accession stringlengths 6 10 | name stringlengths 6 11 | Full Name stringlengths 1 147 ⌀ | taxon stringlengths 3 46 ⌀ | sequence stringlengths 16 2.75k | function stringlengths 6 5.51k | AlphaFoldDB stringlengths 6 10 |
|---|---|---|---|---|---|---|
A6ZRR2 | MDG1_YEAS7 | Multicopy suppressor of defective G-protein 1 | Saccharomyces | MQSSLPQFTFKWPKGPEAIILTGTFDDWKGTLPMVKDPSGAFEITLPVTFDSPSSKFYFKFIVDGQWLPSKDYKVNIDEGVENNFITEEDVIKQRENGSSTLVPESTGLAVSKNAPLIEPEAEKRAKKLRKFKIKRVIKTNKQTGERSIFSQEVVELPDSEDETQQVNKTGKNADGLSGTTTIIENNVGVNEEKAIKPYEENHPKVNLVKSEGYVTDGLGKTQSSESRLYELSAEDLEKEEEEEDEDKGGGKDTSTSADAEASEDQNKEPLSKSAKFEKPEEKVPVSSITSHAKETSVKPTGKVATETQTYETKQGAPTA... | Involved in G-protein mediated signal transduction and in the regulation of polarized cell growth in pheromone-induced cells. | A6ZRR2 |
K7NBZ9 | CUCS_SIRGR | Cucurbitadienol synthase | Siraitia | MWRLKVGAESVGENDEKWLKSISNHLGRQVWEFCPDAGTQQQLLQVHKARKAFHDDRFHRKQSSDLFITIQYGKEVENGGKTAGVKLKEGEEVRKEAVESSLERALSFYSSIQTSDGNWASDLGGPMFLLPGLVIALYVTGVLNSVLSKHHRQEMCRYVYNHQNEDGGWGLHIEGPSTMFGSALNYVALRLLGEDANAGAMPKARAWILDHGGATGITSWGKLWLSVLGVYEWSGNNPLPPEFWLFPYFLPFHPGRMWCHCRMVYLPMSYLYGKRFVGPITPIVLSLRKELYAVPYHEIDWNKSRNTCAKEDLYYPHPKM... | Oxidosqualene cyclase involved in the biosynthesis of the highly oxygenated tetracyclic triterpenes mogrosides and cucurbitacins . Converts oxidosqualene to cucurbitadienol . | K7NBZ9 |
Q01822 | HXD1_MOUSE | Homeobox protein Hox-4.9 | Mus | MSSYLEYVSCAAGGGSGGVGGDVLGFAPKFCRADARPVALQPAFPLGSGDGAFVSCLPLATARPTPSPPAGPAQSPVPQPAAPRYAPCTLEGAYERGAAPASAAEYGFLGSGPAFDFPGALGRAADEGGAHVHYATSAVFSGGGSFLLSGQVDFAAFGEPGPFPACLKEPADGHPGPFQTVSPAPGACPKPASPTSSLPAAHSTFEWMKVKRNAPKKSKLSEYGATSPPSAIRTNFSTKQLTELEKEFHFNKYLTRARRIEIANCLQLNDTQVKIWFQNRRMKQKKREREGLLATAASVASIKLPRSETSPIKSGRNLGS... | Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Acts on the anterior body structures. | Q01822 |
D2Y495 | O161A_CONCL | Conotoxin Cl6.1 | Californiconus | MKLTTVLVVALLVLAACQFTVTDNSGDDPENPSLRSVGENQNPDSTKTITAWATRDMTNMRRGLNRPSKRCLAGSARCEFHKPSSCCSGHCIFWWCA | Probable neurotoxin with unknown target. Possibly targets ion channels. | D2Y495 |
Q6FF50 | RLMB_ACIAD | 23S rRNA Gm2251 2'-O-methyltransferase | Acinetobacter | MAKPEYYYGVHSVESLLELEPERVLTLFTLKGRDDQRLQKILELAEPFGISVQKASRDSLEKLAGLPFHQGVVAAVRPHPVLNEKDLDQLLQNNDQALLLALDQVTDPHNLGACIRTAAAMGIAAVIVPRDRSASLTPTARKVAAGGAEKVKFIQVTNLARTLAHIKAHFFVKVVGTMLDEKALPIQKYDFSGNVAIVMGAEDTGLRPITQSQCDQTVYIPMSGNLQSLNVSVAAGMALYEACRQRLG | Specifically methylates the ribose of guanosine 2251 in 23S rRNA. | Q6FF50 |
Q8NP37 | RIMP_CORGL | Ribosome maturation factor RimP | Corynebacterium | MAFPTTEILSALIEPLAASHKFDLEGLKVTKAGPKSAVAIKVDSDSRPDLDQLEVFSQEIGELFDAAEQRGELNFGAGYTLEVSTPGVDNPLTLPRHWRRNRGRLVALDQDGKKRVARIGALNDAETHVVLIERNKKLLEVTTLELAHSPRAVVEIEFAKPAQDETALAESTFDEATA | Required for maturation of 30S ribosomal subunits. | Q8NP37 |
Q81HM5 | BDBC_BACCR | Thiol-disulfide oxidoreductase C | Bacillus cereus group | MGREKKQEYALLTAWGASFIATLGSLYFSEIMKFEPCVLCWYQRIFMYPFVLWLGIAVAKKDYRIASYSLPIASIGACISLYHYAIQKVAAFSAAGAACGRVPCTGEYINWFGFVTIPFLALIGFITIAVCSFIVIKNK | Required for disulfide bond formation in some proteins. | Q81HM5 |
Q7NEG7 | RL6_GLOVI | 50S ribosomal protein L6 | Gloeobacter | MSRIGKLPIAIPPKVEVTLDGRRVVVKGPKGTLDLTLPDSVEVVREDGRLLVTRRGESRRAREQHGLGRTLVANMVTGVTTGFTKPMQIAGVGYRVALTGRKLTINAGFSHPIEIELPAGIDIEVDPKASAIAGTRNQQGFNFVIKGFDKQAVGDLAAKIRDIRPPEPYKGKGIRYTAEKILLKAGKSGKK | This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center. | Q7NEG7 |
P27136 | TFDE1_CUPPJ | Dienelactone hydrolase I | Cupriavidus | MLSDGVEITSRSGGRFGAYLGKPTTDSAPIVVIAQEIFGITPFIRETVEWLVGAGFGCVCPDLYWRQAPNIELDANVPSEREQALALFRDFDMEAGVNDLSCAIEYARALPFSNGRVAVVGYCLGGALAFDVAARSLADCSIGYYGVGLEKKVSLVPAITRPAMFHMGTKDHYVTEEARSILEEHFGRNKNLSLHWYPVGHSFARSSSPNFDQAATTVANARTLELLAMLKDPS | Ring cleavage of cyclic ester dienelactone to produce maleylacetate. | P27136 |
Q73BB8 | NORM_BACC1 | Multidrug-efflux transporter | Bacillus cereus group | MKETSTFSQKLKQFVLLFFPIFITQMSLFAMSFFDTTMSGHASPIDLAGVAIGTSIWIPVSTGLTGILMATTPIVAQLVGSKKKEDVPQVVIQAVYLAICASFVVMLIGFFAVTPILNGMRLEEPVERIAAQFLSIIAIGIIPLFTYTVLRGFIDALGKTRTTMIITLLSLPINVILNYVLIFGHFGFPKLGGVGAAIASTATYWCILIITVMIIRTKEPFASFHIFKQLYRPSLSSWKEFLKLGVPIGFAIFFETSIFAAVTLMMSNFSTTTIAAHQAAMNFASLLYMTPLSLAMAMTIAVGFEVGAKRYNNAKQYGFI... | Multidrug efflux pump. | Q73BB8 |
B0M3D5 | FAR12_MANKU | Extended FMRFamide-12 | Mantophasma | SPGALEDEHNDNFLRF | FMRFamides and FMRFamide-like peptides are neuropeptides. | B0M3D5 |
C0ZW24 | RS10_RHOE4 | 30S ribosomal protein S10 | Rhodococcus erythropolis group | MAGQKIRIRLKAYDHEAIDASARKIVETVTRTGARVVGPVPLPTEKNVYCVIRSPHKYKDSREHFEMRTHKRLIDILDPTPKTVDALMRIDLPASVDVNIQ | Involved in the binding of tRNA to the ribosomes. | C0ZW24 |
Q9MUQ0 | PSBE_MESVI | PSII reaction center subunit V | Mesostigma | MAGSTEERPFSDIITSIRYWVIHSITIPSLFVSGWLFVSTGLAYDVFGTPRPNEYFTEDRQDIPLITDRFNALEQLNQYTK | This b-type cytochrome is tightly associated with the reaction center of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna comp... | Q9MUQ0 |
A7GG06 | IF2_CLOBL | Translation initiation factor IF-2 | Clostridium | MAKIRVYELAKELNISSKELITLLEEEFSVEVKNHMSAIEDEDADLIKELLSGKEKSEKTKEEDDEIETTAKNPIKESINNKKSNKRDDKNEKVNTENAEDMAIITMTSDTITVKEISDKLEKSYAEVIKELMLMGVMASVNQEINFEMAEKLAAKFDTEILKEEQDEEDDLEDILKDSEEEENLQKRSPIITVMGHVDHGKTSLLDAIRKSKVTSTEAGGITQHIGAYTVELNGESITFLDTPGHAAFTAMRARGAQVTDIVILVVAADDGIMPQTKEAISHCKAAEVPLIVAINKIDRPGANIDKVKQELTEYGLVAE... | One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex. | A7GG06 |
Q7YJT0 | NDHI_CALFG | NADH-plastoquinone oxidoreductase subunit I | Calycanthus | MFPMVTGFMNYGQQTVRAARYIGQSFMITLSHANRLPVTIQYPYEKSITSERFRGRIHFEFDKCIACEVCVRVCPIDLPVVHWRLETDIRKKRLLNYSIDFGICIFCGNCVEYCPTNCLSMTEEYELSAYNRHELNYNQIALGRLPMSVIEDYTIRTTRNSTQIKIAMDKPLNARTVTNF | NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translo... | Q7YJT0 |
B1J1U3 | CYAY_PSEPW | Iron-sulfur cluster assembly protein CyaY | Pseudomonas | MSLSEARFHDLVDATQQALEDLFDESGLDLDMENSAGVLTIKFDNGSQLIFSRQEPLRQLWLADRSGGFHFDYDEESGKWVCEKSEELLGEMLERIVWERAGEKLDFDEI | Involved in iron-sulfur (Fe-S) cluster assembly. May act as a regulator of Fe-S biogenesis. | B1J1U3 |
B3LJN0 | GEP3_YEAS1 | Found in mitochondrial proteome protein 38 | Saccharomyces | MLNLCHALRGVRQFSCSVIVKVKCASCSIKLQDQDPSKPGYYTKPKSLPDSKLNPDLQDLKYLLFSQDIQLSKQAIQNDPDLKTKRDLLLRVICKRCSNALHHNNYNPEEFPESTLNDILNYVPRGSNVMHIVPFVEFPLHLDPNVLKRNDLDTTLVLTKSDQVFKDKNAVSKKVPIFMKQFLKNTLRIDSNKTFAISALKNWNISMFYNYFKNYTYLLGNPNVGKSTLINTLLQKYLGYKVKIDSTGKINSPSEEVMQEAFTNPKNFFKIQAAGVSHIPNLTRSVQAYQVGGKILFDLPGYSTSTSRLRLEEPIDERWL... | Interacts genetically with prohibitins and thus may be involved in the mitochondrial lipid metabolism. | B3LJN0 |
B9L6N0 | RL2_NAUPA | 50S ribosomal protein L2 | Nautilia | MAVKSYKPYTPSRRFMTTLDNSDITSKPTVKKLLIKLPQKAGRNNLGRITSRHREAGAKKLYRIIDFKRNKFGVPGKVATVEYDPYRNCRICLISYVDGDKRYIIQPEGLKVGDTVMAAEAGLDIKPGNAMKLKNIPVGTVVHNVEMKPGKGGQIARSAGNSCQIMGREGKYVILRLPSGEMRYILGECMATIGTVGNAEYQNITIGKAGRSRHLGIRPQTRGIAMNPVDHPHGGGEGRSKGNHPVTPWGMPTKGYKTRKKKQSDKYIISRRKK | One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome. | B9L6N0 |
Q87UP6 | PPK1_PSESM | Polyphosphoric acid kinase | Pseudomonas | MNTEALIEAAVEVDVQEAAPVVEPDIEVIPAIEAPAASLPAIVAPNLDDSSLYIHRELSQLQFNIRVLEQALDESYPLLERLKFLLIFSSNLDEFFEIRVAGLKKQITFAREQAGADGLQPHQALARISELVHGHVDRQYAILNDILLPELEKHQVRFIRRRHWTAKLKAWVRRYFRDEIAPIITPIGLDPTHPFPLLVNKSLNFIVELEGIDAFGRDSGLAIIPAPRLLPRVIKVPEEVCGPGDNFVFLSSMIHAHADDLFQGMKVKGCYQFRLTRNADLALDSEDVEDLARALRGELFSRRYGDAVRLEVADTCPKHL... | Catalyzes the reversible transfer of the terminal phosphate of ATP to form a long-chain polyphosphate (polyP). | Q87UP6 |
C4LDG0 | DAPE_TOLAT | N-succinyl-LL-2,6-diaminoheptanedioate amidohydrolase | Tolumonas | MTDSLVLSLAKDLIARPSVTPIDEGCQKMMAEFLAPLGFEIEPMVFHDTTNLWARRGTTGPVFCFAGHTDVVPSGPAEKWHTPPFEPTIIDGMLYGRGAADMKGSIASMMAAVQRFTTDYPAHQGSIAFLITSDEEGPFINGTPKVIETLEARQEKITWCLVGEPSSTNHVGDVVKNGRRGSLTGDLTIYGIQGHVAYPHLAENPVHLAIPALNELASKQWDQGNEFFPATSFQIANINSGTGASNVIPGEMQVQFNFRYSTELTDSQIKQQVAAILDNHGLRYELKWTLSGQPFLTGSGKLVEATQNAIKAITGQETEL... | Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls. | C4LDG0 |
A7FH13 | MTOX_YERP3 | N-methyl-L-tryptophan oxidase | Yersinia | MDYDLIVIGSGSVGSAAGYYASQAGLNVLMIDSAMPPHQAGSHHGETRIMRHAYGEGEKYVPLVLRAQALWDQLAAQTGEKLFQACGVINLGPDNSTFLQNVQRSAQQYDLPVETLNSTQIREKWPVFTVPDNYIAVFEPQSGYLRSELAVKTLIKAVTEAGCGILFNCPVTAIESHQAGVDVVTIDGTYSATKVVVTAGTWVKELLPTLPVTPVRKVFSWHQADGRYSEANHFPAFTVEMPDNILYYGFPAQNDALKLGKHHGGQLIESAAQRKPFGRYAEDGTEVFSFLRHFLPGVGVCLRGEACSYDMSPDEDFIID... | Catalyzes the oxidative demethylation of N-methyl-L-tryptophan. | A7FH13 |
Q3MBE2 | RS6_TRIV2 | 30S ribosomal protein S6 | Trichormus | MSTVYETLYILRPDLTDEQVELAIAKYQNLLQEQGATDIEVQNRGKRRLAYEIKKQRDGFYVQFNYNAPGKAIAILERAMRLSEEVIRYLTVKQEVTKEKEDKVAVTA | Binds together with S18 to 16S ribosomal RNA. | Q3MBE2 |
Q5LXT6 | RS11_STRT1 | 30S ribosomal protein S11 | Streptococcus | MAKPTRKRRVKKNIESGIAHIHATFNNTIVMITDVHGNAVAWSSAGALGFKGSRKSTPFAAQMASEAAAKSAQEHGLKTVEVTVKGPGSGRESAIRALAAAGLEVTAIRDVTPVPHNGARPPKRRRV | Located on the platform of the 30S subunit, it bridges several disparate RNA helices of the 16S rRNA. Forms part of the Shine-Dalgarno cleft in the 70S ribosome. | Q5LXT6 |
Q128R7 | SURE_POLSJ | Nucleoside 5'-monophosphate phosphohydrolase | unclassified Polaromonas | MKILICNDDGYQASGIIALYEALKIVADVEVVAPEQNNSAKSNALTLHSPMYVQTAANGFRYINGTPADCVHIALTGLLGYRPDLVVSGINNGANMGDDTIYSGTVGAAMEGYLFGIPSIAFSQTEKGWAHIDVAARRARELVEQLMPSLEVVAEGAQPALAPWLLNVNIPNLPDDQIQGVKVARLGRRHAAERVITQTSPRGETMYWIGGAGPAKEAGEGTDFYATSQKFVSITPLHVDLTDHERLPYWEQAAARLTQAH | Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates. | Q128R7 |
Q6AG61 | ATPD_LEIXX | F-type ATPase subunit delta | Leifsonia | MGSATREARARSVSALAGLGSKADLATAEDLFAAGRVVADSVQLRAVLSDPAADRSGKDVLVKRVFGALSAPAVELLGVIAGERWSGQDDVLDAIEELGIRSIAASAPRTVDIPAELLAFGGAVTSDAELELALRSKLADPSAKAALVERLLVGKAAGQTVAITRQLVLQPRGRSVRQALREAARIVAAQDGQTIATVVTATPLPAAQAERLRASLAAKYGDLKLNQVVDPSILGGMRVQIGGDVIDGSVSSRLSKLRLQLAG | This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. | Q6AG61 |
A2BY56 | RNZ_PROM5 | tRNase Z | Prochlorococcus | MNVTFLGTSSGVPTLTRNVSSLALKLSQTAEVWLFDCGEGTQHQLMKSNIKSSQIKKIFITHMHGDHIYGLPGLLATLGLSGNSNGIELYGPSELKFFVLSALKSSYCKLSFPLRFKEVEDKASFNKILFENDKLKVHCACLKHRLPAYGYRVSEKDKPGIFDIKKATDLNIPPGPIYSELQAGKTVKLKDGRSFNGQEFCGPPRKGESFVYCTDTVFSESAINLSKNADLLVHESTFSKEDEKMAYEKLHSTTIMAAKTALLANAKKLIITHISPRYTQKSLIKPSTLLLEAQKIFPNTYLAKDFLTAKIK | Zinc phosphodiesterase, which displays some tRNA 3'-processing endonuclease activity. Probably involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA. | A2BY56 |
Q0HPH4 | ADD_SHESR | Adenosine aminohydrolase | Shewanella | MINTSIPLVDLHRHLDGNVRVNTIWELGHQHGIALPADSLETLAPFVQIQGKETSLVAFLKKLDWMVAVLADLDAVKRVAYENVADAALSGLDYAELRFSPYYMAMNHKLPIEGVVEAVIDGVKAGLKDYQVKINLIGIMSRSFGQAACAQELEGLLAHKQHLVAMDLAGDELGFPGELFNEHFKRVRDAGLAITAHAGEAAGSQSMWQAIQELGATRIGHGVNAIHDPKLMDYLAKHRIGIESCPTSNLHTSTVSSYAEHPFRTFMDAGVLISLNTDDPGVSAIDIKHEYRIAKSELGLSYAELAQVQRNGVEMAFLSE... | Catalyzes the hydrolytic deamination of adenosine and 2-deoxyadenosine. | Q0HPH4 |
Q8R967 | ENO_CALS4 | 2-phosphoglycerate dehydratase | Caldanaerobacter | MSSIIDIYAREILDSRGNPTIEVEVELDSGAVGRAAVPSGASTGAFEAIELRDGDKSRYLGKGVLKAVQNVNDIIAPELIGMEAQDQVAIDKAMIELDGTPNKSKLGANAILGVSLAVAKAAAEELGLPLYQYLGGVNAKTLPVPMMNILNGGKHADNNVDIQEFMIMPVGAPNFKEALRMCSEVYHSLKNVLHSKGLSTTVGDEGGFAPNLTSNEEAIKVILEAIEKAGYVPGEDIVLALDPAATEMYKEDGKYHFEGEGIVRTSEEMIEFWEQLVSKYPIVSIEDGLAEEDWNGWKLLTERLGKKVQLVGDDLFVTNT... | Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis. | Q8R967 |
Q7Z2Q7 | LRR70_HUMAN | Synleurin | Homo | MCGLQFSLPCLRLFLVVTCYLLLLLHKEILGCSSVCQLCTGRQINCRNLGLSSIPKNFPESTVFLYLTGNNISYINESELTGLHSLVALYLDNSNILYVYPKAFVQLRHLYFLFLNNNFIKRLDPGIFKGLLNLRNLYLQYNQVSFVPRGVFNDLVSVQYLNLQRNRLTVLGSGTFVGMVALRILDLSNNNILRISESGFQHLENLACLYLGSNNLTKVPSNAFEVLKSLRRLSLSHNPIEAIQPFAFKGLANLEYLLLKNSRIRNVTRDGFSGINNLKHLILSHNDLENLNSDTFSLLKNLIYLKLDRNRIISIDNDTF... | Renders cells highly sensitive to the activation by cytokines and lipopolysaccharide (LPS). | Q7Z2Q7 |
Q0U6G5 | AMPP3_PHANO | Prolidase | Parastagonospora | MAIAENYDEVLKGKYPAKDHARKVAKWIVDKGGDKKGTIYLEAQKQKLNEDNDGEAPFRQRRYFFYLSGCELPDSYLTYDFPSDKLTLFIPPVEPEEVIWSGLPMSPEEAKAKYDIDDCKTTKEVNPHLASSSETAQSTIYAIPGQISDETTFLSYQNKDLEQLKTAIEYCRVTKSDYEIALIRKANVISTNAHINVMKAAAKAQNECELEAVFLKSCVERNAKNQAYHSIVAAGENGATLHYVHNAAPIKSQNLMLLDAGCEVDCYASDITRTFPIKGTFTDESLAIYKIVLDMQKQCINALKAGVLWDSIHELAHKIA... | Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides. | Q0U6G5 |
Q3KJE0 | DTD_PSEPF | Gly-tRNA(Ala) deacylase | Pseudomonas | MKGLLQRVKGARVEVAGEVVGSVDQGLLVLVAVEPDDTPASADKLLHKLLNYRVFSDAEGKMNLSLADVGGGLLLVSQFTLAADTKSGLRPSFSTAAPPALGEKLFDYLLSRAKQMHGTVASGRFGADMQVHLVNDGPVTFLLQT | An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By rec... | Q3KJE0 |
A2RLU3 | EX7S_LACLM | Exodeoxyribonuclease VII small subunit | Lactococcus cremoris subsp. cremoris | MATKKEEVKFEDNLAELENIVRKLESGDVALEDAIAEFQKGMKISETLKKTLNEAEQTLVKIVGKDDNESEFSAEQKEY | Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides. | A2RLU3 |
Q3C167 | ARGR_STRSU | Arginine regulator | Streptococcus | MNKIESRHQLILSLIMEKKIHTQQELQELLEVNGVSVTQSTLSRDIKMLNLVKVNEDDSSHYVINPIAPTRWEKRLRLYMEDALVMLKPIQHQVVLKTLPGLANSFGSILDAMEIPQIVATVCGDDVCLIICEDVEGAQACFEHLKQFTPPFFFSKL | In the presence of arginine, coactivates the transcription of the arcABDC operon, with other regulatory proteins such as ArcR and CcpA. | Q3C167 |
A1K9V0 | KATG_AZOSB | Peroxidase/catalase | Azoarcus | MNNESKCPFAAAHGVRSPATARANRDWWPNQLNLNILHQHAPASNPLGEDFDYAAEFNTLDLAALKQDLYALMTMSQDWWPADWGHYGGLFIRMAWHSAGTYRTADGRGGGGTGNQRFAPLNSWPDNGNLDKARRLLWPIKQKYGNKISWADLMILAGNCALESMGFKTFGFGGGRADIWQPEEDIYWGAEKEWLATSDKPDSRYSGERQLENPLAAVQMGLIYVNPEGPDGNPDPVASGRDVRETFARMAMNDEETVALVAGGHTFGKAHGAGDPKLVGPEPEGAPIEAQGLGWINSFGTGHGVHTTTSGIEGAWKPNP... | Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. | A1K9V0 |
Q15NT8 | DTD_PSEA6 | Gly-tRNA(Ala) deacylase | Pseudoalteromonas | MIGLIQRVSEASVCVGNEVIGEINQGILLLLGVEKNDNEEKAKKLFQRVLNYRIFSDQDSKMNLNLQQVGGGLLVVSQFTLVAQTNKGNRPGFSQGASPELGKTLYNYFVELGRSSEILCESGKFGADMQVRLINDGPVTFSLNV | An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By rec... | Q15NT8 |
Q3V7I4 | THI4_YARLI | Thiazole biosynthetic enzyme | Yarrowia | MAPPPAVVAHPLSSQATGLDMVHEFNQKLTKSDEHTWESFKFAPIRESTVSRAMTRRYFEDLDKYAESDVVIIGAGSCGLSAAYVLAKSRPDLKIAIVEAGVAPGGGAWLGGQLFSAMVMRKPAEQFLEEIGVPYEDEGDYVVVKHAALFTSTLMSQVLKFPNVKLFNATAVEDLITRKDAQGNLRIAGVVTNWTLVSMHHDDQSCMDPNTINAPIIISTTGHDGPFGAFSVKRLVSMNAIEKLGGMRGLDMGLAEDAIVKRTREIVPGLVVGGMELSEVDGANRMGPTFGAMALSGVKAAETVLEVFDTRKKQNQE | Involved in biosynthesis of the thiamine precursor thiazole. Catalyzes the conversion of NAD and glycine to adenosine diphosphate 5-(2-hydroxyethyl)-4-methylthiazole-2-carboxylic acid (ADT), an adenylated thiazole intermediate. The reaction includes an iron-dependent sulfide transfer from a conserved cysteine residue o... | Q3V7I4 |
Q52689 | CCOP_RHOCA | Cytochrome c oxidase subunit III | Rhodobacter | MSKKPTTKKEVQTTGHQWDGIEELNTPLPRWWLWTFYATIIWGVAYSIAMPAWPIFSDKATPGLLGSSTRADVEKDIAKFAEMNKAVEEKLVATDLTAIAADPELVTYTRNAGAAVFRTWCAQCHGAGAGGNTGFPSLLDGDWLHGGAIETIYTNVKHGIRDPLDPDTLLVANMPAHLTDELLEPAQIDEVVQYVLQISGQPADEVKATAGQQIFAENCASCHGEDAKGLVEMGAPNLTDGIWLYGGDVATLTSTIQYGRGGVMPSWSWAADGAKPRLSEAQIRAVASYVHSLGGGQ | C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex. CcoP subunit is required for transferring electrons from donor cytochrome c via its heme groups to CcoO subunit. From there, electrons are shuttled to the catalytic binuclear center of CcoN subunit where oxygen reduction takes place. The complex als... | Q52689 |
A1TDR0 | MSHB_MYCVP | N-acetyl-1-D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside deacetylase | Mycolicibacterium | METARLLFVHAHPDDETLTTGATIAHYVARGAQVHVITCTLGEEGEVIGDEWAQLAVDRADQLGGYRIGELTAALAELGVDRPRFLGGAGRWRDSGMDGTPARQQQRFVDGDFAEQTATLAAAIDELRPHVVVTYDPNGGYGHPDHIHAHRVTTAAVAASTWQVPKLYWTVTSSSALAAALASMGAVPEEWIRVSADDLPLFGYSDEAIDAALDLTAHESARVAALRAHRTQVSVSPDGRSFALSNNVALPVDPTEYYVLAAGSAGARDERGWETDLLSGLSVG | Catalyzes the deacetylation of 1D-myo-inositol 2-acetamido-2-deoxy-alpha-D-glucopyranoside (GlcNAc-Ins) in the mycothiol biosynthesis pathway. | A1TDR0 |
Q4KLL4 | TM9S4_RAT | Transmembrane 9 superfamily member 4 | Rattus | MAAAMIWWPRFLLLLCLTCKGSTFYVPGVAPINFHQNDPVEIKAVKLTSSRTQLPYEYYSLPFCQPNKITYKAENLGEVLRGDRIVNTPFQVLMNSEKKCEVLCGQSNKPVILTVEQSRLVAERITEEYYVHLIADNLPVATRLELYSSNRDSDDKKKEKDVQFEHGYRLGFTDVNKIYLHNHLSFILYYHREDTEEDQEHTYRVVRFEVIPQSIRLEDLKIDEKSSCTLPEGANSLPQEIDPTKENQLYFTYSVHWEESDIKWASRWDTYLTMSDVQIHWFSIINSVVVVFFLSGILSMIIIRTLRKDIANYNKEDDIE... | Associates with proteins harboring glycine-rich transmembrane domains and ensures their efficient localization to the cell surface. | Q4KLL4 |
P48675 | DESM_RAT | Desmin | Rattus | MSQAYSSSQRVSSYRRTFGGAPGFSLGSPLSSPVFPRAGFGTKGSSSSVTSRVYQVSRTSGGAGGLGSLRASRLGTTRAPSYGAGELLDFSLADAVNQEFLATRTNEKVELQELNDRFANYFEKVRFLEQQNAALAAEVNRLKGREPTRVAELYEEEMRELRRQVEVLTNQRARVDVERDNLIDDLQRLKAKLQEEIQLREEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKKVHEEEIRELQAQLQEQQVQVEMDMSKPDLTAALRDIRAQYETIAAKNISEAEEWYKSKVSDLTQAANKNNDALRQAKQEM... | Muscle-specific type III intermediate filament essential for proper muscular structure and function. Plays a crucial role in maintaining the structure of sarcomeres, inter-connecting the Z-disks and forming the myofibrils, linking them not only to the sarcolemmal cytoskeleton, but also to the nucleus and mitochondria, ... | P48675 |
Q5ZK13 | KIZ_CHICK | Polo-like kinase 1 substrate 1 | Gallus | MSEAGRAAAGPCPEVSPSRSQQLGGLLRCLRDSETRRLELERKLMEYKSSDAYLMKLKYVKLKKYLEEVNERQKRALLRNQTFLNEFNEFEAHVKASSSELIEKMVRYGREIKSGLSFQEGDLARGDKEEGCNEQMPQAARQAGIHAKTALSRSLHHPVPFFMGHCMSACSVQQETPQPAACPNSLTALQGDETDGHPTQADDDMQHANKLDEQGGKSYVPMGEKMSIRDSSLHSSLLNFTERKNSTELCSALPDGGSLQSRTADLASDTSVEEVVTREHLVASAKEVCEQPVLLASAPEPSITGPQCNLNTQQAASQDS... | Centrosomal protein required for establishing a robust mitotic centrosome architecture that can endure the forces that converge on the centrosomes during spindle formation. Required for stabilizing the expanded pericentriolar material around the centriole. | Q5ZK13 |
P61631 | LYSC_COLAN | 1,4-beta-N-acetylmuramidase C | Colobus | MKALIILGLVLLSVTVQGKIFERCELARTLKKLGLDGYKGVSLANWVCLAKWESGYNTDATNYNPGDESTDYGIFQINSRYWCNNGKTPGAVNACHISCNALLQNNIADAVACAKRVVSDPQGIRAWVAWKKHCQNRDVSQYVEGCGV | Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. | P61631 |
Q9LDU5 | TI11A_ARATH | Jasmonate ZIM domain-containing protein 5 | Arabidopsis | MSSSNENAKAQAPEKSDFTRRCSLLSRYLKEKGSFGNIDLGLYRKPDSSLALPGKFDPPGKQNAMHKAGHSKGEPSTSSGGKVKDVADLSESQPGSSQLTIFFGGKVLVYNEFPVDKAKEIMEVAKQAKPVTEINIQTPINDENNNNKSSMVLPDLNEPTDNNHLTKEQQQQQEQNQIVERIARRASLHRFFAKRKDRAVARAPYQVNQNAGHHRYPPKPEIVTGQPLEAGQSSQRPPDNAIGQTMAHIKSDGDKDDIMKIEEGQSSKDLDLRL | Repressor of jasmonate responses. | Q9LDU5 |
A4WCV0 | ACCD_ENT38 | Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta | Enterobacter | MSWIERIKSNIAPTRKASIPEGVWTKCDSCGQVLYRAELERNLEVCPKCDHHMRMSARNRLHSLLDEGTMVELGSELEPKDLLKFRDSKKYKDRIASAQKETGEKDALVVMKGTLHEMPVVAAAFEFSFMGGSMGSVVGARFIRAVEQALEDNCPLICFSASGGARMQEALMSLMQMAKTSAALGKMQERGLPYISVLTDPTMGGVSASFAMLGDLNIAEPKALIGFAGPRVIEQTVREKLPPGFQRSEFLIQKGAIDMIVRRPEMRLKLASVLAKLMNLPAPSPDEPRESVVVPDQEPEA | Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA. | A4WCV0 |
Q3J8L6 | FLGH_NITOC | Basal body L-ring protein | Nitrosococcus | MNIKKIVLGIAGFFITGCAAQLPPPDPSFAATRPVATPPPQPNNGAIYHAGYEISLFTDYRARQIGDVITVVLEERTDAEKGSDTAIDRDTSYSLTNPTLLGSGVQFNTPNWLPLASNQDNSLEMAVKAKGAFSGGGDSSQNNRLNGHITVTVAEVLPNGNLVIRGEKVVTINHGNEYIKISGIVNRRDIKPDNTVSSLKLADARLAYVGDGATHEANRMGWLSRFFFSRFMPF | Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. | Q3J8L6 |
O28059 | SYV_ARCFU | Valyl-tRNA synthetase | Archaeoglobus | MEIRKDYDAHEVEEKWLKLWKDEMYYFDWNSEKPHYIIDTPPPYPTGSFHIGHALNWCIIDFIARYKRMNGYEVMFPQGWDCHGLPTEVKVEEKYGIKKGDIPRDEFRRLCVEFTEENIAKMRETARRMGYSIDWSKEYITMYPEYYSKTQLSFVRMYNKGLIYRDYHPVVFCPRCETTIALAEIEYRQGKTKLNYIKFDDDVIIATTRPELIPACVAIAVHPDDERNKHLIGKKVRVPTTPYEVEVIADEEVDPEFGTGVVMICTFGDRQDVKWWKKHKLELRNIVGRDGRLNEKAGRYAGMTIPEAREAILEDLKKEG... | Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-dependent manner. | O28059 |
P59786 | ALGL_PSEFL | Poly(beta-D-mannuronate) lyase | Pseudomonas | MRLPMQKLLIPTLLGLAMFAGSVNAAAPLRPPQGYFAPVEAFKTGDFKNDCDAMPPPYTGSLQFRSKYEGSDKARSTLNVQSEKAFRDSTADITKLEKDTSKRVMQFMRDGRPEQLECTLNWLTSWAKADALMSKDFNHTGKSMRKWALGSMASAYVRLKFSDSHPLANHQQESQLIEAWFNKLADQVVSDWDNLPLEKTNNHSYWAAWSVMATSVATNRRDLFDWAVKEYKVGVNQVDDQGFLPNELKRQQRALSYHNYALPPLSMIASFALVNGVDLRQENNSALKRLGDKVLAGVKDPEIFEKKNGKEQDMKDLKED... | Catalyzes the depolymerization of alginate by cleaving the beta-1,4 glycosidic bond between two adjacent sugar residues via a beta-elimination mechanism. May serve to degrade mislocalized alginate that is trapped in the periplasmic space. | P59786 |
Q8WJR3 | MATK_CERBE | Intron maturase | Cercocarpus | MEEFQGYLELDRSQQHDFLYPLIFREYIYALAHDHGLNRSILLDNVGYDNKSSFLIIKRLISRMYQQNHLIISPNDSNQKKIGGYNKNLYCQMISEGFAVIVEIPFSLRLVSSLEGTEIVKSYNLRSIHSIFPFLEDKFSHLNYVSDVLIPYPIHLEILVQTLRYWAKDPSYLHLLRLFLHDYYNLNSLITKNKSIFSKSNPRLFLLLYNSYVCEYESILLFLRNQSSHLQFTSSWIFFERIHFYEKIKYPVEEVFANDFPAILWFFKDPFMHYVRYQGKSILASKDTPLLMNKWKYYLVNLWQCHFYVWSQPGRIYINQ... | Usually encoded in the trnK tRNA gene intron. Probably assists in splicing its own and other chloroplast group II introns. | Q8WJR3 |
P60746 | RL24_THEAC | 50S ribosomal protein L24 | Thermoplasma | MYRKMEVSLSKDLRKKYGIRSFPVIMGDVVKVISGSRKGEGGKVAEVDHASGLVVVEGITIARADGKQKGFGIQPEKLQITHLDLSRGDRFDKIKSLAARKNIVVEKPEPEPEPRKEETAEAQEAKEEAVAEEKTEVDDNDKQN | Located at the polypeptide exit tunnel on the outside of the subunit. | P60746 |
P72242 | PLY_PSEAV | Pectate lyase | Pseudomonas amygdali | MLKPHGLTPLALTGGILVSLLSVSLSAHAEIATDVATTGWATQNGGTKGGSRAAANNIYTVKNAAELKAALAASGGSNGRIIKERGVIDVSDGKPYTKTSDMKQRARLDIPGKTTIVGTSSSAEIREGFFYAKENDVIIRNLTIENPWDPEPVWDPEDGSAGNWNSEYDGLTVEGASNVWIDHVTFTDGRRTDDQNGTANGRPKQHHDGALDVKNGANYVTISYSVFRNHEKNNLIGSSDSKTPDDGKLKVTNHNSLFENISSRGPRVRVGQVHLYNNHHIGSTTHKVYPCVYAQGVGKGSKIFSERNVLDISGISGCSK... | Plays a role in bacterial invasion of plants. | P72242 |
Q0K5M3 | ATPF_CUPNH | F-type ATPase subunit b | Cupriavidus | MNLNATFFAQMVVFFILWWVVAKFIWPPLVKALDERAKKIADGLAAAEKGKAELELANKRVDQAMAEARTEGAQRVADAEKRAQLTADEIKQNAQAEAARIIAQAKAEAEQQVTRAREALRDQVAVLAVKGAEQILKREVNAQVHTDLLNQLKAEL | Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0). | Q0K5M3 |
Q9RVM9 | APBC_DEIRA | Iron-sulfur cluster carrier protein | Deinococcus | MNDALLRALSTVNDPELHRDLVSLGMIERAELSGDVAQVKVNLTTPACPLKGQIELDVRSALLQVPGVRDVQIEFGAMVRAATQPALPGVKHVVLVGSGKGGVGKSSVAVNLAASLARDGARVGLLDADVYGPSVAHMLGQGQARVTANEDRKMRPIEAHGVRFISMANLSPAGQALVWRGPMLHSAIQQFLKDSAWGELDYLIVDLPPGTGDVQLSLTQTVQVTGAVIVTTPQDVALIDAARAIDMFRKASVPVLGVVENMSYFVAPDTGLTYDIFGRGGSRKLGEQYPLLGEIPLDVEVRKDADAGAPAILAHPESVA... | Binds and transfers iron-sulfur (Fe-S) clusters to target apoproteins. Can hydrolyze ATP. | Q9RVM9 |
P65263 | LSPA_MYCBO | Signal peptidase II | Mycobacterium tuberculosis complex | MPDEPTGSADPLTSTEEAGGAGEPNAPAPPRRLRMLLSVAVVVLTLDIVTKVVAVQLLPPGQPVSIIGDTVTWTLVRNSGAAFSMATGYTWVLTLIATGVVVGIFWMGRRLVSPWWALGLGMILGGAMGNLVDRFFRAPGPLRGHVVDFLSVGWWPVFNVADPSVVGGAILLVILSIFGFDFDTVGRRHADGDTVGRRKADG | This protein specifically catalyzes the removal of signal peptides from prolipoproteins. | P65263 |
Q9UHE8 | STEA1_HUMAN | Six-transmembrane epithelial antigen of prostate 1 | Homo | MESRKDITNQEELWKMKPRRNLEEDDYLHKDTGETSMLKRPVLLHLHQTAHADEFDCPSELQHTQELFPQWHLPIKIAAIIASLTFLYTLLREVIHPLATSHQQYFYKIPILVINKVLPMVSITLLALVYLPGVIAAIVQLHNGTKYKKFPHWLDKWMLTRKQFGLLSFFFAVLHAIYSLSYPMRRSYRYKLLNWAYQQVQQNKEDAWIEHDVWRMEIYVSLGIVGLAILALLAVTSIPSVSDSLTWREFHYIQSKLGIVSLLLGTIHALIFAWNKWIDIKQFVWYTPPTFMIAVFLPIVVLIFKSILFLPCLRKKILKI... | Metalloreductase that has the ability to reduce both Fe(3+) to Fe(2+) and Cu(2+) to Cu(1+). Uses NAD(+) as acceptor. | Q9UHE8 |
Q88X60 | CYSC_LACPL | Adenosine-5'-phosphosulfate kinase | Lactiplantibacillus | MVKSDNITWHQSQVSKAERQALNHHKSVVLWFTGLSGSGKSTIANAVEKALFDQQVGSYVLDGDNMRFGLNKNLGFSAEDREENIRRIGEVAKLFVDAGVITLTAFISPYRADRDKVRANLEVDEFIEVFVDTPLEVCEQRDVKQLYAKARRGEITGFTGIDAPYEAPIDPEITIDTSKQPLTASVQQVLNYLAEHHYVSLVTANEN | Catalyzes the synthesis of activated sulfate. | Q88X60 |
P34939 | CH60_RHILV | Chaperonin-60 | Rhizobium | MASKEIKFGRTGREKMLRGVDILADAVKVTLGPKGRNVIIDKSFGAPRITKDGVSVAKEIELEDKFENMGAQMVREVASKTNDIAGDGTTTATVLAQAIVREGNKAVAAGMNPMDLKRGIDLAVADVVKDLQAKAKKISTSEEVAQVGTISANGDKQVGLDIAEAMQKVGNEGVITVEEAKTAETELEVVEGMQFDRGYLSPYFVTNPEKMIADLEDVFILLHEKKLSNLQSMLPVLEAVVQTGKPLLIVAEDVEGEALATLVVNKLRGGLKIAAVKAPGFGDRRKRMLEDIAILTGGTVISEDLGIKLESVTLDMLGRA... | Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. | P34939 |
B8NJG7 | LEPC_ASPFN | Leporins biosynthesis protein C | Aspergillus subgen. Circumdati | MSATVDNTEANASPPKEFTLRSTIALIGAFMALFCTLGFQNAFGVFQAFYHATILRDHSEFDIAWIGSLLTFMIFFFAAPAGVLVDRVGPTHSLTRHLQPLLTFGAIATILATFMISLCKELYQFLLAQGILLGIGNAFLLCPAMATVTRLFDHHRGAANGIMIAGSSIGGIIWPIMLDQLLNKDGVSFGWTFRIVGFVVLPLCLFMVATIRPAPKTPHDSDREGIELSHGESESDHKAQGAEGPAAIIKNPTFLILCAGLSVATFGLFSPLFFISTYATDQGLSVSLAFYLVSMLNGASMVGRVSTGFLADRYGNFNLC... | Efflux pump that may be involved in the secretion of leporins . | B8NJG7 |
Q9QZQ4 | UTS2_RAT | Urotensin II | Rattus | MDRVPFCCLLFVGLLNPLLSFPVTDTGEMSLQLPVLEENALRALEELERTALLQTLRQTVGTEAEGSLGQADPSAETPTPRGSLRKALTGQDSNTVLSRLLARTRKQRKQHGTAPECFWKYCI | Highly potent vasoconstrictor. | Q9QZQ4 |
Q33DV3 | 4CGT_ANTMA | Chalcone 4'-O-glucosyltransferase | Antirrhinum | MGEEYKKTHTIVFHTSEEHLNSSIALAKFITKHHSSISITIISTAPAESSEVAKIINNPSITYRGLTAVALPENLTSNINKNPVELFFEIPRLQNANLREALLDISRKSDIKALIIDFFCNAAFEVSTSMNIPTYFDVSGGAFLLCTFLHHPTLHQTVRGDIADLNDSVEMPGFPLIHSSDLPMSLFYRKTNVYKHFLDTSLNMRKSSGILVNTFVALEFRAKEALSNGLYGPTPPLYLLSHTIAEPHDTKVLVNQHECLSWLDLQPSKSVIFLCFGRRGAFSAQQLKEIAIGLEKSGCRFLWLARISPEMDLNALLPEG... | Glycosyltransferase involved in the biosynthesis of aurones, plant flavonoids that provide yellow coloration to flowers. | Q33DV3 |
P49590 | SYHM_HUMAN | Histidyl-tRNA synthetase | Homo | MPLLGLLPRRAWASLLSQLLRPPCASCTGAVRCQSQVAEAVLTSQLKAHQEKPNFIIKTPKGTRDLSPQHMVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSGLMYDLKDQGGELLSLRYDLTVPFARYLAMNKVKKMKRYHVGKVWRRESPTIVQGRYREFCQCDFDIAGQFDPMIPDAECLKIMCEILSGLQLGDFLIKVNDRRIVDGMFAVCGVPESKFRAICSSIDKLDKMAWKDVRHEMVVKKGLAPEVADRIGDYVQCHGGVSLVEQMFQDPRLSQNKQALEGLGDLKLLFEYLTLFGIADKIS... | Mitochondrial aminoacyl-tRNA synthetase that catalyzes the ATP-dependent ligation of histidine to the 3'-end of its cognate tRNA, via the formation of an aminoacyl-adenylate intermediate (His-AMP). | P49590 |
Q74EM9 | UPP_GEOSL | UPRTase | Geobacter | MGVHELTHPLVRHKIGLMREADISTKKFRELAAELARLLAYEACGDFPLEVRTITGWDGNPVEIEQIKGKKVTVVPILRAGIGMLDGVLDMIPNAKVSVVGLARNEETLEAHTYLEKFVDKLDERLAVILDPMLATGGSMEATISMLKRNGCRQIRVLALVAAPEGLARVTAAHPDVDIYVAAIDRCLNEHGYILPGLGDAGDKIFGTK | Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate. | Q74EM9 |
Q62267 | SPR1B_MOUSE | Small proline-rich protein 1B | Mus | MSSHQQKQPCTAPPQLHEQQVKQPCQPPPPEPCVSQVKTPCDTKVPEPCHPKAPEPCHPKAPEPCHPKAPEPCHPKAPEPCHPKAPEPCHPKAPEPCHPKAPEPCHPKAPEPCHPKVPEPCLPKAPEPCQPIVPEPCPSTVTPILAQQKTKQK | Cross-linked envelope protein of keratinocytes. It is a keratinocyte protein that first appears in the cell cytosol, but ultimately becomes cross-linked to membrane proteins by transglutaminase. All that results in the formation of an insoluble envelope beneath the plasma membrane. | Q62267 |
Q8LM92 | C75B4_ORYSJ | Flavonoid 3'-hydroxylase CYP75B4 | Oryza sativa | MEVAAMEISTSLLLTTVALSVIVCYALVFSRAGKARAPLPLPPGPRGWPVLGNLPQLGGKTHQTLHEMTKVYGPLIRLRFGSSDVVVAGSAPVAAQFLRTHDANFSSRPRNSGGEHMAYNGRDVVFGPYGPRWRAMRKICAVNLFSARALDDLRAFREREAVLMVRSLAEASAAPGSSSPAAVVLGKEVNVCTTNALSRAAVGRRVFAAGAGEGAREFKEIVLEVMEVGGVLNVGDFVPALRWLDPQGVVARMKKLHRRFDDMMNAIIAERRAGSLLKPTDSREEGKDLLGLLLAMVQEQEWLAAGEDDRITDTEIKALI... | Catalyzes the 3'-hydroxylation of the flavonoid B-ring to the 3',4'-hydroxylated state. Catalyzes in vitro 3'-hydroxylation of different flavonoids. Catalyzes the conversion of apigenin to luteolin, naringenin to eriodictyol, and kaempferol to quercetin. Possesses specific 5'-hydroxylase activity toward chrysoeriol (a ... | Q8LM92 |
Q3AZK3 | CH601_SYNS9 | Chaperonin-60 1 | unclassified Synechococcus | MAKRIIYNENARRALEKGIDILAESVAVTLGPKGRNVVLEKKFGSPQIINDGVTIAKEIELEDHIENTGVALIRQAASKTNDAAGDGTTTATVLAHAMVKAGLRNVAAGANAITLKKGIDKASDFLVGKIKDMAKPIADSNAIAQVGTISAGNDEEVGKMIADAMDKVGKEGVISLEEGKSMETELEVTEGMRFDKGYISPYFATDTERMEAVLDEPYILLTDKKIGLVQDLVPVLEQIARTGKPLLIIAEDIEKEALATLVVNRLRGVLNVAAVKAPGFGDRRKAMLEDMAVLTNGQLITEDAGLKLENAKLEMLGTAR... | Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. | Q3AZK3 |
Q1QA16 | DXR_PSYCK | 2-C-methyl-D-erythritol 4-phosphate synthase | Psychrobacter | MVMTQRIAVLGATGSIGDSTLAILAAQPQHYDVYALSGYHRLDKLLALCQQFAPKRVGVPTAAVDEFAKRLSEAGLDIEVVGGETGLVDIATDSQTDTVVAAIVGAAGLPSTLAAARAGKRILLANKEALVMAGQVMINAVKTHHATLLPLDSEHNAIFQCLPFAIQQDNTQIHRLNHGVRKLWLTASGGPFLQQSFTQMQQASVAEAVKHPNWSMGQKISVDSATMMNKGLELIEACHLFDLPENKINVVIHPQSIIHSMVEYSDGSFLAQLGSPDMKTPIAHALSYPDRIDSGSQPLDLFALSGLEFIEPDLQKFACL... | Catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP). | Q1QA16 |
Q2KTI6 | YIDD_BORA1 | Putative membrane protein insertion efficiency factor | Bordetella | MIKTLLIAPIRFYRFFLSPWIGRQCRFTPSCSAYAIEAIERHGALRGLWLASRRIGRCHPWSPGGLDPVPDPARPQQKNQGSGCCGNHSRTGLD | Could be involved in insertion of integral membrane proteins into the membrane. | Q2KTI6 |
Q03ZQ0 | POTA_LEUMM | Spermidine/putrescine import ATP-binding protein PotA | Leuconostoc | MSEKQVPIIAFNQVDLSFGDTHVLNNVDLEIEAGKFYTLLGPSGSGKSTILKLISGQLTADSGDISFEGQRVNDVPAEKRKVNTVFQNYALFPNMNVFDNVAFGPTLKGMNKTEIKNKVKEMLNLVKLSDFVDREIDELSGGQQQRVAIARALANDPEVLLLDEPLSALDYKLRKSMQYELREIQQRLGITFVFVTHDQEEALAMSDWIFVMNDGVIQQNGSPEDIYDEPINHFVADFIGESNIVDGIMKEDYVVHFVGKDFENVDAGMRPNERVEVVLRPEDLDLTSIENGKLVVTIEDQSFRGDYYEITARDDDGNEW... | Part of the ABC transporter complex PotABCD involved in spermidine/putrescine import. Responsible for energy coupling to the transport system. | Q03ZQ0 |
Q6GJI1 | SYM_STAAR | Methionyl-tRNA synthetase | Staphylococcus | MAKETFYITTPIYYPSGNLHIGHAYSTVAGDVIARYKRMQGYDVRYLTGTDEHGQKIQEKAQKAGKTEIEYLDEMIAGIKQLWAKLEISNDDFIRTTEERHKHVVEQVFERLLKQGDIYLGEYEGWYSVPDETYYTESQLVDPQYENGKIIGGKSPDSGHEVELVKEESYFFNISKYTDRLLEFYDQNPDFIQPPSRKNEMINNFIKPGLADLAVSRTSFNWGVHVPSNPKHVVYVWIDALVNYISALGYLSDDESLFNKYWPADIHLMAKEIVRFHSIIWPILLMALDLPLPKKVFAHGWILMKDGKMSKSKGNVVDPN... | Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. | Q6GJI1 |
A7A1T1 | BL1S1_YEAS7 | BLOS1-homolog | Saccharomyces | MFLTFSMCVNWIIVKMPNRSEELDRLLDKIINSPHRTEASKTLQEIENNQSYILNVQLKKLLRLHDDSFKNKCVSPINYMLEKYTPYMGHTEALQKEAELVDRDLRIIEMTYQLIKKNRNSK | Component of the biogenesis of lysosome-related organelles complex-1 (BLOC-1), a complex involved in endosomal cargo sorting. | A7A1T1 |
O27657 | THI4_METTH | Thiamine thiazole synthase | Methanothermobacter | MKLDDIKISRAIVEGYMEDLLDYMEMDVAIGGGGPSGLTAGYYLARAGLKVALFERKLSIGGGMWGGGMMFNKIVVQDEGREILDEFGIRSEPYDEGYHVADSVEATSTLCSRACQAGLKIFNLMSIEDVMIRDEGITGLVLNWSSVEMAGLHVDPLTVRARAVIDATGHDCEIVKVVERKIGPELNTPDGRIQGERSMWADVGEAALIENTREVYPNLYVAGMASNAVYGAPRMGPIFGGMLVSGRRVAEMIIEKLK | Involved in the biosynthesis of the thiazole moiety of thiamine. Catalyzes the conversion of NAD and glycine to adenosine diphosphate 5-(2-hydroxyethyl)-4-methylthiazole-2-carboxylate (ADT), an adenylated thiazole intermediate, using free sulfide as a source of sulfur. | O27657 |
P0DPQ5 | SRTA_BACAN | Sortase A | Bacillus cereus group | MNKQRIYSIVAILLFVVGGVLIGKPFYDGYQAEKKQTENVQAVQKMDYEKHETEFVDASKIDQPDLAEVANASLDKKQVIGRISIPSVSLELPVLKSSTEKNLLSGAATVKENQVMGKGNYALAGHNMSKKGVLFSDIASLKKGDKIYLYDNENEYEYAVTGVSEVTPDKWEVVEDHGKDEITLITCVSVKDNSKRYVVAGDLVGTKAKK | Transpeptidase that anchors surface proteins to the cell wall . Recognizes and modifies its substrate by proteolytic cleavage of a C-terminal sorting signal. Following cleavage, a covalent intermediate is formed via a thioester bond between the sortase and its substrate, which is then transferred and covalently attache... | P0DPQ5 |
P0CAX2 | MNME_CAUVC | tRNA modification GTPase MnmE | Caulobacter | MTDTIFALATAAGRSAVAVVRVSGPRSSEIAAALCGRLPSPRLASVRTLKHNGVALDAALVLRFEKPASYTGEDSVEFHVHGGRAVVEALLAALSELGARLAEAGEFTRRAFENGKLDLAQAEGVADLIDAETEAQRRQALGQVGGALSQRYDRWRDLLVQALAMLEAAVDFPDEDLPEEVAERARPGLRQLSAELNAALADVSRGRRVRDGFRIALIGAPNAGKSTLLNGLAERDAAIVTDVAGTTRDVIEVPLVLGGYKVLVADTAGIRETADVIEAEGVRRAKAWAEAADLRLWVVDGFHVKQADARPEAIRVGDWL... | Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34. | P0CAX2 |
Q05080 | CYK2_YEAST | Homolog of CDC15 protein 1 | Saccharomyces | MSYSYEACFWDPNDNGVNILLGHISQGIRSCDSMILFFKQRSELEKDYARRLGAITGKLDKDIGTNMDYGKLNETFNVVLSVEKARAQSHSKQSEILFRQIYTDTKAFAANLQARYTTLSGKIERLRMDKFNKKKGCEVLQKKLQDAQIRFRDLQLNENNMIGAKRVEHNKRELLKWESNSQEYKVQLDVLKQEYKASQKFWIHEWAQLSCELQEMENARISFLQSKLQQFATSSMETYILEQTKMDMLTNHLNSFTAADEISTFSKENGTGRLKHKTSKGDMNSSANWAQMSSISTTSKKTESYMDNIRKLSSQLKETE... | Throughout most of the cell cycle it forms a double ring that coincides with the septins. After the onset of mitosis, forms a ring-like structure which colocalizes with the medial actin ring. Mediates cytoskeletal rearrangements required for cytokinesis. In conjunction with the medial actin ring exhibits contraction-li... | Q05080 |
B6EPT8 | RS14_ALISL | 30S ribosomal protein S14 | Aliivibrio | MAKQSMKAREAKRAKLVTKFAEKRAALKVLISDVNASEEDRWNAVLKLQSLPRDSSASRQRNRCNQTGRPHGYLRKFGLSRIKVREACMKGEIPGLRKASW | Binds 16S rRNA, required for the assembly of 30S particles and may also be responsible for determining the conformation of the 16S rRNA at the A site. | B6EPT8 |
B6JM90 | GREA_HELP2 | Transcript cleavage factor GreA | Helicobacter | MNKEPMSMHGYNKICAELKQLKEVERPNIVKEIDIARGHGDLKENAEYHAAKEKQRFIEARIVDLSEIVANAQVIDPSVLAHNKVSFGSTIKILNLDNDKEFSYTIVGSVESDPAKGLISFGSPIAKSLIGKSKGDAVSIQLPNGESDFEILDIYYKEICFDEN | Necessary for efficient RNA polymerase transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by cleavage factor... | B6JM90 |
A1K9L0 | RIMM_AZOSB | Ribosome maturation factor RimM | Azoarcus | MMVLGRIVAPFGVQGWLKIHPFGDDPAAWRKMTHWWLAEDPDGPESAWVQYKLASCRPHGKGLVALLEGVPDRNAAEAIEGRYVGAPRDAMPAPEKDEYYWGDLVGLDVVNETDETLGRVSGLISTGAHDVLQVEDGETERLIPFVAAYVLDVDLAARRIRVAWQKDW | An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Probably interacts with S19. 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 ribosoma... | A1K9L0 |
A4QLH6 | MATK_LOBMA | Intron maturase | Lobularia | MAKFQGYLEFDGARQQSFLYPLFFREYIYVLAYDHGLNRLNRNRSIFLENSDYGKKYSSLIVKRLILRMYEQNRLIIPTKDLNQNPFLGHTNLVDYQMISILFAVIVEIPFSLRLGSSFEGKQLKKSYNLQSIHSIFPFLEDKLSHFNYVVDVLIPYPIHLEILVQTLRYRVKDPSSLHFFRFCLYEYCNWKNFDIKKKSILNPRFFLFLYNSHVCEYESIFFFLRKRSSHLRSTSYEVLFERILFYGKIQHFLKVFVNTFPAILGLLKDPFIHYVRYHGKCILATKDTPLLMNKWKYFFVNLWQCYFSVWFQSQKVNIK... | Usually encoded in the trnK tRNA gene intron. Probably assists in splicing its own and other chloroplast group II introns. | A4QLH6 |
Q8TKQ5 | NADK_METAC | ATP-dependent NAD kinase | Methanosarcina | MAIRKIGIASRCDRPEVLQMVRDIIAHFYSKVQIYVSTATADVLDIEGTPVERMRDKGVELIISVGGDGTVLRNIAKMKDPLPVLGINMGTLGFLVDVEPEDAIETIEEVLYGFSYLERMRVDVFLNGEMLETATNEVAVMSAKPAKIIQFEVYVNDCLLDEMRADGVVFATPTGSTAYAMSAGGPIINPRVNAIVVVPVAPFKLSARPWVIPSDSEITVKLSDHKKEAVIAIDGQKSYRIRPDDVVKLKKSKYPARFVRISDTCFYERVQRKLS | Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP. | Q8TKQ5 |
Q1R627 | RS5_ECOUT | 30S ribosomal protein S5 | Escherichia | MAHIEKQAGELQEKLIAVNRVSKTVKGGRIFSFTALTVVGDGNGRVGFGYGKAREVPAAIQKAMEKARRNMINVALNNGTLQHPVKGVHTGSRVFMQPASEGTGIIAGGAMRAVLEVAGVHNVLAKAYGSTNPINVVRATIDGLENMNSPEMVAAKRGKSVEEILGK | Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body. | Q1R627 |
Q6G983 | EBPS_STAAS | Elastin-binding protein EbpS | Staphylococcus | MSNNFKDDFEKNRQSIDTNSHQDHTEDVEKDQSELEHQDTIENTEQQFPPRNAQRRKRRRDLATNHNKQVHNESQTSEDNVQNEAGTIDDRQVESSHSTESQEPSHQDSTPQHEEEYYNKNAFAMDKSHPEPIEDNDKHETIKEAENNTEHSTVSDKSEAEQSQQPKPYFATGANQANTSKDKHDDVTVKQDKDESKDHHSGKKGAAIGAGTAGVAGAAGAMGVSKAKKHSNDAQNKSNSDKSNNSTEDKVSQDKSKDHHNGKKGAAIGAGTAGLAGGAASKSASAASKPHASNNASQNHDEHDNHDRDKERKKGGMAKV... | Promotes binding of soluble elastin peptides and tropoelastin to S.aureus cells although it is not able to promote bacterial adherence to immobilized elastin and, therefore, is not a microbial surface component recognizing adhesive matrix molecule (MSCRAMM). | Q6G983 |
Q9DG83 | VSP6_PROMU | Snake venom serine protease serpentokallikrein-1 | Protobothrops | MVLIRVLANLLILQLSYAQRTSELVIGGDECNINEHRFLVALHDALSGRFLCGGTLIHPEWVLTAAHCNTHFIIIYLGAHNQSVEFDYEETRYPEKKYFFPCSKNYTKWDKDIMLIRLYSPVRNSKHIAPISLPSSPPSVGSVCRIMGWGAITSPNETFPDVPHCANINLFNYTVCRAAYPELPATSRTLCAGILEGGIDTCHGDSGGPLICNGQFQGIVQAGGKTCARPRKPAVYTNVFDHLDWIKSIIAGNTAVTCPP | Snake venom serine protease that may act in the hemostasis system of the prey. | Q9DG83 |
D2Y226 | H2O01_CYRHA | Hainantoxin-II-15 | Haplopelma | MKVTLIAILTCAAVLVLHTTAAEELEAESQLMEVGMPDTELAAVDEERLFECSVSCEIEKEDNKDCKKKKCKGGWKCKFNMCVKV | Postsynaptic neurotoxin. | D2Y226 |
P26212 | SACT_BACSU | SacPA operon antiterminator | Bacillus | MKIYKVLNNNAALIKEDDQEKIVMGPGIAFQKKKNDLIPMNKVEKIFVVRDENEKFKQILQTLPEEHIEIAEDIISYAEGELAAPLSDHIHIALSDHLSFAIERIQNGLLVQNKLLHEIKALYKKEYEIGLWAIGHVKETLGVSLPEDEAGYIALHIHTAKMDAESMYSALKHTTMIKEMIEKIKQYFNRKVDENSISYQRLVTHLRYAVSRLESNEALHRMDEEMLYFIQKKYSFAYQCALELAEFLKNEYQLHLPESEAGYITLHVQRLQDLSE | Mediates positive regulation of the sacPA operon by functioning as an antiterminator factor of transcription. | P26212 |
A6VQW4 | DEOC_ACTSZ | Phosphodeoxyriboaldolase | Actinobacillus | MQPREIAKFIDHTALTTEKTEQDILKLCDEAVAHHFRSVCINSGYIPLAKQKLTGTGVKICTVVGFPLGANLSSVKAFEAQEAIKAGAQEVDMVINVGLIKSGKWDEVRSDIEQVLHACRGTLLKVILETCLLTKAEIVHACEICRDLNVGFVKTSTGFNKSGATVADVALMRQTVGENIGVKASGGIRDTQTTLAMINAGATRIGASAGIAIIQGLQDNNGGY | Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate. | A6VQW4 |
A7X1P6 | RIMP_STAA1 | Ribosome maturation factor RimP | Staphylococcus | MSKITEQVEVIVQPIMEDLNFELVDVEYVKEGRDHFLRISIDKEGGVDLNDCTLASEKISEAMDANDPIPEMYYLDVASPGAERPIKKEQDFQNAITKPVFVSLYVPIEGEKEWLGILQEVNNETIVVQVKIKARTKDIEIPRDKIAKARHAVMI | Required for maturation of 30S ribosomal subunits. | A7X1P6 |
P30882 | CCL5_MOUSE | T-cell-specific protein RANTES | Mus | MKISAAALTIILTAAALCTPAPASPYGSDTTPCCFAYLSLALPRAHVKEYFYTSSKCSNLAVVFVTRRNRQVCANPEKKWVQEYINYLEMS | Chemoattractant for blood monocytes, memory T-helper cells and eosinophils. Causes the release of histamine from basophils and activates eosinophils. May activate several chemokine receptors including CCR1, CCR3, CCR4 and CCR5. May also be an agonist of the G protein-coupled receptor GPR75. Together with GPR75, may pla... | P30882 |
A0PQW5 | PYRD_MYCUA | Dihydroorotate oxidase | Mycobacterium | MYCLLRRLLFLLPPEWVHKLVFAVLRGATAATPVRRMLTRWLGPTDPVLASTVFGVRFPGPLGLAAGFDKDGTGLDTWAAMGFGYAEVGTVTAHPQPGNPAPRLFRLPEDRALLNRMGFNNHGAGALAIRLACHHPEVPVGVNIGKTKTTPADQAVDDYRASARLVGPLASYLVVNVSSPNTPGLRDLQAVESLRPILAAVLAETSTPVLVKIAPDLSDSDVDEVADLAVELGLAGIVATNTTVSRDGLLTPGVGQLGAGGISGPPVAERSLEVLRRLYQRVGDRLTLISVGGIETAEDAWDRITAGASLLQGYTGFIYG... | Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor. | A0PQW5 |
A4YCH6 | GLMU_SHEPC | Glucosamine-1-phosphate N-acetyltransferase | Shewanella | MALNVVILAAGKGTRMRSDLPKVLHPIAHKSMVQHVIDTAHSIGSDAIQLVYGYGADKLQASLGEQQLNWVLQAEQLGTGHAVAQASPYIADNDTVLILYGDVPLIQASTLEALLAARPENGVAILTVNLANPTGYGRIVREQGKVVGIIEQKDANPEQLLINEINTGIMAVPGKQLKTWLSRLSNNNAQGEYYLTDIIAMAHADGVAIDTAQPQSAIEVEGANNRVQLAQLERAYQAREAEKLMLAGANLRDPHRIDIRGEVTVGMDVMIDINVIFEGKVILGNNVTIGAGAILIDCEIADGAEIKPYSIIEGAKLGVA... | Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted ... | A4YCH6 |
Q8UE18 | RL3_AGRFC | 50S ribosomal protein L3 | Agrobacterium tumefaciens complex | MRSGVIAQKVGMTRVYNDAGEHIPVTVLRLDNVQVVAQRTEDKNGYTAVQLGAGQSKVKNTTKALRGHFAAANVEPKAKLVEFRVSPENLIDIGATLTANHFQSGQLVDVTGTTIGKGFAGAMKRHNFGGGRASHGNSVSHRAHGSTGNNQDPGRVWKGKRMAGHMGQTRVTTQNLEVVSTDEDRGLILVKGAVPGSKGSWIIVRDAVKSAAK | One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit. | Q8UE18 |
A1UTC8 | MRAY_BARBK | UDP-MurNAc-pentapeptide phosphotransferase | Bartonella | MMLFFSSLYDWLPGVNVFRYITFRTVAAMLTSGLIVFLFGPSIISSLKVRQGKGQPIRADGPQTHFKKAGTPTMGGLMILSGVVISALLWGNLFNIYLWVSLFVMLFFGAIGFYDDYLKVTKQTDKGFSGKARLSLEFLVASIASFIILQVGSPGLALPFVKEYFINLGWFFIPFSACVVVGLGNAVNLTDGLDGLAIVPVMVASLSFALIAYLSGNINFADYLQIHYVSGVGELAVLLGAVFGAGLGFLWFNAPPAAIFMGDTGSLALGGLLGIVSVATKHEIVLIFIGGLFVLETLSVIIQVGWFKLTKKRVFLMAPI... | 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, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I... | A1UTC8 |
Q6NDN4 | ACCD_RHOPA | Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta | Rhodopseudomonas | MNWLTNVVRPKIRNILRRETPENLWIKCPDTGQLVFYKDVEQNQFVIPGSNYHMRMGAVARLRAIFDNETWYDVALPEVVADPLKFRDERKYADRIKDARTKTGAHDAVRVGFGKLETSPVVVAVQDFDFMGGSLGMAAGEAIIRGMELAVEKHAPFIMFAASGGARMQEGILSLMQMPRTTVAVQMLREAKLPYIVVLTNPTTGGVTASYAMLGDIHIAEPGALIGFAGARVIEQTIREKLPDGFQRAEYLKEHGMVDMVVHRHDLRPTLARLCRLLTKSPALTVTTAVEAPAEAAAKAEPEATTTEQPGAPAPTEPPA... | Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA. | Q6NDN4 |
A8G3R0 | CHLN_PROM2 | Light-independent protochlorophyllide reductase subunit N | Prochlorococcus | MSKVEFNKETGPREVFCGLTSIVWLHRRMPDAFFLVVGSRTCAHLIQSAAGVMIFAEPRFGTAILEEKDLAGLADAHEELDRVVNDLISRRPEIKTLFLVGSCPSEVIKLDLATVAEKLNKRFLGKIKFVNYSGSGIETTFTQGEDGALKALIPLMEDSNEEKLLLVGTLANNVEDRFKKIFRNLGISNVESFPPRQSTELPKIGKNTKVLLTQPYLSDTVRDLKHRGCEIISAPFPLGIEGSTKWFLAAAKAFKISALKVHEIISPLISRAKLALESHKDILKGKRLFLLPESQLEISLARFLHNECEMDLIEIGTPYL... | Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (ChlN-ChlB) is the catalytic component of the complex. | A8G3R0 |
B0B836 | TRUA_CHLT2 | tRNA-uridine isomerase I | Chlamydia | MTKKIVLQIAYQGTSYSGWQYQPNALSIQEVLKTILKKIAGFRISVISSGRTDAGVHAQGQIAHFHCPDHPHFTDPRQIQKMLNALLPHDIVIRDAVMTDGDFHSRFSAIAKEYRYTLSLLPKPLPHHRLFCFSPRYKLNIARMQEAAQYLVGTHDFASFANLGREYSSTIRTLYTLDLSEQEHLVTVICRGNGFLYKMVRNIVGALLDIGKGKYPPEHLLDMLATKDRRKGPPSAPPYGLSLHHVCYPPPYQWFCKHEHNNSSEGK | Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs. | B0B836 |
Q1MFL8 | SSUB1_RHIL3 | Aliphatic sulfonates import ATP-binding protein SsuB 1 | Rhizobium | MTSIAHERFHAVAEEPAYARENAPAVSRSAPAAISLTGLEKSFGGNRVLRGINLHIPAGQFVAVIGKSGCGKSTLLRILMGLDEPSAGELHFEDADGAQASPNARIVFQEPRLLPWLSVADNVVVGLGDGVDSRAAAKAAEAVLAEVQLGEKTEEWPARLSGGQRQRVALARALISRPGVLALDEPLGALDALTRISMQELINRVWRELGFTAVLVTHDVSEAVHLADRVIVLDEGRIALDLPIPHPRPRRHGHPGLCELEGRLLAAILGTDGGH | Part of the ABC transporter complex SsuABC involved in aliphatic sulfonates import. Responsible for energy coupling to the transport system. | Q1MFL8 |
P45758 | GSPD_ECOLI | Putative type II secretion system protein D | Escherichia | MKGLNKITCCLLAALLMPCAGHAENEQYGANFNNADIRQFVEIVGQHLGKTILIDPSVQGTISVRSNDTFSQQEYYQFFLSILDLYGYSVITLDNGFLKVVRSANVKTSPGMIADSSRPGVGDELVTRIVPLENVPARDLAPLLRQMMDAGSVGNVVHYEPSNVLILTGRASTINKLIEVIKRVDVIGTEKQQIIHLEYASAEDLAEILNQLISESHGKSQMPALLSAKIVADKRTNSLIISGPEKARQRITSLLKSLDVEESEEGNTRVYYLKYAKATNLVEVLTGVSEKLKDEKGNARKPSSSGAMDNVAITADEQTN... | Involved in a type II secretion system (T2SS, formerly general secretion pathway, GSP) for the export of folded proteins across the outer membrane. This subunit would form the outer membrane channel. | P45758 |
Q7VJ85 | EFG_HELHP | Elongation factor G | Helicobacter | MARKTPLVRIRNIGIAAHIDAGKTTTSERILFYTGVSHKIGEVHDGAATMDWMEQEKERGITITSATTTCFWRDYQINLIDTPGHVDFTIEVERSMRVLDGAIAVFCSVGGVQPQSETVWRQANKYGVPRMVFVNKMDRIGANFYSVESQIKQRLKANPVPINIPIGAEENFKGVIDLVQMKAIVWNDESMGAKYDVEEIPSELVEKANEYREKLLEAAAEQDEALMEKYLGGEELSIEDIKKGIKIGCLNMSLIPMLCGSSFKNKGVQTLLDAVVDYLPAPTEVAEIKGIDPKNESELSVESSDDGAFAGLAFKIMTDP... | Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respective... | Q7VJ85 |
Q5JIT0 | IF2B_THEKO | eIF-2-beta | Thermococcus | MSEKVDFYDFEKLLDKAYEELPENVKHHHSRFEVPPAQVTIAGNRTIIENFVDIAEAMNRDPNHLLKFILREVATAGTLEGRRAILQGRFTPYLIANKMKKYLKEFVICPVCGSPDTKIIKKGRFHFLKCEACGAETPIQHL | eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. | Q5JIT0 |
C5A075 | RHAT_ECOBW | L-rhamnose-H(+) transport protein | Escherichia | MSNAITMGIFWHLIGAASAACFYAPFKKVKKWSWETMWSVGGIVSWIILPWAISALLLPNFWAYYSSFSLSTRLPVFLFGAMWGIGNINYGLTMRYLGMSMGIGIAIGITLIVGTLMTPIINGNFDVLISTEGGRMTLLGVLVALIGVGIVTRAGQLKERKMGIKAEEFNLKKGLVLAVMCGIFSAGMSFAMNAAKPMHEAAAALGVDPLYVALPSYVVIMGGGAIINLGFCFIRLAKVKDLSLKADFSLAKSLIIHNVLLSTLGGLMWYLQFFFYAWGHARIPAQYDYISWMLHMSFYVLCGGIVGLVLKEWNNAGRRP... | Uptake of L-rhamnose across the cytoplasmic membrane with the concomitant transport of protons into the cell (symport system). | C5A075 |
B8CTL3 | AROQ_SHEPW | Type II DHQase | Shewanella | MSSQAKVLLVNGPNLNLLGRREPGHYGHHTLEQIVSDLQQQAADANLQLEHIQSNAEHLLIEAIHNTDADFVIINPAAFTHTSVALRDALLGVAIPFIEVHLSNVHSREPFRHHSYFSDKAVGIICGLGAQGYQFALQSVIAQLKASQQK | Catalyzes a trans-dehydration via an enolate intermediate. | B8CTL3 |
Q149F1 | RUSD2_MOUSE | RNA pseudouridylate synthase domain-containing protein 2 | Mus | MWRGVPGCLRDIVQWQVALWSHSFVRTWGSCGKAMTEALSAQAEAAGGLKALVQPNGDAGSNTSGEPLLERLEPAAVGKQVPESGDQAQGGEGQLPSNGEQTPAPVADSGKRKKRRGATGERVVPPPKKRRTGVSFSDEHFAETTYYFEGGLRKVRPYYFDFQTYCKGRWVGRSLLHVFSTEFRSQPLSYYEAAVRAGRLHLNEEPVQDLSIVLKDNDFLRNTVHRHEPPVTAEPIHLLAENNDVVVIDKPSSIPVHPCGRFRHNTVIFILGKEHQLKELHPLHRLDRLTSGVLMFAKTAAVSEKIHEQVRDRQLEKEYV... | Pseudouridine synthase that catalyzes pseudouridylation of mRNAs. | Q149F1 |
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