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stringlengths 6
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stringlengths 117
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A0A814NRP6 | MSNVATANDAFAKPVKVNKWDRNALKNALNDAFDKTGLNSGSRCIISSKLKKYDDKYYLTLKYNESTNKSMGSSGVLISSVGSYFDEKGVLCYDRFTSDFKKIYDQARSNARKAK | Function: Component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum. Enhances the enzymatic activity of SPC and facilitates the interactions between different components of the translocation site.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 115
Sequence Mass (Da): 12889
Location Topology: Multi-pass membrane protein
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A0A822GNU5 | MADVVHRISELTHTRLSWFGCSDDDACNRLNHRHTVLMLLIFSAILTSRLFISDLIICWTPGEFTGNFVSYTRHYCYVTNTYYISMNETIPTLNNSHMRRKRSIYYYQWLPILLAFQSLLFLIPRLMWSSF | Function: Structural component of the gap junctions.
Subcellular Location: Cell membrane
Sequence Length: 131
Sequence Mass (Da): 15597
Location Topology: Multi-pass membrane protein
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A0A183IBC2 | MENFDFVTVNVFSDIDSMVKMFTVPSPKLSTKDDPSLWLALLVTHTRDPFIGKVEQSLQASNWQCWTCKPDEEQFMESLLTLMPSVLLVDLRGRKTKEQWNKLKLSLLERRGLRYQQYHRLCNALSIALDHCESAIEICDHENHVLFVNNAYEQLTGCSRKEVLGTESSDLRRKSLPKNKLKLTNQDSKSSASEWKFVPADQHLENYLLGLFSHKIFLKRVEMDMKSMKVQSDFRLPPITILKKLVEAPLSQSNILKVVDLLQNVQKTSTLDEEVQNTIQKIVKILKSTELYSPLIPRFSYEDKIASDLFSGLVMNGPQKISANQRRTSLYEVMQNEKKKSSESHVLDADVRTDLKSLEWNFDVFTLEKLTMKRYGTNFKYNKYKCLNVRRRPLATLVMEIFQQWNVHEFLDCSLSCLDRWIQAIEANYHAENPYHNSTHAADVLQATAYFLSTPFLSNIIEHSDAVASLLAAAIHDVDHPGKTSTFLINTNHPLALMYNDLSVLENHHVAFAFNLTLTNTDLNIFSQLSRDAYISLRKRIVDMVLATDMMKHFEYLSKFKQTVLESGVFYNYNISSFFQEMSSRAEASSKLLNSVDPRRTVCQMLIKVADVSNPIRPWKFCKKWAYRIVEEYCNQTDEERAKSLPLTMEVFDRNTCNIPLTQCRFTDMFIREMMELWCRKNRFLSSQTMEIVRAF | Pathway: Purine metabolism; 3',5'-cyclic AMP degradation; AMP from 3',5'-cyclic AMP: step 1/1.
EC: 3.1.4.53
Catalytic Activity: a nucleoside 3',5'-cyclic phosphate + H2O = a nucleoside 5'-phosphate + H(+)
Sequence Length: 696
Sequence Mass (Da): 80809
|
A0A183IAP3 | FRLSCTRLGQWAIGYVAPDGNVYQTIPQNKSLIQALIDGSREGFYLYPDGRNVNPDLTWALQPSPEGHVKVTPEQYEIYCEMGTTFQLCKICAENDKDVKIEPCGHLLCTPCLISWQESEGGGTCPFCRCEIKGTESIVIDAFEPRLNLAATQHQSIHIATAKLIEPVAEVRLLSIRTLCFVNKT | Pathway: Protein modification; protein ubiquitination.
Function: E3 ubiquitin-protein ligase which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and transfers it to substrates, generally promoting their degradation by the proteasome.
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: 185
Domain: The N-terminus is composed of the phosphotyrosine binding (PTB) domain, a short linker region and the RING-type zinc finger. The PTB domain, which is also called TKB (tyrosine kinase binding) domain, is composed of three different subdomains: a four-helix bundle (4H), a calcium-binding EF hand and a divergent SH2 domain.
Sequence Mass (Da): 20621
|
A0A0M4MM54 | MTKIVVVTGTNTDVGKTITTASAIAATRVRAPHLQVGLIKPAQTGEVAVEKNSLGYTECGDCGDVAVVRALLGETAETPAPLPVWEGIRYPEPLAPDMAARRAGMELWDAAHFADVIEEAARDVDVLFVEGAGGLLVGLGEESCGAPTTLVEIAQETARRNTAHEVLILLVSQPHLGMLNQCVLTWRELQRAGLSLAGIVFGTWSENPDLPMRLNADEVLRLTGVPVIGRIPCGVGKFQPQQSGSVAAAGDQWWSQLPWCDSGEASRQ | Pathway: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 1/2.
Function: Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring.
Catalytic Activity: (7R,8S)-7,8-diammoniononanoate + ATP + CO2 = (4R,5S)-dethiobiotin + ADP + 3 H(+) + phosphate
EC: 6.3.3.3
Subcellular Location: Cytoplasm
Sequence Length: 268
Sequence Mass (Da): 28453
|
A0A8J7YSD9 | MNDVLPFGLRRFVVFLHAVPTDGSFSLNDLPGSGGRVDVAARCVGAALLVSNGIRKDASVTFIFEGRAERALSVSVFGQTVRYLNPDERTTAALIKNALQKARKTESGFSSPGIYFRRDRTRSILEGVSENTKRYYLKEDGQRIGAIRQPATFFLGDNKDLDESEEMMMDDLGSERVSISGRSIHSDQCIVISNWIMDNGTC | Function: Specifically catalyzes the N1-methylation of pseudouridine at position 54 (Psi54) in tRNAs.
Catalytic Activity: pseudouridine(54) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylpseudouridine(54) in tRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.257
Subcellular Location: Cytoplasm
Sequence Length: 202
Sequence Mass (Da): 22320
|
T1EDV8 | MEDLLKSYVLSQETYYQIRDTISQELSLGLSKSCERSSIKMLISYVQNLPTGREIGEFLALDLGGSNFRVLLIHLNGSPSAFRMESKIYPLTDSIKASVAVELFDYIVDCVDDFLKTVKISHYPVPLGFTFSFPVIQSGLASGRLVQWTKEITCDGVVGEDVVRLLHEAIQRKKTLQVECVALVNDTVGCLMSCAYEDIQTYMAVIIGTGSNASYVEKVRNIEKWQPDADETSDEMIINTEWGGLGDNGCIDFARGPADYIIDDRSLDKRRQIFEKMISGRYLGEVARLVLLEAVKANLLFHQPGRLVEAFTKEYGFLTKYLSEIESDTGKTHSKTRRILTELGVKDLTYDECSLVYKICRVISKRSAYLCAAGIAAVLNNMNRPEVTIGVDGSLVRCHPTFLDHMLQFTKKLINPGINIKMRLSEDGSGKGAALIAAVSIRKMH | Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 1/4.
EC: 2.7.1.-
Catalytic Activity: ATP + D-glucose = ADP + D-glucose 6-phosphate + H(+)
Sequence Length: 445
Sequence Mass (Da): 49633
|
A0A183IU64 | MKIKDLLQCEESAFIMVTDDYGHCFCEVTGSKELGAPISAGTVSQWSDLLMNVKYLSYEDIPLEFKAYLRSIFDDAAIISNSLTIQPILGSATNGSSSIIAVLCILHSNSLSCSSSTRSKSFDDLLNLCNDTATSVIRICYSFEKQRSLTKLNGFILTLLRNVFSNLGCGLLFYQPLINFPFSCSLYLLDHDNNELVAEVVESDENQHEVLKEIRFPLGQGIAGQVAVSGNMINVKHYVPESRIVITEEKLSLSCARNVLCFAVKDKTAVIAVIQLVNKIDTQFYTDHDEHLAELLSSYCAISISHVRSSLPLAIAEEDVLRLSLCNIPEPSSIKPDFLSFSFSPRCLSLHETHIACLTIFDDLGFIQKFRIKRKKLSRFLLLVEHGYRDVPYHNWYHAFTVTHFCYLLQKKLGIMNIYLSDVQRVSLLVACLCHDIDHRGTNNSFQLQSGGIFKNISTFQKTALAQLYSSEGSVLECHHFAQTMCIFNMEECNIFAQLPSQVDIMFLYEDFGV | Cofactor: Binds 2 divalent metal cations per subunit. Site 1 may preferentially bind zinc ions, while site 2 has a preference for magnesium and/or manganese ions.
EC: 3.1.4.-
Catalytic Activity: a nucleoside 3',5'-cyclic phosphate + H2O = a nucleoside 5'-phosphate + H(+)
Sequence Length: 514
Sequence Mass (Da): 57810
|
A0A0B6ZJX7 | MASPKIEVAVKSCCPSIGEGPHWDVKSESLLYVDIMTGGIHCWDSATGQESKINLDGSVGFVIPCDRGGLIAGLNRTISYMDWDTAEATTLAEIDQGTRNRFNDAKCDASGRLWAGTMGFESIPGKVDSGQGSLYSFSTDHKVTKQAGSIDISNGMDWTDDNSIMYYIDSVPRKVFAYDFNLEDGTISNQRTVVEFQPGTDSTYGLPDGMCIDNEGKIWVACFSASRVHRFDPETGKTLQTLEFPATNITSVCFGGKNLDELYVTSSQWRLPDESKDVQPLAGSIFRVTGLGVKGRAPNNFKG | Catalytic Activity: D-glucono-1,5-lactone + H2O = D-gluconate + H(+)
EC: 3.1.1.17
Subcellular Location: Cytoplasm
Sequence Length: 303
Sequence Mass (Da): 32982
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A0A4Q9MHK4 | MKGNLISLHLLLGLSLVPAVVSSSGDRADEFQSCVSLCQSRTCEPSSLASLSLALRLTRWTCVDDCKYQCMHLITNRAIQHGWPVQQYYGKWPFWRFAGMQEPASVLFSIFNLVAHFGGLRKIQTRVPDSHPMKKYYITFAFASMNAWVWSSVFHTRDLPTTEKLDYFSAALAILYALYYTVIRLFHIYPIERDRLTTTSSSSRAGIRVLWTLLCTLAFLGHVSYLTLLPRFDYSYNMIFNLAVGMSHNLLWLSYSLPSFLSFITRYPGRPRTYRPRHAYKPALFALLTTAATALELFDFPPWGELPSFKILETDLNYVFLDIGPVSEGHALIVPKFHSNRMDEVPDEHLAEILPLAKKIAKALDVVDYNILQNNGKIAFQHVFHVHFHVIPKPNEREGLILDVQHWPRKEVQKEQLAAALEKIQARLELSTSNLAD | Function: Involved in the lipid remodeling steps of GPI-anchor maturation.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 437
Sequence Mass (Da): 49971
Location Topology: Multi-pass membrane protein
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A0A183IEP0 | MDNGGNVILAHDIEGENAVRKTADIGSLDGEWNFESFLLSENVLKGLKAAGFKKPSPVQQQAIPAGRCGIDLMVQAKSGTGKTCVFTVIALETVQPQNPCVQALIIAPTREIASQIXXXXXXXXXXXXXVVETIGVFVPNLKCSCVIGGMTLKEGSCAQFGHIVTGTPGRLCQLIKQNDLLVDKVRLFVLDEADKLMEEDYSEDMRFIRSALGSNKQVIAVSATFTEALHKDLNNLMKSPIFINPSKMDIQLLGTVATLSRKAFVVVSGVKQYVFCITGYLNSKILALHWLLTSISFSQCIVFVNFQDKVTMIYEKLKKLNWPVEYMCSKLNQNLRSGVIKHLKAFQCRVLISTDLASRGIDASHVNLVINFDVPSSAEVYFHRIGRAGRYGIYLMTSVSSIILKSILFSQGDMALP | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 417
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): 45821
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A0A6M3R7S7 | MTEFQQPHSPLPPKPVDVDVIENAIADLLRGLGQGDKSEVMAQTPRRVAELYAQTINPGDIDIEEDFKVFDNPGMQDLVLVNDVHYVSMCEHHLAPAFGIAHLGYVPDRKVAGYSKLKKGLNYLARQPQLNERLVVDAVDFLEARLQPKGIGLVLRSAHCCIALRTNAPSQEVVTVFERRGVLREEQYWQPLWQSAVAEKPSFLGR | Pathway: Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1.
EC: 3.5.4.16
Catalytic Activity: GTP + H2O = 7,8-dihydroneopterin 3'-triphosphate + formate + H(+)
Sequence Length: 206
Sequence Mass (Da): 23094
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T1G8U6 | MNKLCLILLVAINISSAFAGPGTVGLKALFDIRIGDEYVGRIVFGLMNETCPLTVANFAALCDGKLPGGVGYMNSTFHRVIKNFMIQGGDVVNGNGYGVKSIYNNGSNFNDENFILKNYIGWLGMANAGPNTNGCQIYINTVLTPWLDNKHVVFGKVLSGWDVVKQIENNPIDSNDRPIKPVVISYSATFPVDKPFDVPLASI | 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: 203
Sequence Mass (Da): 22007
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A0A0B6ZLX1 | MMILAYFTFGALSVLCLIFQYWAHRTRRNVSVGNNPQFIKFQRGYFAVYLVAMFADWLQGPYLYKLYSYYGFHEQQIAVLYVFGFASSVIFGAWTPIAADQFGRKKLCIFFTVAYSLSCLLKLSTSYGILLIGRLVGGLATSVLFTAFEAWYIHEHLETHDFPKEWIPITFQRASMWNGILAVMAGIATNIFSEWIALGPVAPYMMAVPFLIFVGVIISTHWNENYSMHKVKFGHLCYEGLKDILSSKRIFMIGAIEALFESVVYIVIFLWTPILEPGKPSLGIVFSCFMVCILIGQAVFQILSSRGVAITKILLFVVILSLVSILVCVYSTHPRTRNLNTSLVAFLVFQFCVGIYFPLMSLLRIRVIPDAHRYAIMNWFRMPLNLISCAVLMLLHEDVFLHGNHLIFVVCVGLLSLMLFATYKFIKTPQTQEEIDEDQGGSAILLLESEHIHNIF | Function: Mediates high-affinity intracellular uptake of the rare oligo-element molybdenum.
Subcellular Location: Cell membrane
Sequence Length: 456
Sequence Mass (Da): 51902
Location Topology: Multi-pass membrane protein
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D2TX70 | MINRNNKFIELLVKYFSVGVINTLIHWLVFVFLIHFLNFQQASCNFFAFSFAVTFSFFANARFTFRKKATRKRYISFVIFMGIISYFIGFIADRFNYDPIFTLIIFSAISFVLGFLYSKFVVFKDIEC | Function: Involved in O antigen modification. Involved in the translocation of bactoprenol-linked glucose across the cytoplasmic membrane.
Subcellular Location: Membrane
Sequence Length: 128
Sequence Mass (Da): 15200
Location Topology: Multi-pass membrane protein
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T1ED30 | MNKFLHWYSSDKLPKKTFGRMLTVVCVGEKHEVDDVESEYSLKISLQPLKLNIDQDSLMFLYTFFNEISTTASRNPPPTFSAAPSQHATPTRTVRIATPSLQRQQSADLLKFDDDNDDEKLVSNMADLLQQQHVDDSEELLADSKQTSRPIFFKSLQFAPSVLIKIDYRGKRIENNSLVSIVAGLTQLSCSQITLKSLHYRHGLLGFEKLVLYMLNEWMVDVKRNQLTDFLSGVGPMNSLIQLVKGFIDLFWLPLEQYRKDGRILKGLRRGTHSFATCTALSALELTNKMLQAIQLVAEAAHDIVSTGPSIQSKNKLVSKRSGRPIDARDGVTKACALLRQGLANRCTEFCNEVIKEHEQKGVPGVIGEVARQIPPTVIAPVVLAAEASGTVLTGIRNQLVPVRKKEDEDKWKVDSKNKLSFQE | Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) = a 1,2-diacyl-sn-glycero-3-phospho-L-serine(out)
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 424
Sequence Mass (Da): 47524
Location Topology: Peripheral membrane protein
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A0A523AX96 | LKELLRERSDYADPLPLKELATLEEGELVRVVGMVAEKKETPGGHLVIKLEDPTGQAAVWVFRGKSEELWEKAAEVIPDEVIGVEGTVRSGDKFPRIVARDIVWPDLPMREHPTMAEEPVCAVLLSDLHVGSKMFLREVFERFLNWLEGKAGNASQRDLASRTKYVVVAGDLVDGIGIYPQQEEELYLHDIFRQYEEVARLLERIPDHIKLILSPGNHDAVRPSEPQPAIPKEVAGRLYELNSVMVGNPAWVSLHGVKFLIYHGRSFDDLVSILPGSSRNDIPSMMVRLLKKRHLAPMYGGKVAMVPEERDFLVIDEVPDVLHCGHIHISGLKKYRGVWAVNSGTFQGMTSYMRERGIVPTPGMVTVMDLQKNQPLVMRFA | Function: Possesses two activities: a DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3' to 5' direction. Has a template-primer preference which is characteristic of a replicative DNA polymerase.
EC: 2.7.7.7
Catalytic Activity: Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Length: 381
Sequence Mass (Da): 42850
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A0A091A1I0 | MDKLDWIQQLRQELQDNILPFWINHTVDTERGGFIGFIDQELKPERQADKGLVLNARILWTFASAHRLFPSEEYLETAQRAYDYLLEHFLDREHGGLYWMVDCEGRPAQDKKQVYGQAFVIYALAEYALATSNREALDLAADIYRLLEKYSYDPVHKGYIEALSRDWKQTGDFSLSNKDLNEKKSMNTHLHVLEAYTNLYRVWKSPELRHSLSELIEVTLDHIIDPQKAHFWLFFDEEWQVKSRHISYGHDIEGSWLLVEAAGVLGDPALLQRVKETAAAMAEAVYNEGVDKDGGIWNEAGPSGLTDTNKDWWPQAEAMVGFYNAYQLTGDERYRTAAANSWKFIQTYLIDRERGEWFWGVDQSGASLPGEPKVSPWKCPYHNSRACLEMLGRLQG | Function: Catalyzes the reversible epimerization of cellobiose to 4-O-beta-D-glucopyranosyl-D-mannose (Glc-Man).
EC: 5.1.3.11
Catalytic Activity: D-cellobiose = beta-D-glucosyl-(1->4)-D-mannopyranose
Sequence Length: 396
Sequence Mass (Da): 45779
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A0A183J8R7 | VVVAPPSLYIQHVRHALTKKVEVAGQNCYNVAKGAFTGEISPAMLKDVGCSWVILGHSERRQIIGESDQFIAVKVKHALSENLGVILCIGETLEERKAGETLEVCTRQLQAVL | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
EC: 5.3.1.1
Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
Sequence Length: 113
Sequence Mass (Da): 12309
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A0A6T7I828 | CWFEDEETGTALRWQLFAGVLYDLRRRPAGEEEETSSSSFTLPWKIRVHFSLYPSSQLLELDDSGEYGIMTTVERTFRNSLKQALFLQYASSKVAMNMNKLSHQKIWDAVVHSNYTLYQEVNTDLQAISGDVPERQPDEDRNNNNNNSKAAPPQQIPVRLLINHKPAIQRPCRDLTITLGDLLNEWIPESFLVDMKEPSEHLLSWSVQGIQPPLSASVLDLWKGLCHPDHFLYITLITR | Function: Involved in autophagic vesicle formation.
Subcellular Location: Preautophagosomal structure membrane
Sequence Length: 239
Sequence Mass (Da): 27483
Location Topology: Peripheral membrane protein
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B5SQA9 | DPDNYIPANPLNTPPHIKPEWYFLFAYAILRSIPNKLGGVLALVLSILILMIIPLLHTAKQRSMMFRPISQCMFWILVADLFTLTWIGGQPVEYPFVVIGQLASVIYFLMILLIMPITSMIENQL | Function: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
Subcellular Location: Membrane
Sequence Length: 125
Sequence Mass (Da): 14259
Location Topology: Multi-pass membrane protein
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T1FUZ0 | MQNDWIKCIRQEINDFKWPPSKNARICSDHFCNKDYKGYDGERKVMLKKAFPCFQDIKKVILSYLFNNFNKIVLNNYSQCHFINTTLKGGYKTLMQFSEISKYTIVTYDLGDKKSPSNFPPEGGYMKAKMDKLEKQSCAKEKRSNIFRGISIYVNGYTDPTSEVLKRLVTENGGTYQYYYLKSRVSHIIATNLPKSKIAHLRDEKVVRPNWIVDSVSAGKLIPCQNYLLYNQHSTFFDSLKDFTSSKSVMNLNTSKPSTSFLTSFENSLSPTTTTANNDVTMDVSNDEEAPAIRVKKVGNELIDDHLNDQLPAYGEADDWGEDDEEDENVSECLRSTDHLQDVSRVSNSSSANAEGDDATQLNQSSNISSEPLNRNENLREHHQHSPQPQLPPANPSIISKQSPAGGFQINNVSEFFNKSRLHHISQWKLDAKSYVTRLQKLATKSGSGGVHKFPGREKLMKLKITEEDVVPVVPNGDGDVYIPEASNGDERVYAHIDLDCFFVSVALINRPDLRGKPLAVTHLRADDANRQGFNSKSDIACCSYEARQAGVQNGMLFGHAKKLCNDLVAVPYDFEAYQRVSKVFYDVILSFTLYVEAVSCDELFVELTQLMKVTSATAEEIVTCMRKDVFEMTQCTCSCGVGSNMLVARLATRKAKPDGQHFVERGGEREFMRGVQVQDLPGIGYSLHDKLKSMNLVTCGDVLRQRTTLHQLQQTFGSKMSEADSFLADLSKEVSRRLTLINKKGKHITLKVKVRSAGAPKESYKYMGHGICDNVSRSSTLKVATNQADVISRECANLFRTFKIGIQISSLESTAQHRQHLTISSSSRPSSSLSTSTNHTNNIRKYATKMDAPLQRHITNESGADVNETLHFNDDNNNNNNNNNNNNNNNDEFSLSMSQIDLETMRELPSEIQNEIREALCNKKLKQQHQQNDVHNNIVSNNKNNNNKQNDVSDKRERNIIDSFNNVEKIQQQHQLLLLRHIFNQRRSSAQVDEASSRIESNRISLKAQTKPSFQLSVSRWN | Function: Deoxycytidyl transferase involved in DNA repair. Transfers a dCMP residue from dCTP to the 3'-end of a DNA primer in a template-dependent reaction. May assist in the first step in the bypass of abasic lesions by the insertion of a nucleotide opposite the lesion. Required for normal induction of mutations by physical and chemical agents.
EC: 2.7.7.-
Subcellular Location: Nucleus
Sequence Length: 1023
Sequence Mass (Da): 115602
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A0A183IMW4 | MFKLTRCQHEDLLLRTFDFPIRFVAAPKSCSVGRIAYVVYVPVALSDFDLRELIRSTWARNFKADSTVKFIFVVGSHWLNESSMVRLDSEMRRERDILRSDTIEHYYNLTLKTYAVFKWIHRYCRHAKYVVRADSDTVLKKDNLDHFLKASGQTLKRTIVGHCHQFHCPTRYPSAKNCIPFSSFSTGLLPRYCFGFSNVISGDLVSQMLRHWQSLPYFHLEDIFLSGILAEALGDVQRVDRQDLFDYQTRFDSFACDMTQIASASYPSIEQQREHWTKYLNRCHRS | EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 286
Sequence Mass (Da): 33581
Location Topology: Single-pass type II membrane protein
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T1FZ20 | KDCCICCDSLKNVSSFPADDDESCEDNPNRVIKLHKCSHVFHYNCLLAMYNSGKKEGSIQCPSCKYIYGIKYGDCPSGSMSYEILNNCSLSGYPDCGVIKITYDIKNGIQESFHPNPGKQYTATGFPRYGYLPHNLDGLKILQLLKKAWFRRLTFTIGTSVTTGRANVVVWNEIHHKTEMDNKSGHGYPDPEYLNNVTKELTFHGVVEKDDNELEYND | 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: Cytoplasm
Sequence Length: 218
Sequence Mass (Da): 24658
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A0A350IEH7 | MMIDNFHIITLTHQTINVDQIGHFVVKHQTKDDLKDKLTQVKNQFDIDEIVYLSTCNRVSYIFYRENELEENYLKQFFHSINPELSEDRLNKLSNFVRLHSGIKAINHLFELSASIDSLVVGEREIFRQYRESYDQSVQWSLAGDHLRMLDKYTVTTAKEIYANTKIGEKPLSIVSLAIKSMLNINPDPSQRVLLVGAGETNRLVGKFLKKYNFTDITIFNRSLDNAKELSSTLGAKAYHISELSNYAEGFDILVVCTGSTETIISTDIYSQLINRDESKKIVIDLSVPHNVDEDVQNGFDMHYVNIEELRTLAEQNLEHRKNEIGLAKKIIKGRLFEFQKVYQQRQIEKAFGKIPQEMKAIKERAVNTVYSKQIESLDDDAKALVIEMMNYMEKKCVSVPMKVAKEI | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
Function: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
EC: 1.2.1.70
Catalytic Activity: (S)-4-amino-5-oxopentanoate + NADP(+) + tRNA(Glu) = H(+) + L-glutamyl-tRNA(Glu) + NADPH
Sequence Length: 408
Domain: Possesses an unusual extended V-shaped dimeric structure with each monomer consisting of three distinct domains arranged along a curved 'spinal' alpha-helix. The N-terminal catalytic domain specifically recognizes the glutamate moiety of the substrate. The second domain is the NADPH-binding domain, and the third C-terminal domain is responsible for dimerization.
Sequence Mass (Da): 47060
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A0A967ZP66 | GRAELVVQKLTEIGVDRIVPFTAERSVVRWDDDKAARNVARLRRVAREAVMQSRRAWIPRIDEVATFEALAGEPGAVMAERGGAPPEWRSGIVLVGPEGGWSGAERAAPLPRVALGAQVLRAETAAIAAGVLACALRDGRVANVE | 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
Subcellular Location: Cytoplasm
Sequence Length: 145
Sequence Mass (Da): 15471
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A0A945B941 | MKSLLIVGFGGFLGAISRYLINIFMLKIVSSSFPWSTLLINVLGSFLMGALVEVFSQKINFSYELKLLLFVGFLGSFTTFSTFSLDAVSMFGRGENLYSFLYISLSVLLSVGSLIFAMHIMKSYIL | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Location: Cell membrane
Sequence Length: 126
Sequence Mass (Da): 14000
Location Topology: Multi-pass membrane protein
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Q45RR2 | MEPETSTARTAEHALSWTRRGALIILEGVDRSGKSTQCRMLVKALLEMGVEAELMRFPDRTTPIGQMINSYLLNKSDLDDHVVHLLFSANRWEAASDLKRKLMKGTTIVLDRYAFSGVAFTAAKPGFELEWCKRTDVGLPKPDLVVFLAIEASAVESRGGFGDERYEVSAFQAAVRENFEVLMKDVTVNWRKVDAARTPEQVHGDILRLTDDAHNAIYDSRDGFDDTIPTLWS | Pathway: Pyrimidine metabolism; dTTP biosynthesis.
EC: 2.7.4.9
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Length: 233
Sequence Mass (Da): 26137
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A0A967UQA7 | GPDLPARKLVEEATEVLVAAKDHAAGAADDRRLAEEVADTIYHLLVVCAERGVAPADALAILVERSR | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
EC: 3.6.1.31
Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-ribosyl)-5'-AMP + diphosphate + H(+)
Sequence Length: 67
Sequence Mass (Da): 7089
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A0A0B5QHF6 | MTELKQVYKCEICGNIVEVVHNAGGTLVCCNQPMKLKAENTTDGATEKHVPVIEKVEGGVLVKVGSVEHPMLDNHYIEWIEIHTESNVYKKFLKPGEKPEAFFKVDEPVLFAREYCNLHGLWAEKNS | Function: Catalyzes the one-electron reduction of superoxide anion radical to hydrogen peroxide at a nonheme ferrous iron center. Plays a fundamental role in case of oxidative stress via its superoxide detoxification activity.
EC: 1.15.1.2
Catalytic Activity: 2 H(+) + reduced [rubredoxin] + superoxide = H2O2 + oxidized [rubredoxin]
Sequence Length: 127
Sequence Mass (Da): 14342
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A0A099YAV8 | MINLFDKWDQAARDFRLAQLIAQLKLPTVVIHDDGFLPRKVQSPLQYYCPRSDEGQPLYFDQIPVPRFWRIVGSSRGAQIYDLNHKRADVVFTKNDNTRQVKQVRWLNDSGQLQWVDEYDRFGHLFAKTSWADNRAWLKQFFDEQGQVVIESHLDNGSLFLNTRQERRHFKSLPDFVSSYLQKSGLNLDRIFYNTLSTSFLTTLKLPKSGHDTLFWHEPVQNKLPGNLDYIYQNETRTRHVIVQDYRVWQNRQKLFKTNQHVATDYLGIVYPHPRGNSLRPAILILTNSDQIMQLENLVKILPQFEFHIAAITEMSDRLMGMQKYENVYLYPVVKMDTARNLMRKCDIYLDINQGDEILDAVRAAFENNMLILGFNETMHEPRLIADENRYAAAEFDKMAIKIVQAVSQADEMQRLIDTQRQQAGDEPAARFQAGIEALIND | Pathway: Protein modification; protein glycosylation.
Function: Required for polymorphic O-glycosylation of the serine-rich repeat protein in this bacteria. A stabilizing protein that is part of the accessory SecA2/SecY2 system specifically required to export serine-rich repeat cell wall proteins usually encoded upstream in the same operon. The GtfA-GtfB complex adds GlcNAc from UDP-GlcNAc to the substrate protein, attaching the first sugar residue. Stabilizes the glycosylation activity of GtfA. Has no N-acetylglucosaminyl transferase activity on its own.
Subcellular Location: Cell membrane
Sequence Length: 442
Sequence Mass (Da): 51694
Location Topology: Peripheral membrane protein
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A0A7C4I3Y9 | MKIMQHPLLSDILRLCRVYGIRPRRKYGQNFIVKRTFLERMVNYADLDDNDVVLEVGAGFGILTEIMAKKAGKVIAVEKDPKIIKALQDRLRDFNNVEIVHGDVLKVNLPTYNKVCANPPYSISSKLLFKLLEEKPETIILTLQKEFVDRLIAAPGTKEYGRISIMVNYKATVKVLEYVPREYFYPKPKVDSALVEVRALREPVVKVADERFFTLLVRELFTQRNKTLKKALRLALHNLNARYEIPASLTYILSKRIYELTLEDCALITNELLSMREYPS | Function: Specifically dimethylates two adjacent adenosines in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.
EC: 2.1.1.-
Subcellular Location: Cytoplasm
Sequence Length: 280
Sequence Mass (Da): 32364
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A0A8T5JHV6 | MSYPNQIRLVRFITFVAGAAVMGLEIMASRLLAPRYGDTVYVWGNLIAVIMGALAVGYRRGGIAADKYPNINRLSNLIFNAGVLIMLVPVTTPLVLEILGGFNLGNSIGSLLASVVLLFAPTVYLGMVSPYAVKLCVDDVVKIGGVSGGLSSINTVGSILGTFFTTFVLIPRFGTREIISSLGVMLIVISLIGRKGRYVVTVLCIVAVLMIPNTLIMGRLGTIGSSPVYSASSSYSKITVVENEGQGIRTLYLAEMTQSAMYMNGSTKLVFRYTDLFNLGFGYNPNITRVLFIGGGGFSSPKQFLSDYPWVDVDVVEIDPKVVDVAYRFFEIPTAEPRLTVSVGDGRQFLEDAGQYDMIVLDAYSPTYIPFHLMTVEFQEMVREHLNAGGVVISNIIGSLVGDTSELLWAEVSTVGAVFPHVDLYRTKETLGSVVQNMVLIAYKSTEPVSGAILRSNLIDKFGDTKRVTSYMKARIGADTPETELILSDNYAPVDTLLNPVTLNAYNEQGTQDTESMISPYLIVAMWVLALGILFGASTYLE | Pathway: Amine and polyamine biosynthesis; spermidine biosynthesis; spermidine from putrescine: step 1/1.
Function: Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to putrescine (1,4-diaminobutane) to yield spermidine.
Catalytic Activity: putrescine + S-adenosyl 3-(methylsulfanyl)propylamine = H(+) + S-methyl-5'-thioadenosine + spermidine
Subcellular Location: Cell membrane
Sequence Length: 542
Sequence Mass (Da): 58807
Location Topology: Multi-pass membrane protein
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N6TL25 | MKNESESPEKNLEEGTSLSKRAKKILIPPNSPKSVKTKRANFLIRKLKLKSKSVPVRAELAEIAQPSQSSSPQPAERQTPEGDENFRLAKAASETNLQDSWKSSETIEKDTTSATSFTKSEISVDYSEFYVSSEPRKSILERAKSLENLRKMPAYGELILDSAALVSNANANKPKDHLYKILVIGDLGTGKTSIIKRYVNRFFTQHYRATIGVDFALKVLKWDENTLIRLQLWDIAGQERYGNMTRVYYKEAVGAFIVFDVTRRNTFESVANWKTDLDSKVQLPDGSPLPCVLLANKCDQQKEGLVTNPAKMDEYCRENNFAAWFETSAKDNINIDEAARALVEKVLEKDSIINSEKKNDTFSITRDSNESSEKKCAC | Function: The small GTPases Rab are key regulators in vesicle trafficking.
Subcellular Location: Membrane
Sequence Length: 378
Sequence Mass (Da): 42599
Location Topology: Lipid-anchor
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A0A948RMA5 | MISYIEGTLIERGADHLVVGVGGVGFEVKAPAGTVDKAPEVGGKVSLFTHLHVRQDVLALYGFESARARDLFVKLMSVSGFGSQKALSVLSIFSPDGFIKVVQAGDSDALTIIPGVGKKGAERLILEMKDKVEPAGEDLTGIPVGGLQPFQEAAEALVQLGYSRSEAHAALKSFPSPDEGTTVEEMLQWALKSAR | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. HJ branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Subcellular Location: Cytoplasm
Sequence Length: 195
Domain: Has three domains with a flexible linker between the domains II and III and assumes an 'L' shape. Domain III is highly mobile and contacts RuvB.
Sequence Mass (Da): 20594
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G7IEK4 | MAFKHRSIAYLLSILLFVSLHVANGIPPETICGSTVNPTYCKNILANQNGNKKYLMMVGEGINQTVITGDHNVVDGFTTFNSATFAVVGQGFVAVNITFRNTAGPSKHQAVALRSGADMSTFYSCSFEGYQDTLYTHSLRQFYRECDIYGTVDFIFGNGAVVLQNCNIYPRLPLSGQFNSITAQGRTDPNQNTGTSIQNATIKAADDLAPKVGTVQTYLGRPWKEYSRTVFMQSFMDSFINPAGWHEWNGDFALNTLYYAEYSNRGAGSSTVNRVTWPGYHVIGATDAANFTVSNFLSGDDWIPQTGVPYSSGLI | Pathway: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5.
Catalytic Activity: [(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O = [(1->4)-alpha-D-galacturonosyl](n) + n H(+) + n methanol
EC: 3.1.1.11
Subcellular Location: Secreted
Sequence Length: 315
Sequence Mass (Da): 34535
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A0A2K9AYA5 | MVSDNSSVRKSHGNANKPALVITDYTGWRSLLNPLWCYNGFRMAVVGLTCFGLIMVFSSSTVTMAAQGKSPFVQLLNQGVFCILGLIVGFFAMVMPVGFWKRIGLPLMLCSILVQALTFTPLGIDVYGNRGWLNLGFTTIQPAEFMKFALCVWLPTALRAAKKLYRKQGMKAYTVPLGVSAVGLLTVIGGKDLGTAMILIFIGIVAFLIAGFPGKWMGIGVLVMAAMVAVLAISSPNRMRRILATYGDCSAADAQTVCYQSMHAKYAIASGGFLGVGIGNSREKWNYLPAAHNDFIFAIIGEETGFVGCAIVLLFFAILGWCMIVVALQVADRYVSMVLMCVTIWIVGQAMVNIGVVVGVFPVLGVPMPFVSAGGSSMVMCLAAAGLVVGLMRCQPQIKQSRQSV | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Catalytic Activity: [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+)
EC: 2.4.1.129
Subcellular Location: Membrane
Sequence Length: 405
Sequence Mass (Da): 43395
Location Topology: Multi-pass membrane protein
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T2MH45 | MSVSAFICRVARSRVGFFQHKNTKSIIFITTEIQKLQNSNSNFELSRNICSSASPFSHKRLFTSCWENQGRLNDMSIKRNYATMPPHEKVLLPNLSPTMTTGTIVSWEKKVGDKINEGDVLALIETDKSTMEMETPEPGYLAKIIVPVGTRDVAINQLIAIIVSNEEDLDAFKNYTGEETTKTLDAKLDASPSTVASHSPPVVEEPPPPSSTNRVFASPLAKRVALEKGIDINNVVGSGPRGRITVADIENFKTPLIAPKIEKVTAAPISKQPSPELQSTPSVFQPSLVQPPVAEGVMFKDIPLSNMRKTIAKRLTESKQTVPHYYLTSEINMDKVFELRSQLNAESLGAFKLSINDFVIKAAALSLRKVPECNSQWFSEYIRQFENVDVSVAVSIDGGLITPIVKDADKKGLTAISADVVALANKARDKTIQPHEFLGGTFTVSNLGMYGISNFSAVINPPQSCILAVSASEDRVVPDQTSETRMKISKMMSVTLSCDHRVVDGAVGAAWLKTFRGYLEKPITMLL | Cofactor: Binds 1 lipoyl cofactor covalently.
Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).
EC: 2.3.1.12
Catalytic Activity: (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + acetyl-CoA = (R)-N(6)-(S(8)-acetyldihydrolipoyl)-L-lysyl-[protein] + CoA
Subcellular Location: Mitochondrion
Sequence Length: 527
Sequence Mass (Da): 57775
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U3U6Z8 | MEQEYCIEQLNNRYKVIDFMKSSTLAFISSTVLVIISITIMNFKGFNWGIDFTGGTIIEIRLKKTINLKSLRETLAKVGFHELLVQRFGNSHDIILRIPPVHKLATQELGSKIVSVIKNTFHQNAIIKRIEFVGPSVGSDLIQTAALALMSALIAILIYISYRFEWRLACSIVLALIHDIIINCGILSFCHIELDLTTLASLMSVISYSLNDKIVISDRIRENFRKINSSFSYNIINISLTQTLNRTLITSITTLLIILILFIFGGVLLKSFSLTMFIGVVIGTISSIYISSALVLKLGIKREHLLIQSIEKEGLNN | 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: 317
Sequence Mass (Da): 35582
Location Topology: Multi-pass membrane protein
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A0A3D4A074 | MAGTSTQPPTITDDGSRPPGESQRGFRYFSNILVDKFEWFFVSFIYVCGWSAILFVLAIFFFVFIEGLPAITGSGEGQLDLVDFFTNEKWIPESAKKPQFGIFAMLMGTLSVTVLSMLIAVPLGLGAAIYVSEFASNKTREILKVLIELLAAIPSVVWGFVGYMVLGPILLDTFDSAVVGINLLNGGIILALMSVPVIVSMSEDALRAVPDSYREAAMALGANRTEMVFKVLFPAAKHGLLAAVLLGVGRAIGETMAVLMCTGHAVQIPEGLLDPVRTLTATIAAELGETAPGDMHYQVLFVIGIVLFTFAFLINIIADVIVKGIRMEKHG | Function: Part of the binding-protein-dependent transport system for phosphate; probably responsible for the translocation of the substrate across the membrane.
Subcellular Location: Cell membrane
Sequence Length: 331
Sequence Mass (Da): 35630
Location Topology: Multi-pass membrane protein
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A0A0B4KJH9 | MDGFGSDFSAGGSGGKVDTGTIMEQVKVQIAVANAQELLQRMTDKCFKKCIGKPGSTLDNSEQKCIAMCMDRYMDAWNTVSRTYNSRLQRERARM | Function: Mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space.
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 95
Domain: The twin CX3C motif contains 4 conserved Cys residues that form 2 disulfide bonds in the mitochondrial intermembrane space.
Sequence Mass (Da): 10566
Location Topology: Peripheral membrane protein
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A0A248UIG1 | MQGTIAVALGGALGSVLRYWFAIWLAPVSRDLPWGTIVVNIIGSFAIAFFGALTMASSRFEVPEIWRLAFMVGICGGFTTFSSFSVQTFELLRLGMPGRALLNVSISLFACLAATALGYVAAQAISRV | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Location: Cell membrane
Sequence Length: 128
Sequence Mass (Da): 13642
Location Topology: Multi-pass membrane protein
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A0A7C4I1W6 | MSGELVSGVPSLGYPVKQVFEGDIVLLVPDGEVLGRQRADSIAFYNPAMELCRDIAVSCLQVYQRTLNQGLIIAEPLTATGVRGLRYAKEVKGVEKVVIGDVNPEAVKLAKVNVAINALSDKVIVEQADANLLLSVYVARKTRFNAVDIDPFGSPAPYISAALRSLRDGGLIAVTATDMPPLCGVHPMVAERRYGGTSLRSDFCHEVAVRLLLSAICREAGKQDLGIEPLLCHFTRHYVRIYSRIRVGAVKADASFRSLGYAVYCPKCGFRSLISGGIGIDVPNRCKNCGNKLQRAGPLWAGRIQDKDFCTNVLREVEARSFKLKNLELRLLKLLQAEAEGPPLYYVLDRICHLAKVAEPSLEAVISKLRSNGFKATRTHFNLKGVKTDAPITRLISIVKELRRS | Function: Dimethylates a single guanine residue at position 26 of a number of tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.
EC: 2.1.1.216
Catalytic Activity: guanosine(26) in tRNA + 2 S-adenosyl-L-methionine = 2 H(+) + N(2)-dimethylguanosine(26) in tRNA + 2 S-adenosyl-L-homocysteine
Sequence Length: 405
Sequence Mass (Da): 44372
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A0A967UER1 | GLTLARKILLGDTLKEQKKNINKYDDSLGCTIGEELLKPTQIYVKPILEMLDSGIDLKAMVQITSEGYGNLNRVQSEGIKFVIDPLPDPLPIFELIQSWGEISDAEMFKVFNMGIGFCVVVDSANDADVVHTICNKYDISCHGIGFVDSSSRKLVEIPEKKLILDKEKGLFNI | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 2/2.
EC: 6.3.3.1
Catalytic Activity: 2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ATP = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ADP + H(+) + phosphate
Sequence Length: 173
Sequence Mass (Da): 19220
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A0A9D9CB96 | MLNVIIFGGPGSGKGTQSKLLAEKYQMTHLSTGDLLRAEMEKGSELGRIAKSYTDGGNLVPDEMIIKILAATIDEKKDAKGFIFDGFPRTVAQAEIFDDLLKERGYKLDALFELVTPDEVLIERMLSRAQTSGRADDNPETIRKRVEVYHQQTAPVLDFYKARSMYTPIDGMLSIEGAAQAVADEVAALL | Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from ADP: step 1/1.
Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Catalytic Activity: AMP + ATP = 2 ADP
EC: 2.7.4.3
Subcellular Location: Cytoplasm
Sequence Length: 190
Domain: Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis.
Sequence Mass (Da): 20915
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T2M9V1 | MSLCECINTEENQNILKSSKVVVMETCKSESDEDLIDCHSKERNNVLCNKHEIKCTNSEEDNKEETIPNDNINKIEETKDCHLKSSDEILEKIFIVNDNVNEVSIDKSVDENFEYCSEPKPSCNKEERNLFIENNPTIVKQNDTYHLKWFEWKGEQTPVVTQNENGPCPLIAIGNVLVLARKITIPKMQQFITAKQLIEHIGDCILAEFPKFNESEEVQLNHAQNLEDAIDILHKLQNGIDVNVKFGGVTDFEFTRECIVFDLLRIGLYHGWLVEPQDEVTLKAVNGFSYNQLIDKIISKSDDSESLAESIAIEDFLSRTASQLTYHGLCELNLTIKEEELCVLFRNNHFSTLYKHKGELFILVTDQGFLTEPAVIWETFSNIEGDGQFVNSEFKSVVFESDKQTSKSMSPTLSKRQSLCQEDRDYLIALQMQHDEQGLYSRSPSNDYSDSDRALAASLQTQENELASYPQQHSYQNPQENLSQSQNRTEASRNNDTQQGKNKCCIL | Function: Hydrolase that can specifically remove 'Lys-48'-linked conjugated ubiquitin from proteins. Has exodeubiquitinase activity and has a preference for long polyubiquitin chains. May play a regulatory role at the level of protein turnover.
EC: 3.4.19.12
Catalytic Activity: Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
Sequence Length: 507
Sequence Mass (Da): 57984
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A0A0M6WV69 | MLTGKNALVTGASRGIGRQIALTLAAAHAFVIVNYNGSKEKADAVVAEIKAAGGDAVSYQCNVSDFDECQNMITALIKEYKHIDILVNNAGITRDGLIMKMSEADYDAVLDTNLKGAFNTIRHMSRYFLKQKSGRIINISSVSGILGNAGQANYSASKAGVIGLTKAVARELASRGITANAVAPGFVETEMTDVLADAAKENLLSQIPLGRPGNTKDIANAVLFLASDAAGYITGQVLSVDGGMAI | Pathway: Lipid metabolism; fatty acid biosynthesis.
Function: Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis.
EC: 1.1.1.100
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] + NADP(+) = a 3-oxoacyl-[ACP] + H(+) + NADPH
Sequence Length: 246
Sequence Mass (Da): 25697
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A0A938EQC9 | MLATGNKDKVRELEALLAGTQVTAAPDGFDPDETGTTLVQNARIKAEALRPDAPADAWVVADDSGLFVHGLDGRPGVYSSRYAGPDATYADNCNLLLTELGDSHQRGAAFACVLYCIAPDGAVLISSGVLAGEITREAAGADGFGYDPVFRPRSDQRTLAEMTRDEKAEISHRGRAARGMARMLGIAGADGGADAQEAAA | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.
EC: 3.6.1.66
Catalytic Activity: H2O + ITP = diphosphate + H(+) + IMP
Sequence Length: 200
Sequence Mass (Da): 20808
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V6LFZ1 | MQKFFSTSLTLLTTIFELLYFQQQLTNLQFTISLLLPINFCVSIIRVQYFTHPQNLEMQGSKFCQFCQTSRPLQTRHCRACNLCRQRFDHHCQFLNSCVYGQNFNIYVKIYITGSIWGLFGLFVLKNKLSWAVSLTAFVQYFRGYFILCRVRFITGVTVTEQKNNIVADFNYQLWKQKLGGSMLLWLFNPFVRVNEG | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 197
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 23245
Location Topology: Multi-pass membrane protein
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A0A6A4T9X8 | MEVLSVLNLGDIAQVFSKMGMFPVFDLAYYIVSILYLKYEPGSVEVSRRSPVASWLCAMLYCFGSYILADVMLGGSPIDYFQYNSHILLASAVWYLLFYCPMNLFYKCVAFLPVKLVLVALKEVVRTRKIAAGVHHAHHAYHHGFFIMVIVGYVKGSGVALISNFEQLLRGVWRPETNEILSMSFPTKASLYGAILFTLQEAQWLPVSKSTLILAFTLFMATSKVVMTARHSHGSPFALIESWVCHLLFGSALGGPEEDHHHPPAPSSSPLKTKEELGDGTRKRKAKKAE | Function: Monovalent cation channel required for maintenance of rapid intracellular calcium release. May act as a potassium counter-ion channel that functions in synchronization with calcium release from intracellular stores.
Subcellular Location: Membrane
Sequence Length: 290
Sequence Mass (Da): 32340
Location Topology: Multi-pass membrane protein
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A0A3D4A5B2 | MQCSSVEGMMTYTLDLFRSFIKRASKCIMLCNWQRESTFLRSIFLIPPVTSLLTRMLGILNLNKPPGMSSRDAVNAVVRCTGRKIKVGHAGTLDPIAQGVLIVLIGKATRLADFVHHYPKSYSGTFRIGYQSNTDDSEGEVVQIEDAPEITLGDLQDACSAFIGEIQQVPPRFSAVKINGKRAYKLARRGESVDIPPRQVTIHNLEVSRYSDPEFDLEMTCSTGTYVRSVGRDLARNLGSQAIMTDLTRSSIGPFGISDSISVEELKKLDANSLEQKLLSPFMAISDAPVIKLNSELVKMICNGRFIDDPNGGEQTWLGCTDESGNPIAILKRTDDGQLRPKVVLRPDV | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
EC: 5.4.99.25
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Length: 349
Sequence Mass (Da): 38472
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A0A7C1A7V9 | MNTSSRDGLTLPTIHSGHRQRRSPMGKLRITSTVIAALAGGVAARRVYERLARFEISEVSMTPTLRPGDRVLTWERTPKRGDIVVFEHPARPEFWLVKRVIGLPGEQVTIRDGRVLVDGSILEEPWTDESSGPDTEWSLDAHEAVVLGDARRLSAGDSRQLGPLPVDALLHTVIARYWPNPARIA | Catalytic Activity: Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
EC: 3.4.21.89
Subcellular Location: Membrane
Sequence Length: 185
Sequence Mass (Da): 20527
Location Topology: Single-pass type II membrane protein
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A0A7R9KZL0 | MVGFSADRFVDLSGDHPLVLSAEDFTCGICLHVFNNAVDTQCGHTFCYHCLHRWLSRADHKTHALKDCPECRQILATRKRPLRESVTDATVMLISGLEIPYTPCRRLNSVIDKLRIKCQYEWNGCPEVCPLESLLAHQMSCEHRKCRECCLPAGLSAEDHNCVQLLARDRNEWIRKYKAVLREKQEMSEELTQLSAQMDSLAETHALPNRSAIHSVLFGKFMTTGQSIEFTEEAIRLTNIITENSSTTFKHNVVIQYVDLQSMSICADPSLPLMAIKPNSECALKIVNWLSIAPFLLDVESKDKSRIVIVFKYIFTDLFAIQVINRCKLLNSECKCKTIGATEAQSLLDGRT | 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: 352
Sequence Mass (Da): 39871
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A0A7C4JBQ1 | MKVIPAIDVVSRKVARLYMGDIGKATVYQLRPIEALRKWEQEGAEIVHIVDLDAAHGRGSNMEVILQLIAEANVEVQVAGGIRSLDKALMLLEAGASRVVIGTVFIEKPELAKEFIRQLGSDKVIVALDHFKGKVAIRGWREITDRPLIGEVRRAKEMGFNWVLISSIERDGTLSGINEESIEEIVKLGDIKLLVAGGVSSLDDVVKAKRAGAYGLIIGKALYEGLINLREAIRVGLREV | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 4/9.
Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide = 5-[(5-phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
EC: 5.3.1.16
Subcellular Location: Cytoplasm
Sequence Length: 240
Sequence Mass (Da): 26284
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A0A967JX17 | MIDIKFKHLFYVSNLLSILRFFFLIPIFYYLSKTGTYADIMVLVCIAVAALTDVFDGYFARLLNQKTDLGKILDPLADKIIIVVGMLGLVIHRGFPLTLVVFLGYRDLMILIGGLLIARRSSEIIESNFWGKANTFMAATTAFVFVLSDGWWGAYILMVLTYLSILFSGTAYMFRGFERLQVNIGMRFLWGIIFLIPVFLIFYLTPGHLLGMD | Pathway: Phospholipid metabolism.
Subcellular Location: Membrane
Sequence Length: 213
Sequence Mass (Da): 24231
Location Topology: Multi-pass membrane protein
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A0A2D5YBD8 | MKRNLHNDSLASLDGPVAILGDGISGRAAQKLLHAKGRVADLFDEKNRIFTESHAQHYSFIVQSPGFRPDHAWLKLAVDQNIPVFSEVDLGLSYSDHLEVVAITGTNGKTSLTSILGHITKRLNMDSIVLGNIGVPISDGVAGDSVRKKIIFHETSSFQSLTSRSFYPDAVLWTNFSSDHLDYHRSDREYFMAKLKLADNCAHPENVMIGSSVWAVARKFGIKLNPKFQVIEALTCRDLPGNVASFHKSIPQLENLAFAVHWAKQQGIAKAEFFEALQGYQPHPHRLHKVTTINGVSFWNDSKSTNFASALAACKTFSNPVIWIGGGKSKGEETEKFCAHLHPFLQSAFLIGETAEELAAKLALRGIKAEVFDNLKGAVLRAYKFAKGYVDVLFSPGFASFDMFSNYIERGNSYESLVFDLKSACQVTTKLPVNNLHASY | 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-muramoyl-L-alanyl-D-glutamate
EC: 6.3.2.9
Subcellular Location: Cytoplasm
Sequence Length: 440
Sequence Mass (Da): 48622
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A0A0A1RW80 | MANVLMGLQIVLSIILVASILPQDSKSAVPTEFGGEGTQSYFKPKGKEAFLGRVTKISAVLFFLNALALVIIK | Function: Involved in protein export. Participates in an early event of protein translocation.
Subcellular Location: Cell membrane
Sequence Length: 73
Sequence Mass (Da): 7794
Location Topology: Multi-pass membrane protein
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A0A4U9Z2U7 | MEFTYQYTGQGQQVKYFLKEQGVSKGLLAKIKFQGGKIFVNDHEQNVLFSLAQNDRVTIVIPPEGEHETMLADPTPIEIVYEDAHLLIVNKPAGISSIPAQYHPTGTMANRVKAYYQAQHYEDQVIHVVTRLDRDTSGLMLFAKHGFAHAKLDSQLRKKQVVKKYQALVAGDLSALSAHSEIDLPIARDLTSLLKRKVSEEGKEARTEYWLKQRNSDCALVDIQLHTGRTHQIRVHFSAIGCPLLGDEMYGGPMAFGIRRQALHCCQLQFQHPFTNEPLAFELPLPADMAAVCSAIDKQ | Function: Responsible for synthesis of pseudouridine from uracil.
EC: 5.4.99.-
Catalytic Activity: a uridine in RNA = a pseudouridine in RNA
Sequence Length: 299
Sequence Mass (Da): 33566
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N6T3Q9 | MADVLSEIVLPEDLKKFEKIYHEQLYRNDVTPKAKFEYAWCLVRSKYPADIQKGIVLLEDLYRNDVEGQRDYLYYLAIGNARIKEYAKALGYVRSFLSIEPGNVQLISLKENITKKMQKEGQRGIFVAGGALLAVGALVGVGVALAKNK | Function: Involved in the fragmentation of the mitochondrial network and its perinuclear clustering.
Subcellular Location: Membrane
Sequence Length: 149
Domain: The C-terminus is required for mitochondrial localization, while the N-terminus is necessary for mitochondrial fission.
Sequence Mass (Da): 16786
Location Topology: Single-pass membrane protein
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A0A076JGN3 | MDIVVAITLFVLALLIGVEVIGKVPATLHTPLMSGANSIHGIVIAGVVIVAAHATSPLAWVFIFLAAVLGTMNVVGGYVVTDRMLEMFKSDKGKKKEEEAK | Function: The transhydrogenation between NADH and NADP is coupled to respiration and ATP hydrolysis and functions as a proton pump across the membrane.
EC: 7.1.1.1
Catalytic Activity: H(+)(in) + NAD(+) + NADPH = H(+)(out) + NADH + NADP(+)
Sequence Length: 101
Sequence Mass (Da): 10645
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A0A944ZIT4 | MRRISSSFLFVVLLVTAGVTRVSASDSVAPQLQRFARTEYLMGVDFRIDLYASSEMDAARAFKAAFSRIADLDRCMSNYRADSELSLLCTNTTKNMSTKVSEDLWKVLVYANRISYLSNGAFDVTIGRVTKLWRRARRRKEIPSEQRLAEELEFVGFEKLILNPADQSVMIRTPGLLIDLGAIGKGYAADEAMRILEDLGITRAVVNASGDVRFGAPPPDSTGWPTGIGALSAAGPPILLQSQSQGAVATSGDAFQFLEINGKRYSHILDPRSGMPVQVRSSVSVWAATGMAADALASAVSVLGPRRGLRLVRKLDGVEALVIWDRDGDGTGAMFRSRGFPLEK | Cofactor: Magnesium. Can also use manganese.
EC: 2.7.1.180
Catalytic Activity: FAD + L-threonyl-[protein] = AMP + FMN-L-threonyl-[protein] + H(+)
Sequence Length: 344
Sequence Mass (Da): 37444
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A0A946ADK3 | MRDLYPLSKRFDIRHVPVDDVHTLHVEQSGNPDGVPVVLVHGGPGAPWSRHNLRVFDPEHYWVIAFDQRGSWRSTPHGELKDDTTPHLVADMERLRELFGLERWIVFGGSWGSTLSLAYAEIHPERCAGLVLRGISLGRTMENQWGFHHSRQIRPQAWDALVASIPEDERGDLDGALMRRMLDPDPAVHWPVIKGWMDQAEELGRSRHPDLELDEEDLDTPETDVVCARISITYFANDIFLPRNSLLDNAHRLAGIPGAIIHGEDDFNCPLANARDLHKAWPQARYRPIRDAGHSALDRNIRLALVETMNDFKTLEVEQS | Catalytic Activity: Release of N-terminal proline from a peptide.
EC: 3.4.11.5
Subcellular Location: Cytoplasm
Sequence Length: 320
Sequence Mass (Da): 36415
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A0A352JVG7 | MGEFDKIMAKAFRLAEKGLGYTSPNPAVGAILFRDGEIIAKGYHRKAGLPHAEIEALNVAGERARGATLFTTLEPCSHFGKTPPCVDAVIAAGVSKVVSAAFDPNPLVRGRGFSRLKDAGIEVIFDVLKEEAVDFYRPYTKFITTGFPFVTLKYAQSLDGRLATKTGNSQWISSKQSLLYSHKLRAINDAIIIGRQTLISDNPQLTTRLVKGPNPIRIVVSASGKLPFNRAIFTDGLSSTYVATLSRAIRNSADHFQVISVRGGRKGLILKDLLSKLAKMGVMTALVEGGSRMLTSFLSQKAADKIVVCTAPILIGDGISAIGDLGIKKLTDSLKLVDVRIRPSGPDIIVSGYLDWK | 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: 357
Sequence Mass (Da): 38488
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A0A1H5X1S6 | MDTLLPAFIGIPGGPELLVVLLLVVLLFGADKLPKLARSSGQAMGEFRRGRNQIEDELREAAEPTPARADAESTERI | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system.
Subcellular Location: Cell membrane
Sequence Length: 77
Sequence Mass (Da): 8329
Location Topology: Single-pass membrane protein
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A0A2E8VWM8 | MPDLGKYAFSVLTSYGISFLLIGCLVAYILYRNYRIRIDLEKEDNS | Function: Required for the export of heme to the periplasm for the biogenesis of c-type cytochromes.
Subcellular Location: Cell inner membrane
Sequence Length: 46
Sequence Mass (Da): 5335
Location Topology: Single-pass membrane protein
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A0A7K3ISZ5 | MAYKADILLGHIIKLHGHKGEVIIKLGNDFRNKLPVLEWVFLEIEGKPVPFLISGSEYSGSDTLLLRFEGYDSSEKVKEFLNCKVFLTQKTTGITKSRDPENILGFKIHTIDNKLIGKVTGITENPGQLLLNVDTGSGNTVLIPLHENLISRIDRRRKIITMDLPEGLTELN | 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 not for 70S ribosomes.
Subcellular Location: Cytoplasm
Sequence Length: 172
Domain: The PRC barrel domain binds ribosomal protein uS19.
Sequence Mass (Da): 19279
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A0A7R9LPT3 | MANNCNDLHIGYDLTILQYIVMFVMYCINIVFAGVMSNIGTLTAAHRYGTHKAFKAKWPLRVILVVLQTLSGQKTLIEWARDHHTHHKYEGTNADAVNINRGFFFAHMGWLMLKRHPECEQKRSNVNVDYLWSDPIVRFQYNYYEPLVAVFCIIIPTLIPIYLFNETIVNSFHLCFLIRYAYTLQLSFCGNSLAHINYGSKPYDKSMTSVHNDHLIYATLGGAYHNYHHVYPWDYSESEFGWDVNFNVNTAFIDLFHAIGWAYDLKKAPKDMIEKRKERTGGQQKLNFIQKNPIYDWIYGFFLSSIAVWILLPTKAIYNALNEV | Subcellular Location: Membrane
Sequence Length: 324
Domain: The histidine box domains are involved in binding the catalytic metal ions.
Sequence Mass (Da): 37779
Location Topology: Multi-pass membrane protein
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A0S5U1 | MVSQCRQNFHQESEDAINNQINMELYASYQYLSMAYHFDQDDVALAGYFKFFKHQSDEEREHAQKLMKYQNKRGGRVVYKDVQGPQFQVSTPVSALEAALELEKKVNESLLNVHAIAGKHSDPHLCDFLESEFLDEQVESINEIAKLITNAKRCGDGLGVYQFDKLSLSS | 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: 170
Sequence Mass (Da): 19458
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A0A3A0DM47 | MAITIDEVKHLAKLAKLRFEEEELPKIAQELDAIVGYMEQLKELDVTDVPATSHVLDLYNVFRADKVEQENTAQDILQNAPAQKMGYFSVPKVIG | Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
EC: 6.3.5.-
Catalytic Activity: ATP + H2O + L-aspartyl-tRNA(Asn) + L-glutamine = ADP + 2 H(+) + L-asparaginyl-tRNA(Asn) + L-glutamate + phosphate
Sequence Length: 95
Sequence Mass (Da): 10714
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A0A1C2FZ87 | MRLLCDLGNTRIKWAWAEGATLSGFGSGDYSGVEAYTTRLTGSVRPTMIAAISVARHRNEAFVRFCEEQWALAPQWYPSLREGFGVSSLYEPPETLGADRFAALAGARARFPGQAVCVADCGTAITVDALDGDGVFQGGAILPGLSAAACALRLIAPRLTGSPGDRFYAAYGRTTQDAVGGGLMLGAAGAIERLFRDQGAVLGHDARLVLTGGDAARLAPYLSTPFEHVAHLTLEGLAVMVS | 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: 242
Sequence Mass (Da): 25365
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A0A072U1Y4 | MIPWDGIGCYFSGIALYCLGITICKDAEILKSVTRVNQLKELEQLLDTQNSALVVAISGKVASESTIECELSGLKGVIVEEAVEQHFLKHKHNDSWIKDSALTSFTSKEIPWYLEDSTDRVDVVGAQSAKDFVLPVKHEVFKPSNPRLISKALHYIRGLKELGFNRTERTLPIGTTVTVVGEVTKDDAGAIRIQQPRTGPFYVSPKTIDQLIIANNGNLLRWFKHASIGLAIVGSCLIANRTIQYILLRWRQCKLLKRVLDAAAKKSKQGIEGEIDDNFLAGGQGDLPDLCVICLDEKYNAAFLP | 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: 305
Sequence Mass (Da): 33752
Location Topology: Multi-pass membrane protein
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A0A946E2R1 | MRKLSVLLLTSACLFVSAPALAQSTDVQSLAHEMERLRNDLVDLQRFVYAGEGEALVVSPGLESSQDAAQFQLSLQQVEERVRLLTGRVEELEYQQRQLLARMDTLIADLERGAAVPSTGELVMSEDTVTADDGGAVDIVPNTTETTAGVAGAILPPGSEMDQYNFAFSLLRKADYEGAQMAFDEFITLHPDSELTGNAYYWLGSTHFVRDQYRDAAVAFLKGYQEGPTGPKAADNLLKLGVTLSRLGKPDEACATFKELSNKFPEAAQILLDEASDEAASAGCS | Function: Mediates coordination of peptidoglycan synthesis and outer membrane constriction during cell division.
Subcellular Location: Membrane
Sequence Length: 285
Sequence Mass (Da): 30849
Location Topology: Peripheral membrane protein
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Q8GUN7 | MELNLSSMATKIPCSGLIPIRSLLNPSKSLSHLPRVSFSVSSPHSLKLMTSTKLIAMASASSRDFEMSNLTALSPLDGRYWGKVKDLASSMSEFGLIYFRVLVEIKWLIKLSNIPQVTEVPSFSKEAHKYLQGIIDGFSMDDALQVKKIERVTNHDVKAVEYFLKQKCESHPEIAKVLEFFHFACTSEDINNLSHALMLQEALSSVILPTMDELIKSISLMAKSFAYVPMLSRTHGQPASPTTLGKEMAIFAVRLSVERRYLSETKIKGKFAGAVGNYNAHISAYSNIDWPHVAEEFVTSLGLTFNPYVTQIEPHDYMARLFNTISQFNNVLIDFDRDIWSYISLGYFKQITKAGEIGSSTMPHKVNPIDFENSEGNLGKANAELAFLSMKLPISRMQRDLTDSTVLRNMGGALGHSLLAYKSAIQGIGKLQVNEARLKDDLDHTWEVLAEPIQTVMRRYGVPEPYEKLKELTRGRAVNEESIRKFIKSLELPEEAKDQLLKLTPHTYVGAAAALALAVDDAVHLGH | Pathway: Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 2/2.
EC: 4.3.2.2
Catalytic Activity: (2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamido]succinate = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + fumarate
Sequence Length: 527
Sequence Mass (Da): 58816
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A0A520KFQ7 | MAETQKSQPQKPKEVLKDVVLVGKKPLMSYVMAALMQLTQSDSITIKARGRAISRAVDVAQILTNRFLGDSSIKSIKIDTETIGDPPRNVSIIEIVVSGKPLKK | PTM: Acetylated. Deacetylation by the SIR2-homolog deacetylase may regulate its activity.
Function: Binds double-stranded DNA tightly but without sequence specificity. It is distributed uniformly and abundantly on the chromosome, suggesting a role in chromatin architecture. However, it does not significantly compact DNA. Binds rRNA and mRNA in vivo. May play a role in maintaining the structural and functional stability of RNA, and, perhaps, ribosomes.
Subcellular Location: Cytoplasm
Sequence Length: 104
Sequence Mass (Da): 11360
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J3JUW5 | MRSTISEQTKLDKKNQFSLWAYNQLLVFFCLVGLGLSLYSYTVELAMEGNKNYKPYCDISPHMSCTKAFGSSYGKGLGIFGENSIFNKPNSFFGIVFYSMVATLSLVNSPITVTASLVLIISSNFASLYFMYVLYFILKDLCLVCIGTYIVNVTNLLLITSKFKKIREINRTELKRQKSNLKKKPE | EC: 1.17.4.4
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 186
Sequence Mass (Da): 21096
Location Topology: Multi-pass membrane protein
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V6LXC9 | MQTNQNSQIPFFPFTPQQPQLDFYKFIYGSLSKPAVILTELNTGGGKTLLSACAALNQPKRRIIYATRTFQEVLNVVNQLKKLKTTFSLSFLASKQKTCINPDVRFSSDIDHTCSQIYRNCQFYQNSLNYHSQNINDMEDFEVAQICPFFANRAASKTAKFVVCSYNYIFDSEISALNEFDESSILIVDEAHNIPKVATSSISAQFTKNECEKCAQDIAILIKALKSITTIKSLPLQFILQLQIILNEIKILKNIESARVYDVQFETSRIISQQKYDKNMLLEGIRYLKIVVQVLKQANISIVISKQIINLTKFASILMYVDLYPNQAYKFALTVDYPFMKFEDSTKIILANQRNIVELTCLDCAIGIEKIIKGFTNIIFMSGTLRPFHISKQIMGLDRLQFKYQLNIIQFSTYLDKNFKLFLLTSGLNREEITLNFTHRFEQNTVVSVANVLIQLSKTVSDGILLFFPSFAFLEQFAAFTQMLNLKIQGNRLIFFESNNTLESQHALNCHMVACDMGRGSIFCAVARGSFAEGIDIGSQYGRLVVIIGVPYMFRQSARIQAQMKFYQSLDISEDEYMEFDALQITQQAVGRICRKSSEYGCILFVESRFKPVVRMLDHWAKSKGFKETHARQIIQGIKDFLLEQQMHKIKE | Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
EC: 3.6.4.12
Subcellular Location: Nucleus
Sequence Length: 652
Sequence Mass (Da): 74699
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A0A7R9L5I9 | MSSALMATVGQLLRSGQRDDEYVSQLSQELNQLIQNWFGIRQWLVVRPHLPQLSQIIYYSVTTLSGLQTLGEEYVNIVQIDGNRLVVPKLLKRFTALMLQTYSPYLLSTENRRNYFYLSKRVTDIRYVSLNRSIGATDGSTNRLRSVYKVVGYLTLSQLLISFLVRFYSSQNSCGESSDDTFESSDCQTSVKTIEPEVTASDKCCLCLEKRRQTTATTCGHLFCWKCITEWLRLKTECPLCRQPLQTASVWRRDVRQRPPLVDTCSAGSASLNGFALRPSVRSVDNPYRHID | Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Membrane
Sequence Length: 292
Sequence Mass (Da): 33339
Location Topology: Multi-pass membrane protein
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T2MGM7 | MIKSVFLLQGRSQVFKILRRKGVPALVTCRQSSSHHESDEAFDARWETYFQRPSLDGWELRRGMNNLYGYDLVPEPKIIIAALKACRRLDDFAMSVRILEMVREKAAGDKEIINFINNQLKGTLDELGISTPEELSLN | 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.
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 138
Sequence Mass (Da): 15827
Location Topology: Peripheral membrane protein
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A0A2U9BAV4 | MAGLMEDEVFKAFSTYAAIVILKMMLMGPMTGFYRHARGAFSNEEDVSGKSAEEKKKQLRTHPDVERVRRCHLNDLENIVPFVMVGLLYALTGPELSSALLHFRLFAGSRIFHTVAYVGALPQPSRGLSWILGMLVTFSMAYRVLSTVLLL | EC: 2.5.1.18
Subcellular Location: Membrane
Sequence Length: 151
Sequence Mass (Da): 16897
Location Topology: Multi-pass membrane protein
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A0A945XJQ5 | MHPFGQESPNTGMAGEEEILRLIQKHLDDTSPPPPQGIGDDCATWMPPAGETVLLTTDPVIFGRHFDASHEPEHVGAKLLKRNLSDIAAMGGHPGPAILALAMGPDVQLEWLTRFIDGLATTCTTYNIPLAGGDIASSEPGIFIATLSQTGSAPNPVSRVGALDGSSILVTGALGGSLMGHHLHFEPRLPEGQWLAIQEEVLSMTDISDGLAKDLHGLLPAGMQAILDIENLPVDEAVQATGANAIAQALCDGEDYELLFSLDPQTDLNAFLEAWPFDTNLCPIGSVFRGEPAGILVDKNTGTRIQYGNGYEHFKTTD | 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: 318
Sequence Mass (Da): 33746
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A0A960BSW4 | MSVGLTDAAKRRGGAASGPARDPRTPTGRAADSRLRSHPLLWGESLKTKGSPVAVESRAEGITYPPLDELLEKTDSKYSLVIEAARRARQINAYYSQLSEGALEHVGPLVETYQHEKPLSIALREINDGLLETSTVTVEETEA | Function: Promotes RNA polymerase assembly. Latches the N- and C-terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits.
EC: 2.7.7.6
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Length: 143
Sequence Mass (Da): 15498
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A0A2D8VBV9 | MNPFPKIRTFYKETMLELSKASWPDFAELRGSTVVVIIGVAILGCFIAVSDFSLSNWVEYFTQLLREG | Function: Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.
Subcellular Location: Cell membrane
Sequence Length: 68
Sequence Mass (Da): 7734
Location Topology: Single-pass membrane protein
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N6U7S0 | MYIYVDICSNGSSLADLKACYGCSGGNNSACASNTFNTSSEEIYISDCLKVYHLYNTTEAVCLKVVGWSDDDSNIVQRSCAPKTVGDTEVCEYLTKNNTYTQLYGINGTTTCNTCTSDYCNGSTSHLGSAFALFLSIFTIWHRSHAQVDADNVETSCIRSEEGLNGEQEHMSLNAFTAKLKLRRGIKLL | 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 excitability.
Subcellular Location: Cell membrane
Sequence Length: 189
Sequence Mass (Da): 20690
Location Topology: Lipid-anchor
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A0A948Z8F2 | MTLWQEGMIRLARSANVKTFAQRQPWLRGLASQFVGGADAHAALHKANELASNGIAATQFYLGEYVTDPAIIDHTVAQLQTAIAAAADKSLDACASVDPTQIGLMIDEQTCTTNAARIAIAIRKAVPQTRQGHDALMIDMEDATVTDATLRLYWELRSEDLPVAITIQAYLHRTHADLDKLIIAGAWVRLVKGAFAERSRVAVRSVADRDSRYRQCATQLLSRAARESGVYPSFATHDHRLIEEIIAQAKAHDWSPEAYEFEMLYGVRPELQRDLVRRGHRVRVYLPFGNDWFPYAIRRVGESPRNLRFVTSALTRHAARPPQP | Cofactor: Binds 1 FAD per subunit.
Pathway: Amino-acid degradation; L-proline degradation into L-glutamate; L-glutamate from L-proline: step 1/2.
EC: 1.5.5.2
Catalytic Activity: a quinone + L-proline = (S)-1-pyrroline-5-carboxylate + a quinol + H(+)
Sequence Length: 324
Sequence Mass (Da): 36221
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A0A967K517 | MFSILIVLHIFISLGLIISVLMQSAKGEGLAGAFGGGGGVSGAV | Function: Involved in protein export. Participates in an early event of protein translocation.
Subcellular Location: Cell membrane
Sequence Length: 44
Sequence Mass (Da): 4289
Location Topology: Multi-pass membrane protein
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A0A923G1L1 | MLELTDAQIGTWVATFMLPLFRVTAVLMTMPIFGTKMLPARIRLYAALAITVVIVPGLPPLPEFEPLSLRGFLLCGEQVIIGAVFGFSLQMLFQAFVVAGQIIAVQMGMAFASMVDPANGVNVAVVSQFMTMLVSILFLLMNGHLVVFEVLTESFTTLPVGSGLLVNHFWELAGRLGWVLGAGLLLVLPMIAALLVINVAFGVMTRAAPQLNIFSIGFPLTLVLGMAIFWVGLADILSHYQALASEALQWLRELARAR | Function: Role in flagellar biosynthesis.
Subcellular Location: Cell membrane
Sequence Length: 258
Sequence Mass (Da): 27933
Location Topology: Multi-pass membrane protein
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N6TWE1 | MGISTVVHLIIAGHFWFGCYYNWFHVNVPLEVSDLGDAKFRTKQLKFLTYWDALLQSIFFTICVLNDFIGSNERFPKKRPLIRKIKDFVLPALAFPVSMFVSVTFWGLYAVDRELILPKALDPYFPGWLNHLVHTNVIIFSFFELIWSYRKYPSRKVGLSVLCAFMLTYLVWMHYIHFCTNKWVYRVLTVLDLPGRIAFFIGNLSFAVAMYILGEKINNIRWGHITKAKAHKK | Catalytic Activity: 12-(9Z-hexadecenoyloxy)-octadecanoate + H2O = (9Z)-hexadecenoate + 12-hydroxyoctadecanoate + H(+)
Subcellular Location: Membrane
Sequence Length: 233
Sequence Mass (Da): 27342
Location Topology: Multi-pass membrane protein
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A0A0B5QGX5 | MQKTKMIFTIGPASDNEETLRKFIEIGMSAARLNFSHGTHETHKEKIELIQRLSKEMNSATAIVLDIKGPKIRTHNFVNDGVTLNDGDDFDFICGEEILGDEKRCSISYDVLYQDIKVGGKILVDDGLLKFKVTGVEGKTIHTKVVVGGEIKNHKGVNVPNVVIKLPSITEKDIEDIKFGCKMGVDFIAASFIRKASDILDVKKVLKENHGEHIKVIAKIENQEGVDNIDSIIEVTDAVMVARGDMGVEIPIQKVPIIQKMIIRKCNEAGKVVITATQMLDSMIRNSLPTRAEASDICNAIFDGTDAIMLSGESASGCFPIEAAKTMSKIAQEAEEYLDYNHLTARLREPSLTDYAAAISYSACRTANILHAKAIVAATKSGATARLLSRYRSKAPIIAITPYEQVRKGLSLNFGIFPMPCKMFNSTDEILTEAKNTVFSLNFTQPGDDIIVAAGMPTTQTGGTNMLKIEKI | Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5.
EC: 2.7.1.40
Catalytic Activity: ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate
Sequence Length: 472
Sequence Mass (Da): 51699
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A0A654FF66 | MEAGSSNSSGQLSGRVVDTRGKHRIQAELKRLEQEARFLEEELEQLEKMDNASASCKEFLDSVDSKPDPLLPETTGPVNATWDQCKKSIDLDVSLNLRRPQCQIHATTRKSSTVAVGDPHTNASQFQIVLEKFSFLDGLHVVFGQVVEGLDVLRSIEDEVGTLNRIPSKPVVIADCGEL | 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: 179
Sequence Mass (Da): 19716
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T2MJ00 | MAGNDQMDAELQRFLAIEGQKAKFQQHVHNLTDICWDKCIEKSGSKLESKQQACLSNCVGRFIDVSNFVINRLSQKSG | Function: Mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space.
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 78
Domain: The twin CX3C motif contains 4 conserved Cys residues that form 2 disulfide bonds in the mitochondrial intermembrane space.
Sequence Mass (Da): 8788
Location Topology: Peripheral membrane protein
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A0A1C2G073 | MSAYRSGTIAVFGRPNVGKSTLINRLLGHKLLITSPKPQTTRHRILGIKTTADAQFLYLDTPGLVWGGKGALARQMDGATASALAEADCLVLVAACPRLQDDDERALDFVKGLRGDRPLILALNKVDRMAHKEALLPLLAALAERRIATEIVPLSARDGSNVEALEAVIARALPEREALYPEDQLSDRSDRFVAAEFVREQVFRRFAQEIPYVTTVDIESFREEKHLVRIEAIIYVEKEGQKAILVGQGGAGLKAVGSAARRALERHLGRKVYLGLWVKVRGGWSDDARALQSLGYGSDN | Function: An essential GTPase that binds both GDP and GTP, with rapid nucleotide exchange. Plays a role in 16S rRNA processing and 30S ribosomal subunit biogenesis and possibly also in cell cycle regulation and energy metabolism.
Subcellular Location: Cytoplasm
Sequence Length: 300
Sequence Mass (Da): 32889
Location Topology: Peripheral membrane protein
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A0A7R9KCX5 | MFISITIVLVNVLALSVAKNLPQVGANNAELGAQYWTDFSRIALQEAYQSKPVLNRAKNVILFLGDGMGVSTITPSRILKGQLRNHTGEEARLAFDDFPYTSLIKTYNVDYQVPDSAGTATAFMCGVKTNKGVLGVTGRVARGETDCELVHKNSVSSILKWALDSGRSAGIVTTTRVTHATPAGGYASVANREWEAWIPYQSNTQSNKCKDIARQLVENEPGANLSVILGGGRRYFLPDHQTDGPNGEKGLRIDGQNMIDKWLQQKRESGLPDHRYRYVDSRQKLAAVDYSRTDYLFGLFNGDHMSYDRERDATIEPSIEEMTDAAIRVLRKNANGFVLLVEGGRIDHAHHENHGVMALHETVAFDRAVELAVRSVNLDETLVVVTADHSHSLTMNGYPKRGTDIRGINGNHDDNGVPFTTLMYGNGPGYQHDRVDPSTVNTSNISDLKYRNVAAIPLVSAHHGGEDVALYAIGPMAHLFRGTQEQSYVAHSMAFAACIGQFKNSDYDHCNRSSSATNISTTFFSSYLIISFIFISFQLI | Cofactor: Binds 1 Mg(2+) ion.
EC: 3.1.3.1
Catalytic Activity: a phosphate monoester + H2O = an alcohol + phosphate
Sequence Length: 540
Sequence Mass (Da): 59469
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A0A7C4DVH4 | MGATRFEGCYTALVTPMKSDFSIDFEGLRRLVEFQVEEGVSGVLAVGTTGESPTLTHEESIKVIREAHEVAGGRCIVIGGTGSNSTEKTMEMTREVYDFGVRCVLLVDPYYNGPSSLEIRREYVEPVAESFPDVQVIPYVIPGRTGTQLLPQDLAILHSKFKNVRAVKEATGNIENMKLTRRLCGEDFDILSGDDDKTYEMMINPEIRASGVISVASNVAPRAVQKFTKAILENRSKEAEDLLEALKPLFSIVTVRTEEETPYGKVSCRARNPLPYKVLMNILGMPSGPCRRPLGKMTKKGLEVVLNAARTVYERNPEILKPIEDFFDVDLSRRLYGKRFLEGLAYDQY | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4.
Function: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Catalytic Activity: L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + H2O
EC: 4.3.3.7
Subcellular Location: Cytoplasm
Sequence Length: 349
Sequence Mass (Da): 38961
|
J3JYM8 | MDGGGDRTERLHASNVAVIREVYDGSNSQELFEMQLEKYLDSCCAIIVIEPTQLGDETARWITAGNILHKLAVVGGLSSVVTGFVWPQTFVPQAPLGIISVLCTGLYTALWQFDHCVKYQVEKDPRKLARLPILSVITAASPVVLVRKDDTRRKVLHCTISLTAAALCVYRLYASVK | Function: Plays a role in mitochondrial morphogenesis.
Subcellular Location: Membrane
Sequence Length: 177
Sequence Mass (Da): 19505
Location Topology: Multi-pass membrane protein
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A0A7R9PZJ8 | MSFMACVLTVSDTCDVDHSKDTSGPLLTSRLTGKGFDMIETAIVADDVLRIQGKLCEWSDRALGVDLIVTTGGTGFTARDVTPEATKAIVDRDAPGIAHALISGSLKATPMAMLSRLSAGIRKRTLIINFPGSAKACDECLAIVEPVLSHAIHQLRGDTTATASAHKQLQQPLRSKVQLQSVGLRPRHSQYPMISMDTAINRIIGECVAITDVEYIDLDCLDQLMGRLLADSICAAVPLPPFRASIKDGYAVVAADGSGDRKVLAKAATAGGQVPMESIELTSGCCMRVSTGAPLPAGCDAVVQVEDTKVVQLSESGEELVICIENVPKVGQDIRPVGCDIPCDGKPIVNRFTQLGPIELGLLASIGIHTRIPVFRRPVVAVLSTGDEIGNVGQTLGPYQVWDSNRPILMSLLRQNGVQSMDLGIAVDDVNDVFGRMRRGLLAADVLITSGGVSMGERDLLKHVMEVDFGAQIHFGRVNVKPGKPVTFATVSIDGRKKYIFGLPGNPVSAFVTFNLFVKPLLDCLSNKDTVNGLADIKTYQRCQRVRLECDEKVYRLDDRPEFARAVVSFGTTGLEAGFPTARLTGNQRSSRLLSAKDANALVLLPQKSDSVDKISCGDFVTAFLI | Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
Function: Catalyzes two steps in the biosynthesis of the molybdenum cofactor. In the first step, molybdopterin is adenylated. Subsequently, molybdate is inserted into adenylated molybdopterin and AMP is released.
Catalytic Activity: ATP + H(+) + molybdopterin = adenylyl-molybdopterin + diphosphate
Sequence Length: 626
Sequence Mass (Da): 67055
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A0A7R9Q020 | VLVAYIALFIFDLSERGIQWFDPFFTIWEVDSRFALIFIITASIASIGYFMFLCFHIWLAFRNISTKQSSLPSMSSTRRLIYQGIIYRFKFLLLATLVCAAATVVAYIMGQVTEDQWHWEDADPYVEPLQWTSAMFTTVYALWNCYVITLLILYAPSHKELGQNVDSMSEEIEFNRLTEHDENNEHKTENVMGSSGGTSEASDMSLLQHLATKSNID | Function: A segment polarity gene required for wingless (wg)-dependent patterning processes, acting in both wg-sending cells and wg-target cells. In non-neuronal cells wls directs wg secretion. The wls traffic loop encompasses the Golgi, the cell surface, an endocytic compartment and a retrograde route leading back to the Golgi, and involves clathrin-mediated endocytosis and the retromer complex (a conserved protein complex consisting of Vps35 and Vps26). In neuronal cells (the larval motorneuron NMJ), the wg signal moves across the synapse via the release of wls-containing exosome-like vesicles. Postsynaptic wls is required for the trafficking of fz2 through the fz2-interacting protein Grip.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 217
Sequence Mass (Da): 24917
Location Topology: Multi-pass membrane protein
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A0A6A0HWD4 | MPSDTLRLNKMIFHAYHGYWEEERQVGQRFEVDVELHIDVAQAAGSDNIRDTVDLYKVYQTVERVVTKNTFKLVETLTHAIADTLLQEFHLPQVRVRVRKPNSPVPGISDGIEVEIHRERAAQG | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 3/4.
Function: Catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin.
EC: 4.1.2.25
Catalytic Activity: 7,8-dihydroneopterin = 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde
Sequence Length: 124
Sequence Mass (Da): 14279
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A0A072UY93 | MFQTKSNLDHHEPLVLKSAIYSRILLITLIIFFRILASPYDTSASLNPPCLTATTTTTPNETHRSPIASSIENGIIWDSVYFIRAAECGYEYEQSYAFLPLLPLFISFFSPHRSLLALSSYLINNLAFVLAALYFYRLSIAILKDPEIALRATILFCFNPASIFYSSIYSESLYAILSLGGVYYFVSGRNNLAVLLLALSGLARSNGVLNAGYVCFQTMHRAYHALFQNKNFTLALQIIIVGAFRSACIFAPFVAFQAYGYYNMCVGRFPDEIRPWCKARVPLLYNYIQSHYWGVGFLRYFQLKQLPNFLLASPILSLAFFSIVHYAKSRPRIFFSLGFDTTIEEKSCDVMFLSEDLSRSKVAGSVEKSSVRIEGRGRM | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Function: Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis.
EC: 2.4.1.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 379
Sequence Mass (Da): 42874
Location Topology: Multi-pass membrane protein
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A0A7R9QDP6 | MGWLMCRKHPDVIEQGKLVDMSDLAANPVISLQRKFYVPLVALIWAAFPTLTPYYMWGEGLWEAWFVCVMFRYVLILNITWCVNSAAHYWGYKVPYDKTLNPVECNIRHVMDYKASEYGPFVGFNPATMFINTMAVLGQAYDLRQPSADMIEERQKRTGDMANTKLSMY | Subcellular Location: Membrane
Sequence Length: 169
Domain: The histidine box domains are involved in binding the catalytic metal ions.
Sequence Mass (Da): 19599
Location Topology: Multi-pass membrane protein
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A0A497N8V6 | MTWRTRGNHYYRLAREKGYRSRAAFKLLEAIRAFRLVRPGEVVIDLGCAPGSWLQVAREVVGPNGLVLGVDIKPVEPLGYENVKIIQADALSDEALELLRAELPGEADVLLSDMAPRSTGIRELDHARQIELAGRALELARELVRPGGRAFVKASQGALLSKLLSTFRRSFRSVRCFKPGASRPESPEIYIIALGLRKGAGATGLGRRQ | Function: Specifically methylates the uridine in position 2552 of 23S rRNA at the 2'-O position of the ribose in the fully assembled 50S ribosomal subunit.
Catalytic Activity: S-adenosyl-L-methionine + uridine(2552) in 23S rRNA = 2'-O-methyluridine(2552) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.166
Subcellular Location: Cytoplasm
Sequence Length: 209
Sequence Mass (Da): 22984
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