ids
stringlengths 6
10
| seqs
stringlengths 16
1.02k
| texts
stringlengths 117
4.4k
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E0VXB6 | MEPDNLPYRAEYAKSGRASCKGCKENIAKESLRLAVMVQSPFFDGKQPNWYHFSCFFKKFRPKDSSSIAHFESIRWDDQEAIKNKIGKTTKSKKRNKPSPSNIPDLGDYKVEYAKSKRAKCKVCEETINKDEIRISKKDYEGEIALKYGPVDRWHHVDCFVKAREELEFFSSGEVLPGFKTLTEEDQNLLKTKIPELNNHSSKDGPSPPKKLKEDVNDEFKKKLKKQNDLIFKYHDLLKPLKKPELQLLLEFNNQEIPEGPTRMIERLTDGMAFGALKKCEKCKGQLNFTSGKGYTCTGYSNEWLKCEAVNTKPSRVPFKVPNELKEKYTFLNKFKGKVLERLFNESPKKDEPLSSDENLSKTPLKTFKFFIHKTHEKNSDKIKKLISELGGEITKKFEKDLTAVISTSNELKNMKNSKTLNSAQKAEIPVVSDKFFDDINSCTSKKEFVQKINENKISPWNFDPSKITIVEEDDKIVVTKKSVYPAKESRVNKSKMFKSNESVKKVTVKDGLAVDPDSKLEQIAHVYRKGNDIYNFVLSLVDVQSDKNSYYKMQILESDKKKKYWVFRAWGRIGTTIGGNKCEEYETLEDCIDLFKETFEEQTGNKWEKRKKFKKVPGKKIMLDIEHYNEEKEKDKLKPKLDSKTLSKSVQNLITLIFDIEAMKRTMLEFELDLNKMPLGKLSQKQIRKAFEILTTLQNLIKKNSERSHYIEKTNMFYSLVPHDFGIGSPPLLDNNEIIKQKIEMLNSLLDIEIAYRLLQECEGSGNSIDDHYGKLNAEIIDLDPETDEYKTIEIYVKNTHAKTHTNYSLEIENVFKIERKGESERYEKNSKMSNRKLLWHGSRITNFAGILSQGLRIAPPEAPVTGYMFGKGIYFADMVSKSANYCNTSKKNCTGLLLLCEVALGKMLELTQAKNIVKLPSGKNSVKGVGRTQPDPTEVIISPTGVEVPVGKGVDADVKDSALLYNEYIVYDVSQVKIQYLLRMKFNYKI | Catalytic Activity: L-aspartyl-[protein] + NAD(+) = 4-O-(ADP-D-ribosyl)-L-aspartyl-[protein] + nicotinamide
EC: 2.4.2.30
Subcellular Location: Nucleus
Sequence Length: 992
Sequence Mass (Da): 114027
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A0A8T2HUL5 | MAALSKHTPTIQSTPSALAILPLARPFCGTQSLPASATGRSTLVANPPPLRARGRALQELLDGKDEEKEEAEDPGLPAVTTLSWESPLTILKYPDPRLRAPNAPVGCFDDSLRQLAEEMFVVMYDDDGVGLAAPQVGANVRLMVFNETGDKEKREAEVVLVNPRIISTSKDGKVFEEGCLSFPNLYGDVIRPSKVRVRAQDLSGKSFVINISGFPARIFQHEYDHLQGTLFCDRMVPEALAETRKELVKMEEEFIAANPGVEVQRIPNV | Function: Removes the formyl group from the N-terminal Met of newly synthesized proteins.
Catalytic Activity: H2O + N-terminal N-formyl-L-methionyl-[peptide] = formate + N-terminal L-methionyl-[peptide]
EC: 3.5.1.88
Subcellular Location: Plastid
Sequence Length: 269
Sequence Mass (Da): 29482
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A0A662CLW0 | MFRTWSMMIRPQRVEFDQESLTSRYGKLVVEPLEKGFGITLGNSLRRVLLSSIPGAAVTAVKIEGVPHEFTAIPGVKEDVTEIILNIKELQLKSYTEEPVTMYLDVQGPGEVKASQIDTGHKVDILNPDLVIATLDSEKSRLIMEMKVERGKGYLPVEKRHGEDLPIGTILVDAIFSPVVKVNFSVENARVGRETDYDKLILEVWTNGAVHPQDAVAMAAKILKDHVTIFANFEQEMEEMDEEGGEREKEELVKRLNKSIDELELSVRSHNCLKKMGINTIRDLVQRSEADLLKVRNFGKKSLEEVKSVLEEMHLSLGMDLKGLEEEEEEIG | Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
EC: 2.7.7.6
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Length: 332
Domain: The N-terminal domain is essential for RNAP assembly and basal transcription, whereas the C-terminal domain is involved in interaction with transcriptional regulators and with upstream promoter elements.
Sequence Mass (Da): 37397
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A0A0C9PI02 | MMASSKDDNSESVQFFEGVEKLLEIWFTSTDGQDRKRDLRDIPRHKWESLLKIVRCEIISFCRNDQVDAYVLSESSMFVAKRRLILKTCGTTTPLQCLETLLDLVEEYTGFDEVEDLFYSRKNYKRPELQNSPHRAFEDEVALLDTIFQDGEAYCLGDVDNDCWYLYVLNREHSASSPPEPDQTLEVLMTNLDPSIMSIFTRDVCSSASEATKKSGIDKLIPTMRIDDFLFEPCGYSMNGVSKSGNYMTIHITPEPEFSYVSFESNIPEASYTEVINRVLNTFKPDKFVVTIFANKESIAANSPRELEETDYLNVHGEWLRNDVQYCRFKNYDLTCAFYSKFPS | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Pathway: Amine and polyamine biosynthesis; S-adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine: step 1/1.
EC: 4.1.1.50
Catalytic Activity: H(+) + S-adenosyl-L-methionine = CO2 + S-adenosyl 3-(methylsulfanyl)propylamine
Sequence Length: 344
Sequence Mass (Da): 39714
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A0A963IFA9 | MLASLALRSAVAPRLLPPALESHSMRPDPTPPAAARTPPRPSHTSRRLAALAQLTLVVAAHALALHLLVRPDTVTPPAPQTAIEVTLITLPAPTPLAPPEPVPAAPQAPAPPPPRPVVAPAPPPKPVLKQRTPRPKPAPPPLAKSSTAPVPAETPDTPPEPAVEAPDTAPETPATATPMEVAAAPAPAAAPPAECSDAGYLYKPDPPYPRLANRMNQQGTSLIQADVASDGAVDNVRLHRSSGYPRLDNAALKAVAGWRFNPARCGNTAKASQVIVPVEFKLEKP | Function: Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates. It could act to transduce energy from the cytoplasmic membrane to specific energy-requiring processes in the outer membrane, resulting in the release into the periplasm of ligands bound by these outer membrane proteins.
Subcellular Location: Cell inner membrane
Sequence Length: 285
Sequence Mass (Da): 29537
Location Topology: Single-pass membrane protein
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A0A379JJS5 | MNIEVPTLVLGAIAAAFALFSLALAALIGPKRYNRAKLEPYECGIEPTPHAIAGGPGNAAGQRFPVKYYLTAMLFIIFDIEIVFLYPWAVHFDSLGLFGLAAMALFIFNVSVAYAYEWRRGGLSWD | 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 a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
EC: 7.1.1.-
Subcellular Location: Cell membrane
Sequence Length: 126
Sequence Mass (Da): 13832
Location Topology: Multi-pass membrane protein
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R1DWP8 | MLTEATLTIGPSFSIEAEGRGRICSCPVWLALWLVVLTAPFYRWFTKAQPALSAPAFAVGVGLYVAASLMLVLATNIEPGTVPRNALWTPPSEDLIGQPLTRSRSQNVRRMSGGVSVLRGVEMRHKFCTTCGVERPIRAVHCRITDRCVEKWDHYCWYMGMTVGRRNHPPYWSFLALALLMTVYYFATGVLALRRLSHDARPESGALVAALAYDPLSCALLLFAAVMGAVLLHLVCLHAHNISVNLTTYEKFRRPFTKEWSDGSRERNPFNLGFARNWTEAFLPLCLPPPECMLAPRQAPAEDETDDSDAALRTCPTSSTSL | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 322
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 35761
Location Topology: Multi-pass membrane protein
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A0A402CYQ7 | MTAFRSPLSLHPYSDPHERIMARALRLASRGRHASPNPMVGCVLISPDGAVVGAGFHPRAGEPHAEVWALRSAAPGAARGATAYVTLEPCSHCGRTPPCSLALVEAGVSSVVIAMLDPDTRVSGRGVEILRNAGIDVTLGVLEREARELSAAYIKHRTTGLPWFVLKTAASLDGKIATRSGDSQWITSPPARRAVHRQLRDRCDAIVTGLGTVIADDPSLTTRLGARSGRNPWRIVVDSRGRTPLESRVVRQASVDGRTMIATTEQCPSEHRELFERAGCHILICSQDVEGRVSLPDLAARLGTRGDMIGVLIETGGQLAASALNSGIVDRWTAFLAPKVIGGDAAPGPIGGLGAAQMSDAQKLSTWKLRRCGPDIVIDARIW | Cofactor: Binds 1 zinc ion.
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 2/4.
Function: Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5'-phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)-pyrimidinedione 5'-phosphate.
Catalytic Activity: 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)-pyrimidine + H(+) + H2O = 5-amino-6-(5-phospho-D-ribosylamino)uracil + NH4(+)
Sequence Length: 383
Sequence Mass (Da): 40745
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A0A1S9Y1Z3 | MRKKRVLPGFGLSLGFTMLYMSLFVLIPLSIVFIQTSQLGWKKFAGVITSERVLHSYQVSFTTSLAAAIVNAIFGLLIAWVLVRYTFPGKRLLDGLIDLPFALPTAVAGITLTTLYAENGFIGKIFSVFHIKVAFTQLGIIVALTFIGLPFVVRMVQPVLQSIDKEVEEAASSLGASRFQIFVKIILPEIFPALLAGFSLAFARALGEYGSVVFIAGNMPMKTEIAPLMIMTKLEQYDYAGATAVAAVMLIISLLFLLFINMIQTWSRRHELKSE | Function: Part of the ABC transporter complex (TC 3.A.1.6.1) involved in sulfate/thiosulfate import.
Subcellular Location: Cell membrane
Sequence Length: 275
Sequence Mass (Da): 30309
Location Topology: Multi-pass membrane protein
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M4T0Q4 | MRSTLLFTTIYIVLKVGISSAQKVAERTANEQVTDFCSADIYYESIENEVKEWTATAIAEAASHEAEAKMLTLAAEVQRTSQKGAAYKVLATLAQDRANKAAAAAAATAKTLSAALTIISRTRAQISTFYGLAEQKATSERIRHETMAGSNTLLRSGSPSRKCAATLTRTTPQSATCSDEQGKAAKLKSIAGALAMAKAVKSILKAKTKLAEVKVAFEGVGNLGTSSGWNVHSTATHCEDHASGQAAASANHAIAITGITEKYAISFDDVKLDQEPDGEAAKEPQTTNEQRSYFVSEQQLAEAIRQARQAQITKTPLLQTESIEKVASSEAAAALYDFMTGQHSNRPEKKPEAEKVAKLIFGEVTGSINDDFIKPLSKDKLTIPTSGKPIEGSTQKLAQENFDTAMVYYFSPNTKKEIANTAGDEAEGDEKADVADKSGEKKDGDNKAATTQCTATEADKCDKTKCDWNAEKNECKVKVGVSIESAEKVGTENTTGSNSFIIKAPLWLAFFYWDIIYKVFLFNFIKIVNLSISRDFNKLYNI | Function: VSG forms a coat on the surface of the parasite. The trypanosome evades the immune response of the host by expressing a series of antigenically distinct VSGs from an estimated 1000 VSG genes.
Subcellular Location: Cell membrane
Sequence Length: 542
Sequence Mass (Da): 58567
Location Topology: Lipid-anchor
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R1CQU2 | MKSKSLLVAVALASRCEAFAGPRPPLRTSHARGDAQPHSSSPARLRGGGGGGAAAALALDVNPVILRLTRDSMAELLTSCAIGYGATKAGYLSGSQIRSLAGVVFNVFLPAMLLTSVASTVAEQQAGAALAVMPIAAWAQVAVGASVASVSLALLRLPRRSSAGRGVSVLSSFGNAGVLPLLFVSSLFRGAAQEATRRRATSLVAMFLLGWSPLFWTLGYALLTGHAALSPAAAAAAAAAEPAATATAAALSPATSATAATAATAALPVGAARAARLRQLRASLRRALSPPIAACLAGLVVGSAPPLRAALLPAAAPSAPSLQSWLPLFRCLEALGKAYSPAALLVLAGSLAAPTEQRRAGEGELGASASHVVAIAVARFCAVPLLSFALLHAALRAGLLPADPLRDLVLLLQSCMPSAQNSVLALQVDGSPERAARMARVLLAIYLIAALPVAGILSLLLQRYSAVGGVGLATLGL | Function: Involved in cellular auxin homeostasis by regulating auxin metabolism. Regulates intracellular auxin accumulation at the endoplasmic reticulum and thus auxin availability for nuclear auxin signaling.
Subcellular Location: Membrane
Sequence Length: 477
Sequence Mass (Da): 47846
Location Topology: Multi-pass membrane protein
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A0A7J4TIU9 | MALQRCFIALEIPQEALAEAVRIQSILRKQALLEGNFTASESIHLTLKFLGEIPEETIEGVKGRLMEVVIPRGSCTLASAGVFSPHHVRIIWLYLAGDPVMELQRRVDASLDGLFAPEQRFMSHITLARVKRLTDKKRLLAVLDAIAINPITFFLRSFSLKKSVLTPKGPSYTTIVHYEK | 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: 180
Sequence Mass (Da): 20182
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A0A4Y2L3J2 | MHMWRLGDRTLPWGIRVDGGSDWIALHRNFCSYLTQQNNTLLQGLMTVFRYTLLPAESFFHTVLQNSEFCETVIDNNLHVTNWKRKQGCKCQYKHIVDWCGCSPNVFKPEDWPRLQKGKYSATSRYELFEIRRCRAAKFCFEIRMTFEIRGTSTICTVLKQKESIKGITPAKGVTIISKLRSSLHEKMEKLLMVWVTEKQLKGDTLTQGIICEEARAIYGDLLNQSPRTSTDEASEDSFKASRGWFDNFRKRTGIHSVVRHGEAASSDEKAAEDYLKTFSELIEANGYIPQQDFNCDETGLTFM | Pathway: Glycan metabolism; chondroitin sulfate biosynthesis.
Catalytic Activity: L-seryl-[protein] + UDP-alpha-D-xylose = 3-O-(beta-D-xylosyl)-L-seryl-[protein] + H(+) + UDP
EC: 2.4.2.26
Subcellular Location: Golgi apparatus membrane
Sequence Length: 304
Sequence Mass (Da): 35072
Location Topology: Single-pass type II membrane protein
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A0A2K4C2C5 | MTTIIDNYIDRFANYLQERNNLDRIAYLKVRLGLQVVVSNIIKLVVTYGISFLCGLFFYTLTTHLSYFVIRQYAHGAHAKSSIQCHVLNLLLFVLLPWLIVYTQISQVIMFIVAVFSFIILCIYAPSETKKQPIPQSIVKDLKIKTIVVSLIVIAISFLFPDPYPQLIYTGVFLIAVSQLPIFSTKEDVYL | Function: Essential for the production of a quorum sensing system signal molecule, the autoinducing peptide (AIP). This quorum sensing system is responsible for the regulation of the expression of virulence factor genes. Involved in the proteolytic processing of AgrD, the precursor of AIP.
EC: 3.4.-.-
Subcellular Location: Cell membrane
Sequence Length: 191
Sequence Mass (Da): 21874
Location Topology: Multi-pass membrane protein
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R1CXC0 | MLSAMLDGSTDGEQALLLRKMAKRDTVTKLKALGELREALSAHGASWAAELMPHWVPHFVRLSGDGSWQAAAAADAHARRVGSALRAASHLLAVAAESGEAPASGARAALEAALCGGEVWRLGSAASSFVRTGAYGWAGSVLSHSTALAAGTAAEMAGLLLGGLKESEPACHAALWEPLLLLLRDHGAAVSCSEAARHTLPRLVSLLEHGCHGAAPTVARALLPLVSLLPAPLFEPPASAALPPAAALLAALWRGLGASALPPQHGAHLLRAYGELLQLLVVRTSARGASAAPLLREALCGRAAAVVGDAVLPP | Pathway: Protein modification; protein ubiquitination.
Function: E3 ubiquitin-protein ligase. Component of the ribosome quality control complex (RQC), a ribosome-associated complex that mediates ubiquitination and extraction of incompletely synthesized nascent chains for proteasomal degradation.
EC: 2.3.2.27
Catalytic 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: 314
Sequence Mass (Da): 31935
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R1DHB6 | MGAPDVLMLVLPFLVLCGGVCGVGWCFLARTLLRARVEGYRKLVRRGEELQRAPDVEAARRPSRRPEGLRVAVVGGGWTGVRVVGALRRRGVQQITAFEQAASLGGSACGASLHHLGTGELRPPELLASLESLARRSAAWGHFRFRSAVRALNYDPTRREATLRVQRTDGGRFGAEVEYGPFDCVVWASLDGRPSPPHEQTVRYQEAFQGRITHASALLPEELEEAAARLERVVVVGASKAACDLVLALRRNGHASSLTWAVRRPYTFLRLEALADASASGAALHLANGVAAAAAPFAPRLSGLVWARWADDWGAFRVGVLSEAELSLLRSTRLVVGEPLSFSEGGIHFSGGRWYRHLIAPRCPVLASAAECFTGFGPAHGETVARLLVDHLCDADSYSLGEEELEAETRSHCSRGQQLFGAPRGRLNPAPQWLLLLLDLTSQGLLEFTDLRDIFRGALRTVRLPRGAPHSDE | Pathway: Siderophore biosynthesis.
EC: 1.14.13.196
Catalytic Activity: L-ornithine + NADH + O2 = H2O + N(5)-hydroxy-L-ornithine + NAD(+)
Sequence Length: 473
Sequence Mass (Da): 51359
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A0A7C4E2Y1 | MDKLVFVIIDGLGDRKCRELYGKTPLEAASKPFLDYFARHGKVGLINVIDPSIAPTSEHGILSLLGYDVIATRFPRGPLEALGIGINVGEELAFRTDFATLRDGIIVDRRAGRIREGVKELERDINQKIYLEDVNFVFKSTIAHRGVLIFYSNKFELSDCISDTDPQAVNVPPNLCKPLILRESEIRTSAIVNEFIRKTHLLLEYHRVNLQRKARGLNEANFLLLRGGGIGLPRVEKISLKYRRFWCCISGSPLEKGIARLVGMEVVDIPEATGDIDTDLRAKARALIERLDEFDCFLIHIKGTDEAGHDGNAELKKEFIEKIDGLFFSELFSNLSLRRTVICVTCDHATPCELGRHSNDPVPVLISGGKIKGDGIDNFSESSCRRGSIRMNGRYLLPMLMELLK | Pathway: Carbohydrate degradation.
Function: Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
Catalytic Activity: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
Sequence Length: 405
Sequence Mass (Da): 45367
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A0A192H0C2 | MRLALHEALKGRYLTYTNPMVGAVFVKNNKIIGVGHHLGFGYEHAEVNAFHNVQSPEEVNNSTLYVTLEPCSHFGKTPPCCRQLVAWGVKRVYIAQKDPNPLVGDKGISYLREHGVEIHLGLEQAAAEQLNQFYNFFYRQQRPFITLKVAQTLDGRVSLDGEQRTYLTDEVANQDVQKLRGDYQAILVGSGTVLADDPKLTVRHQLKYPPVRVVLDRRGRVTPVQQVTDDAAPTWLFTENQKSTAKLADTAVKVFYRPKWTIKLVIQELAQAGIQSVLVEGGPQLHDAFLLANNWQRLIVYQTNQLAGGTSLAAFQSRRQSTELTTLEIRSVKKIGNAIKITGEMA | Cofactor: Binds 1 zinc ion.
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 2/4.
Function: Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5'-phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)-pyrimidinedione 5'-phosphate.
Catalytic Activity: 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)-pyrimidine + H(+) + H2O = 5-amino-6-(5-phospho-D-ribosylamino)uracil + NH4(+)
Sequence Length: 346
Sequence Mass (Da): 38763
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A0A0C9REF3 | MVNLLLRSMKEAETFLEFQCGITSAERNFRRSAGFYLKLNVAVLLTAFCMRIHAQKEIHNLTMYGFTETEEKILPPLNVSHIYNNATDYLRLSSGLGGRSGKTRGKRSVVHLYNMLVCATGCNPLTYKGYGCYCGFLGSGYPVDGIDRCCWMHDRCYDATGCPTFSEYFIPYYWKCYRGHLPICAVLHGSWGGSGSCAQRLCECDRAFAQCLRRFPCPSSKAVCTSSPLRLVQNIFMIF | Cofactor: Binds 1 Ca(2+) ion per subunit.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+)
EC: 3.1.1.4
Subcellular Location: Secreted
Sequence Length: 239
Sequence Mass (Da): 26978
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A0A0T5PBN7 | MQTTAQSELHGADLIDEIIRLSDFNFQRLPMLEIIGERFVENLSVALPEHTRVICEASLAQFEYMPLAQIIDALPTPPMIATCSGSLLDGDFMMITDPQLALTFVELSLGGTAEGALGDVPKAYTGIECGFGAQLARILLRELQSSMSVIGPMELELENIETDPEAANIAPQASLCVRFKISVAMAGRTGALYVVLPYDTLEPIRANLAKVHFGDGGNGDRGWQKLISGQLERAHLNLEVILAEQSVSLDRLMRLKPGDVLEIYGSEDSDALVRCEGTPVFRATTGKRNNGHAAVQITKMLELPEGEVE | 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.
Subcellular Location: Bacterial flagellum basal body
Sequence Length: 309
Sequence Mass (Da): 33566
Location Topology: Peripheral membrane protein
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A0A7R9AIL5 | MWAANIAHQAREENRIESDLGLRGVIDSLTAVRRTCAICQHVEYIEVPIVYTQVVTVATYSFYFALVLGSQYIDPDNDPKSSGDNSQKLGGLNTYIPFVAIFQLILYVGWLRVAESLIDPYGEDDADFELNWLIDRHIKVSSATSRFLHPVLTGHPVLTGQRVLPYDSWLCSKVSHVMGEGLNVDFKQYTWNDMFPWLFNKALAPRPKLLAFANMMDKDKGSKSGGFRVERRKERFRRMREGDSPNHRKPRLRFSHVDVPFRGNLGIDASD | Function: Forms chloride channels.
Subcellular Location: Cell membrane
Sequence Length: 271
Sequence Mass (Da): 30939
Location Topology: Multi-pass membrane protein
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A0A496R0P1 | MSETPCTSVKSWFLKELKSELMQIQLWLLLPTPRLLLKRLKKKLKKAKLKKKVKKTAKRPVPKNRKSRSMPPFIIMGLGNPGPRYELSRHNIGYHVTDLIMQKPPMRLRRRLFASYFYLRLFNFTDRKSIVLIRSAGYMNNSGDILPSVMRRYRFTPEDFIVIVDNIDLPPGVCRLKKGGGDAGHNGLKSLISRMGSSDFYRLYIGVGRPAAGVSVVDHVLGNPEADDSRKILQACVRAADAIKSLADKPVSRVMEELNRREYS | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
EC: 3.1.1.29
Subcellular Location: Cytoplasm
Sequence Length: 264
Sequence Mass (Da): 30128
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A0A959F2G3 | MHRQTFNRQERLKRRKVIARLFAEGQTFGQFPLRVFWLPVPEKQEVAAQFAVSVPKRSFRRAVDRNRIKRQIRETYRLLKPGLYERLPASAPPVALLVLYTAKEPLPYPEIERAMKGVLQRLAKKLRSTNFSVEDPPPLS | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
EC: 3.1.26.5
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Length: 140
Sequence Mass (Da): 16394
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R1F2W0 | MSTTLSLAGVAAAAALKVVIAGAAGGLTARRLRLDARVLTALSEVNKELFIPLMIFTSCAEGITASMLTHLKGVPVMSLAFMLNGLVCGQLAARLTAAPRAARPITTALCGFSNVVGLPLPLLLSITAAVPALAGPADPSLPEAHAQSLESRTLSYLFLVNVVMSVCMWAIPLICLTLGASLLVGRAADDTTPVGGAGEHGGGAGGGGGGGAGGGGGGGGGDKVGGGGGGGGGGGGGSGGPGGLLFSGATTRLVLVAKLLVVPAANLGVVLAALRLGLLPPAGSNPLLPVVLLIVGGSPTAMNMSTISTLSGVGQREVATVLFWQYCLAGVTMSLWATVGLALFLPDGGGAGAEEIELGSGDL | Function: Involved in cellular auxin homeostasis by regulating auxin metabolism. Regulates intracellular auxin accumulation at the endoplasmic reticulum and thus auxin availability for nuclear auxin signaling.
Subcellular Location: Membrane
Sequence Length: 363
Sequence Mass (Da): 35143
Location Topology: Multi-pass membrane protein
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A0A0T5PDV1 | MDKFSGQKSAVQYLYPPVEPFDRRMMDVGDGHTIYVEQSGNPEGKPVVVLHGGPGGGCSPAMRRYFDPKVFRIVLFDQRGCGRSKPHASVEANTTWHLVDDIEKIRGALGIERWIVFGGSWGATLALIYAQAHPDRAVHLVLRGVFTMTQAELDWFYGGGAGRFWPETWEQFQRLIPEDERGDMIAAYHRRLFSGDRAEEARYGKAWASWENALATVGSSGVGGESPPDYARAFARLENHYFTNAGFLETDGQIFDNIPKISHIPGTIVQGRYDMICPPESAFRLARDWEKADLRMIPLAGHALSEPGISAELVRVMQALGRD | Catalytic Activity: Release of N-terminal proline from a peptide.
EC: 3.4.11.5
Subcellular Location: Cytoplasm
Sequence Length: 323
Sequence Mass (Da): 36015
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A0A2G6GM63 | MRNLIFRLFFIVLFGGLLFVYVFPWSSYGINIPFSGKDYKLGLDLQGGIELDYKVDLEEARKEKDYNKQKEKSIIEGLKSIIDKRIETLKINDSVITSADYAGEEHIIVQIPLKGNNDLENGNNIKKAKEAIGKVVKIEFKEERTEITDVDIQERKKLSFDAFKEAKANFEIASQKFKDNYENVFSGTMSGTLEDMKNYFSLPENVNIGLYDGVLTGNYKKHYEILDGELVEVSGDAGYWILNILYLYDEKQELVISSGTGTETSTGTELVNVPSISFDYIFINQKPSEWKPAKDKKGRILNDKYFVKSSVQYNEAFQPQVELNFNDEGAEIFGELTSRLIGKPIAIFVGGQLLTAPNVNSAILNGRAVITGDYTPEEASKLSTDINTGVVPAPIYLTSEKAIDSKLGASSLEKLIVAGIVGFLIIFMFLIIVYRLSGFLASISLFMYIVMVLAVIKSFSIVLTLASIAGLILSIGIAIDANILIFERIRDEIKLGKNLNDSVIIGFKKSWSAIWDSNITGFIVAVILFIFGINLIKGFGLILAIGIVVSLFSAMYISRILVVLLSKETKNKKLFIGIKK | 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: 580
Sequence Mass (Da): 64631
Location Topology: Multi-pass membrane protein
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A0A7R8X5U2 | MMSVFSKTEVGTVKRILDDDSGSDDEKTPAKVIKSVGAAEKPTDLLTGSDKSLQKKEDGERSIGTLSKNYLLGLIKPKIQLKKHTGSTSQLQNCSEVEHPRQKLCENSQNLLPTTLPSSSLDLQSDPPQFQKAVNGEMEDKEGSGKESNIVDSDVNHVNEAFQIGLDTSRHKYNANGLFKGKADEVEALSSIYGKDFTVEDESTQTYSISICCSGNDRNLRDLEASLQFSFPAEYPSKAPPDYQLSCPWLRGDKKQTLCCQLEEIYWSVILHVLTINENPGESIIYMWVQKIEEFLSERQREEEDTILAKKMSSLLKEESLQEEKVVDFSDCPPITHGGVIVDRKSTFQAHLVQVTSLHQVKQVFRKLLENRKIADATHNIYAYRIFDTQKKSFVQDCDDDGETHAGSRVLHLLQIIEARDVLVVVSRWYGGTLLGPDRFKHINNAARMVLQIAGFIPESSSPSKKKGKLRVRSIGSILAAATTMSAKAKIQQRPSSDMAAFREVFQKSQKVVVLTGAGVSAESGVPTFRGPGGYWRMYQAPELASPMAFRGNPSLVWEFYHYRRELMASKEPNPAHIAIAECEKRLQKEGRDLVVITQNIDGLHARAGSSNIIELHGNLFKTKCLECGEVAVNTDSPICPALEGKGVFFNPESAMHNMEGVLDRLPDPDAPDARIPEIQLPRCKKQACGGLLRPYVVWFGEALDPQVLDAAHATLDTCDLCLVVGTSSVVYPAAMFAPQVARRGIPVAEFNIEPTPATHSFGSMRTDAPRGLGSLNRRAVLSSRSLRDVLM | Cofactor: Binds 1 zinc ion per subunit.
Function: NAD-dependent lysine demalonylase, desuccinylase and deglutarylase that specifically removes malonyl, succinyl and glutaryl groups on target proteins. Has weak NAD-dependent protein deacetylase activity; however this activity may not be physiologically relevant in vivo.
EC: 2.3.1.-
Catalytic Activity: H2O + N(6)-glutaryl-L-lysyl-[protein] + NAD(+) = 2''-O-glutaryl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide
Subcellular Location: Cytoplasm
Sequence Length: 792
Domain: In contrast to class I sirtuins, class III sirtuins have only weak deacetylase activity. Difference in substrate specificity is probably due to a larger hydrophobic pocket with 2 residues (Tyr-561 and Arg-564) that bind to malonylated and succinylated substrates and define the specificity.
Sequence Mass (Da): 87669
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A0A6P8M5E7 | MCEEDLTDPIAPEYSYVFDFEKNYSYGDTQEWLLDNIVYCICYVVFYVTVIIVGISHMLEHPKYNLKRSRALWYGLMALLSIIGFSRTAPELLFALLHHSFYHSICLPSNYYQNPVSGFWSLALVILKFVQMFDTMFVVLQKQEMTFLHVYRHLSIIIYFYFTYTETTAAMRWFSVMEYFINFCIYSYYAVESMEYKLPLCLIITCRVMQILQMMTGYILTIIAYNQRDIHKLNCYITHESTAIGSIYYIATACFYAKYFYSTYISRKQKKRGRKTK | Catalytic Activity: a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-chain 3-oxoacyl-CoA + CO2 + CoA
EC: 2.3.1.199
Subcellular Location: Membrane
Sequence Length: 277
Sequence Mass (Da): 33012
Location Topology: Multi-pass membrane protein
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R1EDK0 | MAIVKTITQSNRISLPAAGEDVPRARRPGEQDKSDQYSSPKRQPAKGELFGVCGELLFLKLPFLVAHRVFAKKRIAESKNQLNVGIGGDIPIFPPFALMLGATLGVSLRLALGQWTFLPSSVATISYRIGGFVVGLEAMLMRCEDALEEHNTKAFFTEVRGLATNGPYSVSRNPMYLGFFCMIPACTVLSDSVWMLLSMMLVPLYIHNVVIPKEEKFLVGLFADKYTEYCTRVPRWL | Pathway: Phospholipid metabolism; phosphatidylcholine biosynthesis.
Subcellular Location: Membrane
Sequence Length: 237
Sequence Mass (Da): 26352
Location Topology: Multi-pass membrane protein
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A0A7R9AAW8 | MKMAPQYNIYLCGSIRGGRQDVQIYGKIAEKLKEYGTVLTPFVADPNVRDEEDLDDRAIFERDNGLMAQADVLVAEVTVPSLGVGMELGWALRDKRIPILCLYRPQNELSALVRGLADGNTNQVKDYKEEELDQIIEDFFNILAVKNVAESGDK | Function: Catalyzes the cleavage of the N-glycosidic bond of deoxyribonucleoside 5'-monophosphates to yield deoxyribose 5-phosphate and a purine or pyrimidine base.
Catalytic Activity: a purine 2'-deoxyribonucleoside 5'-phosphate + H2O = 2-deoxy-D-ribose 5-phosphate + a purine nucleobase
EC: 3.2.2.-
Subcellular Location: Cytoplasm
Sequence Length: 154
Sequence Mass (Da): 17266
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A0A7J4L3T7 | MKWEERHRYTIKGGKNMAANPGYRTKEQITGADCVVGALLEHNVPFVTGVTGGAIMKIYDAIGESGIRVIDAAQEGGAGHLAEGYAMATGRPGVVVVTSGPGFTNVVTPLYDAYMDSVPLIVISGQVAASAIGTDAFQEVDAYGLSLPIVKHSYLVKDARDLPQVMVEAFYLATNNRPGPVHIDIPKDVAQCLLGEIPEIDYSSNAFNHNPITRLNGELEDALEMLYLAERPVVYIGGGVITARAANIADLVRKLNIPAVTTLKALGALPYDKLNLGMPGMHGTAYANYALGNADTILVLGSRLDDRVVSNLEQFAVKRIIHVDIDPTEIDKRVIAVSPFHADVGEFITAMLARAQEGSGRYHDWHAQIAQWREQFPMEFHQGAGVISPQYPIAVLDEILRNEDAIITTGVGQHQMFAAQYFHPRGQRRFLTSGGAGTMGFGFPAALGAKLAHPERIIVDIDGDGSFLMNVQELATAHKHNIPVKAMVLTNGAMGMVRQWQTLFFNQGYVASHLGTGGYPDFSMIAQGFGIPGRRISRPEDVQPAIEEMLGATTPYVLEILVDKDAQVLPMVPPGKRVDSDMITIQGARERR | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 1/4.
EC: 2.2.1.6
Catalytic Activity: H(+) + 2 pyruvate = (2S)-2-acetolactate + CO2
Sequence Length: 592
Sequence Mass (Da): 64118
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A0A384DH55 | MKSRIPVVLLACGSFNPITNMHLRLFEVARDHLHQTGMYQVIGGIISPVNDNYRKKDLVAAHHRVAMARLALQTSDWVRVDPWESEQVQWMETVKVLRHHHSELLRSLPQTEGLDHGRARSTAPTAVPELKLLCGADVLKTFQTPNLWKDAHIQEIVEKFGVVCVSRMGHNPKEYISGSPILHRYRHNIHLAREPVQNELSSTYVRRALSQGHSVKYLLPDAVITYIKDHNLYTRDGSCKGSGTQRNEGKTSWGEPATPPRSSS | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from nicotinamide D-ribonucleotide: step 1/1.
EC: 2.7.7.1
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Length: 264
Sequence Mass (Da): 29871
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A0A1S4FU22 | MAILVACHYIMEKHFVRVNWSLFLIFSSAGLVPFSIDKRTLHVRESVGKFILWLLVVSINITCFYQIYSNSLRGNWHGMVVKFSQWCILILITVDAGCILVQALLCRRNHMLLINDIVVDDFIIREKYRLQLNDQRIKRRTLIKILLLGLHWSLIHVCEIISTQEKLLALQKALTSVPLVWLLNVRLSMQIFYIDLVAERLHILNGELQFLGNEDMNFANGQPNFREVIRRVQQTYTAIWKCFRKINCIFGWSTVTLVLKLFVLLIITSFWCINGQKSFNNNGWLYLESSLSIVFIISSLALLCHSAANCKRKSLDTAEALLKPDYDYEDLDVRDFLAQMQHQPFVTSANGFFDIDYCLLGSTLATTATYIVIMLQLEGN | Function: Gustatory receptor which mediates acceptance or avoidance behavior, depending on its substrates.
Subcellular Location: Cell membrane
Sequence Length: 380
Sequence Mass (Da): 43911
Location Topology: Multi-pass membrane protein
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A0A7C4IAE4 | MRLKIREFFSECGRIIKIARKPEMKEVNEIFKICLIGILVIGLMGFSIQGLLFIFTTLTGSVEAAILPTFALGIAFLYLLFKFLKY | 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: Membrane
Sequence Length: 86
Sequence Mass (Da): 9809
Location Topology: Single-pass membrane protein
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A0A7R8XFQ8 | MAETQDIRFDVVALGGAIYDIIGYVGRFPEVGETVNGTGLMEGFGGKGANQAVACAKLGGRTAFIGRVGDDGTGRATVENFRKWNLDASRVQLTPGASSATALIHVERSGANKVVVVNGANDHVSEGDVQDAADVIEASKVLVCTLEVPKEAVRRALEIAARRGITSVLNAAPEPSSMPVDLFSLPSIVNVNETEAAQATGLKVETVEDAKDALRSLLKDKGCKGVILTLGENGCLYGHRDEPENVVHVTTESVSPIDTTGAGDSFNGAFAFFTACHSELPMRERLSRACAVATRSVLSHGTQSSFSTRDQLPHALFL | 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 2/2.
Function: Catalyzes the phosphorylation of ribose at O-5 in a reaction requiring ATP and magnesium. The resulting D-ribose-5-phosphate can then be used either for sythesis of nucleotides, histidine, and tryptophan, or as a component of the pentose phosphate pathway.
EC: 2.7.1.15
Subcellular Location: Cytoplasm
Catalytic Activity: ATP + D-ribose = ADP + D-ribose 5-phosphate + H(+)
Sequence Length: 318
Sequence Mass (Da): 33455
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R1FF78 | MAPMEVETVATVGARKWSPGSWRSCETLQMATYEDSQDSYAATMDKLSKVPPLVQPGEVDALREQLAAAARGEKFIVQGGDCAERFMDCTADYLEAQLKLIVQMGALMESATGMPTVRVARMAGQYGKPRSSPVEKHASFGEIKYWHSCATLNTMRGLQMADDFGASTVGDLDVDFLKPSPHYAAWSKAADKAKAAAAATKPGAMQLDLEEALTRPVAGEGQQMPQPRGRRKGHYNLSAHMVWIGDRTRQLLGGRAEYFRGIRNPIVRQVDELCFERGELKELCAILNPDKVEGRLVLITRYGAEKVAALLPAHIKAVQESGVPVVWQCDGVHGNTVTASCKLKTRKFDDVMAEVSRALQVHRESGSTLAGVHLEMTGQAAVTECTGGVVNIEEDMLTRQYDTYCDPRLNYAQSIEASLVIANALGAR | Cofactor: Binds 1 divalent cation per subunit. The enzyme is active with manganese, cobalt or cadmium ions.
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 1/7.
EC: 2.5.1.54
Catalytic Activity: D-erythrose 4-phosphate + H2O + phosphoenolpyruvate = 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate + phosphate
Sequence Length: 428
Sequence Mass (Da): 46667
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Q0IF52 | MNNNINGVVDGESVVEFSTLDAKVQELINAAIKVRNNAYCPYSNFAVGAALRTKTGEIITGCNVENGTFAPSVCAERNAICKAISEGFREFESLAVVAYQETEFTSPCGTCRQTLSEFCNKNMPVYLAKPSPARVMLTSIDKLLPHAFRPNFLHK | Function: This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis.
EC: 3.5.4.5
Catalytic Activity: 2'-deoxycytidine + H(+) + H2O = 2'-deoxyuridine + NH4(+)
Sequence Length: 155
Sequence Mass (Da): 16958
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A0A384D7H6 | MDCKVSNGPGLQDEHITNLLVFGFLQNCSNSNFHKELEVLGREVSMPAYLPEDYDDGLQTDGNRCSYFLESGERDSQGQEEIIQDIARQLAQIGDDMDHSIHPGLMNNLAMQFMNVNLSEEDRRKSLAAALEQVMQTYPMDMEEEKTMLILAMLLAKKVADHTPSLLRDVFRTTVNFINQNLFTYVRNLVRNEMD | Function: Induces caspases and apoptosis. Counters the protective effect of BCL2.
Subcellular Location: Cytoplasm
Sequence Length: 195
Domain: Intact BH3 motif is required by BIK, BID, BAK, BAD and BAX for their pro-apoptotic activity and for their interaction with anti-apoptotic members of the Bcl-2 family.
Sequence Mass (Da): 22297
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A0A7R9FU01 | MDIQREYNMKNTSYPKTKIKILLLENISESAIKEFTNSGYVEVKTFKGALEEEELIKQLKDVHLLGIRSKTTVTRKVLEKAEKLLGIGCFCIGVNQVDLKAATEKGVAVFNAPYSNTRSVAELVMGLMIMLIRKVPDKNKAAHEGIWLKDAKGCFEMRGKTLGIIGYGNIGSQVSVLAEGFGMKVVFYDVERKLPVGNSQAVSKLSDVLKQADIVTLHVPSDKTTRNLINATTLAQMKKGALLLNYSRGDVVDLAALKKALDKGHIAGTAIDVFPEEPEKNGAAFHSELQNVSNVMLTPHIGGSTEEAQFNIGIDVAVKMVNYLENGSSYGSHTVPSLNLSPQANTHRILHIHRNIPGVLGEINTKLSSHNINIVGQYLKTNEQIGYVVLDIESKLSKEALSLLKEVKGSIKRKPSGHKGTFGHALIVAGSTEKTGAAILSSTAALKSGCGLLTAAVPSSAVTPLMCRLPEAMVLLRDIDLAISSVDISKYDAIGFGPGVGVTKESAALLFHILYQHQQPLVIDADGITLLAQNKGWFELLKPNIILTPHVGEFDRLTKKHTSHTSRFETQLAFSKKHKVTILLKGPQTTITTADGKVFKNTTGNNGMATAGSGDVLTGIITSLCAQGYAAVEAACLGAYLHGYAGDVAAAKFSKT | Pathway: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 1/3.
EC: 1.1.1.95
Catalytic Activity: (2R)-3-phosphoglycerate + NAD(+) = 3-phosphooxypyruvate + H(+) + NADH
Sequence Length: 656
Sequence Mass (Da): 70538
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E0VQP6 | MSEKKVRKLGIIDPCSYSNPEKVRIKHLALFLDINFEKNILQGKVHLTCEKKENVTTSHLVLDCKDLKISKVVHLSTNKNLNFEIGESYQSFGSALTITLPVKETNENVYEISIEYETSPEASALQWLSAKQTLGKLEPFMFSQCQAIHCRSIIPCQDTPSVKFPYTAEISAPKQLMVLMSGIKNGDPQLVETNKLKWKFTQKIPIPSYLIAIVAGRLKGKILGSKSSVYSEPEILKECAFEFSETDKMLRAAIKICGPYVWDKYDLLVLPPSFPFGGMENPCLTFAGDRSLANVIAHEIAHSWTGNLVTNENFEHFWLNEGFTTFIERKIIGALYGEPQRHFYAILGLESLKETVTTLGESNPLTCLVPQLKLTDPDDAFSCVPYEKGHTFLFYLETLLNEDGKFSAFLQSYLDKFKFLTVKTNDFKNHLYEFFDNRTSILDSIDWNTWLYCPGMPPVIPDYDRSLLIVVENLIEKWWNWVPTEECLFNCCPFTIAEFEPLISAQKCMFFSKLLEKESFDIQKLKLMHKVYHMEEVQNSEVKFAWLRVCVKSKWQDRIPDVLKFLNDQGRMKFVRPLYRDLYNWEYSREIAIDNFNKNRKYMMFVLANQLEKDLHLNEVKTNN | Cofactor: Binds 1 zinc ion per subunit.
Subcellular Location: Cell membrane
Sequence Length: 624
Sequence Mass (Da): 72222
Location Topology: Lipid-anchor
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A0A8U0QEE4 | MAAAASTRPHDAMACTSEVIPAERQNTEYNTLSVEAAAGPTVATQRSSDMVCGVCFEAVLEKDNPRERRFGILPNCSHCYCLECIRTWRTVKCHDIKTVKLCPECRTRSHFFIPSDHWIEDEEDKLKLIQTYKDFLASKPCRFYDRGPGTCHFGSKCFYKHHWQEGVQDGVQDGVQDGVQDGVQAHSFQPQTIHPMWTMVWTENGYTWRMSSETEQQDTGYHFYLNQMLLMLMADDN | Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Length: 237
Sequence Mass (Da): 27234
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A0A7R8X567 | MAQEKVLAKSSYFMNSCPESRESLESQAKANFLGSTPEEASRASVMGLGAICRHANKLLGDFYNQACMDLAKALLGKVLVRKLGDQVLKGKIVETECYLGGDDKASHSYNGKRTERNAPMFMKPGTSYVYRIYGMYNCFNISSTENRGFHEQSGLDEFYLIGDGAAVLIRSLEPLEGQETMQQLREKKRKPESIRKKLKDFELCNGPSKLCISMNLEKTTCNGQDLANWPALWIEDSENVREDCIVACKRIGIDSCGPEWADKPLRFYILGNRSVSVPYPYLTSLHLPSPELAWCYVNNCLILSILAIALTLVLYKSKDDHKSHPSSNLTGADAGDILSDSPSADSSPLVEGLRSQKVRSTYKTIAASLTADEAEEERRAESTQLNHIFGLLKKEEKKFGIQSLEDLKHQLHLYKA | Function: Hydrolysis of the deoxyribose N-glycosidic bond to excise 3-methyladenine, and 7-methylguanine from the damaged DNA polymer formed by alkylation lesions.
EC: 3.2.2.21
Catalytic Activity: Hydrolysis of alkylated DNA, releasing 3-methyladenine, 3-methylguanine, 7-methylguanine and 7-methyladenine.
Sequence Length: 416
Sequence Mass (Da): 46402
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A0A4Y2VCK9 | MIPIWCWGETAWNSFFVAAMARYCTSLNNTWLVNSAAHKYGDQPFDKYIEARDNRVVALLGIGEGWHNYHHVFPWDYSTSELGYTLNLTKVFIDFMAMIGQAYDLKTADANAIRNKKLKSGDGTRLDFNDKPKHALNGS | Subcellular Location: Membrane
Sequence Length: 139
Domain: The histidine box domains are involved in binding the catalytic metal ions.
Sequence Mass (Da): 15842
Location Topology: Multi-pass membrane protein
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B3U4U0 | MKNIVILGSTGSIGTNTLDIVDRFPEEFHVVGLTAGSNDEKLEAQIRKFRPAFAALANEAAAAKLRDRCADLPVKILAGNEGVAEVAQSQDAELVISAIVGGAGLLPTLAAIRAGKQIALANKEPMVMAGALMQAEAKKHHVRIFPIDSEHSAIFQSLEGHRREDVKRIILTASGGPLWGFSREQLQDVSPERALQHPNWKMGSKITIDSATLMNKGLEVIEARWLFDIPETQIEVLVHRESIIHSLVEYTDRSVIAQLGLPDMRTPISYAMRYPERMPLDLPSLDLTEISTLTFFKPDHARFPCLQLGYEALRIGGTMPATMNAANEVAVEAFLQSGIRFLDIPDIIRSTMEAHAPRPIDGLDDALDADHWARDKAESLVHALTR | 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: 1.1.1.267
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + NADP(+) = 1-deoxy-D-xylulose 5-phosphate + H(+) + NADPH
Sequence Length: 386
Sequence Mass (Da): 42368
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A0A968VM56 | MSEIKDTETMPEDDSVLSNVSGLMVNLEDRVETRILEETMKTSYLSYAMSVIVSRALPDVRDGLKPVHRRIIYAMHKLNLTPGSKYMKCARVVGDVLGKFHPHGDASVYNALARLAQEFSVRYTLVDGQGNFGSIDGDSPASMRYTECRMDKPATYIIQDIEKDTVDLVDNYDGSQREPQVLPALFPNLIVNGQTGIAVGMATEIPPHNLSEVVEAALALLENSELTIDQIAEFIKGPDLPTGGIIYGKNDILNAYKTGRGRCALRSKAELTENRIIITEIPYQVNKADLLIRIAGLVSDKKITGVRDIRDESNKDGIRVVIECKRDASPEVILNQLYKLSDLQTNIHFNMLALVNRGRQPKLLNLKQILEEYLAHRDEVVVRRTQFDLKKAEDELHILDGLKIALDFIDEVIKLIRGSYDKEEASKKLQERFELSERQAEAILLMRLQTLTNLDKSKIEDERLAKLKLIAELKEILENPTVKKALISKEIREMAEKLTSKRRTEIVDHNIGEYNKEDYVEEEDVLIQLTKSQYIKVLPITNFRQQGRGGVGVTSFNPKDEDWVKASMIANSHDYIYAFTNLGRVFRTRVFELPSGSRIGRGQALINYLDLREDEKVSTILTVSKEDEEDQAGSIIFATQNGLVKRTKLIDFKNVRKTGIIAIGLKEGDKVIEVRLSTSDEDKIILSGSNGKTVIFDRTQLSPLGRTAQGVKGMKLKGNDKVISLQIADFDFSEEDSEAADTSSNALIEDKVNSKEYPSLLVVTENGFGKQTHLGGYRKTKRAAGGVKTLNMTVKTGKPVLVEILAGDEESLIVTTKKGTTIRISPAEISQLGRNTQGIKVIRLHSNDQVVSGSVV | Function: A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner.
Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA.
EC: 5.6.2.2
Subcellular Location: Cytoplasm
Sequence Length: 856
Sequence Mass (Da): 95575
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A0A7J4KPZ6 | MCFFKKQPVVRQLDYSRPFVILNFKTYKESSGANALKLAKIAEKVSLQSKVNIIVCPQSIDLKEVASNVKIPVYAQHTDNSVLGKSTGNIIAENLADNNIHGSLLNHSEKKLDIKDIEKTVVKLKELDMKSVVCAKDNVVAKKLSSLKLVKPDFIAVEPPELIGGEKSVSESGPEIIERSVKACNGLNVLVGAGIKSNQDVMTALKLGAKGVLLSSHYVLSKDPEGFLRELIKGI | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
EC: 5.3.1.1
Subcellular Location: Cytoplasm
Sequence Length: 235
Sequence Mass (Da): 25565
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E0W2V2 | MKLLLIFVVAIFGIVFAEDEFCYNDVVAACKPAGTEELVNCNARYGGINSVEYDLQSFANKHLTHSFQYLLLSSHFGNYEKNRMGFSKLFRKLSDSTWSEGIELIKYLTKRGGSMDFKSKRQEDTLTETQNDTYELYELESLAKALDIQKSFATEANRIHTQAVEDAEVQSHVQNEFVHKFRDTIRELSGHTNDLKNLMASSKQNSLHVYLFDEYLQKLY | Function: Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. 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: 220
Sequence Mass (Da): 25371
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A0A7R8X4Y6 | MMSRSISCYHVVAVMRPVQSMSCSKMRFMLLQSRKSLDMVFRRSSADARVQPPMGGPPPRRIGAYGFALLSVPILTFCLGTWQVKRRAWKLRLIEELGRKTHLQPIELPLEYILALNVNSDPMMMRDMEYRPVRVQGHFLHDQEMYIQPKSLIKKGAVSSGGGIVSSPQTIGGALVITPFRLSDGQGTILVNRGWVPRKLISPGSRQKGQVEGEVEITGIFRITDPRPPFAPHDNPDSKFFHRRDVEQMAALRGTLPIWVDADDRSTVEGGPIGGQTLVSIRNEHFSYIITWYVRNGEKLPISPIYTYPRIEMASPVPTMDSVDDEVLLTTHASPEPTKASFSMGAAEDWQLPLKYRRRPLDDYEIEYINKGGPPEL | Function: Probably involved in the biogenesis of the COX complex.
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 377
Sequence Mass (Da): 42501
Location Topology: Multi-pass membrane protein
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B3U0E6 | MWKGAAVFLLATLAIGWHLRYQGPVEVPDLPNQYWGPGKPVPDPKDIKPFKIDVPKEVIDDLNKRLDSTRSFVEPLEGSAWTYGISSTYLKTVLNHWRKKYNWSQRQALLNKYPQFKTKIQGLDIHFYHVKPQVPKDRKVRVLPLLMLHGWPGSIVEFQKIIPMLTTAKPDENFVFELIIPSLPGYGFSQAAARPGLGPAQMAVVFKNLMQRLGFEQFYTQGGDWGSLITANMAVLYPKKVIGTHLNMCFIESHKAHFLSLVGAYIPSLVVDSEHYSKMYPLSYHFGRLIEETGYLHIQATKPETVGAALTDSPAGLAAYILEKFSTWTNPDYRFRDDGGLLEKFTMDELLDNLMVYWVTNSITTSQRLYAECFSKANRELGVDKMPIFVPTACANFPHELAYRSETILKERFTNLVQFTHPPRGGHFAAFEEPELLANDVWSFVHKLEQRLSDEKRQKQEAKKEKAKKA | Function: Catalyzes juvenile hormone hydrolysis.
Catalytic Activity: 1-(4-methoxyphenyl)-N-methyl-N-[(3-methyloxetan-3-yl)methyl]methanamine + H2O = 2-{[(4-methoxybenzyl)(methyl)amino]methyl}-2-methylpropane-1,3-diol
EC: 3.3.2.9
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 470
Sequence Mass (Da): 53700
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A0A4Y2JSK2 | MLFSLIPALEILNLLLNPGKTQSHEFVMEVTDKTKGDVKGGTLIQYENKIRLLEIPQVPKERVSRIALVFLLCRFSRM | Pathway: Glycan biosynthesis; glycogen biosynthesis.
Function: UTP--glucose-1-phosphate uridylyltransferase catalyzing the conversion of glucose-1-phosphate into UDP-glucose, a crucial precursor for the production of glycogen.
EC: 2.7.7.9
Catalytic Activity: alpha-D-glucose 1-phosphate + H(+) + UTP = diphosphate + UDP-alpha-D-glucose
Sequence Length: 78
Sequence Mass (Da): 8942
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E0VAG6 | MAENIYHTVKLFLYYSQIFGLNPVVLRKKNSENYFQIFWIGIFYSLSLAAFLCFSFQFSIGNINMFADNDSDIIKVSERSLSIYEFISFFVSWCLFDIVSWTFILVVFSFLYLVYKKFFQINQKLVKVLSDYDKTDPEHLDFTEKIFFVTHRIIEGERVPTPHPTNNADMRKYVIKKVKQIRHLHILLVKISQDLNRIFSTRILTIVSLNVILLCFSSFLLILMLVLGRRDSVLGTAVIWVSVRFFPTCVLIAPFCLVSNEADRTSALVHLYMSKVEDVDLLEQLKIFSMQLNNRKLTFTTHGFFDLDGKTILSVIGASFAYLVVLLQFHMTMNTLKQSKDNTTSNYKDTMA | Function: Gustatory receptor which mediates acceptance or avoidance behavior, depending on its substrates.
Subcellular Location: Cell membrane
Sequence Length: 352
Sequence Mass (Da): 40966
Location Topology: Multi-pass membrane protein
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A0A846P3F5 | MLRRKKIRIGDHVLIEKSRKRYFGMLMPKPEFGDPGTIVIKLDNGYNVGFDVKGLKISKAKFEEPESVEEEMRYELGKTSKSLLKVDFDPRKPKVALISTGGTIISRVDYRTGGVYAVENPKELLHNVPELSKIVNLKMSNPLNKMSEDFDPSDWVSLAKHVARELNSGKKGVIITHGTDTLHYTSAALSFFLKGLRKPVVLVGAQRSSDRGSSDAGMNLVCASHAALSNIGEVGICMHGSTNDDYCLFIRGTHARKMDSERRDAFRSINEYPLAEVWPDGRIEMKNRNYKKRKDNTKVKVDSKFEPKIAILKVYPGADPDVINYYVSKSYKGFVIEATGLGHVPTNGKNEWISTIKKHTANGIPFVTTLQTIYGRINTNVYTNLRILYRDAGAIPGDNMLTEVAFVKLGWILGHTKNMEEIKRMISTNYAGEITKRTLAGHFLY | Function: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln). The GatDE system is specific for glutamate and does not act on aspartate.
EC: 6.3.5.-
Catalytic Activity: ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
Sequence Length: 445
Sequence Mass (Da): 49939
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E0VL89 | MYARSSSNYLKKCLTFILIFGSLIVLLIIFYLENSVKVNNAQSEILLFNEAWIQEDEKLLNLTNFRYVIKNDVCGEPFRKNTLAILIVTSYAGDVETRSAIRRSFPAKTLLKFGVRRVFLLALIDEKKNYNQVSQAAIEDENRRFGDIIQGNFIEDYRNLTYKHIMGLQWASNHCQQAKDKYLLAGYVMTHMKPIRESTNKWYVSMKEYSRSNYPNFLSDDLFVTGLLVEKTNISLFKLNRFYTTHHEYLKCCIDKPGYACDYLIGPLGNDNKLFFKFQKYAENCFYKNCKKRKEENSVKNTCIATWKENPFGKGHALIDPVKLR | EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 325
Sequence Mass (Da): 38002
Location Topology: Single-pass type II membrane protein
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A0A7J4TEB0 | MPILRTLRGSAAVKELQAAADDALLKAELKVRPVQKAVKAFGDKALIEYTQRFDSVGLSKHTLEVSKKERIQALKRLPKKIVAALATAGRNIETYAKLQLPSEWKREVQPGIFLGQIIRPLLRVGCYVPCGAAPLPSTALMTVIPAKVAGVAEVIVCVPPKEHSWEVIAAAEFAGADRIFRVGGAQAIFAMAYGTETVPKVDKIAGPGNIFVTAAKRLAFGDCGIDMLAGPSEVLVYSNSGNPVFIAADLLAQAEHDASARPLFVTTNEALAKEVNAEAEKQLSELPHSTTASASLRKNGAIVMVKNEEEACAVINALAPEHLELYEMTGSLLAKVRNAGAIFGGPYSAEVLGDYVAGPSHVIPTGGTARFRGALGAHDFVKIITYQEISRDGFNSLADAAATLAETEGLLAHKHAVEVRKKQC | Cofactor: Binds 1 zinc ion per subunit.
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9.
Function: Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine.
EC: 1.1.1.23
Catalytic Activity: H2O + L-histidinol + 2 NAD(+) = 3 H(+) + L-histidine + 2 NADH
Sequence Length: 424
Sequence Mass (Da): 45049
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A0A385YMH6 | LYLLFGAWAGMTGTALSLLIRAELSQPGSLLGDDQIYNTVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLSSAGVEAGAGTGWTVYPPLAANLAHAGASVDLVIFSLHLAGVSSILGAINFITTCINMKSPTLSQYHTPLFVWSVLITAVLLLLALPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLF | 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-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 218
Sequence Mass (Da): 23240
Location Topology: Multi-pass membrane protein
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A0A7C4I224 | MLEIKYHDGLARIGILHTEHGKIELPVFCPVINPNKLIVEPKEMARRFKAKMIMANSYIIFKHPDLREAALRYRIHRLLKFKGAIMVDNGGYQIHRYRGVEIDFAEILKFQEEIGADIGITLDLPTPASAGRREAKRSVEITLQNARESLKLMRRKNMLWSAPIQGGKFLDLISKCAKELSRLPYAMHSLGEPVQFLNNYEFTQVCYMVHAAKSKLPISRAFHLFGVGLPSFMPLATLLGCDIFDSASYALFASDDRYMTDIGTLRLEEMQELPCNCEICSRYDIKELKEMLKGERERLLALHNLYVLFKVIKEIREAIIENRLFELCAVRCRSHPRLFEAYLKALRIFSKLFDKYDPMRKRSGLFYTGEETKLRPEIRRAKMRVRRIFGTKLIPAALDQTYPFFQSLSIEGKPLFKFSKGIVKDLERIRKIADYQFGRGIGRVLFPGNVKIFKSPTTGKIRRIYSDSELLATLRPRDGFLCLRIAGALRIKDKLKNNRVFVEGKPEVEELVRSGRNLFVKFVERADPNILPRDEVLILNSKNELLGVGEAVLSSEEMKVMQRGVAVKTREGLKLQR | Cofactor: Binds 1 zinc ion per subunit.
Pathway: tRNA modification; archaeosine-tRNA biosynthesis.
Function: Exchanges the guanine residue with 7-cyano-7-deazaguanine (preQ0) at position 15 in the dihydrouridine loop (D-loop) of archaeal tRNAs.
EC: 2.4.2.48
Catalytic Activity: 7-cyano-7-deazaguanine + guanosine(15) in tRNA = 7-cyano-7-carbaguanosine(15) in tRNA + guanine
Sequence Length: 577
Sequence Mass (Da): 66481
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E0W2C3 | MHGRVKVRTTEEQKEIARQEKQKKAIEFKKIMNQILEKRSLQIHDEEGLNLTGNLLTGNPDIITLWNYRREIFLSFKNDEDLESYQKLLEKDLQLTEQCLRVNPKSYGSWHHRIWILDNLPKPDWNKELNLCTKYLQLDERNFHCWDYRRIVAERSNVSHLSEYEFTMKKIETNFSNYSAWHLRSKLLPKIFPDEKKKFPINEEKHNEELELVENAAFTDPNDQSAWFYLRWLLGLKEPKTSIIYAKCSDEIYIITSKSLTMDSNENKNYEIKINIKINDVKLDGVWINGNLQPQSCLWIFKPHQQIQPADCISISLSDNNSVYETINVQPQGFYLSKLNFHSVLSENLLETITKQLDSCNQLIELEPDSKWTLLTSIFLMLTIDRLKYENEIKNTIDKLTLIDSLRKNYYLDLRSKIIIELELLKNNEREKLNLSRQNLTCLYHSQYLHGFVEIDLSYNSLKSDSLKYLYNLLNCKILNLKKNSIDNLNSLSVLPKLEILIVDDNLIENINIETLKKYDKLIKLSLINNPIADKTDLIIDLSNFFTNIQFNCSNS | Function: Catalyzes the transfer of a geranyl-geranyl moiety from geranyl-geranyl pyrophosphate to cysteines occuring in specific C-terminal amino acid sequences.
EC: 2.5.1.60
Catalytic Activity: geranylgeranyl diphosphate + L-cysteinyl-[protein] = diphosphate + S-geranylgeranyl-L-cysteinyl-[protein]
Sequence Length: 556
Sequence Mass (Da): 65646
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B6VM96 | MRLHIKFPINRNLYKLAGIAPQRKNCSVNKRKGLSLISQLYSNTCFKNAKLSSDNPSEKGYIDGNRRVIDRNTMQPKISGVILAGGRATRMGGNDKGLTLLNGLPLYQHIANKLRPQVDELILSANRNLEIYRQSRYQVVTDLTPDFSGPLAGMLATLKSASHDWVVFVPCDVPDFPANLVAHLWQGKQQAMAAYAADDGNRTHPTLALLHRSLVSQLSNYLADGDRKLMLFMHKIGATAVQFADNPIAFTNLNTPEECQNWEHIQEIKK | Function: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
Catalytic Activity: GTP + H(+) + Mo-molybdopterin = diphosphate + Mo-molybdopterin guanine dinucleotide
EC: 2.7.7.77
Subcellular Location: Cytoplasm
Sequence Length: 270
Domain: The N-terminal domain determines nucleotide recognition and specific binding, while the C-terminal domain determines the specific binding to the target protein.
Sequence Mass (Da): 30164
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A0A496QYD1 | MRKQIDKRIQEGLNADYREGDSPLLKELEKQLDEYFLKKRTGFDLPLLTIGTDFQKAVWTALLGVKYGQTRTYSDLAEMIGKPEAVRAVGSANGANAISIIIPCHRIIGKGGSLGGYAGGVNTKRKLLELEGQPLLDWED | 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 irreversibly inactivated.
Catalytic Activity: a 4-O-methyl-thymidine in DNA + L-cysteinyl-[protein] = a thymidine in DNA + S-methyl-L-cysteinyl-[protein]
EC: 2.1.1.63
Subcellular Location: Cytoplasm
Sequence Length: 140
Sequence Mass (Da): 15464
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E0VAZ7 | MAGLVKMAIDRYENILDSISDPRVNDWPLMDSPIPTLLMVVTYLYVVTFLGPRLMANRKPFQLKRILVVYNAFQVAFSSLMLWEIFFILRKKDNQVSLLHLYHHSLTPIETWICVKFLAGGHGTFSNLINNIVHVIMYFYYMMSAMGPEYQKYLWWKKHLTTIQLAQFTLVFFHSAQVLVFDCGYPKFIAALLLVHSTIFFALFFDFYQQAYKKKEKVKQT | Catalytic Activity: a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-chain 3-oxoacyl-CoA + CO2 + CoA
EC: 2.3.1.199
Subcellular Location: Membrane
Sequence Length: 221
Sequence Mass (Da): 26020
Location Topology: Multi-pass membrane protein
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E0W075 | MGNKSILMFNKINRQPGKRFVKNLLDFSIRENHYDIAIAGGGLVGTSMACAVGKNSKLSESKVILFESASQKSFKKKAKDDEYSNRVVSINPGSKKFLENIGAWKFISDLRYKTVKKLQVWDACSDALITFNDDLMKDVSYIVENDLILNALEEVCSNLKNVTVKYESRIKKIVPPSDKNKMVHLEMENGDEYTCNLLVGADGFKSKTREVIGGQYLSWNYDQKGIVATVKLSEPTENVVAWQRFLPTGPIALLPLTNELSSLVWSTETKKAEQLLGMNEETFKDSLNDAFWKSYPKNELVSSATASLDKMLSSLTLKSFGSHQLPPSVSSIVPGSRAAFPLGFGHSIKYYRPGIVLVGDAAHRIHPLAGQGVNLGFGDVELLTNKLGDSVYNGNKIGCSRVLADYESERQREILPMLITTDFLQKLYSTSFAPVVLVRSLGLQITNALHPLKVRFLQ | Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Function: FAD-dependent monooxygenase required for the C5-ring hydroxylation during ubiquinone biosynthesis. Catalyzes the hydroxylation of 3-polyprenyl-4-hydroxybenzoic acid to 3-polyprenyl-4,5-dihydroxybenzoic acid. The electrons required for the hydroxylation reaction may be funneled indirectly from NADPH via a ferredoxin/ferredoxin reductase system to COQ6.
Catalytic Activity: 4-hydroxy-3-all-trans-hexaprenylbenzoate + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = 3,4-dihydroxy-5-all-trans-hexaprenylbenzoate + H2O + 2 oxidized [2Fe-2S]-[ferredoxin]
EC: 1.14.13.-
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 458
Sequence Mass (Da): 50877
Location Topology: Peripheral membrane protein
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E0VBZ5 | MSAAIKFSNRLRELRIHLCQKNTTSDGVRNFINSHYLSLKQTNPKCPILIRECEGIQPKLWARFDNGEENMICLSNKNSDEILKQFESLVKGSVK | 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.
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 95
Sequence Mass (Da): 10939
Location Topology: Peripheral membrane protein
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A0A0T5PC37 | MDMIILASLLIFTLLIFSGVPIALGFLGATVFVAVTKDYDPDFLLPAGFAAFNSVTLLTLPFFIAVGYLVTAGSVASRLINLADAVFGRVRGGLGIVAIVVSCVFGAISGAAASSVIAIGTTMIPQMEKQGYPRGYSAALISSAAVLATMIPPSLAMIMFAFVTGQSVAACFLATVGPAIVLATLFSLLNVIMVRRMPGVVSPKPMSFKGIATDLRDRTKPAIGAIMLPVVILGGIYGGIMTPTEAAAVAVFYVIFLSLVVYRDMSLKQMVIALRASVASTGTMIVMTFFAALLGRLYTMEQVPNQVSDVLLSLSSDPLVLLLLINLLLIITGMVMDELSAILLVTPLLFPVVLQLGVHPIQFAAIIGTNLGMGMMTPPMAGIMYVGARVGRVTIDKMIGTSMILILFGSIPVILLVTFWPPLSLALPQLLGVVR | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 435
Sequence Mass (Da): 45694
Location Topology: Multi-pass membrane protein
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A0A402CQF7 | MLLVIDAGNTNVTFGIFEGSQLITHWRIRTEHGRTGDEYAALLTTLFQSENLRFTDIDGICIASVVPSATTDLRRLAERHFQHDPLVVSGEIPLGLTVRYHPVTDIGADRLVDAVAAVHKYGAPCIVIDFGTATTFNAIAAPSAPGEPPVYLGGAICPGIALSAEALFSHAAKLAAVEIVRPPHAIGANTVHALQSGMLFGYAAQVDGMVARFRAEMNAPDCPVIATGGHVSVLISEVGTSITATEPLLTLEGLQRVYAHSQTN | 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)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Length: 264
Sequence Mass (Da): 27902
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A0A084WT58 | MLSAVPALFEYSQNWFNKNRDVRSMHLPLADSPGAVLGIIAVYLYFVLIYGPRLMNKRKAYNLLSVIQAYNMLQIIANGAVFIKICYNVFIVCDRFSFRCQPIDFSTSNAGWDEVYISYAYFLLKLLDLIDTVFFVLRKKQSHVSFLHVYHHSVMVATAYCGLVFVPGGHALMLGLWNTLVHTVMYFYYFLASLGSANIWWKNYLTRLQLVQFVYLAIHFGQPLVDVLSQYLLSKWLMSVPKAAS | Catalytic Activity: a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-chain 3-oxoacyl-CoA + CO2 + CoA
EC: 2.3.1.199
Subcellular Location: Membrane
Sequence Length: 245
Sequence Mass (Da): 28205
Location Topology: Multi-pass membrane protein
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A0A7R9A9J6 | MAAHMPAGGGHVLGAPGRGLWGSWGGGGMGKEVGDLLALYFNSLFYNEHFQNGDRWGYGLEIILTPVFLFINCFSRSLGWLFVGGVVFFTGFVIFIAHWIGIPYYWEKSPVLCISLIILGYWLMINIIFHFTMGVLVSPGYPPCLLELSFPYAFLAPADAVSNSSCFFQDAAVPEVSAICKKCIAPKPPRTHHCSVCNRCILKMDHHCPWLNNCVGHYNHRYFYLYMVYMCLGCVFILVFGFRILMEQAFCSFKGDRQDGEKEGARKGFLQSIFVSHEILVCFNRMCHHFRTILLFILQIGLFGLELNTHDHRADLLLSTASLCLGTLVILGFLAYSHGRQISRGETSIEAHINKQMRKQFETAGLKELENVAGSVIKQSESPSSEARETTVIVHYATGKSTKEVSQLTQVPVDVVKKLVPKRQPYTQRRYGQKGKWMECPFCNESVKPILVQQHMRRHIFPWSCGHCGQGFPLQKSVTAHHRDMHPGLDSFFIQDQQEPVNVLRTFYRYQGMEEFTFLGVTYKCSQTTDLLPRRKKKKQLLAGSPSTITDVISSAVGPNELENLSAVTVADSQED | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 576
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 64946
Location Topology: Multi-pass membrane protein
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A0A084VDL8 | MSHLRQCCVPCCKNEKFSLVHKFPSDNERAERWRQALTIDNFLGMPIEVIRKRYFVCSRHFRDSDYKNKASRSLNTTAVPSINLFALDAPEGLRRKIPSPVRPPMVAYFRASGSGVTEQAEQEVALIEALEEPPEHHHEQDDKTLAEFIKTEEFIQQHDQQSDKSSSITYELNNFIDDSFTSDPTITMTTITKGDLLEATPTATDLNRDLTIHSPCSVAGKRALLKRPHSSISVDVVTVPVKTVPQGSTPPTPSPGKQGRFFPPQSPLLVPVPTTSEPIVLKRVKMAPFVKERKQITTSCAMTQTDDLQTSTDNGQNEAENLEGEQDQEHEGAENVPVASTQSTKILALLECTPENLQRLQKKLIDQGGALCLDERLLHLDDEDEAVREGDKAMAPSKADDKSKFLTIRNAQTQATTSVSYVWLRDHCRCAECYNATTFQRSYTILDLPLDIEPESCNINNERIDITWKDGHQSTYDLNDIFENNLDTYRKRLAERRSQLVLWDRALISSVSNGSTKTSGLARVTLNELLCEDDVMRQVVRSLVTYGVAFITKVPPNQQSTEIAVKRIFPIHRTLFGEMWTFSDTMDHSDTSYTNAYLGPHTDNTYFSDAAGLLVLHCIQFNGTGAESILLDGFEATERLRKADPDAFERLCRYPLEAEYIEEDKHHRYVAPIIRRHPCSSVDDPDESIVEQIRFNLYDRAPLRTLPPEMVPQFYADYQQLAREISNEELHWKFQLTPGTVMIFDNWRLLHGRMAYRGKRVMTGCYVARTEFQSVARTMGLIE | Pathway: Amine and polyamine biosynthesis; carnitine biosynthesis.
EC: 1.14.11.8
Catalytic Activity: 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysine + O2 = (3S)-3-hydroxy-N(6),N(6),N(6)-trimethyl-L-lysine + CO2 + succinate
Sequence Length: 783
Sequence Mass (Da): 88891
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A0A8T5K3H2 | MPKITLNKKETLKLVGKNIPDKQLEESIPLLGTDLERVTKDKIEVEIFPNRPDMLSEEGFARALSSFMGIKTGLKSYKVNSSKYKYIIDSKVKSVRPYCGAAVVKGVKFTEASLTGFMNLQDKLHTTHGRNRAKVAMGAHDLTNVSFPIKYTTKPRSFKFRALGDSEENTISYILQEHPKGSAYAHILDKKEVPIWIDSKNQVLSMPPIINSEQTKLTIKSKDILLDVTGSSQESVDQALNILVTALADRSGKIYSVNNQPKLKPHKLKVNINKVNKLLGLNLKKSEISKLLAKMGMKYSPSTSSVEYPAYRTDILSEVDIVEEIAIAYGYNNFSSSIPNISTIAQEDPFEKFKNIIANICTGLGLQEVSSYHLSNLEDETTKMKLNLKPIKIKNSISSEYNVLRPTITPSLLNVLKINRHNEYPQNIFEMGNVFLKNGNNIEEPTRIGIALCHSKADYTEAKKALDSILSSLGLTGKYESTDHPSFIPGRVARVSIKNKKVAYVGELHPEVLNNFDIDTPTATIELNLTEIFSLI | Catalytic Activity: ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + H(+) + L-phenylalanyl-tRNA(Phe)
EC: 6.1.1.20
Subcellular Location: Cytoplasm
Sequence Length: 536
Sequence Mass (Da): 59809
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A0A0G3XIY1 | MNSLPLFFRIRDRKVVVLGEGEAAEAKRRLVIRAGGECVGEPEAHHAALGFVAMEDEKQAEAAAIRLRCKGLLVNVTDRPALCDFTVPSIVDRDPVLIAVGTGGASAGLAKVLRLRIERILPQRLGALARALGTARAAMKARWASPAQRRRVLDVALDAGGALDVLAEHDDDAVGRWLATDDAETASGTHRIDLRSHDPEDLTLRDARLLGSADVVAHDPQVPEAILVRARADAIRCGIGEEPDEGLVVVIHAAP | Pathway: Porphyrin-containing compound metabolism; siroheme biosynthesis; sirohydrochlorin from precorrin-2: step 1/1.
EC: 1.3.1.76
Catalytic Activity: NAD(+) + precorrin-2 = 2 H(+) + NADH + sirohydrochlorin
Sequence Length: 255
Sequence Mass (Da): 27212
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A0A8U0Q378 | MNSRMAASSSRVMLGPLVAAIDQGTSSTRFLVFNAKTAELLSHHQVEINQSFPKEGWVEEDPKEILQSVYECMERTCEKLTQLNIDISNIKAIGVTNQRETTLVWDKETGEPLYNAIVWLDLRTQSTVERLINKTPGRNKNHLKHKTGLPISTYFSAVKLRWLMDNVDEVAEAVLTHRAMFGTIDSWLIWCLTGGKSGGVHCTDVTNASRTMLFNIHTLDWDPELCKYFDIPMEILPKVRSSSEIYGLMKSGSLSGIPISGCLGDQSAALVGQMCFQEGQAKNTYGTGCFLLRNTGAKPVMSEHGLLTTVAYKLGRDKPACYALEGSVAIAGAVVRWLKDNLGIIQTSTELEKLAASVGTSYGCYFVPAFSGLYAPYWEPSARGIICGLTQFTNKSHLAFAALEAVCFQTREILDAMNQDSGIPLTQLQVDGGMTSNRLLMQLQADILCIPVVKPSMPETTALGAAMAAGAAEGVSVWSLRPEDLSEVTSEKFEPQINPEESEFRYARWKKAVQRAMNWETTEPISNGNGETSIFSSVPLGFYILGSMLMLIGAKYIAGHK | Pathway: Polyol metabolism; glycerol degradation via glycerol kinase pathway; sn-glycerol 3-phosphate from glycerol: step 1/1.
EC: 2.7.1.30
Subcellular Location: Cytoplasm
Sequence Length: 561
Sequence Mass (Da): 61618
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A0A7R9FSA2 | MAGNETTPAGTLREYYDQFSWALEYGSDKRVKGWFLMSSPVPTTVACIAYVLFMKWIGPRLMRDREPLQLKNLMVAYNIFQILFNVFILSLGIDSWLFEYSLTCQPVDYSLRPRAVRMVHAAWWFYFSKFVDWFDTLFFILRKKFDQVSLLHIVHHGIMPFSCWFGVKFTPGGHSTFFGLLNTQVHIIMYLYYTLAALGPKYRKYLWWKQHLTTIQMATVFVHAVQLLFVECDYPKVFVYVLMSHAIMFTFLFLDFYKKSYMHQDKRKAQRVSNGVPVPIKSSSEENSRGKKDGKNEKGANGITNGIHHNDEGLRKRATVKTVSQDISQVVNTESGKEESEATSLRAKVPSLAKQILSFNPGICFPVIHDASDH | Catalytic Activity: a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-chain 3-oxoacyl-CoA + CO2 + CoA
EC: 2.3.1.199
Subcellular Location: Membrane
Sequence Length: 374
Sequence Mass (Da): 43245
Location Topology: Multi-pass membrane protein
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A0A7J4L8R5 | MPEKQRCFIALDLPKEMISELKKIQEELRKQNLFIGKFTEENNIHLTLKFLGSIQNDTVTKVKDRLKGIKLNSFEADIDELGIFSEEFIRIIWVKLNGNEVFELQKQIDDKLIDFFPKEERFMSHITIARVKNIKDKQPLFDALKKIKMNIKGQIKSFSLIRSVLVPSGPIYEVIKRYEL | 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: 180
Sequence Mass (Da): 21171
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R1F4X2 | MGNGSSSQQQQHPAARPNRQTRASQSAQRPAAAGASAAAYPGANHQAAINASARPNGVPLAQVQAQLLEGMRPEQSGGYGYNPQRAVAPRPTVQKTVTIRNEVNLKKPSLCATPHPDDPSKLLLEFKFDASADCQIGVYYLATEPAKADGAGAGAGYSPKDAGSTPPKEERRKGLGQSYKVPLSHPLDTGAYSEAELCWQPARAAPAGREDRYPIIVCLEATSTQSGSAQSQTTFATLARIVGEGGGGGEAEWVVKPLKQKIQVGASSYELQEIFGIDQSRETRAGAAGAAGASSAAGAAGDEDNGAECVICMSEPKDTTVLPCRHMCMCASCARSLRVQSNKCPVCRSTIDSLLQIKVSKGYSSRENSSSLGAAAVPAAGASAADQPEDGVAPPAPAAATAAPTAAAGEGSADAGEGLADGSAAAAGERDATPPPGEAEVP | Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Length: 442
Sequence Mass (Da): 44934
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A0A6G0XK98 | MLAKISTLLAASIAISLAFSFDDSRPNIDYDYDIDEDHLMPRSVIMMIPDGTGPNIWTLARNMIDPTHKKMLHIDPLLKGTVQTYSNTSLITDSASSATAYSTGFKTYDAAIGVDMEKKPLGTILEAAKARGMVVGMIVTSRVTHATPASFAAHIDDRDLENDIADQYCANTNLDFLLGGGKRHFSDACLAKLKAAGYTLSYDKDDLAAYRKANEQSGALRIFGLYHKSHMSYEVDRIRGETKEPSLSEMTEHIFAILKNNKRAQKHGFFLMIEGSRVDHAGHSNDAGSMGKEAIEFDNTVGVVKKFVYSNPNVAMISAADHGTGGITLGRVDLYKWFPEPMVKQLMSTEWMESLFSKERATYDEASALKKITDLITKNTATTEVPENWITIFKGEVKKLVADPKYKTDNLLVYMGQCISETARIAWTTTGHVGTDVNLYCAGPSVFTRRCDGNHDNTHVNEIMTNYLNLDLQPITLKLRGFKPNDDKTAPPPVTPTPTNATNTPTASITFPPTTKAP | Cofactor: Binds 1 Mg(2+) ion.
EC: 3.1.3.1
Catalytic Activity: a phosphate monoester + H2O = an alcohol + phosphate
Sequence Length: 518
Sequence Mass (Da): 57072
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A0A7R8X4G7 | MEKTVTVSAPVNIALIKYWGKRNDKLLLPLNDSLSITLAQDDLRTVTTIQASPDFPTTCLWLNGREEDVSSPRLQNIISGIRNFVKEKCGENIPGIFGWHLHIVSTNNFPTKAGLASSASGYASLTFALAKLYGLDEENLSVIARTGSGSACRSLEGGFVLWNMGKKEDGSDSSSVQLFSHTHWEDLRVFLVVISSSQKSVGSSQGMLRCRETSGLLRQRLLSVGGRKEDLIEAIKRKNFEQFAKLVMQDSNEMHAVCLDSYPPLMYMNDASHAVCQIVHEYNSAIGQTVVAYTFDAGPNPCLMMQESISSDFMGLLEYFSGVMKNGTWKGIPVSRKYPSDELLSKIPSAQSPKPIPVEMIISTRIGEGPQVLPQDSSLIDSFGFPVIYG | Pathway: Steroid biosynthesis; cholesterol biosynthesis.
Function: Catalyzes the ATP dependent decarboxylation of (R)-5-diphosphomevalonate to form isopentenyl diphosphate (IPP). Functions in the mevalonate (MVA) pathway leading to isopentenyl diphosphate (IPP), a key precursor for the biosynthesis of isoprenoids and sterol synthesis.
EC: 4.1.1.33
Catalytic Activity: (R)-5-diphosphomevalonate + ATP = ADP + CO2 + isopentenyl diphosphate + phosphate
Sequence Length: 390
Sequence Mass (Da): 42845
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A0A402CSK9 | MNIKDIGGEEGFIERMRQTHAGAVGDGLILGIGDDAAIFETPAGRQSVVTTDMLVEQVHFRRDWSDPYSIGWKSAAVNLSDIAAMGAEPTLAFLSIAFSQGESVETLDRIYDGFSDCLNRYGARLAGGDTNSTPDGMVISVTLMGSVKSGQAFTRSGARPGDVLLVTGALGDSAAGLGLLQKYGLARSEKVDKDLINLHRRPQPRVMISRVLAETGQVRAAMDLSDGLLRDVSKLCAASQVGVRIDTAQLPISNATQNAAKMLAQDPTLLALQGGEDYELLVAVAPESVDAVREAVPSLTVIGEILKSGRRIVAANGVDDLDPGAGGWDHFAQ | Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine diphosphate from thiamine phosphate: step 1/1.
Function: Catalyzes the ATP-dependent phosphorylation of thiamine-monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active form of vitamin B1.
EC: 2.7.4.16
Catalytic Activity: ATP + thiamine phosphate = ADP + thiamine diphosphate
Sequence Length: 333
Sequence Mass (Da): 35122
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E0VGW0 | MNPKTYPLSFFFFFFLLSFILQIGLVISRDNFDEQKTQEYWHRLGENDLMSSLKLVKNEKTAKNVIIFVGDGMGPNTITASRIYRGGETSTLDFETFPNVALIKTYSVDRTVPDSACTATALFGGVKTNAEVTGLDGSVTVKDCLSSLNEDKKVSSIMDWAQDVGKDTGFVTTTRVTHATPSALYSHSANRHWECEATMPQSASHCKDIARQLIEDLPGRNLKVIMGGGRQCLTWNITDKPENPIDQWACKRNDARDLITVWKSDKEKRKSSYQVLTNTKDLSNLNYDKTDYVLGIFSNSHMPYEDARDKSPEGPPSLKDMTSAAIKILKKNKNGFVLAVEGGLIDYAHHRGFARRALGETVMFNDAIAEAVKLTGNDDDTLIIVTSDHSHNLNINGYSYKKNDILGIAMNSKADGVPFTTLTYSTGGIKNYQYEVTANKKIQRKDPTGDDTTAYNYTQQAGIVNDESTHGGVDVPIFATGPMSHLFHGVHEQNYVAHVMAYAAKMGMYKNRPDLPGENSGVGANSIPFTLTTILSIILTTNFLFRYVIF | Cofactor: Binds 1 Mg(2+) ion.
EC: 3.1.3.1
Catalytic Activity: a phosphate monoester + H2O = an alcohol + phosphate
Sequence Length: 550
Sequence Mass (Da): 61019
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R1FMC2 | MKRVVNCRCIQRVVLSAIGWIDWAFSLLLRVVGPVLVVLANSLIALVSVQWIFGLAPVYVTAPYGVVASGLVHAFGIYLLLNILFNYWGCLLTRPGFPGDHLAAVEAAAERATRDSTVPRVRFCKRCRVPKPARTHHCSVCNRCVLKMDHHCPWVNNCVGFFNYRYFLLFLLHLAAGCVFVMCTCLLGHLQGHDLLSARNSSVLFVAVLCALGIFLFWHVYLVLTNQTTIEFYSNRMDAMEARREGRTFRNQYSLGYRANAEQVFGPRTRSYLGWTLVSRTRPPGDGVDWPTHPREALHHV | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 301
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 34038
Location Topology: Multi-pass membrane protein
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A0A1C9CAC6 | MNNLIQLFGLFSLDHPHHQLGFNPNILETNVINIIILLSGLIYVLKNFLGSSLSIRQEKVLIAIQEAEEKLNQATIRLEQSKNQLKQTQDIIANINHQANLTAQKVQKDIIQQGKIDIEKLTQSSKASIANAKEQIKKQIQKQIINLAIHRVFMELNNQLTSEIQSSIIDKKISQLNIKL | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
Subcellular Location: Membrane
Sequence Length: 180
Sequence Mass (Da): 20447
Location Topology: Single-pass membrane protein
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A0A7R9A2E5 | MKVDSHIQIMFLTRSEYDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIQTAEGVILAVEKRITSPLMEPTTIEKVVEIDKHVGCAVSGLIADARTMVDRARIEAQNHWFVYGEKMSVESVAQAVSNLAIQFGDSDDDGAAMSRPFGVAILFAGCDELGPQLYHMDPSGTFVQYDAKAIGSGSEGAQQSLKEIYHKGMTLQEALKAALTILKQVMEEKLNSTNVEVGAVTPTKSFHLFTKEQVEEVTSDGGDGMRMDMPLHLTADAMRILEAFLASDPKSTVSMSDVDEVLEELLNPGLRRNPGNISFTAVFGTFAVVSLILLIHGCLSGWTWRKLLMLFFISVFSASLLFNWILLYQKKLSERHQTLDAGIPSECQENRSFFFSIFRSIKANLFGAYGSRANCEEYMKALYVDPMLEVSPGVVVAETLAQFILHPLERMGSELAKFQGAIVSEVGWMGSIVVLALFIILVIVVLLVGCGYSFQVWPFIRISPTPSYQRQLSRQQPQAEEVIRQYVQDVLRDALPAVQHSQSESTLAHLGVRPRSQIAMHHESLAEVDPGDRDTSRRSLLLRRHRSLQAPQGNANDVVETLERLVRLRCSTTLPPSVCQQLEIAEQYLERVALGDHLSSSEEGTARPDSHVENSPLIRKMKSMLDVDEVGQEPNHADGS | Function: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity.
Subcellular Location: Membrane
Sequence Length: 669
Sequence Mass (Da): 74065
Location Topology: Multi-pass membrane protein
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A0A7M1KBC2 | HGMCIGNDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWMLPPSLTLLLSSSMVENGAGTGWTVYPPLSSGTAHAGASVDLAIFSLHLAGISSILGAVNFITTVINMRSSGITLDRLPLFVWSVVITAILLL | 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-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 153
Sequence Mass (Da): 16431
Location Topology: Multi-pass membrane protein
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A0A4Y2N2I3 | MTTEDTWSIITDKPINSEIPAYQAQSFGIQLCSVSQTNSHEIELPIHLRYQQPHDCKIYGKHVAINLGDAVIYVRTHSDGLSTTNCFHIENDDLWIENKVELKTSFQVPVGCAEDLYINARPCSPDFESLRLLVMETSDSKQGLPKLKASNFATIPQESQQGSYTFP | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Function: Essential component of glycosylphosphatidylinositol-mannosyltransferase 1 which transfers the first of the 4 mannoses in the GPI-anchor precursors during GPI-anchor biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 167
Sequence Mass (Da): 18791
Location Topology: Single-pass membrane protein
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A0A496R882 | MSDEDLELGNAIEAESSDTIEEPKKRRVFSDRMAKMLMFVAIAIVALLVSVTVSFLTYRFMDRGNRSRQFPVISDAYNTEVPTYSMWDFLNGEGYDLRAQTADAERYTVSAKIKLGFDGDKFKDLSSELTSKNDALMDTIRFYFSQKTREQLLDEAAVKQELISKINSLLANGEVEQILFLQYQIIGL | Function: Controls the rotational direction of flagella during chemotaxis.
Subcellular Location: Cell membrane
Sequence Length: 188
Sequence Mass (Da): 21428
Location Topology: Single-pass membrane protein
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A0A183CQ04 | MAKSEFSVDRDLHRMNELIEQTLKMNDRELPNLARLQQNIQSPFFNAVKNVYEFVYEQQLNSAEPSNEIALSSAAAKATGSAHPRVIDLPKTDQGLGFNVMGGKEQNSPIYVSRIIPGGVADLHGGLKRGDQLIAVNGVNVEREKHETAVRLLKSAKGSVKLVVRFTPKLLDEMDKRFEEQRRRTLQHSPSFNRSAH | Function: Plays a role in establishing and maintaining the asymmetric distribution of channels and receptors at the plasma membrane of polarized cells.
Subcellular Location: Cell membrane
Sequence Length: 197
Sequence Mass (Da): 22118
Location Topology: Peripheral membrane protein
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F0V7W3 | MAGGDQRKKKKGKERLDKFYHLAKEQGYRARSAFKLLQLSQRFNLFQKNCSRVVDLCAAPGGWLQVAAKHCPVASTIVGVDLVPIQPIRGVETFTGDITTAACAAKLRKLVKFGEVDLVLHDGSPNMGTDWSVDAFNQNVLVLSAARLACQLLAAGATFVSKVFRSGDYAALLYVLQTLFDRVDATKPQASRAVSAEIFVVCRGFKKPAVLDERLFDPKYVFLQAEDETGEQPSKKALKDEEGGEAAEGESDEEEGIFFGTKGGKKGQFAELVRRRAKRHRNGDILAGLRRISVDEFFRSKDPTTLLVEQAREIFFQDGALPLEEAVRAHRLTTQEIRDCLTDVQVLGKAELAAILKWRFRVKKEISVALGLSKHSAEERKDGEHEKEAEGEEDGEEDADGSDGDSDAGIDEELSRLHASVSRREAKQQKRAAQKQKQLEMRKKLTRGAFFDAAEGPSDPDLFRFDAKAIEMLETKEEKLVDASLLLTGGEEDEEGTQKKGRRSRADGGEGEDVVAGSDESEDDGQLDDLDDVDRMEIELTLAHRLRKQREAEALAAGPKKKQTRREKVTGEWMQELQAFRNSMQRRAGEALAERRRAEEEENDDDDDEDNDEETSKEVFEDGLSESLGSDSRVGGNLRGATQADRWFSQPMFGGLQLRGDGEREASDDEFNPVIKAGRLQGTEGKKRQTGAEDSSSEDGQRTDEEDSSADVTRELADHDLPQVPLSEKQQQKRKRAAQAEKERNKKQRRKAAADGLMAPDSDEEDDKTGLRGKARIEEVPAPPEIQRPTDPDEVAEIQALGSLLVQKSARMDLIDGAYNRFAFNDDALPEWFEEDEKVHLRPELPVTKELMREYRQKLLDISRRPIRKVQEARARKKLREKRRLQKVKSQAAAVAESTEFTEAAKARAIDKIARQARRADGKRGKDYVVTRRVGGGKLAQKKAGKKGDGNNRVKLVDRRLKKDKRAMKAAMKKRGGKRGLKKKGRKA | Function: Probable methyltransferase involved in the maturation of rRNA and in the biogenesis of ribosomal subunits.
Catalytic Activity: a ribonucleotide in rRNA + S-adenosyl-L-methionine = a 2'-O-methylribonucleotide in rRNA + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.-
Subcellular Location: Nucleus
Sequence Length: 988
Sequence Mass (Da): 110379
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G1UDQ1 | SSILGAINFIVTIMNMRAPGMTAHRTPLFVWAVFITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPNGGGDPVLYQHLFWFFGHPEVYILILPAFGIVSHIVSTFSSKPVFGQLGMIFAMLSIGFLGFIVWSHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMFDGNIVFTTPMLFAVGFIVLFTFGGLTGIVLSNSGIDIALHDTYYVVAHFHYVLSMGAVFAIFAAFYYWIGKITGVTYPEMLGKIHFWSTFIGVNLCFGPMHFLGLAGMPRRIPDFPDAYTQWNAIASFGTFVTIIASMFFVYVVAVTFTSNNRVGYNTWAKESNFMHIAETDYLVEHFKKS | 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-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Membrane
Sequence Length: 353
Sequence Mass (Da): 39327
Location Topology: Multi-pass membrane protein
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M4ST69 | MQTVTSNTQHEGIKTTSILHRYKALALTLFIAVSMPRTGKGAPGDGLNAAEFRALCNLAAIADWQGETTTLATINSKEKQEIEILNMSASQATWQAAFPDAKQPDPDPQPACSAEDKRIHCLKDYKKFKHLKTTLKTESDTEETRDRHKLVPNIQESPEGKRIQKQLHDLATEAADIINTYDSQHGQLKQKLGAALTTVLKQALYGTGTAEKAGKYEDKWTATSTRTTDCAQRKAGTSLRGDLACLCINDDTANKQMCGQKVGPDNSNNWQASATATNINGLVSKCKTLVKPQLSTQTIRAALANFDGKLKSHAGGTKDAIVLGTPHTDGSCGGQANVACIDYTEQLTPRPEGAQNKINWYQHLDQAASTLQELQAAEIKRQQALRRITALKKRAYSL | Function: VSG forms a coat on the surface of the parasite. The trypanosome evades the immune response of the host by expressing a series of antigenically distinct VSGs from an estimated 1000 VSG genes.
Subcellular Location: Cell membrane
Sequence Length: 398
Sequence Mass (Da): 43387
Location Topology: Lipid-anchor
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A0A0D9ZGI1 | MLFSIAFMLFNMGLTSYIIGNITNLVVRETSNTFKMRDMVQRVSEFGSMNQLPEAMREQMLASVQLRFRTEEQLQQEVLSELPKAVRSGVMKHLFKSAVESCYLFQGVSDSLIVQLVSKMKAKFFPPKANVILENETSTDCYIIISGEVEALTTLADGTEKHVKRIGPRGMAGEIGVMFSIPQPFTIQSRRLTHVVRISHTHLL | Function: Potassium channel.
Subcellular Location: Membrane
Sequence Length: 204
Domain: The segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino acids. The pore-forming region H5 is enclosed by the transmembrane segments S5 and S6 in the Shaker-type (1P/6TM) and contains the GYGD signature motif which seems to be involved in potassium selectivity.
Sequence Mass (Da): 23033
Location Topology: Multi-pass membrane protein
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A0A1Y0BHT1 | MVPGNTEYLCTGFTVTCDLREGTTTGISASDRARTIRALAAQEYVSADFNRPGHVFPLRAHLEGVLGRPGHTEAALDLARLAGRYPGGVLCEIALPDGEMARLSDLATFARRWGLKLISIEDLIAWRRENGQ | Pathway: Cofactor biosynthesis; riboflavin biosynthesis; 2-hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1.
Function: Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate.
EC: 4.1.99.12
Sequence Length: 132
Sequence Mass (Da): 14382
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A0A7C4E4P5 | MKFTKIKEEGNESLFLVEGVTPAFINSLRRACMSEVPVMAIDEIEIIENKSAMYDEILAHRLGLIPLNTDLDYNLKERCKCGGKGCSRCEVRLKLDVEGPRIVYAKDLKSDDPKITPVYPEIPIVELLEGQKVDLVAIARLGFGKEHVKFSPCLAIHRNFPSIKIDVKKCNGCNACINVCPKHILVERDKKVAIDTEKLMECDLCLACVDACKENAIEVYGEEDKYLLYIESWGQLSVGQILKSAIQNLVKKLREFKRAAKL | Cofactor: Binds 1 [3Fe-4S] cluster.
Function: DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
EC: 2.7.7.6
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Subcellular Location: Cytoplasm
Sequence Length: 262
Sequence Mass (Da): 29503
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A0A6G6YB89 | MMFLSPLLGYFSMVLFSVTLALSAHSMFFFWISLEVNILAILPVLTSAQSPASNEIALKYFISQGIASIFFLCFSLLSLKISSLTLMAMVMILFKMGLPPLHSWMVSIFLASPLWVIFLISTVQKLIPLHILAVMQIPSSLLTGFVLLTLVLSLMTAKNMQSIRPMLILSTFGNSCWMAASTLLSKLWLWFLFFYSLFLASALKSLLSFNIQKLSSLLSESQFVKILCFLNFLNLAGLPPFSGFLLKLTLLKTFLLYAPLTLMLLLISLSLIVLYVYLSITFFGLASFSASTNQSTHPSSIFMGILTLISSLFAPLLMFLSP | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
EC: 7.1.1.2
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
Sequence Length: 322
Sequence Mass (Da): 35810
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R4V8L3 | MRGDKPSIQDIELDLQELVLPANLLADEILETEEVEPPPESQAYRIVTCCGICERKVRLFVSATSSQIRVQQELFLAGLSIICVACCRDLTQHGGSR | PTM: Highly phosphorylated.
Function: E7 protein has both transforming and trans-activating activities.
Subcellular Location: Host cytoplasm
Sequence Length: 97
Domain: The E7 terminal domain is an intrinsically disordered domain, whose flexibility and conformational transitions confer target adaptability to the oncoprotein. It allows adaptation to a variety of protein targets and exposes the PEST degradation sequence that regulates its turnover in the cell.
Sequence Mass (Da): 10758
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A0A496QZE4 | MIVIKAAVAVTTAYLFGSVNFAIIFTRIIRGEDIRTLGNKNPGASNMGRVVGRGWGILVLVLDALKAIIVILPARIWLFNQGGALDYGVLYLMGITAVLGHIFPIWYTFKGGGGVSTMLAVSLWFVPLEFLISVLTGGLLALAIMRKKENWFTQWSPIFFITLTPFLTLAVNLSVSIPIWKRISLGGHPWTVIAGCFALSLMMLGLNYRLVKAKATGNDWEKHETI | 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 phosphate + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-phosphate + phosphate
Subcellular Location: Cell membrane
Sequence Length: 226
Sequence Mass (Da): 24811
Location Topology: Multi-pass membrane protein
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A0A1Q0XET5 | FWINIILIGGVLVSLICLWQMDLKALIAYSSVAHMGIVLSGLMTMTYWGLNGSYTLMIA | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
EC: 7.1.1.2
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
Sequence Length: 59
Sequence Mass (Da): 6508
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R9QJQ3 | TLYFIFGIWSGMVGTSLSLLIRAELGTPGSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLISSSIVENGAGTGWTVYPPLSSNIAHGGPSVDLAIFSLHLAGISSILGAINFITTIINMRLNNMSFDQMPLFVWAVGITAFLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF | 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-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 219
Sequence Mass (Da): 23647
Location Topology: Multi-pass membrane protein
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B8ZHS8 | TLYFIFGAWAGMVGTSLSILIRSELGHPGSLIGNDQIYNVIVTAHAFVMIFFMVMPMMIGGFGNWLVPLMLGSPDMAFPRMNNMSFWLLPPSLTLLLTSSMVENGSGTGWTVYPPLSSTIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSIGITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF | 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-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 219
Sequence Mass (Da): 23603
Location Topology: Multi-pass membrane protein
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Q6W0L9 | MVVLLTSCFMSLVMSFLFKNFLICLAFSPSIFLLALHSSPFGGWLGCTGSYFGLIQSFSSWNMSVSLMLQISVLLMEILLMKLNLSIKSCILILAGSSIFYLTDSWLMFFISFEFTLLPIFYMVYAYSTTPERLRASWFLFIYTLIGSLPLFVVIFCVGKLSFWMFPSCVGLEMFNPVFISMAFLIKLPLYFM | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
EC: 7.1.1.2
Subcellular Location: Mitochondrion membrane
Sequence Length: 193
Sequence Mass (Da): 22080
Location Topology: Multi-pass membrane protein
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A0A1C5QA72 | MEAWNISYIYTVIFMMLINNILVYVLSRTPGFGKSERWILQLLIAVCVCDLSDVFGILFKQTAGRNVLFILDAAFIFSVASISLFFLCYSENIYGSNMFKKRIPLITIHIPIDVLCIIIVASYRTEWIYKYPQILMIANIYNAYSVLLSLWRIHKEKNAEKRKVLWQPVFYIVPFFIGIFLQCFFNTMPWANTSLTITILLIFVNNQQRLLQKKTQDAEAAVRAKSEFLSHMSHDIRTPINGMMGMLDIAQAHLNNPEKMDLCLSKMRGAADQLLSLINDVLDMSKIETGSIQLVEEPFDMIRLLNGTLAVQEIIASEKSLTIEQDIEGAIEHPCVCGSPNYVRSILVNIISNAIKYTNPGGDIFVSARELSCDGEYVKFEFIVSDTGIGMSEEFAEHIFEPFTQEHAENRSSYQGTGLGMSIVKNLINKMKGTITLETKQGEGSTFTITLPVKLDTVCFEETETEEEETSIEGMKILLVEDNDLNLEVAQYILEDAGAEIIVARNGLESVELFEQSESDSFDVILMDVMMPVMDGLTATKRIRKLKRKDARTVPVIAMTANVFNEDIIAAKEAGMNEHIAKPLDFDKLIHTLAKYFLKMDKKLIS | 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 sporulation process.
EC: 2.7.13.3
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Sequence Length: 606
Sequence Mass (Da): 68561
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A0A1B2WI03 | TLYFIFGAWSGMIGTSLSILIRTELGHSGSLIGNDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALILLSSSGMMDNGAGTGWTVYPPLSSLISHDGSSVDLAIFSLHLAGISSILGAVNFITTVINMRSTGITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF | 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-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 219
Sequence Mass (Da): 23621
Location Topology: Multi-pass membrane protein
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A0A846P0E8 | MKAKEFVREYYWVFLLVLVFSTAFYLRGIPGTKLEYPRLQAIDPYFMFRMGEEIVEGRGLPTNDYLAHWGTNPGGPDRTRESIVTFYAYPIVYFILNPLFGVSWYWTAVWTPAFFGALQVLFMYFLGKELFNKKVGLLAAAFLAFVPGILYRVSAGFIEKEPVGGMFMLLTFIFFVKAFKVGEVDREISWRHILLHPFSVLHKTSLSEERLRTIKSVLYGTLSGIFLFLMSLSWGGTKIVLMVIPLFVMISLLLNRYDSKFLLSYVSFFVSFSLLIIVLGYSILSVAPVSLTGVDMIVNYVALFAFLIRFGVERFNVIDKKYVPYAIPALFVIGLFVFGIASYVNIELGEWTADIIARTSQPISYGVIASTVAESQTAGGFMRDSLTTFGTGYSIAALKWPDLTIYLSAVYFAWIGLFIMIYEFVFKRRRKEFLLVSVLFATSLMLAMGAVRLNFLFAFPVALMAGYCLVRGGEFVMSRTRNLRGRLPDYMKMVVGVFIGFVVVSNFASGWVMANSIGSSLDNSWYQALVWLRDNTAEDAVLLEWWDYGWWFHYVAKKITLVDGGY | Pathway: Protein modification; protein glycosylation.
Catalytic Activity: an archaeal dolichyl phosphooligosaccharide + [protein]-L-asparagine = an archaeal dolichyl phosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine.
EC: 2.4.99.21
Subcellular Location: Membrane
Sequence Length: 566
Sequence Mass (Da): 64402
Location Topology: Multi-pass membrane protein
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