ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
A0A2H1WZY1 | MHEGWPAVCAPPGAARRPLKVVREMNRLGMIVDLSHVGENTTRAAIKLSRAPVVFTHSSVYSLCNHKRNVPDDIIHSLKENGGIIMVNFFPDFVKCAPNATISDVAGKLSTIVVLTHTLTQK | Catalytic Activity: an L-aminoacyl-L-amino acid + H2O = 2 an L-alpha-amino acid
EC: 3.4.13.19
Subcellular Location: Membrane
Sequence Length: 122
Sequence Mass (Da): 13327
Location Topology: Lipid-anchor
|
A0A5P6VQE4 | MVGLVLVSHSAKIAEGLKDLTSEIAAAHKGIVAAGGMEDGSIGTDAIRISEAIRQANDGDGVVVLADLGSGVMSSETAIELLEDENIKVKLADAPIVEGTIAAAVSAMVGSDLEAVLKAAEDCRGVRKIPE | Function: Component of the dihydroxyacetone kinase complex, which is responsible for the phosphoenolpyruvate (PEP)-dependent phosphorylation of dihydroxyacetone. DhaM serves as the phosphoryl donor. Is phosphorylated by phosphoenolpyruvate in an EI- and HPr-dependent reaction, and a phosphorelay system on histidine res... |
A0A671Q8A4 | MLSSLFLLKVFFVFINSSYSSGANAKLRYQITSGNVGGVFDMEPEVGTIFIAQPLDYEQNKLYKLHVLASDGKWEDYATVIVTIVNKNDEAPVFSVNEYYGSMTEELDGSPVFVLQVLPLHSLYCANAKLRYQITSGNVGGVFDMEPEVGTIFIAQPLDYEQNKLYKLHVLASDGKWEDYATVIVTIFIIDEVTGKIYAQITLDREARAVWRFVVLATDEGGEGLTGFTDVIINVWDINDNAPLFACAPDNCNGDVTENSPPGTSVMEMTATDLDDAAVGQNAVLAYKIVGNAALNGANRGADVFSINPATGTVSVAMSG... | Function: Cadherins are calcium-dependent cell adhesion proteins.
Subcellular Location: Cell membrane
Sequence Length: 754
Sequence Mass (Da): 82169
Location Topology: Single-pass type I membrane protein
|
L0EUD9 | MRFSNSFVDDLLARVSISQVIGNYVTWDKKKTNVVRGDYWACCPFHQEKTPSFHCNNNKGYYYCFSCHASGNHISFLSAIKGFSFADAIQQIADIAGVSVPRSDLQTQKSNKTEEETLISIIEMATLFFQNSLQNQSAEYARGYLNQRGINSRSIEIFRLGYAPDNRHALTEYLTERGVPREKIEASGLIVHGSDIPVSYDRFRHRIIFPIFSAAGKVIAFGGRALSKDIAAKYLNSNETILFRKGELLYNFFGARNALKRILPEEISKRKGVQPQSRETVVLVEGYMDVISLHQSGIQNVVSPLGTAITERQLQLLWQL... | Cofactor: Binds 1 zinc ion per monomer.
Function: RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.
EC: 2.7.7.101
Catalytic Activity: ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.
Sequence Length: 656
Domain: Contains an N-termi... |
A0A9D8KGB0 | MFDSRVLGVDPGITVTGYGVITGGKSPTVVSAGEIKPASRLTMAEKLEAIFRETEEVIEKTSPDAVAVEGIFHAKNVKSVIRLGHARGVILLAAARANLVVYEYSPREVKAAATGYGAAEKAQVEKMIKRILNLPDDVGSHACDALAVALCHLHTFKVTSSKERA | Cofactor: Binds 2 Mg(2+) ion per subunit.
Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair. Endonuclease that resolves HJ intermediates. Cleaves cruciform DNA by making single-stranded nicks across the HJ at symmetrical positions within the homologous... |
A0A671M5K4 | MLSSKKSDPGSSSSSGGNGGDRAPETLSAPQAGPAGPSGPGIADVKKKERASPSGEPGGPPLLHPPGPGGVDQDSAEGRRTSRRKRAKVEYREMDESLANLSEDEYYSEEERNAKAEKERKQVIPPPNAFQGAAFQSRLPHDRMTSQEAACFPDIIGGPQHTQKVFLYIRNRTLQLWLDNPKIQLTFEATVQQLEAPYNSDAVLVHRMHSYLERHGFINFGVYKRVKPLPSGNPMAVVSKQVNMELAKIKQKCPLYEANGQAVPKEKDEMVEQEFNRLLEATSYLSHQLDFNFLNNKPVSLGQALEVVIQLQEKHVKDEQ... | Function: Histone demethylase that can demethylate both 'Lys-4' (H3K4me) and 'Lys-9' (H3K9me) of histone H3, thereby acting as a coactivator or a corepressor, depending on the context. Acts by oxidizing the substrate by FAD to generate the corresponding imine that is subsequently hydrolyzed. Acts as a corepressor by me... |
D8IC81 | MFIKSNTTDIVKPSIKDEKAIENIKKAAQIAQEAIDLAFEYSLSGTRASKIDKDVEKFIKSKGAYPANLEVPEYGFSTSISIGNEIAHGRPTNKKILVQGDIICIDIGVKYNGYYADCARTMVVKGNQLSSTNKKAYKLIKACKESLEHAIYKLRPNILLSTYGREVEKKVNEYGYSIIKSLTGHGVGYEYHEAPYIYNFYHPNNDVKLEENMVLALELMITEGSDKYIIENDGWTISTADYSFAAHFEHTVLIKKNGVEILGID | Cofactor: Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe(2+)-... |
A0A968N8D3 | MAAERILAPSPIDLNCDYGETFGGSLVQDDVTLLQYVSSINIACGAHSGDPDVMRRALTQARTHGVAIGAHPGFPDISGFGRRLLHMSPDEVYNSVLAQVGALAALARAEGLTLTHVKGHGALYNHAAHDLPTATAIAQAVATFDPALILVGLSGSAMITAGEQAGVRVAREAFVDRAYEADGSLRSRRLEGAVILDNQHALAQALSIAREGTVITYAGTQIDVPAETLCLHGDTPGARERAAVVRQGLAAAGVVVRRLGV | Function: Catalyzes the cleavage of 5-oxoproline to form L-glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate.
EC: 3.5.2.9
Catalytic Activity: 5-oxo-L-proline + ATP + 2 H2O = ADP + H(+) + L-glutamate + phosphate
Sequence Length: 261
Sequence Mass (Da): 27127
|
F2I8U0 | MKLETYQGASVEEAIAAAKEGLQVSDISMEDVKVLQEPKKGFFGFGSQPAIIQVSLADGEPSVDEIVAEVAVEAETVTDPVADTAPATTEVVEEATVVEALDDSQSAASQATSELSSDSQVAHTLDSQSASPSDVSDSAELEPVASQSEPASESVATDYSTTDSQSQDADYEEDEEEEAEDSSYPFDWGVEDVAHYLIDVMEAYLVDVTIDVEDMDDLIIFHINTDKPGLVIGKHGKIINSLETLAQILTHSHVRKRVAVEVNVGDYRERREQTLEKLAERTADQVTVEREDVTLSPLPARERKIIHRCLSKYSHIKTQS... | Function: A probable RNA chaperone. Forms a complex with KhpA which binds to cellular RNA and controls its expression. Plays a role in peptidoglycan (PG) homeostasis and cell length regulation.
Subcellular Location: Cytoplasm
Sequence Length: 335
Domain: Has an N-terminal Jag-N domain and 2 RNA-binding domains (KH and ... |
C4V7D0 | MKEVKAATDLELLVNKIDSTGYICRLKQSVKTCKICNIKHFISHDWFTDLEKEFKDDYFETLCTKLHGKVFFPKVENIFTFTYFFPLADTKVVILGQDPYHNLNQAMGLAFSVPNNVKIPPSLKNIFQELKNDILDFVIPKHGNLEAWAKQGVLLLNDVLTVEQHKPGSHSDLGWKIFTKAILSKINETCQNVVFIFWGNYARSKSKYVNKHKHLVLEAAHPSPFSAYKFFGCKHFSKTNEYLVKNGKSPINWNL | Function: Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine.
Catalytic Activity: Hydrolyzes single-stranded DNA or mismatched double-stranded DNA and polynucleotides, releasing free uracil.
EC: 3.2.2.27
Subcellular L... |
F9Z9V2 | MKIKTGIGIDVHRLEAGREFWLGGIKIGHEKGCVAHSDGDVLIHAICDALLGATGLGDIGQHFPDTCPAYKGIDSKLLLQKTKALIDHRGYAISNIDSVVCLQRPKIRPFIDDMRHCLAEILELDVDDLSIKATTTEQLGFEGREEGVSAYATVLVYKL | Cofactor: Binds 1 divalent metal cation per subunit.
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 4/6.
Function: Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP... |
A0A1Y5TY12 | MLRHCLHLFFGMFFLPLLLAASPPAGADIPDETYEALGLTRDAPPKDLYGALIKRYYDPGKGHGKGAFGELWQPTPFTRYLDPKTLYVAPDMDFEATREECVECHSTVTPGWVHSWQKSVHGDLDEIRGLPAGDSRAYKKELIDQVEANLHSMGVLPEGQNLDDVGCIDCHMRVGALKGNHKADLKMPDAADCGQCHVQQFAERESERDTLTWPQEQWPAGRPSHALSWQANVETAIWAGMEQREVADGCSLCHTMQNTCNSCHTRHEFSAAEARKPETCSTCHNGVDHNEFEAFSMSKHGVVYATQGHDWDWQQPLSTA... | Cofactor: Binds 8 heme c groups per subunit. One specific heme c group is called heme P460.
Function: Catalyzes the oxidation of hydroxylamine to nitrite. The electrons released in the reaction are partitioned to ammonium monooxygenase and to the respiratory chain. The immediate acceptor of electrons from HAO is cytoch... |
R6C9F2 | MRNEEKPGRAWLEIDTGRIRENYRSLCASAPDGCDIMAVVKADAYGHGAGRVAKLLQEEGCRYYAVATLEEAISLRSAGILGDILILGYTMPRDAFLLQHYDLIQTIVDEKHGQELAKSGSTVRAHLAVDTGMNRLGIPAKEEETILRLLKLPGIRIEGIYSHMSVADSRQKEDIVFTNGQIAEFTGLKKRLGRMGYGHLYYHCQSSYGFLYYPVPGMRFARVGIALYGCTSNSAEESYPVALKPALSLKARISCVRMVAPGEFVSYGRTYKAVEDRKIAAVTMGYADGLPRNLSGQGYAFIKGRKAPIIGRICMDQLML... | Pathway: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1.
Function: Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids.
EC: 5.1.1.1
Catalytic Activity: L-alanine = D-alanine
Sequence Length: 375
Sequence Mass (Da): 41154
|
R6CC44 | MISISEYPVPVLTGDFSHKTIHVKVPGSKSITNRALLLAMLSDGKSHLTGAQFSEDSSHFLQCLSDLSFDVASSPETGEVSVHGLSGRLPVKKASLYVGSAGTAARFLSAVLGVSEGEFFLDASEQMKKRPMAPLLSALQSVGCDISFAEKEGFFPFTLHARGFQNTDLTIDIDKSSQFLSALLIAAPLAKEDVKIKVAGTHGMAYIEMTCRMMEQFGVLTEHPSPDTFLIKAGQTYRAQDYAIEPDVSAACYFYALAALSGCSVIVDGVPEHSLQGDTEFLNILEKTGCRVTRTNEGICITGPAACAESAGVKSADAGS... | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7.
Function: Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-ph... |
A0A9D8PPY4 | MSADDLHKWGKTERGPRSVYFRTFGCQMNVHDSERMRGLLSRDGITAVDSPHDADIIIINTCSVREKPEEKTYSEIGRYRRLKEKKEGLVIGVTGCVAQQKGEEIVRRFPYVDLVLGTKNVGAISNIISEIVSGKKPIVKTEFHDNNCIEPFEPFPRDPDNYTAFVTVIQGCNNFCSYCIVPYVRGREMSRPSTDITDEIKSLIDTGIVEITLLGQNVNSYSDPKNGLRFPELIRKISKIDGIYRIRFVTSHPKDMSDDLISCFKEIETLSSHIHLPVQSGSNKIIKMMNRGYTVEDYIDKIERLRSVRSDLAVTTDIIV... | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that re... |
A0A2K8NS24 | MIRCQKTFKSTTSKPTLYLVGTPIGNLADLSPRAQTILQEVDWIFCEDTRTTEQLLKHYGIQNKLISCHKFNEQSRVDKLQQILATGQSMALVSDAGVPIISDPGAKIVREILHRLPNQINVSGVNVGPAYIHALVASGYESPNHYFYGFLKSRGFEAKKRELTNVLMTLPEKTIIVFYESVHRIKETIAFLAEILPPTTSVMIARELTKTNEEIIQGPISELAAYVAADQMVLKGEFVVLVSKETNWSKNWTLDEIVQATQKLTSEGHSLKAAASIISLESGWPKNKIYQLMVEKQK | Function: Catalyzes the 2'-O-methylation of the ribose of cytidine 1402 (C1402) in 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine(1402) in 16S rRNA + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.198
Subcellular Location: Cytoplasm
Sequence Length: 298
Sequence Mas... |
A0A2H1V1I0 | MNPSGVRFTDHLMGLSHLSQNKTATLFTQLYRGHATRTVMPLANLYDDIRLILRSEGDLSTEGLSAGPPKDLTVTTKKFFRELFPVAYHNVLKLDAKQFTPDYEICLKDAYDAVQPFGDVPQQLGTSLARSLEAARALLQMLAVGADTLSAAEHVLASGADNCAERLLRTGGCSRCHGHEARPCRNYCLNVARGCIGSLLSELDGPWAGYVEGVERLTKVDADVALRELETKVSKAIMYALENRAVSENK | Function: Cell surface proteoglycan.
Subcellular Location: Cell membrane
Sequence Length: 250
Sequence Mass (Da): 27370
Location Topology: Lipid-anchor
|
A0A225MRK4 | MTKPLNKVFIASRGEIAVRIIRACRDAGIQTVQAYSTADSETSAVHMADESICIGGPKPSDSYLNATALIDAARHSGADAVHPGYGFLSENADFAQAVEAAGLVYIGPQPEIIRMMGDKVKARQCAQEAGVPVSMGSPDTIESDEQAIDIANRIGYPVLIKAAAGGGGRGMRVARNEAELKDNIGRAIKEAETAFGSGAVYIEKFLERIRHIEVQIFGDGNEVIHLGDRDCSIQRRHQKLLEEGPASVLDPETREHIRNAARQLGQSLGYRSAGTVEFIVDPRTREFYFIEMNTRIQVEHPVTELLTSTDLVAMQLAIAA... | Pathway: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1.
Function: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form ... |
A0A6V7VMF6 | MKRLDCKALHYQWGRKGAESTVAQLRKDTIEEDEFYAELWMGTHTRGPSQVKEGEARIPLADYFRDHPDVLGQHERDGVGLQFLLKVLSVGKCLSLQLHPTREQARELHAADQTNYPDANHKPELTIALTNFEILCGFQMPDKILSNLRSHEALVELIGEKVLSSFGATTDEEEKKGALKNIFTQIWTIPPEEIGTLLTKLLSDIFLKEQRSQTDELIMGLSEHFPEDIGILAPLFLNYVKLEPGQATFLGPNEPHSYLSGDCIECMAQSDNTVRAGLTPKFKNVPLFCENLTYRMGGPPIFEPQHLAGGVFEYSPEVQE... | Cofactor: Binds 1 zinc ion per subunit.
Pathway: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 1/2.
Function: Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer r... |
A0A0P8Y625 | MRLMGKSSYNSFGILGGSFDPPHLGHLRLCEIALKKLKLSKIFWVVTKKNPFKKKAFFSLKKRLYESKKISKSNKKIKVIYLDKKIRSSRTINVIEYLRKINKANKIYLLIGSDNLVSFHKWKDYEKIIDLCHIVVFSREGYDKMARKSAIMESFKNKKIKFIRNKKINISSTIIRKYYNNQ | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
EC: 2.7.7.18
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide... |
I0HG84 | MPVAAPPRERVTDDPLHAHGGGHRGGHGAGHSGGHGAGHSGGHGPGDGHPAGAPAGEAHRDGAPAVPPLTATAPPAEPEADPPALPIEEPGESPAEPLTEAEVDGEALAAEIGNELAAQSGESPQTGESPQTGQSPQTGEPQPAPARAEPHEWRGIILVTGTDTEVGKTIATAAMAAAAQAAGLRVAVIKPGQTGIATGAPTDAEVITRLAGPETVRTLAEYPEPLAPLAAAKVAGQAALDLFETVDAIRAEAEKHDLVLVEGAGGLLVPMGLRPSGEPWTFADLATTLGANVIVVARAGLGTLNHTALTLEALHRRGVY... | 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.... |
A0A1G1LR46 | MISPAEAMVLIRRHAVKPKIKIARLGECLGAVLAADIRAPFPMPVADNSAMDGFVIRSKDAGLASVKNSVRLKIIGTLKAGDSKQVHLVSGTACRIMTGAFMPQGGDCVIAKEDAVIVGNHLIVKHSVCEGQHIRRRGEETRKGQKLLTQGVILHPARIGILATFGYARVPVYCKPKVAVLATGSELVTPGKKLSRGKIYDSNSWMVCAALERMGIDPSRVLTLRDDRGKVKKAILDVLRESDYLLLLGGVSVGDYDVVKDALKQSGVKTIFWKVSQKPGKPLFLGRKYKKVVFGLPGNPAAVFTCFYEYVYPALRQTMG... | Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
Function: Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP.
EC: 2.10.1.1
Catalytic Activity: adenylyl-molybdopterin + H(+) + molybdate = AMP + H2O + Mo-molybdopterin
Sequence Length: 414
Sequence Mass (Da):... |
A0A4Z2DEG1 | MVMDTTCSPMTERYLLSTYRHVLELFILISMSVFGAKSVLKLFKKYKGEFLRAGFAGVDMNKPTKPTIPEAQGVICGVVFLSIMFLFIPVPFWRFLVRKAETQSNEICSSDKIREGQEAFFKSQFIQYLAGLLSVCCMLFLGFADDALNLPWRHKIGFPFVAGLPLLMVYLANEGTTRIAVPVMFRGSLGGSVDIGVLYYIYMGLLTVFCTNSINIYAGINGLEVGQAIVIGASLILFNLIELMGYHWRVHLFSLYFLIPFLAVCWSLYRVNRYPAKVFVGDTFCYFAGMTFAVVGILGHFSKTLLLFFLPQIINFPI | Pathway: Protein modification; protein glycosylation.
Function: Catalyzes the initial step of dolichol-linked oligosaccharide biosynthesis in N-linked protein glycosylation pathway: transfers GlcNAc-1-P from UDP-GlcNAc onto the carrier lipid dolichyl phosphate (P-dolichol), yielding GlcNAc-P-P-dolichol.
Catalytic Activ... |
A0A357LBX1 | IERAASEIGAALRDKAAYTVVAVKSTVIPGTTDGVVLHALERASGKKAGPDFGLCMNPEFLREGSAVEDFTKPDRIVIGAIDPRAAEVFGRIYAKFDCPKPVISLRNAEFCKYASNALLATLISFSNEMAALCEATPGADVEVALDCVHLDRRLSPVIDGQRVKPGILSYIRPSSGYGGSCFPKDVAALRAFARDRGVDAELLNAVSAVNDRRTAAVLDLAEARIGAFKGKRVGVLGLTFKSGTDDLRHSPAVTLTEQIIDRGGHVTVYDPIATEIARNAFGDKVRYAAGALDAVNGADVTVIGTAWPEWSALNWAAVKS... | Pathway: Nucleotide-sugar biosynthesis; UDP-alpha-D-glucuronate biosynthesis; UDP-alpha-D-glucuronate from UDP-alpha-D-glucose: step 1/1.
EC: 1.1.1.22
Catalytic Activity: H2O + 2 NAD(+) + UDP-alpha-D-glucose = 3 H(+) + 2 NADH + UDP-alpha-D-glucuronate
Sequence Length: 352
Sequence Mass (Da): 37300
|
A0A671KWV4 | MPAKCLTIFLFAFCFAFCAVASALVKQKLAQVILKKQKAVLERTNSNPLSSPSVAYRLETALITAHSCLSAHAHRLMCFSSDFKIKVFSSEPNLKVKHKLKKHLNTRKSPLTRKESAPPAVKHRVPDTLGNYNTLPLLLRSVVIIRRSHTFFPCSNTSQKYNMIFYFRHLSDIVFIKHPEILSLQSRLWETQKQLQHLRRQTAHMETLAVPMMLGAAHRPLSRTQSSPASTSLTLPDKALPLTTAQEPPQSQPRFTTGLVYDSQMLKHQCTCGDNSSHPEHAGRIQSIWSRLQERGLRGQCESIRGRKATLEELQSVHTE... | Catalytic Activity: H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl-[histone]
EC: 3.5.1.98
Subcellular Location: Nucleus
Sequence Length: 679
Sequence Mass (Da): 74477
|
A0A2K6PQI9 | ASSARPCPPESRKPRWRRSLARARGRADGRCPSPGRETAVGTAGLGTEERRALEREQARHGDLLLLPALRDAYENLTAKVLAMLAWLDEHVAFEFVLKADDDSFARLDALLAELRARDPARRRRLYWGFFSGRGRVKPGGRWREASWQLCDYYLPYALGGGYVLSADLVRYLRLSRDYLRAWHSEDVSLGAWLAPVDVQREHDPRFDTEYRSRGCSNQYLVTHKQSLEDMLEKHATLAREGRLCKREVQLRLSYVYDWSAPPSQCCQRREGIP | EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 273
Sequence Mass (Da): 31390
Location Topology: Single-pass type II membrane protein
|
A0A6C0N8C5 | ICQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLSSSGVEAGVGTGWTVYPPLAGNLAHAGSSVDLAIFSLHLAGVSSILGAIN | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A381H474 | MPLSDSEKAALPKTDIRAVHEALDVEHRAYSREDDSPQGSVKARLEQAWPDSLAEGQLIKDDEGRDQLQAMPKATRSSMFPDPWRTNPLGRFWDRLRGRDVTPRYLSRLTKEEQENEQKWRTVGTIRRYILLLLTLAQTVVATWYMKTILPYQGWALINPADMIGQDLWVSFMQLLPYVLQTGILILFAVLFCWVSAGFWTALMGFLQLLIGRDKYSISASTVGNEPLNPEHRTALIMPICNEDVDRVFAGLRATWESVKATGNAAHFDVYILSDSYNPDICVAEQKAWMELIAEVQGEGQIFYRRRRRRVKRKSGNIDD... | Pathway: Glycan metabolism; osmoregulated periplasmic glucan (OPG) biosynthesis.
Function: Involved in the biosynthesis of osmoregulated periplasmic glucans (OPGs).
EC: 2.4.1.-
Subcellular Location: Cell inner membrane
Sequence Length: 721
Sequence Mass (Da): 81383
Location Topology: Multi-pass membrane protein
|
A0A6V7U879 | MFSSLKRANYNVIEEVEDENEPGTLKSMELGRVTDIKLNEEEEVEEECHQHFESSAPPIHHGVAVSFSGKGDAELQASSDPAAEWDHIKDVDQFFAYIYEYYQQRGLTCIALRSLFSLLRFAFVVLFSTFLVNCVDYDVLFYNRNTTLDGRPLPAKRAIHNAFIPRCYARINPLMSLALFLAALFWLAHLFRIFCRLVQFSEIRRFFISQLEIADSEMQNLTWAQVVERLCGVQKRLHLIVNREAITPLDVCQRILRHKNYFVALVYYNILPPRIRLPFFGHVHYLSNGLRFNLEWLLFWGPWSPWKGPYALKDEFKDPA... | Function: Phospholipid scramblase involved in autophagy. Cycles between the preautophagosomal structure/phagophore assembly site (PAS) and the cytoplasmic vesicle pool and supplies membrane for the growing autophagosome. Lipid scramblase activity plays a key role in preautophagosomal structure/phagophore assembly by di... |
R6BKG4 | MQIKSGIDIIEVERIKSSIDEMGDNFLDRVYTENEIQYCESKKKNKYQSYAARFAVKEAAFKAVSTLIKDKYSISWKNIETTNDENGRPSVKFISLTKEVEKELAKIESIDVSISHLEKYAVATVNILF | Function: Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
Catalytic Activity: apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-[ACP]
EC: 2.7.8.7
Subcellular Location: Cytoplasm
Sequence Length: 129
Sequence Mass (Da): 14809
|
S2XNT2 | MNEWKKLNQKIASQSLKKKWAISSAAVIFLSFATMSIILYVALKGWLYQQEEQEVNRTMQDLTAFFESQGPFLTVQDIQSNTGLMKSIVDKDQTVRLLNADGIEVLQINNTSTFKAFKDIDVPEEGYALNDYDNSSISAIGNVRLGRFKGYIQLEHPLKSFQSTKTYILTAMLLFSVCALLLSGWIGYILASYLLKPLKDLKMTMDDVVAHGFEKELTISYDAKDEIGELIIVYESMMAKLKYSFEQQQQFMADASHELRTPIQVVEGHLSLLNRWGKDDPEILEESLGISLREVHQMKTLVDEMLELARGEQMKAQPPT... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 468
Sequence Mass (Da): 53203
Location Topology: Multi-pass membrane protein
|
A0A1G7BKI2 | MVAAIVAFCVGVLFCLLLTRPAIVVLKRLGWSQFVRADGPQTHLVKKGTPTKGGLVFGAGTVVAYAVAHAVTGEAVTTSAVLVLLAMVGMGAVGFVDDYLKTHHQNSAGLPERAKIVGQLLVIALLVPVALWGADRAGRSLVSSSITFVGDVELLDLARWGPVVAVVLALAWYGFLSIGTTNGVNIVDGADGLLAGCAISSLSAYALMLVFQAQNSCSGAGGAGCFDTVHPQDLAVVTCALLGNLVGFLWWSCYPARIFMGDTGSLGIGGFLVALAVLSRTELLLPVIGVIYVMVTSSVLIQRYYFRFTGGKRFFKMAPL... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yield... |
A0A969FTQ3 | MNDLSTESVLTGTAAAPGIAIGPALRYRQPAVAGHGFRLVQAESRYRETGTAHLEIQRLDEAIAATDAAMRETEARLQAEGKGAESHIFESHRALLHHPGLYDRAVTLISKAGWRAPDAIVEAGEHQASPLGDTDNPYLKAYAANIRDVVGQVRRFLVREQTLADLLTRPSIVVADDLGLSEWMDVPRERLLGLALAAGGTTAHSMIMARSLGIPTVIGLGTAALRTLRDGVMLALDGTTGQVVVAPSEETIAHLRVVAAELAEHQAAMYRQRDLPSITRDGQHVVLLANAGTVIEAQAAREWGAAGIGSLRTELLFLGQ... | Function: General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. Enzyme I transfer... |
A0A6N4RCA1 | MPTTSAAKAPATVLVVFGASGDLTKRLLMPALYNLAGNHLLDEEFEVIGISRSAMSDAEFQGKQAEFMSTFTQQRSGDSSQKLDEVAWKWLEKRLSYTSASFTEDDTYQQLSKRLGKRNAVFFLAVPHEAFLPIVNGLHANGLMQQGKNTSRRVVIEKPFGHDHASAINLNQHMLGMFKEEQIYRIDHYLGKETVQNISALRFGNRLFESTWNGEHIESVQITAAETVGVEGRGSFYEPTGALRDMIVNHLFQVLSLITMEPPATKSADAIRTEKAKAIQSIVPLSETDLQHDVVRGQYTAGTVNGKDVPGYTQEDSVAP... | Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 1/3.
Function: Catalyzes the oxidation of glucose 6-phosphate to 6-phosphogluconolactone.
EC: 1.1.1.49
Catalytic Activity: D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-lac... |
A0A9D8PLU6 | MDNVIWIIPLLPLAGFLINGLGGRRLPDWLVSLVGVSLPVASFVLSVWAFLKLLKLGEGAEVTCTLYTWIFSGDFQVSLAFLLDPLSAVMALVVSGVGSAIHLYSVGYMHDDKSFARYFSFLNLFLFSMLVLVLAEDLVLLFLGWEGVGLCSYLLIGFWFDDMEKAKAGKKAFIVNRIGDFGFFIGMALIVLTIGTLNVPGMKEILESNPGVITTGMATAITLFLFVGATGKSAQIPLYVWLPDAMAGPTPVSALIHAATMVTAGVYMIARLNFLYVLAPTTMIIVALIGSLTALYAATIGIAQNDIKKVLAYSTISQLG... | Catalytic Activity: a plastoquinone + (n+1) H(+)(in) + NADH = a plastoquinol + n H(+)(out) + NAD(+)
Subcellular Location: Membrane
Sequence Length: 643
Sequence Mass (Da): 69987
Location Topology: Multi-pass membrane protein
|
A0A7S0SDK7 | MGRHKRQRLPAALFIGGSSLIFATFVFVAPAMPRLNPATLDFPPVLHAVQTTADAHGAGKDTPREFVAQHGKQMDEVPVRVGLPFIPARDEAGRAVSSGTGAHNLREEVTMAGQADNPELVSSASEVSAAHARMDAPFGVRVEHGSELQANVIDPRSIQIVSLDNPRAFLYKRFMSDAECDFMVAHAKPNMYKSGVVNADSGGSSLSNIRTSTGSFLPLGMNDLVKRVEQRIASWSQIPVSHGEPMQVLRYEIGQEYQPHFDYFFHKGGSANNRIATVLMYLSDVEEGGETVFPNTQKPERRNETQFSKCGNTGKAVKPS... | Catalytic Activity: 2-oxoglutarate + L-prolyl-[collagen] + O2 = CO2 + succinate + trans-4-hydroxy-L-prolyl-[collagen]
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 438
Sequence Mass (Da): 47698
Location Topology: Single-pass type II membrane protein
|
D8IDY8 | MNITAKTTLTALFASPCKHSLSPIMHNKSFEKLSLDYVYLAFEVDKNNLKEAVASIKTLNMRGVNLSMPNKKEVIQYLDNISESARLSQSVNTIVNDNGVLTGHSTDGKGFIKSLEEENVNIKNSDVTILGIGGASISIITEFALYGVKEISVFKRDNNWTEQKKIIDNIQDKTNCKIELYTLDNKKELKKQIDKSKLLINATSVGMKEDASIIEDKTFFRDDLIVADCIYSPAKTKLLQIAEKENCKIINGMGMLLYQGALAFEMWTSKKMPVDYIKNIIFN | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.
Function: Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydr... |
A0A1F7FE20 | MQNKLRLLPSVDRALQNPKISAAATVYGPETVKNELRKALDSIRKEILANENAEIAAAEELIEMIADRVIAGCKIISQPSLRPVLNATGILIHTNMGRAPLGKKVFADICATITGYSNLELNLETGERGSRNIHASSLLKHITGAEEVLVVNNNAAAMVLALTTLAKDREVIVSRGELIEIGGSFRIPDILAASGAKMIEVGTTNKTRLSDYENAITTNTAILLKAHKSNFSVNGFTEEVELAELVKLGKKHNIIVLYDLGSGLLVKPATLPLASEPDVKSSLATGVDLLTFSGDKLLGGPQAGIICGRSELVKRLAKAP... | Pathway: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; selenocysteinyl-tRNA(Sec) from L-seryl-tRNA(Sec) (bacterial route): step 1/1.
Function: Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis.
Catalytic Activity: H(+) + L-seryl-tRNA(Sec) + selenophosph... |
A0A9D8PQD8 | MEKELKELEDMIKYTFRDKDLLRLSLTHSSYVKGEDVFGNERLEFVGDAILDLVIAKALFELYPDRDEGWLTQVRSGLVDDQTLFAKAESLGLGEYIVLGKGEASQGGRTKPSILSGAYESLVGAIFLDGGYEACESFVKSEFQSVLIVDDDHDPKNAKSVLQEIVQKESGDLPKYEVISEEGPDHKRKFVVAVYIDGVEKGRGEGRSKKEAEMAAASSALDIEE | Function: Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the o... |
A0A1Y1S156 | MEKINNFFVIEGLDGSGTTTQLHRIGRRSEGLSPVLFPTFEPTDNPIGQLIRKILHKEVTVPHDTLMRLFSADRSLHLFEKNHGILDRIASGETVLSDRYLFSSVAYQSLYASLDDVLQLNHFPLPQRVFFIELSPELCASRRKTRSKEELFDETEMQRKIRDNYYRAFECFPDLDIQIIDGSASIDEITRIIWRSLPYPPIE | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
EC: 2.7.4.9
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Length: 203
Sequence Mass (Da): 23532
|
A0A9D8KGQ5 | MEEKYMRRALTLARRYEGRTSPNPPVGAVVVLGGEVVGEGFHKGAGHPHGEAEALNAAGKRAKGADLYVTLEPCSHHGRTPPCTEAILKSGVKRVFIGTDDPNPIVMGGGARILEDGGVQVSFVEPGGRLGRDIRVLYEAYKKFVVEKRPFVVLKAAMTLDGKTATSTGDSKWITSERARRFVHGLRKRYDAVLVGIGTVKADDPELTVRLTVGRNPTKVIIDPRLEIDTGANIFTKGFTKGGADVIIAADEGADEEMAKKIEGTGATVIRLKRGEGREGGLDLDRLLSELARRNIMSLLVEGGAKVFTYFIKYGKFDKI... | 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... |
A0A2N3DM33 | MTPRIIIAARPFEEGKARLSAALSPAARARLNRRLFDHVLAAAGPERCIVVSRSAALLDRARAAGATGLAETGTELNAALTEAAAAAGEGPLLALSTDLPLLTPADIAAMIEAGASADIVAAPDASGTGTNALLMARPGLIPYRYGPGSFTAHQDAARRAGLHFARIDRPGLAQDIDTPADLARLPPDFRRP | Pathway: Cofactor biosynthesis; coenzyme F420 biosynthesis.
Function: Guanylyltransferase that catalyzes the activation of (2R)-3-phosphoglycerate (3PG) as 3-[(R)-glyceryl]-diphospho-5'-guanosine, via the condensation of 3PG with GTP. It is involved in the biosynthesis of a derivative of the hydride carrier cofactor co... |
A0A7K0K0Q5 | MCSDNPPLPGSMARARELVEILVSKGVRNWYYAPGSRDAPLGYALAGLAETRAIDLVVRIDERDAAFMALGAARVGKLAAVVMTSGTAVGNVLPAVMEAYHAQLPLLIVSADRPASLRGTGANQTTWQPGMFRNFVGFEADLQPEDGLAALREAALRAVEVSLNGSRENATNLGMALAEFSPNQPDLNRPLRNTPTDPGRSLSSTPLHNAPTNPAVQFASATPPSSPDPLCADAPTIPPHEFPGPVHLNVSFVEPLVPAEVEAAFAAKHPAPAPASVPVPVPASEPVSAPDAVAGPGFTGSVIIVGDNQGGPDWRAGERD... | Cofactor: Binds 1 thiamine pyrophosphate per subunit.
Pathway: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 2/7.
Function: Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting s... |
A0A1S8CZS7 | MKGKFIVIEGIDGSGTSTQSQLLFDYLNNQGNKSHLTYEPSNGPIGNLIREIFKGRVTVCSDEILFDKQLALLFAADRHDHLHNPIDGMENFLNKGLNVVCTRYFFSSYVYHSRTHEERQFLYEINKDFLKPDLIIYLDNPIDVSLARMSNRSVKDAYENIEKLKIVKKNYDLVIQEYQGEVVKIPADLPVQNIHQRIIDSINNL | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
EC: 2.7.4.9
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Length: 205
Sequence Mass (Da): 23651
|
A0A2X2YG99 | MSPTVAASVWRGWRWWVSHKVNGVSELHSNLMVQSLFADFASIFPTRFCNVTNGVTPRRWLALANPSLSEVLDENIGRTWRTDLSQLSELQQHCDFPLVNHAVRQAKLENKKRLAILIAQQLNVVVNPKALFDVQIKRIHEYKRQLMNVLHVITRYNRIKEDPEAEWVPRVNIFAGKAASAYYMAKHIIHLINDVAKVINNDPQIGDKLKVVFIPNYSVSLAQVIIPAADLSEQISLAGTEASGTSNMKFALNGALTIGTLDGANVEMLEHVGAENIFIFGNTAEEVEELRKQGYKPREYYEKDAELHQVLTQIGSGVFS... | Function: Allosteric enzyme that catalyzes the rate-limiting step in glycogen catabolism, the phosphorolytic cleavage of glycogen to produce glucose-1-phosphate, and plays a central role in maintaining cellular and organismal glucose homeostasis.
EC: 2.4.1.1
Catalytic Activity: [(1->4)-alpha-D-glucosyl](n) + phosphate ... |
A0A1V5W9M8 | MKFQRIFCVFSPLYWTLTYLRNKAYDTGLYSSTSFTTPTICVGNITVGGTGKTPHVEYICSLLQDTFRTAILSRGYKRKTKGYLLASPLTTVDELGDEPYFLYKKLQKTNVAVCEKRVLGVTKLLQDNPTIQAIILDDAFQHRAIKSGLNIVLIDYNRPIWNDCVFPGGMLREGTYALERAHSIIITKCPNNLTNTEMEMWKRKLHITKQTLFFTTIKYTSIYEAESKKQHDIPTILSSKHILLVTGIAQPKPMYTFISQYCKDITHLNFADHHIYTNDDYALILQQYKTYRTTIVTTEKDAPKILEITRNQLPIYVLSI... | Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 6/6.
Function: Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form te... |
I0HBP8 | MDVNHRTLPRRKVERTVTTRSEDTQTMDHAPQLIQERSAPPATLVIFGASGDLTRRKLLPAVESLARHNRLPDQFALVGVARTPMSDEQFAESALGGRSLAEKRQLNGGIRYVAGGYDDPETFKRLAEVLDELDAQRGTSGNRLFYLSTPAGAFEPVICGLAGAGLNQESENTFSRLVIEKPYGRDLATARELDGVVHQAFEESQVFRIDHYLGKDTVQNVLALRFANSIFQPIWDRSWVDHVQITVAETLGVGTRGGFYEHAGAMRDIVQNHVLQVLALALMEPPVSFEGENLRNEKVKLLQAIRLPTDRDIADAAVRG... | Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 1/3.
Function: Catalyzes the oxidation of glucose 6-phosphate to 6-phosphogluconolactone.
EC: 1.1.1.49
Catalytic Activity: D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-lac... |
Q0AZ74 | MLLDYHIHALAHGEYDYSESWLRLFAENARRERLAEIGFSEHDEYLPRIKPDKLKRLQEDFPELKIRMGLEVDYHPGREKEIQQMLVNSNIDYDYIIGSVHFIDGWGFDHPDFKAQFATQDIDDIYADYFSLVNQAVNSRLFDVVGHLDLIKIWGHRPVKKSILAYVEPVLNSIKAAGMVVEINSSGLRKAVGEIYPSRQILEPMLALNIPITLGSDAHHPSQLGEGLEEATGLAQGVGYRQLVTFSGRRRQLVKI | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 8/9.
EC: 3.1.3.15
Catalytic Activity: H2O + L-histidinol phosphate = L-histidinol + phosphate
Sequence Length: 256
Sequence Mass (Da): 29257
|
B1H0L4 | MNIKQIEDEYFMHTYKRGDLVVKETKNQFIWDENGRKYLDFFAGISVCNVGHCNEAVIKAAKKQLDSFSHVSNLYYAPPQIKLGEELVKRTFPGARVFLSNSGAEANECAIKIARKWGFLNPSKEGNRYEIICFFNSFHGRTLTTLSATGQDKFHKFFKPLQEKFVFAEINNMDSVKKLANNRTVAIMIEPVQGEGGIIPSDETFLKELRAFCDDNNFLLIFDEIQCGMGRTGKLYAFENYGIKPDIVTLAKSLANGLPLGASIAGEKCAGTFLCGDHGSTFGGNPVSCAAALAVLNIINSEFLNNSLKIAEYLRIKLEN... | Cofactor: Binds 1 pyridoxal phosphate per subunit.
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 4/4.
Catalytic Activity: 2-oxoglutarate + N(2)-acetyl-L-ornithine = L-glutamate + N-acetyl-L-glutamate 5-semialdehyde
EC: 2.6.1.11
Subcellular Location: Cytoplasm
... |
H3CDZ9 | AVISMCGHLFCWPCLHQWLEMRPSRQQCPVCKAGISREKVIPLYGRGSTSQEDPRLKTPPRPQGQRTEPESRGGFQGFRDTGFHMSFGIGAFPFGFFTTVFNANDPFHRPGNGNLNNGNNNWQDSLFLFVAIFFFFWLLSV | 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: 141
Sequence Mass (Da): 16049
|
E1QWQ9 | MVDDSSGRLVLVDLADRELGFCEKLPCHQKGLLHRAFSVFLFDGNKVLMTQRSLCKYHSGGLWTNSCCSHPRVGEGLDEAVARRLYEELGISGVTCREAGHYCYRATFDNGIVEYEYDHIFVGDYAGPLSLDPTEAMDARWVDAAHVARDVRKRPETFTAWLPGVLPIAFAAQAVRW | Cofactor: Binds 1 Mg(2+) ion per subunit. The magnesium ion binds only when substrate is bound.
Pathway: Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from isopentenyl diphosphate: step 1/1.
Function: Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isope... |
A0A1G2HME8 | MFSKKYRLSVKEFENTIKKGKSYSSKFFFLKLLKNNYGVIKIGVAVSKKLAPKSAQKNYYKRILRHLLKESCPKTSVHYNVILTAKENIKNVKFNDLKQDAIELLQKTELHK | 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... |
A0A1G3H2Q7 | MGGLGTAICKALSQSGFTVAANCLPNFPPRDEWLVRMKAEGFDFIVAEADVSNNESCAAMIKKLEEEVGTVEVLVNNAGITRDNLAMRMKDEEWDLVIETNLKSVFRLSKLVMRGMMKARCGRIINISSVVGEGGNPGQINYAAAKAGVAGLSRALAQELGSRNITVNCVAPGFIDTEMTRGLSDAQRDALLARIPLGRLGQPDEIAATVVFLASEQAGYITGSTVHVNGGMYMT | 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-... |
A0A671S2D4 | MAERGAHLTTAASAENRPSIFEVLAQDSLMSAVKPALLHAVKILATSNPARYGFLWQRFDEIYAILDVLLQHHFLSHTSASFSENFYGLKRVGEDGTRAAHLGLRRRQHWRSLFLLALLPYLHTKLEKVLARQRDEDDFSIRLPQSIMQKLYRAFLAAYPFVCMAWDGWVFCHQLLYVFGKTRTHSPLLWLAGVKLSYLTANDIHSLDLKPSGPALSPSQSFGEKFQRLVSTAVGGLAVSLSTSLSIGVFFLQFLEWWYSSENQSTVKSLTSLPTPPPPLHLHSQETSHTHIKVKLQQESEFLSPPLSPLSFNRPPKA | Pathway: Protein modification; protein ubiquitination.
Function: Component of a retrotranslocation channel required for peroxisome organization by mediating export of the PEX5 receptor from peroxisomes to the cytosol, thereby promoting PEX5 recycling.
Subcellular Location: Membrane
Sequence Length: 318
Sequence Mass (D... |
A0A2E1XFG3 | MNLLPQFGFFELMLVAVVALIVVGPKDLPKLMRSAGRMVAKARSLAGEFTAAFDQMAREAEMEELRKEIDELKKNNPVADAKRAVDEAVAPVEKEFRDEAREIDKAVREQTSEKSSAPSSASDKAASNPSANEAAKS | 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. Together with TatC, TatB is part of a receptor directly interacting with Tat signal peptides. TatB may form an oligomeric binding... |
A0A225MYF0 | MTLNPSPDPLPFDRAIAVKTFLRPIATHLEDPDVTEIAIVRPGELYTREHGAWQLHECQVLTYPHLEALATALAAYNHMAKAPILSVLLPRGERGQIVQPPACLDGTMAINIRKHTQAAFTLDELKAQGAFDAMADTAAECTTGNVSAIDQQLLSLKSAGDIPTFLHVAIQARKNLVVAGATGSGKTTFARSLIDRVPIDERLITIEDVHELILPRHRNRIHLMYGATRGRVSPTDSLAACMRLSPDRIFLAELRGPETWDYLAALNTGHPGSVTTTHANSAADTFNRLAVLIKQSPTGGNLDLETIQAFLRQTVDIVLY... | Function: Part of the Type IV secretion system.
Subcellular Location: Cell inner membrane
Sequence Length: 339
Sequence Mass (Da): 37499
Location Topology: Peripheral membrane protein
|
A0A0K8MDM2 | MFVSSEGFLPEFAPGSAEIFIGLSLLMFLVIGAFRGDSYTRTLGYLCIVVALMTVFIISFADKNTGIFFNGLFIRNSFTSFCKITILLTVSCVLWMTLRSLERENMARFEYPLLVLFSALGMLIMVSANDLMSMYLGLELQSFSLYILVALKRDRLIAAEGALKYFILGALASAFILYGSSFLYGLAGSTEFSSLFSVFKDPALTSSPPLVMGILLILGGLAFKLALVPFHMWSPDVYEGSPTPVTVLIATAPKIAAFALFIKLFVHMIGDLNIIWEQAVVILSVLSIALGAFAALFQNNIKRLLSYSAISHMGYALFGL... | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ... |
A0A5C7EG95 | MNATRSPFFLRTLEPIYTAIALVIVAYHGIAVLWTFHNAMEHYTVHLGAILLLIALYTAIDRGGATKGGKRLAWFVFAGVMAACALISTVYLYAMAQELELNQPFITGFQYFIGLILLIAVFGLNWVVWGTALTVVCLAAALYFGLGHLFPSPVVELKFSPEVVMSYLAGMGGPRGVYTFIPLSADTILLLLVYGGLMTSTLVLDMFEEIGKAIGNLLRGGVAYSCIAASSLVGMVTGQTVSCIALSGSMTIPTMIRGGFTKDQAGAIEVMAANGSQIIPPVMGLGAFLMAVILGISYVEVAAAAILPAFIYMITLAIAV... | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 643
Sequence Mass (Da): 68768
Location Topology: Multi-pass membrane protein
|
A0A839SR30 | MTAKQPKKPTQDRRPPALIVAGPTASGKSALALDLAEALDGTVINADALQLYRDLRVLSARPDAADESRAPHRLYGVLEARQAASAGLWRGLALEQMAEARAQGRLPILCGGSGLYIKALVEGLAPVPTVPIAVREAAAGELTRLGNAAFHAALTEKDPEMGARLRASDPQRMLRAWSVLEATGRSLAAWQALPSGDPAPYRFMIVVLMPPREVLRTRCDERFEMMLAHGALEEVGALLARNLPANLPVMKAIGVRELGAYLGGALSLSDATTQAQAATRRYAKRQATWLRTQVGLEGEGRLLLTEQYSESHTQKIFTKI... | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
EC: 2.5.1.75
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylall... |
A0A238UMH1 | MGSRRAGGIKKVKRLRVKNPDNMKVPYDLNSYIRVLKLASTPSMDEFMQVSKIAGAGIILVGVIGFLIFAIMSLLPGVGA | 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: 80
Sequence Mass (Da): 8620
Location Topology: Single-pass membrane protein
|
A0A7J8GR04 | MGNVPSAVKHCLSYQQLLREHLWIADSVAGALDPAQEASQLSGLPEYVKIVEVGPRDGLQNEKVIVPTDIKIEFINQLSQTGFICKAVNKTTNSKVAQASFSA | Pathway: Metabolic intermediate metabolism; (S)-3-hydroxy-3-methylglutaryl-CoA degradation; acetoacetate from (S)-3-hydroxy-3-methylglutaryl-CoA: step 1/1.
EC: 4.1.3.4
Catalytic Activity: (3S)-hydroxy-3-methylglutaryl-CoA = acetoacetate + acetyl-CoA
Sequence Length: 103
Sequence Mass (Da): 11153
|
A0A0R6I707 | MGTLYLLFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGIEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGISSILGAINFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWF | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A0P9UBJ2 | MFDLLNCMVMIPKMDELLPACNEGRSTFAMKMGLYATNAGAGLTSDLAQSYVPPDLWKRYRSGFFEFGGVPVDKLQKTLEEWKEMLDPAQYQVCRLKGTERPFSGKYNETKTEGVYHCICCNEPLFDSTTKFDSGCGWPSFYAPLEGSAVVEVRDVSHGMIRTEVVCAKCDAHLGHVFPDGPPPTGLRYCINSVCLELVPRQ | Cofactor: Binds 1 zinc ion per subunit. The zinc ion is important for the structural integrity of the protein.
EC: 1.8.4.12
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol + L-methionyl-(R)-S-oxide-[protein]
Sequence Length: 202
Sequence Mass (Da): 22556
|
A0A931Q842 | MDYSYIYNIECGGQMEIRSHIKEGIILIDKPKGLSSYDVIRRLRREIGMEKMGHSGTLDPLATGLMIVGVGIGTKKLSELIKLPKTYEAEILLGIRTTTCDMEGEVLDEKSPLELDLSEIAPLLESMRGKIVLEVPVYSAVKVKGERLYELARAGKRVNPPEKEMEILNTVFKKCFRSESYYILELVMEVTSGTYIRSIAEEIGRRLGLPATLNNLRRTKIGNYKIENALKLD | 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: 233
Sequence Mass (Da): 26271
|
H3CE99 | QDALTVVVEDLRLCSVKPFEDIERRFCFEVLSPSKSCMLQAESEKQRQAWIQAVQASIASAYRESPDTSEEKRLDRAASPSTSSIDSASEARERGARGDAILQRIQALPGNQQCCDCGQADPRWASINLGVLLCIECSGIHRSLGVHCSKVRSTLDSWEPELLKLMCELGNAVVNRIYECSSQDGGSRKPLPSSSRQEKEAWIRAKYVEKRFLKKACSAHAGQRKPERRRQECRRHSSSNSLAKTRRRYRQEVGSASPSTLSAEAAKFRRESLFCPDELDSLFSYFDTGSGPRSLSSDSGLGGSTDGSTDFLLFGSVAEE... | Function: GTPase-activating protein for the ADP ribosylation factor family.
Subcellular Location: Endosome membrane
Sequence Length: 506
Domain: PH domain binds phospholipids including phosphatidic acid, phosphatidylinositol 3-phosphate, phosphatidylinositol 3,5-bisphosphate (PIP2) and phosphatidylinositol 3,4,5-trisph... |
H3CQL6 | CDLNYYGPLCNKFCRARDDFFGHFSCNLSGSKVCMEGWTGPECKEAVCKQGCHQSHGFCSEPGECKCHYGWKGPLCDQCVTFPGCVYGSCTEPWQCVCDVNWGGLLCNKDLNYCGNHQPCKNGGTCTNTEPNEYQCECQEGFRGRNCDIAVRQCDRSPCGHGASCQEIPGGFRCLCPPGWTGRTCQLDANECEVSVCIHAHSCHNLIGGYLCDCLPGWVGPNCDIRNSSCQDLCQNNGHCEDLVSGSRCVCPPGFSGTYCQNAPRPCEGAPCLHGGQCVETAGTSATCICPAGYSGNLCERALDLCDPNPCQQG | Function: Putative Notch ligand involved in the mediation of Notch signaling.
Subcellular Location: Membrane
Sequence Length: 314
Sequence Mass (Da): 33848
Location Topology: Single-pass type I membrane protein
|
F9Z9I0 | MKKNVVVIAGGNSSEYEVSIKSGNHIFSEVDGEKYNKYLMILRGRDWMVEIGDQKFPVDKNDFSFEYQGKKVVFDFAYITIHGNPGENGMLQGYLDMMGVPYSTCNTLVEAITFDKYTCTNYLNAFGINTTHPIMLVRGKAFDKEAVLKAVGLPCFIKPNAEGSSFGVSKVKTAADFDAAVEGAFKMCREILVESFIDGIEFTCGLYKVGDKKVVMPVAEVVPKKEFFDYEAKYDAKMSDEIIPGRFSAEITGRIQDMASEVYDILRCEGIVRIDGFVRGEEIIMLEVNTTPGMTANSFVPKMVRVMGLPLRDVITGIIE... | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
EC: 6.3.2.4
Subcellular Location: Cytoplasm
Catalytic Activity: ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) + phosphate
Sequence Length: 326
Sequence Mass (Da): 36... |
D8ICH4 | MLLENRPPYSFIAWLTVLVFLPYVGAIFYLFLGVNWKKSRKKLSARLPEDMIRKHFSSLLEEQMNIIDNMGGNYAKHTNLVKLAIKSGYSPITVQNQVYVFDEGKDLFDDLINNLKLAEKTIHMEYFIWRSDELGNKIKDILIKKSKEGVKVRLIFDGLGSMLRISRKYKRELKKNGIEFLYYHDPFSIFWTRYVNYRNHRKIVVIDGIVSYMGGMNLGQEYIDGGKRFASWRDTHMRIVGDACNLIQNVFVCDWHNAGGRDLDNLMDNGSSLMQELFPSSTTDKYLPMQIISSGPDSKWDSIQKIYSKMIADAKESIYI... | Function: Catalyzes the reversible phosphatidyl group transfer from one phosphatidylglycerol molecule to another to form cardiolipin (CL) (diphosphatidylglycerol) and glycerol.
Catalytic Activity: 2 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) = a cardiolipin + glycerol
EC: 2.7.8.-
Subcellular Location: Cell inner ... |
A0A2N5G5I8 | MKKTAFFLILISLIGKFLGFGKYVALSYYFGAGIISDAFVLSITIPTVIFAFIGIGLSTSFIPVYNDVLSKNGQEYANRFTSKLITLLLFINTALVALVFFNTDTIIKLFASGFTTEAIKLTNTLIKVSIIGVYFSGTIYILSSLLQVKKIFIIPAISEIPINIFSILGIYFASKGNIVYIQLFTIIGTIIQFIILYLLTIKHGYRYKFHNNLFDENVKKLLKNSIPAVLGISVNQINIIIDRTIASHIIIGGLAILDYANRITDVIQSVIVLSIISLVYPQVSKQAVSEDFSKVNYTIYQSVVSIMSIIIPITVYYIVF... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Involved in peptidoglycan biosynthesis. Transports lipid-linked peptidoglycan precursors from the inner to the outer leaflet of the cytoplasmic membrane.
Subcellular Location: Cell membrane
Sequence Length: 498
Sequence Mass (Da): 55258
Location Topol... |
A0A2N2L1Y4 | MKPQIDIVIEEGISPELERIEQIAETIWEEERVQGEYEISILFCGDDRMRELNRQYRGCDSVTDVLSFSSKAFDLALGVQGEKWICDIIIDTKYIQSQKGSNGYTQEIEEVLIHSFLHILGYDHMKTKDKEKMETKENYYKQLLQGVS | Cofactor: Binds 1 zinc ion.
Function: Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 148
Sequence Mass (Da): 17260
|
A0A1Y1S0G2 | MAISHAVINEISDKTSMVDLVSEYTSLRFSGGQYSGLCPFHSEKTPSFSVNEEKKLFYCFGCHKGGNLFQFVMEMESLNFSEAVHYLGQRAGVEILEEKDRQNQSRVGALFDLYAGVTRSFHYLLKETGTGKKALDYLYARGFSDDIIDTFQLGYAPQDPNWLYDFLKKKGYSSDFLAESGLFSRNDSRYPLFRNRLIIPIASTQGRVIAFGGRLLEGEGPKYLNSPETPIFRKSRTLFGLDKAVKAVRSSGRFFLCEGYMDVMALYQAGIPESLAPLGTSFTQDQANLLKRYADRGILLFDNDDAGQAAAAKSIVLCAK... | Cofactor: Binds 1 zinc ion per monomer.
Function: RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.
EC: 2.7.7.101
Catalytic Activity: ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.
Sequence Length: 583
Domain: Contains an N-termi... |
W5T0N9 | MILLLAVKGPAISAVAKALDICTIAIRKTIDAGLKKVKEAMKISPNDTLISFDKQPLKLKTSTINTENIKSFKGNAFLNLM | Function: The Vlp and Vsp proteins are antigenically distinct proteins, only one vlp or vsp gene is transcriptionally active at any one time. Switching between these genes is a mechanism of host immune response evasion.
Subcellular Location: Cell outer membrane
Sequence Length: 81
Sequence Mass (Da): 8773
Location Topo... |
A0A381GYN6 | MATAFAVRSTSGIEVAIITGRKAKLVEDRCATLGITHLYQGQSDKLIAFGDLLDKLGVAPENVAYVGDDLIDWPVMEKVGLSVAVADAHPLLIPRADYVTHIAGGRGAVREVCDLLLLAQGKLDEAKGQSI | Pathway: Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis.
EC: 3.1.3.45
Catalytic Activity: 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + H2O = 3-deoxy-alpha-D-manno-oct-2-ulosonate + phosphate
Sequence Length: 131
Sequence Mass (Da): 13868
|
H3C1V7 | MPAKTYRLGVFVELRKRLQTGLIIVGKDLTTNPGDVSVTGGDSCLNIRTPSKSLSLALPAGVTLEQGSCIPTPAGQSCGDELHFRLRITVSKGPGPEASDSVTEKLRAKRTYCFYCQSCMTRLLEDREFKRVLPLPNGNWNALVDDWCCHPDPFANRKLLPRADDCLLGDSFFLLTRDGSCEQTLAEEGCIYLCLCYFQKTCRRLALVSCQCCSSVVGEAVSPETLRLYITQVVVEPAEGDGNPEPPLSRSVFLERTIAARLLELSSSLSTFHFSVQTPDGKPFLLLWMLNGDSVVASVPETCDEAERSPGPAAASSCDP... | 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: 2.3.2.26
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine... |
A0A1S2R9K6 | MKYYYSQYERPEIGKLYLLADEEALVHMTYNPADFEKHAAACHPAQMDEHQVFKELRIWLDGYFSGVNKEFTIPLRENGTEFQKQVWNRMKEIPYGETKSYSEIAYEINRPKAVRAIGQASKANPYPILVPCHRVVGKKGQLTGYAGSKTDIKDRLLTLENKNWATRQIN | Function: Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irrever... |
A0A2H6HTP8 | MDLLHHPLAFAMLASYFIGALPTAVIIAKRVGNIDILEQGSGNPGASNIYRLFGPQWASATLMVDLFKGYLPVVLSQQFASSMIHPIYAQNEIAVMVWVGFAAFLGHVFSPFLRFKGGKGAATGMGATFAIAPQATTLAILVYGVALFIWKKFAAGTLAAALSFPIFLYFREGGQEPESLIWGLLVPILLVTTHRQNIARIMHGDELPMNSAKGENKEG | Pathway: Lipid metabolism; phospholipid metabolism.
Function: Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
Catalytic Activity: an acyl pho... |
A0A7K0K215 | MLLTMLKTAAEGDLALYDKVLWPFMWIIGWIMRGIHELLGLVGVSQGVGIGWVLAIIGLTVFVRLLLVPLFVKQIKASRAMTLAQPEMTEIQKKYKGKRDQDSLMRMQEETKAVQKKYGASMSASCLPVLFQMPIFLALYRLLYNMKPVADGTLPGNDAIGGMGQVQAQNLWESTFFGQSLGLTMFGPGSDMYTKIVIGIMVAYLVLSMLFQTMFLTMKNMSYEQLHSDNPMVKSTKSMLYFMPLVYLFTGPVVQVGLLIYWVTSNTWMIAQQFFIIRSYPTRGSDAAKWREPAHEKKFEAYRAKEEARLASEIEKINLN... | Function: Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispa... |
F2I5X5 | MLFFSWTCDQEVYVKTFLRQKGVSRRQLAKIKYHGGTIIVNNKRVGSKYFLSLGDQVTIIYPAEGSQDQIMAVDFPLDILYEDRDYLIVNKPAGYTSIPSQFKDEYSMANFVKAYFVRKNYENQVIHVVTRLDRFTSGAMIFAKHKYAHSQIDQLMQSGGINKQYLAFTHSAIGSDQHGLIEAPIGRKEGSIIERCIRADGQHAKTEYWLEDSQAGLYRYRVQLHTGRTHQIRVHFAYLGAPLCGDDLYGGSQEAGLSGQALHCQRLAFKQPLTQEDLVIEAPLSQDFKTWLASYQKGDA | Function: Responsible for synthesis of pseudouridine from uracil.
EC: 5.4.99.-
Catalytic Activity: a uridine in RNA = a pseudouridine in RNA
Sequence Length: 300
Sequence Mass (Da): 34123
|
A0A969FRB8 | MPTAPTPRPRPSDADALPHRVRQRLIEHQLWHRECLVVVAVSGGPDSLGLLHALWRLRTEDDHGPALHVAHLDHRFRGSQSEEEARFVAHIAHEWNIPATVEPYDVPALAQATNQNRQAAARAVRYAFLARVALAVGADAVAVAHQADDQAETVLLHLLRGAGPAGLRGMRVAVAWEEWRGEVPGFEGAAAVSGNRPLLIRPLIDCTRAEIVQYCDEHRLAPRHDPSNESRSYTRNRIRADLLPHLAEYNRQIVAALGRTAQVCADDYAGIQAQLDAVWTADLVRPHEASLRFCKARWAQLLPALQRYVLRRAARLLTGT... | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34)... |
H3CDQ3 | VKSKKKKLKKKLKAADHHSNQPQDQDEGMMGDGQAPPLFSAPHSQPGGRGSLGRTREHFQSERVDQLRHSDLINDYVEPRQTWTTREVAMKVHSSFRVLGLFSHGFLAGFAVWNTVVVYQLAGEQLSSLRNLLQQYQKLAGPAQSLSYLLLAISSVSAFDRRLNLARASMALRGFLRLESAALAFFCGLVLLWSAEQTGPDLHRGSLFSANQTLWPPSSEQQVLRPWMVVNLVVALLVGVAWVVVSTRPNTDYTADFLLTMEVDGLPRADVSLDVQA | Function: Component of the transition zone in primary cilia. Required for ciliogenesis.
Subcellular Location: Cell projection
Sequence Length: 277
Sequence Mass (Da): 30736
Location Topology: Multi-pass membrane protein
|
A0A2H1WCA1 | MKHQRRYKCVAGLLGVRNLRVAQESGIRRRVVVSLRSSQPIRVKARLSQSLTLTFRYYFRLSNILRRTLNLIAYPGDIRRSLFSSYRLLNRFCYVPRRLIAPKPNTYTFTKAVAESAVSERAPAAHYACAIFRPSIVVSSLRHPFPGWIENLNGPSGV | Function: Catalyzes the reduction of fatty acyl-CoA to fatty alcohols.
EC: 1.2.1.84
Catalytic Activity: a long-chain fatty acyl-CoA + 2 H(+) + 2 NADPH = a long-chain primary fatty alcohol + CoA + 2 NADP(+)
Sequence Length: 158
Sequence Mass (Da): 18093
|
A0A2H1VFU9 | MPPPSRGIGFGIPYLITIFMGVRVVLHYISALNDPAVQSYLLYSSVLGLKVLSMAFLTARVRYAKNVFANPEDAAAKKGKVKYDDPDVERVRRAHLNDLENIPVFWVLGALYLTTAPSAWLATTLFRVY | EC: 2.5.1.18
Subcellular Location: Membrane
Sequence Length: 129
Sequence Mass (Da): 14404
Location Topology: Multi-pass membrane protein
|
A0A6V7TYG3 | MGKLPKNFALLKRSENQRISRRRLQENSSFSSNVSSGEDDKKELLDDIVTDWKDSDWAPSISAVFKILFSIRLSASLWSIISDCDEVYNYWEPLHLVLFKRGFQTWEYSPVYGIRSWLYILLYAGPAKFLIKIFPESKVALFFSLRFLISFFTLFSELFLYRAICQRISNSIGRTFILFSTFSSAMFGASCAFLPSSFSMSLNACASAFYLFEYWSLSIFCTAISALIGWPFSAILGLPIVIEMLIIRKRKLALKFLFYSILFGLSICLLLFIVDTHFFGRPVLAPLNIIFYNIFSSNGPNLYGKEPISFYLKNLFLNFN... | EC: 2.4.1.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 590
Sequence Mass (Da): 68672
Location Topology: Multi-pass membrane protein
|
A0A2H1WMJ1 | MHNIRGDLVVGVRSSSDAMNSSVERDETFSPKTKKKLSKKPSFIKNAVLDLFRSKTKNSQKVSRQKSLCESDLQQRHNVPQMPMLRREKSDLSDMSIHMRNQQIRNQMLQRSNSSSCEKPVLKPILKRQSSFCDERNGSICTVRDYDAKPVMKSLRRQNSMCDIETEPKVTPLLRRQNSLIEYNRRGIYGQSPSFNMITKIDPIYQRQQQVKHEPFHPTQPLPPEPVYQSKDHLVYDPIPKPRRTYTSVYDTSTETPYASRSEMSNQSFENPYGNKQTIGMPLMDPPYATRAECMKESPYATRAECARESPYATRADCVR... | Function: Receptor for netrin required for axon guidance. Mediates axon repulsion of neuronal growth cones in the developing nervous system upon ligand binding.
Subcellular Location: Cell membrane
Sequence Length: 997
Sequence Mass (Da): 113000
Location Topology: Single-pass type I membrane protein
|
A0A7J8E3Y2 | MSVLAQAGGRWRSAAARAVIPCLWRGKYFCSGKEPVENNPVTPMLRHLLYKIKSTGPITVAEYMKEVLTNPAKGYYVYRDMLGEQGDFITSPEISQIFGEVISI | Function: Arginine methyltransferase involved in the assembly or stability of mitochondrial NADH:ubiquinone oxidoreductase complex (complex I).
Catalytic Activity: L-arginyl-[protein] + 2 S-adenosyl-L-methionine = 2 H(+) + N(omega),N(omega)'-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-homocysteine
EC: 2.1.1.320
Subce... |
A0A7S2S3D3 | ASGEVTKLIARMGIDRIGFTLLGSLGCVAAYGCFMLHLERNKQLFYLDKVAKRTTVEEAVRDDDPEKLVLIKGVVESQGETLVAPKSQVGCVYYNLTKKRITEDMVKTKERKSKKSSRKGETKTSETTYPSFITSESVVEEHSDQANWAVVSLEGHVESVLPVEGNVKLASQPFVELEESFNQFEEPKGGGNKRTVGYRYTEKILRSGTPVFVIGCIHQTTNGPVLCEPAQGPFIISTYTPSELTSKLKAQKRGWLFVSIILASVG | 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: 266
Sequence Mass (Da): 29357
Location Topology: Multi-... |
A0A6V7VNX5 | MISNARIADTLASDGHNVTLLEVGFREVALNASKVANKILVPGPFIDSKEYDPSLMAKMAFKEVDLTMDFIVGSIWLTTFNNACEKFLLVSEKLFDKLRNEKFDIIISEQLNFCGAGVGHLLGIPTNILVSSCPIQEHVASILGLSNPASYVPSLYYSNLPDKMSIYERTTNLFRQYAGYVYLIYGVDPLTKIFKKHYGATFPDLRTIVAESPFVFVNVDEFLDFPRPIFSNIIYIGGLGMEEGKNTKINKIEVFIWGPSKTSILFIVSPYPFR | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
EC: 2.4.1.17
Subcellular Location: Membrane
Sequence Length: 274
Sequence Mass (Da): 30722
Location Topology: Single-pass membrane protein
|
A0A6V7XVM7 | MDTLKIGCLLQGNFLAKLPCYPHEQRNKPNIQHAPIRSVPLNKEEIKLAVKNILRYVPSRFHKELAAPPIEQIKCSNRQAAAIVLMILNNLDPDIAQFPQELVTYGGNGQVFSNWIQFRLTLRYLGEMDENQTLIMNSGHPQGLFPSHADAPRMVISNGMMIPNYSTKELYDKYFALGVTMYGQMTAGSFCYIGPQGIVHGTTITLMNAIQKYLGRGTSPSGKVFVTSGLGGMSGAQAKAAVIAGCIGVIAEINEKAIKKRHSQGWLDIYSSDLEEIICWIKQNKAEKKSISIGYLGNVVDLWERLVAEPEGTILVELGS... | Pathway: Amino-acid degradation; L-histidine degradation into L-glutamate; N-formimidoyl-L-glutamate from L-histidine: step 2/3.
EC: 4.2.1.49
Catalytic Activity: 4-imidazolone-5-propanoate = H2O + trans-urocanate
Sequence Length: 337
Sequence Mass (Da): 37265
|
A0A223PK73 | FMGYVLPWGQMSFWGATEITNLLSAIPYIGTTLVEWIWGGFSVDKATLTRFFAFHFILPFIIAALVMIHLLFLHETGSNNPSGIPSDSDKIPFHPYYTIKDLLGF | 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 membra... |
A0A6V7UGY8 | MSDKSGIRLNDIVQMATEKENIEPEYRMRTIESLARHIEAALRYQHTATSRTQYTLHRVFKCFNLRYYESYVTGMYLATKVFYVGNVLTNLLLVNKFLETNNYSIYGLGVLYDLLLLGKSWTQSGNFPRVTLCDFEVRVLGNIQRHSVQCVLVINIFNEKIFILLWLWFCILFFITLFDGLYWFSVSLFHRDRFRFVLRHLELTSDPDRPELFRKEKRKQVEHFLKAYLKVDGVLVLRMIALHAGVMYCTEITDALWKRYLSQHPENLIDEDSVLINFARTQSIRRRIGCSASSTSLAPNHNGSSGGSAGRRVIQRNAHA... | Function: Structural component of the gap junctions.
Subcellular Location: Cell membrane
Sequence Length: 593
Sequence Mass (Da): 66815
Location Topology: Multi-pass membrane protein
|
Q4SRM3 | SKDDAPNDTFMIPRKEINMVTDMGKWKQSQAYADYMGFVLSLNKVVKGKKLTCEYKVSETVQKLLQLLGTLEQWIIETPPVDQPSRFDHPTLEPRHFIDAKVVNEHHQDYMFLDCIKFINEMKTGPFAEHSNQLWNISAVHSWSKVNQGLIKMYRAECLEKFPVIQHFKFGSLLSIQPVK | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
EC: 5.2.1.8
Subcellular Location: Cytoplasm
Sequence Length: 180
Sequence Mass ... |
A0A1C6C2I5 | MKNEDNTNNKNKKKKGRKKRRPGRIIRNIILGIVIAFAALFLLGNLFFHYKYGETIFSCAKFGKEAVAESTADTFRPNQASTVYSSDGKEIAKLYEDTESTYLDFDNIPKNVINAFVAVEDRTFWKNSGIDVKGIVRVSLNFLKTKGDVAQGASTITQQLSRDIFLTNEKSLVRKVKEIFIAMNLNKKYSKEEIMEYYCNNVCFANGIFGIEDASQTYFNKPASQLTLSEAAYLCAIPNRPEYYNPFKDSSNAITRRDKILEDMYECGYITQQEMNDAVSEEITIAKQEDNDEFYNYETSFAIKCATEYLMGYLYDFNFQ... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-term... |
A0A921ML48 | MQRITVIGSVNRDHLYSVPHIVRPGETIASESYRTGWGGKGLNQAIALAKAGAQVSLAAKIGHEDYPSLSALCSAYSLDISQVHACALPTGHAIIQLDTAGQNCIIVHAGANGSFTEQDIQSFLAGCRAGDIFLLQNEINSSAQIISEIKKKGGRVALNPSPFTPDILRWPLECLDYLILNETEAASMTSADSSEKALDHLCSAYPALNVFLTLGSEGSCFACGNTRHFHPTHKVNAVDTTGAGDTYTGFLLAELARGSAVEDAMSIATEAACLCVTRPGAVDSIPSRAELPSLN | 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 ... |
A0A839SPG3 | MAPGINIIAILLVGAAIGSFISALVERLPDCKGLVAGRSRCPDCGETLKVRDLIPLVSYLLLGGACRACGKAIAWVYPVAELGALFLALTVIVVFRDPATAPGTLWLAAGLGWCLLALILADVRRFLLPDMLVLPLMAAGIASVFLEPQAQWQSIGMARIFGAALGFVLMEAVRRLYFWIRGRDGLGFGDVKLMAAGGAWLGWPLLPHSLALAGILGLVTVFILRLTGRVLGPSDALPFGAFLAPAIWILWILGKTAPDFIGILVGF | Function: Plays an essential role in type IV pili and type II pseudopili formation by proteolytically removing the leader sequence from substrate proteins and subsequently monomethylating the alpha-amino group of the newly exposed N-terminal phenylalanine.
Catalytic Activity: Typically cleaves a -Gly-|-Phe- bond to rel... |
A0A2H0B6M7 | MTIFQAFILGIIQGLTEFLPVSSSGHLALVQHFMGLPQVPIAFDVLLHMATLLAVVYILSRPINDLVVKTYKAIVSRKINQIPKLLWLLIIGTIPAAILGLLFNDYMDTIFQSVRYFSIGFLITSILLNIASHIRSQEKSLKQMSLMESFKIGVFQAIAIFPSISRSGATISGALLAGFGVKDAFTFSFLLSIPAILGASILHIKQIFYINSSQIPAYSVGFIAAAISGYIALLVFRQTLINKKLSIFAYYCMFLSLLIFFFVK | Function: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate
EC: 3.6.1.27
Subcellular Location: Cell membrane
Sequence Length: 264
Sequence... |
A0A7J8ER24 | MVNPTVFFNFAVNGEPLGCVSFEQFADEVPKTAENFCALSTGKKGFGYKDSCFHKSILGIMWPGGDITRHHGTGSKSVCGEKFDDENCILKQAHGSWPLVHGKYWTQHRRLPVFRLHCQA | 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: 120
Sequence Mass (Da): 13432
|
A0A1C5WB81 | MTKKEFKQLTDQKILILDGATGSNLQKRGMPAGICPELWITEHPETLQQLQSEYIKAGSDILYAPTFSGNRIKMEEYGLGDQLEEINTKLVQICKENAAGHVLTAADITMTGAQLEPLGDLKFEELIQVYKEQLSILAAAGVDLIAIETMMSLQETRAAVIAAREVCPELPVMAALSFTEAGKTLYGASAESAVAVLQELGVDAVGLNCSAGPDKMKAVLKKMAEVSKIPLIAKPNAGLPSLDENGNTVYDMNKEDFCTYMKELIGEGAQLIGGCCGTNPEYIAELKALTKSFERPVKTGKSKLYLASEREVFAFTEGQQ... | Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-methionine from L-homocysteine (MetH route): step 1/1.
Function: Catalyzes the transfer of a methyl group from methyl-cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor u... |
A0A1C5NHF1 | MEAGMITTVLLVACATICIGVGIFYFFINNTKNKGRICILLLGIGGGIWALGSALYGNCTDDRLAQDFFCMTIVGFNLYVIAIVIYVACLTGVKIKGYGLMVGLGILTSLVDGVSFGSMRIRHFYRVNGRTCFTTEFHGSVFYHWMYIMLCFLCCIYIVLYWSKKIMRKSQRKYVAYIILGNTIMLLSAIPDTVLPFYGIKSYPSSVYGVTVSFLMTVFFSIRYDTFGISKLTVSDYLFNQIDYGVMVYDYQRTHILHNTNAEVLFGADVEQPFEELVACGGKKEEFAEQLYQGKLEHCKVKCLQGNQILSVTSSMVCDE... | Function: May play the central regulatory role in sporulation. It may be an element of the effector pathway responsible for the activation of sporulation genes in response to nutritional stress. Spo0A may act in concert with spo0H (a sigma factor) to control the expression of some genes that are critical to the sporula... |
Q4TBT6 | MVHYSSEVLLREVCDSESGHNLPTVLVEITATVLDQEDDDDGHLLALQIIRDLVDKGGDVFLDQLARLGVINKVSTLAGPASDDENEDESKPEKREPGRRIRQLRFLQTAFGRLLADPRNAHPLFCAALPLAAESRSEFLEKLQRARSQVKPVTSSQPILSTVAPTKLTVGNWSLTCLKEGEIAIHNSDGQQATILKEDLPGFVFESNRGTKHSFTAETSLGSEFVTGWTGKRGRKLKSKLEKTKQKVKSMARELYDDHFKAVESMPRGVVVTLRNISTQLESAWELHTNRQCVEGENTWRDLMKTALENLIVVLKDENT... | Pathway: Protein modification; protein ubiquitination.
Function: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates.
EC: 2.3.2.26
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugati... |
L2GX65 | MLKYINLYNLAGTLVGAFALSSIALNYFSKNMHFIFRIALCQSFYILEVLNILTNASKSRLFPTCMQLSSRLFIIWCICYRYGFADAVVHIMLLCWFVSDTVRYLFYFSRNGTVKFLRYNLFIVLYPLGTLCEIVLVSRVERACTGVLKYFLRVVMLCYIPGFSFLYVHMIRRRRWTDKNRSAAQRKKDK | Pathway: Lipid metabolism; fatty acid biosynthesis.
Function: Catalyzes the third of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzy... |
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.