,8-tetrahydrofolate + L-serine
Sequence Length: 514
Sequence Mass (Da): 56942
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A0A4U9HQI5 | MGPVMLDVEGYELDAEEREILAHPLVGGLILFMRNYHDPAQLRELVRQIREASHHRLVVAVDQEGGRVQRFREGFTRLPAAQSFAALLGLEEGGKLAQEAGWLMASEMIAMDIDISFAPVLDVGHISAAIGERAYHEDPQKALQIATRVIDGMHEAGMKTTGKHFPGHGAVTADSHKETPRDPRPQAEIRARDMSIFKSLISDNKLDAIMPAHVIYPDVDPRPASGSPHWLKTVLRQELGFNGVIFSDDLSMEGAAIMGSYAERGQASLDAGCDMILVCNNRKGAVSVLDNLSPIKAERVTQLYHKGSFSRQDLRDTARW... | Pathway: Cell wall biogenesis; peptidoglycan recycling.
Function: Plays a role in peptidoglycan recycling by cleaving the terminal beta-1,4-linked N-acetylglucosamine (GlcNAc) from peptide-linked peptidoglycan fragments, giving rise to free GlcNAc, anhydro-N-acetylmuramic acid and anhydro-N-acetylmuramic acid-linked pe... |
A0A0G4IMP4 | MLSMPGVVIYGDDGQMLRGTALRKALREELAKLEAGTGEERRPSSPPASGAKEPEGEPLDDELPIIVDDASDEKDDEKDDGELDEVLVDKQAEAYEDDDTQGSDEGRDRNFRYRSITQASPFKWRATAPRLAFDRNNTILIVVTMYNEEQDELSLTLRAISRNIKHMCKILKRSALWKSVAVCIVSDGRAKANPATMKFASSLGILSVSTMEQAPKNTAVHLFESVIRLVDDEAAGTLLPPLQVVFAMKEQNRGKLHSHLWFFEGFAHVMKPKFTFLLDVGTLPQDSAFLGFYRALDASTNIAGVCGRMKTRHHGIVDYL... | 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: 903
Sequence Mass (Da): 100687
Location Topology: Multi-pass membrane protein
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D7R6D7 | VLFQHLFWFFGHPEVYILIIPGFGAISHIVASYSNKPEPFGTLGMIYAMLGIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATIYGSKVKYDTPMMWALGFIFLFTVGGLTGILLSNSSLDIMLHDTYYVTAHFHYVLSMGAVFSMFAAFTFWFPLFSGVTFHSRWSKAQFILMFIGVNLTFF | 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... |
A0A0G4ITA0 | MAPSIEEWWAEIPPVTKALMIAAIGTTAVVSLGIVHPADLYLDTHAVVRHVQVWRLLTCFSFLGTIGIGWFLQLYIISKYGATLEKEYFRGATSRADFVFMLVFSASVLVLASLVVPGLYFLGPSLVTVLIYVWSRSDPHIPVTFFGFRFQAWQVPFLLMVFHVLMGGSALPDIVGILAGHAYYFSTTVVPRAYGVTLVKTPAFLIGQLAQEGPARAGMSWRRTGQGHRLAD | Function: May be involved in the degradation of misfolded endoplasmic reticulum (ER) luminal proteins.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 232
Sequence Mass (Da): 25579
Location Topology: Multi-pass membrane protein
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A1X4J0 | ILVGMWSGVLGLMLSVLIRMELAEAGKYIMDSHIFNVCVTSHAFLMIFFFVMPTMIGGFGNWLLPLMLGAPDMAFPRLNNLSFWLLIPSLFFLLMSSVLGDGVGTGWTVYPPLSSELGQPSVSVDLSIFSLHLAGASSIMGAVNFISTVINLWVEKSKYDLMSLFCWSVVITAVLLLLSLPVLAGGITMLLLDRNMNCSFFDPIGGGDPILYQHLFWFFGHPEVYILILPGFGLISQIILFESGKKQVFGTIGMIYAMMAIGVLGFVVWAHHMFTVGMDVDSRAYFTSATMVIAVPTGVKVFSWLATSFGSRMSFTTSML... | 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... |
A0A0G4IS01 | MDASDHDVVAPPESAPDVPSPKSLSDDVFVGKESPVASSKDKCDEPVDEKKGAAIEIAADGAQALNEIETGAGDSDNQKEPSSNPDSLSPDRVSNQFVARHDANIGEKVDITPQRAALYKDTGEEEIHEPPELVSDTVQREPDIVRQTRQASVGQSSHDPRKSLSVVVVELSATRAVQTPLSMSKFSLQSGYYGMQGRRPTMEDFHAQIQHPEFNNLVPAVDLDGRQRHFFAIYDGHGGPWCAEYCSRTLHQNLIRNPLFKDDSKKALHDAVVETDDTFCALIRDKGLSESSGTTAIVAYIVDDLLLVANVGDSRAVMCR... | Function: Enzyme with a broad specificity.
Subcellular Location: Membrane
Sequence Length: 497
Sequence Mass (Da): 53797
Location Topology: Peripheral membrane protein
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A0A811ZTY7 | MPTAWATPGAPEAPPCANQSCAPSELVLLGFAHVPALRPLLATLFLAMFLLTLLGNALIVLLTALDPALRAPMYLFLRHLALVEMCFSLDIVPRLLLTLLRPGRGVSPAGCALQLLLVLSCVTSECFLLTTMAWDRYVAICRPLRYGAIVSPRLCHLLAATCWLAGVPVSLVFTIWLFRFPFCGPRGIRHFFCDIAPLLSLVCADTRVFEAHVLAATVLVIMVPFCLIAASYTKILATVLRMPSARGRHKALSTCASHFVVVLLFYGTTGVIHLRPKASYSPESKQVVSLSYTLVTPMLNPLIYSLRNKEVRAALGRVCC... | Function: Putative odorant or sperm cell receptor.
Subcellular Location: Cell membrane
Sequence Length: 329
Sequence Mass (Da): 35862
Location Topology: Multi-pass membrane protein
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U6IZ32 | MDIIGEVPQERDESKFENLLKPIRLKYQSVIDKSNPYTKTRWCITFAFLALYVLRIYFIQGFHIISYALAIYILSLFIHSISPQVDPEFADLLDEAPTLPRTEADEFRPFIPRLLEAKFWYYATRAIIISLLCTFFSFLDIPVFWPILVVYFILLFTVMMKRQIKHMITHRYVPFSYGKPHPTGKVLVS | Function: Involved in the retrieval of endoplasmic reticulum membrane proteins from the early Golgi compartment.
Subcellular Location: Membrane
Sequence Length: 189
Sequence Mass (Da): 22309
Location Topology: Multi-pass membrane protein
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A0A0G4J7Z7 | MTQVTVTQPEKKRRRRNKAKAATAPSETQQENVGQKEALPEPASGGGEVPAETVGVAGDQVQSGDATAPQPAKKRRRGTRGKSQAVAGREAEPEAPNNVNQSGPVEEADPEPVNDGNENAQNEEDVKGAEGPSADVDDTSRNVNPADVALDYDFGSLELSTATRSALTDIGYERMTEVQARCIPLLLSGADVLGAAKTGSGKTMAFLIPAVELLYKAEFKPRNGTGVIVITPTRELALQIYGEARKLLKYHSQTHGIVIGGGNRKQEEDKLKRGVNVLIATPGRLLDHLQNTNFTFKNLIGLVIDEADRILEIGFEQELR... | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 630
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): 69558
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A0A6G1EL41 | MSAILAASLAGAAGLLALVGVAIFLIVLFLRHRRRASDSSESSSSGPAQPEQQGARCMTLEELSSATRNFSNVNLIGHGMFGEVYKGLLQDGTIVAIKKRHSPLSHEFIQEVNYLSSIRHRNLVNLLGYCQENGMQMLVYEYVPNGSVSTHLHGAELPTIK | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
EC: 2.7.11.1
Subcellular Location: Cell membrane
Sequence Length: 161
Sequence Mass (Da): 17479
Location Topology: Single-pass membrane protein
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U6JJS2 | MGLKRLNVIAAVANNGGIGKENKLPWKIREDMTFFSRITSTAQEGKKNAVILGRRTWLSFPPKFRPLPSRINVVVSTQLESVPEGTHLVKSFEDSLHLLESLIDSGQVDEVFIIGGHGLYKEALEQEVYPVRLYYTHIMKDFDCDTFFPSVDWERFKPIQLDTVDSDLRHSGDIEFRFAVYEKQPHPLNDH | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1.
EC: 1.5.1.3
Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH
Sequence Length: 191
Sequence Mass (Da): 21917
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V6CKR0 | MGKIMLVLGSLIGLCCFTITTYAFSPSGWTNAHATFYGGSDASGTMGGACGYGNLYATGYGTRTAALSTALFNDGASCGQCYKIICDYKSDSRWCIKGRSVTVTATNFCPPNFALPNNNGGWCNPPLKHFDMAQPAWEKIGIYRGGIVPVLFQRVPCKKHGGVRFSVNGRDYFELVLISNVGGAGSIQSVFIKGSKTGWMAMSRNWGSNWQSNAYLNGQSLSFRVTTTDGETRVFQDIVPASWTFGQTFSSPVQF | Function: Causes loosening and extension of plant cell walls by disrupting non-covalent bonding between cellulose microfibrils and matrix glucans. No enzymatic activity has been found.
Subcellular Location: Secreted
Sequence Length: 255
Sequence Mass (Da): 27538
Location Topology: Peripheral membrane protein
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A0A813TF02 | MVPFLMSKLDSNSSQSEISNQDEVLSHRLAQKIEPSNNADKAAEPHGLQPRMSDSLGNYEPRDQPTRTGPGEGGVPVILSPAEEQAAQKTISQYGFNMIASDKISMDRSIKDTRPAECKNWIYPEPRYLPKASVILVFFDEGWSVLLRTVHSVINTSPKELLKDIILIDDGSSDPDSKERLEKYIERWNGLVKLYRTGERVGLIAARTLGAEKSTGDVIVILDAHCECVTNWLPPLLTRIAMNRRALAVPIVDGLEWKTLEHTNIYGSSNFRGIWEWGFLYKETEVPAQELKKRKHQSEPYWSPTHAGGLLAIDRQWFFE... | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 572
Sequence Mass (Da): 65481
Location Topology: Single-pass type II membrane protein
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A0A0G4IRI0 | MAGDWTQSSLNAMTADALRELCRDCKLSSSGRKSELVARLLQHKQSRGVAGTIASRKGVSEIEAIRRPSLEEKRVLPPEQRILPTRRQSPRRPVQTVNLNETVPMKVETRSVRQVSSVPVPAPVPEPVEPAARSPIAVKQEQGPIVSEEQEPIVSEEQEPVFQENQDPPAPVAVRQELSVTTSGHVEDRMEEDHFTAIPTETAPPSCISVAFVCHSNLNRSMEAHHVCRLADPFGNQGATLFSFGAGGRVNLPVPVASAAMSFEFGSATYLDMFNYLSTSDNEEFYRKMGVLDMLQRNMGVKEMPERWQLEGRHFDLIVS... | Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
EC: 3.1.3.16
Subcellular Location: Nucleus
Sequence Length: 402
Sequence Mass (Da): 44677
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K7LP51 | MNNSSGGGGRGTLMGLSNGYCGRSPFTVSQWQELEHQALIFKYMLAGLPVPLDLVFPIQNSFHSTISLSHAFFHHPTLSYCSFYGKKVDPEPGRCRRTDGKKWRCSKEAYPDSKYCERHMHRGRNRSRKPVESQTMTHSSSTVTSLTVTGGSGASKGTVNFQNLSTNTFGNLQGTDSGTDHTNYHLDSIPYAIPSKEYRYVQGLKSEGGEHCFFSEASGSNKVLQMESQLENTWPLMSTRVASFSTSKSSNDSLLHSDYPRHSFLSGEYVSGEHVKEEGQPLRPFFNEWPKSRESWSGLEDERSNQTAFSTTQLSISIPM... | Function: Transcription activator.
Subcellular Location: Nucleus
Sequence Length: 341
Domain: The QLQ domain and WRC domain may be involved in protein-protein interaction and DNA-binding, respectively.
Sequence Mass (Da): 38022
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A0A068WAJ6 | MMNSQMLNRSREKKLWCSLSVVMTSVPRFSSTVKELRILFSPVNASSAGVREFIGKSYVGLRNSNPGVKFMLREGNSISPRIYARYGFGKESFVSVDNASPTEIMDKICKLAKA | 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.
... |
K7MJX3 | MNRTPKRGFSLIDFGCRDFKARISRSGNDVVGGEKAWEVGIHMADVDDAVAPLHYRFSPHRNRASLSEPLLPRVPLTVSSSSFSMLSGTHYMRLHIWNMDDVHNYYHSLITFDFVAPSTFFAESKPWMDKRVLKNVASTRPLSARIFKAIADPPTTSLQRLKGLTTGGLPTFVDVGNSFSAPAIVEDNFINQKVVMMGDDTWTQLFPHHFERSYPYPSFNVKDLHTVDNGCIEHLLLSLYEEDWDVLIAHFLGVDHAGHIFGVDSTPMIEKLEQYNTILESGPGSSHENTMLVVMGDHGQTLNGDHGGGSAEEVETAIFA... | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 568
Sequence Mass (Da): 63494
Location Topology: Multi-pass membrane protein
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K7LFK3 | MSKDKDATNLSRTFKYLLATQFLSRGIPFIFNTWIVRHLTQEDYALYAVQFHLLVTCILFLSREGFRRACLRMDLKCDGSSMGDVVKLMKVVWMSFPLGIFITIVVCLFVFWWQQISYSSPHGQAILINGFACILELLAEPVYILSQNLVLLELRLMVETVATLSRCLTMYFLIVKQTGMEKSIIFALSQSAYGACLFLGYWGYLLLSQKFRVSYLFPFREGKMIDFDQQLSKMCILFTFQSFRKLILQEGEKIVLVWLDTPYNQAVYGLVDKLGSLVVRLVFLPFEESSYVTFARSASGQYPGKSKKLGNSLTESLKLV... | Function: May be involved in N-linked oligosaccharide assembly.
Subcellular Location: Membrane
Sequence Length: 376
Sequence Mass (Da): 43046
Location Topology: Multi-pass membrane protein
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Q9XK92 | FGSLLGICLTTQIITGLLLATHYTADSTLAFTSVSHTCRDVQYGWLIRNLHANGASLFFMCIYLHIGRGLYYGSYLYKETWNTXVLLLLTLMATAFVGYVLPWGQMSFWGATVITNLFSAIPYIGQTLVEWAWGGFSVDNPTLT | 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... |
K7KHK1 | MLVDEWLHADDGYYKRPRGGQNQYGYNNNGEHVLNIPPPPGAGWGAAPQPPQMISSDMSNSSFSGSHGPVLPPPHPTVALGFNQSSFTYDELSAATGGFSQRNLLGQGGFGYVHKGVLPNGKEIAVKSLKSTGGQGDREFQAEVDIISRVHHRHLVSLVGYCMSESKKLLVYEFVPKGTLEFHLHGKGRPVMDWNTRLKIAIGSAKGLAYLHEDCHPRIIHRDIKGANILLENNFEAKVADFGLAKISQDTNTHVSTRVMGTFGYMAPEYASSGKLTDKSDVFSFGIMLLELITGRRPVNNTGEYEDTLVDWARPLCTKA... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
EC: 2.7.11.1
Subcellular Location: Cell membrane
Sequence Length: 461
Sequence Mass (Da): 50305
Location Topology: Single-pass membrane protein
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A0A0R0GV98 | MKQSEATSLAARKRGKWGYIWPMWTSLLLHLLAILLFTTGFLLTRTELPYHSHCSDVSHSPCFSSNNNGSCWTKPATNRLLIIVLDALRFDFVAPSTFFAESKPWMDKLRVLKNAASTRPLSARIFKAIADPPTTSLQRLKGLTTGGLPTFVDVGNSFGAPAIVEDNFINQLVQNGKKVVMMGDDTWTQLFPHHFERSYPYPSFNVKDLHTVDNGCIEHLLPSLYEEDWDVLIAHFLGVDHAGHIFGVDSTPMIEKLEQYNTILERVIEVLENQSGPGSSHENTMLVVMGDHGQTLNGDHGGGSAEEVETAIFAMSFKKP... | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 949
Sequence Mass (Da): 105572
Location Topology: Multi-pass membrane protein
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K7LMQ5 | MSVPPPLAAVMWMSFMVAQWPWLEHQALIFKYLKAGLSVPLDLLLPIYKSLQLMSSHPSMGYYGKNSWKRLPI | Function: Transcription activator.
Subcellular Location: Nucleus
Sequence Length: 73
Domain: The QLQ domain and WRC domain may be involved in protein-protein interaction and DNA-binding, respectively.
Sequence Mass (Da): 8405
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A0A2A2L7D0 | MARRYDSKTTIFSPEGRLYQVEYAMEAISHAGTCLGIMAEDGVLLAAEKRNVHKLLDDSVLNEKIYRLSNNISCTVAGITSDANVLINHLRWWAANYRLRFGEEMPVEQLVQELCNEKQRFTQRGGKRPFGVSLLYAGWDKHYGYQLYQSDPSGNYTGWKATCIGNNHAAAVSLLKQEYKEQSLEDAKKLAIKVLWKTLDVKLASEKIEMAVLKRKDGKTVLEELTDKELETLIAEHEKKEKEAETMAEKMPTPSDQTELAFLRLLERTKKLCDNVETNAHKIQAAAGQLEALLNKMHELNKAESNELVQYTRELNQLRI... | Function: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity.
Subcellular Location: Endoplasmic reticulum m... |
C6TMF0 | MANYGTTQRIPTSSTPQSTADTYEPEPKAPHEKFYSDFRIYCPINIPSTSEAAGVRIMRNMCNFGLYYTLFVWIILFITLIPQRKVSLILFVIMTYVTTLYFLLLRAFPNSVVLHRIIDKRVVLALLAIATAVQLILTKAGIHLAVTLASSVPVLLVHAVLWASYDAFEVEDSSAKGELAPLAGHSESVADNSDAV | Function: May be involved in both secretory and endocytic intracellular trafficking in the endosomal/prevacuolar compartments.
Subcellular Location: Membrane
Sequence Length: 196
Sequence Mass (Da): 21665
Location Topology: Multi-pass membrane protein
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A0A068WLC2 | MTGINTTVSVKIIMHPSRRIAVICLFLAFILCIINHLNILGILGGPRITKEVGNRLSHFKSEDTYKPLMCSINGYMSPGCYQLKNSTLVVDFKHIKYWCEMEGYLNPTEDVFHISNGGAQSISPLTFKTHEPLGYYMGNRFSSKPEGKARILLVDAEHTIPISRQWDPRGHPYPIQIAQFGLACYSRYRTLQSWKPSPHAFPYQMVVDFKSQFASHLNCSSDNNHCSFGEKAGSVSYKLTGANLSHNLTALITKGANWPRGTRLVINVSLRLSTRRRAQIHFACTDTFGEGSVVIENDYWALGYSESVDLKVVFFQKHCR... | Pathway: Glycan metabolism; heparin biosynthesis.
EC: 5.1.3.17
Catalytic Activity: [heparosan-N-sulfate](n) = [heparan-N-sulfate](n)
Sequence Length: 678
Sequence Mass (Da): 76484
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I1J3Y5 | MGGFAMGYTFDSKSGLTMAALLLMIVSFYAGILFGNNAPLYVSQLVSHSSSSSSPPNNVSSNGTTKFTNKVALTYWKTPLVIPETGMDVCPLTFNEYIPCHDVSYVATLAPSLDFSRKEELERHCPPLEKRLFCLVPPPKDYKLPIKWPLSRDYVWRSNVNHTHLAEVKGGQNWVHEKDQLWWFPGGGTHFKHGASDYIERLGHMITNEAGDLRSAGVVQVLDVGCGVASFSAYLLPLDIRTMSFAPKDGHENQIQFALERGIGAMISALSTKQLPYPSESFEMIHCSRCRIDFHENDGILLKELNRLLRFNGYFVYSAP... | EC: 2.1.1.-
Subcellular Location: Membrane
Sequence Length: 437
Sequence Mass (Da): 49442
Location Topology: Single-pass type II membrane protein
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A0A0N7B2Z1 | FFFVMPFLVGGFGNWLMPMMINSPDMAFPRLNNLSFWLLIPSLLLLILSMFISVGAGTGWTVYPPLSNKIFHSGVSVDLTIFSLHLAGASSIMASINMISTIYNIRVNFMMMNKISLFSWSILLTSILLLLSLPVLAGAITMLLFDRNLNTSFFDPSGGG | 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... |
I1LIY2 | MVSVVLPLIIHFEPHYGQTNMLVYLGICSLVGSLTVVSIKAIGIAIKLTLDGISQIVYPQTWFFLTVAIICVITQLNYLNRALDTFNATIVSPVYYVMFTTLTIIATAIMIGPGQDISSIASEICGFITVLTGTIILHMTREQEESNMQKTFTWFIGEDLMKDVENEHLILIHDSDYLER | Function: Acts as a Mg(2+) transporter. Can also transport other divalent cations such as Fe(2+), Sr(2+), Ba(2+), Mn(2+) and Co(2+) but to a much less extent than Mg(2+).
Subcellular Location: Cell membrane
Sequence Length: 180
Sequence Mass (Da): 20136
Location Topology: Multi-pass membrane protein
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A0A160ACC0 | TLYFIFGAWSGMVGTSLSIMIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMMGGFGNWLVPLMLGAPDMAFPRMNNMSFWMLPPSLMLLLASSLVENGAGTGWTVYPPLSSSIAHSGASVDLAIFSLHLAGISSILGAVNFITTIINMRSTGISFDRMPLFVWSVGITALLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF | 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... |
A0A068WW14 | MKNHTILCKCFPSETCVKRSSECASLVGCFYSVQKDALGYVVDEHYGCLLNNSFSIISCLNFRGTNTTCCFSSNSSDYCNAHLPVNKHQNTSALFFPLTFFAVLCILLFILAFVYIKGNFSKHEKPLTKHSSTYFPEFTDSGSGSGKPFLVSRTIARQTILLVCIGKGRFGEVWRAVCNGEVVAVKIFSSRDGASWTRETQIYTTALLSHRNILAYYASDMISRGGCTQLWLVTAYHAAGSLHDFLSTAEGVTPQCGLKLARSIAAGLAFLHSEVVGFRGKPPIAHRDIKSKNILVMANNEACLADFGLALVKTSKGMNG... | EC: 2.7.11.30
Subcellular Location: Membrane
Sequence Length: 553
Sequence Mass (Da): 61504
Location Topology: Single-pass type I membrane protein
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A0A3N7G3G7 | MKSPCSPYVRRTPASGVRSTSERIPYSPTSSSYSGSSAVKKRDPLFAVAKSVAGVFGACLMPPEPEPNDSKAFGSSEELKAPSVVSNTSGSSERRQGSNRGIYSSPFNSVREREPGSVNFTMEEIYTATRNFSPTFKIGQGDFGTVYKGRLQDGTAVAIKRAKKSVYDKHLGEEFQSEIRTLAQVEHLHLVKFYGYLEHEDERIVLMEYVPNGTLREHLDCMHGNVIDLAVRVDIAIDVAHAVTYLHISPNYSQGHKVLQHSPHRKLSSQGSRFWFC | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
EC: 2.7.11.1
Subcellular Location: Cell membrane
Sequence Length: 277
Sequence Mass (Da): 30750
Location Topology: Single-pass membrane protein
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A0A0G4IU12 | MSTAMQELEARDALRFSWMRWPSTKVEASRVVAPLAAMYTPLAVQDYNGQVQYEPVSCSGKACRALLNPYSELDYHNRIWVCPFCLTRNHLPQCYNDIGQYNLPAELMPEYTTIEYVLPVEPVPPLHILFVVDTCTIDLELDKLRESLIAVLPQLPPNALVGLITFGKHVAVHELGFGECSKCYVFRGNPKNDNVSSTFVADMLGMSAPAAAGAPGPSPTNKNAQQQRQQHQHQPCFFMPAETCTPAVTSILADLVPDPWPVKGDERPSRATGVAASVAIGLLETVAAKRNGRVMFFSAGAASAGPGKIVSVKLEETIRS... | Function: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules.
Subcellular Location: Cyt... |
A0A816ASH6 | MTSAPSDVPDAHTFYNNPQQQGLKERDESRILYMRNFNNWIKSTLINEYLQRLKNEQPERSNEIHVFDMGCGKGGDQLKWQSARVRFVTFADLTENSVEVCKQRYNERKNHSSYKADFYTLDCTKELIQEKLGSSKPCFDLVSSQFVLHYSFDKIESADRFLRNAAELLRVGGYFIGTTVNSCQLVQQCRAAESQQISNDVYSIHFDPSVDLSEKTGEGIPLFGAKYHFNLHQVVDCPEYLVYFPLLEKLAHKHGLELVDRQTFKDYFDNNKYSGEARNLLARMKALEYYELPSDRPDNNRGLPINHNQYRHAAKYINER... | Catalytic Activity: a 5'-end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.56
Subcellular Location: Nucleus
Sequence Length: 366
Sequence Mass (Da): 42998
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A0A5B8MTF5 | MVVVRTAKAYAAFDGRTEVTDEDVGRVVGMCLGHRTRKDPLDPLGGVQKVNAVFKRIFADGLTYEDELIVPLRKQSGGAKAEQGGAKKKATGPVVKPVAEVSSAEKAQAAQKKKEAVVAPPPEAVFFGQWTEEEDELVLFQQSDQGRALSISYEDAAACLGRTSNAVKCRWHSQVKGKVETMSSEEYTLRLERGARRWFQFRKQG | Pathway: Porphyrin-containing compound metabolism.
EC: 6.6.1.1
Catalytic Activity: ATP + H2O + Mg(2+) + protoporphyrin IX = ADP + 3 H(+) + Mg-protoporphyrin IX + phosphate
Sequence Length: 205
Sequence Mass (Da): 22545
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I1JK63 | MVKFTIVVIFLFFMFPIAFADLRVGFYSSSCPRAEQIVGQVVQRRFNRDRSITAALLRMHFHDCFVRGCDASILIDSTRGNQSEKAAGANGTVRGYELIDEIKKALERECPSTVSCADIITLATRDSVVLAGGLKYDVATGRRDGHVSQSSEVNLPGPRSTVSRVLEVFSANGMSLDEMVTLLGAHTVGFTHCSFFRDRLNDPNMDPSLRAGLGRTCNRPNSDPRAFLDQNVSSSMVFDNAFYKQIVLRRGVLFIDQQLALDTLSKGLVTVFAGNNAAFQRSFADAMVKMGNIKVLVGNEGEIRRNCRVFNSAS | 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. These functions might be dependent on each isozyme/... |
A0A0G4J2M3 | MAGGGGGAGAGIHAGYAAGPVFRAWQQPFVDVRPEDLVMPVFVTDADPRACQAVESLPGVNRYGVDALIDALHPLVDIGLRSVIVFGVVSSSQHKDAFASAATDPKGPAAVAIRQLKRAFPDLVVIADVCMCPYADHGHCGVIDADGRVDVESSVARLAQIALFYAQCGADVVAPSDMMDGRVHAIKDALRRDGFGSRVPVLSYSAKFASCFYGPFRDAAKSAPSKGDRSGYQLPPGSTGLALRAVARDIAEGADFVMVKPAGPYLDVISAVRQRCEVPVFAYQVSGEYAMLRHAASAGAVDLRQAALESLIALKRAGAT... | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4.
Function: Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensat... |
K7K4D8 | MSSPHNSSPDNETPDNSTPDDADNSSSPSSQSPPPSSPPPSSPPPSSPPPSSPPPSSPPPSSSSSPPPSSPPPSSSSSPPSPSPPTSNNPSPPSPNGSSQSPSPPGSSRSPPSFESPSPPHKSLDSPPSSRNSGSGSDSGSRDSNGGGGDDSSKAIVGAVLGIGSVLLILVIVCVVCSRKKKKNRMYYYAGEQSMGKGNNNNYYNSGQHPNYYGGPHGDHVVRMQQNGMGPGGGGWGAPPPPPPMMMSSAEFSSNYSTGPAPLPPPSPNLALGLKGGTFTYEELAAATNGFNDANLIGQGGFGYVHKGVLPSGKEVAVKS... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
EC: 2.7.11.1
Subcellular Location: Cell membrane
Sequence Length: 634
Sequence Mass (Da): 66905
Location Topology: Single-pass membrane protein
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A0A497TBM0 | MEKLIIAGADESGRGAVIGPMIMVGVSIHSDKEHFLRKFGVKDSKELTAKKREKLSKSIEKIAKDIIVLEIGACKIDNYRRSGISMNKLEAMKFAEIINLLEPKTAYIDCPDTNKAKIEGLIRRMLNNNVKLVVEHFADKKYPSVSAASIIAKVERDKRVKKLEREYGEIGSGYPSDPITQEWLRNWLKENKDFPEIVRKTWVTAEFMTKERLQRKLSSFFKNVLKFG | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion 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.
Subce... |
A0A846Q7A2 | MISVKKIREVEKKAEAMGISEAIMMENAGANVARILNEKIGLKGKRILVFCGTGNNAGDGLVFARHSLVYGAKVDVYFVKDPKILRSDITRKNFGILGNIKSLGKPVKFYVKNIPRMKYDILVDALLGTGLKEIVSEEYAKVIEKFNSMEGFKTSIDCPSGINSDNGKLMGSAVKPDLTITLHDRKRGLNPGNSGEIIITDMGIPKI | Cofactor: Binds 1 potassium ion per subunit.
Function: Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX... |
A0A7J4TC79 | MAAIKTWIQALRIPFTTASVLPVILGLAIAWSQGNAWNWGHALLVIFAVAFLHLGTNAANDIYDHYSGNDAANQYHNAFSGGSRVIQEGKLSPREILFASLSLLFAGLLLGMVIAASLQSWTLAFLALAGFLCGFFYTAPPFRLGYLGIGEFLVFLMFGPIAVLVGYFALAQGFDLLPLLASIPVGILVMLILLLAEMPDLEADKKTAKKTFVVLFGRERAVYFLAISLLIAYLFVGTGVALRIMPPLTLLMLLTLPLAVGVLKKAKKHALEPMGIVPAIGGIITLHAATTAILIITFIALALIG | Pathway: Quinol/quinone metabolism; menaquinone biosynthesis.
Subcellular Location: Cell membrane
Sequence Length: 305
Sequence Mass (Da): 32651
Location Topology: Multi-pass membrane protein
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A0A0R2L7Q3 | MRKQERQAIISELITNETIGNQDELQKHLAAQGVSATLATLSRDLKELHIVKEPNASGKASYRMLQIPTAASAELFAQQFREVVIDFTQVEFMNVVKTTPSDGNALAAVVDDLDETKITGTLAGHDTILVISPSKDAASELHEQWQAYLN | Pathway: Amino-acid biosynthesis; L-arginine biosynthesis [regulation].
Function: Regulates arginine biosynthesis genes.
Subcellular Location: Cytoplasm
Sequence Length: 150
Sequence Mass (Da): 16462
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M4SS56 | MDALQGVETAEAATTAAALAATLDQSVYGDKPEAHPGKQASAAVRRTATRGICASGAKIGTSQALADALLCLCWTDTGSPPQGQGSVCRKNLGNTLTSTWDTASATVSAAYAQIKGACKLQTGHTITAANIAEALTAVKHKIAQHKEGGYLGKYEGEFSCDGKNANGVCIKYPDFSDKGNKAFEEIEWVKKLRSVETALRKREAAVARVDTLTTALETQTAAAWLIPQRAKTSQQKREGVSPKQHTSTGNGNKQQADQCEAIKKATECKEKQPNCEWQGKNDEDGPHCKVNKTHITKEAAQTGTNRGNEETTTDKCSQAK... | Function: VSG forms a coat on the surface of the parasite. The trypanosome evades the immune response of the host by expressing a series of antigenically distinct VSGs from an estimated 1000 VSG genes.
Subcellular Location: Cell membrane
Sequence Length: 371
Sequence Mass (Da): 39496
Location Topology: Lipid-anchor
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A0A1V2BM56 | MAGQCIILMGVSGTGKTTVGQALAQALGAKFIDGDDLHPRQNIVKMAASQPLNDEDRGPWLERIADVIFSLEQKNESGVLVCSALKKRYRDRLREGSGSLRFLWLTGEYECILQRMQQRKGHFMPEALLRSQFAALEAPDASERDILAVDIAPDVASIVAQSLNLLEPQSLQGMPA | Pathway: Carbohydrate acid metabolism.
EC: 2.7.1.12
Catalytic Activity: ATP + D-gluconate = 6-phospho-D-gluconate + ADP + H(+)
Sequence Length: 176
Sequence Mass (Da): 19292
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A0A084WAJ7 | MAAKATAKPAIFGGLVRYYDEFYTLFNGLVQGYYLNRYGGSLAEVFYGLTRVSVKSKSFNKRDRNWSFVVLVVLPYALSKMETLCNHWREDYEAGKQISIERRLLFRLVPFVKAFYESVKLIHYVSYLANATETHSPALRILRLGLTYLSEEEESWSFKDIFQGKIRVATMLSTALLRWLELSAFFLQFIEWWQTEANIGDLSKLPIPDAPSLDTNASKYANVRLLLPVYSKSPTKRKQMPGH | Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Membrane
Sequence Length: 243
Sequence Mass (Da): 28051
Location Topology: Multi-pass membrane protein
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E0W0J4 | MELIEIWLLDKINARLVIKTKHFINDIEDNTTIVMQTDPLQILKYNYIELVKTSKTLKFIVDDNNLNEKGINWIKVILFPKIINIMLNSSNLKTIKNGDLKKKNFSFTNLVDIVRYYELYEKMKLKYAKFLIENWTENTDPKKFVYEDIGIASYLMLLWNSDNLPAGKEKKQKFVDLGCGNGLLVYILNSEGHLGVGIDLRKRKIWDSYNSDTILKEEIIIPSVDTIYPEADWIIGNHSDELTSWIPIMAKFSNDHCQYFVLPCCPYELNGQKFQRKNSSMSSYQDFIYYVKNISEMCDFNTLVDRLRIPSSKKVCLVGF... | Function: Adenosyl-L-methionine (AdoMet)-dependent tRNA (uracil-O(2)-)-methyltransferase.
Catalytic Activity: S-adenosyl-L-methionine + uridine(44) in tRNA(Ser) = 2'-O-methyluridine(44) in tRNA(Ser) + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.211
Subcellular Location: Cytoplasm
Sequence Length: 458
Sequence Mass (Da):... |
A0A384CR21 | MAAPLSVEVEFGGGAELLFDGIKKHQVTLPGREEPWDIRNLLVWIKKNLLKERPELFIQGDSVRPGILVLVNDADWELLEGAPWPGDPAAFHSLCLSLNTE | PTM: C-terminal thiocarboxylation occurs in 2 steps, it is first acyl-adenylated (-COAMP) via the hesA/moeB/thiF part of MOCS3, then thiocarboxylated (-COSH) via the rhodanese domain of MOCS3.
Pathway: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis.
Function: Acts as a sulfur carrier require... |
A0A7R9FP81 | RVLFIEIKGKTSRDPMEKLETLRLNIWNANIWLPGNVTWEDMKSKPGRPMPEFQDLLYAFPFSISFLLFRIIFDMLIMEPLARAEVQSVSTVGPCQQSKVGMGKEYMALSSDLFTHLLVPQGNGSLNAGRKWIEREKGSLRSVKEQLEIRKIRETGYRSVAHSIVFLFGVWTMADKPWLRNTDLCFWNPPHPVPWDIWWYYMLELGFHITQTLMLPFDVKNSDFLAQLTHHVVTIGLMMGSWTAGTIRIGSIVLLVHDCADVILQCGKLLKFFKGPDPDATVFKVFLAFTATWILTRVIYFPLYVNIPATKAILHFDYFY... | Pathway: Lipid metabolism; sphingolipid metabolism.
Subcellular Location: Membrane
Sequence Length: 380
Sequence Mass (Da): 44117
Location Topology: Multi-pass membrane protein
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A0A174GHJ5 | MLEKVKEIVAEGLDVNAADLTEETTFESLGADSLDLMDMVMTFEDEFGVEIDTEAIGDLKTIGSVVTYIEGLKK | PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine of apo-ACP by AcpS. This modification is essential for activity because fatty acids are bound in thioester linkage to the sulfhydryl of the prosthetic group.
Pathway: Lipid metabolism; fatty acid biosynthesis.
Function: Carrier of the growing fatty... |
R1BFK4 | MPFWRSRDDGSDSASTTSRGSASLKPAGPPPPGEHSQRWPLTASLWRALRFHAGSIAYGAFLLAVTQLLRRGLQWLERQSAGGGTGVTMRCLRCYTRCLGRCMSYINSFAYIFVALDGDAFCSACRETFLLTARYPAQAVINVTVQSLLFGVQSVGIPLACGVVSYALISSGVWPTWVDAAGRWLEEAASGSPLTGPAADGAGVAQLAEGGGGGLSAQPLLRWMQDQPGVEPLLPSLAVAALALFVGRALASVYECTVSTIFVCAMRDAEAYGGAHVTSALRASLKLEGKGGTRNSAALARAKSANSRGLVVRGKGAEAD... | Function: Choline transporter.
Subcellular Location: Cell membrane
Sequence Length: 334
Sequence Mass (Da): 35033
Location Topology: Multi-pass membrane protein
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A0A2E7FQL2 | MLGLGWSEMLVIGIVLLVVVGPKDLPMMMRNVGRMMGTVRRMGNDFRREIDKAIAADEIAEAKKAISDPLKQTSAEINREFNSIRNGKVEPTGKLKPPATGEESVVDAIHAQAGMTPSRAEPSAASAALRAKVSESVAKPANAATTEAEQPAPIADAPAKTKVKAAPRKAATSTAKTSEPKSKAPAKAAKPAAAAKAAKKPAAKKTADEKPAAQQKSASKTGATKTTARKAAPARKKAVAETGGDK | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. Together with TatC, TatB is part of a receptor directly interacting with Tat signal peptides. TatB may form an oligomeric binding... |
A0A651GIP6 | MLARLHGGRERGEDRRSAGAGPAVGHVPTAVGWRAPRSGADVADVADPPDPAVPEDLQAAVPEGLLARARELRTNAYAPYSGFRVGAVVVTASGRRFEGVNVENVSYRLTTCAEQAALAAMCAAGPLEEVVVVAVAGDGPSPCTPCGACRQTIAEFGTDAVVHATGASGPVLTTSIAELLPDAFTTERLRDRGEVAGGGA | Function: This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis.
EC: 3.5.4.5
Catalytic Activity: 2'-deoxycytidine + H(+) + H2O = 2'-deoxyuridine + NH4(+)
Sequence Length: 200
Sequence Mass (Da): 20342
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A0A1B9BCA3 | MFAGIYTPSITPLREDGSIDLENWEKHVDNLIAAGINGVLLFGSIGEFYAFTVEEKQEAIRHMTKHVAGRTQLLVGTGGTNQEEVIALTNYADECGADAVVIVSPYYFGPSEEVAEKYFSAIAENTKLPILLYNFPDRTGSDLTPELVARLAGKYESIVGIKDTVDNASHTRKIVQAVHPIRKDFSVLSGYDEYYLSNRVSGGAGILTGMTNVEPETFVAMHRAYERGDYAIAIQQATRVANLMRIYDVSDLFITAIKAAVKVKGLPINTVAKEPALQANAQTEAAVRNILES | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.
Function: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
EC: 4.3.3.7
Catalytic Activity: L-aspartate 4-semiald... |
A0A193KDD0 | MKKLLIILPILLALILSGCSSASSGTSAKTKQYASNHDLNGQASWYGNAFHGKLTASGETYNMRAYTAAHKTLPFGTIVRVTNTENNKSVDVKINDRGPYVKGRVIDLSLVAFNKIGDSSKGLAPIKIDILDDSNTFRYKH | Function: Lytic transglycosylase with a strong preference for naked glycan strands that lack stem peptides.
EC: 4.2.2.-
Subcellular Location: Cell membrane
Sequence Length: 141
Sequence Mass (Da): 15332
Location Topology: Lipid-anchor
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A0A7R8X6Z4 | MSAKNRQVCIFADEVEVINYLASTIQQSANEVLQEPAVCFFIGGSAAKLVCEAVTKIQSDWSRWRVAFCDERLVPSTHEESTYAAYAKYLQNSNPTLLNNFIKVDTSLPVDEAARDYEQKLHSLMSSEKGCSDLKWPHFDILVLGVGEDGHTASLFPSHPLLDEASKWVAPISDSPKPPPSRVTLTLPAIWAAGKCIFPVIGGGKADILKRILCPGDGGENLPVHRVMQSSKNTLWILDSKSAEKLEEFF | Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 2/3.
Function: Hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate.
EC: 3.1.1.31
Catalytic Activity: 6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate + H(+)
Sequen... |
E0VMM1 | MIFLIFFGIFFISNSCFGANILYLVPLPAKSHYILGEKLVKELAGRGHEITIISSFKMSNPPKNIKEIIMPASLEDFGLFNKGKESGTFQLRKMSPIDFILFSAVGNMMTNKTLSDPNVRNLLKSNKKFDLIIGECFLTEGLLGGFSYKYKAPMIGVATFIPNTWSNEMVGNPASSAYVPEPILPYTNEMTFYERCMNFFYGMLSQYAYYNRHIPAQDKIMKSFFGQNVPDLRELIRNTSLVLVNHHHSMSFPRPYLPNMIEIGGYHVNPPKPLPKDLQKYMDESKDGVILFSMGSNLKSSDLPESRLVEILTAFSKLKQ... | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
EC: 2.4.1.17
Subcellular Location: Membrane
Sequence Length: 522
Sequence Mass (Da): 59458
Location Topology: Single-pass membrane protein
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A0A1X4XYW6 | MNGLLLINKPSGIKSFDVVKKVKGKFNEKVGHSGILDKFACGLMVIGIGKATKLLSFFEKSYKVYKAKIIFGYETDSLDITGNIVHNNDYLPNIEEIYRTINQKFIGKAEQTVPIYSNVKVKGKRLYKYALSKQNVDLPTKTIYISSIDILSYNQGVLEIKVVCSKGTYIRALSRDIARSLNAYATVTYLERLYIYPFSINEAVDLSYVSQEHVIPFEKVKYMTKIDTLEVFNGIAN | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
EC: 5.4.99.25
Catalytic Activity: a uridine in RNA = a pseudouridine in RNA
Sequence Length: 237
Sequence Mass (Da): 26827
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E0W4F7 | MFSYCLRNTKRSKIYPDPEKFDPMRHAPEEKSKRENISALYFGEGPRICIGNRFGFFQVKVGLLTLLSSYRVSPCEKTPSQLKFNVGSLVLTVEGR | Function: May be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 96
Sequence Mass (Da): 11007
Location Topology: Peripheral membrane protein
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B5T2Z3 | MMKVLIFIIMLNFNIMINNKQIMMKLLVMMLMVISLMFTYSINFNENWMNLYSWMGMDLLSYMLSLLSLWIIMLMFMVSLNFKNIKMFSFILLLLLLSLMLSFMSINYFMFYLYFEISLFPTFLLIMGWGYQPERINASMFMLLYTMFASLPLMIILFYLLSYFNSLNYLIILNNTMKFTYLKLLMYLYMIFAFLIKLPLFMLHMWLPKAHVEAPICGSMILAGVMLKLGGYGIIRSMMMMLNYSKYFNYIITIISLLGMFMLSVICLRQYDLKLLVAYSSVVHMGMMLLGAMSLTKWGMVGSYLMMMAHGLCSSALFIL... | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed... |
R1EE71 | MFVHYLSKFVDWTDTFLMIGSKSFRQVSFLQVFHHATVGMIWGALLRKGWGGGTCVWGAFINSVTHVLMYTHYLVTSLGLHNPLKSQLTNFQLAQFASCVLHAALVFASETVLPARLAYIQLVYHPTLLFLFGFQMKWVPSWITGQTITGRESEAPEKKVA | Catalytic Activity: a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-chain 3-oxoacyl-CoA + CO2 + CoA
EC: 2.3.1.199
Subcellular Location: Membrane
Sequence Length: 161
Sequence Mass (Da): 18184
Location Topology: Multi-pass membrane protein
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E0VIF1 | MTEVKKSWNVVSNLEEIIEILTSENFDKFGHHLFNSNIPEKCFLEPCILGVDEAGRGPVLGPMVYSVFFCSINDADILKDIGCTDSKVLTEKKREDIFDLINQNNDKLGWAVDLLSPNLISNRMLQRKKYSLNEIAQNSTIKLIESLLEKNITLKDIFVDTIGPADKYQEKLSKLFPNSKVTVKSKADLLYPVVGAASICAKVIRDTAVQQWKFPEKITIDAEFGTGYPGDPKTKKFLLESKDSVFGFPNLVRFSWSTSAKLLEEETLVEW | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Catalytic subunit of RNase HII, an endonuclease that specifically degrades the RNA of RNA:DNA hybrids. Participates in DNA replication, possibly by mediati... |
Q7WTY7 | MTDRFPDGITVTTPNPADSGSGETLASPFPEPEPISTNPSKGAKVRPADRIFQGLAEGSGILIVALIAAIGVFLLMRAIPALARNEENFFLYGGNWVTTDTSAMHFGILDLLQVTVFVSVFALVLAMPVALGIAIFLTQYAPRRLAGPLAYMVDLLAAVPSIVYGVWGLYVLAPVLKPVAVWLNENLGWFFLFSTGNASVAGGGTIFTAGIVLAVMILPIITAVTREVFMQTPRGQIEAALALGATRWEVVRTTVLPFGLSGYISGAMLGLGRALGETIALLIILRGTQTAFGWSLFDGGYTFASKIAATASEFNDQFKA... | Function: Part of the binding-protein-dependent transport system for phosphate; probably responsible for the translocation of the substrate across the membrane.
Subcellular Location: Cell membrane
Sequence Length: 351
Sequence Mass (Da): 36936
Location Topology: Multi-pass membrane protein
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R1E841 | MAQPRGVRVGLCLALLCYLPSSASLALPEAFRRARARNARLQRSASSPAPRPPPSAAPLASGEVALPPSLEERLSSALGVRSLNPLQRLALPHALGGGDTLVHAETGAGKTLCFALPIAASLAAADGAASSPAACDGSVHALVLSPTLELCAQTAAVLNALLPGCAAVVATDEAARLLSGGAAASALAGARVLVSPASLALALLPASEAPAGGGRRASGAAMRADAGRSRGAGRRGGGGGRRPAAGGRGGGGRRFEEGGEGGAVTAVRSRSLEPGGLLGSLRLLVLDEADALLGTLGKYATQRQKESRSRHPKPAALVVK... | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 593
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): 58941
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R1EFE7 | MAETPGGKQSPGSKASKKVNDSKFGETIVEEIQVSVTVMLTGVALVEMGYDKELRAAMYEMADAWGCINTYLPQHVTRKRILDFQGETWKDKQETERPNKNYKRAPGWTNANSKPDAGAAAAPPSACPMRADGGAAPSGRAAAAEPPKASGCPVDHSKWSAWAGRSAAAAGGDGEADINPDNRMPVLSQQPAAGQDAVLDTSRVVSSIPQGRAGATERWVYPSEQQFYNALVRKGKDDGVDTAAMPSVLEYERLHCDTCDPAKVSLLRFQGRPFELSPKARLKTALGLAPRPFDRHDWTVDRPNPEVRYIIDYYDASASR... | Function: Lyase that catalyzes the covalent linking of the heme group to the cytochrome C apoprotein to produce the mature functional cytochrome.
Catalytic Activity: holo-[cytochrome c] = apo-[cytochrome c] + heme b
EC: 4.4.1.17
Subcellular Location: Membrane
Sequence Length: 468
Sequence Mass (Da): 49327
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A0A402CRN4 | MTTDLLLRAAVGDDLLSNEPMSRHTTLKVGGPARWFWAARDVDDLSRVLTACTEHEIPYLFIGHGSNLLMSDAGYDGLVIQNRCKGSRIGAETYSESGVSFGSLFYQTAREGFSGLEWAIGIPGTVGGALVSNAGAYRGNIGPLVRSVRVFADGRDQEVGPEWMEFSYRDSRLRRSGIGRTVILSCMLHFEDRGDPETIIARAKDYQAQRRAKQPYAPSAGSFFKNVTDKAFAQTLPDLPDALKAAGVVPSGFLIEACGLKGLQVGGAQASEKHANFLINAGGATASDLRRLAYKVKGLVHEKFGVTLEEEVLYVGDWSE... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
Catalytic Activity: NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
EC: 1.3.1.98
Subcellular Location: Cytoplasm
Sequence Length: 323
Sequence Mass (Da): 35087
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A0A9E6YYZ2 | QPGSLLGDDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGISSILGAINFITTILNMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNT | 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... |
A0A6P8LLP7 | MATGIALIYPALLTVLAENNYTIFPDETGVPHLIKIDNSPLTELELAILGINVESVSFNLYTRDNPMIGDVLNLNDVVSVRKSHWNPHRETIIVTHGWNANGRSSSCTLVRDAFLNVWDSNVIIVDWGNIAKNLLYSVVAKSVPRVALRVADFVNFLQTSAGLRTSKLKIVGHSLGAHVAGLSALEIGRSSQVAEVIALDAAKPMFEHKGPDGRVDKLDARNVQVIHTCAGYLGLNISVGTSDFFANDGRNQPGCVNDLIGACAHSRSYEYYSESVMNSKGFLGVSQNGAMAYMGGPTLDPKAKGTYTFQTNYQYPYAVG... | Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+)
EC: 3.1.1.32
Subcellular Location: Secreted
Sequence Length: 321
Sequence Mass (Da): 34734
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E0W2H3 | MSLAKKISFGNFCQLCSKIKSADHEKKIIILRNYISNWKKKAKDIESDGLNLDDSFFPIFRLLIPHLDRERGAYGIKERTLAKIYISILSLPKDGEDALKLLNCKNPKTSYFNNCDFASIAFCILRNRCAEGGQLSVEEVNKHLDKISTSHAANEPRNVDAELISLLKSTNAEEQKWLIRILLKDVKLGLSENVIFKCYHPDARELYDSSNSLRKICDLLNDPEIRLNEIQIQLFTPFKPMLSEECDIQKIDYYLKRSCHFFIETKLDGERFQLHFEEGNFKYFSRNGYDFTTNFGSSKREGNLSPRIFKRIPPHVKSFV... | Catalytic Activity: ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.
EC: 6.5.1.1
Subcellular Location: Nucleus
Sequence Length: 891
Sequence Mass (Da): 102161
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A0A656Z8G7 | MISVTSAQLDAWLAAFIYPLARILAMLAAAPVFNNTGMPRQIRLVFGIAISLAIVPALPPIETIPPGSWHGIAVLGQQILIGAIFGLTLRIMFTAVDIAGEIIGLQMGLSFASFFDPRNSAQTSVMSSFLGLIMTLLFLAMNGHLLMLSVLAESFQLLPISTTAFAAPGFSALLAWSAVMFATGLMLALPLITALLIANISLGVLARIAPQLNIFAVGFPVTIVTGYAMLLFSLPHFGGVLQHLYDQGFDALAAVLQAGGALNPNPPAP | Function: Role in flagellar biosynthesis.
Subcellular Location: Cell membrane
Sequence Length: 269
Sequence Mass (Da): 28241
Location Topology: Multi-pass membrane protein
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E0W2C1 | MSDWTDPRCKDPFNYTALPRDQPPLMTCNGCCVKMVRNAKSPYESVRRTCTTQLQINLFMVDHVCMMESSNTGHMCFCEEDMCNSSPSIHLSLPSQLTSSLYLSSSHPRDLSYPPLFNSIAFKCF | Function: Required for homeostatic regulation of sleep under normal conditions and after sleep deprivation. Important regulator of the Sh K(+) channel, acting as a signaling molecule that connects sleep drive to lowered membrane excitability, possibly by enhancing K(+) channel activity and thus reducing neuronal excita... |
A0A196SKI7 | MELKSCLWCQDIEKSPIPEECLSEDVIVGIDEAGRGPVMDSKQLTAEKREHLLGDIQAADSIGYVIRTLSPKEISANMLQTKPFNLNEMSHKAAMDMIRELLRMKVKVTEVYIDTVGDPEKYESKLQAAFSFTTIKFKVSKKADALFKCVSAASIVAKTRRDHIIENHSWEEAYMEGKSFGATGSGYPSDPTTKAFLANCMHPVFGFPTFIRFSWSTIPKLIQEKNGAVVVWKESLEDEDSPHRRPKKKYRKEESRLCKEHSIESCSF | Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
EC: 3.1.26.4
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Length: 268
Sequence Mass (Da): 30364
|
A0A913XIM4 | MASIGYRTNYTYGYIVEYSKPCFDSWLLIPGENLWNSGLRGFLYILAMFYFFLGIAIVADIFMSCIEVITSKKRKVTRYDPEKQESVEIEVFVWNETVANLTLMALGSSAPEILLAVIETAQELGRDPTGDDKDGLGTFTIIGSASFNMLLITAVCVISVPSGTVKMVREFGVFIWTAIWSLFAYVWLLVTLKWVSPGEVEIWEAFVTLAFFPLLVFTSWCQDHGWWCRSSRVLSVEPPEVRVVGMMERPSSHMMVHRSMELRVIEQHRISVSEHDIKELPKSKDKLKEVVSLWKGQKPDANSNETVESLAHAFKHFKEA... | Catalytic Activity: Ca(2+)(in) + 3 Na(+)(out) = Ca(2+)(out) + 3 Na(+)(in)
Subcellular Location: Cell membrane
Sequence Length: 956
Sequence Mass (Da): 106228
Location Topology: Multi-pass membrane protein
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E0VI43 | MIFVSKIHTLLIFNKSTRLKRFFCTKPVRVRFAPSPTGLLHLGGLRTALFNYLFAKSQNGIFILRIEDTDLERKIDFATENLIKDLEWCGIKFDEGPYFQTERINIYKKYAKQLLENDSAYYCFCSKERLELLRKEMIKTGEVPRYDNNCRHMSKDEIDDKLKSGSQPCIRFKLTKYNEPIPDLIFDSIKHDVHEVEGDPIILKADGFPTYHLANVVDDHLMKISHVLRGVEWQISTVKHILLYKAFNWTPPLFGHIPLLLNADGSKLSKRQNDINIQQLRNNGYFSNAILNFVIKSGGGFNINHDEKCTKIFLMNELVN... | Function: Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
EC: 6.1.1.17
Catalytic Activity: ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu)
Sequence Length: 507
S... |
A0A402CYP8 | MGTGKSAIGRAIARGLSVRHLDTDCEIERRFQMDIPRIFAEHGEAAFRSAEQDVLRRLTQRGSPAAAPPRLVISTGGGTPMREENVELLREIGQIVWLSAPIATVLQRVGRNLKQRPLLAGHQDNPQQRIRQLMAEREPRYASLAELRVDTSPFASPKDAAAHIISLLQQNEDI | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.
Function: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
EC: 2.7.1.71
S... |
Q5L7U3 | MKTKLIILLILTTMIHTNTVNAQHSQLKRADFQQTIDGKQTDLYFLRNKNGIEIAITNFGGRVVEFWTPDKKGHFEDIVLGHDHVDKYLHYKGERFLGATIGRYGNRINKGKFTLNGQTYQLPINDTPNSLHGGFKGFDMVVWDVEQPDSQTLQLTYLSKDGEEGYPGNLQVSMNYKLTDKNEFIITHQAQTDKETVINLTHHSFFNLHGAGNKDINDHILMINADKFTPVDRTLIPTGILQDVEGTPMDFRRPTPIGKRVNDSFEQLEFGHGYDHNWVLNRKTSNTPELAATVYEPASGRYLEVWTTEPGLQFYGGNFF... | Pathway: Carbohydrate metabolism; hexose metabolism.
EC: 5.1.3.3
Catalytic Activity: alpha-D-glucose = beta-D-glucose
Sequence Length: 376
Sequence Mass (Da): 42875
|
Q17C24 | MGKLNTSYGNYCYQTGTMLDRAVTKYCTSRNDYSESTAGDEASLQLGRLICCRGGVRQMRYDYEDDNLGRVEDMSGRDGTKCDRDELDERHVEAIDESRLAYRAEGNSNIVLALIDDHQVLRLRKTTISCPGGKDTVDLERFVKFSRVIASCFSRRYVPHPKLGRLDTYDLDEFNKKLAKFRPVNRLAKEIQVRDCILYPDVAFLPVTLDPLTFRNQDFGQDTVRGHWQNTYCVEIKPKQGWCLDDLCYGEGLIRDQLFGCWNADQLIDLSSMDKCRFCLFQYSKLRNKMIGKISKYCPLDLFSGKPIRMLNAIKGLIGS... | Function: Phosphorylates Ins(1,3,4,5,6)P5 at position 2 to form Ins(1,2,3,4,5,6)P6 (InsP6 or phytate).
EC: 2.7.1.158
Catalytic Activity: 1D-myo-inositol 1,3,4,5,6-pentakisphosphate + ATP = 1D-myo-inositol hexakisphosphate + ADP + H(+)
Sequence Length: 581
Domain: The EXKPK motif is conserved in inositol-pentakisphospha... |
E0VFL7 | MDSLPIAYLTRSEIFSACHRLHSKDLTEEENKKIYGKCNNINGHGHNYKVEVTLKGPVSPVTGMVVNITDLKSYMDEVIMKKLDHKNIDEDVDFFKNGGIVSTTENLAIYIFNELRSLLPNPNLLHKVKIHETDKNSVVYRGEIT | Cofactor: Binds 1 zinc ion per subunit.
Pathway: Cofactor biosynthesis; tetrahydrobiopterin biosynthesis; tetrahydrobiopterin from 7,8-dihydroneopterin triphosphate: step 1/3.
EC: 4.2.3.12
Catalytic Activity: 7,8-dihydroneopterin 3'-triphosphate = 6-pyruvoyl-5,6,7,8-tetrahydropterin + H(+) + triphosphate
Sequence Lengt... |
A0A402CXQ9 | MIPLIDPFGRAIQYLRISVTDRCNLRCVYCMPLDGVPYDAPEEVLSFDEIMRLVNLLAGHGLRKVRITGGEPLVRKNLPELVQRLAAVPQITDLGLTTNAVLLENQAQSLWDADLRRLNISLDTLQPDRFVKIARFAKFDEAMAGLAKAEALGFAPIKLNMVVMRGVNDDEILDMAALSLDHPYDVRFLEYMPIGQVTPWEWRASYVSNEEVIQRLSERFELQPIEAASSSTSRVFQIPGAVGRVGVINPISHKFCASCNRLRLTANGALVPCLADNYEYDIKTPLRAGASDEELIGHVKAALAHKPEQSDFEGRVERGG... | Cofactor: Binds 2 [4Fe-4S] clusters. Binds 1 [4Fe-4S] cluster coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine and 1 [4Fe-4S] cluster coordinated with 3 cysteines and the GTP-derived substrate.
Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
Function: Catalyzes the cyclization of GTP... |
E0W0K4 | MDYLGDIICLSLDSVIFGVCLKAYLRNKHALHSIENAPEFGIDKHLEVFLNKNSGKFPYIAVRGSVKALGPAIKSLNHPSISGVIQKLSIRDMSFREAHQDFGLTENQRTINEIFNSIPFALTSRRGDVEVEVIDALAAEILDLEVVSDRFDPSNLGFMDHMWGFFTGIRKRGLQTIEEILKEGAYITAVGEVQKDGGSLRIQPPTDGTPFFISTMPVNSLVRRLDEKVKYYGWISFGFGVLGIFLFGTLIRKYFKKHNEWLKKEAERKRLESTRKERRKNVRNTEDLPMDKLCVVCQSNPKEVILLPCGHVCLCEDCSE... | 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: 342
Sequence Mass (Da): 38726
Location Topology: Multi-... |
A0A2K8N6D2 | MKAYPLSFRPVFQERIWGGSRLREFGYSGASDGIGEAWVISDHDHGPTPVADGPLAGKRLSEVMKANPEWFGLPPGARFPLLVKVIDASEDLSVQVHPDDRYARPRGDAGKTEAWFVLFAEPGASIVYGHRAQTREDFEKRMKEGAWGNLLVKVPVRAGDFFYVPAGTLHAIGRGLLILEIQQSSDTTYRVYDYDRVGADGRKRDLHVKEALAVTRCPSPKPQRPGYARSGRVGAVIEHLVRGEVFTIDHWLVDGEARVDECGVFRLISVIQGSGEVVWDHGRRSVAKGDHLLLPAVLHPVVLSGRFEALFSAPVISTRA... | Cofactor: Binds 1 zinc ion per subunit.
EC: 5.3.1.8
Catalytic Activity: D-mannose 6-phosphate = D-fructose 6-phosphate
Sequence Length: 321
Sequence Mass (Da): 35439
|
A0A6J1NAH3 | MADTTTYCRMLGHVLTIAMHVGNIVYMNRGFSPEVLQDPQLKAFGKLQPRYFTVWTFVLQIINACTGLVCDYLVISNSENKLYKLPKHLRGFKNTLFSAILWPSTWVVCSIFWGLYLYDRSLIFPEFIDKALTTTSNHIMHTAIIFVVLWEVYFTPRVEPRSHRRNILHILTHLLLYLAVLFYTHMQHGVWLYPIFSLVYGTIYFPLINIAIGVIALTFYYLQWTIINYLWSDSAKTKKIT | Catalytic Activity: 12-(9Z-hexadecenoyloxy)-octadecanoate + H2O = (9Z)-hexadecenoate + 12-hydroxyoctadecanoate + H(+)
Subcellular Location: Membrane
Sequence Length: 241
Sequence Mass (Da): 28217
Location Topology: Multi-pass membrane protein
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A0A174CXF5 | MKTNRKVICSSSAVRYAETLFELNIPKETIEKTREIFSEVPQITDVLDNPTIRQEKKEQVIDKVFPREMRNFLKIVCRYRKVRLLGEIFDAYDMRADEEEQIIRAVLFYTALPSEEQKKGMESFLCRKYGAKRAYIEMKKDDSLIGGFILRVGNDEYDRSTKGRLDRLEQRLTRR | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During c... |
K4JC34 | VEKELLPGFHQFEWQPALKNVSTSCNVGIINGLSGWTSSVDDSPADTITRRFRYDVALVSALKDLEEDIMNGLRENGMEDSACTSGFSVMIKESCDGMGDISEKHGGGPLVPEKAVRFSFTVMSVSILADGAEDEVTIYTESKPNSELSCKPLCLMFVDESDHETLTAILWPIIAERNAMKESRLILSIGGLPRSFRFHFRGTGYDEKM | Cofactor: Binds 1 divalent metal cation per subunit. Mg(2+) or Mn(2+).
Function: Catalytic component of the RAG complex, a multiprotein complex that mediates the DNA cleavage phase during V(D)J recombination. V(D)J recombination assembles a diverse repertoire of immunoglobulin and T-cell receptor genes in developing B ... |
A0A7J4TDG7 | MQVQAVMVHPKALKKIKEKEKAKEQIMGYFAQASAAFPADQKKASLFIHKARRVAMKHRYRMPPELKRRFCKRCYAYLQPGVNARMRIHQGNKVVTCLDCNHIERIPFKK | Cofactor: Binds 1 zinc ion per subunit.
Function: Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends.
EC: 3.1.26.5
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Subcellular Location: Cytoplasm
Sequence Length:... |
A0A0D1W8F4 | MKKVAVIGAGYAGLAVSIGLARCNAMVRCIDIDEKKIERLSQGNVPIHEPEMEGMLRRQLADQRLTFSTDMIAGIMEADIIFIAVGTPGQEKGAPDVTAIFSVTDTIAQHIRKDVVVAIKSTVPPGTCEAVQTRLHDWIRGTYACDVVANPEFLREGRALRDFLEPDRIVLGGTDERAITVMQELYAPFVAAGVPFYMTDWRTAEMIKYSANSFLAMKVAFINEIARLCDAVGADVTVVAEALGADPRIGNQHLSPGPGYGGSCLPKDTEALALSARQAGAPLAIVEAVIESNRLQQKYVVEKIKREWSNLQGLCIAVYG... | Pathway: Nucleotide-sugar biosynthesis; UDP-alpha-D-glucuronate biosynthesis; UDP-alpha-D-glucuronate from UDP-alpha-D-glucose: step 1/1.
EC: 1.1.1.22
Catalytic Activity: H2O + 2 NAD(+) + UDP-alpha-D-glucose = 3 H(+) + 2 NADH + UDP-alpha-D-glucuronate
Sequence Length: 434
Sequence Mass (Da): 47787
|
A0A660TSV4 | MEIIVSDTIGFCSGVRKAIRGAEKALKGNSKIYCLGDIIHNKGVVNQLKEKGMVFVKSLDEIPNGASFIIRSHGLPFETIENIQKKAVHIYDFTCPKVKKSHKLVESLKNHKRPIVIVGNREHPEVKAIFSLTENRGIIIEKPEEVKTKLNTDECYVLVQTTFKPVLFYEIVKEIVSFTKKAIIYNTLCEETTKRQEEVKDLATKVDMIIVVGGKHSSNTKTLFSISNSMVKSVHIENADELQNDWFKEVHRVGIVSGASTPDDDIDRVIEKIYYFERNNEDETQR | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Pathway: Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from (2E)-4-hydroxy-3-methylbutenyl diphosphate: step 1/1.
Function: Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of is... |
A0A7R8X0J0 | MRDRVFEWELAGEWAEDVQWWFMDYWTLSFVFVAVYLILVFWGRILVVYRGLPEVYRSIRHDSLYHSMCLGMNLRHIPMVSVLAILFVISKFIELGDSVHRPSEAAFPLPPLGVLARFFIILNVLPHAFMYPYYTAGRRNWEGTHRTKGILLNLAIRFELLRPTRKMKEARRSTSCVTSEDGLLLSSLSLRSILNALPQSQLHRSRVQGKRIRGTIGKKSRFFPTSEDSKRNSTPLGLLPLTDSDFILSSKAKTDARQPGKKPHDYSAESHGMMFPEGIVEEEYDSPHQSRARPALGPNMFHDPSAYPKPNYPIFNGSRY... | Catalytic Activity: a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-chain 3-oxoacyl-CoA + CO2 + CoA
EC: 2.3.1.199
Subcellular Location: Membrane
Sequence Length: 440
Sequence Mass (Da): 51525
Location Topology: Multi-pass membrane protein
|
E0VWC4 | MSQLNLVLEKLYEEYYKKTSTKLKIVDAYLLYVFLTGVTQFVYCCLVGTFPFNSFLSGFISCVSSFILGVCLRLQVNPQNKSDFMGISAERGFADFIFAHVILHLVVMNFLG | Pathway: Protein modification; protein glycosylation.
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 m... |
A0A402CTZ4 | MPNPKLIIGTRGSALALTQTNTIADALRRVHLGLEVEIRTINTRGDATQAANVPLASFGEKGIFAKELETALLDGEIDLAVHSMKDLAHTMPPGLVLAAVPKREDPRDALIGSTLDSLRQGALVGTGSVRRRALFSSRRPDLRFLEIRGNIDTRLKKLEDGGYDAICLAAAGLKRLGLADRVTEYLDPEWFVPDPGQGALALQTRESDVQVRGLLSAVNDMASFVTTRAERGFLRAVGGSCQTPVGAHARHIDGGLMLRAMLVGDDGLMRRAEAGGAPGMAEELGARVAKMLR | 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: 293
Sequence Mass (Da): 31303
|
F0VJ37 | MSLARRTQQPLLALPPRAVFSRGLGPGFAPPFQSRRRSCARRDPSTSWLSPSVALPPLRNSLLSASAHHASLPTSFPAFHDPRKAHFSTVQTHEETHETSTAPRILSSSSSDIVENLAAECFLVDVFGRGHGLPASAGEGAERAKAENAESAAKQRTERRDLRAPLLFLWRNDKTIVIGRHQNAWSECNIQKMDESGVKLARRYTGGGAVYQDLGNTCFTFLDPVATHNKERNNKIILRALEKAFGIKCSASGRNDLVASDGRKFSGAAYSKLPHGWLHHGTVMREVDCEALGRYLTPSKEKLASKSIKSVTSRVVNLKT... | Pathway: Protein modification; protein lipoylation via exogenous pathway; protein N(6)-(lipoyl)lysine from lipoate: step 1/2.
EC: 6.3.1.20
Catalytic Activity: (R)-lipoate + ATP + L-lysyl-[lipoyl-carrier protein] = (R)-N(6)-lipoyl-L-lysyl-[lipoyl-carrier protein] + AMP + diphosphate + H(+)
Sequence Length: 484
Sequence ... |
A0A402CZP4 | MRAAASVTRSYLWPVLSVAAATGCFSLLRPYVDKGQASLLYLPIVLACAVRFGFGPAILGALLSFLCWDLFFLPPFYTLAVDDPKDWLSLAIFLLAAVVTARLAAQARAQTQEARTRESEIETLFEASETVSRVIRADRVLAALADQLQTLCGATRCLVFRRLGPGVALQLAPDGANEVPIDAQTLGRIASLAEAACANDRVIGLGASQHLWAKAVTDTDASLGGDGARIGVYIPLHAADALVGVLHVGPRGDSRPYSALEERLILTLANHAAVVIARDRLTQQAAEATALREADTLKDALVSLVSHELRTPLAAIKASV... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 529
Sequence Mass (Da): 56295
Location Topology: Multi-pass membrane protein
|
A0A6P6F8A3 | MAKTTDSIRDVRKRTTESKSELQSIENKQNNDFLVNYQNQSYNIQKFLRYHPGGTKILRYFKNRSLEKAFEEFPHSQAAFHLLQEFTLNQEKYQKYENLIDWDKAILGQVGSLGHHYWEWVNLPVYRDIKLFKSNILESLTITPWYLIPIVWIPMSLYFFYKGLARIAAINTESTVFEPLTSFIFGIFIWTMLEYVVHREVFHFKPPDNSKLFITLHFLLHGVHHKAPFDKRRLVFPILPALLVAKLLLMIYNMVFPQTIIYFILSGTMTGIGIKIFIFIDFIININDVSNVKKICLIGYMIYDLTHYYLHHGAPKFGTY... | Cofactor: Binds 2 Zn(2+) ions per subunit that likely form a catalytic dimetal center.
Pathway: Lipid metabolism.
Function: Catalyzes stereospecific hydroxylation of free fatty acids at the C-2 position to produce (R)-2-hydroxy fatty acids, which are building blocks of sphingolipids and glycosphingolipids common in neu... |
R1EUF5 | MHSPRAANNEPSSSTDIERPALSISPPAGGPSPAPCACAPCSAPRCQSAPLPLVIVVIIALNYIPYVLWTLERRRHLALTITLVVIFHALLGLVVCAWAYTCGTDPGVPPSQWQRRMAALAKARPGSSELKVCRRSGLYKPPRSHFCSVTRRLTLNMDHYCPWVANTVGHYNRKFFLLFLLYTCLLLAYVLLSIAPQLPDLFDWALDGDGRWVGGVAYAVVLGVMLAVDVLLLLLLGPFMCLHWKMAMRNQTTIDGDKLPQYDIGLSANLEQILGRRRLHWFCPCYCDGPVGDGVHWPTKTGGAALVPLGGSGTPLRTSA... | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 408
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 42983
Location Topology: Multi-pass membrane protein
|
R1DEG2 | METSLNRCLEATGANFGRASARFGPWAGAEERAEEEAAAPVYRSAKPPSSDMPRLTRGFSVHVPWLGRISGGTSAQKRLQTLAVFSFSLYGLLPLIAISWFVVLLCLINPLTLPFILGYLYFVFVADKAPTAGSRAPFLRQLTTWWHAYCDYFPMLLVKTAEYVLGYHPHGIISVGAFGAFATDGARTLSLVASGAQPREGRGFSSLFPGIERRLVTLPINFTVPFGREYILSMGACTSDKATFRSVLGRGSGSAVVVVVGGAEESTMVTPGQIDLVLERRKGFVREAIMAGASLVPVLAFGENDLYAVFHTDDTHPIAR... | EC: 2.3.1.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 432
Sequence Mass (Da): 47220
Location Topology: Multi-pass membrane protein
|
A0A8T5IWI0 | MVKSWKKEIIGEKIIIINSKNKSLLGMEGNVIEETKNTITLGNGKKLLKSHITIKINGEIIEGKTLQKKPEDRIKK | Function: Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
EC: 3.1.26.5
Subcellular Location: Cytoplasm
Sequence Length: 76
Sequence Mass (Da): 8583
|
A0A378YGM8 | MARVVVEVMPKAEILDPQGQAIVGALGRLGHPGISDVRQGKRFELDVDDNVSDDELERIAESLLANTVIEDWKVVRL | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 1/2.
Function: Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent ... |
A0A660SXT5 | MLLRAWLINLFPELWKNSIDVNILKRINLPRNASCLVALSGGGDSVAMLDLAYKESVNYGLTLYAAKVMHGIRSGEEEEAEARLCERLCKERDIPFEVLTADVDTVEDIQLRYGCGPEQAARDFRRNLLENHKVKITADYILFGHTADDNLETVFMRLLSGSGPEGLSGISQDTSSTFRPLLGLTRSDLREYLVSRDIPWIEDRTNMENIYRRNRLRNELIPLVTDIFPGWEKALETLGERSKEAADALSRAAASQLPCRKTGDDCCWNEADWDSASEYLKALSLWEAFNHLDNSRIPDRQLPWKSLKEARRSINEKRSW... | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34)... |
A0A651GL02 | MRERPIGVFDSGLGGLTVLHAMVDLLPAEDLLYLGDTARYPYGERDLADLQRISLAVAEELVDRGIKLLVVACNSATAAALPELREALDVPVVGVVDPGVRAAAATSRTRRAVVIGTRATVASGVYEDAADRLDLGLVVRTVPCPGLVELVEEGRTSGPEVTAIVRDRLAPLLSARIDTLVLGCTHFPMLARPISEVVGRDVTLVSSADETAFEVRDLLERLGWLREEEEAAGGRRHYLTTGDPDTFAALGERFLGAPLGSVERVTLAALEPRTPVDPTRRRGSRRAGRRQAEESRWSSAAT | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Provides the (R)-glutamate required for cell wall biosynthesis.
EC: 5.1.1.3
Catalytic Activity: L-glutamate = D-glutamate
Sequence Length: 302
Sequence Mass (Da): 32449
|
A0A6J6ANA3 | MQRLPKIVRVLAVISFTLVVVLFAALIVNSFQNAGKPLTTLTPQGPSSESIQKLLVPVTSIAAVVFVGVLGAALLISWKFRERKDSDPDEFPEQVHGKTALEIGWTILPALILAGIAVGTVMTLINLNREEPNSINVQVAGQQWWWQYKYDVNNDGNFDGPEDITTATEMVIPAGRPIQVTTTSNDVIHSFWIPGLNGKRDAVPGLRNPLKLQADEPGIFRGQCTEFCGLSHANMRMLVRAVSTSDYDAWVKNQLKDHAADPTDPTALAGKKVWQALCAQCHVIDGINDVKMKETKPPLVSGVAPDLTHLMTRGTFAGSI... | EC: 7.1.1.9
Subcellular Location: Membrane
Sequence Length: 406
Sequence Mass (Da): 43860
Location Topology: Multi-pass membrane protein
|
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