ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
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A0A1L0B6U7 | MVVCVNCGEYIAHGKLFIKYSNNSYKLLDCPKCGKIIDKYIEYDHLNIFINIILLKKGVYTHLVYNSDNEILNKRLKYIVLSFEVYITWVYQEHLIHLIRSSSKINIGMINQIADQFSIIDFVFKQNAFWQYCFFIQHCFLEQLIFLKLVNFTFSKYLYHGNKNSLKIFENTLLLSYISRLIFPILMLIWPYDSSIIIPSYIMKWLTNYYIIESVNLIINKKNNYNMFFNKMLLSFAFAFLVKVLLQNILMNSAFVIMKSTIFPLCGWDFHVYNVDIFNKHRILKDFINQLVLC | Function: Mediator of sterol homeostasis involved in sterol uptake, trafficking and distribution into membranes.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 294
Sequence Mass (Da): 35091
Location Topology: Multi-pass membrane protein
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A0A914H0F9 | MHFCAFASVKKYSHQCHTYEWRHFLTRSEAIISVIKFARQRMHYLEDAIELLEYLPDELRKKCKELQQLDVQYSVAFDKLQRDSRYLFDNIGQMEPFGLEQKNRELLGKFQSVHDIGSGKVQVAEYLQLTLEKYQERVAKDLAEFKTELEAENPGETELIEKNFVQTMSATSSSVGLSADVLENLSCASDSLGQQIIHPLRPFAPAAMAEHLNGDEMFEGSASTETEPISKGQRAQQFDDFRIPSNQLNRRPSLLDAPTSSSATLMAYEDIFDAEVAIPAKKLKPTPIPRFLAHVGAVQQQETVEMDHQREGSASSISTT... | Function: Component of an histone acetyltransferase complex.
Subcellular Location: Nucleus
Sequence Length: 538
Domain: The PHD-type zinc finger mediates the binding to H3K4me3.
Sequence Mass (Da): 60738
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A0A1I8NS67 | MTQEISCTFIGVSLVMRRLLGDLELKPFIWTLNALGLISCQYNDNHNGKKQFSRTQYHKIRSVAIVAFIQILCVSMFIYWLLYRDEFDIKAYNRTGHIYMNINFVFGCCVVSIIYLHFFLWQLFYMQLLATIMKHQRNFSVSRCHGWNLRHCFFLYSFLSITAVWNNYKAFEYTQLKLGAWTCYQVMYDVVFITCGIVVILFVAMTKILNCCLHHLNSEIYKLLTEAQSIQNSRHLGWLLAQRKNLLDLCQQKISDRFGLLIVLVVAFIVFSASSGPFYLISVTLKQKIDNSTAYVVNFLVTLYWNVPWMTIFVALLTCN... | Function: Gustatory receptor which mediates acceptance or avoidance behavior, depending on its substrates.
Subcellular Location: Cell membrane
Sequence Length: 404
Sequence Mass (Da): 47185
Location Topology: Multi-pass membrane protein
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G0EDS6 | MCIKPRTRRDAGDLAALAALTNIGGVAVEVNDDDWGFVRRVFEDAGLTVLRRVTIEVRKAGDVPRVASEARKKGYDIVAVLPLSDEAARYAARDERVDLVVVRPGMARLVDSSQAGLHRMGGGAVELQVTPLLSQKQGFRTLMVVSRRAVAYSVPLVVSSCATTMWEFIPPRSIEALLSALGVPENYAKAFTYSHPWSIARRRMRRD | 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: 207
Sequence Mass (Da): 22778
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A0A1Q5PSJ7 | MPESRKRKKNGKSVSQIAEKKTEIKPDWTEGIKPSPSWWAPVFCTLAIIGLIWLAIYYMWSAQYPIPGIGHWNMGIGLGFIFAGFLMVMRWR | Function: Involved in cell division.
Subcellular Location: Cell membrane
Sequence Length: 92
Sequence Mass (Da): 10616
Location Topology: Multi-pass membrane protein
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A0A087TPK9 | MIFLKHFSALKLNLQESSFYRAASFKALKYDLQEEDVVNNAKTRSAEAAHALKVLSEYASAGGGSRGIHRHTIVNKKLLVRDRLKLLFDPDSPFLEIGLLAGMSMDYGHIPAAGSVAGIGKIHGHFCIVGANDATVKGGAFFPISIVKQIRVQQLSYLNRLPCIYLVDSAGAYLPLQADIFPDKEHGGRTFYNEAVLSSLGIPQIAVVCGSSTAGGAYCPTMAEEAIIVKKSGVVFLGGPPLVKAATGEIVSEQVLGGA | Pathway: Amino-acid degradation; L-leucine degradation; (S)-3-hydroxy-3-methylglutaryl-CoA from 3-isovaleryl-CoA: step 2/3.
EC: 6.4.1.4
Catalytic Activity: 3-methyl-(2E)-butenoyl-CoA + ATP + hydrogencarbonate = 3-methyl-(2E)-glutaconyl-CoA + ADP + H(+) + phosphate
Sequence Length: 259
Sequence Mass (Da): 27533
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A0A087UE77 | MGANVIEVLSVFFKDYRNNTPQRMKIIDAYLLYILLTGINQFVYCCLVGTFPFNSFLSGFISCVASFVLGG | 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... |
A0A3A0B3C1 | MQEVIINYILICILCYITGSIPTAYILVKRRYNKDIRLEGTGNVGAMNSFEVTGSGKAGIFIFLIDFLKGLIPVLILTGVIKLSFALLILPSVLLIAGHNYSIFLKFKGGRGLSTAMGVMFTVNILMILFWLIFYFIAHKIKSNVHLASIAASILYVLPLVFFPGFVNRFTLNNSVTNDQNFLLFTFCASISILILLKHIDPLQDLLNNKNEK | Pathway: Lipid metabolism; phospholipid metabolism.
Function: Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
Catalytic Activity: an acyl pho... |
M3AM92 | MSSRDLRPTKKRKSEDINGPNIASDFSADQPSKRSKTNNTAPKPQRRPKATQTKSIAIKTPQKSQEKNMSSIDQPITHDPSHPSPLTLTLTLTESTGDIFSAPPNTLLIHACNTEGSWGAGIAAAFKSHYPSAYTIYHDHCHMHGGELWQKALLIPPQPDDENEHFIGCLFTSRSKGRRKDSPSRILGATEPAMRDLLRLVRENGEVGEVRMCRVNSGLFGVKWEKTKGVLEGIEVEGEGVREVKVVSREE | Function: Highly specific phosphatase involved in the metabolism of ADP-ribose 1''-phosphate (Appr1p) which is produced as a consequence of tRNA splicing.
EC: 3.1.3.84
Catalytic Activity: ADP-alpha-D-ribose 1''-phosphate + H2O = ADP-D-ribose + phosphate
Sequence Length: 251
Sequence Mass (Da): 27789
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A0A7S1X8W5 | MASIYVTEPPTKGKVVLRTSVGDVEIELWPKEAPKAVRNFVQLCMEGFYHGTVFHRVVKDFMVQGGDSTGTGQGSDSIYGGQPFQDEFHSRLRFTHRGLVACANQNEPNTNSCQFFITLDACDFLNKKNTIFGRVVGD | 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): 15352
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A0A7S1SRY6 | STSLSRKLTKLLRHSAKQRGLHIRPDGFVQLSEVLSLPEFRGLGIEQVRQIVAADNKQRYSLNEDHSDGVLIRANQGHSIQSLDEEAMFSKIVGQDQLPACVVHGTYMSSWPSIKEQGLLRMKRTHVHMAKGLPRENGVISGMRGSCEVVIHIDIRAAMAAGIEFYESANGVILSSEVPPRFFISAVHRKTGTDLLASAAGSAATGQVG | Function: Catalyzes the last step of tRNA splicing, the transfer of the splice junction 2'-phosphate from ligated tRNA to NAD to produce ADP-ribose 1''-2'' cyclic phosphate.
EC: 2.7.1.160
Catalytic Activity: 2'-phospho-[ligated tRNA] + NAD(+) = ADP-alpha-D-ribose 1'',2''-cyclic phosphate + mature tRNA + nicotinamide
Se... |
A0A1I8P1U5 | MSRVALLWFGFLTYFNFYTCCTILRIDLTKRRLKNPNRFIKAVVYFGNILPLVSMPYSLALNFEHTQLYVANPLALSAHNVNAVMRFLVVTVVIVTIRNRDARLTKWLEKAMEIQVQYFDRFSQVPKDISHRKWLYLNSIISVIHNIITAISAYNESKKNIHALDGADLDGLLCMVTCQHMYMLHHAALLCYMRECLSTLHNQLRIGQFDADLSFIYYNIRKLLHELNGIYNPVLLVIHLCLIISNSLVGYVVLLTMMIPELSSGLFLYLFGGKVYLLFLVHMYIYYELCDSVEKMVKETDDILKEISTPNTNSDYDKAL... | Function: Gustatory receptor which mediates acceptance or avoidance behavior, depending on its substrates.
Subcellular Location: Cell membrane
Sequence Length: 373
Sequence Mass (Da): 43161
Location Topology: Multi-pass membrane protein
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A0A836CS78 | MSARVRSRSRGRGDGQESSDTAETVAARKLGGKKSQRKEPPAKNVEVEPGQEKEGGASVVQEPELEGSRQELDVEKVEGELGDGPDVKGKIPPNVVPAKIPEGEKHIHEHAETKQHNLAVDLYYGGIYCFMCKDYVYDRDIEQIAKEEQGEALKLQASTSTEVSHQQYSMPGLGEKYPTWETTKPELELLGHNPRRRRIASSFTIGLRGLINLGNTCFMNCIVQALTHTPILRDFFLSDRHRCEMPSPELCLVCEMSSLFRELYSGNPSPHVPYKLLHLVWIHARHLAGYRQQDAHEFLIAALDVLHRHCKGDDAGKAAS... | Function: Deubiquitinating enzyme that removes conjugated ubiquitin from specific proteins to regulate different cellular processes.
EC: 3.4.19.12
Catalytic Activity: Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attac... |
G8XTH0 | MWTFTVSFLLTLVSASSANFDNLTCVELTRRCFAGESFTPYNDKWLHPLIDVSQNDGNISQLLRFDPSTKHASPTIPLDDTFMDYLTLLHNNPNQLRVLLALLRSDVAPTWMTLMKGYSECGDTGPVYTCINDVCRAYDLRRLTYGQSIFTENVMGFEFGDQGQFSTVLVLRNPHSKTHRPIRIPVATRAKRDGLQLFYALYNFLREFFVRHNLETSLVERLDKYYQGIPNEFKQPVVNNPALLHNGVKTVDVRQHTR | Function: The heterodimer glycoprotein H-glycoprotein L is required for the fusion of viral and plasma membranes leading to virus entry into the host cell. Acts as a functional inhibitor of gH and maintains gH in an inhibited form. Upon binding to host integrins, gL dissociates from gH leading to activation of the vira... |
A0A087TQ59 | MRMLIKGVDDILHFGVLLSIIIRWVVSRFPYSGAGKPLMYGDYEAQRHWMEITVNLPVNEWYKNSTKNDLLYWGLDYPPLTAYHSMICGYLAKWLNPDWVTLYTSRG | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 107
Sequence Mass (Da): 12576
Location Topology: Multi-pass membrane protein
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Q8SUE1 | MKILVAGTPGVGKTTFSSRISEMFGIPHIEMSRYIEENNLYEEYSETYKSLLFDDRVVRKSLEMYVIGKDSYIVDTHSCGMVKGMSFDLIFLLTAPVEVLYKRLKKRGYDEDKIKENIECEIFGVVEEEVEEFFGAGYYPVGEEEGKLTPEEAIDVIGKKMNGTSATAAP | Function: Broad-specificity nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates. Has also ATPase activity. May be involved in rRNA maturation and transcription regulation.
Catalytic Activity: AMP + ATP = 2 ADP
E... |
A0A0C1QK33 | MKNIRDNLDLSGKKVFLRADLNVPIVGNKVIDDTRIIRLIPTINFLRSKGAIIILASHFARPEGKFIPEMSLKNIVPALEKHISCKIKSIDDCIGNKVENEINRSAAEDILLLENLRFYNEEENNDIKFAEKLASLADLYVNDAFSCSHRAHASITGITRFLPSYAGLLMEEEISNLNLVLNSKAAPSVAIVGGKKVSTKFKILSFLADKVDYLIIAGAMANTFIKAQGGEVGKSYFEEDFINEARDFFNKTYKAKIFIPDDYVVKDAVSSEIEVLDTDQLKPSSQIFDIGTTSVIDICNILSSSKVVLWNGPLGLFEDE... | Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5.
Catalytic Activity: (2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP
EC: 2.7.2.3
Subcellular Location: Cytoplasm
Sequence Length: 394
Sequence Mass (Da): 43220
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A0A1L0CMN7 | MSILAEVCKKASLGYCYTLSDYEDFTNFTYLSKCYSRSFILLNSFISQPGSLFINLLTFVAIIMLLFSIKNKYTAVGRSEICFLFYNLLISIALSIVVDNGFIGQSSSNYPLFVSVQMASISICYATLALTGLVNLKLWEDNTWLSKLIFKISAAIIGICSFVYHYETLTKSKPSLIQSKATAILLTDYGINAAFIIIYVVCQCLTSVFIVKNYWMIGAQLLGLLFFMSGQIISHIFSINICQQSNHYLDGMFVLSLSNLLSIMMVYKSWAISTTEDLEFSVNMLSNDEILDLESEKI | Function: Chaperone required for the export of the chitin synthase CHS3 from the endoplasmic reticulum.
Subcellular Location: Membrane
Sequence Length: 298
Sequence Mass (Da): 33488
Location Topology: Multi-pass membrane protein
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N1Q7N1 | MSAPHGYSLRPFIKRPNSHPFKIGDAKRIKPRNTSSSLSPEANEGLSNAPSDPTSANASPASTEDGTLQRLRELISSMPVPATKNSTLRTRKLASKTRSRNVLAPLELHHSADNHDASPHDVDLRYPSGLAERFAFARRTYKKDHRYARQLDPFVDLVHTISVLLESTLGPKGPQVQICSALRQAWLGHENWSAGGGTQTFKDTIEAVNVLTGHQGHKRPELTPDFLEHFFDQLHDRVIADNCTDLLHRSNAKSTENVYGELRPKFLSRIFKDVGLDSKSVYLDLGCGVGQTAMQASLETQCEAHGIERERKVHALAQFH... | Function: Histone methyltransferase that specifically trimethylates histone H3 to form H3K79me3. This methylation is required for telomere silencing and for the pachytene checkpoint during the meiotic cell cycle by allowing the recruitment of RAD9 to double strand breaks. Nucleosomes are preferred as substrate compared... |
A0A933YK88 | MTHLKQVGSSTELYTRPLTRALQANTAVRLLEDSRPRIATLLREGELKLGLISPLDYAKESSDYRIIPNVGVAAERSCGSLLVRFREGVKNIRSLAVDPTYASEVVLAKIILSELFDLEPMILPMNAPVEVMLQKAEAALLVGNAAFRARDDSEDVIDIVEEWDEMTGLPCVFGLWCGREPDLKPEYIEMIQHAMQKGVAGIADIAQEFLPDERAAVIDYLESFAYTLDERATAGLGEYMKYLYYHGLLPDVAELNFYKGTAEEADDLLPKDVSPN | Pathway: Quinol/quinone metabolism; menaquinone biosynthesis.
Function: Catalyzes the dehydration of chorismate into 3-[(1-carboxyvinyl)oxy]benzoate, a step in the biosynthesis of menaquinone (MK, vitamin K2).
EC: 4.2.1.151
Catalytic Activity: chorismate = 3-[(1-carboxyvinyl)-oxy]benzoate + H2O
Sequence Length: 276
Seq... |
A0A7L3IZ77 | KALERGLVKALKKLDDYLRTPLPEEIDADSTEEEKVSKRKFLDGDDLTLADCNLLPKLHVVKIVAKKYRNFEFPTEMTGLWRYLKNAYARDEFTNTCAADKEIEQAYADVAKRLSK | Subcellular Location: Membrane
Sequence Length: 116
Domain: Members of this family may change from a globular, soluble state to a state where the N-terminal domain is inserted into the membrane and functions as chloride channel. A conformation change of the N-terminal domain is thought to expose hydrophobic surfaces th... |
A0A1X2H372 | MSFGRWKRYIEEGDLVFVHVTRDSMVPIVIKINDQLHNRFGYFHHNDMIGKEYGSKMVSHNYKGFVYLLHPTPELWTLMLPHRTQILYSADISFISTYLDMKPGSRVIESGTGSGSFSHCIARTIAPTGKLYTFEYHAERAALAAKEFADHGLSDIITTQQRDVCKDGFGLTDVANAVFLDLPAPWEAIGAAKAAFLQHRTGKICTFSPCIEQVARSVHALNEHGFVDITMFECLIRNHNVSPVQKLDFGKAITKKRTLEETEEAVETMLVSKTPVETRGHTSYLTFATFLPAIENNVALSEVELQKEAELVEELEKEAE | Function: Catalytic subunit of tRNA (adenine-N(1)-)-methyltransferase, which catalyzes the formation of N(1)-methyladenine at position 58 (m1A58) in initiator methionyl-tRNA.
Catalytic Activity: adenosine(58) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methyladenosine(58) in tRNA + S-adenosyl-L-homocysteine
EC: 2.1... |
B9SI09 | MKNKAELVVVSMPGVGHVVSTIEFAKNLIERNDQLHISIIVMKFPTTPFVDQYAKSLTASQPNLQLIHLPDQVEGLPTLQVFAKSVQSYYSAVIACYKPHVRKIVSDMISSRSSPDSVPVVGLVLDLFCVSLIDVGNEFDLPSYIFFTTGTPFLSLMLHLPPRHEQVGTEFSFSDPDVSLPGIANPVPIKCLPDAVFNKDGGYDTYLNVGRRLKDVKGILVNTVSELESQALQYLNSAQITSIYTVGPVLHLKSQPHPDMEQGRWGKIKTWLDEQPESSVVFLCFGSSGSLSVSQVKEMALGLEQSGHRFLWSLRLPPVK... | Pathway: Pigment biosynthesis; anthocyanin biosynthesis.
EC: 2.4.1.-
Catalytic Activity: an anthocyanidin + H(+) + UDP-alpha-D-glucose = an anthocyanidin 3-O-beta-D-glucoside + UDP
Sequence Length: 478
Sequence Mass (Da): 53103
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A0A6L5NSY8 | MFIWGKVFGAIIGFMFGRVVGAIFGCWLGHQFDRRRMISQYNNNIRNVQSVFFRSTFALLGNMAKATGRVTEADIQIASLLMDRLNLIGQSRIDAQQAFRDGKQASFDINQQLKEFATASRGQHALRRMFLEIQVQMALHDGDLHKNEMAILTSIASELGLMAQLKQIIANIQSEFSHHKASSQPHSMTVPEAYALLGVEESSSDQQIKRAYRKLMNENHPDKLVAKGLPEEMMALAKGKAQDIQSAYQLIKSERGMR | Function: Regulatory DnaK co-chaperone. Direct interaction between DnaK and DjlA is needed for the induction of the wcaABCDE operon, involved in the synthesis of a colanic acid polysaccharide capsule, possibly through activation of the RcsB/RcsC phosphotransfer signaling pathway. The colanic acid capsule may help the b... |
A0A4Y7S0S0 | MIKVLVVDDSPVVQALLIHILSSDPEINIAGAANNGEEALYYVKTYKPDVVTMDMHMPKMNGFEATRKIMETHPVPIIILSASWDHVDVEQTFQALGAGAVAVLEKPAGTTHPDFDHMARVLIQTVKSMSEVKVVRRWARFRPASLAATHPPVVFEKNPAEINCVAVGASTGGPMALQTLLAGITSDFPAPLLVVQHITKGFLQGMVEWLANSTGLSVSIATQGTYPLPGHVYFAPDSSHLGVDNTGRIFLSKKEPEHGLRPAVSYLFRSVAEVFGPNAAGVLLSGMGKDGAVELRLMKENGAATIVQDKESSVVHGMPG... | PTM: Phosphorylated by CheA. Phosphorylation of the N-terminal regulatory domain activates the methylesterase activity.
Function: Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate resi... |
A0A8R1DVR3 | MELTLIARCRDGLILATSIEGNSDQSGDSSMVKYSNQAKMIFKKLAGSPAQQSVESGPFVFHYIILENICALVLCDRNFSRKAAFHYLNDIAREFLNNYSTKVEAVVRPYHFLDFDKYIQQSKIKHNDSSKYTMNAVSNELQDVTRIMVTNIEDVIHRGEALNILEHRASELSGLSKKYREDARALNRRSTIFKVAVSIGVVGVLFLILRFIIF | Function: SNARE involved in targeting and fusion of ER-derived transport vesicles with the Golgi complex as well as Golgi-derived retrograde transport vesicles with the ER.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 214
Sequence Mass (Da): 24317
Location Topology: Single-pass type IV membrane... |
A0A8R1ERV1 | XVNKVISYGSCQFPTLGFVTDRYKAIENFVSEQFWKLLVEHTRDGHKVDFLWARNRVFDHDTALVLHEDAKEAKEGVVEQVTKKPKSKWRPQALDTVELEKLGIQN | 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... |
U5IB79 | RTRMALREKGVDFEYRDENLREKSPLLLQMNPVHKKIPVLIHNGKPVCESAIQVQYIDEVWPHKNPILPSDPYQRAQARFWVDFIDKKMYEAQRKVYATKGEEQETGKKEFIEILKTLETELGDKPYFGGDVF | Function: Is involved in the conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.
Catalytic Activity: glutathione + RX = a halide anion + an S-substituted glutathione + H(+)
EC: 2.5.1.18
Subcellular Location: Cytoplasm
Sequence Length: 133
Sequence Mass (Da): 15682
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Q8SVQ3 | MEALLKILKGPVRDHAEYLRRFILDFKNERKELEIRLGKIVSKEDGSRMKVDTVAPIVFRNIPVDYRFESAVDPGDFKVLKKQFSFCKGESTNDVVIINEDGRETYENDELKKVEKKTRSQKLDIYIPGKRYDVRLVLNEENEMFKRPSKKKAIVKRVRRRETYFIEPYGFDFTEVVLSGEKDEKEKRKFEIEVEVFNSEKLVSNDFISLIYNFNVDLAIQ | Function: First step of mRNA capping. Converts the 5'-triphosphate end of a nascent mRNA chain into a diphosphate end.
Catalytic Activity: a 5'-end triphospho-ribonucleoside in mRNA + H2O = a 5'-end diphospho-ribonucleoside in mRNA + H(+) + phosphate
EC: 3.6.1.74
Subcellular Location: Nucleus
Sequence Length: 221
Seque... |
A0A914HD68 | MNSSVNSCEAGDVCSSSTSSGDEFVDLDLEFSSAGEMLFSLPKKDKSFVEQSLKEIEAGCQKEGGGVVELSYPRVGLPHVGPTAQTKIVLPAWVVESKRFSAQIDTSDDHMHNGLQLDNLRPEFLHILQKSISFWFPVQRSVLPTLLQSANSVLPPRDLVICSPTGSGKTLCYVLPMLNALRICAFSPSSVFALVIAPVMNLEFEKLNFFGANIVLLGKNDYRSERSALFPNGTRKCKAHVIVATPGRFVEHLLDENGDLDLSMLRYLVVDEADRMQDMARMEWLELVEKYANVPSVGTLSVSSLTDRSHNNWLQRILVS... | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 548
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): 61834
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A0A2N1NTS4 | MIRDFNNIALYLSLCVLRLWCSTLPGYIHPDEFFQSPEVMGGDVFGYEVFRPWEFEQSPQCRSIVIPALTIGLPFNILKILNVWAIKFGYGDIINSHSVFITERLSFFFLSFGIDYTVYTIAQLFYPNNAIQSLLVLASSYVVLIFNTRPFSNSAELILLALLFCTYVKGSTPKFPLRRQPGDSSTDRDEFPVNLAFLFGCIAAFGFFTRITFILYAFPIGIAFLHYIFLSARAQGKSWHSKFSELFPACLGLVTTTGICVLADSLYFGTLKVTFGGVILNNDHIFEFLSNPAKFMKIGWHGKFIITPLNNFIYNINSEN... | EC: 2.4.1.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 632
Sequence Mass (Da): 72316
Location Topology: Multi-pass membrane protein
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M2ZXM8 | MADFAAAQKRILKRRAARESALTAANTAARESRTAQLTALPPQLRAYAFEFLSFWDFLKSPHGTRPAFRVGQVDAELLDEALLDLLKKQAGEGLKLYGAHLKDDYSREITFFLRTCMWKLSIWDHGQSYGASLQGLKYVDARGKPDPNTLVRKEATTWQRLLYGIISVGGRYGWARWEDRLSSLENGYDEPTPLIRRLSQWTTYLSTTHNIAAFISFLVFLYNGRYRTLTDRLLRLRLVPASNQTSREVSFEFLNRQLVWYAFTEFLLFLLPLVGISRWRRWISRAWKKMKIGMMKLAQGNPEAGIDDEDEDIKKGELAF... | Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Membrane
Sequence Length: 507
Sequence Mass (Da): 57629
Location Topology: Multi-pass membrane protein
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A0A1L0B042 | MIGALRNNNFLRQNLKLYNLRANKPMGVCKSIILPYNIYHRSFGTTKETLYKKDKPDHTKQQSINNKEYYLSQTNNFLTKMKINLRWLLKKSMKPFNIDDMSAFVSVFLWTHLTMILLWTTGFFSLIILLLNTVMAQDYLATKFGEIITNNNSSNMLIVFENAILPDLKSGKIVFQNVFVSKRPRDKKENKVIKASHLEAARRAEYALQSQQKIYLPVIFDPKFKEGNYTQYDLTIKELEVSLSFKKWFQGRGLIEEMSISGIRGVVDRTNVQWKEGDDPRNYLNVKQPGDFEINNFKMNDVLFTLYPPDGLRPFKVSIY... | Function: Involved in the organization of the mitochondrial membranes and the global structure of the mitochondria. Also required for mitochondrial distribution and mobility as well as for the maintenance of mitochondrial DNA nucleoids structures.
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 567
... |
A0A2Z2P4A2 | MLFNSSLFLFVFLPIVLGLFYWLLWRNSFRLAIAALTACSLFFYGFWNPAYLPLLLISIVCNYAIGRSLYLQPSRILLSLGIAFNLSLIAYFKYAHFMVSIANEVTGNSWVMHQILLPLGISFFTFQQITWLVDVNKGGSERPRFIDYVLFVSFFPQLIAGPIVHHQEMMPQFKRLQSQNDTLGTSGASGQPGIFSANFIAGNISVGLTILCIGLFKKVIIADSLALYASPIFQAAELGITLTSYEAWLGALAYSLQLYFDFSGYSDMAIGIARLFGITLPMNFNSPYKSRSIIEFWRRWHMTLSRFLRDYLYIPLGGSR... | Pathway: Glycan biosynthesis; alginate biosynthesis.
EC: 2.3.1.-
Subcellular Location: Cell inner membrane
Sequence Length: 542
Sequence Mass (Da): 60955
Location Topology: Multi-pass membrane protein
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A0A1I8P9S4 | MGEHTKSSASTEHMQQQQHQQQQQEASTSSGSAGLTPSPEAASSAAAAAAASTGASGPSLTAKDARELQEIRNLLWGPSIRVDVFRRWSQGFEFSDVEPSALVQKQGGPCAVIAPVQAYILKILIMDTPGHFLKDLTPDKCKSLLIQALCTILSKCKAQHIRLVTLPVDKCSEAKETSSADAPPNDRGDDDICDSDVANLNSSEAMAEAAPPYASDVIGGDDISLTTMADEEISPEEYHNRLNVIHFNSIEELERYYSHNFDILSAKYGVLLFMYTVLLTKDIENVNSELLDTSEPLIHNTYGYGSQALINLMLTGRAVA... | Function: Hydrolase that can remove 'Lys-48'-linked conjugated ubiquitin from proteins.
EC: 3.4.19.12
Catalytic Activity: Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting... |
A0A1G4WSK7 | MGAVTEAGSRAVPRLHDREWQLRAKCRNGDASLFFHPDGERGRARKRRQQLAREVCADCPVARECGAYSISFQEAFGTWGGLSEDDRRRYLETVRAP | 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... |
A0A087U9B4 | MSGPTIPPSYISDLEWSCYFQPNESDSNVTCLYEPELHEPKDPSYYSLKYQIVGTVFQGIVLIVGILGNIMVVIVVTRTRSMHTPTNCYLVSLSIADFMTLIASVPNEILAYYLLGDEWIWGRVGCAIFIFLQYLGINVSSLSITAFTVERYIAICHPMKAQIVCTVSRAKKIIIFVWIFACLYCSPWLFLTKTKPLHYKGVQDRETCTFALSRQNYLGYFFADFILFYIFPLLLSCVLYGLIARVLFSRDIQKNSDGKSNGMVSPQESKKSSTNGTSARAQKGKESLGNMSSK | Function: Receptor for thyrotropin-releasing hormone (TRH). Upon ligand binding, this G-protein-coupled receptor triggers activation of the phosphatidylinositol (IP3)-calcium-protein kinase C (PKC) pathway.
Subcellular Location: Cell membrane
Sequence Length: 294
Sequence Mass (Da): 33128
Location Topology: Multi-pass ... |
A0A087UT08 | MALYEVFSHSLKIKHKSTLCSKTSLFYILATALQFVFPMLVAYYIQGFLKRTEAYREQPDVSFKHKMLLILETKFPEQLIFWSTYKKLNQMMSSRTLRLIPEIEHREDDVNRDGKKDEIQMSIDISLTDQEIHSVKLILIFDYKL | 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: ... |
A0A286S4H1 | LMIGAPDMAFPRMNNMSFWLLPPSLTLLLSSSIAENGAGTGWTVYPPLSTNISHSGASVDLAIFSLHLAGVSSILGAINFISTIINMRATGMSPDRMPLFVWSVGITALLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHP | 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... |
A6MUS4 | MGVALLFRNLPVSYDLSYFWNLGSFLGKILMIQISSGFLLVFYYSNSSFFSFDSVQYLMFEVNEGWFFRLLHFNFVSLFFIVSFLHFLKGFFYSSYRLKSVWSVGVILLVFLMLISFLGYVMVWSQMSFWAGIVITSLLGVVPYLGLDFILFFWGAFIFGGNSLKFFFALHFLLPFFLVFLVFFHLYFLHFYSSSSSLFFFSFFVKKSFYPFFWFKDLLNIFLVLVYFGFFLIAPFFFSDFLMFEEINFLVSPVHIVPEWYFLFAYAILRSFTSKVLGVFLLFLSILVFLGFVFLGSKKGLNDISNKSLVLVFVLLWFFL... | Cofactor: Binds 2 heme groups non-covalently.
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 p... |
Q74Z56 | MRLQGKMDEYISERRYCYLYPALLLGGEVIKLILGEETIEHDRKTWYLLNGGNFVNQLFVHHGVLLWTLLMGLVLALQYHVRTTEFDPLPLDARQLGPVRRHPLKMLGSMAVQTVIKVLLVVTVLQALFWFMDHLFVWTGGRCTVSDTKDSVACRRLGGEWVGGFDISGHFCLVMNLSLVLWLELTELQRYMHSQEIQLRKFAWARTTVLGALGVWLALLAITAIYYHTFVEKLLGTIFGYSTSLVIYYVLPRINRGLHYL | Function: Fatty acyl-coenzyme A (CoA) diphosphatase that hydrolyzes fatty acyl-CoA to yield acyl-4'-phosphopantetheine and adenosine 3',5'-bisphosphate. Preferentially hydrolyzes unsaturated long-chain acyl-CoA substrates in the endoplasmic reticulum (ER) lumen. This catalytic activity is required for maintaining ER st... |
A0A1G0D7K8 | MRRAAMEKARDFDSAVISDMAWLKQASANDVQAGILMYAPVYKYGMPHNTLAERRANIAGWVYAPLRVSDLMADILGEHSTEVDIEIYNGKEVVGEHMMYDSDNIPRAHLLTKDARFQATTHLDFTGQHWTMVVHSLPNFDALEDDEKPKLVAIGGIGISILLALLTWLYLYDRERTHNLLRQNRYLSMRMFAILEEERRNLALELHDEIGQWLTAIQFQAKTMSKIAESASPLHTSIRIINESASEMHEALHKIVHNLRPSRLDALGLVASLNKLVSEWCLNHYGLVKCEFVPEGELGVLGDNLNITLYRIVQESLNNA... | 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... |
A0A2G9PQY2 | MLIKCQHRQKTFYTICHRNRFIFYLFFINIMIIIVTGVPGTGKTTLSKAIAECLKHEYVDVNAVIEEHKLSEGRDEKRDCAIVDIKRLEKALSKKISTSNDLVIDSHLSHYLPSELVDVCIVVRCDLKILKTRLEKRGYSEEKVRENLDCEILDMCLNEAEEIGHNILVVDCSGKVDIKDICQKIKAVH | Function: Broad-specificity nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates.
EC: 2.7.4.3
Catalytic Activity: AMP + ATP = 2 ADP
Sequence Length: 189
Sequence Mass (Da): 21717
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V5UTB5 | WAAMAGTALSLLIRLELSQPGTLIGDDQTYNVVVTAHAFVMIFFMVMPIMMGGFGNWLLPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLASTAVESGAGTGWTVYPPLSSGLAHSGPSVDMTIFSLHLAGVSSILGAINFITTVINMRSSGMVMERVPLFVWGVMITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQQAGKKEPFGSLG | 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... |
A0A0B2V372 | MFVYTLYGLSVVCALLYVYTRSKATSSEDAQFLSFQRSYLVVYLLAVAGDWLQGPHVYALYESYGMTKHDIELLFVAGFGSSLLFGTFIASVADKYGRKSSCFLYGMLYAGACITKHFANFWILMLGRLLGGIATSILYSAFESWLVFEHNKRGFNEQLLTTIFSHATLGNSLVAIISGVVAQYAADLFGYVAPFDVSLCVLTVMSVVLVFTWPENYGDQKAAVWQHFVDAVDSMKNDGKVICLGLIQSLFEGSMYVFVLEWTPALTHASNGEPIPHGYIFASFMVAIMMGSSMFKMLTRYHRPESFMRVVLLVSSVCLA... | Function: Mediates high-affinity intracellular uptake of the rare oligo-element molybdenum.
Subcellular Location: Cell membrane
Sequence Length: 508
Sequence Mass (Da): 56189
Location Topology: Multi-pass membrane protein
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A0A8R1IFW7 | LFSTFSDSPVTEKVDAVPARLIKEERRSSSADTVGTGGDHVELFSICYSGKTLRLPTSQPHMYQVIYRILKQVYLPLVPQILVGLPKGWTEVILDHNQVAECAKKYNMAAKPYAKNWGGSYNTDTLREWGHPQCTFRVARDIVNFAYECAVPRPSDLNNHYKSFSSETYGETNLEQMASIIDELRLGPSDVFVDLGSGIGQLVCFTSAYTKIKKAVGIELSPLPAGHAVDLSNYFKK | Function: Histone methyltransferase that specifically trimethylates histone H3 to form H3K79me3. This methylation is required for telomere silencing and for the pachytene checkpoint during the meiotic cell cycle by allowing the recruitment of RAD9 to double strand breaks. Nucleosomes are preferred as substrate compared... |
A0A0B2VTM5 | MEGLRSSNEIRQAEAASELAEMLLLGNEESLPNLPVKDIVHALIALLQKEHNFELMLTAARCLSNMLEALPRALPIVIDAVPFLLEKLKRIECIDVAEQSLMALEVMSKRNGKNIMAAGGIAATISHVDFFSVPSQRLAFQIAANCASFVTVNDFAQVRDSLADLTQRLLIEDKRCLESICVLFCRLVDNVRGHADKLREVAGQNHALLKNVQQLLLVQPCAVGPNTFQALVRMLRHMASKCSDLAVALINMDFARTIRFLIIGTEGEDRSLEMVNRPSQQLQELVFLAGELLPRLPSEGVFEIDSVMMRSHAAFHEIPP... | Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.26
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Length: 912
Sequence Mass (Da): 99475
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A0A8R1IEI5 | MPPGEPVASNSEKDEDVFSEPKEKRYQPCFKKSDPFVEPLLNFDADTSKMEEVYSAVSHWTQIALDLKAKGYPIAEGINNWKKFDAKTREDARMLDDFLNLFISKNLYAQDKPYEVLRVLIAQGTPYLEFKEKMSRVDFSIKCNTIWENDAVAYRCNTCALTPCMSLCESCFDANGHAGHDYTRFFSREGGACDCGNQDVIREQGNCPEHGDESKRPKYEMNDVCIAEYIVMKLLVRLFLDYRGWLWSHRDFPAKV | Pathway: Protein modification; protein ubiquitination.
Function: Ubiquitin ligase protein which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation.
... |
A0A3G1SAB2 | HKDIGTLYLIFGAWSGMVGTALSVIIRAELGQPGSLIGNDQIYNTIVTAHAFIMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLTIGLLTESGAGTGWTVYPPLSSNISHSGASVDLTIFSLHLAGA | 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... |
A0A8R1ECI1 | TLPETKVIYFLHFWTLSAFLYAISKSPNTQLIGKIDEDVMFFPDQLLPLLETGEVNYNSTVIYGSKYGAGSPVNHDDLSKWHVPKSAFNCRFYPEYFAGPIYFTTRKAAERILRASKHRKFISVEDILITGIIAGDVGVVKKHLPMIFPFIVSEPAKEGRQILGWHKLKSNLQYEEEFNELRNSQCIPCKKLLKSFGDENE | EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 201
Sequence Mass (Da): 23039
Location Topology: Single-pass type II membrane protein
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A0A2G9Q1J0 | MMLKSIYKPDGGKLVRIEVDLLDNSINQIKICGDFFLHPEDGLEMIEANLVGIRMMERDIRMSIKQTVETKRLTLFGITPKDIAKAVMMAR | 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: 91
Sequence M... |
A0A087TVJ0 | MFYTVHALFFFSIPSHKEFRFLLPIMHIALMTSSVVMYRISVNKLRVFGFEVNKTCNVILIATNLLVNIPLSIYMGLFHQRGSVDAALRLADLVTENSSVLFLMPCHSTPYYSYIHKNISMKFLTCEPNFENADGYIDEADEFFENPMEWLTKNYDSNRNQLLPTHIVMFDKLYDNISIFLKKFHYKLCFTAFHSHFTQ | EC: 2.4.1.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 199
Sequence Mass (Da): 23354
Location Topology: Multi-pass membrane protein
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A0A1C8C392 | HIISQESMKKETFGMMGMIYAMLAIGLLGFVVWAHHMFTVGMDIDTRAYFTSATMIIAVPTGIKVFSWMATIHGTKIKYTPQMLWSLGFIFLFTIGGLTGVVLANSSIDIVLHDTYYVVAHFHYVLSMGAVFTIMAGIIHWFPLFTGLSMNNYLLKIQFFTMFISVNMTFFPQHFLGLSGMPRRYSDYPDMFLSWNMVSSIGSLISTASILMFMFIVWNSLATMQKILFNSNFNTSIEWIQ | 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... |
A0A2G9PUC6 | MKLRTKLILYFTFVILLMSTFLAGFYILYITNYLTTDRQQALNSLAINTKNEIERVLTRGYDDVQFIANSHSFNVQTHLSGELLDSLNLIQETYGIYDDIVVLDLDGNVISSTTYSYHDQFGKKDWFKKARDGSVVVSNAHMILDKSLPVINYLAPIRSTDGNITAVVSIQYPLDHLWDITDKISTNKKLNIYLLNPFGMYIVHPDKKMIFSRANDDLPLSGFSSKDGVIEYETKDDRQMIGGYSKMFDSVDYMGEGWTVVVEESRDQYLAVIKNSYIILGLSSVILILLIILLYFKLNSWFIVPIDVLQKGINSVKEAD... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 596
Sequence Mass (Da): 67525
Location Topology: Multi-pass membrane protein
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A0A7S1SR33 | MSDNPFSTNDNPFEAPVATSGIVAAVESEDSPTAGAWGGAVSESAPPTVPVDANPYSKPPSAAYDGAYGDGGGGGGAYGGGGGGGAAYGGGGAYGNSEPAKGNKDLSERERELARREAELAQKEAQISRLETEAAQNASKVAADLKNWPRCCPIVRHDISGEIPPAWQGPVTKTYWSYLGLIVCLVMNCIAVTVLSFGTGKELGSFFMAVIYLVTATPLALFLWYLRLYNATIRDRAITFAVFFLMYLVHVIFCFWAAISPPIGSAGSQWSFAGIFTTISAFGNGLGYGILCIISTALWGLEAIWSLLVLQQTYSQFRTG... | Function: Probably involved in membrane trafficking.
Subcellular Location: Cell membrane
Sequence Length: 349
Sequence Mass (Da): 36535
Location Topology: Multi-pass membrane protein
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A0A5N0T720 | MSRYVSVLVTRPQPQADELAARLARSGIPALLAPAFRFEAMPKPPVWPDPDDDGSRSLWLFTSPRAVAFGLPLLGQRIPAQARLGAIGPATAASLEEAGRPAWIVAGGQHTSEDLLADPRLRERQGTAFIVTAPGGRGWLGPGLERLGWAVRTLDVYCRVPLAPPPGVLGALAESGPVISAWTSGNAMEALLGQLGEASRRAVTGGLFVVASARLQAMAIGLGARQVTIANSASNAHLRAAIIEAWQAGADGRGHESRG | 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... |
A0A8R1IGX3 | XAKQLEGGKRIGYGARALNEGGFQSIPKLHFPGGCLVGCSAGFLNVAKLKGTHNAMKSGMVAAEAIFDEIQTERRRCADELKATRNIRPSFNTSLGYIGGLIYSGLFYVFGRGLEPWTLGHGKKDNEKLIPAKRREGD | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Accepts electrons from ETF and reduces ubiquinone.
EC: 1.5.5.1
Catalytic Activity: a ubiquinone + reduced [electron-transfer flavoprotein] = a ubiquinol + H(+) + oxidized [electron-transfer flavoprotein]
Sequence Length: 138
Sequence Mass (Da): 14982
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A0A0B2UUY8 | MRSTRRSLVKRTFTIFATVLALFIVVFTVTRARPVHIIRNYASYSVTVNSLLLPEFVHPGGPSNYCPEVPTVFVIRTHPNDTTSREFVRKTWGRKVKNSLVFALGTDELGAIRNETLLEYQMHRDILVLNFIDSYYNLTNKAISTLRWASEYCTKPTVIYQGDPDVAVFPDAIKRFFGNIRRGQPYIFGKCLLDEAVHRDPSDKWYVSKELYAPSTYPTFMPGGANIFSSAAPQKLLEAMEPLEPYFHLEDVFVSGILAERAKIPRICLETIAFTWELGNLHKCWQDPLLAILEVGSPELVQKAFNDVDRGMAGCRH | EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 317
Sequence Mass (Da): 36087
Location Topology: Single-pass type II membrane protein
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A0A379GGS1 | MLSTKDMLVLGMMVFALFLGAGNIIFPPMAGFQSGNQWFSTSLGFLVTGVLLPFLTLVTVAIRGRGERLSIDLPSWFAVLFWIALYLIVGSTFAMPRVTNTAYEMGFLPLGLIEKNTTTHLTFALIFNLLSMFFMLKQGTMISAIGKFMTPALLILLVVVGIAVVAKPLSPIEEPTGLYAVNGFFSGIIDGYQTMDVLSAMAFGGIVARALYTKGITNPKQIGFITIKAGMISVLLLAALYLCLFYFRCHKSRSICFC | Function: Component of the transport system for branched-chain amino acids.
Subcellular Location: Cell inner membrane
Sequence Length: 258
Sequence Mass (Da): 28151
Location Topology: Multi-pass membrane protein
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B9T756 | MNQQAGAPSYPVLTGRRDGMTSKAASVDLPSPSISLNDALEYFSSKGLDMLDFVTLLGAHSMGKTRCRYVEDRLYNFNNTGKPDPYMDQAFAAQMRKLCPPRTKKGQSDPQVFLNPDSGSNYKFTESFYKRVLSYKSVLGVDQQLLYNNDTLQIAQEFAANFEDLRRSFALSMNRMGNINVLTGNAGEIRQNCHFTNKK | Cofactor: Binds 2 calcium ions per subunit.
EC: 1.11.1.7
Catalytic Activity: 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O
Sequence Length: 199
Sequence Mass (Da): 22351
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A0A3P6BUK8 | MARPGEHITILTYSRTRIHVYHQVPCNAGAKTLVNNGYDPEVIDIRSLKPFDLYTIGNSVNEVPKPYAGTLEEWKVVQPAQIATAVEQLCQ | Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2.
EC: 1.2.4.1
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] + H(+) + pyruvate = (R)-N(6)-(S(8)-acetyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue acetyltran... |
A0A3P6BGX3 | MEHCESLQQRVELALKLKSIPYLFVQEDLHNKSQALLQHNPVHKKVPVLVHKKRNGPQILPQDPYKRSKVRFWASYIQLHLFRCGDESGENRRRRARESSHRGEGEAEHHRERRAQGYFLGY | Function: Is involved in the conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.
Catalytic Activity: glutathione + RX = a halide anion + an S-substituted glutathione + H(+)
EC: 2.5.1.18
Subcellular Location: Cytoplasm
Sequence Length: 122
Sequence Mass (Da): 14506
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A0A2P6G3Q4 | MISTEEALKKLLRLVKKKSKHRVPIEDCADRILANDLVAKHSQPPFSASSMDGYALKSKNKNPGTILRIVGECAAGKSFNGILKNNEAVKIFTGAPLPQGADCVVIKEDVTVQNNFVKINETIEFSNFIREKGIDFRKGYILKAPTKIRPATASLIAAMNYNEISVYEKPSVAIIPTGHELVKPGTKLPPNKIIASNSYGIAAMLKSFGAEPHLFPITDDDVPSIQGKINEASNCDLILTIGGASVGDHDLIVKSAKLIGLKLAFHSIAMRPGKPLLAGIINKKILVGLPGNPISSLLCCYLMVKPVIEKMLGLGSTTNK... | Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
Function: Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP.
EC: 2.10.1.1
Catalytic Activity: adenylyl-molybdopterin + H(+) + molybdate = AMP + H2O + Mo-molybdopterin
Sequence Length: 400
Sequence Mass (Da):... |
A0A021VRU1 | PAPASGASGVDWLGDALAEAAAADVVLDGLLGIGARGGLRGTAAEVVRLLAEVLGQLESVGAGHVAALRPAVVAVDLPSGLAVDTGAVPGPVLPADLTVTFGVPKPGLLLPPAAHLVGRLEVVDLGLRPVLAERSVAPALVRLGAADLAGLWPVPGPGAHKYSRGVVGVVAGTATYPGAAVLTVAGAQGAGCGMVRYVGPDRVREAVVAAHPEVVTGSDAQVRVQAWVLGPGLDPADEDQADRARAALAGAVAEHLPVVVDAGALWLLPDRVPPRVVLTPHAGELARLLQGRWVDVDREDVEAEPLRWAREAHDRTGATV... | Function: Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent h... |
A0A6C1SYV9 | MIRTFLGLELPQHIRSQLVLQQFLMPVKRKLPPENFHITLVFLGEANNAQLDALDLELSRLDVTPFTLTLEGLGLYGKGKAHNLHALVRPEPDLMALQEKLLRRAREAGFTPDKRRYHPHVTLSYLRPGSFEQRELEKAVAHSSQFRTEPFEVTEIALFRSHLRPDGAIYDVLERYPLSAELRALKQ | Function: Hydrolyzes RNA 2',3'-cyclic phosphodiester to an RNA 2'-phosphomonoester.
EC: 3.1.4.58
Catalytic Activity: a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + H2O = a 3'-end 2'-phospho-ribonucleotide-RNA + H(+)
Sequence Length: 187
Sequence Mass (Da): 21528
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A0A961KTM5 | MTLRLAALLISGALVLAGCAGAPNDNMRNTGSDNTGVYQQDSPEFFVHQVGDRVHFAVDQSTLSAEAMSILDAQAAWLGQNGEFSALIEGHADEQGTREYNLALGARRAAAAKDYLVSKGVAGGRLRTISYGKERPIEICSTEDCWSRNRRAVTVVSAGSS | Function: Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity.
Subcellular Location: Cell outer membrane
Sequence Length: 161
Sequence Mass (Da): 17119
Location Topology: Lipid-anchor
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A0A2D9IS81 | MLHYIFKKEISFPENDELEAAVFGMGCFWGAEKKFWERKGVKLTAVGYAGGSTKNPNYRDVCTGLTGHNEVVKVLFDPSELSYLELLSTFWENHDPTQLNRQGNDIGTQYRSGAYYFSDTQKRILLETKAIYEDDLQKAGFSSIMTEIKKAPEFFIAEDYHQQYLAKNPHGYCGLGGTGVTLSEGSKTSIEAF | Function: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
EC: 1.8.4.11
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionine = [thioredoxin]-dithiol + L-methionin... |
A0A3L6G4D7 | MHCALNKLSPRPLTSKLIFIAVHFWAPTFKWGISIANIADFAKPPEKISYPQQVAVACTGIIWSRYSLVITPKNWNLFSVNVAMAGTGLYQLSRKIRQDYLSGEKDAAPQLQE | Function: Mediates the uptake of pyruvate into mitochondria.
Subcellular Location: Membrane
Sequence Length: 113
Sequence Mass (Da): 12679
Location Topology: Multi-pass membrane protein
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A0A7Y7DRT7 | VGGGVRTGADVRALLLAGADKVSFNSAAVANPDVVAEAADHFGSQCIVVAIDAKTVAPGRWEIFTHGGRRPTGIDAVAFARTVAAKGAGEILLTSMDRDGTKSGFNIPLTRAIADAVDVPVIASGGVGTLDHLVEGVTEGHASAVLAASIFHFGEYSIQQAKAHMAAAGIPVRPA | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9.
Function: IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ... |
A0A3B3HHR9 | MPGSAQISYMGPWPKDVGIIALELYFPSHFVDQAELEQYDGVAAGKYTVGLGQARMGFCSDREDINSLCLTVVQRLMERNGLSYDSIGRLEVGTETIIDKSKSVKTVIMQLFEDSGNTDVEGIDTTNACYGGTAALFNAVNWVESSSWDGRFALVVAGDIAVYATGSARPTGGAGAVAMLVGPNAPLAFERGLRGTHMQHAYDFYKPDLMSEYPVVDGKLSIECYLSALDRCYSVYRNKIHTQWQREGSDQRFSLEDFGFLVFHSPYCKLVQKSVARLMLNDFLNHPNPNTETGPFTGLDAFRDVKPEETYFDRDVEKAF... | Pathway: Metabolic intermediate biosynthesis; (R)-mevalonate biosynthesis; (R)-mevalonate from acetyl-CoA: step 2/3.
Function: Catalyzes the condensation of acetyl-CoA with acetoacetyl-CoA to form HMG-CoA.
EC: 2.3.3.10
Catalytic Activity: acetoacetyl-CoA + acetyl-CoA + H2O = (3S)-hydroxy-3-methylglutaryl-CoA + CoA + H(... |
A0A8I1IHN4 | MRLMLVIALAVLVAAGFHAFLYQAFRVPSGSMKPTLLVGDSILVSKLAYGGPFRGCILGWCPEAPPIGGLPERGDVIVFRDTVHGGYAAKRIVGLPGDEVAMLGGRLYLDGQAVEQRPGVMFHEVYEAQGQLGQRPLCANPDAGPGAYCLKPVQIETLPNGVTYDTLQIGAAAVDTTAPIVVSAGAYFVMGDNRDNSTDSRFDRAGGGYGSVLLADIVGRVEMILFSTAADDVMAPGTLRRSRLFLPISEARLRRAQ | Catalytic Activity: Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
EC: 3.4.21.89
Subcellular Location: Membrane
Sequence Length: 257
Sequence Mass (Da): 27296
Location Topology: Single-pass type II membrane protein
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A0A520P5F3 | MDINHKNFELSFEIFPPRNLKASFKLWRTIEVLDKLNPNFISVTYGAGGSTRDLTQSAVSVIAKEYNIDVAGHLTCVGSSKKEVIDIALEYEKVGAKKIVALRGDLPMDHGNRINDTDSFSSSVELIASLKKNTSFELYVAAYPNVHPNAQSEKSDLDTLKAKFDAGADSAITQFFYEKEDFLRFRDKCNSVGIHQNIIPGILPIDNWIKTKKFANRCGIIAPQWMNKAYENYKNNEDHNLLSQALCTEMCDELIQEGVSSLHFYTLNDPKLTQKVCEALGRKSCPTNIKKVA | Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway.
EC: 1.5.1.54
Catalytic Activity: (6S)-5-methyl-5,6,7,8-tetrahydrofolate + NAD(+) = (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + H(+) + NADH
Sequence Length: 293
Sequence Mass (Da): 32891
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A0A520P2F5 | MNKSLPRVVMAFDFGIKNIGIAIGQEVTKTASTFYSITAIDGQPNWSELDKIINEWQPHLFVVGDPFNMDGSRSKIQDLADRFSNSLNKRYDINIEKTDERLSSREAKERLEKETIGNKDSSNKHSISAQVILEDWFRSKD | Function: Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 141
Sequence Mass (Da): 16125
|
A0A2A4XGR2 | MSKRNVSKTAKKTTPPKSVASSKKALQGRVSSDARGQQAQWVPWFRNAAPYINAFRGRTFVVVFSGEAVANTHFAGLIHDFALLNSLGIRLVLVHGTRPQVEARLKARASILAREYTTLFHRGLRVTDDTALACVKEAVGTVRVEIEALLSMGLANSPMAGARIRVASGNVVTARPLGVHEGVDYLHTGEVRRIDAEAIKQQLDQNAVVLLSPLGYSPTGEVFNLSAEDVATSAAIALHADKVLYLAEGSGLLDGRKRLTRELTLVAAQKLLTSRRKLPDDMHRILNSAVNLCLNGIKRVHIINRETDGALLQELFTRDG... | Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 1/4.
Catalytic Activity: acetyl-CoA + L-glutamate = CoA + H(+) + N-acetyl-L-glutamate
EC: 2.3.1.1
Subcellular Location: Cytoplasm
Sequence Length: 478
Sequence Mass (Da): 53030
|
A0A920KK01 | MLELSLEHESHIIDDREIIREGTSYTYDTIRSIKGTNKNALLYLIIGFDNLYSFHNWYEYKKILEECNIIVMKRNQKEHSLSIDPSLSKHMTSNRSIFSNVSCGKIFIEDTFEIDISSSDIRRKLRNKETIEELVHPELSKWLSSNYIY | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
EC: 2.7.7.18
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide... |
F7UYK6 | MEEKPIKSYSVTALGTLMKELNQPTFRAKQLAEWLYARHACSYDEMTNLPASLRSTLNQRFPLFAPKIIERSISQDGTRKYLIRFGDGVLVETVGIPSRDNQRLTVCFSTQAGCPMACAFCATGKEGFVRNLTPGEIVDQVLVVQEDFGTRVSNVVGMGQGEPFLNYDNTLAALHILNDENLVGIGSRRMSVSTCGIIPGIERFAGEPEQFTLAISIHSAVQHVRDALMPNVARYSIPDLKRALKHYVQKTNRRVTLEYLMIRDVNDSEEDLAAFKDFCSGLLCHVNLIAMNNIDDSPLQPSDKRTIEQWISALQAQNIE... | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs.
EC: 2.1.1.192
Catalytic Activity: adenosine(2503) in 23S rRNA + 2 reduced [2Fe-2S]-... |
A0Z6I6 | MLGLSGGCDSIALLHLAHAWLDHVGPERRPALRAVHIHHGLAPEADAWVEVCHDVCQQLSIALSVYRVTPVTDEGKGIEAAARTARYSVYRQELKSGEVLLLAHHADDQVETVLQRLLRGTGPKGFAGMPRRRELGQGVLSRPLLGVARSVIKRWADNRELAYVIDASNQDMRFDRGFLRTEILPKLEQRWPGYRESIRRATELQSGLLRQHNAQPLALTANVMGEPAMAYHLKDSAQDSRGVLAYSLHRWLSELLLDVPAAARLTEFVRQCYEARTDRCPEVDVGRGMLRAWRGLICFTPYFVEEAQLSATLVAGQVYE... | 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)... |
A0A7S1UWF8 | SLLLKMLTKFAVIMHVWTGLPFIGSAKKVFAVMSRHFKDGFVTEVTSRSVLMLASYVFSLCIGLLTWVWFDDRFNTSTLPGGGDAAFYILFILSGLFTTWYPVLGLYVIILVDRLLRKVEYQHVWVSPLAALFVSCLAMMFFTYVSAIFLDTIDVLFLCFAVDKDHGVSPDAELAKLMESVPAFVEIENEKADDSSSSQPSRVVATPVVAVPAGSAVEVY | Function: Choline transporter.
Subcellular Location: Cell membrane
Sequence Length: 220
Sequence Mass (Da): 24375
Location Topology: Multi-pass membrane protein
|
A0A7C2IRE1 | MTFWDFFFGVFVELALQAVALFRLLTREDQEPEVRISWVIVVLALPFLGVLLYALFGEARIASAAQDRMNRAIESLGPPGLLTHGVHETADPMSPPFARAASVNGFHAVYGNRIALIRSSEGFIDQLIADIDAAREHVHISFYIWLSDRSGTRVADAVIRAARRGVTCRCLVDGLGSRPLLGSEPWRAMSAAGVRLAISFEYRFSLLQALRSRIDIRNHRKIVVIDGTVAYTGSQNCADAEFLPKARFAPWVDMMLRMEGPVVWQHQYLFMTDWITHSGEQEAARLLHDPPPEPVAMPGIPAVATGSGPVLQRHAVSDLF... | Function: Could be a virulence factor.
Subcellular Location: Membrane
Sequence Length: 480
Sequence Mass (Da): 53434
Location Topology: Multi-pass membrane protein
|
A0A832N446 | MKSNTLKSAFGLIAVTAFSAGTVAVWAETAPRPAKLVVNEEIEMVTEAKPAEGISNLEMAYDGWRFRADETQAVQADDFENPGMIFVEQALDNWNKVEGTEGKSCASCHGAPEESMVGVRATYPKWDESMGKVATIEMEINNCRTTRMGAEPWKYTGGKMTAMNALISVQSRGMPVNVAIDGPAKASWEHGKEMYYTRT | Catalytic Activity: 2 Fe(III)-[cytochrome c] + L-cysteinyl-[SoxY protein] + thiosulfate = 2 Fe(II)-[cytochrome c] + 2 H(+) + S-sulfosulfanyl-L-cysteinyl-[SoxY protein]
EC: 2.8.5.2
Subcellular Location: Periplasm
Sequence Length: 199
Sequence Mass (Da): 21784
|
A0A3B9K7Y8 | MIFITGGRNQGKTAFAEQLLRKKHGLTGGLQEVADGRSCSMEEAENCRILVHAEQLLLRRSEYLRAPEELLKILSEEGGPEILCADEIGLGIVPADAGERAWRDAAGSFSQAAACRASSVYRIICGIPVCLKKEAGEDGDE | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 5/7.
Function: Catalyzes ATP-dependent phosphorylation of adenosylcobinamide and addition of GMP to adenosylcobinamide phosphate.
EC: 2.7.1.156
Catalytic Activity: adenosylcob(III)inamide + ATP = aden... |
F7UUM9 | MSNESNTTTVSPLISPLHGSTGVPGDKSISHRAVLFAAMAEGTSRLSGVLDSDDVRSSLKAVKQLGAQISLEKTPDGSLAGGITGWGAKGPVQPDGPIDCGNSGTTARLLMGVLAPWDISVEITGDESLQRRPMRRITAPLMKMGVRFEPEGRETLPLTETGTRDLRAITYDAPMASAQLKTAVLLAGMYAKGTTTLNEPSPSRNHTELMLPEFGISTTAADRTASVQGPGVPQGCEVRVPGDPSSAAFLVCAAVMKPGSSIQVENVSLNTARIGFTRTLERMGADVNVRHAGSAGKEPYGIISACYTPNLHGCEVPADK... | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7.
Function: Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-ph... |
A0A2N2A8N7 | MVDTNQEPVEKGKPKKKKKESPKKAALKTKVEDKELKTKGEDKGVVKRLPVKKENAPVKKEGAAKSQGGKAPVVKKQTAANLKKFLKGAWSELKKVHWPNRRELVTYTTVVLTAVLIVAVLLFVIDAGLSKLLAFILQK | Function: Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.
Subcellular Location: Cell membrane
Sequence Length: 139
Sequence Mass (Da): 15365
Location Topology: Single-pass membrane protein
|
A0A2E3V7Y3 | MNKNTIFIIAGEKSGDKLGAELILSLKKKNPNFRFLGVGGSLMRASGIESLIDIEELSIXGIVEXXPKLRRLFKLRNMLVNEIXSCQPICLITIDSPDFCLRVAKKVKKYNGNLKTIHYVAPSLWAWRGNRGFKIAKYIDYILTLFPFEPKVLRKYGISGRFVGHPISEIXPNSDKXNKXFRXRIGVGDSERLLVLLPGSRVSEVXRLLPVFLKSIELLDIETSXXKILLXAPKAVVNSVKVLIXASKLNVKXFSEEXNNGSDFELLKKQIFSSADFALAASGTVTLELAAYNIPMVVGYDVNWISRLIIGMLLKIDHIS... | Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
Function: Condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
EC: 2... |
A0Z384 | MSEADDNQPVLSEEEIEALVDHAVTDNVFDDGQFKSHDFGAGEALTLSKWSELDGLLRAHAEVLQGVLLRNFGQQATIEPFAPLFARVGDLIPAMSDRIALITTEIKPLEGESHLEFPGDFLSFLVNQYFGGSTVASPKLAGKVTPSEQRLSEQLAKDVLRTLVEVWSDRLALEPGDLYVDITTDRLSLLPADMGYVVLTYSVACGSDYQGEFRLLLPYESMALQAPRLMPARREEPEVVVEPEWEARLQSAVPEIDVELCGVVSLLETSLRNLLAFKVGTVIPIDEPQTAQLMVEGRGIARGKYGAHDSSRAVQITDFS... | Function: FliM is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation.... |
B5YKC9 | MQTYIDYRKAQKPLNLDNFIVEIGFGSGDFLIALAERNREEIFFGIEKSWIPVNKLLKKCKLREINNIYCTRLDAYWAFQLLFKDKSVKMIIMNYPDPWFKKSHVEKRLTKRENLFIYAKKLIPNGEIKIRTDDYPFVEFTLQESNFLKCFSTSISNPSINEPLTKYEKKWLSMGKSIWDIVLKKEKEPALIEVKKITEVKELFPVKVFNKELNINAISHKEFKIEEGLYLKCFSVWKRNQDYAIEVVLSEKDFLQAFLITAKKKDEYFIIDVSQFSEILKTEGVQKTLNFLANLFVEAL | Pathway: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
EC: 2.1.1.33
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Length: 300
S... |
H2MWL4 | MAPLDLDKYAEIAKVCKYLPENDLKRLCDYVCDLLLEESNVQPVSTPVTVCGDIHGQGDFVDRGYYSLETFTYLLVLKAKWPDRITLLRGNHESRQITQVYGFYDECQTKYGNANAWRYCTKVFDMLTVAALMDEQVLCVHGGLSPDIKTLDQIRTIERNQEIPHKGAFCDLVWSDPEDVDTWAISPRGAGWLFGAKVTNEFVHINNLKLICRAHQLVHEGYKFMFDEKLVTVWSAPNYCYRCGNIASIMVFKDAATREPKLFRAVPDSERVIPPRTTTPYFL | Catalytic Activity: H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate
EC: 3.1.3.16
Subcellular Location: Cytoplasm
Sequence Length: 283
Sequence Mass (Da): 32423
|
A0A2E3VAR1 | MSDSLKKLLTEFKYLEQNSANIKNDSIFLAYPGESNDGRNYIPEAINNGAGAIIYDPLGFEWDKKWKLPNMPIKNLKENISSIASEFYNNPSKKINLIGITGTNGKTSTAFWLTQCLENLERKANIISTIGYGSINQLKPSINTTPDGVKIQSIINYFLLEDVQDVCLEVSSHGIDQGRVTGLDFNVRLFTNLSRDHLDYHDSIESYAEIKKNFLLDAKKGNLVINIDDPLGKKIFQESKLNKSKKISFGIENLATLQAKNLTLEKYKTKFDLIYRRKIYKLEVAVQGVYNIYNILAVIGSLVSLGYQIENIRPILKILD... | PTM: Carboxylation is probably crucial for Mg(2+) binding and, consequently, for the gamma-phosphate positioning of ATP.
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in... |
A0A945L5D3 | MDDVEYDSPIGLLRIEADEQGLTAVRFPGLDTPRSTRPRSRNTRNTHLKSAVRDLESYFANCSNPFRTPLSPQGTEFQKSVWTELGKLSNGTTTTYGKIADRIGNPKASRAVGLANNRNPLPIFLPCHRVIGKSGKLVGYAGEIWRKEWLLKHEGALLVFRS | Function: Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irrever... |
A0A1X7PYH1 | MSKSSTDMRTPLGRVRGMGAAHEGTGHFWAVRLTAIALIPLTFFVIGLLFSMIGADFVQMRATLANPFVCLLLLVTIGSGLYHMWLGMQEIILDYAHSEFWKYGLLILNTFFVFAIGALCAFSLLKIAFGV | Pathway: Carbohydrate metabolism; tricarboxylic acid cycle.
Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH).
Subcellular Location: Membrane
Sequence Length: 131
Sequence Mass (Da): 14451
Location Topology: Multi-pass membrane protein
|
A0A9D6C4Y0 | MRSAALSLRQRLMLQLLVIAAVLAVLLYLTVRTVAGRAAEATQDGILGAATIAIAEQLRGSEAGVSVDIPYSAFSILGSISEDRIFYRIDVAGQTLTGYDDLPLPPKPPQGQAPVYYTSDYKQAEVRISAVSRPVLVANRVEPVLVMVGQTRLGQAAIAAQVAKVAAGLGIGFFAIALVLSLVSARSVLRPIDLLAAAVGRRGPRDLRSVEHPTPKELRPLVVSLNGFIARLRAALSRTETFIAEAAHHIRTPLATVRTQTEIALRQSEDEATRRTLRAVIRAVEESSRSAGQLLDHATVIYRAERLADEALDLAGVVRG... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Cell inner membrane
Sequence Length: 457
Sequence Mass (Da): 48616
Location Topology: Multi-pass membrane protein
|
A0A3M2RGJ5 | MGKGRLEAFSDGVLAIIITIMVLELQVPDGSDMDSLVALLPNFLSYVLSFVYVGIYWNNHHHLLHAAGRPSGAVLWANLNLLF | Catalytic Activity: K(+)(in) = K(+)(out)
Subcellular Location: Membrane
Sequence Length: 83
Sequence Mass (Da): 9137
Location Topology: Multi-pass membrane protein
|
M4S2I4 | MTSPIYVALDTPDIDRAMAIATRIRNHVGGIKLGLEFFCANGRAGVKEMAALDLPIFLDLKLHDIPNTVAKAVQALRPLDPAILTVHAAGGRAMMEDAKAAAPTGTKVVAVTMLTSLDGADMQSIGLPPDPHAQVERLAALARDAGIDGIVCSGNEVAAARAIWPEGFFVVPGVRPADGDAGDQKRVMTPRAALDAGASVLVIGRPITQADDPDRAARAIEATL | Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
Function: Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP).
EC: 4.1.1.23
Catalytic Activity: H(+) + orotidine 5'-phosphate = CO2 + UMP
Sequence Length: 224
Sequence Mass (... |
G1Y0Q9 | MGAAGMEPTLAAARRGATVAFANKEVLVCAGSLMMAEVKRHGATLLPVDSEHSAIFQVFDSERVEGVSRLILTASGGPFRNKTREDMARATVKEAVAHPTWDMGAKISVDSATMMNKGLEVIEAHHLFGMPEDKIDVLVHPQSVVHSLVEYVDGSVLAQLGTPDMRTPIAVALGWPCRIATPGDRLNLVTAGHLEFYAPDPGKFPALRLAREAMRAGGCAACVMNAANEMAVAAFLDGRIGFLDIERIVEHTMTTVPHSRLNSLDDVREVDTVARRVAAEAIQAR | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 1/6.
Function: Catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).
EC: 1.1... |
A0A9E5HJY9 | MSILFKNAQIIDPTADDVTTRDLMVRDGKIVDPSGKAETVIECSGKYLAPGIVDIGVKVCEPGERHKESYKTAGAAAAAGGVTTIVTRPDTDPAIDTPEALEFIRRRAAEVAPVNVLHIAALTKGRAGREMTEIGFLQDAGAVAFSDGYRVVQNTKVLARAMVYAKSLGALIIAHPQEPILSDGGVATSGKFASLRGLPHVSPMAERMGLDRDISMIEMTGAAYHADQITTARALPALERAKKNGLNITAGTSIHHLTLNEFDIADYRSFFKMTPPLRSEDDRIAMVEAVSAGLIDIISSQHTPQDEESKRLPFEAAASG... | Pathway: Lipid metabolism; phospholipid metabolism.
Function: Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
Catalytic Activity: an acyl pho... |
A0A9E4M4D7 | MTKTGHFVTLEGIDGAGKTVQSKLLAERLKAEGIPLVVTREPGGGSGGGPIRDLLTGELTGTYSNETEILLFTADRRNHLDSLIGPALAEGKLVICDRFVDSTRIYQGLGRPQLRRLIDRLHQAVIGLEPDMTFIVDLPVEVAVKRIRTRSGSDRRFEQFGKEISALRDGFRRLADEFPNRCRIVDGTMPPEHLAEELYRMTGSLIS | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
EC: 2.7.4.9
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Length: 207
Sequence Mass (Da): 22898
|
A0A522C9B2 | IRAVVDAVGDRATVVAGVGTYDTRHSVEAARTAEKAGANGLLVVSPYYSRPPQEGLLAHFRTVAEATGLPVMLYDIPVRTGVALAHETLLRLAEHPQIVANKDAKADLFAAQRVMAEADLAYYSGDDALNLPLLACGAIGVVSVTGHVVADRHRALVEAVDAGDLKRAREINASTIPVTVGIMTRTQGAIMVKAALALLGRPVGPVRLPLVDATDEQRAVLAVDLAAGGLALP | 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... |
H0WT42 | MPIPQLLVLFGSQTGTAQDVSERLGREARRRRLTCRVQALDSYPVGLQLKSPRFLFFFYCVTFGEYSFPCTSENFWRFIFRKSLPSTSLCQMDFAVLGLGDSSYAKYNFVAKKLHRRLLQLGGSALLPPCLGDDQHELGPDAAIDPWLRDLWVRVLELYPVPQGLTVIPAGVPLPSKFTLHFLQETPSTCSEEQRVASPDSQGPPSELQPFFAPMVSNRRVTGPLHFQDVRLIEFDITGSGISFVAGDVVLIQPSNSAAHIQQFCQVLGLNPDQSFLLQPRESGVPCPSRLPQPCSIWQLVSQYLDITSVPRRSFFELLA... | Function: NADPH-dependent reductase which is a central component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Transfers electrons from NADPH via its FAD and FMN prosthetic groups to the [2Fe-2S] cluster of CIAPIN1, another key component of the CIA machinery. In turn, this reduced cluster provid... |
W6KCX9 | MKLSWKIFTFTFLIAALTLSLVGAHTVDRIVGILIDHTLSSVQGHAGREAKVLENHFRDAMSDTLLLASTYAARELPATQSEAGRLAIIGEMQATFMTLLREKPAYTQVRLICREGKELVRVNQVGGIIDVVTEDRLQDKSNRYYFKETIDMPPGELFVSAVDLNREEGKIVVPHQPVVRIATPVASTGGTVVGILVINLDLNTLLDEIASPEEGGILVVTNEQGDYLYHPDNSLTFGFEFGHENRLPGEYRLVPQWNRWMQSVDRPAAVKFATDTSIIALQKIFLTGDLAFGPDRTLALGVIVPQAILHGEGDLMQRHF... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 625
Sequence Mass (Da): 68093
Location Topology: Multi-pass membrane protein
|
A0A5C2S3V4 | MSAARPRTPSFLLPRSWSLASHSRQAFSAYAHVRTRTSSRAETNEGVVFRSQGVRPSRRASSSVGGIAAVPTYGYCVMFGGNSALRAKAKEAKCVEVVEATVWELIECPLSGRGGAVEREAFFADLIVVADGCFSNFRSQVMGKAAIQPMLKNHFVALLSYQLGTHDTRVLVDVKNPVPSELKNDRLRRMPNSLLPSSEQGKQTKEGVLLLGDSWNIRHPLTGGDMTVAFNHVVLLRDMLLDVKNLADWSEIKPVLYRWHWARKPLSSTVNILSVALYDLFGAHDPLLEVLRTGCFKYFELSGNCVREPVTLLAAIEQAP... | Function: Catalyzes the stereospecific oxidation of squalene to (S)-2,3-epoxysqualene, and is considered to be a rate-limiting enzyme in steroid biosynthesis.
Catalytic Activity: O2 + reduced [NADPH--hemoprotein reductase] + squalene = (S)-2,3-epoxysqualene + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]
EC: 1.1... |
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