ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
A0A2K5S1M7 | MGAHLVRRYLGDASTEPDPLNLPTFPPDYGFPERKEREMVATQQQMMDAQLRLQLRDYCAHYLIRLLKCKRDNFPNILACKHERHDWEYCEHQDYVMRMKEYERERRLLLRKQRREKKAAAELAKGQGPGEVAPEVSL | Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
... |
A0A1Q9GD17 | MNIKRWFSWTLLTDIRDGMRLTLRYMLSKGVTMQYPDKEKWVPYPRHRGHPYLRKDKQGEIKCVGCELCANICPSECITVIPYEDSQGKRRPKIFELDSRRCMYCGLCEDVCPEEAIALGSHLEYSTLDSNDMVLNKEQLLNLPGKNKEGGMIVPATLKAGAQVVAVPSDSEIEPKEQEAKDQELNTQEPKKQGPETRGPKNQGKDWWQAIHRH | Cofactor: Binds 2 [4Fe-4S] clusters per subunit.
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 (fo... |
A0A501PPD2 | MMRILVLGAGAIGGYFGGLLLHSGADVTFLVRRRRRNLLKKNGLVIHTPDQDYDIAVADHLVEQVDEPYDLVILSCKAYDLEEAIKAITPAVGPDTHVLPLLNGLRHYDVLDETFGAEKILGGLAKNICTMQKDGSIRSWSRPGNVTFGPRSEEQLDFCRQLEELLLRAPISVTHSSHITSALWDKFCLITVLGAINCLLRGSIGDIMATRNGRDIALAIIDECAGTAKAAGYPLSEASLDYLQSSMTREGSDYTSSMFRDMELGKSVEADQLVGDMLIRAEDAGLSTPFLKAAYCTLQTYMLRREKS | Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 2/2.
Function: Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid.
EC: 1.1.1.169
Catalytic Activity: (R)-pantoate + NADP(+) = 2-dehydropantoate + H(+) + NADPH
Sequence Length: 308
Sequen... |
A0A949SWS5 | MAAESRMTAVTIYTDGACSGNPGPGGFGVLLQSGRHQKELAQGYRLTTNNRMELMAVIAALSILTRTCEVTLYSDSRYVVDSIEKGWAKSWRARGWRKADKQPALNADLWSQALDLLGKHKVRLVWVKGHASNPGNNRCDEIAVAASRSAHLLADEGFEIARSSGQASLLPEA | Cofactor: Binds 1 Mg(2+) ion per subunit. May bind a second metal ion at a regulatory site, or after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
EC: 3.1.26.4
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Subcellular Location: Cytoplasm
Sequence... |
A0A7C4TP32 | MTWVVRLDPLRPDKDVICRVADILRGGGLCAFPTETVYGLGADGYNSDAVVKVFNVKRRPMDNPLIIHVDSVRMFEEVSENVPETAYKLIRNVWPGPLTLIVRKSSKVPKEVTAGRSTVAVRCPGHPIALELISTLGRPVAAPSANLAGRPSPTTAEHVIKDLVGLIEVIIDGGETFFGIESTIVDLTTDPPTLLRPGPITVEDLVRILGSDVRVPNFARGFSEAEVALSPGVKYRHYSPNTSLILIEAKDY | Catalytic Activity: ATP + hydrogencarbonate + L-threonine = diphosphate + H2O + L-threonylcarbamoyladenylate
EC: 2.7.7.87
Subcellular Location: Cytoplasm
Sequence Length: 252
Sequence Mass (Da): 27388
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A0A160T1I6 | MQTVESMEPYEQSELYKLRHTTAHVMAQAVLELFPGAKIGIGPPIDDGFYYDFDLGEDDNGRRRTFTAADLERIEKRMRQILAGKHPLRYRVVTADEARELFQDQPYKLEIIEGLLRGEFNEYGDEEEGPAADLVISTYRHDTFEDLCKGPHVAHTGLIPVDAFQLMSSAATYWRGDESRPMLQRIYGTAWFSKKDLKRHLQLLEEAKKRDHRKLGRELEIYIMDEEVGPGLPLWLPNGVILREELEKLAFELEDAGGYQRVATPHIAKEELYLRSGHLPYYTESMYPPMEREDIRYYLKPMNCPFHHKIYASKPRSYRD... | Cofactor: Binds 1 zinc ion per subunit.
Catalytic Activity: ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + H(+) + L-threonyl-tRNA(Thr)
EC: 6.1.1.3
Subcellular Location: Cytoplasm
Sequence Length: 614
Sequence Mass (Da): 70878
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A0A3M7PAT8 | MENFKPKQMVSIDLKTIFGVVRSNKLSLVEQFVAKKGVNILNELDSEGFTPMHWAVYDGSVETVRYLLNNNAIHDSSSNKANQSPLHWACAKGRLEMVSLLVEKGINVNQKDSKGYTPLITASQFGNAAIITYLISLGADLDAEDNNGDNALHWAVYKAHPDVTRLLILFGVNPKTIDKFGQTILHLACLSGNLNIVQQLIEQDFIDSQICDRNGKKAIDLARNRGYSSLVDYLERHEKMRRKKSFESKLKMLLFGPVGNSKCVFLTIQALYIFYEYPIYLFRILPDTWSDHMYLNLFFILNSILMWFFYYSVHLCEPGF... | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 516
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 59551
Location Topology: Multi-pass membrane protein
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A0A1F3IJL7 | MAKPFHIIVVAGGSGKRMNSAMPKQFLKINGIPVIAVTFNRMNAVIPGCRFTVVIAERDLKYWNDCSNYISFHSSINIAFGGPERFHSVRSGLAFVRNDEVVAIHDAVRPLFTGDVIRQGFMVAEKSGSAIPVIPLSESIREINGGLSKSADRSRFRLCQTPQFFQATLLLDAYRQSYTQSFTDDASVVESSGYPIRIIEGNPENIKITTPADLKFAEAILPGLT | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6.
Function: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
EC: 2.7.7.60
Catalytic Ac... |
A0A1Q3RNV3 | MLISIKVQMEAYFTDKANEWVIADQTRLKQVLINLVTNAIKYNKPNGLVKFYVELDEAKVKFHIEDEGIGIPSEHHGSIFNPFYRLNMENNFFVEGTGIGLSVAKEMTELMNGKITLTSELNEGSHFVVTLPRAELNSEPIDYAPNNAKRKIAFNTIKVLYVEDNIANLKLMQRIVENMDGVTLVQTQFGERAVALALNESPDIILLDLNLPDIDGFEVLKRIKKEKELSEIPIIAVTAHAMPEDQAKIKLAGFDSFIPKPIEIERLISELERLTRK | Function: May play the central regulatory role in sporulation. It may be an element of the effector pathway responsible for the activation of sporulation genes in response to nutritional stress. Spo0A may act in concert with spo0H (a sigma factor) to control the expression of some genes that are critical to the sporula... |
A0A178M685 | MRLIERLLPHDTRYDFIRYRLIAFGITALLILGSITSIVVKGFNFGIDFAGGILVEAQSTTGPADLHGMRATLGGLGLGEVSLQEFGTTGRDVMIRVQRQEGDEKVQMAALGKVKEALGEGFSYRRVEIVGPKVGGELVRDGVLAVALSLLAIAVYVWFRFEWQFGVGALISTFHDVITTFGLFSITGMEFNLTTVAAILTIAGYSVNDTVVEYDRVRENLRKYKTMSLYELLNLSINETLARTILTVSTVFVTVLALLMFGGDVLHGFSVAMLWGLIIGTYSSIYVAMPMLVYFNLRTGKDRAEDEAKAEAAAVGEKAP | Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA.
Subcellular Location: Cell membrane
Sequence Length: 320
Sequence Mass (Da): 35000
Location... |
A0A6M6JPZ4 | MPTPEQVVLVDDAGRPVGVAEKATVHGRRTPRHLAFSCYGFDAAGRVLVTRRARGKRAFPLVWTGTCCGHPAPGEDMADAVHRRLEHELGVRAHDLRLVLPDFSYRASDVNGVEEHEFCPVFVCSLDGDPDPRPDEVETWEWWGWERFLDAAAGGELSPWAALQAPLLADTVDPRTRRTG | Cofactor: Binds 1 Mg(2+) ion per subunit. The magnesium ion binds only when substrate is bound.
Pathway: Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from isopentenyl diphosphate: step 1/1.
Function: Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isope... |
A0A3M7PTA3 | MNATNDNKMSNANTWSTVMAAATVRKRKANIAPDHPKRVLFCLDLTNPFRKLCIKFVEWKPFEYLILVSIFLNCVALAVYTPYPNKDNDKINSLLEYVEYFFLTIFTCECVLKIIAYGFVLHQGAYLRNYWNLLDFAIVMIGILSAVTDILDQNSPEKNLSLDLKSLRAVRVIRPLKLVNGVPSLQVVLNSILRAMIPLFHIALLVIFVIIIYAIIGLELFCGIMHSRCEIKYNRGPDHIGSLDASLEEWRPVFSEDIPCISSQKYSSPSKGYVCPQPDNANETIECRSEWEGPWYGIINFDNIGLAMLTVFQCITMEGW... | Function: Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells and are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death.
Subcellular Locat... |
A0A7C5HWR3 | MLLAVDIGNTEIGLGVWEEGWRARFRVRTVVGKTPDEYGALLEGLLAGDSLDRQAVQRAVIGSVVPALTHVFRELLSRWLGRPPLVVGPGVKTGLNLRVDHPSEVGADLVANAVAAYERFRTDCIVVD | Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5.
EC: 2.7.1.33
Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Length: 128
Sequence Mass (Da): 13872
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A0A7C1BUV1 | MSKCGKGNAYLLGSKVVIFDIEFAKCLFSEGFFGKPVGVKKPKTTDINLPIELSLIEALYLCELGILKVFEGDKEVSFNELYERAKKLIPSFERIYPTYKELRERGFIVRSALKYGADFALYRLRPGLEHAPYLVKVLDYNEKLDPGDLIGWGRLSHSVRKDLLLAIVGPDGNRKYIMLKWLKP | Function: Endonuclease that removes tRNA introns. Cleaves pre-tRNA at the 5'- and 3'-splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3' cyclic phosphate and 5'-OH termini. Recognizes a pseudosymmetric substrate in which 2 bulged loops of 3 bases are separated by a s... |
A0A2T3XUM0 | MVSMINKPDQTDLILQDRELAELRLAYLWYNLCDHWKSFLSIVFAVLAIVGLYAILTTPVYHATVLLQVDKKHGTVLGALADVTNPAVDTNGAIDGELDVITSRKIVDEAIRETHLDTRVSVVNYVPLLGRLYARWHRPPRDTLAQPVLGLSDFAWGGERLAIQQFDVPEELYGKGFYLTVGQADHWVLRDQKERVVADGKTGELKHFPIATDYGMKEIEILVTGYLARPGTVFRIVKQSPNDAYAAVLKSMKVGETNKGSSMIRVTFSNADPSVAAAFLNDVANGYVALDIKHLARQATASLKYLQDKLPSLKQALYAS... | Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
Subcellular Location: Cell inner membrane
Sequence Length: 747
Sequence Mass (Da): 82642
Location Topology: Multi-pass membrane protein
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A0A7C6SB16 | MIATYPIIAAIILILDQLTKLIIRMNIQPDEKIYIIGEWFSITFVKNTGAAFSIFSGNKFVTVGMTSILVIACLIFIIYEIKDGGSKFLSICLTFIFAGGVGNLIDRVVMGYVTDMFSFGNFPVFNIADISVTCGCLLTVVYILFLQKRKESEEGTETIAANEDKEKTNNE | Pathway: Protein modification; lipoprotein biosynthesis (signal peptide cleavage).
Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, ... |
A0A8K0WS14 | MRAQIVAIAVSVLAQAASAAVEAKNVIYVIPDGWGPASQTLARDLQGLIESGTNRTNPIIGKLAVDDMVNGLVRTYSANRLITDSAAGGTALATGHKTNNGWVGVTPDRRPVGSILEAAKLAGLGTGLVSTTAITHATPGAYSAHTVDRNNQNLIAEQQLGRVHPLGSVVDVLLGGGRCNFLPQGAEGSCREDDIDLYAYAEELGWSVARNRSEFDEFERGLGAARLPILGNFASGDMRLEIDRREVQDEPSLLEMSQTAVQALHRATHCKDKGYFVMIESAKLDTSGHAGDVPAHAVGTWHFNEVMKWLSEWIDEHPDT... | Cofactor: Binds 1 Mg(2+) ion.
EC: 3.1.3.1
Catalytic Activity: a phosphate monoester + H2O = an alcohol + phosphate
Sequence Length: 486
Sequence Mass (Da): 52871
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A0A938WPH6 | MSTSSNIAIVSYQSPCGKLLLGAFDGRLCLCAWARELHPGRAQASLERRLGVGACEMASPVTTEAALQLDEYFAGNRVAFTVPLMLVGTEFQQEVWRQLMSVPYGHTVSYGCLAQLLGRSGASRAVANANGANPVSIFVPCHRVVGADGSLTGYAGGIDAKRFLLGVEGRANL | 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... |
A0A8B7PPZ1 | MMFTAWDFLRSTERMLLQHLGMKGDTVGGAHKLDAGVAQGRGSSPYLIDNAQLRQRAGAGYTKSSKKPYEALELTSDEREGKKRLQNGENIFLGYTGYVDTDDPSILISVVPENWPPQNAEEEFAARVYLETAVVFKGSKNQQSSIDVSVLIPKGQGTECDWHRDPRRQKQAQFCRRHEGYGTLCRCKDPLDPQRLRRSSNFIHMSESIPIAMLTATKCHFFYRQLMSLLLATGAAQTDILVLIDGHQEETAQLAAIFGLPVIEHRHEGDAGTSTPLNAHFRFSLFTAFSTFRNASKVIILEDDLIVSPDFISYFHQTAW... | Cofactor: The cofactor is mostly bound to the substrate.
Pathway: Protein modification; protein glycosylation.
Function: Initiates complex N-linked carbohydrate formation. Essential for the conversion of high-mannose to hybrid and complex N-glycans.
EC: 2.4.1.101
Subcellular Location: Golgi apparatus membrane
Catalytic... |
A0A3S4DKD3 | MSSLHLISRYAGGADESAPLHKLGGEAWSKARQKAAEKVRDVAAQLLDIYAQRAVKPGFAFKHDREQYREFCQSFPFETTPDQEQAINAVLSDMCQPVAMDRLVCGDVGFGKTEVAMRAAFLAVHNHKQVAVLVPTTLLAQQHYDNFRDRFANWPVRIEVLSRFRSAKEQQQVLDDTREGKVDIIIGTHKLLQSDVHWHDLGLLVVDEEHRFGVRHKERIKAMRANVDILTLTATPIPRTLNMAMSGMRDLSIIATPPARRLAVKTFVRQYDELVVREAILREVLRGGQVYYLYNDVENIEKARNRIAELVPEARVAVGH... | Function: Couples transcription and DNA repair by recognizing RNA polymerase (RNAP) stalled at DNA lesions. Mediates ATP-dependent release of RNAP and its truncated transcript from the DNA, and recruitment of nucleotide excision repair machinery to the damaged site.
EC: 3.6.4.-
Subcellular Location: Cytoplasm
Sequence ... |
A0A178MCT9 | MMGTTLAMDVDIAGITADSRAVAPGFLFAALLGTKADGRDFVPAALKAGASAVLAPEGSDLDLPPGVAQITDANPRRRFAQLAAAFHGDQPKSVVAVTGTNGKTSTAVFYGRLMEELGHHAAAIGTLGILARGWDNRGGLTTPDPAALHDALARLAHLGVSHACIEASSHGLDQYRLDGVRLTAAAFTNLTRDHLDYHGDMESYGRAKLRLFTELLPPGAVAVINMDSPEAPRFAEAAAAHGLKVLGYGRNGAELRLVESSPRPFGQELRLEVLGRAVTVALPLAGDFQAMNALAALGLALASGADAEAATAALERLDGV... | 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... |
A0A7R9IHP2 | MKQFWTPGELRYESLSKAKMKQVLITLWNVPEGSRPGILVEHVKNLFMVYKMHELRVSQKQRLKEWETEMNYISSDSAKIYVENEADLEGPPRNFTYINHYIAGDNVTIPKSPPFGCLCEPECTIGSFCCGKLWNSRSAYGRDQRLLAELGTPIYECNKLCRCPPNCRNRVVQNGRVIDLAVFRTKNGCGWGLKAMQVIGKGAFVCEYTGEVITNKEADKRFNYAFTGDKTYLFGLSYNSKTNYPYSVDGSLFGNITRFINHSCDPNIVVYPVWVDCLDPNIPRLAFFARRMIRRGEELTIDYMCQLKEEEEIISETFLS... | Catalytic Activity: L-lysyl(9)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(9)-[histone H3] + 3 S-adenosyl-L-homocysteine
EC: 2.1.1.355
Subcellular Location: Nucleus
Sequence Length: 354
Sequence Mass (Da): 40563
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A0A1F3J3P4 | MRRNRSRFLNRQRPLVIWFTGLSGSGKTTLSDSLNTAILQKGYFTKVFDGDVIRTGLCSDLGFTDADRHENIRRTAEVAKMFSDSGLIVLCSFISPTHEIRDLARKIIGEDRFVEVFVNCPIEICELRDVKGLYKKYRLGLVKNMTGFDSPYEPPTHPTVEIRTDLWDINKSTRYLIRQVLKQVKYRKEK | Pathway: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 2/3.
Function: Catalyzes the synthesis of activated sulfate.
EC: 2.7.1.25
Catalytic Activity: adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate + ADP + H(+)
Sequence Length: 190
Sequence Mass (Da): 22009
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A0A2H0KRB7 | MAIKGKKIWLDGGMYDWDKVFIHPVNQSLHYGLGAFEGLRFYLHHEMVAPVIFRLRDHTERLFNAVKVLGLEIPYSRDEVSRAIIETVKANKCPEGYIRPLVFLGGATRNFGDLVLVENSEMGFAKVSQVHLMIAVWPWGTYLGSEALEKGIRLATVAVPRPHLSHAKICGNYPATLMTKQLAMKNGYDEGLQLCDGLVAEASAANIFIVKNKRLITPPLSLSILPGITRDTIMTLVIDLWVHAIGVVEERSFGISELYAADECFLCGTAVEITPVREVDNRTIGLGKAGLTTKKLQEIYFKIVHGESRQYAGWLTEVR | Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 4/4.
Function: Acts on leucine, isoleucine and valine.
EC: 2.6.1.42
Catalytic Activity: 2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate + L-glutamate
Sequence Length: 319
Sequence Mass (Da): 35567
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A0A2T2QYR0 | MIRIVMILAIDWGKKRMGCARADARARLPEPFGSFVHDDDIFQQIRSTVKAQQVGIIVVGLPRNMSGEETRQSREVRRFVAELKNQLQCPIVLQDETLTSHYTGELRQRFPHADTDSLAATLILGDYLQSI | Function: Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 131
Sequence Mass (Da): 14866
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A0A2H6K2A9 | MGGGGNVLSSDRMKNAPEWIAVGRIGRPHGTGGEVLVRSLTDRNERFSRGSEMFISQPGDGTKRPVKVASARKSAKGPLIRLEGYTTRERARELNGRMLFISASELALPEDGSYYGFQLEGCSLYAGERRVGVVVRLAESRANAYLEVKPEEGGDDFAIPFVREVILSVNLERQRIEIPENFME | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but ... |
A0A0R1UST1 | MGAYLLWLVILVLADQGLKWWTVVHLQLGQTKTIIPQVLALTNVHNDGAAWSSFAGMQGPLITVGIIVLVIGTYYLIKHVKTKPVHCVAVVLIMAGAIGNLIDRVMQGYVVDMFMTKFINFPIFNIADICLTVGTILLIILILRED | Pathway: Protein modification; lipoprotein biosynthesis (signal peptide cleavage).
Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, ... |
A0A5C6M5N0 | MVETNIGQFILELGCEELPAGQIINISNHIKNEIIAKLNLAKISFGDFISHYTPRRLYFQIDNLLLDPIDQTEILKGPPEKISRNPDGDLSQAGLGFAKKNNLETSDLYFEDGYLCAKKTLKGQSAKSILETSIPEIVSSTPGVRFMRWADGETKFARPIQWILAVIVSTKSPKQILDFSIEGLSASDISYGHRFLGNGAITVSEPKKFIEDLRAQGVILDLEDRKKIIMDSANKLADSVSGVVVFDENLLTELCLITENPAPILCSFDTKFLAIPDCVLKTVMIHHQRYLPIETEYIDSSSSDVTKRRLTPYFIAVSNN... | Catalytic Activity: ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl-tRNA(Gly)
EC: 6.1.1.14
Subcellular Location: Cytoplasm
Sequence Length: 742
Sequence Mass (Da): 83070
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A0A1R4A8Z3 | MDEILPHYTEIIDGNLFWDGTNILEVAKDYGTPFIIYSENILRGNYRKIKNAFNKYFKNVSIDFAIKSNFNPSLISILSSEGCGMDASSVNEIKIALLSGVSPDNISFTPNNVTIEELKFAIDKNITINFDSLSQFRMVLDHLPEIVSFRIKIDYGKGEFPGIKTAGKGAKFGEIPELALQGYREAKEKGCRRFGIHVMAGSNVRNADHFKLVAQKILEVVKNFEEELGIEFEFVDMGGGFGVPYRPEEGELDVMDTAKNIADVFKAFYTEKGREIPRLVIEPGRYISSNSGLLVGKITDVKRQESNFTGTDIGMNILMR... | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; L-lysine from DL-2,6-diaminopimelate: step 1/1.
Function: Specifically catalyzes the decarboxylation of meso-diaminopimelate (meso-DAP) to L-lysine.
EC: 4.1.1.20
Catalytic Activity: H(+) + meso-2,6-diaminoheptanedioate = CO2 + L-lysine
Sequence Le... |
A0A0B4IKD9 | MYILFSSSLFLMILTILVMSLASLLSKKSITDQEKASPFECGFDPKSSSRIPFSLQFFLIAVIFLIFDVEIALLLPLICILQFSTMLYWYWVSSIFMLILLLGLYHEWNQGSLNWATN | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity of complex I.
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NA... |
A0A3B9QPM6 | MTLANGLTLLRGLLIAPVVVAVLADRPWIALFFFILAALTDAVDGLVARSRHEVTFVGAMLDPAMDKLLYMALFSALAAVGGLPPLGPVLYAIPQLGLGIGTLVLWRRRREFGARWPGKTAAALTALAAVCLLVAPWGRLPFWAAIAANFLSALYYLILQANRRTRGEGGQRAPSTSPGGGAESPGARRGA | Pathway: Phospholipid metabolism.
Subcellular Location: Membrane
Sequence Length: 191
Sequence Mass (Da): 20130
Location Topology: Multi-pass membrane protein
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A0A1G2HH24 | MKKGFKALTAFIKRKRKLISIIVTIVSIFVFLLWLNNNAKTTNSSQEPELSSFEILRESDPGLADIYEIVARQDVELVVIDELRNTIQVYPVPSEDDTIFTSERPIIFIYPDAVEDELFNRLVFESGVEQKLEFKNNGGGSTNIWMWIIIFGIFFLTIRWVIKKRRTMSDGNGSGNNANNGGTTKSIAQEIKPENIETRFSDVAGIDEILVEIKEIEDFLKNPAKYKDQGARLPKGVLLYGPPGTGKTLIARALAGETGATFFSANGSEFVEIFVGSGAARIRDLFKRARKKIPSIIFIDEIDGVGSHRTQGVGSGGDTE... | Cofactor: Binds 1 zinc ion per subunit.
Function: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
EC: 3.4.24.-
Subcellular Location: Cell membrane
Sequence Length: 653
Sequence Mass (Da): 72891
Locat... |
S0G6J1 | MTARQRQIVSSGSFVISRKQPLVLDAYLGSCVGVALWDPVAEVGGFQHLLLPEPIDGGTPWQPEKYAKTGLPLFIQALCNQGANKTRLKATVAGGGLIGPVSPLDLDLDIGGRTAEIVCNLLEKEKIPVIEREIGGFFGCKMSMDLSSGETGISPLLNPGDFKTSAGLLPPTPAQLQETIQKIKPIPQVVLKLLRMLHDDKDSLKDMAKQVRQDQVISARVIQLCNNVFFSLKMKADSIDRALVLLGEKQFLQLVLSATMKDVFCDETHGYSLCKGGLYTHSVGMAMACEKMAQRISRQISPSVAYTAGLLHDIGKVVLD... | 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: 446
Sequence Mass (Da): 49299
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S0FZM6 | MGFDLTPVQVEQMACHAAQLEKWNQHVNLTAIKGPAPLAHKHFLDAVAIQPYIRGNSGRWMDMGTGGGFPGLPVKLLNPGIRMVLVDASRKKIHFLKHVIRMLKLDGIDAIHGRVDDLHHDPWFVGRFDGILSRGVADLDRLAGLAAPLLAKEGILYALKSPGAREEITDALDEKFFIQWDDYELPDGKETRSLVRLTLKQKSS | Function: Specifically methylates the N7 position of a guanine in 16S rRNA.
EC: 2.1.1.-
Subcellular Location: Cytoplasm
Sequence Length: 204
Sequence Mass (Da): 22703
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A0A260ZDQ5 | MEVIFEESAADCTAGHLKAIDGTFVIKDAVLLEFKIKGEVAGKIKTPCDGVVSFGKGLKPGVALSKGQVIATMSECQHDIVIKDMCGDCGKDLREKGGRAGQRKEQATANVSMIHHVPELIVSDSLAKKIGSADETNLITTRKLVLLVDLDQTIIHTSDKPMSADAEKHKDITKYNLHSRVYTTKLRPHTTEFLNKMAAMYEMHIVTYGQRQYAHRIAQILDPDARLFGQRILSRDELFSAQHKTRNLKALFPCGDNLVVIIDDRADVWQYSEALIQIKPYRFFKEVGDINAPKDSKEQMPVQIEDDAHEDRVLEEIERV... | Function: This promotes the activity of RNA polymerase II.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
EC: 3.1.3.16
Subcellular Location: Nucleus
Sequence Length: 494
Sequence Mass (Da): 56342
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A0A1W1V938 | MIIGIGTDIIEIDRMKEALQTNLRLSERLFTSGELDYCQQKCNSFESFAARFAAKEAMTKALGTGFRNYNWTDIEVVKDDLGKPSINLKGNALMKAEELGVTHIHLSLSHGKDYATAMVVLEGS | Function: Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
Catalytic Activity: apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-[ACP]
EC: 2.7.8.7
Subcellular Location: Cytoplasm
Sequence Length: 124
Sequence Mass (Da): 13744
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U1QE58 | MPTGGSQKPTTGGGQPDSGSETADHPREKCGVVGVALEDRAAARPLYHSLYALQHRGQESAGIVTHDGFQQHTHVDMGLVGDVFGPGDLESLAGSVGVGHVRYPTAGSINNCCAQPFSVSFKSGSLGLSHNGNLVNADELRAELAANGHAFTSDGDTEVIAHELARNLLDGDLVRAVRQTMDRIHGSYSLAIGYDDTVLGVRDPKGNRPLCIGELEDGYILASESAAVDTLGGELIRDVQPGELVVLESDGSGYETYQLVEPENTAHCFFEHVYFARPDSVIDEQLVYEVRRRLGRHLWAEAGIESDVVMPVPDSGRAFA... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2.
EC: 2.4.2.14
Sequence Length: 405
Sequence Mass (Da): 43263
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A0A1I4G3I6 | MKNLDLFDVLDDTTPTQKAETEKEREKKPESPPPTPPASSEGGNDNDDGSFDLAEYTHQVYLRYAISVVKGRALPSVSDGEKPVQRRILYAMHRLGLTQGSKPVKSARVVGDVIGKYHPHGDSASYEAMVRMTQDFILRYPLVDGQGNFGSRDGDSPAAMRYTEVRLTKFAELLLSEVDAGTVDFRPNYDGSEQEPVDLPARLPLLLLNGASGIAVGMATECLPHNIREVGNAAIALMRNPSISVDDVLQHIQGPDFPGGGQLISSTKDIREAYATGRGIFRVRARWAIEQQARGQWRMVVHELPPGVSVKKVLEEIGEY... | Function: Topoisomerase IV is essential for chromosome segregation. It relaxes supercoiled DNA. Performs the decatenation events required during the replication of a circular DNA molecule.
Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA.
EC: 5.6.2.2
Subcellular Location: Cell me... |
A0A7R9ICK7 | MQISSTWAGVSQGLAAIFGIIGSVSFPFLRQRIGLKLVGMVGLGSEQELTEVRVCFPVEIASILACIISIWLPGSLFMAVAIDPTWKPNVENGTKNSDDSSEEKASVMALLGGIVLSRFGLWLADITITQIMQEEIEENKRGVLNGVQDSLNMGMDMLKSILVMVYSYPAQFGYCIILSFISICAGFVCYSIYYFKEKPNTANQEQKNEDGKVSTENETEAENSHVTKVHIAQPPQNAS | Function: May be involved in iron transport and iron homeostasis.
Subcellular Location: Membrane
Sequence Length: 239
Sequence Mass (Da): 26157
Location Topology: Multi-pass membrane protein
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A0A0P1AJ29 | MLAKRNLAAQLYVRGFSARVLSTVVKNEVQKFNAAASDWWTPKSRTGVGPLHQINPVRVKYIRSHVIMHFGHTNDDDPMPLRGLRVADVGCGGGILSESLCRIGGTMVSIDPGKENIAAATEHAATSCHTNKIEYRQCTSDDLVKQGEIFDVVCSLEVIEHVSSVPAFLQSLTPLVKPGGLLFLSSINRTVLSAALAIGAAEYMLRIIPPGTHDWNKFVQPSEIEHELRKDGIIVKDISAVNYIMCAVKPSIK | Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Function: O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway.
Catalytic Activity: 3,4-dihydroxy-5-all-trans-polyprenylbenzoate + S-adenosyl-L-methionine = 3-methoxy,4-hydroxy-5-all-trans-polyprenylbenzoate + H(+) +... |
A0A5B7RBD6 | MTRAAGTPPGTVRVASVGGVPVLVSASCLVVVALLAVAFAPRAEDVVPGLGTWAYATGALVGVLVYVAALVHECAHAAVARRYGHRVSSVALSVTGGRTSVEGEARTPGEEFTTAVVGPLASLALGLAALGGRLVVDDGVLALALEALVVANLVLGLLDLVPAPPLDGGRMVKALAWRIVGSPRRGALAAAWGGRVTAVLLLLAPALRQPLLGTPPGLSDFLVCGALALLLWTVATQEIAVNRMRLRLGDVVLADLARPALTVPPDLPLAEALRRAAEIDAGGIVTVDATGRPLGLVPDAGVESTPAERRPWVATAALAE... | Cofactor: Binds 1 zinc ion per subunit.
Subcellular Location: Membrane
Sequence Length: 382
Sequence Mass (Da): 38638
Location Topology: Multi-pass membrane protein
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A0A117KJI7 | MSLIMITGGARSGKSEFAEKLALEKEETASFI | 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... |
A0A117LP45 | MYLYDAAATREADRRAMTETGVPGLVLMENAARSAANHIFSFYGKPSRVVIACGSGNNGADGMALARHLLLYDMEPVIILAAEPDKLSDFATRQFTIIKKLGINVELSREMTDENLHKIFDTSDLIVDGLLGTGAKGAPRGETQRIIFFLNAAKKPVLALDVPSGVDSSTGSVSTVAVKATSTVTFLAAKTGLFVMPGRFFSGQVVTGHIGIPHWSVLPTETDTFVPDDKTAFSLLPKRNSFTHKGQRGAVIIFGGSRLYQGAPFLAARGALRAGAGIVVVVTPEEDILPAFGALPESIIFRAPSQKGFLLPEAYDAAMK... | Cofactor: Binds 1 potassium ion per subunit.
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... |
J0IH33 | MAKPNPEELFNLGMLSYDKQDFSKARKYFEKACDLNNGGGCGALGDLYDDVEKNLIKAAQLYSKACDLNISRGCGALAVLYINGQGVEKDLTKADQYFSKACKLGDQEACEALKEK | Function: Hydrolyzes 6-aminopenicillinic acid and 7-aminocephalosporanic acid (ACA) derivatives.
Catalytic Activity: a beta-lactam + H2O = a substituted beta-amino acid
EC: 3.5.2.6
Subcellular Location: Secreted
Sequence Length: 116
Sequence Mass (Da): 12700
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A0A8B7P9Z5 | MKTIVCATFFFFGLISVGLAVKCYECNSHEMPECKDMSSKALQSLVDCDSKTNDTHVYTLCRKLHMFMDEQVGENLKENRIHRACGYVEDEDMYKRGNCYYKSGYNTRTWVCSCKDDECNAASTTLVSLAGLVSLLVVARLM | Function: Required for homeostatic regulation of sleep under normal conditions and after sleep deprivation. Important regulator of the Sh K(+) channel, acting as a signaling molecule that connects sleep drive to lowered membrane excitability, possibly by enhancing K(+) channel activity and thus reducing neuronal excita... |
A7SF52 | MAVEMCFLGKGFRCLVLFLFILQLFTPIFSIKRKLNLQEYLCPPKIQECKDKNISLVYVSAESADHDNVVHFVWSGFQGPSIINAYSEKLPEKHAKPGLNVKWENLFKNDTEGALEFTPKVDYITAFSLSSVLQFADPKDEIYFTKTGGVIEHNLRSVQWRKVILDKDNDNATFVGEFLGGTISFSCAAADHDDRDEEPPRPRYSSNSTRFTVNLSHLKTNSTDRLALEFVSVVKSEESMPSCSREFQSIDDEHSPGIFRTVVINNTYATYSSFISWKPVMYTKLDRGLKTQLPAFNYLYKNGKFEQTKISSKHCFHLTE... | Function: Required to protect lysosomal transporter MFSD1 from lysosomal proteolysis and for MFSD1 lysosomal localization.
Subcellular Location: Lysosome membrane
Sequence Length: 425
Sequence Mass (Da): 48008
Location Topology: Single-pass type I membrane protein
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A7SRZ7 | MSDRTIVENFRDREGYRCGYCGSTDSNYSHGMWAHQLTCQDYQDLIDRGFRRSGKYCYKPDLNKMCCPCYPIRCEALHFRATKSQKKVLKRMTKYLTVPQAEGGRTIPCLLQQGNYHVPLQKTRPCIVKMLRMTGKVLTFITVCNYDECKCQITLDYGEMCGLREKSQITRFSTITPGKGPDPSKPPCRKAKDIRRQRRQQKKKNGVEEYRRFLCSSPLVVSAPHMGYGSFHQQYWLDGRIIAVGVLDILPSCISSVYLFYDPAYSHLSLGVYSALRETITLHTLCAQRRIAGFPLSSVGLNSTPTNTRDWIRLGRVIYP... | Function: Involved in the post-translational conjugation of arginine to the N-terminal aspartate or glutamate of a protein. This arginylation is required for degradation of the protein via the ubiquitin pathway.
EC: 2.3.2.8
Catalytic Activity: an N-terminal L-alpha-aminoacyl-[protein] + L-arginyl-tRNA(Arg) = H(+) + N-t... |
D7CU50 | MLGDMTFFERLAARIQETDSRVCLGIDPRPEAHPLTHPDRFAGDPAQVAKAAVYYFQAILEATAPLVACAKLQAAFFEVLGIPGLIAMAQLIADLKARGVPVIVDAKRGDIGSTAEAYARAYLGDGVFGADALTVNPYLGGDGLAPFAEQAARAGRGVFVLVRTSNPRAAELQDLELRGGQRLYERVAESVAALAEGCRGGARYAPVGAVVGGTAPEALAALRARLPHVWFLVPGYGAQGGRPEGVAGAFDAEGLGAVVSSSRALTYCSDGADFAERAREAAAEMRRAINRALGGR | Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
EC: 4.1.1.23
Catalytic Activity: H(+) + orotidine 5'-phosphate = CO2 + UMP
Sequence Length: 296
Sequence Mass (Da): 30881
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A0A101GIF2 | MELGRARSLAVTLLEGAGIESADLEADLLLVWATGFQRGYIHAHPEKILSEEQLKTFFEATERRCGREPLQHITKEAGFFGLSLLIEPGALVPRPETEIAVEAALESFRGGLFVDWGTGSGCIAAAILENAPRSFCVAVERSPSAIRVAWRNFKKLGQISRVLLWHGSDPWQVPLKAHSASLLVSNPPYIPDPVIPLLMPEVRIHDPLSALSGGSDGLDAYRILLPWAWHVLETGGTLVLETGGKEQCERVKALGAFGFRCEKTLCDFSGIARVLVLKKE | Function: Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif.
EC: 2.1.1.297
Catalytic Activity: L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release... |
A0A961NE84 | KIDKAEAHVDWAKPARAVLRHIHGLSPFPGAWAEVQLDGETVRLKLLRCALADGHGAPGDLLDDRLTIACGDGAVRITELQRAGKGAMKAADFLRGTPLRPPLRFT | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
EC: 2.1.2.9
Catalytic Acti... |
A0A0P6WW09 | MLLCIDIGNTNIKFGLFAGDQMCCHWRIATDRNRLADEYAVLLLNLLATSGLGVADVKGVAVSSVVPALTQVFEEIARRYLHQEALMIADGVDLGMRINTEYPKEVGTDLIVNALAARHLYGAPVIVVGFGTATTFSAVSKEGNFEGVAIAPGILTSSDSLFRATATLPQVALAHPVAAIGKNTLQSMRSGIVFGFAELVDGMVRRIRRELGGQARVVATGGLAELIAPESQTIEMVEPNLALIGLRLLYERNRLA | Cofactor: A monovalent cation. Ammonium or potassium.
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5.
Function: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
EC: 2.7.1.33
Subcellular Location: Cytoplasm
Catalytic Activity: (R)-pant... |
A0A3P1Y4H9 | MDFMQVLIYPSVLMGSLGLIFGVLLALASIVFFVKPDLRVQLIREALPGANCAGCGYPGCDGYAEGVVADGAKTNLCSVGGAPVAERIAEIMGVKAEKSVPMHAFLKCRGTPERSPRNAVYSGIQDCRSAAILPGGSPNACPFGCMGFGTCVKVCVFGALSIVDGLATVDTSKCVGCGTCVATCPKSVLTLVPRGENVAVACNSHWKGPTVKKVCSVGCIGCGLCSKVCPAGAITMDRDVAVIDPEKCVNCGTCIAKCPAKCIESVPAC | Cofactor: Binds 3 [4Fe-4S] clusters.
Function: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
EC: 7.-.-.-
Subcellular Location: Cell membrane
Sequence Length: 269
Sequence Mass (Da): 27539
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A0A2I0R1U8 | MKVNKDGNGYTFAFSIILVIVVGVILSSLSIGLDPLKKANVAVKKKMNILSALGVESTRQDGSDKYDEFIKDSYVISHNGVLQEDLPEEKKAFNLDVQKQFRDKTIEVSDRLYPIFEAEKDGATIFVLPVVGKGLWGPIWGFVALADDYETIVGTSFDHKGETPGLGAEIAQDFFENRYNGEKIADNGQFTPIKVVQNGTGSEEQKVDGITGGTITSKGVEKMVNKTMRVYYKYFSKNK | Function: NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol.
Catalytic Activity: a ubiquinone + H... |
A0A0E9NIZ7 | MNLILLLPEDLSPDSTTATLIDSRRCNHIHTVLHPSPGFTIQVGLLNDKICTATVLSCSPKVVELRLPSRDDSAAWRNPPKKLPFTLVLALPRPKVLDRVVLAAASLGVKSLILIPAWRVEKSYWGSPKTQPARLREQVLLGLEQACDTVEMTIEKVERFAPWVRSWTDKPQGRRFFAHVEGGRECPYNILSANSDGDNLTQEDEGEGVVAVIGPEGGWVPSEVDALTEAGFDCVGLGPRILRTETAVACLEWERSFDQRAVVLLAVCINGMVDACGRPSENACPLTLYFPFKLGNAMPTECVGLAGGLVVRHSLSWN | Function: Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit.
Catalytic Activity: S-adenosyl-L-methionine + uridine(1498) in 16S rRNA = H(+) + N(3)-methyluridine(1498) in 16S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.193
S... |
A0A124FR71 | MRAERKEPIIAPSLLSADPLFLGEAVGSLENETNWLHLDIMDGHFVPNLSYGPALVRSLREACGEAFLDVHLMVEKPELLVRRFAEAGADYLTVHVEATPHLHRVLGMIKDEGKKPGVTLNPGTPTEWLKPVLHMVDIVLVMSVNPGFGGQAFIPETLEKVESLFRWREARGLSYLIEIDGGLGLDTVERAVLAGCDVIVAGSAIFGAKDPADMVRALRRRALEAIRS | Cofactor: Binds 1 divalent metal cation per subunit.
Pathway: Carbohydrate degradation.
Function: Catalyzes the reversible epimerization of D-ribulose 5-phosphate to D-xylulose 5-phosphate.
EC: 5.1.3.1
Catalytic Activity: D-ribulose 5-phosphate = D-xylulose 5-phosphate
Sequence Length: 228
Sequence Mass (Da): 24980
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A0A2K5PPW8 | MFCTCIPFFFRRTFLKSTEYKCLMSTVVLFIVQCRILLRISEIDLQILSKVQAQYPGVCINNEVVEPSAEQIAKYKELVAKTSNLKNIKFAWHKETSSEYQSRILEKKELQKWDFIHMIQMLYYVKDVPATLTFFHSLLGTSAKMLIILVSGSSGWAKLWEKYGSRLPRDDLCLYITSSDLTQMLDNLGLKYECYDLLSTMDISDCFIDGNENGDLLWDFLTETCNFNATAPPDLKAEIAKDLQEPEFSAKKEGKVLFNNSLSFIVIEA | Function: Inactivates histamine by N-methylation. Plays an important role in degrading histamine and in regulating the airway response to histamine.
EC: 2.1.1.8
Catalytic Activity: histamine + S-adenosyl-L-methionine = H(+) + N(tau)-methylhistamine + S-adenosyl-L-homocysteine
Sequence Length: 269
Sequence Mass (Da): 30... |
A1WN04 | MHQAPAPPAEPASYEAALHELEQLVARIESGQLPLDQMLAGYQRGASLLSFCRQRLDAVQEQIKVLDDGPLQPWVQQ | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
EC: 3.1.11.6
Subcellular... |
A0A447J960 | MLTIADTIFTSHLFTGTGKYTSSRVMQEAIAASGSQLVTMAMKRIDLSQGHDDILAPLRELGIKLLPNTSGANNAREAVFAAQLGAGGARHQLDQTGDPPRCPLSAAGPG | Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
Function: Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is provided by the thiocarboxylate moiety of the carrier protein ThiS. In vitro, sulfur can be provided by H(2)S.
... |
A0A1G2HH22 | MHDPVLLKTILSNFSPSPGNNFIDCTAGEGGHTIPLAKAVAPNGKVLAIDADSEQIANLKSNLEKEKIENVVSAHGNFKNLKQITAENSFPPADGILFDFGFSSWHIENSGRGFSFQKNEILDMRYDPTDKSIPTAADYLNSASAQDLEKIILEFGEERFAHNIAREILYARRKKTIETTQDLVNIVLEATHSRGKINPATKTFQALRMVVNNELEIIKYGLFAALDVLKPKGLIATITFHSLEDRLVKGILKEWAKQNIGEVVNKKVIKPDYIEIKRNRRSRSAKLRIFRIL | Function: Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(4)-methylcytidine(1402) in 16S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.199
Subcellular Location: Cytoplasm
Sequence Length: 293
Seque... |
A0A1G2HHZ8 | MRPIILLDSGVGGFSVYKPAKELLPNEDFIYIADKKYFPYGDQPAKIVQERVFSIAQWAIENKAKMFVLACNTATVTAVKKLRKKYSSIPVIGMVPVIKTCVEQTKNGKIGVICTPRTARSAYQKELITRFANDKNVYIRSCPGLVESIESIKGHAVDNLSELQKALLYLKNKNIDTLALGCSHFPLVKDNIQNLAGENVLILDSGGAVSRHIKRVLKNNKDLYKSNHKGRTQFYTTAKPSEFDIMIKRYLNLKSRSKLLRV | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Provides the (R)-glutamate required for cell wall biosynthesis.
EC: 5.1.1.3
Catalytic Activity: L-glutamate = D-glutamate
Sequence Length: 262
Sequence Mass (Da): 29467
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A0A1W1VBU3 | MNRIDQTFKKLASQNKKALIPYVSVGDPNLEFTERLVLKLAEEGADLIELGIPYSDPVADGPTIQKASARALSGGVTLEKIFSLILRLREKTQIPLIIMSYFNPIYVKGMENFTKKASASGIDGIIIPDLPVEEAGIFNELAKEQGIYLINLIAPTSNKRIKKIVQNSKGFIYCVSSLGVTGARAGNFNNLETFLQNIRAETDLPLAVGFGVSTSEQAKNIAQYAEGVIIGSALINQIEKNIDQNYFNQEKALSDASSFIRDLKGAMSI | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5.
Function: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
EC: 4.2.1.20
Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-s... |
A0A7V5GXW6 | MSHAWRCRCVSSPMISFWRSGSRVRSVRIAEREVGQATVLGYGRTGRAVAEYLHEHGVKTFVSDSSCLSDADRNSLMNLRIAFEDGGHTQRAIEGADVIVPSPGIDPTAAIMQLARVRGIPIISELDLAYLRSGDTRIIAVTGTNGKSTTVRLIEGILRGEGIDAIAAGNIGLPFITLADDPPDVVVLEVSSFQLEQSNLFHPQVACLLNISPDHLDRHGSMEEYVAVKMSIFARQAANDTAILPRGIDPSKSTIAARIARFDDVGLPENPFVESLPPHNRSNLRAAIACCRGILPDLKADDIDLPSLEGAFHLPYRMQE... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
Catalytic Activity: ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-... |
A0A6A0GZQ2 | MCYECSSWTDPRCSDPFNFTLPRAKQPPTEECDGCCVKLVQHIGTREFNKIPLENLIISLHGISADI | Function: Required for homeostatic regulation of sleep under normal conditions and after sleep deprivation. Important regulator of the Sh K(+) channel, acting as a signaling molecule that connects sleep drive to lowered membrane excitability, possibly by enhancing K(+) channel activity and thus reducing neuronal excita... |
A0A950TC81 | MDDVRTPVQRIERLTPLAHVLTAIDRQVTPIAPTQVDPASARGRVLAHDIDADQRPPVALALRDGYALRSEETADAGSYASAPLSLAVRVEVGEPVPRGADAVAPLDAVADDGTTPQAVAPIAPGEGVLLPGQDCDGAQPVLQAGCVLRSLDLAVLSGLGVSRVPVRIPALRIVQTRRNDDVAHAISAMLADLVGCHASAELSPDGAEAALQDPQDADGVIVVGGSGAGTNDHSVRALAGAGRVVAHGIGLSPGETSAFGFIEHTPVLVIPGRLDAALAVWHVLGARIMARLSGCTDTPAVRHAKLARKIASTIGLVEFV... | 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: 369
Sequence Mass (Da):... |
A0A672UM23 | MTPALGWGVTLGLALGAVGWGLLVASLPHSVWGMAGGQATAVASVAITRGLWNDCATDASGVTSCVPLVSLITLPGYLQGSRLLAVLAALLGVPGLALGGGSGARRSARAAGGALLLLAGLCSLAAAGWFAAATSQEFFDPQHNGVRFEPGPGVLLAGGGGAMAAVGGAVVMAAARGPPRSRSAPPPAASLGDKYVRNAYV | Function: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity.
Subcellular Location: Cell junction
Sequence Length: 201
Sequence Mass (Da): 19581
Location Topology: Multi-pass membrane protein
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K9SG07 | MTDISTQPDRSANASNHMPNDHEWLEIGKIVAAQGIKGQLRVLSDSDFPERFTKPGQRWLRRSPQSTPEPIELKNGRAIPGKTNMYIITLVGVENRDQAEALRGSLLLVAAGDRPKLAEGEFHIDDLIGCEVFLQATGALIGKVQSLFVAGNDLLEVKAIASSKTVLVPLVEAIVPVVDTKAKRIEITPPDGLIDELLERKV | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but ... |
A0A5S3YTS2 | MVSKSRIEALSDAIFGLALTFLVVKMEIPKSYAEFENMSHGFIGFFITFLMLFIIWNNQARLLSSIDKVDAPLKALLACFLFTILFFVFPLKYMFTLALETFFPFYQSAIKMEETLTLSQISQLIHIFSSTLMAIFGLLMLMNIYIYKNREKLILTVSKISIKREIFTDLAIVLIALLSHIMVYLLSANLLYLTGMVYLLILPSRWLLGKRYKEESALPLNSST | Catalytic Activity: K(+)(in) = K(+)(out)
Subcellular Location: Membrane
Sequence Length: 224
Sequence Mass (Da): 25749
Location Topology: Multi-pass membrane protein
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A0A662EYS1 | MHDLFHSLDQHLCNPIDRFIAALNRRLYNDISVREEMRVPPERLPEPPFHPVPLHRRPPLPRDDDPDPLLLPLQDMERKTRTLPHRAFPIDRLKVPSVFQAHRGRETAITAAGHTRTIARSRVHFKVSAVDFPSPSEPATLRMTMDERVYTVSELNRKSRELLEGAFNPIWVKGEISELKRAASGHLYFTLKDESAELSGVKFRSRIPGIPEAVLEPGTVVIAYGKLTVYEPRGRYQLVASLIQPIGEGALQAAFERLKRRLQEEGLFDKAHKKPLPRFPERIGVITSPDGAAIRDIHSVLSRRWPLARIFLFPATVQGE... | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
EC: 3.1.11.6
Subcellular... |
A0A9E1C8T2 | MVRAVSAKNFRSFALNTLFAGVGGATFYAANPPIACWPLSFFSLALLFLISLHARPKSAFLFGWIWGAFYFYLLFDWAEIAASLLAARLALAAIEALFIGLCTSLWALLYRRLLPLNFSAPPWQKLLLLAGGDSLLWVVTEQLRSAVPYGGMPWGNTAFIFVDAPLLHLAPWGSIQLVSFTAVFIGILLGYALKQLREKQIFRSGRAAVGAVLLLVLPLLVPSGAVATQNLRIGIVQGNVPDVAKLAPGESRALIVTENHLQATYLIADQNPDLVLWPESASDRNFRRDYAAGKMVEKAVAAIAPAPLLLGTQNYFSNVR... | Pathway: Protein modification; lipoprotein biosynthesis (N-acyl transfer).
Function: Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation.
Catalytic Activity: a glycerophospholipid + N-terminal S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipopr... |
A0A1J0I0U6 | LSANLAHAGASVDLTIFSLHLAGISSILGAINFITTIINMKPPAISQYQTPLFVWALLITAALLRLSLPVLAAGITMLLTDRNLNT | 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... |
A0A9C8DGR3 | MPGLRDQPERASRPYLPGEERRPRATAGFPKVTEGAITLGFDPGLATTGYGVVQACDHGWVVIDGGVITTPHGTSRPERLHDIYNEARELINRYHPRGVAIEEIFFATNARTAMLTAETRGVLLIATHGLPVRGYTPLQVKKRITGYGKAKKQQVQAMVKELLGLAETPRPDDMADGLALALCYLFDLQGVNKEEHDYL | Cofactor: Binds 2 Mg(2+) ion per subunit.
Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair. Endonuclease that resolves HJ intermediates. Cleaves cruciform DNA by making single-stranded nicks across the HJ at symmetrical positions within the homologous... |
A0A8K0WS64 | MSKRSADAMPSASKKRKTDKGPKFYAVRCGWQPGVYDSYDKCSTQTTGFKGAIFKSFTSRKDAEDFVAGKKVETPSDEPTRYYAVAVGRSTGIFTDWAEAEPHIKGASKPKYKKFNSYAEAVEFIKENGDRDAVEALGETFDPSPPPPPPALALPVQVEAPSKRARVSRGGKAEPGTVPRSDILQVWTDGSSRANGRKDASAGIGVYFGPNDPRNLAERLEGEAQTNQRAELTAMLRAMEMVPNEQSMMIWSDSRYSINCVNTWAETWETKEWKTATGGEVKNKDIIVKIRAKVKERGKAGAVTLLEWVKGHGMNVGNNA... | Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
EC: 3.1.26.4
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Length: 358
Sequence Mass (Da): 39050
|
A0A346KN56 | MLTFIYMIMFFIILSTLILLINLFISSKSLSNREKISPFECGFDPLSNSRLPFSIQFFLISLIFLIFDIEITLLIPLIYMLYFMNKIIIFSSLLFIFILISGLIIEYLEKSIDWKTN | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity of complex I.
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NA... |
E0UP52 | MISQDSIEALKARLDIVDVVGNYIELKKAGGNFKAPCPFHDEKSPSFVVSPQKQIYHCFGCGAGGDSVKFVMEYEKLNYPEALEKLADSYNFTLTYTDNKHNKPRSQVMDKLNEWYQMLLSKNQTALNYIKERGIYESSIEKFGIGYAPESQATLNYIRSQQFSIKEAIDMGVVGYNQERNQTYARFVERITFPIFSANGSIVGFGGRTITGHQAKYVNSPETAFFNKSRLLYAYHLAKQSLHKKQEIIITEGYLDVIMLHQAGFDNAVATLGTALTHEHLPLLRKGSPRVVMAYDGDKAGRAAALKASKLLSASGFNGG... | Cofactor: Binds 1 zinc ion per monomer.
Function: RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.
EC: 2.7.7.101
Catalytic Activity: ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.
Sequence Length: 556
Domain: Contains an N-termi... |
A0A6A3BQ10 | MVYTHSVPPEVTSASEPARRKRGRPRKHAAAVAPAVGPWRSWVFEEVSVGCIRWGRFKIILLSGSYVRNEIGRITGGLGVCQVIGGVGGPLKAAGPVQVIAGTFTIDNEKDVSAGAKGDASGGKLPSPAGGLGGSRFMMQRRGMHMAPRSTDWRISLDDVELTGKTDQTPQNEDYGRHVRLPFGVRRGRAAPDALTVVENGAAWSMEMGLWKSWSFVQ | Function: Transcription factor that specifically binds AT-rich DNA sequences related to the nuclear matrix attachment regions (MARs).
Subcellular Location: Nucleus
Sequence Length: 218
Domain: The PPC domain mediates interactions between AHL proteins.
Sequence Mass (Da): 23439
|
W6KFH1 | MPRNFVVCSLPSDNDTRTNLVYLNPADHETEVGDAEFVIISAFPFSVRPNPKVQRGFIAFNSIQRRLLNLSVTAGTTVSIAHVPQKQPEILEITLCVDHIVLSKRNGTLDCREFSDFCKARFMGQCFRQTQQLAVVLDSGMRLLATVANLKLDSTGEKSEIGYLGALTSIIVTATERSGIALTNISDGQLDAQQHQIIQNFNLESLGIGGLKSEFGQVFRRAFASRIFPPSYIKKLGIKHVKGVLLHGPPGTGKTLIARKIGEILNCHEPKIVNGPEVFNKFVGGTEENVRNLFAEAEAEQAAKGDQSRLHLIIFDEFDA... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Required for vesicle-mediated transport. Catalyzes the fusion of transport vesicles within the Golgi cisternae. Is also required for transport from the endoplasmic reticulum to the Golgi stack. Seems to function as a fusion protein required for the delivery of cargo p... |
A0A8B7NKQ2 | MDSRARIRAAHEQHVTGHAGCQWYEVLLALYPVFPATIFLATLAPSTHDHRLLQGRTVLEVLVVVVPIVAAQTFANDLLVALAVFLSLAAAVAYTFSTSPAKNVVVETSGRDGVTLVRSIVGLSTAVAILAVDFHVFPRRFAKTEEFGWSLMDVGAAGFLLINALVDMRPNAVRSVRTVLRETCVLLALGCARLLSLPAIDYQQHASEYGVHCNFFFVLAFTKIICGPWCWSVSAAGAAAAACCCTALQHCCTALLQDWVFSSQLRDSLVSGNREAVVGATGYVALYCWGAALGKVVLRQKSGGTAYEHSARSLARGCAV... | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Function: Probable acetyltransferase, which acetylates the inositol ring of phosphatidylinositol during biosynthesis of GPI-anchor.
EC: 2.3.-.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 448
Sequence Mass (Da)... |
W6KWT2 | MVPFLLALAFILGTIYHVNKAISRFQCYRARINYDYDAIIVGGSIAGPAIAKALSDQGRKVLLVERKLFTKPDRIVGELLQPGGIGALKVLGMEQCATSIGMPCKGYVVTDTSGRQLELSFRRGIQGVSFHFGDFVQNLREFIYKNCREHITMVEGTVNTILTEGHTCYERAYGVEYTVVEDYHEPENPFRVDPPKPGKVSYLTKTATAPLIVMCDGGASMWRARYQHYTPVADYHSNFTGIILKNATLPIEQNGTIFSSKSATILCYRLDPNEVRVLVITKYARLPRLTKFCEWLLEEVAPSLPEGMRKEFIHAVSETS... | Function: Catalyzes the stereospecific oxidation of squalene to (S)-2,3-epoxysqualene, and is considered to be a rate-limiting enzyme in steroid biosynthesis.
EC: 1.14.14.17
Catalytic Activity: O2 + reduced [NADPH--hemoprotein reductase] + squalene = (S)-2,3-epoxysqualene + H(+) + H2O + oxidized [NADPH--hemoprotein red... |
A0A6A3B7N0 | MDVKLKERKHNRSSLRVGFIHPNLKKDGIGIENFLKGKVILITGATVFLAKVLIEKILRSVPDVSKIYLIIRGKDMEDARQRLKYIVDIELFHCLKQKHGEHYEAFMWSKLVTVIGDVAHPTLGIPEDLAVEIAKHVQIIVKVAADTAFDQSKMILRYDVALQVNAMGPCNLLNFAIKCKILSSSCIHHQALLKDIQEKEDLWRKRDVLVRKIAWETVCVLSETTVLENEMKLASDYKKLLKPNDVLLIYESQNISALIVRPSGILSTYKKPFPGWIEGIKYLLLDPVIVYYGKGKLTGFPLNPNCSFDIVNSRRHSCEY... | 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: 495
Sequence Mass (Da): 56725
|
A0A6A2XWV2 | MHVKLKGHDLYKYTPSPGSIDEQEQLDNENNPRSLQAGFIHPKPKKDGIGIENFLKGKVILITGSTGFLAKVLVEKILRSMPDVSKIYLMIRGKDMEDARQRLRKEIVDIELFKCVKQKHGKHYEAFMCSKLVPVVGDVGLPTLGIQEDLAVEIAKDVQIIVNIAGDATFDQRYDVALQVNAMGPCNLLNFASKCKNIELFVHTSTNSVKRYSREGRFMEEKECFSPRDSMGRQVCVLSETAVLENEMSMRSKTSVPIVIVRPSGILSTYKEPFPGWIEGIKMADPIIIYYGKGKLTGFPLNPNNSIDFIPADIVVNTML... | 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: 395
Sequence Mass (Da): 44568
|
A0A6A2Z627 | MATSEVKDLGTWGSPFVRRPRIALNIKCVKHEYIKEKKLFEAKSELLLRSNPVHKRAADYFTDEIMFSDRDLKPTREFQSSSMEIMSQSANLSLSYNTSTRLGLPWCPAMKSIVTHGEEVEEAAVAQLKEGLTLMEEAFGKQREGFLWAIEMLNGMKLLDESNTPALVNWADRFCSHAAVKNVMPHTHKLAKLAKMVLRKVFLSKI | 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: 206
Sequence Mass (Da): 23431
|
A0A1I6LG00 | MEIFEKIKKIINENFTIEGKLTEETNITEGLGLDSFDFVTLVTTLEEEFNIEIAEEEMYQIKTLEDAVQIIQKKL | PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine of apo-ACP by AcpS. This modification is essential for activity because fatty acids are bound in thioester linkage to the sulfhydryl of the prosthetic group.
Pathway: Lipid metabolism; fatty acid biosynthesis.
Function: Carrier of the growing fatty... |
A0A498IG01 | MGAEKLNFADMQPFEPVLEGEENPPSHGSDSVVKTQHRFASVVYQKPEAALGDQQPGSATRMTIFYGGQVLVFNDLQAEKAKEIMGLATTGSSKIFAGFVKKLGFENQSNVVAENNSQEIKAPQYRRPSTE | Function: Repressor of jasmonate responses.
Subcellular Location: Nucleus
Sequence Length: 131
Domain: The jas domain is required for interaction with COI1.
Sequence Mass (Da): 14323
|
A0A498HFG4 | MLDSIVEVLARKVLNKHVHIQVGGKSVVNKDITQFVEVRSKMGLAVSILKCHCARLCATSSTTWEEKNWCLPKDMQHVTLCLGVYLRMDSSLSFHGNKDQTDRESTTSDFKTNVCNLLIATSLASRGLDVKGVELVINFDTPDHYEDYVHRIARKARKDWKALKKAQAKDYGFEDDKSDSEDEDDGVRKAGGDISQQAALAQISATAAASKGVLGGVTLPGTAVVPGVLVGHKGAA | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 236
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): 25612
|
R7XXB1 | MLKRLVAISATLACLSLAACGNEGGESATDPTTEETTSETTSETPAETESAAGACEYVEGGSPAVREVELPPSEPTVSGEVKVVFQTTLGDIPATLDADATPCTVNSFVSLAEQGFFDDSPCPRMATAPSFGILQCGDPSGSGSGGPGYSYADELTGEETYEAGTLAMANAGPDTNGSQFFFVFNDSPGLTPDYNVFGSVDPAGLKLLTKAAKKGDDGSHPAGGGVPNAGPIDITGVTIG | 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: 240
Sequence Mass (Da): 24146
|
A0A498HBW4 | MEVVQFLIQITLFLWSLSSAIPAVASQPSLAKPNCPAHCGNDTISIPYPFGIGADCFMNAWFEITCDNSTYNSPRRPIPRLNHPSLKQLEVLELSMNGTLSVRNPITFFGDCGTNRTLAEQAPNLTGSPFVFSKRNWLFSVGCGGIALMKLMNGSSVGGCLSICGDKGDILEQLNEPDNCNGINCCQTTIPGNLTNFNTSFQEVKGLLNASDTTSGSGSCKYAFLADEAFGMVTGLDYIHLVGVPGVLEWNWSQYTESEIFGTASTTFRDANSGTVCASNNSCSCGNGLEGNPYVVDGCQEIDECKHRFWSFKCLSRANV... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Subcellular Location: Membrane
Sequence Length: 590
Sequence Mass (Da): 65132
Location Topology: Single-pass type I membrane protein
|
A0A6A2XVD8 | MQQVILEAKGTFDNQLKIQKLKDTIFAVNEQLTKAKKQGAFSSLIAAKSIPKSLHCLAMRLIEERISHPDKYTDEEKPIPREFEDPNLYHYAIFLDNVLAASVVVMFKLKDYNGAHIEVKAVEDYKFLNSSCVPVLGQLESANLQKFYFENTLENATKDTTNVKFRNPKYLSILNHLRFYLPEMYPKLHRILFLDDDIVVQKDLTGLWKIDMDGKVNGAVETCFGSFHRLVSDLFHVYAQYMNFSHPLIKQKFNPKACAWVYGMNFFDLDAWREKCPEEYHYWQNLNENRTLWKLGTLPPGLITFYSTTKPLDKSWHVLG... | Pathway: Glycan metabolism; pectin biosynthesis.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 372
Sequence Mass (Da): 43290
Location Topology: Single-pass type II membrane protein
|
G0WDB6 | MISNDDDDYMDYITSTKYEGQLDDLLMEITQMSEQFLHEQERKVDSTLNEITQSVETMKQDNNTLIETQSSGAGTGTDTAMMMIDIKDFPSNIEKFNKLLELLKMVHLDQDSLDYFLRYTVLSNDGSKNKPLSLKSIDDPQFVSLEREVDNLQNNEIAQQLNEINGTKLKIFKINDTIFQSNNELNELSLNLGNEIDECWDLLNEFNDLKDKKLNSTTKNGVKTSRENDPVNDTYNEFKKLNDQNVKLTKLNDEMNLVQKSVARFKNKTHKYDDKDKDTNGNDEIDKEKQTLEVLNGLIKLFENTFMKISSNLNNLKISP... | Function: Involved in kinetochore-microtubule binding and the spindle assembly checkpoint.
Subcellular Location: Cytoplasm
Sequence Length: 409
Sequence Mass (Da): 47557
Location Topology: Peripheral membrane protein
|
A0A0E9NIY9 | MTTLVQYDSSSDDDANERDPAVEPAAVSTLPSLPSTFHNLYATKPRVGDDPAFHQGRKRAHRHVEGQWATHIYTEFWPDVKLMSILDRIVKKAGSLDKGWTSLLVSELGNQLALHISLSRPLTLWTDEREDFTRALSRVLADIEPFEMTLDNISTFVNDERTRTFLVLEVNEGISEFGGVLRALEAVMKQFKQPALYTVDTARFHVSIAWRLGGEEMKVKQLLQFVEEFGEELQALWKDTSKTIRVKEVKAKIGNQIWVKKLGELNLPHLRRTRSSSIAAADIILKFNGSPDRNILAFGMYNLASLKLRLRYRLQLLFHG... | Function: Phosphodiesterase responsible for the U6 snRNA 3' end processing. Acts as an exoribonuclease (RNase) responsible for trimming the poly(U) tract of the last nucleotides in the pre-U6 snRNA molecule, leading to the formation of mature U6 snRNA.
EC: 3.1.4.-
Subcellular Location: Membrane
Sequence Length: 909
Seq... |
A0A3B9QLZ9 | MRVPLVLLGCGRVGQALLEEAASLDLQFLGVLDSTGGVVDGGGIPQGRLSQLLSRKREGVALGELGVPGEGATSALLALLRERRGLLVDVTAADTRPFLFSALEAGWGVVLANKLPLVGPWEDFRRLSSVGYEATVGAGIPLITTLKALLGSGDEVHLIQGGLSGTLGFLLAEVERGEAFSQAVRRAMARGYTEPHPAEDLSGADLARKGLILARTLGLPLELEEVELEPLASPAGRGLPVEGFLQGLRAQDAELRRRLEGAKRRGLTLRYVVEVSSAGVRAGLREVDRKSPLARAQGVENVVVINTRRFKGHPLVLAGP... | Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 3/3.
EC: 1.1.1.3
Catalytic Activity: L-homoserine + NAD(+) = H(+) + L-aspartate 4-semialdehyde + NADH
Sequence Length: 344
Sequence Mass (Da): 36181
|
A0A238F5K2 | MMHPWSLPDDTVPIIMVVGSINDDEFFEVPHIVNTGETIASTRYTRRLGGKGANQAVAAARAGGSVSFYGHIHCDDTARIRQALKLDRIDVSHLTGQRNFATGRALIQLSTTTKDNSIILFPGANHASSTFSPYFPGSLVPNAAQQRRQERIRVHGPRPTPHGSTKYCLLQNEIPLSRTIGAAQWAETESRTTKVMFNPSPMLTTLQIKENEEALMEHVHWWIFNEGEAKALLEALQDGEDEAVGVAVESGDVLGGLGRCFQRKKGATTGVVMTLGAEGVESLVLVEGVWERLKVGPGKVGAGGVRDTTGAGDCFTGYFA... | 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 ... |
Q68QF6 | MTRRRCKEWCTAQLWMRKLGSDTPSHHRGSLSAPLRNSTDPCRPPMRRRRSTAPSMRRLWGIYGSRSGLLILIDSSRYCTTVGSAVSDFQSPKQGPLCTVEDILTDYKRDVLLNVLLPSATKMLLDALRVNRVAGNLKTTGCRRYTVPPAHSTTGVPDADFVIYLSAVPANGLAGFGGLCQMDIVGRPVAGMINIAPRVIHIGMEIQKVIRLIVHEILHALGFSSPFLSIGKKNRRGYKVNYIKSESVVARAREHLNCSTLKGPETENKDRTSHWKQRNHMDDIMSPRVNKWMYLSAVTLAVMEDTGHYAIDWSRAETPK... | Cofactor: Binds 1 zinc ion per subunit.
EC: 3.4.24.-
Catalytic Activity: Preference for hydrophobic residues at P1 and P1' and basic residues at P2' and P3'. A model nonapeptide is cleaved at -Ala-Tyr-|-Leu-Lys-Lys-.
Sequence Length: 471
Sequence Mass (Da): 52941
|
A0A3M7SRB0 | MQIKANEALDSVSKIETTTGAGQDELVQRTISKDIHIDYDNGPIGKGRFGTVWKAKWNGDDIAVKVFFSMHESSWSRETDIFQTNLFHHEHILRYITSDIMGLGCTVNMIILTEYHPLGSLFDYLQNNTLNINILSNFLYSIASGLNHLHLEIFSTNYKPCVIHRDLKTKNILVKNNLECCIADFGLAVKFDSLTNRIYGLEDFSLRQGSVRYMSPECLNETLNLRSQECLKKSDVYSFSLVMWECLSRLRVKDIEPEGHRPPFYEYIAGDPEIESMKHLVCAQMIRPRINFLENTSDQRLQQIIDIMQECWSSNPAERL... | Catalytic Activity: ATP + L-threonyl-[receptor-protein] = ADP + H(+) + O-phospho-L-threonyl-[receptor-protein]
EC: 2.7.11.30
Subcellular Location: Membrane
Sequence Length: 336
Sequence Mass (Da): 38785
Location Topology: Single-pass type I membrane protein
|
A0A6A3B7F0 | MRIWKLSCEIEVRTFEFVGTCNVAERLLSEDLEINDWLCTYDPSDIYVIGPMCKCKLFENWSALDSLQEAVHLNAGNVLGAEDNRPIPKWEMIIRRTLNKSLEPESKHKCYSAPPSPVLRTSSVADVVADEIDALPLQMRCNQHLETAKVLSISTRFDFTPVENSVFCSPHPPALTDSRLKISHHSSGNLESMLLHELPNLEVDDSFSEVSDEFLVSPIGIGLMGYMGNKLHNELGRGHVFDGWKEGVINFPLTYKYEINSDRCVGKIPREGEKKKRYPAWFDRILRSGKGIKQLCYQRAELRLDHCPLSSTFWRCYELN... | Cofactor: Binds 2 calcium ions per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/... |
W6KUW4 | MKKYYAVAKGYQRGIYATWAECYKQVHGYSGARFKGFKTLEEAKIFFEESSGSTCCNNSRGSEHHNISESSCNENDMCDAKSHDKRSCSCKHSFPLPHDSNVVDNCSDSQPSAKYPRLYDSESRTRLQIAVQGDELPSMLLDGHLVATQEVYVDGACHGNGLRGFSRAGYGGYYGEGDCRNFALPLSSNEKHTNNRAELRAVIHTLHQGVHDAGGSVASLMANEVDYSTPVPLYRLRVYTDSKYVVEGLTNYSKKWVKNNFTLSNGKTPVQNQDLWKELTLLRDGYNTCFSYQHDARPHRYISSNTFNSGEGFEIRHVRG... | Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
EC: 3.1.26.4
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Length: 348
Sequence Mass (Da): 39029
|
A0A6A2X8F8 | MVFKYKKDERLIEGSECSVCLNEFQEDESPRLLPKCSHGFHLAYIDTWLRSHQNCPLCRAPVVSDTMVAQTSASEPSFISSGSSNKIMVETDVGEGRTCGIEDGNTSENCRKNLGHSDGNVLSDLDGIQATRRSVSFDLTAAKHKHGSSLDTELEQLEYSKGKIHSSRCKVMRSCPSGGCLSKGAVSMKRFFSSGGIFLLSKPNRTQGSILPL | Pathway: Protein modification; protein ubiquitination.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
EC: 2.3.2.27
Subcellular Location: Membrane
Sequence Length: ... |
A0A6A3BF00 | MASASLLKPSPVVDKSEWVKGQTLRQPSVSVVRYHPVAPSGLNVRASSYADELVKTAKTIASPGRGILAMDESNATCLDGLASRSAAYYQQGARFAKWRTVVSVPNGPSELAVKEAAWGLARYAAVSQDNGLVPIVEPEILLDGDHGIDRTFEVA | Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4.
EC: 4.1.2.13
Catalytic Activity: beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate
Sequence Length: 155
Sequence Mass (Da): 16494
|
A0A498JBB1 | MSSILWFSAVRNESGVAVCASKNANNQPLTGVVFEPFEEVNKELDLVPTLPQVSLALQKFIDESKATINEHINVKYNVSYIYHAMFAYFDRENVARKGFFKESIEEERDHAKKLMEYQNKHGGRVKLQLILMPVSEFDHPKKGDALYESRKKEEKKQKAWLPTNAQQPKLQVD | Function: Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Has ferroxidase activity. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation.
EC: 1.16.3.1
Catalytic Activity: 4 Fe(2+) + 4 H(+) + O2 = 4 Fe(3+) + 2 H2O
Sequence Length: 173
Sequen... |
A0A291I6R6 | WGLGNWVVPLMHGAPEMPIYRLNELSMWVLIPSLYGLIMSSIMDQGAGTGCSVYPPLSNNMFHKGYSADMAIFSLLLAGISSILGAINNNSTILNIRTCMYNKEIMPLFVWSVMITAFFILMSLPVLAGAITMLLTDRNLNTSFFDPAGGGD | 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... |
A0A1S9CJX7 | MVIGYQGVPGSYSEQALIQLFGLVHPTKYYKEFEDVFIGLEIDEIKYGILPIENSTTGSITQNYDLLRKYGYYITAETGVKIEHNLLVIPETKMEEIEQIFSHPQGFEQSTIFLKQFFPNVKQTAYHNTAISAEYVKNQNIKTFAAIASKRAAQLYGLDILESNIQNNKENWTKFIVVSKVAESDPSCDKMTLLFEIRHEIGSLHQILAEFAKFDINMSKIESRPVGNGTFSYFFYIDIQGNKESLNIKDAFKNIKKLTQNFKVLGYYKKTV | Pathway: Amino-acid biosynthesis; L-phenylalanine biosynthesis; phenylpyruvate from prephenate: step 1/1.
EC: 4.2.1.51
Catalytic Activity: H(+) + prephenate = 3-phenylpyruvate + CO2 + H2O
Sequence Length: 272
Sequence Mass (Da): 31198
|
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