ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
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A0A4Z2CN81 | MQLSRVRWCTAFCYRLNVVSLNKISNSFNIYFNRKSVYWLHLIWNFFVLCHIKCLLFFLSPLVIAYRKIKGVDLSENFVFVTSDATKMPSHLVKYAFGPTLTVEIKPKFGAIPLWPATGVVNLAKNSASLFCLRQEHSSKRSRWKDLSTYCPCDLFSGDRDRLVHGLNALLTTPQNNFRVYLDSHPIYSHDIDKLGYGLYRFFHLEHDSISLNKQQNEPPNCFDHQNVCGHSNECQFSNDRDRLIRGTLLEALLHKFDSTNDDLITRVPLNSSDRQPFSMCCALHLNGKFHSTQCGNCHNLGKKYTLPEGCILQRILSVQ... | 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: 463
Domain: The EXKPK motif is conserved in inositol-pentakisphospha... |
A0A7S2WEQ9 | MFLWRGGFRVGSKEKTSDGKLHTSRWLVLGYIVPMLATLSFFTMADHKEERFLSMTYPMICFCAALSIDIMDRTVQYFVGGAFLTLERLLIVLGVFACCVLSVSRSTGLHMNFYAPIEVFEHVNQLDQLDADLAGATVCLGKEWYRFPSSFFLPQGVSVHWTKSAFDGQLPQPFSPWPEGTKKVHSYFNDENRGDPTRFFDVSKCDYAVDLNVGTDFGAIGRWDEMWSRKHCASFLDANLSPAFIRSFYIPFGYSAKKNVYAEYCLLEKNSRV | EC: 2.4.1.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 273
Sequence Mass (Da): 31111
Location Topology: Multi-pass membrane protein
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A0A0G1WR53 | MSKNIVKSMRPSSSPMSFKKSTTKDKKRQSIHFIGVGGIGVSALAKYFLARGVSVSGSDIKETEIVNELVKLGVRIKIGPHKAQNIPFGTARVIYTAAVRKENPEYREAKQRRLPTQSYAEAIGELTKKYETITISGAHGKSTTTALCALVLEEGYCDPTVIIGTKVKEFGDSNFRGGYGPYLVLEADEWNKSFLNYSPKIAIITNIDAEHLDTYKNLDDVKKTFLQYLKKIPSDGMVVANWDDRNVKDVVWQSKKRVIWYSQKDRDAEEIKKHLKIPGEHNLSNALAAARLGSLLGIPYVHILQALSGFRGVWRRFEFK... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
Catalytic Activity: ATP + L-alanine + UDP-N-acetyl-alpha-D-muramate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine
EC: 6.3.2.8
Subcellular Location: Cytoplasm
Sequence Length: 461
Sequence Mass (Da): 51858
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A0A7S0SQZ1 | GGGGGGGGGGGVISNSSGGDEGDGVAAGVDAPSASGAADAGGGGRGSGSTPEELGLGSVDAGVSGLNGRPVEWHETLDAVPPGPTILVAHEFFDAMPVHQFTRTKRGWCERLVAIRGQAPRPTSSAKSTAKPGSGGANLVEGSAAAAIWSSRRVDNAQPANGTDILIDTTDTADT | 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... |
A0A6V7XXD2 | MSIFVPIVFVLLQLLQGCQSFGPAAKKTITLQSKLVVTKNFDCGFTRYIPDPKKMGDGGANEYQQPVIEVRNGATLSNCIIGAKEGFKAADGVHCEGSCTLKNVWHEKVGEDAVTFLGKFSDKPPSILMIGKIVLRFVIKCKYSYSFT | Function: Pectinolytic enzyme consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin methylesterase and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins. Favors ... |
A0A142CDA0 | NHSYFMQDGFKISFYYFLFSELMFFFSLFWFFFDSSLIPMEEIGESWLPKGVEMVQPFSIPFLNSLILLSSAITLTWVYYNFLMLKKKMLFYFFTLLLGLMFLMLQFFEYKMMIFSM | 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-cytochrome c oxidoreductase (cytochrome b-c1 complex, comple... |
A0A6V7VIE9 | MFEQPQHSSSLTPSLSDNSISGMTNNSMLNSQTLEEYCWYWGAASKEEISAAMENQQNGTFAVRDASTKGQYTLTLRIDGTNKLIKILVENGRCGFTQDSMDFDSMASLVQFYQTCSLRDFNEKLDTCLLYPLNSPQSLTCQNSMKSDSTIDPSYRVSLLKCTFEAIHAEYDRVSRRYDQLFNQQLALNEEYNRKQRTESAYADVLKIFERKIAELKTTISGEKDLNDRDRESLTINIELQEERMEEIGKAQNLMRAAIQNIGLSLQKINEELGRLKPLLLKLHKKCEKYRDKLLEMSKQKVTHAQLDRVVQSVSLALDS... | Function: Catalyzes the post-translational methylation of isoprenylated C-terminal cysteine residues.
Catalytic Activity: [protein]-C-terminal S-[(2E,6E)-farnesyl]-L-cysteine + S-adenosyl-L-methionine = [protein]-C-terminal S-[(2E,6E)-farnesyl]-L-cysteine methyl ester + S-adenosyl-L-homocysteine
EC: 2.1.1.100
Subcellul... |
L2GWC0 | MSEIKNAQNVLNDPTKRIEEKMRALFYLRNVLTDESALIIGDAIYKNTSVLLKHEMAYVLGQMKLQCSKEILIKVLDDENEDEVTRHECAEALGNFNDKEMVPILEKYLRHASLPLKETCYLAIKKIQESKDGVDLSKFDSRDPAIPLFKDINEQNIECAGKMLDDPNECLYRKYKAMFYLRDCGTEKAKKFLVGAFKDESALLKHELAFIMGQMRMDEGIEVLNKVMNDGNEHGMVRHEAAEALGAIATDDCYRYLQKNIDSDCDILRESVLVALDVLRYENGEETEYACVL | Cofactor: Binds 2 Fe(2+) ions per subunit.
Pathway: Protein modification; eIF5A hypusination.
Function: Catalyzes the hydroxylation of the N(6)-(4-aminobutyl)-L-lysine intermediate to form hypusine, an essential post-translational modification only found in mature eIF-5A factor.
EC: 1.14.99.29
Subcellular Location: Cyt... |
A0A6V7XLS8 | MDPTLNFKNETTRVKYIYVIQANPESVELLDIKNNKLVTEAFHSDRPLINYFNHPMTHFGPMMATACKETIQQHQLLQQLTNEKFDVGISEMYEYCSAALFHKLGVKTKLAAFAIPLLQMVGRKFDIPSFASFVPNTFASHLGLQSSFYYRFFNFYNEFYDWIWMDDYILREEEQIVLQEFGSDFPDLKYLTKKVSLVFFNSNPFFEMPRPTSNKIVYIGGLVDNLATEANKKLEPKIKKILDEAVEGAVLFSFGSIADTTKLNLKIIEGIVKGFRRFPNIQFIWKLDSETIKNMSELISPVSNIHTFEWLRQPAILVHP... | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
EC: 2.4.1.17
Subcellular Location: Membrane
Sequence Length: 397
Sequence Mass (Da): 45557
Location Topology: Single-pass membrane protein
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Q4SKA0 | LQKAIDLVTKATEEDKAKNYEEALRLYQHAVEYFLHAIKYEAHSDKAKESIRGKCMQYLDRAEKLKDYLKNKDKQGKKPVKESQSNDKSDSDSEGENPEKKKLQEQLMGAIVMEKPNVRWNDVAGLEGAKEALKEAVILPIKFPHLFTGKRTPWREHLALRLVKNLFELARQQKPSIIFIDEVDSLCGSRNENESEAARRIKTEFLVQMQGELTPTGPPGMTDPRNPGRKTLPNTALLPGGVGVGNNNDGILVLGATNIPWVLDAAIRRRFEKRIYIPLPEEPARAQMFRLHLGNTPHSLSDGDLRQLAHKTDGYSGADI... | EC: 3.6.4.6
Subcellular Location: Membrane
Sequence Length: 423
Sequence Mass (Da): 47544
Location Topology: Peripheral membrane protein
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A0A357LGZ3 | QDMEFVQFHPTALYLPSSPPFLLSEAMRGEGAQLRNNKGELFMHRYHPMGALAPRDIVSRAIWAEMAATKARHVYLDVTHLGAEFVKRRFPTIYATCLRYDIDITEEWIPVSPSAHYMMGGVWTDLNGATTVPGLFAAGEVACSGVHGANRLASNSLLEGLVFGARAAMAAVAYAGRHEVPSLAAQEAALKTEHFGSLDDAEKLRSSLRRAMWGHVGVIRSGESLIRACAQLSRWAQLVAQPFSNRAALEVKNMVHVGQCIAEAALWRENSVGAHYRSDFPQAKRPGWQQHSRLSMGEGISGKKSRKSRGLLLALRGRTG | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate from L-aspartate (oxidase route): step 1/1.
EC: 1.4.3.16
Catalytic Activity: L-aspartate + O2 = H2O2 + iminosuccinate
Sequence Length: 320
Sequence Mass (Da): 35103
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A0A6V7WW13 | MLFLSLSLHFLIKILILDYITNQLVNLINKHFPSIIISICTLSEPLKKEYAKINNLNFNDLMTDGKAKELVRKEMIEFGEKLRKEDFGIFCRKAFIERKIQNSPPLPTTNPSTTNKFKEIILISDCRRPTDFEFFKNNFKNSSIICVRINSKIEIRQKRGFLFIEGIDNEESECALDEFKNWDFNLFNNEEEKEGGKGEGEVEKELKNIINYLKQLFN | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via mevalonate pathway; isopentenyl diphosphate from (R)-mevalonate: step 2/3.
EC: 2.7.4.2
Subcellular Location: Cytoplasm
Sequence Length: 218
Sequence Mass (Da): 25586
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A0A7S0X5B0 | PPCSSARVRAPLHATPHPHIHAPPSSATPPRGLPEITALWPYEHAARHRHPRRETGGTQLFGLYSHSAFVSAGLGGEVLARVGGTSMALRHGMRAATSSVLVWGAAGLMRAPLIGTRPSACHEATVWRSRAMGCAPASPTACGGSASSNQGAMAIPASTSASDASGFAAARNVGRGGMMGRREPVAAVLPFSLRALRHFSASSHAGDKLSGDVLGDLLGNAKAVAIRLELGALAEVQTHMRYAEFADVVKANSGGDTKESEVAEACRTLQAAGVIIRLEDVVYLHPSELTRDVLRALPTVPSSVFGVTEEEMRELEAELV... | Function: Mitochondrial inner membrane calcium uniporter that mediates calcium uptake into mitochondria. Constitutes a pore-forming and calcium-conducting subunit. Mitochondrial calcium homeostasis plays key roles in cellular physiology and regulates cell bioenergetics, cytoplasmic calcium signals and activation of cel... |
A0A6B7KA21 | GDDQIYNVIVTAHAFIMIFFMVMPIMMGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLIMSSLVESGAGTGWTVYPPLSSTIAHSGASVDLAIFSLHLAGISSILGAINFITTVINMRSTGITFDRMPLFVWAILLTALLLL | 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... |
A0A6G8IRX4 | WFFGHPEVYILILPGFGLVSHIIMHESGKLISFGHLGMIYAMLSIGILGFIVWAHHMFTVGMDIDTRAYFTSATMIIAVPTGIKIFSWIATMQGSFKYKSPQMIWCMGFVFLFTIGGLTGVILANSSIDIVMHDTYYVVAHFHYVLSMGAVFAIMASIIQWFPLFTGTVMNKKFLKIQFSIMFIGVNLTFFPQH | 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... |
Q4RGA9 | MQEVQQSKEKTLANNRTLAEQNLALQPDLEHKKEQLTKSYRCLQEDFESYQLRKSTLDHRTGSSSLDTLLALLQAEGAKIEEETEVSAPLRPWWGFSVWSLPPPTRVTVRFPPRLSPPEHGRLLPGRGNDPGPLHRRVSEQQEAGSPEEGEDREAAGGGAEGPAPPPGLRLRLPLSGRVGGGAGGERRQLLPHGPGPEEAPAPTVTACPRSEPGPRRRPSARRLLRIAVPRHPSQNGPALSQRVFGLPQPLPVPVPPRAASEAPPAPGPTARFYHTVESVRGDAAYRPEGFSLQLLGAAHPSFHPPKNPPTGDLGTGAPH... | Function: Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies. May be involved in cell growth and differentiation.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
EC: 3... |
D5BVE1 | MIGKWESRVDRALASRLGLAVGLALIFLFAFTLRFDNLSFWLDNPERTLFGDPPRPLMLTVDSYIYLDLGRDLLEGTYESDLPTRHVPQGAERPPTAPLLAVMLAGLQKLTGAAPEWIAIVLPPFLGALIVLPVYMLGSLFATLVWSTPSPSTRRIAGLAAAAAAAASPYFVFRSSIGWFDTDSLNVVFSALAAALALRAALARDQRQRIIAWVLYSLVLVLFLWWWNTVPHIVFGLWVLPGLATLLFHLPRGWELVTVAALVLLGLVGAVAIAGWQVLNPVAQFQMVQGLFTYIAEQTGWIFPETGQAVSEQQATGWDQ... | Pathway: Protein modification; protein glycosylation.
Subcellular Location: Membrane
Sequence Length: 742
Sequence Mass (Da): 82411
Location Topology: Multi-pass membrane protein
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A0A7S2SMR7 | MATNPNFARNQDMPPKGGYTPFDVRRKLPKARMSGAFMFGAVSLMTMYGYYQIGQTNIERRKVRRETRERRAHILPFLQAEEDVRYNLAVAVYEDEERRIMKDVPGWEVNKNVYNHKEWMPAFDNRPW | Function: Complex I functions in the transfer of electrons from NADH to the respiratory chain. Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis.
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 128
Seque... |
I0GYF5 | MLSSHHNGLKTAALLGVLTGLILTVGYWLGGSGGLVVAVIISLATNAFSYFYSDKIALRSMGARPVSEAEFPELYTMVRELATEAGQPMPRLYVSPAMQPNAFATGRDPQHAAVAVTVGITRLLTLRELRGVIGHELSHVYNRDILISSVAAGLAGIVTMLAQLAFFLPFTSSDDEDSPNPAGLLLMMILGPLAASIIQLAISRNREFQADASGATMTRDPLALASALEKIHYGTQRMPLPAEGQLTSSAHLMIANPLRGGGIAGLFSTHPPMEERIRRLHVQASLVR | Cofactor: Binds 1 zinc ion per subunit.
EC: 3.4.24.-
Subcellular Location: Cell membrane
Sequence Length: 288
Sequence Mass (Da): 30720
Location Topology: Multi-pass membrane protein
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A0A8I0GD33 | MRASSEAAREAGRDRLIALIAEDGETAQTLSGELFALADLLNDQPKVAAALTDPTRAGEDRARLAERLLTSVTPACRDIVATMARQRWSHIDDLAHAADDLGAQALAIHARSRGVSEQLRNDLFDAEEVIANHRDLRITLSERGQLSAGDRVGIIHRIFDGKVSQDAVTLLERAVRAEGAGHIASTLRRYRDDVAAIEGVTIATVHAATTPTEEQVERLRRALSTKMGCDVVLNVAQDPELVGGMRVSVGSTIYDGTIRSALDEAERRLAGKARA | 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... |
R6B7H6 | MREVSVEDFKLFKEKVDNFITKDAETFYFRNLMEAIHDSDYMNEVNSIIEYVSKERTAKEIDELFQMLRAKAEGQFELRDKTEKYEKKVNYSLRGLAYFCLVEALNENSSFSEKIIEDIKKKYGKDYLDIVKKIDRAYLSVDGKTILKEQNLQLPNDEEMKKYLVMKKWQDEQRLYSMKRIRPLYPLELEYIDEPDQNLMLIHKKTLVKRAKEDLKKMKIVPIEYLAKLYEAGLEDELKDMIGGKALGLTKLRASEIRIPKTYVIPYYVEIEDNEIKNLLDENKKYAVRSSANAEDGGIHSFAGMFDSYLNVEKKNITDR... | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Function: Catalyzes the phosphorylation of pyruvate to phosphoenolpyruvate.
EC: 2.7.9.2
Catalytic Activity: ATP + H2O + pyruvate = AMP + 2 H(+) + phosphate + phosphoenolpyruvate
Sequence Length: 598
Sequence Mass (Da): 69132
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A0A0L0BGB5 | MNNRTPHSAASQDAGRHADEHLDDGHEYFADDYEHPEPVEDFFATQDQGAHGAKKPRSKAKRRKRLRRTVVMLVVLGIFAGTVYGVALMLRDMLGFDTVTDYAGPGGDETVFTVDSGAGPLAIANGLQAADIVADSGTFVSALTSIAGGREVQPGEYEMRLQMSSADAAEALLGDDPTLVSYAAVARDLRQNEVFGILSESTGIPVAEFEALAADPTQFGLPAQALSLEGYLHPGEYRFDVDATAPEMITEMITATQDRLVQDGITDPAEQYRILTIASIVQAEAGEGDYATVAGSIDNRLTPGNTETNGLLQSDATVAY... | Function: Functions as a peptidoglycan terminase that cleaves nascent peptidoglycan strands endolytically to terminate their elongation.
EC: 4.2.2.-
Subcellular Location: Cell membrane
Sequence Length: 414
Sequence Mass (Da): 44478
Location Topology: Single-pass membrane protein
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A0A6V7W633 | MVSTSGQIDCSEVQKPIGPQPLTSSQLNKEVDEGEISDEVFSGDVDTRNASPSKNQQKETMNNELDAVTLSNLVRAPPPAVSRSVIVQALYLLIEHHNNKEKQTDLDEYTITCRLRSRNSATQGKEGAIVRHKDGPFNQTNHIFIASRLRDLEKLGRAKLVSSNARYEEIKQPAPMNLFTLIRIASERLNFSPKYTMELANRLHKSKLLTNPTTFAKAYPAGFPNEDFIKNIIKQADELCKLRVDTRLILANFVRPKSKELRGFNSNNTTVGGVNSNTSSVPIHPCILSTSENLETMLDQCLENDEMELLKLICQYFFAT... | Function: Introduces a single-strand break via transesterification at a target site in duplex DNA. Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. The scissile phosphodiester is attacked by... |
Q4SAD1 | MRRQMRRRALSSLKELDAFPKVSESYVETSASGGTVSLIAFVSMALLAVLEFFVYQDTWMKYEYEVDKDFSSKMRINIDITVAMKCQREYRNPLKCSRRRREDDCCVFPAADVGADILDLAETMITSNGLQYEPTVFDLTPQQRLWQKTLLLIQSRLKEEHALQEVVYKTLLRGAPTALPPREDAAVEPLNACRIHGHIYINKVAGNLHITVGNLQLLPSDRPPVLRRGAAGRRQSAGRHGEDYLQKQPDVPVLRHRGSHPVGHAPDIGGHAPVFRDRAGEQSGRGCGGAPCRSLRAAFLPGAGDRPRRRQPRRLGHLRE... | Function: Plays a role in transport between endoplasmic reticulum and Golgi.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 356
Sequence Mass (Da): 39817
Location Topology: Multi-pass membrane protein
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A0A7S0X8Y8 | SELAARLAARAASNAREVEVTDRQGNACWVEKTDAGADADADALRDFIVAATAKDCSVMLALRRLEYHGRDKDARLIPAFGNEVGNSGMMMIDVAAPGGRRIVGGGGDDSDSGRSGGGSGGVHYKQTISGGGGKSLGVHYGQTVRDSDPS | 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: 150
Domain: The EXKPK motif is conserved in inositol-pentakisphospha... |
A0A7S2RTL4 | MIRGSGRVVVVGINVLDMKSFVKRIPVVGETCLSTKFEEDFGGKGANQAYQASLLLKESGCPVSFVSKIGNDARGHTMVSHMQKAGVNMDHVSIMEDIYSGCSSLLVDEEGQNVIVVSAGANAYLDESDILKAKDVITDSSVILGQLEAPLEATVAAFELASAQDKKTLKILNTAPIPSKLSADFYRLLDLAHIICPNEIEAEQLTGHSDPTQAADTLLEECPNCDAVVVTLGKDGALLAKRNFKTKIAGVDGIVAKDTVGAGDSFMGALGASLALGDTLLEAVEKANRVAAFSVSNYGTQSSYQSTFI | 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 ... |
A0A061HBA9 | MSNPRSAAAGTVKVKKEVEGTLEDHPTIPGAQVLTTADGKKKLIRQRGKRGGAKNNKKTSSSTSDAVRANKAGKPTKDAEVKADAAKKVKKDKNSDAPSEHSLRIARYHTLEKELARTTDPAEQARIKAEQEQLGGLEAYQEDSLKGGDRLKGGESGKWCAEQVEKLRGKKAMRVLDVGAIAGTSYDKFPWIKATSIDLNPRSERVQKCDFFDLPKPANEEEKFEMVALSLVINFVGDLKKRGEMLLHAHHYLRPGGYLYLVLPLPCLTNSRYLTHDHLRSIVSSAGYDVVVQDDSKRLTRWLLKRKKSPRNKWDRTVYR... | Function: S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the N(1) position of an adenine present in helix 65 in 25S rRNA.
EC: 2.1.1.-
Subcellular Location: Nucleus
Sequence Length: 354
Sequence Mass (Da): 39198
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A0A162XHY8 | FIFGAWSSMVXXLSMLIRAELGCTSSLIGNDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLSAPDMAFPRLNNMSFWLLPPSLTFLLTSSMVESGTGTGWTVYPPLSNIIYHSGASVDLSIFSLHLAGISSILGAVNFISTILNMRVKGNLFDKVTLFSWSVMITAVLLLLSLPVLAGAITMLLTD | 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... |
A0A1E5IGW5 | MAENIKDKIKAVSFEIVWEAKGIDFVSLKCRNPLVGDRQSQGIVAGFVSMEDGTGIVHIAPGHGQEDYQAGLEYGLEIISPVNDKGLYTKEVPEFENIHIYKANPLIIEKLGREGKILAKLRLTHSYPHCWRCGNPIIFRATPQWFLSVEHNDLRKKLLEAVKNVRWVPKYSGNRITAMLERRPDWCLSRQRLWGVPIPVFYCKECGEPLLDSKVIDKISALFGEKGSNLWFEMSEEELLKGTGAKCLSCNSANFKKEEDILDVWFDSGVSYEAVLSSGNYKDLEYPADLCIEGSDQHRGWFQTSMIPSVAVKGKSPYKN... | 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 ... |
A0A4Z2DDD0 | MSADGVLNDFLAREKKDLYGLESDLNFLPNGDNNGSEHPKVNDEPECIRRWAISFQKRIDVKDDAERKSLSVLEEQGLKDLHDWALQYRDSLSRGQKLSRAHDKELRSAQKKAAEASVGMAQVDAGQAVLWERKEQTPKLSRQIQRIINGI | Function: Clathrin is the major protein of the polyhedral coat of coated pits and vesicles.
Subcellular Location: Cytoplasmic vesicle membrane
Sequence Length: 151
Sequence Mass (Da): 17171
Location Topology: Peripheral membrane protein
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A0A6V7XZ17 | MAGCRFGQSMGSYVSWLYVFIKALYLLNVTGQFFILNSFIGSTYRWWGIDVLNALLAGENWQDSPIFPRLTLCDVPIRRLGDTPRYTLQCHLRINTYNEKIYLFIWWGFLLVSILTFFNFWYYLLVLICLPCTQENSVRHLLKQDRHENMVYSAKKRDRKLIKSFAEEALCKDGILLFWFIEGHAGPLIAREILGEIFDYYKGKMVNFVDFYIDS | Function: Structural component of the gap junctions.
Subcellular Location: Cell membrane
Sequence Length: 215
Sequence Mass (Da): 25399
Location Topology: Multi-pass membrane protein
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L0EVT6 | MKIKNVLLSSVACLLAVSSAKAADAVKAEPETAEGVRVCEAFGSGYFYLPGSETCFKIGGYLRFEGDYGKNQYGTAGNLRSWDAFARAQVDLNAKTDTELGDLSSLISLRADGRNSTSRSVFLNQGYLSLSGFKVGYFRGWWDDDIVGETDTLANDETRLVSASYTYNAGLFGAGISLDGLGRYGNKDIGVGGKLSAAFGPVKANVIAGYDGGTKKAAVRGIVSSEVGPGTLEVAAVFANGMNYYYGVSRASLAVGYQLHVTDKFKITPGFQYFWGLGKYSAYADSAGAPVKVSLNTWRSGLAFDYEIIKNLDALLSVQF... | Function: Forms passive diffusion pores that allow small molecular weight hydrophilic materials across the outer membrane.
Subcellular Location: Cell outer membrane
Sequence Length: 346
Domain: Consists of 16-stranded beta-barrel sheets, with large surface-exposed loops, that form a transmembrane pore at the center of ... |
A0A4Q4NMD5 | MDSLGGGIANADLSKLSDRDKQELQQFAMNEGQKARIQSSIHSLTDTCFRKCIPAGTVKNGKLDKYEEPCMRQCVDRFLDANMVVLRELERLRG | 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... |
Q7Y435 | MFNLEIDDLMIESFEKWLLTEEEENFGSIAPVQCLKPKQNPKQLFAVQTRDKDVIVRLCNFTNKTPKIIRMGDKTAHVVLCEMNKSGRIVQLKNGLGDNPIAVMASAFDVVMETARKSQLDAVMFRFNVSRMKGKTELVKRVIERLVRRTPKFEVFQQEVMTSKKIALVVVKRRGMAIDKIKGIKLDESLFTKVESDLGDRWVSKATGESLTKDEAYAASLVSEEERNAEAEQRVAAKSRLTKEEMLKTQATYNSDYVNHPEKINLKPEEDITEAEPKKQFNTLIDRQALERSTARSLNDWTSDIITRYGFMRTIFESEA... | Function: ADP-ribosyltransferase that efficiently ADP-ribosylates one of the two alpha subunits of host RNA polymerase RPOA on an arginine located in the C-terminal region. ADP-ribosylation of RPOA alpha subunit enhances the transcription of viral early genes. Also ribosylates RPOA subunits beta, beta' and sigma 70 and... |
Q4RI45 | MNEPGPAVSATNVGASGRSPSKTVAPRAAGSTVRQRKATSSGTRSGSRSTGSAGTGGMWRFYTEDSPGLKVGPVPVLVMSLLFIASVFMLHIWGKYTRS | Function: Necessary for protein translocation in the endoplasmic reticulum.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 99
Sequence Mass (Da): 10274
Location Topology: Single-pass membrane protein
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A0A0S1AZZ7 | MAGLQRTTYGVVAAGGALILLCGLLPWTWRAIPAHPLAWSVTSVILVAAYMALALLLLLPRLARVRVLAARDVSELETSRKALETGNRELQAMAGRLFSVQEDERRAISRDLHDDIGQAVTAIKLAAHAAMDEDDAQRRREDLEQIVELVDSTVVRLRNLSMLLRPPQLDALGLEAALRWQAGQLFRSSPVELLMDVEDLPQRPHNEVEQACFRIAQESLTNALRHALASQVRLCLEDDGGGRLRLRVTDDGEGFDPDGPRGLGLVVMRERAQSVGGWLRIHTAPGEGTQVELHLPYRMPQAAACQGA | 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... |
A0A6J1XBH4 | MAQELSEKDLLKMNVEQLKKEVKNTRVPISKTGKEIKDFVEAEAGNDPLLKGVPEDKNPFKEKGGCVIS | Function: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.
Subcellular Location: Cell membrane
Sequ... |
A0A6V7X3E1 | MVVGGSSLIGADTSDSDLDIIFIIPITCLSNEEINKCRECKYNIKQYQKLCRDHDILFGDGEYVNSILKHLVNLINKARNDEPTNIYQINFINGRVPLIEINYRSQKMDILLAPIPFKNIPESLNLTSYENDEIINDNINTLNKSIDKMMETDDIQYIKSILILTGYRYTYRAKFHLIHYSTRENFTLLLRAVKLWAKKKHIYSNIFGYLSGSILIVMVTKICLIYPFGEINFLLQQFFQIYGAWSWPLPLITEQMTLNILEDKFKNFKNFWTFDKLNSSEDGLFSGDKMPILTSLFPEQNTAHNVNEFTLKIILREMKK... | Catalytic Activity: ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide
EC: 2.7.7.19
Subcellular Location: Nucleus
Sequence Length: 340
Sequence Mass (Da): 39664
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Q5BXE0 | LNPSSRLKGEKDWKKYETARCLHKVIDKIRADYRADFKHKEMRIRQRAVALYFIDKLALRAGNEKDEDEADTVGCCSLRYEHIKLHEELNGQPYVVEFDFLGKDSIRYQNSVSVPKRVFKNVKLFLKNKKENDDLFDRLNTSVLNQYLRELMDGLTAKVFRTYNASRTLEEQLERLTNPDDPPHAKLLAYNRANRAVAVLCNHQRSVPKSFAKSMENLQKKVQIPYNSSSYIADRCKT | Function: Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at the specific target site 5'-[CT]CCTTp site in duplex DNA. The scissile ... |
A0A2H1VV58 | DPISPHQVSIVFHSAATLKFDEPLPVAIDQNVRSVQRLLDICDQLPNMQAFIHVSTAYSNAELAVVEERVYPAPVPLAQACTLAETLPGDLLGQINTQYISPKPNTYTFTKALAETVVQEHGNRGYPVAIFRPSIVISSHRHPFPGWIENLNGPSGVVVAAGKGLLHVFCCRSAARADMLPVDMAIDTLLCVAWETAVD | 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: 199
Sequence Mass (Da): 21609
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A0A7S2R987 | MDAVKRKRQERNKRRAAKKRSRKMDAYSKVGGKVIGVVGTDGGAIGGDVAGAGKESAKVGKSKTVKRVDCKSKVKSKSMQKLASVFKIDDGDLARAGKEVLAWMIAPTSVETFFQDNYEDKPLYISRPDQRNYYEGLLSKKLIQQLVKDGKLKHNRDFSLTQYRNGSRKTLKHDTEQIATSSTVWPLFDGKEKCSVRLLRPHEHSTFLWKVVSSLEGFFKCGGGANAYLTPRGSQGFAPHYDDIDALIIQLEGKKHWTVYEHYKTPQSVLDKEQSEEGDKSEEGDDKEDDEEEEEESEDDEVEKARVAKDLFPRYPLKSS... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Oxygenase that can act as both a histone lysine demethylase and a ribosomal histidine hydroxylase.
EC: 1.14.11.-
Subcellular Location: Nucleus
Sequence Length: 581
Sequence Mass (Da): 65698
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A0A6V7U3C0 | MTSRPLIYGTSGFRAKADEQLQLIVYRAAFYAAVRAKKLGKAVGMMITASHNPGCDNGLKLVDPSGRMLAMECEEELTKIANGTEEEFEKFKNEEIQQIKNNEEKDNPTPIIVIATDTRPSSAILYEEAVKGIKLLGISVDIKYFEHHTTPQLHYIVRAINEKKPVDDYIQQFRRALEKSREFLNFEENTNLSPLYLDCANGVGSLWIAKYLENNGFICKNGLDVTKEGEVENLDKNIILVNLFNINTNDGELLNNGCGADFVKIKTSLPANFPTNLPVGTRCASFDGDADRLIYFYPNLEGKICLLDGDHICAIFTKFI... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route I): step 2/2.
Function: Catalyzes the conversion of GlcNAc-6-P into GlcNAc-1-P during the synthesis of uri... |
A0A1C8ZRZ6 | MKVLFFRPESDGEDTYNFNTTINGIEIINIPLFKVECIQYNLPEDVEMFDALAFTSRNAVRCFKDVNLIKDLKVYAIGDETAISIKERFGICPIVPKKFTSMELAEKILRDGVRTLIAVRSKLANNDMRKTLENKIRYIEVYDYDLSTIYNNIELAGKLISNCEVDGIAITSSSIARVIAKYINKECMTKIFSIGPVTSRVLIEIVGEAKIIESKTHSISGILETIVKVMGNNG | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 3/4.
Function: Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III.
EC: 4.2.1.75
Catalytic Activity: hydroxymethylbilane = H2O... |
G2SPK7 | MRKKDDVLEIGVLNLMHDKEDTKRRFERVLTREDCRVNLTWFYPVMHYQDREVPENVRQMSQPLDLNKVKELDAFIVTGAPLEKLDFDDVTYISELQELFDCLSTEGIEQLYVCWGAMVAANYFYGVDKYLLNQKLFGVYPQVILENSPLLEGLSDGFLAPHARYAELSCSQVREVPELSVVSVSETNHLFLAEARKERQTFLFSHLEYGRDALDKEYYRELQAHPEDAPVLAKAANYYDDPAKMTGMRFGWGKAQRHFFENWLKQAEENRFKKVCTQ | Pathway: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine from L-serine: step 1/2.
Function: Transfers an acetyl group from acetyl-CoA to L-serine, forming acetyl-L-serine.
Catalytic Activity: acetyl-CoA + L-serine = CoA + O-acetyl-L-serine
EC: 2.3.1.30
Subcellular Location: Cytoplasm
Sequence Length: 278
S... |
A0A2H1WI93 | VRNRMGFANFNLLLFGQVISYFLASKLLFDKVNETIHIVIDEYFHIPQGLAYCNGNYSYWDPKITTLPGLYLVSSVVGTYFKCNTYNLRVFGNQYINDVRLSKRSLIAKDVDKSKLKRYYGLKDVYYAARYHLSTGPNRTTIPFRNRETAEAQAVINTITIFSTLTPTIKFFIN | Catalytic Activity: a dolichyl beta-D-glucosyl phosphate + alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodoli... |
A0A2H1WVQ7 | LTRRQRIIQRNRTERLSDLLDWRNLGIYYRQARAEALKIVYPDYVDHMDQELGKRFNYPRPISEPPSPTHSMRRERKSSSSDDANTNEDTIPNEDIIAKKNQINIRKSLEILNISDDGTDPALEISFEKPNFAESEHENYRTPNENFLEPLNEAMVEQIDQLIAKLQDCA | Pathway: Glycan biosynthesis; glycogen biosynthesis.
Function: Transfers the glycosyl residue from UDP-Glc to the non-reducing end of alpha-1,4-glucan.
EC: 2.4.1.11
Catalytic Activity: [(1->4)-alpha-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->4)-alpha-D-glucosyl](n+1) + H(+) + UDP
Sequence Length: 170
Sequence Mass (Da... |
A0A6V7XZD1 | MDLKRMIYFLEVIITKTINIDYLNILNCYQLIKMCIKYCFCNYNDDESQKCNYDEKTCIKDEFAACFRVVRQEFNEETKTFELIHLFGCAPLEKGSNGSHLTCNAWRFAHSSPKSIFCCYEGNYCNKHLTIPSFPLIERSTKKIEYSTSYSSIYTLESFFFTFFGFLIGLCLIILFAIPLIRKKRGGKKEEEEIISLTKNNLENSKSFFEDSGSGAGRIILNKRRIALDLQMKEIFSKGRYGEICKAIYRGSYVAVKIFNTTEEESWRNERDIYLSQMFNHENILQYIAADILSNVDSLTQMLLITDFHPLGSLYDYLRS... | EC: 2.7.11.30
Subcellular Location: Membrane
Sequence Length: 398
Sequence Mass (Da): 46165
Location Topology: Single-pass type I membrane protein
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A0A6V7Y6S5 | MNQHPKGKFEHFPDFRNVMYIGGIVVEEQGILTRRKTKKKKPECIVYVAFGTVYEDGGLKDNLLEMLNIFNGHQNCLFKIRIGKNEITETYKATNIEFLEGFAPQQEILAQTNTKLFISHCGQNSFNEAMYAGVPLLCIPKFADQFYLSSLAEHLGIGKFVWVSRREKINENGIEVKKEIKNENFIVDFSEALDEMMSGNYSRNDYKEGCMQLRTA | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
EC: 2.4.1.17
Subcellular Location: Membrane
Sequence Length: 216
Sequence Mass (Da): 24826
Location Topology: Single-pass membrane protein
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A0A6V7XRM4 | MNVAGGMTIDDAKFMINDVFLNYHNFQFKIKLPHFTPTNVQNIEITNEFIEQKQILFDPNTKLFISHCGQNSLTEAIYAGVPLICIPYDGDQFLNSSLIEHLGIGIFVSLWEDNKKKNKNPAFGNEFTSAVAEMLGK | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
EC: 2.4.1.17
Subcellular Location: Membrane
Sequence Length: 137
Sequence Mass (Da): 15474
Location Topology: Single-pass membrane protein
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A0A4R1HEC2 | MTESEKKAAQHNLADASERSSRRRLPLPDWPTTRQFLAALSALGVTLLILGLMNIWDFLHAEQSNWLHLANSVLLVSGIALLAFTFHVARRDLVAPLTELRHWVNEMHNGKLSARLPKSDQPDFSKLYRDINALAERLESLSLDMQSEVEQQTNRIQQKTHSLEILYDIAANINAANDLEDLLTRFLHTLKDVVNARAGTVRMLTNDGNMQLIASSGLSPEVVKKEQLVSIDRCLCGQAAQNGEVYALDDLKGCGQFAGRPFFDTEKVEMIAVPLRYRGKVLGVYNLFTKQHGLVEREDMKDLLTSIGHHLGMAIEKSRL... | 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... |
A0A1T4WZQ3 | MFSRIQQKYPGIRFANLGIGEICVSSLPLAVSTVLGSCVAVTMFCPVTRTGGLFHALLPERAPHGKLHDAEPCRFVDEGIRELLRQMERSGADMPRLVCKIFGGANAVFEEFYAVGMRNVDMARQVLAEEHRSVQSEDVGGTRGRKLFFITHTGEVFTKKLSSDVCFLPEGNANR | Function: Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis.
EC: 3.5.1.44
Catalytic Activity: H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)
Sequence Length: 175
Sequence Mass (Da): 19320
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Q4SY57 | VAIIIPYRNRHEHLKHLLFYLHPMLVRQQLDYGIYVINQDGEGVFNRAKLMNVGFAEAAKEYDYECFIFSDVDLVPMDDRNLYRCFEGPRHLSVAIDKFDFKLPYSTIFGGVSSFSKQQFLTVNGYPNTYWGWGGEDDDMYKRIVFHGMSINRPDHMKGRYKMIKHQRDEHNEVNPKNPDKLSHTHETMDKDGDGGRYMPRDCLSQHKVAIIIPYRNRHEHLKHLLFYLHPMLVRQQLDYGIYVINQDGEGVFNRAKLMNVGFAEAAKEYDYECFIFSDVDLVPMDDRNLYRCFEGPRHLSVAIDKFNFKLPYSSYFGGV... | Pathway: Protein modification; protein glycosylation.
Function: Responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 430
Sequence Mass (Da): 50500
Loc... |
A0A6V7V162 | MFYKNIKLFILLIKCLFIFIQKSEEANILVISPALSLSLIYKMGHLADLLVNAGHNVTVFIPEMDNIEETGTKLAQKIIRMKGLFNVIEQITNFDAFNEEISSYSARRSEDEGMVIYCESILKKKDELEILKNSNFDLAFSNMIDYCLQGIIKYLGIEKQIWISTGPLPEGPLWFLGIPLPLSISPLLQQTTMLGPRMNMMERATNIWQFALSWYSVMQTLRKENELFRSYISPDFPSLDKVLAEVDLAFVYNDEFLDPALPTLPKVISIGGLGIKPANYSINKFGIKLVKAIESSKKGTIIFSMGSITDTKFFNKEKWQ... | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
EC: 2.4.1.17
Subcellular Location: Membrane
Sequence Length: 534
Sequence Mass (Da): 61580
Location Topology: Single-pass membrane protein
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A0A317PHP0 | MTKLRTTILLSLAAFTLAGTMQPSQAGNGWGPGDFKPGIHKPFKPGFKAPGPKGPGPKKPHHHHDNNFEGAALGLLGGMIIGSAIANAQQQPVYVDSGNAHVAWCIDRYRSYDIPSDTYMSNSGYRKYCNSPYR | Function: Has immunoglobulin-binding and hemagglutination properties, and can bind to mannose. Essential for virulence. May be involved in LPS biosynthesis or polysaccharide transport.
Subcellular Location: Cell membrane
Sequence Length: 134
Sequence Mass (Da): 14486
Location Topology: Single-pass membrane protein
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A0A1E4ZIN9 | MIEDFTEPSPFKPVKHQWAYDHWKSQQQQHWIPEEVEFGQDIEDWQKISDNERNLLTNIFRYFTQGDIDVAGGYCDKFIPYFKNTELRMMLSTFASMETIHIDAYALLISTVNMPDTEFNAFNDYKEMSDKHEYLNNFNMNSPIDVLVSIAVFACFTEGLQLFGSFTMLLNFSRFNLMKGMCQVVTWSIRDETIHVSGMVRLFHAFKKSLGIKDSEIHERITDIASDVVKLEEAFINLAFEMGDQKGLTAQETKQYIRYLCDWRLKNMGIKPIFNIKEHPLPWLIPLINTVEHANFFEARATEYSKSSTTGAWGDAW | Cofactor: Binds 2 iron ions per subunit.
Pathway: Genetic information processing; DNA replication.
Function: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.
EC: 1.17.4.1
Catalytic Activity: [thioredoxin]-disulfide + a 2'-deo... |
Q6QUX4 | MTFMEVAKPKWYERALVIAVQGVFFNAYFAAYLISPKLAHRI | Cofactor: Binds 2 iron ions per subunit.
EC: 1.10.3.11
Catalytic Activity: 2 a ubiquinol + O2 = 2 a ubiquinone + 2 H2O
Sequence Length: 42
Sequence Mass (Da): 4892
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A0A2H1WHD0 | RVVALYVAPAVVREQLRELAARAPDLDDTEVEISWGAREVRAVYCVEERRLELRVWLAPAHPLVAPRLAAAGAGGAGGVQWLQLYMAQQHGSVLGALRLWTGAVCARVEAAPQCYICYCRLQPSTGRLPKVPCHQCKNKFHNLANGSRRATNPTARCAERRSDVPVPDPRPRRGVVSVYILLCTLDTLNRLNYENEFGINRFFT | Pathway: Protein modification; protein ubiquitination.
Function: E3 ubiquitin-protein ligase. Component of the ribosome quality control complex (RQC), a ribosome-associated complex that mediates ubiquitination and extraction of incompletely synthesized nascent chains for proteasomal degradation.
EC: 2.3.2.27
Catalytic ... |
B3PML0 | MKYLLGNLKMNFTYQECEKYLDTLEKALSEANLKNVILGVAPSAEAMSLILKFKDRHFLFGTQNIFYKDKGAYTGEVSIRSAKEFGLDFTLTGHSERRHTFGETNDLINKKIMAINQTTIQPILCIGENLEEFNQKRTKDVLTEQITSALKNVDSNLDNLIISYEPVYSIGNGQVPENNYIEQVVSLIKKITNNKYKVLYGGSVAPKNIEELNKIKNLDGYLVGSAALDAVAFVKMAQTMDKQ | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
EC: 5.3.1.1
Subcellular Location: Cytoplasm
Sequence Length: 243
Sequence Mass (Da): 27350
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A0A3G3AFE4 | FIFGIWAGMVGTSLSLLIRAELGNPGSXIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLISSSIVENGAGTGWTVYPPLSSNIAHSGSSVDLAIFSLHLAGISSILGAINFITTIINMRLNNMYFDQMPLFVWAVGITA | 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... |
A0A061H6X6 | MKLVSLLVLLPLLAGSVSGSTRLERSVRSTPPSSSSAAARPSSGGDAAALLTAARNKLEETEDALLHSLIARGKLAGVHGGSGVSDWHGCADVFKSLPAMPRDNTTLPHQWKGHANQPDFLLAHVPSSTATTADDDAGGASSSSTIDRFFYANIAGALSGSPTTAAGAAAKAGGAVAEAGAGATRAEMLASSLSLQLISDRIHIGEDVARAKLAQDRQTLCPLIAARDSQGLVKAVTNTTQEQAVLDRVLRKVSIWSARPAPAPAPAAGAGTANTAPATTSTTSAATSDPDAARIETFANNVQQLFKQFLIPLTTQLEVV... | Pathway: Metabolic intermediate biosynthesis; prephenate biosynthesis; prephenate from chorismate: step 1/1.
EC: 5.4.99.5
Catalytic Activity: chorismate = prephenate
Sequence Length: 328
Sequence Mass (Da): 33595
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A0A558NR03 | MSVQNAEQQLKFLLQQGLPLDSRPYRVLAQQTGLSEEQVLQRIQHWQQEGLIRRMGAIVDHHQLGYNANAMLVFDIPTEQVDLVGETIAASGRVSLCYRRPRRPGWHYNLFCMIHGRCRDQVLQQIAQLRQSLGLSVFPFQILFSRQQFKQCGGDYFEPDAKGAANGN | Pathway: Porphyrin-containing compound metabolism.
EC: 4.1.1.111
Catalytic Activity: 2 H(+) + siroheme = 12,18-didecarboxysiroheme + 2 CO2
Sequence Length: 168
Sequence Mass (Da): 19226
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A0A830GN09 | MRLRSGFLGVLFVVALVLSTVVFAGFALHRSAITTQERQALESDAWTVATDIDTRLREKRSTVALWASNDAVADHGSTAQQRAVTTLRRQTAFEGASVVAANGTMTAFDAADASPEDRATLVGQDFGDRTYVQTALRGQSHISTPFEAESGNYVVILSAPIRTNGTVVGTLNAAFHLTATDFFERATASLTSGRSLRVATRADTTLYDQSREFDAPLTATATVESTGWRVTVAADRTPLERRLRQSTGLQVGAVLATLLVVASLGVWASRRTIEQIERLSDGLGELEAGEYDTSLDLGPATEWRRISDRFDALAATLDRR... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 545
Sequence Mass (Da): 58858
Location Topology: Multi-pass membrane protein
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Q4TC88 | MSRSYNDELQFLDKIGSNCWRIKKGFVPNMQASGGELLRERRAGEADVRGAAERLSGRRGRLPPSHEADRERGGAARNRPRQWRLPEEVHRSPRRSLRLRLRHRQHGSVRHERPGSRGVSRGRRLRHQLRRPAAEDQPGRGRRPAGEGAAGPVAVRPHPRGRRLQGRHPHGGQGPGGGPGDGRGLVPEGGLRLGRGQGALRGVRAHAAGRPQQGVLQGQEEGPPSAGHSGSREPLRRDPGGGGDLQRLRRQEDGRRPPGPGVRDDPQRQPRPGPPGGHRRAGCHGEGHEEGPHLGQRPSAGVCAHHLAGGPGLPEGDGGG... | Cofactor: Binds 2 manganese ions per subunit.
EC: 6.5.1.8
Catalytic Activity: a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + a 5'-end dephospho-ribonucleoside-RNA + GTP + H2O = a ribonucleotidyl-ribonucleotide-RNA + diphosphate + GMP + H(+)
Sequence Length: 531
Sequence Mass (Da): 57370
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A0A6V7U4D8 | MTRKKSNKTASNNNNSDPFKRIQNTRQCPKCNKKVDYSIYLEHYEKCKNREGEVEEDDDDIIFCGEGQGHKENEQVSREVNNSKKNQKRTDKSSVVVNVEEEDSRSNSEAPRSSALNSGIVSENVFDGNARRAPASPITICDDSSNEVPITVFKPKNYCSDLPLAQIYDLCVERLQSFLNEQEELLRNLPPPKCDTNRPLDLTDENDSLMDPPPTENLSNKLLPVHYSLRFVWQILQKALHCVKNGHENILETATKFWGDSLRKVYSFLTTSVPAQQLFCRILVRRRGFHIARNIRYHDLGPKLMPLFIELCENGFFEEA... | Function: Nuclease required for the repair of DNA interstrand cross-links (ICL). Acts as a 5'-3' exonuclease that anchors at a cut end of DNA and cleaves DNA successively at every third nucleotide, allowing to excise an ICL from one strand through flanking incisions.
Catalytic Activity: Hydrolytically removes 5'-nucleo... |
A0A8I0KNS5 | MTLSLVALTRPDTDMFTLRLRELMSRRAIVRGAAVTEQVPLDGQPAGALAAIATADWVCVTSPSAARLICSATSPIPDGVRVGAVGEATARVLRDHGLRVDLVAGGSGRDLVAAFPPPTRPGRRVVLPASRRASSTVPDGLTQLGWSVDRVDLYDTRPLPRIPEVFAAADVVAATAGSAVRALAEAGLWHREGPRLVTIGRPSWRVARDLGIPSVAHAPTPTPEGFAAALAPFCPLV | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 3/4.
Function: Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III.
EC: 4.2.1.75
Catalytic Activity: hydroxymethylbilane = H2O... |
L0JVH6 | MAQVEAPAVDHPLDPLTAEEIEAAADIFEAETDLDGEIKYHNITLAEPPKPKVKEFEPGDTFDRKAAIVAREDGETYEATVSLAENTVLEYEHLPDVEPAVMPEEIEEAREIVKNDPEWREAAAKRGVENFDLVMVDPWSASGFEPEEHKGKRLCRALSWIKTSENDNGRARPIEGLFAFVDLDEMKVVEIEDNGVPDEDSPLPPEDADYRADRVETRDDYEHLDVVQPDGPSWEVDGNKVEWLDWELRVGWTAREGLVFHDVKFNDGDESRQVLHRASACEMAVPYGDPDPNHSWKNAFDIGEYHAGRMANQLTEGCDC... | PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue.
Cofactor: Contains 1 topaquinone per subunit.
EC: 1.4.3.-
Sequence Length: 659
Sequence Mass (Da): 74974
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A0A7J8K2R1 | MALIEVERKFVPGPETEDRLQELGGTLEHRVTFRDSYYDTPELSLMRADHWLRQRENSGWELKCPGTAGVSGPHTEYRELTDEPTIVAQLYEVLGTEVLGAGGVIAVLGPLGLQEVASFVTSRSAWKVVLSRVDKEEHSLKVDLDTADFGYAVGEIEALVNEEAEVPAALEKINKLSSMLGVLAQEKAPAKLIMYLQRFRPQDYQRLLEVHSSREKPQGTKDARQ | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Hydrolase highly specific for thiamine triphosphate (ThTP).
EC: 3.6.1.28
Catalytic Activity: H2O + thiamine triphosphate = H(+) + phosphate + thiamine diphosphate
Subcellular Location: Cytoplasm
Sequence Length: 225
Sequence Mass (Da): 25147
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A0A101T181 | MNWHERAACRSEDPELFFPVSDDGSSLLQIERARQVCHRCPVLRECRGWALRNGETDGVWGGLTPRQRRELSVPDPAGA | PTM: The Fe-S cluster can be nitrosylated by nitric oxide (NO).
Cofactor: Binds 1 [4Fe-4S] cluster per subunit. Following nitrosylation of the [4Fe-4S] cluster binds 1 [4Fe-8(NO)] cluster per subunit.
Function: Acts as a transcriptional regulator. Probably redox-responsive. The apo- but not holo-form probably binds DNA... |
A0A6V7XDP2 | MAPPPDTPVGSVWRRASLLAAVTGTEPLSRTAAVATAGATTDMFFQATLARSFISTLKLRGDDDVVDRLNYYYTPIMLAIACLVVSAKQFGGSPIECWVNPHSRESMEEYIEAFCWIQNTYWVPMYEHIPDSHETREGGNIKIHLKFKKFLGQQIGYYQWVPFILIAQALAFSLPCILWRLLNWQNGTNIHHLISAAEGARTVLDQNEREKVFHALALTFTEMIDLRETEYCPHPAASIFTRFRPTRLLKGQLISCLYLFIKCFYTANILLQFSLLNAALKSDEYLFYGFQVISDLIEGKAWTK | Function: Structural component of the gap junctions.
Subcellular Location: Cell membrane
Sequence Length: 304
Sequence Mass (Da): 34607
Location Topology: Multi-pass membrane protein
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A0A1F7G0T5 | MLLEAMRTPACGVMIARGDLAVECGYQRLAEVQEEILWVCEAAHAPVIWATQVLENLARDGIPSRAEISDAALGNRAECVMLNKGTHILAAVETLDDILRRMQNHQDKKSSMMRKLKMANTFSFSCLTAQCNPGDDPSTHPVQLQDSQAVLKKTPAFQKHPALNNSVIQES | 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: 171
Sequence Mass (Da): 18827
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A0A126Z673 | MTTVLVVVGPDIGRRGLRLPGGAAAGQGSGANESVAELRRGLEGLDGLVDVAVDFRQTDDEAELITWLHQAADDGWGVVLDPGGFTHYSYALRDAAALVVDTGLPLIEVHLANPASRDDFRAAGVISAVSTGIIAGLGVDSYRLAVRAAAERVQLRAAAAAPAAPSAG | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.
Function: Catalyzes a trans-dehydration via an enolate intermediate.
EC: 4.2.1.10
Catalytic Activity: 3-dehydroquinate = 3-dehydroshikimate + H2O
Sequence Length: 168
Sequenc... |
Q4S225 | MFTLSELVVLMAVLSATASGYFVSIDAHAEECFYERVNSGTKMGLMFEVAEGGFLDIDVEITGPDGKQIYKGDRESSGKYSVAAHMDGTYKFCFSNKMSTMTPKIVMFTIDIGEAPKGQDMETEAHQNKLEEMINELAVAMTAVKHEQEYMEVRERIHRAINDNTNSRVVLWSFFEALVLVAMTLGQIYYLKRFFEVTGSGKTLAFVIPIIELLLKREEKLKKMQVGALVITPTRELALQISQVMEQFLQRFPQFTQILLIGGSNPIEDVEKFKDQGANIVIATPGRLEDMFKRKADGLDLACWVKSLEVLVLDEADRLL... | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 493
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): 55550
|
A0A6V7WHR5 | MLNKWAEENFKADYEFLIGGSLMLEVNTKNSDIDAIYVVRKNTEYFWDEEREENNDGTKKLKSRATQFFGRLSSKCLDNKEKNCSDQSFYCYLCLQDKVSNLKRITEIRVPLLKFKFYGIDIDISYVQIPEEIKDNKNWMDEALNNAENNSLGRVFPLSGYKSNLIIKELLPKEEQKIKIFRSALILLKIWAENNSIYGNQFGFLSGTSMLIMLTKIYLLYPNTCSVLVIVDRFFLTFLTWLVWITLIFKAKLFIKSLI | Catalytic Activity: ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide
EC: 2.7.7.19
Subcellular Location: Nucleus
Sequence Length: 259
Sequence Mass (Da): 30372
|
A0A6V7WRW2 | MYMRRGPEKLAVVDLTTTKKIPNMLVECRMDCTDLLHKDANLFYLLKRYGGRTLVFCNSVSAVRRLQAILRKLTRRNIDTLPCILHGRMKEKERLKSVEKFAASENSILLATDVAARGLDFQSVQQIIHYQVPQTTENYIHRSGRTARALNSGLSILFVDPMDLQYYQKICRGMEKNEDLEVLTIDDRKLFESCKYLVELATEAESIEHRGRKQRTKSSWFQRMAKEADLIWDSGEESISTQKNVLDDDNWHQKKMDRKLKQIETTLQKMLYSLTPSNLCKENNNHEAEDKHNEDAKERVRKRMKLERGKNKWLKKRPKL... | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 321
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): 37679
|
A0A968NAS4 | MDIFLIVFLVVQVLIITLAVTTGFAYLTWYERRLLARFQNRVGPNRAGPLGLLQPVADAVKLFFKEDVIPTASDKVVYLLAPVLAVMTAIVIWAVIPFGCFNLNGDHTACFDPARRDEVWNALQVAEVNIGILFILAVTSIGVYGITLAGWASNSKYAMLGGIRASAQLISYELAFGMAVLSVVMFGGTLSTWEIVLAQEGLWFFFPLILGFLLFMISATAELVRTPFDLVEAEQELTSGYNTEYGSMKFALFFMSEYIKMIAMSAIATTLFLGGWRFPGLETLGDGVAALAGPWPAAIIVGLVSLGSFLLKVAMFLFML... | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ... |
A0A0M8SD95 | AIGRAGNPDTLDGVDVVVGTGTSIVSGEGLIATAGAVDTHVHLLSPRIMEASLAAGVTTIIGQEFGPVWGVGVNSPWALKHAFNAFDAWPVNIGFLARGSSSDAAPLVEALAEGGASGFKVHEDMGAHTRALDTALRVAEEYDVQVALHSDGLNECLSVEDTLRVLDGRTIHAFHIEGCGGGHVPNVLKMAGVPNVIGSSTNPTLPFGRDAVAEHYGMIVSVHDLKPDLPGDAAMARDRIRAGTMGAEDVLHDLGAIGITSSDAQGMGRAGETIRRTFAMAAKMKGELGPMAGDGEGDDNARVLRYIAKLTINPAIAHGL... | Pathway: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from urea (urease route): step 1/1.
EC: 3.5.1.5
Subcellular Location: Cytoplasm
Sequence Length: 354
Sequence Mass (Da): 36673
|
A0A6V7XPM1 | MNFYRQRFFHVLAFRLCCCFFSNTWFVPDEYFQSVEVAYHIVYGKGHLSWEWLPEWALRSPLHPLIYAFPFWLLKLFCLDFGFIIRWIPNIIHAFLFAIADICFINWAKSVIGFSFDALYIILPLYFTNWFIVYCSTRTLSNTLECCLMLIALNFYTKNDANYVETKKNDDSEEENLAKFSILKIDSFCICLIFVSIAAVIRPTTWLLWIPLCYGHFVFYLLEGLDVINQEIVTERMEKYILSYSPFVIIIPLFTFILDSFYYGRPTSTFFNFFHFNIIKSGNALFGSHPWHWYFTQGLPSILLFASIPLFTILVKLIRS... | EC: 2.4.1.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 350
Sequence Mass (Da): 41757
Location Topology: Multi-pass membrane protein
|
A0A1V5VW57 | MKLSILAAIDRNYGIGKDNALLWHLPADLRFFKTKTTGHTIIMGRNTFESIGGGKPLPNRTTIILTKNPHYNAPENCKIAHSLQHAIDMCANKDELFICGGAQIYALALPLVHTMYITHVHATLQADTFFPKWNPNEWKKVSETHCDADEKHAYSYTFAEYIKY | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1.
Function: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.
EC: 1.5.1.3
Catalytic Activity: (6S)-5,6,7,8-tet... |
A0A2L2TPU9 | MEKTTAQYLKEDIFVEKIHSEKIRGAYRAWDGQAMDVDISWGYYRGVPFYCIIKEQNQGKRDSLIVVRSFLYKFNIRDTKPTTIFSSRFLLSMTDWLSQEVRVDQVDHLIGMDPDTVFQNNFISELLKESKYPNTVGVCGYVAVDFSGGNWNLWSIYQNAEYTIAQGLRRLHQSIATKKVSCLPGCCQLLKICDMTCGDKVLIEQFGYYPRHLDGMIKRIRTTASEDRNHICQLLTTFPEAQSRQALRARAYTDVPHSWSVFLSQRRRWTLGATSNDLLLFTARHCQWWERILAFSNVLTWSLNVFVIASIGCMIVAFMH... | Function: Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non-reducing end of the growing chitin polymer.
Catalytic Activity: [(1->4)-N-acetyl-beta-D-glucosaminyl](n) + UDP-N-acetyl-alpha-D-glucosamine = [(1->4)-N-acetyl-beta-D-glucosaminyl](n+... |
A0A5B7TKX3 | MNIKKFIKKNLLIELLISMCVILFVYAAISKFLGFENFLAQIGQSPVLSSFTYWVAWIVPISEVIVAILLITPNYRLFGLLSFYSIMVMFTTYIVIILNFSDFVPCSCGGILESLGWKQHLIMNISFCLLALYLLFQMTNTTSKNFDDQQKLIKHIKES | 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: 159
Sequence Mass (Da): 18255
Location Topology: Multi-pass membrane protein
|
A0A6V7UK02 | MLFGKPIHILMHQRRAKRAVSDNMSVRINMQKDETELVKNGRKPSKTANGDHSGENEPSHGSFGDIMVHQAIHTIEYVLGCVSHTASYLRLWALSLAHAQLSEVLWDMVLENAFAFNDIKGYIALYAIFFAFGVLTFSILVLMEGLSAFLHALRLHWVEFQSKFYLGQGYIFAPFFFKDILQRASASC | Function: Essential component of the vacuolar proton pump (V-ATPase), a multimeric enzyme that catalyzes the translocation of protons across the membranes. Required for assembly and activity of the V-ATPase.
Subcellular Location: Membrane
Sequence Length: 188
Sequence Mass (Da): 21315
Location Topology: Multi-pass memb... |
A0A6V7VS02 | MGWAEDSRKIDKLVEGANEQLRMLYIPLLKNDKQILVENDEMIEQDNSIQTVFHRLQMLPYFVQRGLCNSYYPSRRFRRYNTNLDIEELIYHISHRYDVPERLDLVLQKIVGHSSKHQSIKNAFTAGISRSFKYIWPKLVKGILKK | Pathway: Lipid metabolism.
EC: 2.7.7.41
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 146
Sequence Mass (Da): 17383
Location Topology: Peripheral membrane protein
|
A0A1W9VQE0 | MGKNYFITGIKHCGKSTIGKKISKPLNLDFLDLDNLIESNVKMGVREFYKNQGRENFMLQESNSLKSITQNHSQGFVCATGGGICDNPLAFNQLKKIGYVILLIEEFDLTYNRILAGGIPAFLTSENPKKEFYELYIKRLEIYRTNADIIIECKARDPEIIKNEIIQKLEELHNVRK | 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... |
A0A7J8BKG7 | MIFPVYRCALRRLRRLRGRSFSTSAMEVAFRGVRKVLCVAEKNDAAKGIADLLSQGRMRRREGLSKFNKIYEFDYHLYGQNVTMIMTSVSGHLLAHDFKMQFRKWQSCNPLVLFEAEIEKYCPENFVDIKRTLERETRQCQALVIWTDCDREGENIGFEIIHVCKAVKPSLQVLRARFSEITPRAIRMACEHLAEPDQRVSDAVDVRQELDLRIGEEPLELFDCLRAVGHELRNQQRVCVSIRAAPCSFLPRFPGAAFTRFQTLRLQKIFPQVLAEQLISYGSCQFPTLGFVVERFKAIQAFVPEVFHRIKVTHDHRDGT... | Function: Introduces a single-strand break via transesterification at a target site in duplex DNA. Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. The scissile phosphodiester is attacked by... |
A0A1V5W9M2 | MNIIQEGNGLTQVLKIQVSAADYADKVEATLKDYRKKAKFDGFRPGTVPMGIVKKMYGKYVLVEEVNKLLSDALSNHIAENKLPVLGEPLPNMEQQQSINWDTDTEFEFCFDIAIAPEVSVELSKKNKFDYYKIVADDAIIQEQIDHLTARFGSQQSVDTIEGTELVRGNFTQVGVENPYKREGGTLLLSKVATESELQVFKNAKIGDTVEFNPKKAFENDTELSSMLAADKDQTDVLYADYQFEITEILRFAKSDVDQSLFDKAFGEGVVSSEAEFKDKIRADFEERVGPNSDYKLLLDIKKKLVESAKFDLPEEFLKR... | Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
EC: 5.2.1.8
Subcellular Location: Cytoplasm
Sequence Length: 448
Sequence Mass (Da): 51412
|
L2GRS5 | MSGPISAETQDVSDYKSCTSQLCMTTVHKFAFIPLYLFSSLVSTLLNKHITTTLEFHPTFLLLLMQSVIIVALLMLLKTINVCTFVLELRHMFYWIPSAVSMVLMIFSGLRALSHLSISMFTLFKNYSVIVIAVLELLLLGRTISRLSVLCFAMMIVSGMLVDYSETRVDRVGYAWICTNVVASAVYVIVLRMTIVHHIRARQREAEKNTRRGDKKDAVAHSPHDHGRKCYVDDEGIAATDRAGKELLRRMLRVVTSDETGDAMHPDTREMPSGAVCTTRNGGTCTAPVIVFCNEAARKVRNNRIGDYVRMFEGLDGSQS... | Function: Involved in the import of GDP-mannose from the cytoplasm into the Golgi lumen.
Subcellular Location: Golgi apparatus membrane
Sequence Length: 527
Sequence Mass (Da): 58577
Location Topology: Multi-pass membrane protein
|
A0A7S2WHR5 | KNGSKQEMRTWAWSTVPEVRDAYEDYLRAPIIRAWKTDKNLDSKADVWTVTMQMPLSTGEKVHQVQALAFFEYHLDGRAHLSMDGLAYLEHSSPLPGVGLLIEGEARLNQRQALSI | Function: Transmembrane component of the tectonic-like complex, a complex localized at the transition zone of primary cilia and acting as a barrier that prevents diffusion of transmembrane proteins between the cilia and plasma membranes. Required for ciliogenesis and sonic hedgehog/SHH signaling.
Subcellular Location: ... |
A0A2H1VQI4 | MDTLKWLSDLFWDERWWLPRGAKWADVTNGPDKTVLHPDVSDFYYVIPLTIGLLVLRYVLNIYCFIPLGLALGIRNKKKKNLQHIPVLETAYRKNALIKDTTALAKQLDMSERQVERWWRLRRNQDKTSSLTKFCEHAWKTFYLFFSTPTVYYIVWDKDWFWDLDKCYTNYGKHELTMDIYWFYLTTMAYMIALSITFFHDVKRKDFWGMLAHHVVTILLLCISWIISAFRIGIVVIVLLDLTETWLEFVKALKRANFEKLATSLFVAFVPAWFYTRMYLFPLYLYSTSIRSMVFWGHVFALYIVNAMLFVLFFLCVYWS... | Pathway: Lipid metabolism; sphingolipid metabolism.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 369
Sequence Mass (Da): 43747
Location Topology: Multi-pass membrane protein
|
A0A177E4K0 | MPVLLPPLYLAFLATQLYALRIHCPHPPSGLVYPTSIQVLKFFSVVAGSLSWTLIVSLPTSTAIGTTVVIAFFPSSSLLLTWTALTTLSRTFSVIFGRVTPKYIVSTAPFAHVRHPTYISYASELLGAVFFILASYLPTYFSKRIDIEGTGLSMPVRCVGLVTMVAGFMWLYRR | Catalytic Activity: [protein]-C-terminal S-[(2E,6E)-farnesyl]-L-cysteine + S-adenosyl-L-methionine = [protein]-C-terminal S-[(2E,6E)-farnesyl]-L-cysteine methyl ester + S-adenosyl-L-homocysteine
EC: 2.1.1.100
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 174
Sequence Mass (Da): 19185
Location To... |
A0A6N4RBV0 | MEALFTLVMLAIGLSVDTFAAAVSKGASLKKALKKKQKREIAIIFTACAVAAPALGYSIGFLLSELVEAFDHWIAFFLLSGVGLHMAYNGFQPQPTSSSPALNQTKVFLMAIATNIDAVAVGIGIAFTELNIVWVCIATALGTLAAVYLGITLGKRGGKLLGPKAEIIGGLILVLIGFKTLLSHLFG | Function: Probably functions as a manganese efflux pump.
Subcellular Location: Cell membrane
Sequence Length: 187
Sequence Mass (Da): 19580
Location Topology: Multi-pass membrane protein
|
A0A7S0T4E5 | DDRAQRRGLGKFLMFLCESLAKRAGMSGVMLTVQKANQGAMRFYSGAKYAVSLLDPGKVDPWGAAEYDYHILDKLWDPACKLEVEKTAQAAWRENKRRVEAE | Catalytic Activity: acetyl-CoA + N-terminal L-seryl-[histone H2A] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-seryl-[histone H2A]
EC: 2.3.1.257
Subcellular Location: Cytoplasm
Sequence Length: 102
Sequence Mass (Da): 11525
|
A0A7S0SGZ5 | MRASTTLARWSAPRTAPVEPRSSNRLRACPTTSSTRRCRVFCVGDDAKEATRALPDATCVPESRHWSVADSAALYNLQGWGAPYVAASKSLGHVVVRPLGKAGEDGEDDSAPEADLFAIAMEVRARLDSGGPLVLRFPDVACRQAATLRAVFAKAAHTWGYGARFQGVFPVKCCHDKDLLLALVIDGAADGFGLEAGSKPELLLALAVMRRARALQREEPADARPQRDTQVRAHRQDADASLSPPGPPRPSELCGPREPPPPLVVCNGYKDGAYIRLAIGAWSLGVRTVVVLEKPSELPAVIAAVRALPPGALRPYLGVR... | Pathway: Amine and polyamine biosynthesis; agmatine biosynthesis; agmatine from L-arginine: step 1/1.
Function: Catalyzes the biosynthesis of agmatine from arginine.
EC: 4.1.1.19
Catalytic Activity: H(+) + L-arginine = agmatine + CO2
Sequence Length: 863
Sequence Mass (Da): 91459
|
A0A4Z2D0V4 | MEVVEILFVIYVITLVFLCPYTKVEESFGMQALHDLLYLRTNISMYDHIYFPGVVPRSFLGCLLVGSIVSPIIYLSTLLRMDKFISQYIVRICLGLLTTLSLIKFSHCVKKVFGKHVYLRFFMICCSQFHLAFYASRALPNIYALMLVLYSLGHLVKGNQTKFVMSAGIAILVLRSELMLLFGPCLLYGLFAGYIKPRLKLLKTIITTAIISIGSSVLVDSMLWGKLIWPEFEVFYFNTILNKSGQWGSLLCTCMLLFAWIAVVVFSLPLQKVFGYQHGLMYLESTKLLLVAFIFIGLYSFLPHKELRFIIYVLPIFNLA... | EC: 2.4.1.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 406
Sequence Mass (Da): 46364
Location Topology: Multi-pass membrane protein
|
A0A1Y2L9A0 | MKKTVIPASLFAFSILLTSSYAVTAEQSHSKWGYDGAGAPSHWSTLDPANQICGTGKNQSPINLTNRIEADLSPIEFHYDVTAKDIVNNGHTVQINLNSGAYINLDNHRFDLIQMHFHAPSENHIDGKSFALEAHLVHADKDKNLAVVAIMYDIGTENTALASFWTNMPHMAGDSKATPNNTNIASVLSEDRDYYRFNGSLTTPPCSEGVTWLVQKQPQTISDAQLKAFTGTQHGPNNRPVQSVFARPILQ | Function: Reversible hydration of carbon dioxide.
EC: 4.2.1.1
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Length: 251
Sequence Mass (Da): 27561
|
A0A1Y5TY99 | MKQLASLYSTLLDACGLLAGFVFVLLALFVSIDVVIRNVGLGNFGWLIEISEYALYGATFIAAPWVLRLGAHVRVDLVVGNVPRRAALALEIVTDLIGLAISLILFWYSLAATIASAESNSLIFKDLVVTEWWLLAVLPASMALLAIEFVVRLVRAVRGRTEAGNDTVLDGL | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 172
Sequence Mass (Da): 18602
Location Topology: Multi-pass membrane protein
|
A0A1Y4BBR7 | MKHSKGVVRKKKGTGLKIFLLLFFIIGISALVVAYKFIHPIYVDTKEKVFQITSEMDEGTFRRDGNTYVYDKDGAKIGKIGNENYSYVKSSDISTYIKNGYIAQEDKNFAVHHGVDYKALVRAGVSYIKNRGVITQGGSTITQQVIKNNLLSSERTFTRKFTEALAAFELEKIYTKSQIMEFYCNSNYYGNGCYGVEGAARYYFGKSAKEVTLAEAAMIVGTSNRPNDYNPADSYKNATRKKEEVLKNMLSEGYITQEEYNLAIKENPEVVAQPDDTDNDNYMVSYAVHCATLRLMERQGFQFKYGFSSGKEYKKYNKKY... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-term... |
A0A6J1ZN75 | MLGRGVWSSLRQGLSRGLSRKVGGWASGEGRKMDIAGIYPPVTTPFTAIAEVDYGKLEENLHKLGSFPFRGFVVQGSNGEFPFLTSIERLEVVSRVRQAMPKDKLLLAGSGCESTQATVEMTVSMAQVGADAAIVVTPCFYRGRMSSAALIHHYTKVADLSPIPVVLYSVPANTGLDLPVDAVVTLSQHPNIVGIKDSGGDELWGACVPWPMSWGLRCASWSDSASQGNGKMPRSCSTASLSQTLRQTVYPNSILGKSRRRAKVECLSRARQCCSEPHWSLRQEGKCDPALWDPRAEENHGLVWLLRRPLPRPVTGAKPH... | Function: Catalyzes the final step in the metabolic pathway of hydroxyproline.
EC: 4.1.3.16
Catalytic Activity: (4R)-4-hydroxy-2-oxoglutarate = glyoxylate + pyruvate
Sequence Length: 321
Sequence Mass (Da): 34867
|
A0A6V7X584 | MYFKTTHKYFFKILYTIKLKYKFCSLINISKEQLQTYTQITELQTNQISGFWIFIWVLSKIPELFDTLFLILKGRPIRFMHWFHHSMSILFGTINFIGDNAYLVWVVWMNFFIHSIMYSYYMLTCFSFRFPKLYLNY | Pathway: Lipid metabolism; fatty acid biosynthesis.
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: 137
Sequence Mass (Da): 16908
Location Topology: Multi-pass membrane protein
|
A0A7S2RGF2 | QKMVALGLLLLLVGLVTGQHGTDQVYIAEFHLEHSGGTTGKILIKVDPQNAPIGAARFKQLVEKNFYKDACFFRVISGFMAQVGIPAIPHYMPEFKKHIRDEEKVVLSNTRGTVTFAMAGPNTRTTQIFFNFGDNSRLDRLNFPPFGEIISGIEELDRIKVTGEGAPNGPGPSQGLLVSKGNEYLLKNWPQVSCIRQTKIQGSPGGSNTIINAEKIATDTKKNPDVKMVAPAGLRDPVDPKASLYIHNTDSNNFMLVLGVVVVFGVVFFFFRSNKKATQTRDLDA | 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: 285
Sequence Mass (Da): 31263
|
A0A7S0SHW9 | ENFRALCAGDRGTGSETGLPLDYTASTFHRIIPGFMAQGGDFQRNDGTGGESIYGGKFEDESLSHMRHTERGLLSMANSGPATNGSQFFILFDRAKHLDGKHVVFGRLSAGHRVLDEMEGLGSKGGAPRKEVRIARRG | 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: 138
Sequence Mass (Da): 14912
|
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