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 |
|---|---|---|---|---|---|---|
Q74P25 | TUBR_BACC1 | TubR-Bc | Bacillus cereus group | MKLLSNISMSSSEIIDVLCENLNDGIWALRVLYAEGAMNKEKLWDYINQYHKDYQIENEKDYEGKKILPSRYALDIMTARLEGAGLISFKAIGRVRIYDVTDLGNVLIKELEKRVEKNN | A DNA-binding protein that is part of the type III plasmid partition system used to ensure correct segregation of the pBc10987 plasmid (Probable). Binds TubZ filaments but does not influence the GTPase activity of TubZ with or without DNA . Cooperatively binds to multiple regions in tubC (centromere-like site) upstream... | Q74P25 |
A1WY83 | QUEF_HALHL | PreQ(0) reductase | Halorhodospira | MSTEPSKTLETFENPNPERDYTIRMEIPEFTCLCPKTGQPDFATLNLEYIPERHCVELKSLKLYIWSYRDVGGFHEALTNQILGDLVAATQPRYMKLTAHFNVRGGIWTTVEAEHHGR | Catalyzes the NADPH-dependent reduction of 7-cyano-7-deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1). | A1WY83 |
A5FNH2 | MUTL_FLAJ1 | DNA mismatch repair protein MutL | Flavobacterium | MSSIIQLLPDHVANQIAAGEVVQRPASVVKELLENAVDAKATDIKLIIKDAGKSLVQVIDNGVGMTVTDARLCFARHATSKIRQAEDLFSLGTKGFRGEALASIAAIAHMEMKTKQEQDELGTHIVIEGSKFVSQEVAVLPKGTSFAVKNLFFNIPARRNFLKSDTVEFRHVMDEFQRVALAHPNIHFSFYHNGSELYNLPAAGYRQRIVGIMSGKTNEKLVPVNEDTEIISIQGFVCKPEFAKKNRGEQFFFVNDRFIKSGYLHHAVMAAYDGLLKDGSQPSYFLYLQVPPNTIDINIHPTKTEIKFDDEQALYAILRA... | This protein is involved in the repair of mismatches in DNA. It is required for dam-dependent methyl-directed DNA mismatch repair. May act as a 'molecular matchmaker', a protein that promotes the formation of a stable complex between two or more DNA-binding proteins in an ATP-dependent manner without itself being part ... | A5FNH2 |
Q8TRA5 | SIHH_METAC | S-inosyl-L-homocysteine hydrolase | Methanosarcina | MTEQELVESGNMKMEWARNHMPVIAIIREKFEKEKPLKGLKVGMALHVEAKTAVLVETLAAGGAQVAISGCNPLSTQDDVARALDTRKNISCFARYGCCTSEYYEAIDKVLDIEPDITIDDGADLIFKLHKERTDLLPKILGGCEETTTGVHRLHAMEKEGALKMPVIAVNDAMTKYLFDNRYGTGQSAWDGINRTTNLLVAGKNVVVGGYGWCGRGVAMRAAGLGANVIVTEVDPIRALEARMDGYRVMRMADAARLGEIFVTTTGNRDILTAEHFKVMPDGAVLANSGHFNVEIDMEALTSLAKSVKTVRHNIKEYDI... | Catalyzes the hydrolysis of S-inosyl-L-homocysteine (SIH) to L-homocysteine (Hcy) and inosine. Likely functions in a S-adenosyl-L-methionine (SAM) recycling pathway from S-adenosyl-L-homocysteine (SAH) produced from SAM-dependent methylation reactions. Can also catalyze the reverse reaction in vitro, i.e. the synthesis... | Q8TRA5 |
C3P9E0 | NTPPA_BACAA | Nucleotide pyrophosphatase | Bacillus cereus group | MRKIILASGSPRRKELLELAGVPFEIIVSEVEETIGAYSSPSDIVMSLALQKASAVAENNSDHIVLGADTIVTYESRILGKPSNKAEAKEMLQLLSGKTHEVYTGVAIIAKDKTVTFYERTEVTFWELTEEEIDAYVASKEPLDKAGSYGIQGKGSIFVQHIQGDYYSVVGLPISRLVRELKQFNIDVTHA | Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids. | C3P9E0 |
Q72X51 | UNG_BACC1 | Uracil-DNA glycosylase | Bacillus cereus group | MENVLKNDWGPLLAPEFEKEYYRKLAGFLKEEYSTHVVYPKKEDIFNALEYTSYENTKVVILGQDPYHGPNQAHGLSFSVQPGIKTPPSLLNMYKELRDEYGYDIPNNGYLVKWAEQGVLLLNTVLTVRQGEANSHKGKGWEHFTDRVIELLNEREKPVIFILWGRHAQAKKKLITNTKHHIIESVHPSPLSARRGFFGSKPYSKVNTILANMGEREIDWEIPNL | 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. | Q72X51 |
A1TUZ2 | RUVA_ACIAC | null | Acidovorax | MIGKLTGTLLEKNPPEVLVDCHGVGYEVQVPMSTFYNLPAVGERVQLLTQFIVREDAQLLYGFGSAPERQAFRELIKISGVGPRTALSILSGMGVDDLAQAVSLQEAGRLVKVPGIGKKTAERLLLELKGKLGVDIGARPEAANDAQADILQALLALGYNDKEGTAALKALPKDVGVSEGIKLALKALAK | The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. RuvA... | A1TUZ2 |
Q0C454 | DNAJ_HYPNA | Chaperone protein DnaJ | Hyphomonas | MSKRDYYEVLGVERGVDEKALKSAYRKLAMKYHPDQNAGDTAAEDKFKEVGEAYAILSDPQKRAAYDRYGHGAFENGGMGGGSPFGGQGGNPEDIFQDLFSQVFGAGGFAGGRRRSGPQRGADLRYDLEITLEEAFYGKDETIHVPQAVACRPCEGTGAAPGTKPETCETCGGHGRVRAQQGFFTMERTCHICQGRGQIIRKPCKTCGGHGQVKEERKLQVKIPAGVESGMRIRLSGEGEPGTSGGPKGDLYIFVEVVEHDIFERDGPNLYCRAPVPMTTAALGGEIDIPTIDGGRARVAIPEGAQTGRKLRLRSKGMPS... | Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bou... | Q0C454 |
A2BPU5 | UCRI_PROMS | Rieske iron-sulfur protein | Prochlorococcus | MTQLSSNDVPSMGRRQFMNLLTFGTATGVALGALYPVANYFMPLRAGGGGGGTSAKDELGNPITKTGWLATHQAGDRSLVQGLKGDPTYLIVNEGGEIGEFGLNAICTHLGCVVPWDSGANKFICPCHGSQYDTNGKVVRGPAPLSLALAHVDIEDDAVLVKQWSETDFRTNENPWWA | Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. | A2BPU5 |
B8HCX5 | RS11_PSECP | 30S ribosomal protein S11 | Pseudarthrobacter | MPPKTRGAVRKPRKKDKKNIALGQAHIKSTFNNTIVSITDPTGAVISWASSGEVGFKGSRKSTPFAAQMAAEAAAKRAQEHGMRKVDVFVKGPGSGRETAIRSLQAAGLEVGSIQDVTPAAHNGCRPPKRRRV | 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. | B8HCX5 |
Q810S1 | MCUB_MOUSE | Coiled-coil domain-containing protein 109B | Mus | MPGALSGRRMLPSGLCLGRWQLLRTIRARGRGDPRELPSTPQVLCMKLYGNPKYHQALHYGTVEPQDEITVTYKHGLPLVTLTLPSRKERCQFVVKPMLSTVGSFLQDLQNEDKGIKTAAIITADGSEIPASTLMDTLLMTDFKLIINKLRYDIRCHKKEEPSGEHMTELENTKSLVHRLFTILHLEEIQKRRERHLMAKIDHLQEQLRPLEQVKAAIEARSEANTSGLLWAGLALLSVQGGALAWLTWWVYSWDIMEPVTFFLSFANSIVFFAYFIITRQNYTYSSLRSRQFLQFFHKKSQRRCFDVEQYNKLKEDLAE... | Negatively regulates the activity of MCU, the mitochondrial inner membrane calcium uniporter, and thereby modulates calcium uptake into the mitochondrion. Does not form functional calcium channels by itself. Mitochondrial calcium homeostasis plays key roles in cellular physiology and regulates cell bioenergetics, cytop... | Q810S1 |
B1KQ33 | ATPE_SHEWM | F-ATPase epsilon subunit | Shewanella | MAAMTVQLDIVSAENSIFSGLVAHLQVTGSEGDLGVMPGHAPLLTNIKPGMARIVKQDGKEEVFYLSGGILEVQPSSVSVLADVVKRADEIDEKAAEEAKRRAESAMADAGADFNYAAAANELAQAVAQLRVVDTIKKNIAR | Produces ATP from ADP in the presence of a proton gradient across the membrane. | B1KQ33 |
Q56NH2 | BPTA_BORGR | Borrelial persistence in ticks protein A | Borreliella | MRKILFFGLLSICIFLVFFFYKQKENNIIYNKIVEEFEDNIFIDETYTHLFKDSNLKELVFIKSQLIIPELEHKEMMKSTGYYADTYRALSTVYKFDFKVHENKILGFKSVIFEGFEDAKVSKHENNLPSEKWQQLKDFNIGDPNINEKFFHLEFPFVVKNTLRVTISKGFFKKIKKLKRLKIMLISNEDREYKIDIENFLPKYNL | Virulence-associated protein essential for survival of the bacterium within the tick host and therefore within the natural life cycle of the Lyme disease spirochete. | Q56NH2 |
Q4FUE2 | RS8_PSYA2 | 30S ribosomal protein S8 | Psychrobacter | MSMQDTVGDMLTRIRNAQMANKVSVAMPSSKLRKSIADLLVNEGYVASAVVTEENNNKATLTIVLKYFEGKAVIETIQRFSRPGLRQHRGKDAIPTVKQGMGVAIVSTSQGIMSDRAARAAGIGGEIVAFVA | One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit. | Q4FUE2 |
B0YPQ1 | RK20_ANEMR | 50S ribosomal protein L20, plastid | Aneura | MTRVKRGYVARRRRKNLFTLTSGFRGTHSKLFRTANQQGMRALVASYRGRVGRKKTLRRLWIVRINAAVRSDGISYNKLIQYLYKNQILLNRKILAQIAILDRFAFFLIIRSIQREEG | Binds directly to 23S ribosomal RNA and is necessary for the in vitro assembly process of the 50S ribosomal subunit. It is not involved in the protein synthesizing functions of that subunit. | B0YPQ1 |
Q9R0P6 | SC11A_MOUSE | Sid 2895 | Mus | MLSLDFLDDVRRMNKRQLYYQVLNFGMIVSSALMIWKGLMVITGSESPIVVVLSGSMEPAFHRGDLLFLTNRVEDPIRVGEIVVFRIEGREIPIVHRVLKIHEKQDGHIKFLTKGDNNAVDDRGLYKQGQHWLEKKDVVGRARGFVPYIGIVTILMNDYPKFKYAVLFLLGLFVLVHRE | Catalytic component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum. Specifically cleaves N-terminal signal peptides that contain a hydrophobic alpha-helix (h-region) shorter than... | Q9R0P6 |
Q6ID18 | LAC10_ARATH | Urishiol oxidase 10 | Arabidopsis | MVFPIRILVLFALLAFPACVHGAIRKYTFNVVTKQVTRICSTKQIVTVNGKFPGPTIYANEDDTILVNVVNNVKYNVSIHWHGIRQLRTGWADGPAYITQCPIKPGHSYVYNFTVTGQRGTLWWHAHVLWLRATVHGAIVILPKLGLPYPFPKPHREEVIILGEWWKSDTETVVNEALKSGLAPNVSDAHVINGHPGFVPNCPSQGNFKLAVESGKTYMLRLINAALNEELFFKIAGHRFTVVEVDAVYVKPFNTDTILIAPGQTTTALVSAARPSGQYLIAAAPFQDSAVVAVDNRTATATVHYSGTLSATPTKTTSPP... | Lignin degradation and detoxification of lignin-derived products. | Q6ID18 |
Q4UWI8 | EX7S_XANC8 | Exodeoxyribonuclease VII small subunit | Xanthomonas | MAKKSLNESSPVARFEQSLEELEQLVQKMEVGEMSLEQSLTAYERGIGLYRDCQQALEQAELRVRLVTDPARPEQAEAFEPPSLDGG | Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides. | Q4UWI8 |
Q9HJV9 | GMHA_THEAC | Sedoheptulose 7-phosphate isomerase | Thermoplasma | MDAKKYLEEGARARLNLNIEKIIGIADKISSAISSGNKLIVFGNGGSAADAQHFVAELTGHFMKERKPLAAIALTTNTSSITAIANDYSYDVVFSRQVEALAKPGDVVVGISTSGNSKNVIEGIKSAKRIGCHTIAFTGRSGGQLKGVADETLNVDSDLTSIIQEMHITVIHMICAMIDEKF | Catalyzes the isomerization of sedoheptulose 7-phosphate in D-glycero-D-manno-heptose 7-phosphate. | Q9HJV9 |
P12122 | CYB6_DESSP | Cytochrome b6 | Desmonostoc | MANVYDWFEERLEIQAIAEDVTSKYVPPHVNIFYCLGGITLTCFLIQFATGFAMTFYYKPTVAEAFSSVEYIMNEVNFGWLIRSIHRWSASMMVLMMILHVFRVYLTGGFKKPRELTWVSGVILAVITVSFGVTGYSLPWDQVGYWAVKIVSGVPEAIPVVGVLISDLLRGGSSVGQATLTRYYSAHTFVLPWLIAVFMLFHFLMIRKQGISGPL | Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. | P12122 |
Q2SS69 | NANE_MYCCT | ManNAc-6-P epimerase | Mycoplasma | MDLINQIKNTLIVSCQAIGDEPLNDSYVLSKMAYALVLGGSKVLRLSQVEHIKAVKQVVDVPIIGLIKKHYDNSEVFITPTIKEVDQLVDLKVDIIALDATLRTRPDQDLTNLVKTIKTKYPNQLLLADCSSVEDAINAQNLGFDLIASTLRGSTKQTKGHNNLENNYQFLRDLKKVITKPIIAEGGIWTPQQAKEILNLGIHSVVVGTAITRLHSIVKYWNDILK | Converts N-acetylmannosamine-6-phosphate (ManNAc-6-P) to N-acetylglucosamine-6-phosphate (GlcNAc-6-P). | Q2SS69 |
P05351 | VIRB2_AGRT9 | null | Agrobacterium tumefaciens complex | MRCFERYRLHLNRLSLSNAMMRVISSCAPSLGGAMAWSISSCGPAAAQSAGGGTDPATMVNNICTFILGPFGQSLAVLGIVAIGISWMFGRASLGLVAGVVGGIVIMFGASFLGQTLTGGS | VirB proteins are suggested to act at the bacterial surface and there play an important role in directing T-DNA transfer to plant cells. | P05351 |
Q18C67 | HIS1_CLOD6 | ATP phosphoribosyltransferase | Clostridioides | MDYLTIALAKGRIEGESFKKFKKMGLGDSIDTDTRKLIFKDEENKIIYIHVKPSDVVTYVEKGVADLGIAGKDTILENETDVYEIYDLGFGKCKFAVAGLKGDSIYREDEYLKVATKYPNIAKKYFKEKGQKIEIIKLNGSVELAPIVGLSDVIVDIVETGNTLKANGLEILEDICNISARIISNRASYRFKYEQIQNIIRLFEELDN | Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity. | Q18C67 |
A6L683 | MIAA2_PHOV8 | Isopentenyl-diphosphate:tRNA isopentenyltransferase 2 | Phocaeicola | MEKYDLITILGPTASGKTPLAAALAYKLDTEIISGDSRQVYRRMDLGTGKDLEDYVVNGQQIPYHLIDIVDPGYKYNVFEFQRDFLNAYDQVRWKDKLPILCGGTGMYLESVLKGYRLLPVPENPKLRDSLADKSLAELTRLLSTYRKLHNSTDVDTVKRAIRAIEIEEYYKHQSAEYREFPQIHSLIIGVDIARELRREKISHRLKQRLDEGMVNEVKALLDSGISSEDLIYYGLEYKYLTLYVLGKLSFNEMFHQLEIAIHQFAKRQMTWFRGMERRGFTIHWLDACLPMEDKVEKIINLLHTKN | 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). | A6L683 |
Q9K6H0 | ATPL_HALH5 | Lipid-binding protein | Halalkalibacterium (ex Joshi et al. 2022) | MNLLAAGIAAGLAAVGGAIAVAIIVKATLEGVTRQPELRGSLQTLMFIGVPLAEAVPIIAIVVSFILLFT | Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of between 10-14 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits. | Q9K6H0 |
A4XLS4 | RS3_CALS8 | 30S ribosomal protein S3 | Caldicellulosiruptor | MGQKVHPKGFRLGIIKDWDSRWFANDKDFEKYLLEDYKIRRHIKEKLYNAGISRIEIERAAKRIKVIIHTAKPGIVIGRAGSGVEALRKELEKITGGKTISLDIKEIKVPELDAQLVAENIAAQLEKRVSFRKAMKQAMARALRSGAKGIKTMVSGRLGGADIARTEWYKEGRIPLQTLRADIDYGFAEAHTTYGRIGVKTWIYKGDVLPQKGAAAEKGGDK | Binds the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation. | A4XLS4 |
Q67ET1 | TR106_RAT | Taste receptor type 2 member 19 | Rattus | MLTIPEGILLCFITSGSVLGVLGNGFILHVNCTDCVRQKFSTTGFIFTGLAISRICVICIIISDGYLKLFSPHMVASDAHIIGISYLWIITNHTSTCFATILNLFYFLKIANFSHYIFFCLKRKLNTIFIFLLGCLFISWSVAFPQTVKIFNDKMKHRNTSWKFHLHKSKFIINHILLNLGVIFFCMVAIITSFLLIISLWKHNRKMQLYVSRFKSLNTEVHLKVMKVLISFIILLILHVIGILIETLSFLRYENKLLLILGLNFSSMYPCCHSFILILANNQLKQASLKALKQFKCHKKDKDVRET | Putative taste receptor which may play a role in the perception of bitterness. | Q67ET1 |
B9K857 | APGM_THENN | Probable 2,3-bisphosphoglycerate-independent phosphoglycerate mutase | Thermotoga | MLDKQKFVSKLVTTNDTKIVLLVMDGLGDIPVNGKTPLQAASTPNLDSLAKESDLGQTVPVLPGITPGSGPGHLSLFGYDPIKYQIGRGILEALGIGVEVGEKDVVARANFATWDGNVVLDRRAGRPATEESAKVVQLLSEKIKKIEDVEITFYPGKEHRFVVKFTGEGLGDRVTDADPQKEGHPMVWAEGLDEPSKKTARIANELIRKIAEVLKDNPKINFALIRGFSKYPDLPKFPEIYKLRAGAIATYPMYRGLAKLVGMEIIETGQTVEDEINTLKEKWNDFDFFYVHVKKTDSYGEDGKFDEKVKVIEEVDRVIP... | Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate. | B9K857 |
Q96GW7 | PGCB_HUMAN | Chondroitin sulfate proteoglycan 7 | Homo | MAQLFLPLLAALVLAQAPAALADVLEGDSSEDRAFRVRIAGDAPLQGVLGGALTIPCHVHYLRPPPSRRAVLGSPRVKWTFLSRGREAEVLVARGVRVKVNEAYRFRVALPAYPASLTDVSLALSELRPNDSGIYRCEVQHGIDDSSDAVEVKVKGVVFLYREGSARYAFSFSGAQEACARIGAHIATPEQLYAAYLGGYEQCDAGWLSDQTVRYPIQTPREACYGDMDGFPGVRNYGVVDPDDLYDVYCYAEDLNGELFLGDPPEKLTLEEARAYCQERGAEIATTGQLYAAWDGGLDHCSPGWLADGSVRYPIVTPSQ... | May play a role in the terminally differentiating and the adult nervous system during postnatal development. Could stabilize interactions between hyaluronan (HA) and brain proteoglycans. | Q96GW7 |
A6QCQ5 | RL16_SULNB | 50S ribosomal protein L16 | unclassified Sulfurovum | MLMPKRTKWRKQQKGRNRGKSFRGNKIEFGDIAIKAVEAGRIDSRQIEAARITMTRKINRTGKTWIRVFPDKPLTAKPLETRMGKGKGAVDRWVMNIKPGRIIFEMAGVEEELARAALTLAIHKMPFKCKIITAKDSHELY | Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs. | A6QCQ5 |
Q9EP52 | TWSG1_MOUSE | Twisted gastrulation protein homolog 1 | Mus | MKSHYIVLALASLTFLLCLPVSQSCNKALCASDVSKCLIQELCQCRPGEGNCPCCKECMLCLGALWDECCDCVGMCNPRNYSDTPPTSKSTVEELHEPIPSLFRALTEGDTQLNWNIVSFPVAEELSHHENLVSFLETVNQLHHQNVSVPSNNVHAPFPSDKERMCTVVYFDDCMSIHQCKISCESMGASKYRWFHNACCECIGPECIDYGSKTVKCMNCMF | May be involved in dorsoventral axis formation. Seems to antagonize BMP signaling by forming ternary complexes with CHRD and BMPs, thereby preventing BMPs from binding to their receptors. In addition to the anti-BMP function, also has pro-BMP activity, partly mediated by cleavage and degradation of CHRD, which releases... | Q9EP52 |
B8EJI6 | TSAD_METSB | tRNA threonylcarbamoyladenosine biosynthesis protein TsaD | Methylocella | MRVLGIETTCDETAAAVVQLNPGGAGEILSNEVMSQIAEHAAYGGVVPEIAARAHIEVLDRLVARALEDAKIKLAELDGIAAAAGPGLVGGVIVGLTTAKALALASHKPFIAVNHLEAHALTARLTDGVDFPYLLLLVSGGHTQLVAVKGVGDYLRLGSTVDDAVGEAFDKVAKMLGLAYPGGPEVERMAAKGDPTRFDFPRPMQGRAKPDFSLSGLKTAVRVAAQRIHSPSQTDVADLCASFQAAIVDTMIDRSRAGLRLFRERVGDCNAMVVAGGVGANGAIRRALSRFCAESGLRLILPPPQLCTDNGAMIAWAGIE... | Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct ca... | B8EJI6 |
C6A117 | IF5A_THESM | eIF-5A | Thermococcus | MGDKTRVQVSKLKPGRYILIDDEPCRIANITVSSPGKHGSAKARIEAVGIFDGKVRSIVKPTSAEVDVPIIDKKTGQIIAITPDTVQLMDMETYDLFDVPIATGVNEEIKDKLKEGINVEYWETLGRIKIMKLKGESS | Functions by promoting the formation of the first peptide bond. | C6A117 |
P04681 | NODD_RHILV | Nodulation protein D | Rhizobium | MRFKGLDLNLLVALDALMTERKLTAAARSINLSQPAMSAAISRLRDYFRDDLFIMQRRELVPTPRAEALAPAVREALLHIQLSVIAWDPINPAESDRRFRIILSDFMALVFFDKIILRLAREAPGVSFELLPLDDDPEELLRRGDVDFLILPDLFMSGAHPKARLFEERLVCVGCPTNEQLQGQLSLEQYMSMGHVAAKFGRGLKPSVEQWLLMQHGLKRRIELVVPGFNLIPPLLSGTNRIATIPLRLVKHYERTIPLRIIEHPLPLVSFTEAVQWPALHNTDPGNIWMREIMIQEALRIGI | NodD regulates the expression of the nodABCFE genes which encode other nodulation proteins. NodD is also a negative regulator of its own expression. Binds flavonoids as inducers. | P04681 |
Q47TE8 | CH601_THEFY | Chaperonin-60 1 | Thermobifida | MAAKLIAFDEEARRGLERGMNQLADAVKVTLGPKGRNVVLEKKWGAPTITNDGVSIAKEIELEDPYEKIGAELVKEVAKKTDDVAGDGTTTATVLAQALVREGLRNVAAGANPIGLKRGIDAAVARISEELANLSKEVETKEQIASTASISAGDPQIGEYIAEAMDKVGKEGVITVEEGQTFGLELELAEGMRFDKGYISPYFATDLERMETVLEDPYILIANQKISNNNEFLPVIEKVLQAGRPLVVIAEDVEGTALQTLVVNKIRGTFKSVAIKAPGFGDRRKAMLQDIAILTGGQVITEEVGLKLENTELDMLGRAR... | 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. | Q47TE8 |
B8D8D0 | PURA_BUCA5 | IMP--aspartate ligase | Buchnera | MNKNIVILGTQWGDEGKGKVVDCLTKDSSYVVRYQGGHNAGHTLVVNDKKIILHLIPSGLLHKNVIGIIANGVVVSPFELIKEIKMLETHNIFVHKRLFISNSSPLILQYHIEMDIAREKKLGISALGTTGRGIGPAYEDKIARRALRIGDLKNEKTLSIRLEKIVNYYNHQLVSFYKHKPVDYKIILRDLLPTIDLIYDMIKDTTSILHTAIQSNKKIIFEGAQGSFLDIDHGTYPYVTSSNSTIGGVITGTGVGSKSLDYILGVTKAYSTRVGYGPFPTELFDDVDKHFSKKGHEFGSTTGRKRRTGWLDAVALCRSV... | Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. | B8D8D0 |
Q7RXR1 | MTND_NEUCR | Acireductone dioxygenase (Ni(2+)-requiring) | Neurospora | MKAYFYDNLPGDQRLPHDSGKEVTVAELEKVGVLYFRFPDVEGVNTLAAERGYKNRDEIIVSPEKMGAIYETKVRQFFDEHLHEDEEIRYIRDGAGYFDVRNEGDEWIRIKLVKDDLIILPAGIYHRFTTDDTNYIQAMRLFKEEPKWTPLNRTEGLDENPYRQEYVTQFLKAQAEQA | Catalyzes 2 different reactions between oxygen and the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene) depending upon the metal bound in the active site. Fe-containing acireductone dioxygenase (Fe-ARD) produces formate and 2-keto-4-methylthiobutyrate (KMTB), the alpha-ketoacid precursor of methionine... | Q7RXR1 |
Q1C0V9 | RHAB_YERPA | Rhamnulose kinase | Yersinia | MVAIDLGASSGRVMLASYYPGQQQLTLREVCRFTNQIKSIDGSDVWDIDAIEQSIREGLSQLDSEGIALDSIGIDSWGVDFVLLDKQGKRIGQPVSYRDSRTQGVMARAQQTLGSNAIYRRTGIQFLPFNTLYQLRALSEQQPHLLADVAHLLLIPDYLHYRLTGQLNWEYTNASTTQLLNIETGDWDSDLLAYAGVPAHWFAKPGKPGNTIGYWHSANGQQVPVVAVATHDTASAVLAAPLIDADAAYLSSGTWSLMGFESGTPLTHQQAQCSNITNEGGAEGRYRVLKNIMGLWLLQRATDELQIDDLPQLIEQAARQ... | Involved in the catabolism of L-rhamnose (6-deoxy-L-mannose). Catalyzes the transfer of the gamma-phosphate group from ATP to the 1-hydroxyl group of L-rhamnulose to yield L-rhamnulose 1-phosphate. | Q1C0V9 |
P05527 | HMIN_DROME | Homeobox protein invected | Sophophora | MSTLASTRPPPLKLTIPSLEEAEDHAQERRAGGGGQEVGKMHPDCLPLPLVQPGNSPQVREEEEDEQTECEEQLNIEDEEVEEEHDLDLEDPASCCSENSVLSVGQEQSEAAQAALSAQAQARQRLLISQIYRPSAFSSTATTVLPPSEGPPFSPEDLLQLPPSTGTFQEEFLRKSQLYAEELMKQQMHLMAAARVNALTAAAAGKQLQMAMAAAAVATVPSGQDALAQLTATALGLGPGGAVHPHQQLLLQRDQVHHHHHMQNHLNNNENLHERALKFSIDNILKADFGSRLPKIGALSGNIGGGSVSGSSTGSSKNSG... | Engrailed (en) and invected (inv) are functionally redundant transcription factors in neuronal precursor cell NB5-3 specification. Inv is unable to substitute for en in other regulatory processes such as maintaining gsb expression in the neuroectoderm after stage 10 of embryogenesis. Maintenance of gsb expression in ro... | P05527 |
O66511 | FER2_AQUAE | AaFd4 | Aquifex | MAEFKHVFVCVQDRPPGHPQGSCAQRGSREVFQAFMEKIQTDPQLFMTTVITPTGCMNACMMGPVVVVYPDGVWYGQVKPEDVDEIVEKHLKGGEPVERLVISKGKPPGMF | Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. | O66511 |
A1A5X5 | ADIPL_DANRE | Complement C1q tumor necrosis factor-related protein 12 | Danio | MRCWVLAVVTAVLWSQCIPLGWAEGRKVPKRLKEGAPQHTEAFNTTLSNSEELDGSPKQVGENQRVDPLGSWMDFVKRPVGNFPGKCRKRKRPLPGPPGPPGPPGPQGPPGAPGAEVTQEVLLREFKEMIKEATERRAAVDRPSEPSQLPTALITLEGMTSYRRIEEAFHCKLKGPVVVDKKTLAELQNFQTPPAKGAFLRGTGMDQSTGRFTAPVTGIYQFSANVHIDHTEVKRSKSQLRARDNVRVLICIESLCHRYTSLEMIVGLESNSKIFTVSVHGLLELQAGQYTSIFVDNAAGASITIQNGSDFMGMLLGV | Insulin-sensitizing adipocyte-secreted protein (adipokine) that regulates glucose metabolism in liver and adipose tissue. | A1A5X5 |
O58281 | FLA1_PYRHO | Probable flagellin PH0546 | Pyrococcus | MTVVPRKGAVGIGTLIVFIAMVLVAAVAAAVLINTSGYLQQKASGTGRETTQEVASGIKVDRVVGYAPDITGDITRLAVYISPNAGSSGIDLNKVRVILSNGQKEVSLKYNYVYNATSSTQTYVALPQGNIFNDIVLGVNGTSENAASTQVNFNWSLLTGSTFGLIVLQDADGSVKASTPTLNQGDLVIIAIDVDAALGGIPPRTSITGEVIPEQGAPGVIEFTTPSTYTAHVMELQ | Flagellin is the subunit protein which polymerizes to form the filaments of archaeal flagella. | O58281 |
P93654 | SYP22_ARATH | Protein SHOOT GRAVITROPISM 3 | Arabidopsis | MSFQDLESGRGRSTRKFNGGRQDSTQAVASGIFQINTGVSTFQRLVNTLGTPKDTPELREKLHKTRLHIGQLVKDTSAKLKEASETDHQSGVNPSKKIADAKLARDFQAVLKEFQKAQQTAAERETTYTPFVPQSALPSSYTAGEVDKVPEQRAQLQESKRQELVLLDNEIAFNEAVIEEREQGIQEIHQQIGEVNEIFKDLAVLVNDQGVMIDDIGTHIDNSRAATSQGKSQLVQAAKTQKSNSSLTCLLLVIFGIVLLIVIIVLAA | May provide the t-SNARE function in the vacuolar assembly. Promotes the formation of vacuolar membrane 'bulbs'. Required for inflorescence stem gravitropism. | P93654 |
Q3SWE4 | HSLU_NITWN | Unfoldase HslU | Nitrobacter | MTDISPREIVSELDRFIVGQADAKRAVSIALRNRWRRQQLTGPLREEVLPKNILMIGPTGVGKTEIARRLAKLANAPFLKIEATKFTEVGYVGRDVEQIVRDIVEVAINQTRERKRKDVQARAQLAAEERVLDALVGANASAATRDSFRKRLRSGELNDKEIEIETQTSGGGPMFEIPGMPGAQVGAISIGDIFGKMGGRTKTRRLTVSDSYEILINEESDKLLDSDQLTQEAIAAVENNGIVFLDEIDKICVRDGRSGGDVSREGVQRDLLPLIEGTTVSTKHGAVKTDHILFIASGAFHIAKPSDLLPELQGRLPIRV... | ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before... | Q3SWE4 |
B0T8G4 | ACCA_CAUSK | Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha | unclassified Caulobacter | MAAHYLDFERPIADLESKIEELSKLSETAGPGAFESEIQALRDRAQQMRKEAYAGLDAWQKTMVARHPERPHLKDYIAGLIDEFVELRGDRKFADDQAIVGGLGRFRGVPVVVMGHEKGHDTTTRLKHNFGMARPEGYRKAVRLMDMAERFNLPVITFVDTAGAYPGLGAEERGQAEAIARSTERGLVLGTPMVATIVGEGGSGGAIALAGANKVLILEHSIYSVISPEGAASILWRDGARAKDAAANMKITAQDLIQLKIVDRIVEEPAGGAHSDPDAAIQSVGDAVEDELKALMKLSAAELKKQRAARFYAIGREGLQ | Component of the acetyl coenzyme A carboxylase (ACC) complex. First, biotin carboxylase catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the carboxyltransferase to acetyl-CoA to form malonyl-CoA. | B0T8G4 |
Q65JA6 | NRDI_BACLD | Protein NrdI | Bacillus | MIQIVFDSKTGNVQRFVDKTPFRNKRKVSTEEYLDEPFVLITYTTGFGEVPKTTEMFLEKNAHLLLGVAASGNRVWGDNFAKSAEKISKQYQVPILGKFELSGTAKDVELFTQEVERVVTKSSAKMDPVKQ | Probably involved in ribonucleotide reductase function. | Q65JA6 |
A4VMV0 | NQRE_PSEU5 | NQR-1 subunit E | Pseudomonas | MEHYISLFVRAVFIENMALAFFLGMCTFIAISKKVETAIGLGIAVIVVQTITVPANNLIYTYLLKSGALAWAGLPEVDLSFLGLLSYIGVIAAIVQILEMTLDKYVPSLYNALGVFLPLITVNCAIMGGTLFMVERDYNLGESVVYGMGSGLSWALAIALLAGIREKLKYSDVPDGLQGLGITFITIGLMSLGFMSFSGVQL | NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol. | A4VMV0 |
P0DUL8 | HKM10_ASPHA | Hancockiamides biosynthesis cluster protein 10 | Aspergillus | MSTFESLLARNEGLGQLFYQQMLEDPDAIAIVDGDYSLTYASLHAQATHLAQRLDQNDFVHEEPVGIVVQHGILDAVAQVAIIYAGGTCVTLDPALPNQQIERRLNRLRARYILVDTPNKSRGLPFSQIEVEDLPISTELIPTDSPYPVNLSLEHRSHLIHTSGTTSESKAVQIVGRSIVHVANYAPFEPVVKTDVVAHGNSTSFDVALFDIWAPLVQGASIAVLSKATLLDLSAFEAAIDRYKISVMAITAPLVNLAATTRPGMFSSMRVVLMGGEAVNIPAMRKIFEAGPPVHMVNAYGPTECCVYCLARKITLEDLD... | Non-canonical nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of hancockiamides, an unusual new family of N-cinnamoylated piperazines . The NRPS hkm10 and the NmrA-like reductase hkm9 are proposed to convert two molecules of L-Phe to the intermediary piperazine called xenocockia... | P0DUL8 |
Q9DDT2 | BCAP_CHICK | B-cell phosphoinositide 3-kinase adapter protein 1 | Gallus | MTASGTHGGYDVLILYASDAAEWCQYLQNLFLSTRHIRKHHIQSYQLEGESAISDQELDLFNRSRSIIILLSAELVQNFYCPPVLQSLQEALWPPHKVVKLFCGVTDCDDYLTFFKDWYQWQELTYDDEPDAYLEAVKKAISEDSGCDSVTDTETEDEKTSVYSCQLAMNEEHESSKSTGEHLVVQPDHIRCGVQTTVYIIMKCRLDDKVKTEVEFSPENSSSVRVLAELENEYTISVEAPNLTSGTVPLQIYSGDLMVGETSVTYHTDMEEISSLLANAANPVQFMCQAFKIVPYSIEALDKLLTESLKKNIPASGLHL... | Signaling adapter that contributes to B-cell development by linking B-cell receptor (BCR) signaling to the phosphoinositide 3-kinase (PI3K)-Akt signaling pathway. Has a complementary role to the BCR coreceptor CD19, coupling BCR and PI3K activation by providing a docking site for the PI3K subunit PIK3R1. Alternatively,... | Q9DDT2 |
Q9X756 | KEFC_KLEAE | K(+)/H(+) antiporter | Klebsiella | MDSHTLIQALIYLGAAALIVPIASVLGLGSVLGYLIAGCIIGPWALRLVNDAEAILHFAEIGVVLMLVAMGLELDPQRLWKLRASVFDGGALQMVACGVLIGLFCMLLGLRWQVAELIGMTLALSSTAIAMQAMNERNLTVSQMGRSAFAVLLFQDIAAIPLVAMIPLLAASGGATSLMAFALSALKVAAALALVVVLGRYLTRPLLRFVARSGLREVFSAVACSWSSALGLLLEEVGLSMAMGAFLAGVLLASSEYRHALENDIEPVKGLLLGLFFIGVGMSIDFAPWSPNPLRIVILLVGFPAIKMLMLWLIAQPLGV... | Pore-forming subunit of a potassium efflux system that confers protection against electrophiles. Catalyzes K(+)/H(+) antiport. | Q9X756 |
Q5KWB0 | ACCA_GEOKA | Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha | Geobacillus thermoleovorans group | MVAELEFEKPLVELRRKIQELKEFMKTADVDLSAEIEKLEARLAKLENEIYANLTPWDRVQIARHPQRPTTLDYIERLFTNFLECHGDRCFGDDEAIVGGIAKYDGLPVTVIGHQRGKDTKENLRRNFGMPHPEGYRKALRLMKQAEKFSRPIICFIDTKGAYPGKAAEERGQSEAIARNLFEMAGLTVPVVCIVIGEGGSGGALALGVGNHIHMLENSTYSVISPEGAAAILWKDASLAQRAAETMKITAHDLKALGVIDEIIPEVKGGAHRNADEQAKEIDRVLRRSLKQLLALDGEELVRQRYEKFKQMGQVSFLPE... | Component of the acetyl coenzyme A carboxylase (ACC) complex. First, biotin carboxylase catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the carboxyltransferase to acetyl-CoA to form malonyl-CoA. | Q5KWB0 |
Q9SAR0 | 1A16_ARATH | S-adenosyl-L-methionine methylthioadenosine-lyase 6 | Arabidopsis | MVAFATEKKQDLNLLSKIASGDGHGENSSYFDGWKAYEENPFHPIDRPDGVIQMGLAENQLCGDLMRKWVLKHPEASICTSEGVNQFSDIAIFQDYHGLPEFRQAVAKFMEKTRNNKVKFDPDRIVMSGGATGAHETVAFCLANPGDGFLVPTPYYPGFDRDLRWRTGVNLVPVTCHSSNGFKITVEALEAAYENARKSNIPVKGLLVTNPSNPLGTTLDRECLKSLVNFTNDKGIHLIADEIYAATTFGQSEFISVAEVIEEIEDCNRDLIHIVYSLSKDMGLPGLRVGIVYSYNDRVVQIARKMSSFGLVSSQTQHLI... | 1-aminocyclopropane-1-carboxylate synthase (ACS) enzymes catalyze the conversion of S-adenosyl-L-methionine (SAM) into 1-aminocyclopropane-1-carboxylate (ACC), a direct precursor of ethylene. Involved in bacterial flagellin-induced ethylene production. | Q9SAR0 |
P29113 | PIC2_RHIRD | ORF2 | Agrobacterium tumefaciens complex | MSQSPPERFILLDGIRGVAALFIVHRHAEQFFGRDPASSYLAVDLFFALSGFVLAHAYGKKLYEGTITPGFFLKARFARLYPLYVLALALMAAYFICLYVLGLPTPIDDLHRLIDPGELAFALVTGLLFLPAPFTLTLNGALFLVSPAWSLFNELVVNAVYARWGARATMKQTVLVLAVSAVVLMVAAAEF | Seems to regulate the surface properties of the bacterium in the presence of plant cells or plant cell extracts. | P29113 |
A4QLQ3 | NDHH_LOBMA | NADH-plastoquinone oxidoreductase subunit H | Lobularia | MTRPVTGKDLMIVNMGPHHPSMHGVLRLIVTLDGEDVVDCEPILGYLHRGMEKIAENRAIIQYLPYVTRWDYLATMFTEAITVNGPEQLGNIQVPKRASYIRVIMLELSRIASHLLWLGPFMADIGAQTPFFYIFREREFVYDLFEAATGMRMMHNFFRIGGIAADLPYGWIDKCLDFCDYFLTEVVEYQKLITRNPIFLERVEGVGIIGGEEAINWGLSGPMLRASGIPWDLRKVDRYESYDEFEWEIQWQKQGDSLARYLVRLSEMTESIKIIQQALEGLPGGPYENLESRGFDRKRNPEWNDFEYRFISKKPSPTFE... | 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... | A4QLQ3 |
A2RJ04 | BRNQ_LACLM | Branched-chain amino acid transport system carrier protein | Lactococcus cremoris subsp. cremoris | MKEKLAGKDYLFIGSMLFGLFFGAGNLIFPIHMGQEAGDAISQANFGFLVTAVGFPFLGIIALGISQSNGVFELATRVNRIYAYIFTILLYLVIGPFFALPRLATTSFEIGISPFLSNKLQTPLLALFSILFFGTAWFLSRKPTKLLDYIGKFLNPLFLVLLGLILIIAFSHPLGSVHQAEVGKLYQSSAFMNGFTQGYNTLDALAALAFGIIIITTIRQRGVKNSKIIAKETIKAGLISVGLMAIIYTCLSYLGAMSVGKFAISENGGIALAQISNYYLGTFGMIILALIVIIACLKTAVGLMSAFSETFVELFPKREY... | Component of the transport system for branched-chain amino acids. Can transport isoleucine, leucine and valine. | A2RJ04 |
B1LE00 | CEDA_ECOSM | Cell division activator CedA | Escherichia | MKKPLRQQNRQIISYIPRTEPAPPEHAIKMDSFRDVWMLRGKYVAFVLMGESFMRSPAFTVPESAQRWANQIRQEGEVTE | Activates the cell division inhibited by chromosomal DNA over-replication. | B1LE00 |
Q49150 | PQQCD_METEA | Coenzyme PQQ synthesis protein D | Methylorubrum | MTAQFPPPVPDTEQRLLSHEELEAALRDIGARRYHNLHPFHRLLHDGKLSKDQVRAWALNRYYYQAMIPVKDAALLARLPDAQLRRIWRQRIVDHDGDHEGDGGIERWLKLAEGVGFTRDYVLSTKGILSATRFSVDAYVHFVSERSLLEAIASSLTEMFSPTIISERVAGMLKNYDFITKDTLAYFDKRLTQAPRDADFALDYVKRHATTPEMQRAAIDALTFKCNVLWTQLDALYFAYVAPGMVPPDAWQPGEGLVAETNSAEDSPAAAASPAATTAEPTAFSGSDVPRLPRGVRLRFDEVRNKHVLLAPERTFDLDD... | The PqqD region functions as a PqqA binding domain and presents PqqA to PqqE. | Q49150 |
A4J559 | PYRK_DESRM | Dihydroorotate oxidase B, electron transfer subunit | Desulforamulus | MSKVFDAKVLAVYMVAPNTYYMEFDAPDIARLAVPGQFVHVRCGETNDPLLRRPISIHMVSRPKGVLALLFRVVGKGTEILSQQKPGDRVNMMGPLGRGFTLPLPGSKVAVAAGGIGAAPLVFLVQELANIKCQVTVYLGARDKRSILCDGQFIQMEAEVVIATDDGSLGFKGTVPELMKRHMDWRKTAMTYVCGPGIMMKEISTMLAEADVPGEVSLEERMGCGVGACLSCAVKISHHGQISNKRACFEGPVFPSWQVVWE | Together with PyrD, also forms a metal reductase complex able to reduce Fe(III)-chelates to Fe(II)-chelates, as well as soluble Cr(VI) and U(VI), using NADH as electron donor. To a lesser extent, can also use NADPH as an electron donor. Is unable to reduce riboflavin and FMN with NADH as electron donor. May have an in ... | A4J559 |
Q8G2M7 | BEPD_BRUSU | Efflux pump periplasmic linker BepD | Brucella | MTLNRTIRCFAAGAAFIVFAAQPALAQAPGGATPPPPQVFVVDIKPHDVPVTYEYAARINAYRNVQVRARVGGILLHRNFVEGTQVKAGEVLFEIDPAPYQAELEKAQAQVAQAEAQYQQSIRDAERAEQLVQQKVQSAAVRDSAFATRDLNKAAVAAAKAQLRTAELNLSYTKVTAPISGITSQEQVNEGSLIGTDASSSLLTSVTQLDPVYVNFSFTDTEAAEIAKLRAERGATGEDADRLKIKILFGDGKAYDHEGTIDFTSSSLDTETGTLGVRAVVENPNHRLIPGQFVRAEILDIQVKDAITVPKAALMQSAQG... | Involved in resistance to several unrelated toxic compounds, such as dyes, detergents and antibiotics. | Q8G2M7 |
A0A1L2FZD4 | KAX88_ORTSC | OSK3 | Orthochirus | MCRLYAIILIVLVMNVIMTIIPDSKVEVVSCEDCPEHCSTQKARAKCDNDKCVCEPI | Selectively inhibits voltage-gated potassium channels rKv1.2/KCNA2 (IC(50)=331 nM) and hKv1.3/KCNA3 (IC(50)=503 nM). Partially inihibts rKv1.6/KCNA6 (IC(50)=9983 nM). | A0A1L2FZD4 |
P80577 | PEDB_HYDVU | Pedibin | Hydra | AGEDVSHELEEKEKALANHSE | Morphogenetically active peptide. Active in foot development. | P80577 |
Q3K1G0 | NDK_STRA1 | Nucleoside-2-P kinase | Streptococcus | MEQTFFMIKPDGVKRGFIGEVISRIERRGFSIDRLEVRYADADILKRHYAELTDRPFFPTLVDYMTSGPVIIGVISGEEVISTWRTMMGSTNPKDALPGTIRGDFAQAPSPNQATCNIVHGSDSPESATREIAIWFNN | Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. | Q3K1G0 |
Q9RR89 | ISPE_DEIRA | 4-(cytidine-5'-diphospho)-2-C-methyl-D-erythritol kinase | Deinococcus | MTHQPSPVIHHHFAPAKINLGLSVLGVRENGYHDLHSLMVPLTVGDELEIRPAGALTLRVEGADLPTDERNLVYRAARAYLDAAGAAGGADLVLHKRLPLASGLGGGSSDAASTLLALAELYPAPDHRPVDLPALALTLGADVPFFLLGGAALAEGVGERLTPVDDLPPVHLVLANAGAEVSAGDAYRWLDETGDFSGKLRLEAMRLALARGVEVPYFNSLQAGVLARVPSVLTTLEALADAGLHSVLMSGSGATCFGLAHDAAQAQAAAAALAQRCPGWWVTAAQVRLPLSDNSGGRT | Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol. | Q9RR89 |
Q82KE1 | NRDR_STRAW | Transcriptional repressor NrdR | Streptomyces | MHCPFCRHPDSRVVDSRTTDDGTSIRRRRQCPDCSRRFTTVETCSLMVVKRSGVTEPFSRTKVINGVRKACQGRPVTEDALAQLGQRVEEAVRATGSAELTTHDVGLAILGPLRELDLVAYLRFASVYRAFDSLEDFEAAIAELREEQRERPAVDDEDHEDAGAERQGTDRGSGGTVEVPVPATVAD | Negatively regulates transcription of bacterial ribonucleotide reductase nrd genes and operons by binding to NrdR-boxes. | Q82KE1 |
A8G8U7 | MUTL_SERP5 | DNA mismatch repair protein MutL | Serratia | MPIQVLPPQLANQIAAGEVVERPASVVKELVENSLDAGATRIDIDIERGGAKLIRIRDNGSGIGKDDLALALARHATSKISTLDDLEAIVSLGFRGEALASISSVSRLTLTSRTAEQNEAWQAYAEGRDQAVTVKPAAHPIGSTLEVLDLFYNTPARRKFMRTEKTEFGHIDEVVRRIALARFDVAINLSHNGKLMRQYRAAKDESQYERRLGSICGPAFLQHALNISWQHGDLTIRGWVADPAGARQLGEMQYCYVNSRMMRDRLINHAIRQAYQDQLKDDQQPAYVLYLEVDPHQVDVNVHPAKHEVRFHQARLVHDF... | This protein is involved in the repair of mismatches in DNA. It is required for dam-dependent methyl-directed DNA mismatch repair. May act as a 'molecular matchmaker', a protein that promotes the formation of a stable complex between two or more DNA-binding proteins in an ATP-dependent manner without itself being part ... | A8G8U7 |
Q5AQN0 | GATA_EMENI | Glutamyl-tRNA(Gln) amidotransferase subunit A, mitochondrial | Aspergillus subgen. Nidulantes | MSLLLEAERYVANQSSNRMLNAFITPLCRHSGRWHDQAKDADIRGKQGKLRSRLDGRFIAFKDNICTRDFPTTCASKSLDTFTSPFNATVVQQLEDAGAIVAGKTNLDEFGMGSHSIYSSFGHVMNTRRGDDSKFLSAGGSSGGNAVAVATDQCYAALGTDTGGSIRLPAAYTGTVGFKPSYGLLSRWGVIAYANSLDTVGILAKRVSVARDVFDVLNKHDPRDPTSISPSSRSRISSKLNLPQLTSRLTSRPLRIGIPLEYNISELAPSVRQAWCHSLEYLRQQGHTIQPVSLPMTKLALSAYYVLAPAEASSNLAKYD... | Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in the mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln). | Q5AQN0 |
B2V5L9 | QUEC_SULSY | Queuosine biosynthesis protein QueC | unclassified Sulfurihydrogenibium | MLKKENIIVLLSGGMDSAVLLWLSKTIFKDVYTISYSYGQKHSIELEYAKELSKIAGVKEHFIVEVPHLKQLKGSALTDENLEIPSENYPDEPPITTVPMRNLIFLSIAASFADVYEIENIGIGIHSLDSPYPDCRAEFASSAEAVINASSVMVAKKKNRIKIFTPFLGMSKTDIAKLGRELGVPFEKTYSCYKGTVPPCGECATCRQREEALRETFSDTTT | Catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)). | B2V5L9 |
G5ED65 | VER1_CAEEL | Vascular endothelial growth factor receptor related 1 | Caenorhabditis | MTHRTPNFRRFHLFLPLFLKGMIFLLLHFKFLVIFALELPIISLRPKSDCFLFWKCTTDYRIQKNQKIGKFVELTEGQTLSLQCAYRRGTPKFTYPNFLAERVEQEFSEPLNTDYVRIEDIRESDTGSFSCNSTENPAQSDSIHVFVHKSKIFLPSKSVFSKKDLWNELTVPCKTTKLTESKEIELYADGKLVASQDFDPRHGFRITRKGYAAQPSFFECKFNKKNKTQSVDFIISKNEPIDNEYILFWEDSFPFPHVGYNFSLTCHLVYIEPNGNAPKLGELAFECPQCQSRLDNHLVIEKHHNVGRKRLSSAIHIKNL... | Involved in amphid glia remodeling during entry into dauer stage by promoting the fusion of sheath amphid cells which encloses AWC neuron sensory endings . May be involved, downstream of pvf-1, in the positioning of ray 1, the most anterior ray sensillum in the male tail . | G5ED65 |
Q9LA06 | HTRA_LACLA | Serine protease Do-like HtrA | Lactococcus | MAKANIGKLLLTGVVGGAIALGGSAIYQSTTNQSANNSRSNTTSTKVSNVSVNVNTDVTSAIKKVSNSVVSVMNYQKDNSQSSDFSSIFGGNSGSSSSTDGLQLSSEGSGVIYKKSGGDAYVVTNYHVIAGNSSLDVLLSGGQKVKASVVGYDEYTDLAVLKISSEHVKDVATFADSSKLTIGEPAIAVGSPLGSQFANTATEGILSATSRQVTLTQENGQTTNINAIQTDAAINPGNSGGALINIEGQVIGITQSKITTTEDGSTSVEGLGFAIPSNDVVNIINKLEADGKISRPALGIRMVDLSQLSTNDSSQLKLPS... | Degrades abnormal exported proteins and responsible for the propeptide processing of a natural pro-protein and for the maturation of a native protein. It also plays a prominent role in stress (heat shock, ethanol, puromycin and NaCl) resistance during active exponential growth. | Q9LA06 |
Q82VS2 | MURC_NITEU | UDP-N-acetylmuramoyl-L-alanine synthetase | Nitrosomonas | MKHKIRHIHFVGIGGSGMGGIAEVLINLGFQISGSDMHSNSTTRRLQCLGAVIHHTHAAENIQSADAVVISTAIHSDNPEVIAARERRIPVVPRAMMLAELLRLRRGIAIAGTHGKTTTTSLVASILAEAGQDPTFVIGGKLKTVDSHARLGKGEFIVVEADESDASFLYLQPVLTVVTNIDADHMSTYEHDFNRLKQTFVEFIEHLPFYGMAVLCVDDPHVREIISMITRPVTTYGIASEDAQICATNIRHDRCRMHFLAHIGVNGSPRTLEVTLNLPGKHNVLNALAAIAVGNELGVPDEAIVKALATFGGVDRRFQQ... | Cell wall formation. | Q82VS2 |
Q9PA75 | ISPE_XYLFA | 4-(cytidine-5'-diphospho)-2-C-methyl-D-erythritol kinase | Xylella | MGRVDPVSVVVDDGVGWSAWPAPAKLNLFLQITGRRVDGYHELQTVFRLLDWGDTIHLRVREDGQIHRIGESVTGVVEADDLVVRAAYLLKYATNVHLGADIFVEKRIPVGGGFGGGSSDAATVLLVLNALWHTRLDVAVLAALGLRLGADVPVFVHGCNAWAEGVGECLTPMILPGAAYLLLDPGVCVPTRELFLDPDLTRDASPATIGDFIAGTAFGNAFEPVLRRRESAVAGALDVLSEVGFARVTGSGSGCFVEFSTRDEAECALERLPYGLCAWVADGASRSPLLDVLKTMEF | Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol. | Q9PA75 |
B0KF81 | LEUC_PSEPG | Isopropylmalate isomerase | Pseudomonas | MAGKTLYDKLWEAHEVKRRDDGSSLIYIDRHIIHEVTSPQAFEGLRLANRKPWRIDTNIATPDHNVPTTPERKGGIEAIVDQVSRLQVQTLDENCDEYGIVEFKMNDERQGIVHVISPEQGATLPGMTVVCGDSHTSTHGAFGALAHGIGTSEVEHVLATQCLVAKKMKNMLVRVEGQLPAGVTAKDIVLAVIGKIGTAGGNGHAMEFAGSAIRELSMEGRMTICNMSIEAGARVGLVATDATTVAYVEGRPYAPKGEQWKQAVESWKDLVSDEDAVFDTVVELDASQIKPQVSWGTSPEMVLAVDQRVPDPAAEADLVK... | Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate. | B0KF81 |
Q74CF3 | QUEE_GEOSL | Queuosine biosynthesis protein QueE | Geobacter | MSKPGAELEEVFSSVQGEGMLIGLRQVFIRFRGCNLTCDYCDTPAGTPAEPCRIEQTPGRRDFVPADNPVSLDRVAALVEGWQRGWPGVHDSISITGGEPLLRHDILMQWLPVLREHLPVYLETNGVMHAALGLVINHVDIIGMDIKIPSTSGCTDLWDDHRQFLEIANTRRAFIKIVVGEETEDWEITRASEIIAGVNRDIPLILQPVTRAGDTLGIKPVKALELQELACRYLAEVRIIPQTHRFMGQL | Catalyzes the complex heterocyclic radical-mediated conversion of 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) to 7-carboxy-7-deazaguanine (CDG), a step common to the biosynthetic pathways of all 7-deazapurine-containing compounds. | Q74CF3 |
A1AE45 | EX7L_ECOK1 | Exodeoxyribonuclease VII large subunit | Escherichia | MLPSQSPAIFTVSRLNQTVRLLLEHEMGQVWISGEISNFTQPASGHWYFTLKDDTAQVRCAMFRNSNRRVTFRPQHGQQVLVRANITLYEPRGDYQIIVESMQPAGEGLLQLKYEQLKAKLQAEGLFDLQYKKSLPSPAHCVGVITSKTGAALHDILHVLKRRDPSLPVIIYPTAVQGDDAPGQIVRAIELANQRNECDVLIVGRGGGSLEDLWSFNDERVARAIFASRIPIVSAVGHETDVTIADFVADLRAPTPSAAAEVVSRNQQELLRQVQSTHQRLEMAMDYYLANRTRRFTQIHHRLQQQHPQLRLARQQTMLE... | Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides. | A1AE45 |
Q1H4F1 | CH10_METFK | Chaperonin-10 | Methylobacillus | MAIRPLQDRVIVKRLEEERKTASGIVIPDTAAEKPDQGEVIAVGPGKKDDNGKSIPLDVKVGDKVLFGKYAGQAVKVNGEEVLVLREDDILGIVEA | Together with the chaperonin GroEL, 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. GroES binds to the apical surface of ... | Q1H4F1 |
Q0W8X2 | IF2P_METAR | Probable translation initiation factor IF-2 | Methanocella | MATATEIRKDLRTPIVCVMGHVDHGKTSLLDRIRGTAVVDKEAGAITQHIGATEVPLQTIQTLCKGMIGGNIVVPGLLFIDTPGHHAFTNLRSRGGALADLAVLVVDINEGFQPQTVEAIKILKQFKTPFVIAANKIDRIHGWTAKNNSPFLQTFNSQPDHVKGIIETKTYELVGRMSDLGFSSDRYDRIRDFTRNIGIIPISARTGEGIPDLLMILIGLAQRFLEESLKFQVTGPGVGTILEVKEERGLGYTIDTIIYDGEIRVGDTIVIGGREKPYSTKVRALLKPKPNREIRVEERFDRVNKVTAASGVKILAPELE... | Function in general translation initiation by promoting the binding of the formylmethionine-tRNA to ribosomes. Seems to function along with eIF-2. | Q0W8X2 |
P94418 | YCLN_BACSU | Petrobactin import system permease protein YclN | Bacillus | MKLRYLFILLIILAVTSVFIGVEDLSPLDLFDLSKQEASTLFASRLPRLISIVIAGLSMSICGLIMQQISRNKFVSPTTAGTMDWARLGILISLLLFTSASPLIKMLVAFVFALAGNFLFMKILERIKFNDTIFIPLVGLMLGNIVSSIATFIAYKYDLIQNVSSWLQGDFSLVVKGRYELLYLSIPLVIIAYVYADKFTLAGMGESFSVNLGLKYKRVVNIGLIIVSLITSLVILTVGMLPFLGLIIPNIVSIYRGDNLKSSLPHTVLLGAVFVLFCDILGRIIIFPYEISIGLMVGIIGSGIFLFMLLRRKAYA | Part of the ABC transporter complex YclNOPQ involved in uptake of ferric-petrobactin. Petrobactin is a photoreactive 3,4-catecholate siderophore produced by many members of the B.cereus group, including B.anthracis. Probably responsible for the translocation of the substrate across the membrane. | P94418 |
A7NN90 | PYRG_ROSCS | UTP--ammonia ligase | Roseiflexus | MAKYIFVTGGVASSVGKGITVASIGRLLKARGVRVSVQKLDPYINVDPGTMSPYQHGEVFVTEDGAETDLDLGHYERFIDVNLTRLSNVTTGQIYSAVIQKERRGDYLGGTIQVIPHITNEIKARIAAVARQTGAEVVIVEIGGTVGDIEGLPFLEAIRQMRKDVGRDNVLYIHVTLLPHIGATGEVKTKPTQHSVMELRRVGITADVIVCRSDYPIADEIRDKIALFADVDVEAVVPLHTVESIYEVPLVLEEAGLGNYLTLRLGLGVREPNLDDWRDLVARIKAPKRKLAIALVGKYVELHDAYISVVEALRHAGLHQ... | Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates. | A7NN90 |
Q97B93 | RPO3_THEVO | DNA-directed RNA polymerase subunit D | Thermoplasma | MEVKIFKLSDKYMSFEIDGITPSQANALRRTLINDIPKLAIENVTFHHGEIRDAEGNVYDSSLPLFDEMVAHRLGLIPLKTDLSLNFRDQCSCGGKGCSLCTVTYSINKIGPASVMSGDIQAISHPDLVPVDPDIPIVKLGAKQAILITAEAILGTAKEHAKWQVTSGVAYKYHREFEVNKKLFEDWAKIKERCPKSVLSEDENTIVFTDDYGCNDLSILFESDGVQIKEDDSRFIFHFETDGSLTAEETLSYALNRLMDRWGILVESLSE | DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | Q97B93 |
P08883 | GRAF_MOUSE | MCSP3 | Mus | MPPILILLTLLLPLRAGAEEIIGGHEVKPHSRPYMARVRFVKDNGKRHSCGGFLVQDYFVLTAAHCTGSSMRVILGAHNIRAKEETQQIIPVAKAIPHPAYDDKDNTSDIMLLKLESKAKRTKAVRPLKLPRPNARVKPGHVCSVAGWGRTSINATQRSSCLREAQLIIQKDKECKKYFYKYFKTMQICAGDPKKIQSTYSGDSGGPLVCNNKAYGVLTYGLNRTIGPGVFTKVVHYLPWISRNMKLL | This enzyme is probably necessary for target cell lysis in cell-mediated immune responses. | P08883 |
Q86YH2 | Z280B_HUMAN | Zinc finger protein 632 | Homo | MEQSCEEEKEPEPQKNIQETKQVDDEDAELIFVGVEHVNEDAELIFVGVTSNSKPVVSNILNRVTPGSWSRRKKYDHLRKDTARKLQPKSHETVTSEAVTVLPASQLESRSTDSPIIIEPLSKPDYRNSSPQVVPNNSSELPSPLITFTDSLHHPVSTALSVGGINESPRVSKQLSTFEVNSINPKRAKLRDGIIEGNSSASFPSDTFHTMNTQQSTPSNNVHTSLSHVQNGAPFPAAFPKDNIHFKPINTNLDRENELAKTDILSLTSQNKTFDPKKENPIVLLSDFYYGQHKGEGQPEQKTHTTFKCLSCVKVLKNVK... | May function as a transcription factor. | Q86YH2 |
C1CAI9 | RUVA_STRP7 | Holliday junction ATP-dependent DNA helicase RuvA | Streptococcus | MYAYLKGIITKITAKYIVLETNGIGYILHVANPYAYSGQVNQEDQIYVHQVVREDAHLLYGFRSEDEKKLFLSLISVSGIGPVSALAIIAADDNAGLVQAIETKNITYLTKFPKIGKKTAQQMVLDLEGKVVVAGDDLPAKVAVQASAENQELEEAMEAMLALGYKATELKKIKKFFEGTTDTAENYIKSALKMLVK | The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. RuvA... | C1CAI9 |
P22250 | SYE_BACSU | Glutamyl-tRNA synthetase | Bacillus | MGNEVRVRYAPSPTGHLHIGNARTALFNYLFARNQGGKFIIRVEDTDKKRNIEGGEQSQLNYLKWLGIDWDESVDVGGEYGPYRQSERNDIYKVYYEELLEKGLAYKCYCTEEELEKEREEQIARGEMPRYSGKHRDLTQEEQEKFIAEGRKPSIRFRVPEGKVIAFNDIVKGEISFESDGIGDFVIVKKDGTPTYNFAVAIDDYLMKMTHVLRGEDHISNTPKQIMIYQAFGWDIPQFGHMTLIVNESRKKLSKRDESIIQFIEQYKELGYLPEALFNFIGLLGWSPVGEEELFTKEQFIEIFDVNRLSKSPALFDMHK... | Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu). | P22250 |
Q65GT8 | Y2856_BACLD | Uncharacterized methyltransferase BLi02856/BL02021 | Bacillus | MGREFIPLFENWANSYDDTVVGRDLQYKEVFRDYDGILDDVVSRSGHKVLEFGVGTGNLTAKLLAAGKAVTGVEPSKAMREIAEAKLPENAVIVDGDFIDFPDPPFSPDTIVSSYAFHHLTNEEKREAVKRYGKMLGKHGKIVFADTVFKNREAFSAAVKKAKENGFLQLAEDLETEHYPTISEMETIFTSEHFSIAFQKHNDFVWVMEAAKL | Could be a S-adenosyl-L-methionine-dependent methyltransferase. | Q65GT8 |
Q6FMD8 | RPN8_CANGA | 26S proteasome regulatory subunit RPN8 | Nakaseomyces/Candida clade | MSLHHDNVTIAPLVLLSVLDHYERTNTPEGKRCVGVILGDSQTNTIRVTNSFALPFEEDEKNSDVWFLDHNYIESMNEMCKKINAKEKLIGWYHSGPKLRASDLKINELFKKYTQGNPLLLIVDVKQQDVGLPTDAYMAVEQVKDDGTSTEKTFLHLPCTVEAEEAEEIGVEHLLRDVRDQAAGGLSIRLTNQLKSLKGLQKKLNDIVIYLNKVINNELPVNHTILGKLQDVFNLLPNLGYNEETDVSATSNDMVTASNNLQRALTVKTNDELMVIYITNLVRAIIAFDDLIENKMQNKKLQEERNKELQADINKVESET... | Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins. | Q6FMD8 |
Q9B365 | CYB_PTEPR | Ubiquinol-cytochrome-c reductase complex cytochrome b subunit | Pteronotus | MTNIRKTHPLLKIVNDSLVDLPVPSSVSSWWNFGSLLAACLAVQILTGLFLAMHYTSDTATAFNSVTHICRDVNYGWILRYLHANGASMFFICLYIHVGRGLYYGSYMYSETWNIGILLLFAVMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTDLVQWIWGGFSVDKATLTRFFAFHFLLPFIIAALVVVHLLFLHETGSSNPTGIPSDPDMVPFHPYHTIKDILGILMMLTALSMLVLFSPDLLGDPDNYIPANPLNTPPHIKPEWYFLFAYAILRSIPNKLGGVLALVLSILILAIIPLLHTSKQRTMMFRPL... | Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is... | Q9B365 |
Q3BSC5 | EX7L_XANC5 | Exodeoxyribonuclease VII large subunit | Xanthomonas | MADRNDQILTPSQLNSLARDLLEGSFPLVWVEAELSSVTRPASGHLYFTLKDARAQIRCAMFKPKSTWLKFQPREGLRVLARGRLTLYEARGDYQLVLDHMEEAGEGALRRAFDELRARLAAEGLFDAERKQALPAHVQRLAVITSPSGAAVRDVLSVLARRFPLLEVDLLPSLVQGDSAAAQITSLLQRADASGRYDVILITRGGGSLEDLWAFNDERLARAIAAAQTPVVSAVGHETDFSLSDFVADVRAPTPSVAAELLVPDQRELVARVRRAQARMTQLQQHALGNAMQRADRLALRLRAQSPQARLQLLHRRQQD... | Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides. | Q3BSC5 |
Q8GPG4 | DDHA_RHOSU | Dimethylsulfide dehydrogenase molybdenum subunit | Rhodovulum | MLRTTRRTLMQGASLVGAGLFAAGRGWALNRLEPIGDTLAEEYPYRDWEDLYRNEFTWDYVGKAAHCINCLGNCAFDIYVKDGIVIREEQLAKYPQISPDIPDANPRGCQKGAIHSTSMYEADRLRYPMKRVGARGEGKWQRISWDQATEEIADKIIDIYEKYGPGKLMTHTGSGNMSMMRMAAPYRFASLVGGVQLDIFTDVGDLNTGAHLAYGNALESFTSDAWFGADYIMFLLFNPVATRIPDAHFLWEAKWNGARVVSVAPDYNPSSIHSDLWMPIKQGADPFLAMSMVNVIIEGKLYNEAFMKEQTDLPILVRSD... | Allows photoautotrophic growth on dimethyl sulfide (DMS) as the sole electron donor. | Q8GPG4 |
Q4L5V7 | CODY_STAHJ | GTP-sensing transcriptional pleiotropic repressor CodY | Staphylococcus | MSLLSKTRELNTLLQKHKGIAVDFKDVAQTISSVTVTNVFIVSRRGKILGSSLNELLKSQRINEMLESKHIPSEYTELLMDVKQTESNIDIDNELTVFPPEDKEVFSSSRTTVFPILGGGERLGTLVLGRVKDDFNENDLVLGEYAATVIGMEILREKHNEVEKEARDKAAITMAINSLSYSEKEAIEHIFEELGGNEGLLIASKVADRVGITRSVIVNALRKLESAGVIESRSLGMKGTFIKVKKEKFLDELERNK | DNA-binding protein that represses the expression of many genes that are induced as cells make the transition from rapid exponential growth to stationary phase. It is a GTP-binding protein that senses the intracellular GTP concentration as an indicator of nutritional limitations. At low GTP concentration it no longer b... | Q4L5V7 |
P36018 | YPT52_YEAST | GTP-binding protein YPT52 | Saccharomyces | MLQFKLVLLGDSSVGKSSIVHRFVKDTFDELRESTIGAAFLSQSITIHPNDGNETKDVVIKFEIWDTAGQERYKSLAPMYYRNANAALVVYDITQEDSLQKARNWVDELKNKVGDDDLVIYLLGNKVDLCQETPSTETSPDSNEGGDEEQKVRAISTEEAKQYAQEQGLLFREVSAKTGEGVKEIFQDIGEKLYDLKKDEILSKQNRQIGGGNNGQVDINLQRPSTNDPTSCCS | Required for transport in the endocytic pathway and for correct sorting of the vacuolar hydrolases suggesting a possible intersection of the endocytic with the vacuolar sorting pathway. | P36018 |
C1FMK5 | UVRB_CLOBJ | Excinuclease ABC subunit B | Clostridium | MNQFKVISKFNPTGDQPKAIKSIAKGIEKREKFQTLIGVTGSGKTFTMANIIEKVQKPTLVLAHNKTLAAQLCSEFREFFPNNAVEYFVSYYDYYQPEAYVAQSDTYIEKDASINDEIDKLRHSATSALFERKDVIIVASVSCIYGLGNPEEYKKLTISLREGMEKDRDEIIKKLVEIQYERNDIDFSRGTFRVKGDVLDIFPASSSSKAVRVEFFGDEIDRIKEFDVLTGETITKLKHISIFPASHFATSKDRLEVAIKDIEEELEERVKELVSQDKILEAQRLKQRTNFDIEMMREVGYCTGIENYSRVLDGRAKGTP... | The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP bindi... | C1FMK5 |
A8GE04 | ARAA_SERP5 | L-arabinose isomerase | Serratia | MNAFKQREVWFAIGSQHLYGPQTLQQVKAHAEQVVDSLNREAGLPVKLVLKPLVTTPDEITALCRDANYQPQCIGILAWLHTFSPAKMWIAGLSVLHKPLLQFHTQFNAQVPWDSMDMDFMNLNQTAHGGREFGFIGARMRQQHSVIAGHWQDPEAHRRIGQWMRVASAKQAGQQLKVARFGDNMREVAVTDGDKVGAQIQFGYSVNAYGIGDLVSVINEVSRGDVDTLIEEYEASYVLSDAAKINGAKRENLTDAARIELGMKRFLEQGNFQAFTTNFEDLHGMKQLPGLAVQRLMQQGYGFGGEGDWKTAALLRILKV... | Catalyzes the conversion of L-arabinose to L-ribulose. | A8GE04 |
A1TND2 | TRMD_ACIAC | tRNA [GM37] methyltransferase | Acidovorax | MRFDVITLFPELFTPFLASGVTRRAYATGLVDVRFWNPRDYAEGNYRRVDDRPFGGGPGMVMMAEPLERCLRAIRADRGEAPEAVAPLVMFSPIGRRLDHDGVAGWAAGNGAVLLCGRYEGVDQRFVDAHVDVQLSLGDFVLSGGEIPAMALLDAVARLQPGVLNDAGSHQEDSFNAALDGLLDCPHYTRPESWQGQAVPAALLSGHHAQIERWRRDQRLAVTARHRPDLVEAARVAGRLDRADEAVLAKLNGLL | Specifically methylates guanosine-37 in various tRNAs. | A1TND2 |
Q97N21 | SYS2_CLOAB | Seryl-tRNA(Ser/Sec) synthetase 2 | Clostridium | MLDLDLIRNDTEKVKKALLKKIDNVDFTELLKLDDERRKLIHEVEVLKNKKNEASKQISNIKSQGGKVDESFFKDIKEISNKISELETSLEPIKGKMDTFLEALPNIPDEDVLPGGKENNKVVHVYGEKPQFEFEPKDHVELSNIHDLIDYKRGTKLSGNGFWIYKGYGAILEWALLNYFIEEHIKDGYEFILPPHILNYECGRTAGQFPKFKDEVFKVGSNGEGEGMQFILPTAETALVNLHRDEILKEDELPKKYFAYTPCYRVEAGSYRASERGMIRGHQFNKIEMFQYTKPEDSDAALEELIGKAEKLVKGLGLHY... | Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec). | Q97N21 |
Q24U39 | PLSX_DESHY | Phosphate-acyl-ACP acyltransferase | Desulfitobacterium | MMRIAVDAMGGDHAPAEIVKGALRSIEQFDIEVILVGQPERIKEFLPQGEVPARVRIKEATEVVEMDEHPAQAVRRKKDSSIVVATRLVKEGEADALVSAGSTGAQMAASLLGLGRIKGIDRPAIVTVLPTLEGGKLLLDVGANPDAKPEHLVQYAMMGSIYAESILGIQNPKVGLLNIGTEETKGNELTQATYPLLQKAPLNFIGNVEGRAIPYGQAADVVVCEGFVGNVVLKTTEGLAGALFQLIKEKITATPLRKLGALAIKPGLKEIAKMMDYAEYGGAPLLGVHGISIISHGSSNEKAIFNAIRVAKECVESGFI... | Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA. | Q24U39 |
B1VAA9 | TRMD_PHYAS | tRNA [GM37] methyltransferase | 16SrXII (Stolbur group) | MIIEIVTIFPLFFKSFCDNSIIKRALNQQKVQIKIHDLRKYSVNKHQQVDDCVYGGGVGMLLSFPPFFDCLQEIKTPQSKVILLSPQGKIFDQVQANNYASNTPHLIILCGNYEGVDARILKYVDQEISIGDYVLTGGEIAATVVVDAIVRLIPGVIKHESAFSDSHQQGLLKFPQYTRPQIYQNQEVPSVLLSGNHAQIENWRQKESLKITLQKRPDLLINKKLSSKEKVILEEIKQELKNNS | Specifically methylates guanosine-37 in various tRNAs. | B1VAA9 |
Q1LSS2 | RSMA_BAUCH | S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase | Candidatus Baumannia | MYNYFYQGHLVRKCLGQHFLHDQNIIESIVAVIHPLPSQALVEIGPGLGALTKYVAKYVKTITVIELDHNLVAYLANHPILQHKLNILSQDVMKVNFSDLAKKLSQPLRIFGNLPYNISIALMFNLFRHIHMIRDMHFMLQKEVVSRLLAKPNNKNYGKLSVIAQHYCQIDLVLDVPPESFRPVPQVDSAVVRLVPYVIPPYPVKDINKLYLLTSLAFQQRRKTIRNSLRNLFSVEQLLTQGIISTLRAENLSVEQYCCLASTLAECLPKK | Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits. | Q1LSS2 |
B7K1H5 | SYP_RIPO1 | Prolyl-tRNA synthetase | Rippkaea orientalis | MRLSQMLFVTLREDPAEAEIPSHKLLLRAGYIRRIGSGIYAYLPLMWRVLQKVSQIVREEMNAAGAQECLLPQLQPAELWRESGRWETYTKAEGIMFSLIDRRDTELGLGPTHEEVITTIAKEMIRSYRQLPVNLYQIQSKFRDEIRPRFGLMRGREFIMKDAYSFHASEDSLKETYQAMDQAYRNMITRCGLEFRAVQADSGAIGGSASQEFMILAEAGEDEVLYTEDGKYAANVEKAVSLPPDAELSPFTTPEKRETPNTNTIEKLCQFLQCSATAIVKNVLYQAVYDNGKTVLVLVSIRGDQDVNDVKLTNELVRLA... | Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two addit... | B7K1H5 |
Q4FRL9 | PYRF_PSYA2 | OMP decarboxylase | Psychrobacter | MNNAINSPVIVALDNMTKNASLALADQLDPALCRLKVGKELYTRCGPEIVKALHQRQFEVFLDLKFHDIPNTTAQAVLAAAELGIWMVNVHASAGLEAMALAKQRLLDSDFDTLLIAVTVLTSMDNEALMQTGITDGLDAQVSRLAQLTKQAGLDGVVCSAQEAKTLKALCGQDFKLITPGIRLLDDNADDQKRICTPKQALNDGSDYLVIGRSITQAADPAAKLQLILQSL | Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP). | Q4FRL9 |
P07267 | CARP_YEAST | Proteinase YSCA | Saccharomyces | MFSLKALLPLALLLVSANQVAAKVHKAKIYKHELSDEMKEVTFEQHLAHLGQKYLTQFEKANPEVVFSREHPFFTEGGHDVPLTNYLNAQYYTDITLGTPPQNFKVILDTGSSNLWVPSNECGSLACFLHSKYDHEASSSYKANGTEFAIQYGTGSLEGYISQDTLSIGDLTIPKQDFAEATSEPGLTFAFGKFDGILGLGYDTISVDKVVPPFYNAIQQDLLDEKRFAFYLGDTSKDTENGGEATFGGIDESKFKGDITWLPVRRKAYWEVKFEGIGLGDEYAELESHGAAIDTGTSLITLPSGLAEMINAEIGAKKGW... | Aspartyl protease implicated in the post-translational regulation of S.cerevisiae vacuolar proteinases. Acts on YSCB, on YSCY and on itself. | P07267 |
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