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
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A2CE36 | PURT_PROM3 | Phosphoribosylglycinamide formyltransferase 2 | Prochlorococcus | MTVLPKTLLLLGSGELGKEITIAAQRLGCHVIACDRYSGAPAMQVADQAEVLDMNNSEALTAIIRHHQPDVVIPEIEALAVNALAELENEGITVIPTARATAVTMNRDRIRDLASEELALLTPKFAYAGSAEELRHAAEPLGWPVVVKPVMSSSGKGQSVVSNPEGLRQAWQAAMAGSRGNSPRVIVEEFLHFDLEITLLTIRQEDGSTLFCEPIGHEQIGGDYQCSWQPAELSTEQLKQAQSMALSITENLGGVGLFGVEFFLCGNEVIFSELSPRPHDTGLVTLISQNLSEFELHLRAVLKLPIPTIQTADAAASRVILAKDNLSSISYKGVEKALSEIDTQILLFGKPNARPRRRMGVALAKGKSLEAVRSKADRAAASIQVIKGKGVT | Involved in the de novo purine biosynthesis. Catalyzes the transfer of formate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR). Formate is provided by PurU via hydrolysis of 10-formyl-tetrahydrofolate. | A2CE36 |
A4JI72 | LIPB_BURVG | Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase | Burkholderia cepacia complex | MSVSPVAIVSTPVAVSASPAGSPAQHDAPLTVRWRGTEAYQTSFDAMRAFTDARTAETPDEIWIVEHPPVYTLGQAGDPAHLLVADSGVPLVKVDRGGQITYHGPGQIVAYLLLDLRRRKLMVRTLVTRIEEAVIETLAAYNLASVRKAGAPGIYVASGVHGGAKIAALGLKIRNGCSYHGLSLNVKMDLRPFLAINPCGYAGLETVDMASLEVAADWNDVARTLVGRLIANLDGASAAADKPHALEHSND | Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate. | A4JI72 |
P32569 | MED17_YEAST | Suppressor of RNA polymerase B 4 | Saccharomyces | MTTEDPDSNHLSSETGIKLALDPNLITLALSSNPNSSLHSPTSDEPVPESAGKADTSIRLEGDELENKTKKDNDKNLKFLKNKDSLVSNPHEIYGSMPLEQLIPIILRQRGPGFKFVDLNEKELQNEIKQLGSDSSDGHNSEKKDTDGADENVQIGEDFMEVDYEDKDNPVDSRNETDHKTNENGETDDNIETVMTQEQFVKRRRDMLEHINLAMNESSLALEFVSLLLSSVKESTGMSSMSPFLRKVVKPSSLNSDKIPYVAPTKKEYIELDILNKGWKLQSLNESKDLLRASFNKLSSILQNEHDYWNKIMQSISNKDVIFKIRDRTSGQKLLAIKYGYEDSGSTYKHDRGIANIRNNIESQNLDLIPHSSSVFKGTDFVHSVKKFLRVRIFTKIESEDDYILSGESVMDRDSESEEAETKDIRKQIQLLKKIIFEKELMYQIKKECALLISYGVSIENENKVIIELPNEKFEIELLSLDDDSIVNHEQDLPKINDKRANLMLVMLRLLLVVIFKKTLRSRISSPHGLINLNVDDDILIIRPILGKVRFANYKLLLKKIIKDYVLDIVPGSSITETEVEREQPQENKNIDDENITKLNKEIRAFDKLLNIPRRELKINLPLTEHKSPNLSLMLESPNYCNALIHIKFSAGTEANAVSFDTTFSDFKEVEDFLHFIVAEYIQQKKV | Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and serves for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. The Mediator complex unfolds to an extended conformation and partially surrounds RNA polymerase II, specifically interacting with the unphosphorylated form of the C-terminal domain (CTD) of RNA polymerase II. The Mediator complex dissociates from the RNA polymerase II holoenzyme and stays at the promoter when transcriptional elongation begins. | P32569 |
P55342 | BSHC_BACSU | Putative cysteine ligase BshC | Bacillus | MQLTELSIKNQNVFVQHYIDGKEEMSSFFDYSIHHKDMWRERLEDLSSRFFAREELAAYLTSYHNKFGSSAMQSAIEKLKDPSSAAVVGGQQAGLLTGPLYTIHKIISIIVLAKQQEKELQVPVIPIFWVAGEDHDLDEINFVHTSEENGPVKKKLPQSYWKKSSAASTSLDQEKCAAWIDDVFAAFEETDHTNTLLDNVKRCLRESVTFTDFFELLIADLFQEEGLVLLNSGDPGIKKLETAMFQKILRENDELARAVSDQQAFMRQAGYKPIIESGKEQANLFYEYEDERFLIEKDNGRFVIKELDLGWTRDELHTHMEEHPERFSNNVVTRPLMQEFLIPTLAFIAGPGEINYWGELKQAFAVMGFKMPPVMPRLNITILERHIEKKLAERNISLQDAIERGTENQRETYFERQIPEEFTAVMDQAKSQIEAIHKTVRQEALKVDQSLEPLLLKNAAFIQDQLQFLERTVMKRIEEKEGYVLKDYERIQNSIKPLLAPQERIWNIMYYLNRYGPKFFTTFKNLPFSFQNQHQVVKL | Involved in bacillithiol (BSH) biosynthesis. May catalyze the last step of the pathway, the addition of cysteine to glucosamine malate (GlcN-Mal) to generate BSH. | P55342 |
Q2U5K2 | DRE2_ASPOR | Anamorsin homolog | Aspergillus subgen. Circumdati | MSITIDTSVDIDLPTPPQSNGSQKRNLLLAPPSVAAHEEKLRDVFSTFDRSSTDLQMFDRLSAGFVSLPPNTYDLVLVLTDAQSDEAVRLLTRDVYTALVPAMKAGARLQLQQGSLGASEGLEAILAGLVEKDGGFEKPVQEAAVPLKLGGRKKKDKTNGVNGVQNGVATNGASTNGVGMFDPAQNNDDELIDEDALLSDDDLKRPLPRPQNCVPETAKKRRRPCKDCTCGLASQLEEEDRAREAKAAQDLNILKLNTDDLNDELDFTVQGKTSSCNSCSLGDAFRCSSCPYIGLPPFKPGEEVKIMNDMVQL | Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the scaffold complex cfd1-nbp35. Electrons are transferred to dre2 from NADPH via the FAD- and FMN-containing protein tah18. Tah18-dre2 are also required for the assembly of the diferric tyrosyl radical cofactor of ribonucleotide reductase (RNR), probably by providing electrons for reduction during radical cofactor maturation in the catalytic small subunit rnr2. | Q2U5K2 |
A8L1A5 | MSHB_FRASN | N-acetyl-1-D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside deacetylase | unclassified Frankia | MTQSAETVLPPRRVLFVHAHPDDEVISTGVTMASYAARPDTHVTLVTCTLGEVGEVLVPELINLRSDLGDQLGGYRIGELDRSCAELGVTDHRFLGGAGRWRDSGMIDTPANDDPRCLWRADLDEASAALVQVVREVRPQVLVTYDENGAYGHPDHIRAHDVSVRAFADAANPDFAPEAGQPWQISKFYETATPKSFVQAGIEYFRESGGESPFGPAESADDIPLAVPDELITTEIQADEYLPAKVAAMRAHRTQMAVDGFFFALADGIGKRAWAAEHFVLTRGERGPGTEPGAHETDLFAGLPL | Catalyzes the deacetylation of 1D-myo-inositol 2-acetamido-2-deoxy-alpha-D-glucopyranoside (GlcNAc-Ins) in the mycothiol biosynthesis pathway. | A8L1A5 |
P66373 | RS12_LISIN | 30S ribosomal protein S12 | Listeria | MPTINQLVRKPRQSKIKKSTSPALNKGLNSFKRELTDVNSPQKRGVCTRVGTMTPKKPNSALRKYARVRLSNGIEVTAYIPGIGHNLQEHSVVLIRGGRVKDLPGVRYHIVRGALDTAGVENRGQSRSKYGTKKPKK | Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S subunit contacting proteins on the other side and probably holding the rRNA structure together. The combined cluster of proteins S8, S12 and S17 appears to hold together the shoulder and platform of the 30S subunit. | P66373 |
A4X4W1 | MIAA_SALTO | Isopentenyl-diphosphate:tRNA isopentenyltransferase | Salinispora | MSAVDAAAGAADGAHLAAGTVVGVVGPTAAGKSALSVALAHALDGEVVNADSMQLYRGLDIGTAKLTTDERAGVPHHLLDIWPVTEPASVAEYQRLARAAVDDILARGRVPLLVGGSGLYLRAVLERFEFPGTDPVLRQRLEAELAQAGPAALHERLRAVDPDAAANILPGNGRRIVRALEVVELTGAPFTAALPDPSPYYRSVQVGVDLDTARLDERIALRVDRMWADGLVAETRLLADQGLAEGRTASRALGYQQVLRFLAGELTESEAYQETIRATRRFVRRQRSWFRRDPRITWLDSAGSGLVAEALRVVRPAAR | 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). | A4X4W1 |
Q8XDZ3 | ARNA_ECO57 | UDP-glucuronic acid dehydrogenase | Escherichia | MKTVVFAYHDMGCLGIEALLAAGYEISAIFTHTDNPGEKAFYGSVARLAAERGIPVYAPDNVNHPLWVERIAQLSPEVIFSFYYRHLICDEILQLAPAGAFNLHGSLLPKYRGRAPLNWVLVNGETETGVTLHRMVKRADAGAIVAQLRVAIAPDDIAITLHHKLCHAARQLLEQTLPAIKHGNILEIAQRENEATCFGRRTPDDSFLEWHKPASVLHNMVRAVADPWPGAFSYVGNQKFTVWSSRVHPHASKAQPGSVISVAPLLIACGDGALEIVTGQAGDGITMQGSQLAQTLGLVQGSRLNSQPACTARRRTRVLILGVNGFIGNHLTERLLREDHYEVYGLDIGSDAISRFLNHPHFHFVEGDISIHSEWIEYHVKKCDVVLPLVAIATPIEYTRNPLRVFELDFEENLRIIRYCVKYRKRIIFPSTSEVYGMCSDKYFDEDHSNLIVGPVNKPRWIYSVSKQLLDRVIWAYGEKEGLQFTLFRPFNWMGPRLDNLNAARIGSSRAITQLILNLVEGSPIKLIDGGKQKRCFTDIRDGIEALYRIIENAGNRCDGEIINIGNPENEASIEELGEMLLASFEKHPLRHHFPPFAGFRVVESSSYYGKGYQDVEHRKPSIRNAHHCLDWEPKIDMQETIDETLDFFLRTVDLTDKPS | Bifunctional enzyme that catalyzes the oxidative decarboxylation of UDP-glucuronic acid (UDP-GlcUA) to UDP-4-keto-arabinose (UDP-Ara4O) and the addition of a formyl group to UDP-4-amino-4-deoxy-L-arabinose (UDP-L-Ara4N) to form UDP-L-4-formamido-arabinose (UDP-L-Ara4FN). The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides. | Q8XDZ3 |
Q2U0J9 | HEPE_ASPOR | Heptelidic acid biosynthesis cluster protein E | Aspergillus subgen. Circumdati | MDHFNLAGPESNTSITSLEWLGIKNSFTGSHWAHITGLSELHPTGFLCLIATLIIGIVHLTRGPKPTVLPVVNPPGTFELTANRVKKEWLVDARQIIRRGFEKFPGKPFNMIAADVGLTTVLPPEYASEIRNNPSLSFVAFMAHLFFSELPGFEPTREGMFDNDIGITVVHKYLTVNLARITEPLSREATAALKDIFTDNSEWHDANLKAINLALVARLSSRIFLGEELCRNEEWLKITVNYTVDVMKAAERLRRVPGPLRRIVHWFLPEAQKCRDEVKRAGKVIRPVLEKRRREKATMESEGKEALQYNDAIEWFEQMAKSQGTSYDPEVVQLFLSTVAIHTTSDLLTVVMADLARNPEIIEPLREEISSVLRDGGWKKTSLTDMKLLDSVLKESLRLKPIAVVSMRRVAMDHLKLSDGTFLPKGTKMAVSSHRMWDPDVYENPEQWDGFRYVNLRETPGQDKHAQFVSTSERHLGFGHGKHACPGRFFASSELKVALCHILMKYDFELAPGTVVQHRYSGASYYADPAIRVMLRRRNVALPSWFER | Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of heptelidic acid (HA), a sesquiterpene lactone that acts as an inhibitor of glyceraldehyde-3-phosphatedehydrogenase (GAPDH) and a growth inhibitor of the salt-tolerant lactic acid bacteria in soy sauce brewing. | Q2U0J9 |
Q9LZM3 | PPCS2_ARATH | Phosphopantothenoylcysteine synthetase 2 | Arabidopsis | MEDEISSFFESSPPQKNMEEILENLNEFIKLNSSSQGGRRIVCVTSGGTTVPLEQRCVRYIDNFSSGNRGAASTENFVKAGYAVIFLYRRGTCQPYCRSLPDDPFLECFEFSDKTNIQVHTSHLEAVKMAVMDQQTAVAEGSLLKLPFSTIYEYLQMLRLIAEALKDVGPCSMFYLAAAVSDFYVPWKSMTEHKIESGSGPLDIRLAQVPKMLSVLRSNWAPKAFCISFKLETDSKILMEKATKALRKYKVHAVVANELSTRKEEVVVVSSSGNVVVRRECDKPESFVEDNLIRLIVDRHSTYIKESHN | Catalyzes the first step in the biosynthesis of coenzyme A from vitamin B5, where cysteine is conjugated to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine. | Q9LZM3 |
Q70XV0 | ATPA_AMBTC | F-ATPase subunit alpha | Amborella | MVTIRADEISNIIRERIEQYNREVKIVNTGTVLQVGDGIARIHGLDEVMAGELVEFEESTIGIAPNLESNNVGVVLMGDGLMIQEGSSVKATGRIAQIPVSEAYLGRVINALAKPIDGRGEISSSESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILNQKGQNVICVYVAIGQKASSVAQVVTTFQEQGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRERHTLIIHDDPSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKSSSRLGEGSMTALPIVETQSGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKSKLELAQFAELEAFAQFASDLDKATQNQLARGQRLRELLKQSQAAPLAVEEQVVTIYTGANGYLDPLEIGQVKKFLVQLRTYLRTNKPQFQEIISSTRTFTEEAEAILKEAIQEQIELFLFQEQT | Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. | Q70XV0 |
Q6YR01 | KAD_ONYPE | Adenylate monophosphate kinase | Candidatus Phytoplasma asteris | MILILLGPPGIGKGTQASVLSDILKINHIATGDIFRKNFKENTELGILIKKIIAQGLLVPDDITNQMIADYLSKDIATKDFLLDGFPRNVLQARFLDDFFKNSHLFLTKVIYFNAGTQDLMKRIVGRRICPECGKVYHIENIPPKTPGICDKDQKTLIQREDDKPETFLKRLKVFNQETLPLVQYYREQNQLFEVDGMQNIDQVTKMILEVLETDRK | Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. | Q6YR01 |
B3QY23 | RS10_CHLT3 | 30S ribosomal protein S10 | Chloroherpeton | MAVQQKIRIKLKSYDHSLVDKWAEKIIEAVKQTDAIISGPIPLPTESQVFTVNRSPHVDKKSREQFMVASHKRLIEIINPSSKTIDLLMKLELPSGVDVEIKS | Involved in the binding of tRNA to the ribosomes. | B3QY23 |
Q5LNR0 | TRUA_RUEPO | tRNA-uridine isomerase I | Ruegeria | MPRYALKVEYLGTPFAGWQRQKDLPSVQGAIETALARLEPGPHTIAAAGRTDAGVHGLGQVAHCDLTRDWDPFRLSEALNYHLKPQPVAITAAARVAEDWHARFSATERQYLFRLLMRRAPATHDAGLVWQVGHRLDARAMQAAADLLLGRHDFTTFRSSICQAASPVKTLDELRVEAVESFSGPEIRFHVRARSFLHNQVRSFVGTLERVGAGAWAPEDVRSALEARDRAACGPVCPPQGLYLARVGYPEPVFAADRSAAS | Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs. | Q5LNR0 |
Q0I0Q6 | GPMI_SHESR | 2,3-bisphosphoglycerate-independent phosphoglycerate mutase | Shewanella | MTTTKRPIALLILDGWGYRENTHMNAIYHANTPVLDRLNAQYAHGLISGSGLDVGLPDGQMGNSEVGHINLGSGRIVYQELTRISKAIADHEFEQNPALCDAVDAAVKAGGAVHIMGLLSPGGVHSHEEHIEAMCRMAVARGATKVYLHAFLDGRDTPPRSAKGSLSHFDDLFTTLGHGRIASIIGRYFAMDRDNRWDRVSQAYDLITQGKAKFQYDNAVTALEAAYERNENDEFVSSSAITDSEGKVASLNDGDALIFMNFRADRARQITRSFINADFDGFERAVTPKVNFVTLTEYAADIKAPIAYPSENLVNTLGEVLQNRGRTQLRISETEKYAHVTFFFNGGKEEPFNGEDRILINSPKVATYDLQPEMSSTELTDKLVAAIESAQYDVIICNYPNGDMVGHTGNFDAAVKACEAVDACIGRVVDALAKVGGECIITADHGNAEQMTDETTGQAHTAHTSELVPFVFVGRDATIDEGGKLSDVAPTILHLMGETIPAEMTGKPLIHVKE | Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate. | Q0I0Q6 |
Q6LN63 | GLO2_PHOPR | Glyoxalase II | Photobacterium | MLTVQSIPAFNDNYIWLIHNSHNHCVVVDPGDATPVLKVLEEQSLTLDAILITHHHHDHIGGISELKRHYPNLNVVGPASEPIPGISQSVEDGDQVELFGERFMVLGVPGHTLGHVAYVGDGKLFCGDTLFSVGCGRLFEGTPAQMFQSLKKLAALPDETEIYCAHEYTSSNLAFALVAEQDNPHLQRYREDVSRMRAQGISTIPSTLRQEKLVNPFLRCEQPSIKKSVADKAFDDSDLETFAALRRWKDNF | Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid. | Q6LN63 |
B8CLH4 | MNMA_SHEPW | tRNA-specific 2-thiouridylase MnmA | Shewanella | MTSIDPTHLGKKVIVGMSGGVDSSVSAYLLMKQGYQVEGLFMKNWEEDDTDEYCAAADDLKDAQAVCDKLGIKLHTVNFASEYWDNVFEYFLAEYKAGRTPNPDIMCNKEIKFKAFLEFADEILDADYIAMGHYVRRRDIDGTSQMLRGVDGNKDQSYFLYTLSHEQVARSLFPVGELEKSEVRDIAKEMGLITHDKKDSTGICFIGERKFTDFLSTFLPAQPGNIETSEGEVIGQHQGLMYHTLGQRKGLGIGGLKNSSEDPWYVVEKDLVRNVLVVGQGGNHPRLMSNGLLANQLHWVDRKGPAEGAKITLKTRYRQHDVPCTVTYDSDDQIRVIFDEAVAAVTPGQSAVFYDGEICLGGGIIDVLIRD | Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34. | B8CLH4 |
A8YUJ1 | RF1_LACH4 | Peptide chain release factor 1 | Lactobacillus | MDKVMAQLEGLVAHYEELQEMMADPEVINDTKRYMEISKEEADLREVVQKYKKYKEDKKEIADNKEIIANETDSDLIEMAKEENAEIEKEIPELEDQIKILMLPKDPNDDKDIIMEIRGAAGGDEASLFAGDLLRMYEKYAERQNWKVSMIDSEPTEVGGYKRVAIMITGDKVYSKLKYENGAHRVQRIPVTESQGRVHTSTATVAVMPEYEQVDIDIDPKDIRVDVYRSSGAGGQHINKTSSAVRMTHLPTGIVVAMQDQRSQQQNREKAMQILKSRVYDYYESQNQAKYDAKRKNAIGTGDRSERIRTYNYPQNRVTDHRIGLTINKLDRVMNGELDEIIDALILYNQTKQLEELADQNA | Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA. | A8YUJ1 |
C0Q9X6 | RS7_DESAH | 30S ribosomal protein S7 | Desulforapulum | MARKKIVSGHLKNAISKDEHISVKFVNCIMRDGKKSVAEKVFKDAMELVEEKLGESSLKVFEKAIGNIRPSVEVKSRRVGGSTYQVPTEIKSSRQTALAFRWLLRFSRSRSEKGLSNKLAAELLDAYNERGGAVKKKEDTHKMAEANKAFAHFRW | One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center, probably blocks exit of the E-site tRNA. | C0Q9X6 |
Q494F8 | MNMG_BLOPB | Glucose-inhibited division protein A | Candidatus Blochmannia | MFYPIHFDVIVVGGGHAGTEAALASARMQCNTLLITHNIDTLGQMSCNPAVGGIGKGHLVKEIDAMGGSMAYAIDQSGIQFRVLNSSKGAAVRATRAQADKILYRQAIRSILEYQKFLLVIQASVEDLIVSGNKIVGVITPKLGMKFSGTSVVLTTGTFLNGKIHIGMNNFRGGRSGDSESSSLLSERLKELSFQISRLKTGTSPRVHTKGINFGSLRAQYSDDPIPVFSFIGSTKLHPTQVPCYITHTNNKTHEIVRSNLYQSPMYTGLIKGIAPRYCPSIEDKITRFSDRNAHQIFLEPEGLTTPEVYLNGISTSLPFCVQMQMIKSIQGLENACIIRPGYAIEYDFFDPRDLKLTLESKIISGLFFSGQINGTTGYEEAAAQGLLAGINAARFSKNKEGWYPRRDQAYLGVLVDDLCTHGTEEPYRMFTSRAEYRLSLREDNADLRLTEIARQLGLIDESRWKAFCCKKENIEKERQRLRNTYIFPYSSDVAQLNNFLKTPLTHETNGEDLLRRPEINYKKLSQLSTFSPSILDRQVFEQIEIQIKYEGYIRHQQEEIKRHIYNENTLLPTDIDFNIVSGLSQEVIDKLNNYKPYSIGQASRISGITPAAISNLLVWLKKQGLLEHNTC | NAD-binding protein involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34. | Q494F8 |
B9DTE2 | RS15_STRU0 | 30S ribosomal protein S15 | Streptococcus | MAISKEKKNEIIAQYARHEGDTGSVEVQVAVLTWEINHLNGHIKEHKKDHATYRGLMKKIGHRRNLLAYLRRTDVNRYRELIQSLGLRR | Forms an intersubunit bridge (bridge B4) with the 23S rRNA of the 50S subunit in the ribosome. | B9DTE2 |
P61629 | LYSC_PAPAN | 1,4-beta-N-acetylmuramidase C | Papio | MKAVIILGLVLLSVTVQGKIFERCELARTLKRLGLDGYRGISLANWVCLAKWESDYNTQATNYNPGDQSTDYGIFQINSHYWCNNGKTPGAVNACHISCNALLQDNIADAVTCAKRVVSDPQGIRAWVAWRNHCQNRDVSQYVQGCGV | 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. | P61629 |
B8HQE1 | DER_CYAP4 | GTP-binding protein EngA | unclassified Cyanothece | MTLPVVAIVGRPNVGKSTLVNRLTGERVAIVHDQPGVTRDRTYRPSFWQDRDFLVVDTGGLVFADDTEFLPLIRQQVVTALSEARVAILVVDGQQGITAADEEIAQWLRQQSLPVLVAVNKCESPQQGLAQGAEFWELGLGEPFPISAIHGNGTGELLDQVVSYLPPTDQQAGEEDIINVAIVGRPNVGKSSLLNAVVGEQRAIVSPISGTTRDAIDTLVERDGQRYRLIDTAGIRKQKNVDYGPEFFGINRAFKAIQRAEVVLLVLDALDGVTEQDQKLAGRIVDEGCACVIVVNKWDAVEKDSYTIYDYQHQVEQRLNFIGWSDHIFISAATGQRVEKIFERVHLAAEQHRRRVSTSVINEVLEDAVGWHSPPASRQGRQGKIYYGTQVSSQPPTIALFVNDPALFKDNYRKYIEGQFRKQLGFRGTPIRLLWRGKKVREAERKGVLVRDR | GTPase that plays an essential role in the late steps of ribosome biogenesis. | B8HQE1 |
A5U1F4 | EX7S_MYCTA | Exodeoxyribonuclease VII small subunit | Mycobacterium tuberculosis complex | MVCDPNGDDTGRTHATVPVSQLGYEACRDELMEVVRLLEQGGLDLDASLRLWERGEQLAKRCEEHLAGARQRVSDVLAGDEAQNG | Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides. | A5U1F4 |
Q8DMK8 | RL13_THEVB | 50S ribosomal protein L13 | Thermosynechococcus | MTSTVKTPLPAVDDLAPQWYVIDAADQRLGRLAAEIARILRGKNKAIYTPHMDTGDFVIVINAEKVTVTGKKRSQKLYRRHSGRPGGMKIETFDQLQARIPERIIEHAVKGMLPKNSLGRKLFTKLKVYAGPEHPHQAQKPQPLTINTIPGA | This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly. | Q8DMK8 |
A7GT14 | LEPA_BACCN | Ribosomal back-translocase LepA | Bacillus cereus group | MNKEERAKRQSKIRNFSIIAHIDHGKSTLADRILEKTNALTQREMKAQLLDSMDLERERGITIKLNAVQLTYKAKDGEEYILHLIDTPGHVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLEILPVINKIDLPSADPERVRQEVEDVIGLDASEAVLASAKAGIGIEEILEQIVEKVPAPDGDPEEPLQCMIFDSLYDPYRGVIAYIRVVNGTVKVGDKVRMMATGKEFEVTEVGVFTPKTTQRDELTVGDVGFLAASIKNVGDTRVGDTITHAKRPAAEPLPGYRKLNPMVFCGLYPIDTARYNDLREALEKLQLNDSALEFEPETSQALGFGFRCGFLGLLHMEIIQERIEREFKIDLITTAPSVIYKVYLTNGEEIVVDNPSNMPDPQSIDRVEEPYVKASIMVPNDYVGAVMEICQGKRGTFIDMQYLDETRVTLTYEIPLSEIVYDFFDQLKSNTKGYASFDYELIGYQVSKLVKMDILLNGEQVDALSFIVHRDSAYDRGKVIVEKLKELIPRQQFEVPIQAAIGNKIVARSTIKAMRKNVLAKCYGGDISRKRKLLEKQKEGKKRMKSVGSVEVPQEAFMAVLRMDDDK | Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP-dependent manner. | A7GT14 |
A1USY3 | SYP_BARBK | Prolyl-tRNA synthetase | Bartonella | MRLSQYFLPILKENPKEAEIISHCLMLRAGIIRQQTSGIYSWLPLGKKVLDKVCTIIREEQERAGALEISMPTIQSADLWRESGRYDDYGLEMLRIKDRQERDLLYGPTNEEMVTDIFRSYVRSYKDLPLNLYQIQWKFRDEIRPRFGVMRSREFLMKDGYSFDLDYESAKTSYNRMFIAYLRTFSRIGLKVIPMRADTGPIGGELSHEFIILAKTGESAVFCDKRFLEMTAPPVSVDFTDNVVLTDIVKQWTALYATTEEMHNAEEWAQICKSNQLSARGIEVGHIFYFGTKYSEPMGAKVMGRDGKEYPVFMGSYGIGPSRLVAAAIEASHDENGIIWPKPITPFDFGIINTKSDNAKCYGMCETLYQGLVNAGFDPLLDDRNERPGAKFATMDLIGLPTQIIVGPKSAAQDEVEIKDRKTGTKEVLTVEAALNRLSAM | 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). | A1USY3 |
Q58767 | UPPS_METJA | Undecaprenyl pyrophosphate synthase | Methanocaldococcus | MGILGKIKNKLKSIGKRVIIDFYRFLDNSGVLKIYEKILEEAIDKDNLPKHVAIIMDGNRRAAEIYGKDRYYGHYLGAEKVREVLRWARDLGINVVTLYAFSTENFRRPKEEVDKLMELFEKKFYEIADDEEIHRYEVRVRAIGRINLLPKNVQKAIKYAEERTKNYNKFFVNIAIAYGGQQEIIDAVKKIAEKVKRGEIEPEDIDKELIDKHLYTANLPFPNPDLIIRTSGEERISNFLIWQSSYSELYFCDIYWPLFRRVDFLRAVRDYQRRQRRFGK | Catalyzes the sequential condensation of isopentenyl diphosphate (IPP) with geranylgeranyl diphosphate (GGPP) to yield (2Z,6Z,10Z,14Z,18Z,22Z,26Z,30E,34E,38E)-undecaprenyl diphosphate (tritrans,heptacis-UPP). It is probably the precursor of glycosyl carrier lipids. | Q58767 |
Q9L7L3 | GYRB_MYCPA | DNA gyrase subunit B | Mycobacterium avium complex (MAC) | MAAQKKKAQDEYGASAITVLEGLEAVRKRPGMYIGSTGERGLHHLIWEVVDNSVDEAMAGYADRVDVRILDDGSVEVADNGRGIPVAMHATGAPTVDVVMTQLHAGGKFGGENSGYNVSGGLHGVGVSVVNALSTRLEVNIARDGYEWSQYYDHAVPGTLKQGEATKRTGTTIRFWADPDIFETTEYDFETVARRLQEMAFLNKGLTINLTDERVTNEEVVDEVVSDTADAPKSAQEKAAESAAPHKVKHRTFHYPGGLVDFVKHINRTKNPIHQSIIDFGGKGPGHEVEIAMQWNGGYSESVHTFANTINTHEGGTHEEGFRSALTSVVNKYAKDKKLLKDKDPNLTGDDIREGLAAVISVKVSEPQFEGQTKTKLGNTEVKSFVQKVCNEQLTHWFEANPADAKVIVNKAVSSAQARIAARKARELVRRKSATDLGGLPGKLADCRSTDPRKSELYVVEGDSAGGSAKSGRDSMFQAILPLRGKIINVEKARIDRVLKNTEVQAIITALGTGIHDEFDITKLRYHKIVLMADADVDGQHISTLLLTLLFRFMRPLIEHGHVFLAQPPLYKLKWQRSDPEFAYSDRERDGLLEAGLKAGKKINKDDGIQRYKGLGEMDAKELWETTMDPTVRVLRQVTLDDAAAADELFSILMGEDVDARRSFITRNAKDVRFLDV | A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner. | Q9L7L3 |
Q8G197 | SYP_BRUSU | Prolyl-tRNA synthetase | Brucella | MRLSRYFLPILKENPKEAEIVSHRLMLRSGMIRQQSAGIYSWLPIGLKVLNKVCTIIREEQNRAGANEILMPTIQSADLWRESGRYGAYGKEMLRIQDRQEREMLFGPTNEEMVTDIFRSYVRSYKDLPLNLYHIQWKFRDEVRPRFGVMRSREFLMKDAYSFDLDYEGAKMAYYRMFVSYLRTFARVGLQAIPMRADTGPIGGDLSHEFIILAETGESQVYCDRAYLDLAVPGADTDFRNDAQLTDIVTRWTTPYAATDEMHDEADWAKVKPESQVSARGIEVGHIFHFGTKYSEPMGAKVQGPDGKEHLVSMGSYGIGPSRLVAAAIEASHDDAGIIWPKAIAPFGAGIVNMKPGDEGCDGVSEKLYEALTNAGVDPLLDDKDERPGAKFATMDLIGLPTQVIVGPRGVAAGEVEVKDRKMGERQSLGIEAAINMLTAQA | 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). | Q8G197 |
Q493K4 | RS19_BLOPB | 30S ribosomal protein S19 | Candidatus Blochmannia | MSRSIKKGPFIDLHLLKKVEKAIETGDKKPIRTWSRRSTIFPRMIGLTVAVHNGRQHIPIFISDEMVGHKLGEFAPTRTYRGHSVDKKIKKHY | Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA. | Q493K4 |
A0A443HK81 | VDTA1_BYSSP | Viriditoxin biosynthesis cluster protein A | Paecilomyces | MAQKLRFYLFGDQTYDYDEQLRALLTSHDPVVRSFLERAYYTLRAEVARIPNGYQARISRFSSIAELLSQRREHGVDASLEQALTVVYQLASFMRLHSERSLSYPSADDAHCLGLCTGALSAAAVSSSRSLSELLPAAIETVILAFRTGLHASDSGRRIEESSAAAKCWSISLQGLEGHVARKLLEEWSNKKRLPPMSRPYISAYASGGVTISGPPSVLAELRNTPGLSKLRAKDIPIHAPYHSSAIFNQCDVETILSSALIDLASRATHVPILSTGTGRLVWAGTLPAAIQSALQDVLLRPISWENMSCGISTCLQSIDPSEVEVIPIATLAGPLLCRSVQVAKSQIPATIDPKNDVMNEAQSQIAEAMDRAKIAIVGMSGRFPGAENVDSLWELLMAGRDMCKEVPPTRWNVDTHVDPTGKRKNTSKIRWGCWLDNPDMFDARFFNMSPREAPQVDPAQRIALITAYEAIEQAGIVPGRTPSTQEDRVGVFFGTTSNDWCESNSGQDIDTYYIPGANRAFIPGRINYVFKFSGPSYSIDTACSSSLSALHVACNALWHGDIDTAIAGGTNVLTNPDMTAGLDRGHFLSATGNCKTFDDTADGYCRGEGVATVVLKRMDDAIADKDPILGVIRGVYTNHSAEAESITRPHVGAQKAIFQHVLNHSGIRPQDISYIEMHGTGTQAGDMREMTSVLDTFSPQYPGAIQREKPLYLGAVKSNIGHGESVSGVTALVKVIMMMQNNTIPPHRGVHTRLNRRFPSNLDERNVHIAFQATEWPRGQTPRRAFINNFSAAGGNSSVLVEDPPLILKEEGADPRSSHVIAVSAKSPSALRKNLESMRRYAMSEHTEKSLCELSYTTTARRIHHSHRLMFAGSSLEDILREMESKLAIKEPFSPCAPLQSVIFTFTGQGAQYPGMGQVFFNNFSVFRSDLCRLDDLAQKLGFPTFLPIFSASTHARLEGFTPTVVQLANTCMQLALTRLWVSWGIRPSAVVGHSIGEYAALNTAGVLSDADTVYLVGKRAQLLEEKCNRGSHTMLAALASFEKVSRLLDSAPCEVACINGPEEIVLAGPRSHMTDIQKILVAHSIRCTMLQVPFAFHSSQVDPILQDFQSAIEGVTFHKPTIPVISPLLGDFVTETGTFNPNYLARHCREPVNILQALRQASTMNLVHDSSVVMEFGPHPVVSGMVKSTLGNSIKALPTLQRNRNTWEVLTESVSTLYCMGFDINWTEYHRDFPSSQRVLRLPSYSWDLKSYWIPYRNDWTLYKGDIVPESSIALPTHQNKPHSTSPKQQAPTPILETTTLHRIVDEKSTEGTFSITCESDVSRPDLSPLVQGHKVEGIGLCTPSVYADIGFTLGNYLLDRFPTRFGPDTKVVDVTDMVIEKALMPLNAGPQLLRVTASLIWSEKEASVRFYSVDENHTETVQHSHCRIKFSDRSTYQAYQEQISAVKARMFEMKTNSSSGRTYRFNGPMAYNMVQALAEFHPDYRCIDETILDNETLEAACTVSFGNVKKEGVFHTHPGYIDGLTQSGGFVMNANDKTNLGVEVFVNHGWDSFQLYEPVTDDRSYQTHVRMRPAESNQWKGDVVVLSGENLVACVRGLTIQGVPRRVLRYILQSSAKTTQTATSSVPAPSQAPVMVPQIVQVPKAKPISQISGTLTEALRIICEQSGVPLAELTDDATFANIGVDSLLALTITSAFVEELDLDVDSSLFMDYPTVADLKRFFDKINTQHAPAPAPVSDAPKQLQPSSSPVASATPSAPIHGRSKFESVLNILTEESGVEMAGLPDSTALADIGIDSLLSLVVTSRLNDELELDVSSEDFNDCLTIRDLKAHFMSKNSDNGSSAVLTPQPSRDSALPERTRPRVADTSDEEDAPVSANEFTTSARSTSKYMAVLNIISEESGMAIEDFTDNVMFADIGIDSLLSLVIGGRIREELSFDLEVDSLFVDYPDVKGLRSFFGFESNKTATNPTASQSSSSISSGTSVFDTSPSPTDLDILTPESSLSQEEFEQPLTIATKPLPPATSVTLQGLPSKAHKILFLFPDGSGSATSYAKLPRLGADVAIIGLNSPYLMDGANMTCTFDELVTLYLTEIQRRQPAGPYHLGGWSAGGILAYRAAQILQKAAANPQKPVVESLLLLDSPPPTGLGKLPKHFFDYCDQIGIFGQGTAKAPEWLITHFQGTNSVLHEYHATPFSFGTAPRTGIIWASQTVFETRAVAPPPVRPDDTEDMKFLTERRTDFSAGSWGHMFPGTEVLIETAYGADHFSLLVSLLFRD | Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of viriditoxin, one of the 'classical' secondary metabolites produced by fungi and that has antibacterial activity . The first step is performed by the polyketide synthase VdtA which condenses one acetyl-CoA and 6 malonyl-CoA units to form the heptaketide monomer backbone of viriditoxin . The product of VdtA is then O-methylated on C7 by the O-methyltransferase VdtC . The O-methyl group is important for the stereoselective coupling of the monomers at the final step of viriditoxin biosynthesis . The short-chain dehydrogenase/reductase VdtF then acts as a stereospecific reductase converting the pyrone to dihydropyrone via the reduction of the C3-C4 double bond . The FAD-binding monooxygenase VdtE then converts the ketone group into a methyl-ester group to yield semi-viriditoxin . Finally, the laccase VdtB is involved in dimerization of 2 semi-viriditoxin molecules to yield the final viriditoxin . VdtB is responsible for the regioselective 6,6'-coupling of semi-viriditoxin, which yields (M)-viriditoxin and (P)-viriditoxin at a ratio of 1:2 . The non-catalytic carboxylesterase-like protein VdtD affects the stereochemistical outcome of the coupling . The highly reducing polyketide synthase VdtX is not involved in viriditoxin synthesis, but might possibly play a role in the production of additional metabolites not identified yet . | A0A443HK81 |
Q8NEA4 | FBX36_HUMAN | F-box only protein 36 | Homo | MASWLPETLFETVGQGPPPSKDYYQLLVTRSQVIFRWWKISLRSEYRSTKPGEAKETHEDFLENSHLQGQTALIFGARILDYVINLCKGKFDFLERLSDDLLLTIISYLDLEDIARLCQTSHRFAKLCMSDKLWEQIVQSTCDTITPDVRALAEDTGWRQLFFTNKLQLQRQLRKRKQKYGNLREKQP | Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. | Q8NEA4 |
P93438 | METK2_ORYSJ | Methionine adenosyltransferase 2 | Oryza sativa | MAAETFLFTSESVNEGHPDKLCDQVSDAVLDACLAQDPDSKVACETCTKTNMVMVFGEITTKATVDYEKIVRDTCRGIGFVSDDVGLDADRCKVLVNIEQQSPDIAQGVHGHFTKRPEEIGAGDQGHMFGYATDETPELMPLSHVLATKLGARLTEVRKNGTCAWLRPDGKTQVTVEYLNDAGAMVPVRVHTVLISTQHDETVTNDEIAADLKEHVIKPVIPDKYLDEKTIFHLNPSGRFVIGGPHGDAGLTGRKIIIDTYGGWGAHGGGAFSGKDPTKVDRSGAYIARQAAKSIVASGLARRCIVQVSYAIGVPEPLSVFVDSYGTGKIPDKEILKIVKENFDFRPGMMTINLDLKRGGNRFIKTAAYGHFGREDPDFTWEVVKPLKYEKASS | Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The reaction comprises two steps that are both catalyzed by the same enzyme: formation of S-adenosylmethionine (AdoMet) and triphosphate, and subsequent hydrolysis of the triphosphate. | P93438 |
Q5LXA4 | GREA_RUEPO | Transcript cleavage factor GreA | Ruegeria | MEKIPMTPSGFAALEAELKQLKSVERPAIIKAIAEAREHGDLSENAEYHSAREKQSFIEGRIKELEGVLSLADVIDPTKLSGAIKFGARVTLVDEDTDEEKTWQIVGEHEANIEKGLLNIKSPIARALIGKDEGDSVEVKTPGGQKSYEILSIEYS | 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 factors such as GreA or GreB allows the resumption of elongation from the new 3'terminus. GreA releases sequences of 2 to 3 nucleotides. | Q5LXA4 |
Q66V57 | TAC1_ORYSI | Protein SPREADING TYPE OF KASALATH | Oryza sativa | MALKVFNWLNRKKHSNVEYCTINENKAMEEKEDSLRASVTEQDTEALLLRDVLINGILAIGTLGHNVNSLCPESCIEQDEPIIMCDEKVEQEKCEEEKAEAKQDTPVTAPSEPASALEPAKMHSSSMKEDNFMCFVKEEILMHGMEVEDVPNIQERPLLMLEKVEKVRTTLADLFAAEAFSSSDAEDKCYPKIVIVAGASTSKPTSCMEKMHHKKPTKPTSKPLKATRKLSRVMRKMLGKKIHPEQLNGRSNAEGPVTA | Involved in the regulation of tiller growth angle (Ref.1). Promotes horizontal shoot growth (Ref.1). TAC1 and LAZY1 play opposite functions in the regulation of tiller growth angle (Probable). | Q66V57 |
A4WX64 | LEXA_CERS5 | LexA repressor | Cereibacter | MLTRKQMELLDFIKTRMDRDGVPPSFDEMKDALDLRSKSGIHRLITALEERGFIRRLAHRARAIEIVKLPEAMERAGFAPRVIEGDRTEPPRGARPVETANALDLPLMGRIAAGLPIEAITDGAQSVTVPSMMLSGRGQHYALEVRGDSMIEAGINDGDIVVIREQQTADNGDIVVALVADHEATLKRFRRRGGMIALEPANASYETQVYPDHMVKVQGRLVGLIRSY | Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair. | A4WX64 |
Q5NLR1 | CLPS_ZYMMO | ATP-dependent Clp protease adapter protein ClpS | Zymomonas | MSGDKDFDKDSDVTVITRTTPQTKKPQPYKVLMLNDDYTPMEFVVLCLQRFFRMGIEDATKVMLQVHQRGVGICGVFTYEVAETKVNQVVDFARQHQHPLQCTLEKA | Involved in the modulation of the specificity of the ClpAP-mediated ATP-dependent protein degradation. | Q5NLR1 |
A5N2U5 | DPO4_CLOK5 | DNA polymerase IV | Clostridium | MHRVIFLVDMNAFFISCESTRHPEIIGKPAAVAGDPKNRSGIILTANYEARKFGVKTTMVLHKVLKLCPNIIIIPPDHCFYKQKSKEVMGILSKYTPVIEKNSIDEAWLDMTGCERIFGRSYQTAECIMKHINSELGLDCSIGISENKFLAKMASQMKKPLGITKLWKKDIELKLWPLPVEFMNGIGKQTARKLREMKIKTIGELANFDRRYLIKKLGKVGAEIHQFANGIDVSPVTPHSHKDVKSIGKSITLAHDISDIESAKVILMELSDKVGMTARKYNKKGHTVQINIKYSNFQSITRQRTITETYLVKEIYSAGIEMLEKNWNERLPVRLLGISLSGFSKYNEDEQISMFNMLEIDNEKSSVRKIDKIEAAIDSIRKKYGDSIIKSGSLIKKSKN | Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII. | A5N2U5 |
A7HDU6 | TRMFO_ANADF | Folate-dependent tRNA(M-5-U54)-methyltransferase | unclassified Anaeromyxobacter | MGRERVTVVGGGLAGSEAAWRLAQGGVEVELVEMKPGRRSPAHVLDGLAELVCSNSLRSDNPHNAVGLLHEELRRLGSLVLSAADATRVPAGDALAVDRERFSALVTGRLRGHPLVRVRQEELLRLPEGPGLTLVATGPLTGDALAADVAALAGGRLHFYDAIAPIVAADSIDMSIAYARSRYGKGSGDDYLNLPFDEGQYRAFVGALLAGEKVAAHDFEEPRYFEGCLPIEVMAERGADVLAYGPMKPVGLEDPRTGRRPFAVVQLRREDVAGTAYNLVGFQTRLTWTEQRRILREYVPGLAGAEFVRLGQIHRNTFLEAPRVLAPDLSARERPHLFFAGQITGVEGYVESAACGHLAARAMLDRLAGRPFLPPPAATALGALHRHLTGEAHPPGYDYQPTNVVFALFPPLTGRHRGKAARKDAHAERARKEIAPWIDPWTHTARGAAAP | Catalyzes the folate-dependent formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs. | A7HDU6 |
Q93GT6 | CH60_TETHA | Chaperonin-60 | Tetragenococcus | MAKDIKFSEDARRSMLNGVSKLADTVKVTLGPRGRNVVLEKSYGSPLITNDGVTIAKEIELENRFENMGAQLVSEVASKTNDIAGDGTTTATVLAQSIVSEGLKNVTSGANPLGIRRGIEQATQKAVEELQNISTPVESKEAIVQVGEVSSGSKQVGQYIADAMDKVGNDGVITIEDSQGIDTELDVVEGMQFDRGYLSQYMVTDNEKMEADLDSPYILITDKKISNIQDILPLLEQVVQESKPLLIIADDIDGEALPTLVLNKIRGTFNVVATKAPGFGDRRKAMLEDIAVLTGATVITEDLGLELKDATMDSLGKANKVTVDKDNTTIVEGAGDSTAIEDRVQLIKNQVAETTSDFDREKLQERLAKLAGGVAVIKVGAATETEQKELKLRIEDALNAARAGVEEGMVSGGGTALVNVINKVAELDADDDAITGVNIVLRALEEPVRQISENAGFEGSVIIEKLKSEKLGIGFNAATGQWVNMVDAGIVDPTKVVRSALQNAASISALLLSTEAVIADRPDESGNDAGAGAQGMDPSMMGGGMM | 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. | Q93GT6 |
O95013 | O4F21_HUMAN | Olfactory receptor 4F21 | Homo | MDGENHSVVSEFLFLGLTHSWEIQLLLLVFSSVLYVASITGNIFIVFSVTTDPHLHSPMYFLLASLSFIDLGACSVTSPKMIYDLFRKRKVISFGGCIAQIFFIHVIGGVEMVLLIAMAFDRYVALCKPLHYLTIMSPRMCLSFLAVAWTLGVSHSLFQLAFLVNLAFCGPNVLDSFYCDLPRLLRLACTDTYRLQFMVTVNSGFICVGTFFILLISYVFILFTVWKHSSGGSSKALSTLSAHSTVVLLFFGPPMFVYTRPHPNSQMDKFLAIFDAVLTPFLNPVVYTFRNKEMKAAIKRVCKQLVIYKKIS | Odorant receptor. | O95013 |
P92668 | NU4M_OSPRO | NADH dehydrogenase subunit 4 | Osphranter | MLKILVPTIMLIPLTWYSKKQWVWINPTAHSFLISIASLTLLYHSTDLGYSYSSSFYMDSLSGPLLVLSCWLLPLMMIASQNHLMKEPLNRKKTFLTTLIILQTSLIMAFSSSELIMFYIMFEATLIPTLIIITRWGNQNERLNAGLYFLFYTLTGSLPLLVALLYLHSKIGTLHILTLIMNPKPMELSMPNSILWYACTVAFMVKMPMYGLHLWLPKAHVEAPIAGSMVLAAILLKLGGYGIMRITILTQPITAHVYYPFIVLSLWGMIMTSSICLRQTDLKSLIAYSSVSHMGLVIVAALMQSTLSFMGATALMIAHGLTSSMLFCLANTNYERIHSRTMILARGLQLILPLMCTWWLLASLANLALPPTINLLGELAVIISSFSWSHFSIILLGANTVITALYSLHMLITSQRGKFTHHLYPMKPSFTREHILMMLHMIPLLIISMNPKFILGITY | Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity and assembly of complex I. | P92668 |
Q6FW79 | MSC6_CANGA | Meiotic sister-chromatid recombination protein 6, mitochondrial | Nakaseomyces/Candida clade | MLRINQRLLVRSLRDAQYQYLKSTALRFLSSSTQSNVETTPRRSGRLFELNKEYTGKLAQPDGKANIESLYNEFKNDLDKISEFSNGRQGMAPKYGRSRSLSFINRLFQSITNAKNTSSLDPYVVLEQLSKYNLIGPAQYEMILRYYLLVKDAPKDVISLWVKYLEQFTTSNENLMAYTTIAYLKLPDMNEPDCSMLQQILQTERFHTDIPFGRIISIVEQNEVLKRDQELSNRFAYLLNLYATQNKTWFINQLDICYTESRLRSFYNIYSAQRDINNCDIEIITKFMEQFNKLNANSSFPMQVFNEYKDKLSDADGFKLKLGLLDIVSKYPAPSKIQKLQRLLAVWNSYLKPEFGKVGIDASLAYASLIKALNTSGNIEELQNIWEKEIPTEYKNNQVVFEAFLLAIIRRTKITYSQIQNRIDATKFGKLKSVDLAEAIALKIFNENPNDSKVFDDFYQQNSLDSFGSNTSILALKTYGDYIYKTKTDDETYVIANDVRSKVLKLKPQISTQSWKQEVNLILEKFIDIAPSIIPVRVLFEQRGIYQLNFTLQKKILFSEFRKPDGDVQNAEKIFEELMKTDNNKVSQPMRINSPQLMGTMIKGLCQVIGRTHDVSLYPELSKYLEMLPGLEVHMSINWMEQVLRTIRMVFRSGSTKTIPKELLEFSEFIIEKLPAIDPDFNYQFRNDDIAMFKKIGAKSFSKLKSTST | May be involved in the control of meiotic sister-chromatid recombination. | Q6FW79 |
Q708W2 | FXJ1A_XENLA | Forkhead protein 5 | Xenopus | MFDLPRAAPLDMADSWLTFQAEEEQGQESFSSSVNLDDSLTSLQWLQEFSILNSNEGKTPSSSGDSHGYRQLSGAPCSPLAADPACLGMPHTPGKPISSSTSRASHLGLQPMEEIDYKTNPHVKPPYSYATLICMAMQASKKTKITLSAIYNWITDNFCYFRHADPTWQNSIRHNLSLNKCFMKVPREKDEPGKGGFWKIDPQYADRLINGAMKKRRLPPVQIHPAFASAQAAASSDSKRGSAWQMSVNSESHQLLKAFEEITNEQGWNPLGEHGWNSISDGKSHKRKQPLPKRMFKAPRLSSSPMLSQEEQTELGSLKGDFDWEVIFDSSINGFNFSAFEDLEVTPPLSPVTRSVDLTVHGKHIDCPQQWYPMGQDHAVAQNSLDFDETLLATSFLQHPWEENRNDYLSNSANIEQLFDLNEAFPAELNDWSSLGSYI | Key transcription factor required for motile ciliogenesis. Activates genes essential for motile cilia formation and function. Required for ciliogenesis in multiciliated cells. | Q708W2 |
Q9HU77 | HUTF_PSEAE | N-formimino-L-glutamate iminohydrolase | Pseudomonas | MSAIFAERALLPEGWARNVRFEISADGVLAEIRPDANADGAERLGGAVLPGMPNLHSHAFQRAMAGLAEVAGNPNDSFWTWRELMYRMVARLSPEQIEVIACQLYIEMLKAGYTAVAEFHYVHHDLDGRSYADPAELSLRISRAASAAGIGLTLLPVLYSHAGFGGQPASEGQRRFINGSEAYLELLQRLRAPLEAAGHSLGLCFHSLRAVTPQQIATVLAAGHDDLPVHIHIAEQQKEVDDCQAWSGRRPLQWLYENVAVDQRWCLVHATHADPAEVAAMARSGAVAGLCLSTEANLGDGIFPATDFLAQGGRLGIGSDSHVSLSVVEELRWLEYGQRLRDRKRNRLYRDDQPMIGRTLYDAALAGGAQALGQPIGSLAVGRRADLLVLDGNDPYLASAEGDALLNRWLFAGGDRQVRDVMVAGRWVVRDGRHAGEERSARAFVQVLGELLD | Catalyzes the hydrolysis of N-formimino-L-glutamate to N-formyl-L-glutamate and ammonia. | Q9HU77 |
B1YJG1 | APT_EXIS2 | Adenine phosphoribosyltransferase | Exiguobacterium | MEFKQHIKEVENWPKEGISFKDITSLMQNGPAYKQSVDALIDYARKQGADVIAGPEARGFVVGCPAAYAMEIGFVPVRKEGKLPRETVRVEYGLEYGKDVLTMHHDAIQPGQRVVILDDLLATGGTIEATIKMIEQLGGTVAGIGFLIELDGLGGREKLEGYDILSLIRYAD | Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. | B1YJG1 |
Q0BKE7 | HEM1_FRATO | Glutamyl-tRNA reductase | Francisella | MNMALISLAIDYKKSPIEVRSEFALSGLDVSMLYRSILAIDNVVHAVILSTCNRTEVYLEISNLRVVDDILVWWQGYVRNPNYKIKDYFKLRQGTEVIMHLMKLACGLESMVLGEPQILGQVKDSYTLSKKNHAIGKELDRVFQKVFATAKRVRSETRIGYCPVSVAFSAITLAKRQLDNISSKNVLIIGAGQTGELLFRHVTALAPKQIMLANRTIEKAQKITSVFRNASAHYLSELPQLIKKADIIIAAVNVLEYIVTCKYVGDKPRVFIDISIPQALDPKLGELEQNVYYCVDDINAVIEDNKDKRKYESSKAQKIIVKSLEEYLEKEKAIISNSAIKELFQKADGLVDLSLEKSLAKIRNGKDAEEIIKRFAYEIKKKVLHYPVVGMKEASKQGRSDCLVCMKRMFGLNVEK | Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA). | Q0BKE7 |
B7V5G9 | DAPF_PSEA8 | PLP-independent amino acid racemase | Pseudomonas | MLLRFTKMHGLGNDFMVLDLVSQHAHVQPKHVKLWGDRNTGIGFDQLLIVEAPSSPDVDFRYRIFNADGSEVEQCGNGARCFARFVQDKRLTVKKSIRVETKGGIIELNIRPDGQVTVDMGPPRLAPAEIPFQAEREALSYEIEVNGQRVELAAVSMGNPHGVLRVENVDSAPVHSLGPQLEVHPRFPKKANIGFLQVLDPHHARLRVWERGVGETQACGTGACAAAVAGIRQGWLQSPVQIDLPGGRLHIEWAGPGQPVMMTGPAVRVYEGQVRL | Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine and an essential component of the bacterial peptidoglycan. | B7V5G9 |
Q63829 | COMD3_MOUSE | Bmi-1 upstream gene protein | Mus | MELSESVQRGIQTLADPGSFDSNAFALLLRAAFQSLLDARADEAALDHPYLKQIDPVVLKHCHAAAATCILEAGKHQVDKSTLSTYLEDCKFDRERIELFCTEYQNNKNSLETLLGSIGRSLPHITDVSWRLEYQIKTNQLHKMYRPGYLVTLNVENNDSQSYPEINFSCNMEQLQDLVGKLKDASKSLERATQL | May modulate activity of cullin-RING E3 ubiquitin ligase (CRL) complexes. May down-regulate activation of NF-kappa-B. Modulates Na(+) transport in epithelial cells by regulation of apical cell surface expression of amiloride-sensitive sodium channel (ENaC) subunits. | Q63829 |
A8GM80 | ERA_RICAH | GTPase Era | spotted fever group | MYNQRTISVCIIGRPNSGKSTLLNRIIGEKLSIVTPKVQTTRSIITGIITLKDTQVILYDTPGIFEPKGSLEKAMVRCAWSSLHSADLVMLIIDSLKPFDDVTHDILDKLRSLNIVPIFLLNKIDIESKYLDDIKAFLIGNHPDSLFFPISALSGKNINGLLEYITGKAQIAPWLYAEDDITDLPMRFIAAEITREQLFFNLQQELPYKLTVQTEKWEDLKDKSVKINQVIIVSRASYKTIILGKNGSKIREIGSKSRMQMERFFGFPVHLFLFVKVHELWENHPDFYQYMKI | An essential GTPase that binds both GDP and GTP, with rapid nucleotide exchange. Plays a role in 16S rRNA processing and 30S ribosomal subunit biogenesis and possibly also in cell cycle regulation and energy metabolism. | A8GM80 |
Q9P109 | GCNT4_HUMAN | Core2-GlcNAc-transferase 3 | Homo | MKIFKCYFKHTLQQKVFILFLTLWLLSLLKLLNVRRLFPQKDIYLVEYSLSTSPFVRNRYTHVKDEVRYEVNCSGIYEQEPLEIGKSLEIRRRDIIDLEDDDVVAMTSDCDIYQTLRGYAQKLVSKEEKSFPIAYSLVVHKDAIMVERLIHAIYNQHNIYCIHYDRKAPDTFKVAMNNLAKCFSNIFIASKLEAVEYAHISRLQADLNCLSDLLKSSIQWKYVINLCGQDFPLKSNFELVSELKKLNGANMLETVKPPNSKLERFTYHHELRRVPYEYVKLPIRTNISKEAPPHNIQIFVGSAYFVLSQAFVKYIFNNSIVQDFFAWSKDTYSPDEHFWATLIRVPGIPGEISRSAQDVSDLQSKTRLVKWNYYEGFFYPSCTGSHLRSVCIYGAAELRWLIKDGHWFANKFDSKVDPILIKCLAEKLEEQQRDWITLPSEKLFMDRNLTTTS | Glycosyltransferase that mediates core 2 O-glycan branching, an important step in mucin-type biosynthesis. Does not have core 4 O-glycan or I-branching enzyme activity. | Q9P109 |
Q1BV23 | NUOK_BURCA | NDH-1 subunit K | Burkholderia cepacia complex | MLTLAHYLVLGAILFAIAIVGIFLNRRNVIIILMSIELMLLAVNTNFVAFSHYLGDVHGQIFVFFVLTVAAAEAAIGLAILVTLFRKLDTINVEDLDQLKG | NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. | Q1BV23 |
Q24UI2 | RIMP_DESHY | Ribosome maturation factor RimP | Desulfitobacterium | MGESIMEQVEAIIAPVITEQGLELVDVEYVKEGAHWYLRIYIDKEGGVDIDDCTNVSHLVSEVLDKHDPIAQAYMLEVSSPGLERPLKKDEDFERFTGKLVRVLTKEAYQGYKEFTGYLVGLIEDDIVLEYEKEKMAIPRAIVDKANLTFEF | Required for maturation of 30S ribosomal subunits. | Q24UI2 |
A2CAR9 | GLGB_PROM3 | Glycogen branching enzyme | Prochlorococcus | MTTSVALDWVVQDGQRLAECRHDHPFSLLGPQSHEGQWIVRIWMPEASQVELLCDGRTTAMTTPNHSWIFEAALNQDPGRTYQLRVKRAGIVHEQHDPWAFHDEWMGEMDRHLFAEGNHHHIWQRMGAHLMEREGVEGVMFCLWAPRACSVAVLGELNGWDGRHHPMQRRQGGLWELFIPGFKEGTLYKYEIRTQDGHCYQKADPYGFQHEVRPATSSVVARLDRYQWQDEQWMRQRDSRNALDQPISVYEMHLGSWIHAATDEPYIELDGTPRAPVLAADMKPGARLLTYPELADQLIPYVKDRGFTHIELMPISEHPFDGSWGYQVTGWYAPTSRFGSPDEFRAFVDRCHAEGLGVIIDWVPGHFPKDGHGLAFFDGTHLYEHSDPRIGEHKEWGTLIFNYSRNEVRNFLVANLVYWFEQFHIDGIRVDAVASMLYRDYLRPDGEWIANEDGGRENTEAVRFLQQANHVLFQHFPGALSIAEESTTWPMVTQPTDMGGLGFNLKWNMGWMHDMLDYFELDPWFRQFHQNNITFSIWYTYTENFMLALSHDEVVHGKSNLLHKMPGDDWQKCANVRALLAYMWTHPGKKTIFMGMEFGQRSEWNVWGDLQWELLTHDPHKGLQKLVDDLNTFYKAEPALWKDDFDQYGFQWIDCNDNRHSIISFMRRESSGGTWLVVVANFTPQSHSNYRIGVPIGGYYEEVFNTDSSCYGGRNLGNMGGKNTDEFNIHGYEQSLELCLPALSVLVFRHDPKRSL | Catalyzes the formation of the alpha-1,6-glucosidic linkages in glycogen by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position. | A2CAR9 |
Q9M3E5 | LRK11_ARATH | Putative L-type lectin-domain containing receptor kinase I.1 | Arabidopsis | MAQRLHLLLLLFLICFVNLISFSSQQDLSFIYNGFNQDQTNLNLDGSAKFLQDGLLQLTNATTQQKGHAFFNRPFEFGSASSQSPSFSTHFVCALVPKPGVDGGHGIAFVLSSSMDLTQADPTQYLGLFNISTNGSPSSHLLAIELDTVQSAEFDDRDKNHVGIDENSLQSVESASASYYSDKEGKNKSLKLLSGDPIQVWIDYEDTLLNVTLAPLKTQKPSKPLLSITINLTAIFPDRKAFIGFSAATGSLISYQYILGWSFSRNRALLQSLDISKLPTVPRPKKPEKTSPLLIVLLIILAIIVMVVVGGFYLYRRKKYAEVREPWEKPYGPLRYSYKSLYKATRGFNKDGRLGRGGFGEVYKGTLPILGDIAVKRLSHDAEQGMKQFVAEVVTMGSLQHKNLVPLLGYCRRKGELLLVSKYMEGGSVDQYLFHGDKPPLSWSQRVSILRDIASALCYLHTGASQVVLHRDIKASNVMLNGNLQGFLGDFGMARFDDHGSNLSATAAVGTIGYMALELTSTGTSTRTDVYAFGAFMLEVTCGRRPFDPAMPVEKRHLVKWVCECWREGSLVNAVDTRLRGKFVPGEVEMVLKLGLLCTSIIPEARPNMEQVVQYINRHQRLPEFSPNTPGIGVSTPVLMGLPSLAITSSSVTSSVSGPSASPSSANNSMFISHTIIYGDGR | Involved in resistance response to the pathogenic fungus Alternaria brassicicola. | Q9M3E5 |
A5E1F6 | UTP25_LODEL | U three protein 25 | Lodderomyces | MARQVKRKSGADRNDGGGKYNSNNDRSVKRGRSELRTVTRTSRRDRGQDEQHNSHGTGGDFDIEGNVKDGRENVEQDKEEEEEEEDEDKGKAYEALLTLLKIEQKQEMKSGNKMENGRGLENTGSETGEKDNSAVKDDEDEDEDDFGEDENAGVVLEDQKEEEEEEKEDEDEDEEEEEDDEDTPAGINNDAFELHFNQPTEEYLEQEDKLVLKENAKWNIHKKESYDDLSLTSITQSPPGSSITIPSSLLKQKGTDISEYPLKKRVYTAFESTYGPSISKLESILLQPILNYQDINYQYKTFLNSSYRKLYALHALNHIYKTRDRILKNTAKLHQLNEDGDDLELRDQGFTRPKVLILLPTRDACNEIVEMIIKLSGTDQQENKKKFTTQFYTKAETRTNKPGDFQDAFKGNNNDFFCIGMKLTRKTLKLYSSFYSSDIILASPLGLSMILENPDKKKRQYDFISSIEVLIVDRANQIEMQNWDHVNTVMKYINKVPKEFHDADFSRIRMWSINDQAKLLRQTLVFSEYQTPAINNLVSSKSHNLAGKIRFKPVITSENSIMNSIGLRIKQVFQRFPSESPLADPDSRFKFFTNSIIPHLLQSSSYGNGIMIYIPSYFDYLRVKQHFKDSTKYNFGAIDEYSSQSKLTRTRHEFALGKIQIILYTERLHYFRRYEISGVKNLIMYVPPSNPLFYKELIRFIGKSVFKEECDLDLTWAKLIYSKWDANALERIVGNERAPVLCSSQNEQYEFR | DEAD-box RNA helicase-like protein required for pre-18S rRNA processing, specifically at sites A0, A1, and A2. | A5E1F6 |
I6YDK7 | ACCD1_MYCTU | 3-methylcrotonyl-CoA carboxylase | Mycobacterium tuberculosis complex | MTTPSIAIAPSFADEHRRLVAELNNKLAAAALGGNERARKRHVSRGKLLPRERVDRLLDPGSPFLELAPLAAGGMYGDESPGAGIITGIGRVSGRQCVIVANDATVKGGTYYPMTVKKHLRAQEVALQNMLPCIYLVDSGGAFLPRQDEVFPDREHFGRIFYNQATMSAKGIPQVAAVLGSCTAGGAYVPAMSDEAVIVREQGTIFLGGPPLVKAATGEIVSAEELGGGDLHSRTSGVTDHLADDDEDALRIVRAIADTFGPCEPAQWDVRRSVEPKYPQAELYDVVPPDPRVPYDVHEVVVRIVDGSEFSEFKAKYGKTLVTAFARVHGHPVGIVANNGVLFSESALKGAHFIELCDKRKIPLLFLQNIAGFMVGRDYEAGGIAKHGAKMVTAVACARVPKLTVVIGGSYGAGNYSMCGRAYSPRFLWMWPNARISVMGGEQAASVLATVRGEQLSAAGTPWSPDEEEAFKAPIRAQYEDQGNPYYSTARLWDDGIIDPADTRTVVGLALSLCAHAPLDQVGYGVFRM | Component of a biotin-dependent acyl-CoA carboxylase complex. This subunit transfers the CO2 from carboxybiotin to the CoA ester substrate . When associated with the alpha1 subunit AccA1, is involved in branched amino-acid catabolism with methylcrotonyl coenzyme A as the substrate . Shows residual with propionyl-CoA and acetyl-CoA . | I6YDK7 |
Q02VT8 | UPPP_LACLS | Undecaprenyl pyrophosphate phosphatase | Lactococcus cremoris subsp. cremoris | MDFIRAIILGIIEGITEWLPISSTGHLIIADEFIRLNQSAAFKEMFDVVIQLGAILSVVVLYFHKLNPFNKLNPADKQKTPREIQLTWRLWLKVLIAALPAAIIGLPLNDWLDKHFYHFVPVAFMLIIYGVAFIVIERRWVPNHEFSVMDIDRLPYRAALYIGLFQVLSLLPGTSRSGATIVGALLIGVSREVAAEFTFFLGIPVMFGASFIKILHFFKNGNSLNLEQFGVLLVACLVAFGVSMIAIKFLTDYVKKHDFTFFGKYRIVLGIVLLIYAAFKAFLG | Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin. | Q02VT8 |
C0QGT0 | CLPP_DESAH | Endopeptidase Clp | Desulforapulum | MPLIPMVVEQSNRGERAYDIYSRLLKDRIIFLGSAMDDEVANLIVAQLLFLESEDPEKDINFYINSPGGVVTAGMAVYDTMQYIKPDVATVCIGQAASMGALLLAAGAKGKRFSLPNSRIMIHQPLGGAQGQASDIKIQANEILRMKEVLSGILSKHTGQNFDKISEDTDRDFFMSGDQAKEYGLVDHVVASRDELEKAEAAKEK | Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. | C0QGT0 |
A7IAU7 | VATB_METB6 | V-ATPase subunit B | Methanoregula | MKEYRTITKIAGPLVFVEKTEPIGYQELVNIVLSDGTIKRGQVLDTSDDLVVVQIFETTTGIGRDSGVRFTGETIKMPVGREMLGRILSGGGKPIDGGPEIVPEKRLDITGAAINPWARNSPSDFIQTGISTIDGTNTLVRGQKLPIFSGAGLPHNNVALQIARQAKVPGSTESFAVVFAAMGITKEEANYFMQDFERTGALEHAVVFLNLADDPAVERIITPRLALTTAEYLAFELGMHVLVILTDMTNYCEALRQIGAAREEVPGRRGYPGYMYTDLACIYERAGIIKGQKGSVTQIPILTMPGDDITHPIPDLTGYITEGQIVVNRELHRKGIYPPINVLPSLSRLMNLGIGKGHTREDHKKVSDQMYAGYAEGNDLRGLVAIVGKDALSERDRGLLEFADLFEDKFVRQGYDEDRTIEDTLDLGWDLLSTLPVEQLTRIDRDLINKYHPKLKAGAKKE | Produces ATP from ADP in the presence of a proton gradient across the membrane. The archaeal beta chain is a regulatory subunit. | A7IAU7 |
Q96Q45 | TM237_HUMAN | Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 4 protein | Homo | MRTDSGARLEEGHLRPPRALPPVPSQDDIPLSRPKKKKPRTKNTPASASLEGLAQTAGRRPSEGNEPSTKELKEHPEAPVQRRQKKTRLPLELETSSTQKKSSSSSLLRNENGIDAEPAEEAVIQKPRRKTKKTQPAELQYANELGVEDEDIITDEQTTVEQQSVFTAPTGISQPVGKVFVEKSRRFQAADRSELIKTTENIDVSMDVKPSWTTRDVALTVHRAFRMIGLFSHGFLAGCAVWNIVVIYVLAGDQLSNLSNLLQQYKTLAYPFQSLLYLLLALSTISAFDRIDFAKISVAIRNFLALDPTALASFLYFTALILSLSQQMTSDRIHLYTPSSVNGSLWEAGIEEQILQPWIVVNLVVALLVGLSWLFLSYRPGMDLSEELMFSSEVEEYPDKEKEIKASS | Component of the transition zone in primary cilia. Required for ciliogenesis. | Q96Q45 |
D1BS27 | PSA_XYLCX | Proteasome core protein PrcA | Xylanimonas | MTMPFYVSPEQLMKDRADFARKGIARGRSVVVLGYDGGILFATENPSRALHKISEIYDRIAFAAVGKYNEFENLRVAGVRYADLRGYSYDRKDVTARGLANAYAQTLGTVFTTESKPLEVELVVAEVGDTPEADQIYRLSYDGSVADEHGHVAMGGQAEQLGKRLDDGWREGLTLTEALDLATTTLGAVGTDGQLLAAGSERTIDAGQLEVAVLDRARPRRAFRRLHGAALTHGRGAPHGEGAR | Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. | D1BS27 |
Q0B950 | T3HPD_BURCM | Trans-L-3-hydroxyproline dehydratase | Burkholderia cepacia complex | MKISRSLSTVEVHTGGEAFRIVTSGLPRLPGDTIVQRRAWLKENADEIRRALMFEPRGHADMYGGYLTEPVSPTADFGVIFLHNEGYSDHCGHGVIALSTAAVELGWVQRTVPETRVGIDAPCGFIEAFVQWDGEHAGPVRFVNVPSFIWRRDVSVDTPSFGTVTGDIAYGGAFYFYVDGAPFDLPVREAAVEKLIRFGAEVKAAANAKYPVVHPEIPEINHIYGTIIANAPRHPGSTQANCCVFADREVDRSPTGSGTGGRVAQLYQRGVLAAGDTLVNESIVGTVFKGRVLRETMVGDIPAVIPEVEGSAHICGFANWIVDERDPLTYGFLVR | Catalyzes the dehydration of trans-3-hydroxy-L-proline (t3LHyp) to Delta(1)-pyrroline-2-carboxylate (Pyr2C). Is likely involved in a degradation pathway that converts t3LHyp to L-proline. Displays neither trans-4-hydroxy-L-proline (t4LHyp) epimerase nor proline racemase activity. | Q0B950 |
C4K477 | CH60_HAMD5 | Chaperonin-60 | Candidatus Hamiltonella | MAAKDLKFGNDARKKMLKGVNILANAVKVTLGPKGRNVVLDKSYGAPSITKDGVSVARDIELEDKFENMGAQMLKEVASKANDAAGDGTTTATVLAQSIVTEGLKAVAAGMNPMDLKRGIDKAVDAAVEELKKLSKPCKDSKEIAQVGTISANADEKVGTLISDAMKRVTNEGVITVEEASGLEDGLIVVEGMQFDRGYLSPYFINKQESSSIEFDNPYILLVDKKISNIRDMLSILEVVAKEGKPLLIIAEDVEGEALATLVVNTMRGIVKVAAVKAPGFGDRRKEMLQDIAVLTHGHVISEETGDSLEKATQENLGKAKRVVITKDATTIIDGAGEKSRIEARVQNIRKQIENATSDYDKEKLQERVAKLSGGVAVIKVGAPTEIAMKEKKARVEDALQATRAAVEEGVVPGGGVALIRVASKIANSSLKGDNEDQNVGIRVALRAMESPLRQIVVNAGEEASVIANKVKENKGNDNYGYNAQTEAYGDMIEMGILDPTKVTRSALQYAASIAGLMITTECMVTDLPKEEKASDMGSGGMGGMGGMNGMM | 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. | C4K477 |
Q6DEB4 | AR19A_XENLA | cAMP-regulated phosphoprotein 19-A | Xenopus | MSGENQETKAQEESSALEQKEIDDKVVSPEKSEEIKLKARYPNLGPKPGGSDFLRKRLQKGQKYFDSGDYNMAKAKMKNKQLPTAASDKTEVTGDHIPTPQDLPQRKPSLVASKLAG | Protein phosphatase inhibitor that specifically inhibits protein phosphatase 2A (PP2A) during mitosis. When phosphorylated at Ser-67 during mitosis, specifically interacts with ppp2r2d (PR55-delta) and inhibits its activity, leading to inactivation of PP2A, an essential condition to keep cyclin-B1-CDK1 activity high during M phase. | Q6DEB4 |
B5XKA6 | SYT_STRPZ | Threonyl-tRNA synthetase | Streptococcus | MIKITFPDGAVREFESGVTTFDIAESISKSLAKKALAGKFNDQLIDTTRAIEEDGSIEIVTPDHKDAYEVLRHSAAHLFAQAAKRLFPNLHLGVGPAIAEGFYYDTDNAEGQISNEDLPRIEAEMQKIVTENYPCIREEVTKEEALELFKDDPYKVELINEHAGAGLTVYRQGEFVDLCRGPHVPSTGRIQVFHLLNVAGAYWRGNSDNNMMQRIYGTAWFDKKDLKAYLTRLEEAKERDHRKLGKELDLFMISQEVGQGLPFWLPDGATIRRTLERYITDKELASGYQHVYTPPLASVELYKTSGHWDHYQEDMFPVMDMGDGEEFVLRPMNCPHHIQVYKNHVRSYRELPIRIAELGMMHRYEKSGALSGLQRVREMTLNDGHIFVTPEQIQEEFQRALQLIIDVYADFNLTDYRFRLSYRDPNDTHKYYDNDEMWENAQSMLKAALDEMGVDYFEAEGEAAFYGPKLDIQVKTALGNEETLSTIQLDFLLPERFDLKYIGADGEEHRPVMIHRGVISTMERFTAILIETYKGAFPTWLAPHQVTVIPISNEAHIDYAWEVAKILRDRGVRADVDDRNEKMQYKIRASQTSKIPYQLIVGDKEMEDKSVNVRRYGSKATHTESVEDFVENILADIARKSRPDAQA | Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr). | B5XKA6 |
O84281 | NQRC_CHLTR | NQR-1 subunit C | Chlamydia | MASKSRHYLNQPWYIILFIFVLSLIAGTLLSSVYYVLAPIQQQAAEFDRNQQMLMAAQVISSDNTFQVYEKGDWHPALYNTKKQLLEISSTPPKVTVTTLSSYFQNFVRVLLTDTQGNLSSFEDHNLNLEEFLSQPTPVIHGLALYVVYAILHNDAASSKLSASQVAKNPTAIESIVLPIEGFGLWGPIYGFLALEKDGNTVLGTSWYQHGETPGLGANIANPQWQKNFRGKKVFLVSASGETDFAKTTLGLEVIKGSVSAALGDSPKAASSIDGISGATLTCNGVTESFSHSLAPYRALLTFFANSKPSGESHDH | 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. | O84281 |
Q15NR8 | TRMN6_PSEA6 | tRNA m6A37 methyltransferase | Pseudoalteromonas | MKRQGFQFKQFFIEHQDCAMKVGTDSIMLGSWVTGGDLINASETQRFLDIGTGSGLLAIMLAQKSSEQTHISGIDIDKDAIGQATRNMANSPWSHRLDAQQASVQSFTQNCDNPKFALIISNPPYFNSPILTHEKQAQKRVAARQTSELTHHTLLNNVVRLLAPSGVFYCVLPSDVSQAFIELADPLGLSLIKQLTVFSKPDTNALRELLAFRFNDPSCIRDTISRALTSPEPPTRDTLTIYTQSHQYSDQYKALCKDYYLNF | Specifically methylates the adenine in position 37 of tRNA(1)(Val) (anticodon cmo5UAC). | Q15NR8 |
P40384 | SPO11_SCHPO | SPO11 protein homolog | Schizosaccharomyces | MNSNDKKKVVRSWIEQFVHDFVEQLSKPTKDSVNVALKRRKHNSWNGSLDSKANERQKVKVFSFPRNETTIAQLFRVLDCVHEAVISDTVITKRDIYYRDVDLFKRQTVVDELLGDISNTIGCSRSDLNVEASAKGLVFGSIHIALENGTVITATKPLLISHHRISSITSTAKWVLVIEKEAVFQTLTEEALADTIIVTAKGFPDLMTRKFLVKLAKALPDAKFFGIFDWDPHGLCIYSCFKYGSNAYSHEPHSQLRNLQLLGPLYEDIFNKNQEFSLKLNKRDIKMITTLLQFEGFQKEPVVREQLQRMLFIQKKAEIQAILEFPSWIKGKLADADKSGKHSVR | Required for formation of the double-strand breaks (DSBs) that initiate meiotic recombination . Required for crossover recombination and chiasmatic segregation of chromosomes during meiosis I. Also involved in the faithful equational segregation of chromosomes during meiosis II . | P40384 |
Q2EEW8 | RK12_HELSJ | 50S ribosomal protein L12, plastid | unclassified Helicosporidium | MTFNKKINEIITLLSDLNILELNSLINEIRNQFQIPDIVSTIQTGNKTKPEANIIEQKESAEIKKSNFELILQTVPTEKRVAVLKAIRNTTSLDLKGAKDSIADLPKKLLDNLSLEEAEKAKTLLEEAGATVILA | Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation. | Q2EEW8 |
B2V4H4 | RS15_CLOBA | 30S ribosomal protein S15 | Clostridium | MDKARKLEIIKQYGRSEGDTGSPEVQIALLTERINSLTGHLKVHKKDHHSRRGLLMMVGHRRGLLNYLADQDIERYRTIVKQLGLRR | Forms an intersubunit bridge (bridge B4) with the 23S rRNA of the 50S subunit in the ribosome. | B2V4H4 |
A8LRR7 | UREF_DINSH | Urease accessory protein UreF | Dinoroseobacter | MIAARLRLSQWLSPSFPVSGYAYSHGLEQAISTGDIADAEDLLAWLQALLTSGACQADGVLVARAAAGDPLEPLCEAAEALAGSAERWSETRDQGAAFVSTTNALCDTALRPMPYPVAVGARARALGLPVGEVVALYLQAFLGNLISGAVRLIPLGQTEGQQVSQSLHPTISTQARCLATRPLSEIGTGAVRAELAAMAHETQEVRIFRT | Required for maturation of urease via the functional incorporation of the urease nickel metallocenter. | A8LRR7 |
Q1AU18 | RL11_RUBXD | 50S ribosomal protein L11 | Rubrobacter | MGRGRGKRVVRKLKLQIPGGQANPAPPVGPALGQAQVNIGEFVRQFNDATRDRMGQLIPVEITVYEDRSFTFVTKTPPAAFLLKQAAGVEKGSGEPNRSAAGRVSRAQVEEIARTKMPDLNAADVEAAVKIIEGTARSMGIKVEQ | Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. | Q1AU18 |
A5D8T8 | CL18A_HUMAN | Mannose receptor-like protein 2 | Homo | MLHPETSPGRGHLLAVLLALLGTAWAEVWPPQLQEQAPMAGALNRKESFLLLSLHNRLRSWVQPPAADMRRLDWSDSLAQLAQARAALCGTPTPSLASGLWRTLQVGWNMQLLPAGLVSFVEVVSLWFAEGQRYSHAAGECARNATCTHYTQLVWATSSQLGCGRHLCSAGQAAIEAFVCAYSPRGNWEVNGKTIVPYKKGAWCSLCTASVSGCFKAWDHAGGLCEVPRNPCRMSCQNHGRLNISTCHCHCPPGYTGRYCQVRCSLQCVHGRFREEECSCVCDIGYGGAQCATKVHFPFHTCDLRIDGDCFMVSSEADTYYRARMKCQRKGGVLAQIKSQKVQDILAFYLGRLETTNEVIDSDFETRNFWIGLTYKTAKDSFRWATGEHQAFTSFAFGQPDNHGFGNCVELQASAAFNWNDQRCKTRNRYICQFAQEHISRWGPGS | Binds polysaccharides in a Ca(2+)-independent manner with a preferentially binding to fucoidan, beta-glucans and galactans . | A5D8T8 |
Q2U0K2 | HEPA_ASPOR | Heptelidic acid biosynthesis cluster protein A | Aspergillus subgen. Circumdati | MWWPRATADRLQTCTFWFLWLFTWDDEIDQSTSDLFIHIHKANDFRKESLEYVKFCLGVGDDETAKWDFQNNPPNRPLIRSLDVIGAHLQKVYNHDQIMTFVNEIDYYMGCQQREQKRKLTGRLPIVAEYLETRMGTSAVTSMLALNEYGGALILGLKRR | Sesquiterpene cyclase; part of the gene cluster that mediates the biosynthesis of heptelidic acid (HA), a sesquiterpene lactone that acts as an inhibitor of glyceraldehyde-3-phosphatedehydrogenase (GAPDH) and a growth inhibitor of the salt-tolerant lactic acid bacteria in soy sauce brewing. | Q2U0K2 |
Q9X4M1 | ACKA1_LATSS | Acetokinase 1 | Latilactobacillus | MEKILAINAGSSTLKWQLFEMPSETVIAKGMIDRLGLSDSVFTAKYGDNQKFKEVQDVTTHEMAATLLLTRLKELGIVSHLDEITGVGHRVVGGGEAFSDSMVINPVALDEINRLAEYAPLHNPTQAYYIKIFTALLPGVPQVAVFDTSFYSTLAPENYLYSIPQEYYQTFGARKYGAHGTSHRYVAHRAAEILGTPLESQKMITLHLGSGASITAVQDGHAVDTSMGFTPLAGITMGTRSGDIDVSLVAFLAKKLEITMPEMIDILNHKSGLLGISELSPDMRDLEETAATRPQSALALSIFVNRVVKYVGSYVALMNGIDTLVFTAGSGENGSELRADICKQLACFGVKLDEEKNNVRSQERIISADDSKVKVLIVPTNEELMIARDVMRLK | Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction. | Q9X4M1 |
A8W7M6 | PHAT2_AMABI | Phallacidin | Amanita | MSDINATRLPAWLVDCPCVGDDVNRLLTRGE | Major toxin that belongs to the bicyclic heptapeptides called phallotoxins . Although structurally related to amatoxins, phallotoxins have a different mode of action, which is the stabilization of F-actin . Phallotoxins are poisonous when administered parenterally, but not orally because of poor absorption . | A8W7M6 |
P45121 | PROA_HAEIN | Glutamyl-gamma-semialdehyde dehydrogenase | Haemophilus | MLEQMGKQAKDAAFILAQLTTAEKNCALSIIAEQLEQQAPLILAENAKDIELAKQNGLSDALIDRLLLTQERLQGIANDVRHVISLADPVGKIIDGGTLDSGLKIERVRTPLGVIGTIYEARPNVTIDVASLCLKTGNAVILRGGKETQFSNKILIEVVQNALEQAGLPKFAVQAITDPNRELVMQLLKLDRYVDMIIPRGGSGLHELCKQHSTIPVIVGGVGVCHTFVEKSADQNKAIFVIDNAKTQRPSTCNTLETLLVQHSIAEEFLPKLVSHLSAKNVKYHAKSTALNILKQAGANVCEVTEKELRKEWGSLDLNVVVVEDIHAAIEHIRQYGTQHSESILTSSQSLARQFINQVDAAAVYVNASTRFTDGGQFGLGAEVAVSTQKLHARGPMGLEALTSYKWVCEGEYTVRK | Catalyzes the NADPH-dependent reduction of L-glutamate 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate. | P45121 |
Q6CWT7 | PPN1_KLULA | Endopolyphosphatase | Kluyveromyces | MKELQLPEKRKSNTGLSWFPSPRILQVFLVLLGAIVAFLSFSATSSIISSSPKHHSCHDNVEEAAVKYHYSTISSDELPISNERLASLGLTPNQPVKITDIGGKEKSIKGRFLHITDMHPDLYYKENTSIDDTCHRGKPKNDGDRAARFGNAMKGCDGPPDLMYYTLDWIHKNLSDEIDFIIWTGDNVRHDNDRRIPRTEQQIFDMNRQVSELFLKTFKDHESDDPRDLKVKIIPSLGNNDVFPHNLFSPGPTLQTRELYDIWSQFIPPAQQNTFDRYASFFVEAIPGKLAVISLNTLYMFKGNPLVDNCSNKKQPGYKMLLWVGFTLQELRDRGMKVWLSGHVPPIPKNFDSSCSDKLALWLHEYSDIIIGGFYGHMNMDHFIPVDGEKAWDDIANSMAISEYSGFFEQDFLEDAIAAREIRAEGAKPVKKVNYMNGVRDAYYSRISEDVKKLSEKDPLYERYSIVHIGTSIIPTFNPGFRIWEYNITELQTEEEVLHSHQPWDSFFEHLDVEIQKIIEEAEEAEEVEAFEDDEQIDSEIPDVLISKKKKKKGKKGKKNKNSKNWWKTDKTFPKKKPKNLPPGPAYENQLFSPLRFVQYYADLKEIDKQYLKLLKEGKSEDEAASIAFKYQIEYASDDKPYPMKTTLVKDYIELASELSGNDKLWDTFLERAFCSSGYED | Catalyzes the hydrolysis of inorganic polyphosphate (polyP) chains of many hundreds of phosphate residues into shorter lengths. | Q6CWT7 |
A2XLF4 | ZHD11_ORYSI | Zinc-finger homeodomain protein 11 | Oryza sativa | MEQQQERPREVYRECMRNHAAKLGTYANDGCCEYTPDDGHPAGLLCAACGCHRNFHRKDFLDGRATAAAGGAGGAGVGVAPMLPAPGGGGPPGYMHMAAMGGAVGGGGGVDGGGGSGGRRRTRTKFTEEQKARMLRFAERLGWRMPKREPGRAPGDDEVARFCREIGVNRQVFKVWMHNHKAGGGGGGGGSGGPGAGGGAQTSSSTTRGGGDVGVGLSPAMGGDGEDDEEVRGSEMCM | Putative transcription factor. | A2XLF4 |
P23772 | GATA3_MOUSE | GATA-binding factor 3 | Mus | MEVTADQPRWVSHHHPAVLNGQHPDTHHPGLGHSYMEAQYPLTEEVDVLFNIDGQGNHVPSYYGNSVRATVQRYPPTHHGSQVCRPPLLHGSLPWLDGGKALSSHHTASPWNLSPFSKTSIHHGSPGPLSVYPPASSSSLAAGHSSPHLFTFPPTPPKDVSPDPSLSTPGSAGSARQDEKECLKYQVQLPDSMKLETSHSRGSMTTLGGASSSAHHPITTYPPYVPEYSSGLFPPSSLLGGSPTGFGCKSRPKARSSTEGRECVNCGATSTPLWRRDGTGHYLCNACGLYHKMNGQNRPLIKPKRRLSAARRAGTSCANCQTTTTTLWRRNANGDPVCNACGLYYKLHNINRPLTMKKEGIQTRNRKMSSKSKKCKKVHDALEDFPKSSSFNPAALSRHMSSLSHISPFSHSSHMLTTPTPMHPPSGLSFGPHHPSSMVTAMG | Transcriptional activator which binds to the enhancer of the T-cell receptor alpha and delta genes. Binds to the consensus sequence 5'-AGATAG-3'. Required for the T-helper 2 (Th2) differentiation process following immune and inflammatory responses. Positively regulates ASB2 expression . | P23772 |
Q81XT3 | SYG_BACAN | Glycyl-tRNA synthetase | Bacillus cereus group | MYSMEQVVNLAKHRGFVFPGSEIYGGLANTWDYGPLGIELKNNVKKAWWKKFIQESPYNVGLDAAILMNPKTWIASGHVGNFNDPMIDCKKCKARHRADKLIEDALDAKGIEMVVDGLTFDQMADLMKEHEVKCPDCGSEEFTEIRQFNLMFKTFQGVTESSTNEIFLRPETAQGIFVNFKNVQRSMRKKLPFGIGQIGKSFRNEITPGNFTFRTREFEQMELEFFCKPGEDLEWFAFWRETCKNWLLSLGMTEESMRLRDHGEEELSHYSNATTDIEFKFPFGWGELWGVASRTDFDLKRHMEHSNEDFNYIDPQTNERYVPYCIEPSLGADRVTLAFLCDAYEEEQLENDSRTVLRFHPALAPYKAAILPLSKKLSEGATEVFAELAKDFMVDFDETGSIGKRYRRQDEIGTPFCITYDFDSVEDKAVTVRDRDTMEQVRMPISELKGFLEKKIQF | Catalyzes the attachment of glycine to tRNA(Gly). | Q81XT3 |
Q920J4 | TXNL1_RAT | Thioredoxin-related protein | Rattus | MVGVKPVGSDPDFQPELSGAGSRLAVVKFTMRGCGPCLRIAPAFSSMSNKYPQAVFLEVDVHQCQGTAATNNISATPTFLFFRNKVRIDQYQGADAVGLEEKIKQHLENDPGSNEDTDIPKGYMDLMPFINKAGCECLNESDEHGFDNCLRKDLSFLESDCDEQLLITVAFNQPVKLYSMKFQGPDNGQGPKYVKIFINLPRSMDFEEAERSEPTQALELTEDDIKEDGIVPLRYVKFQNVNSVTLFVQSNQGEEETTRISYFTFIGTPVQATNMNDFKRVVGKKGESH | Active thioredoxin with a redox potential of about -250 mV. | Q920J4 |
Q2Y6T9 | GRPE_NITMU | HSP-70 cofactor | Nitrosospira | MTEENRPQPDQPELTVTSESSVQETGENKARTPEQEGEAMPSLEQLLKKAELDAAEHYDAWLRAKAEGENIRKRAQMDVTNAHKYAIENFSTELLSVMDSLEAALAVENATVENFKSGMELTLKQLTATFAKFNIKQLSPQGEKFDPHLHQAMCMVESELPHNTVVQVMQKGYVLNDRVIRPALVSVSKGKES | Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. | Q2Y6T9 |
Q98SH2 | AT2B1_CHICK | Plasma membrane calcium pump isoform 1 | Gallus | MGDMANNSVAYSGVKNAVKEANHGEFGVTLAELRSLMELRATDALHKIQECYGDVQGICTKLKTSPNEGLSGNPADIERREAVFGKNFIPPKKPKTFLQLVWEALQDVTLIILEIAAVVSLGLSFYQPPGGNEALCGSVNVGEEEEESEAGWIEGAAILLSVVCVVLVTAFNDWSKEKQFRGLQSRIEQEQKFTVIRGGQVIQIPVADIIVGDIAQVKYGDLLPADGILIQGNDLKIDESSLTGESDHVKKSLDRDPMLLSGTHVMEGSGRMVVTAVGVNSQTGIIFTLLGAGGDEEEKEKEKKDKKTKAQDGAAMEMQPLKSEDGVDGDEKDKKRSNLPKKEKSVLQGKLTKLAVQIGKAGLLMSAITVIILVLYFVIDTSWVQKRPWLAECTPIYIQYFVKFFIIGVTVLVVAVPEGLPLAVTISLAYSVKKMMRDNNLVRHLDACETMGNATAICSDKTGTLTMNRMTVVQAYISEKHYKKIPAPEAIPENIMAYLVTGISVNCAYTSKILPPEKEGGLPRHVGNKTECALLGFLLDLKRDYQDVRNEIPEEKLHKVYTFNSVRKSMSTVLKNSDGSFRIFSKGASEIVLKKCFKILSADGEPKVFRPRDRDDIVKTVIEPMASEGLRTICLAFRDFPAGEPEPEWDNENDIVTGLTCIAVVGIEDPVRPEVPDAIKKCQRAGITVRMVTGDNINTARAIALKCGILNPGEDFLCLEGKDFNRRIRNEKGEIEQERIDKIWPKLRVLARSSPTDKHTLVKGIIDSTIFDQRQVVAVTGDGTNDGPALKKADVGFAMGIAGTDVAKEASDIILTDDNFTSIVKAVMWGRNVYDSISKFLQFQLTVNVVAVIVAFTGACITQDSPLKAVQMLWVNLIMDTLASLALATEPPTEALLLRKPYGRNKPLISRTMMKNILGHAFYQLVVVFTLLFAGEKIFDIDSGRNAPLHAPPSEHYTIVFNTFVMMQLFNEINARKIHGERNVFEGIFNNAIFCTIVLGTFVVQIIIVQFGGKPFSCSKLSIEQWLWSVFLGMGTLLWGQLISTIPTSRLKFLKEAGHGTQKEEIPEEELAEDVEEIDHAERELRRGQILWFRGLNRIQTQIRVVNAFRSSLYEGLEKPETRSSIHNFMTHPEFRIEDSEPHIPLIDDTDAEDDAPTKRNSTPPPSPNKNNNAVDSGIHLTTDMNKSATSSSPGSPLHSLETSL | Catalyzes the hydrolysis of ATP coupled with the transport of calcium from the cytoplasm to the extracellular space thereby maintaining intracellular calcium homeostasis. | Q98SH2 |
P23694 | PRZN_SERMA | Zinc proteinase | Serratia | MQSTKKAIEITESSLAAATTGYDAVDDLLHYHERGNGIQINGKDSFSNEQAGLFITRENQTWNGYKVFGQPVKLTFSFPDYKFSSTNVAGDTGLSKFSAEQQQQAKLSLQSWADVANITFTEVAAGQKANITFGNYSQDRPGHYDYGTQAYAFLPNTIWQGQDLGGQTWYNVNQSNVKHPATEDYGRQTFTHEIGHALGLSHPGDYNAGEGNPTYNDVTYAEDTRQFSLMSYWSETNTGGDNGGHYAAAPLLDDIAAIQHLYGANPSTRTGDTVYGFNSNTGRDFLSTTSNSQKVIFAAWDAGGNDTFDFSGYTANQRINLNEKSFSDVGGLKGNVSIAAGVTIENAIGGSGNDVIVGNAANNVLKGGAGNDVLFGGGGADELWGGAGKDIFVFSAASDSAPGASDWIRDFQKGIDKIDLSFFNKEANSSDFIHFVDHFSGTAGEALLSYNASSNVTDLSVNIGGHQAPDFLVKIVGQVDVATDFIV | Has insecticidal activity against the locust M.palpalis. When administered orally to locusts at a low dose it causes them to lie on their sides exhibiting sporadic limb movements and muscular twitching, followed by full recovery. When administered at higher doses the same symptoms are observed, followed by death. | P23694 |
Q733N4 | PLSY2_BACC1 | Lysophosphatidic acid synthase 2 | Bacillus cereus group | MVTTYLLFIVAYLLGSIPFALVVGKIGYGIDIREHGSGNLGGTNTFRTLGKKAGFIVTIADILKGTLATSLPIIFALDIHPLWFGLAAVLGHVYPIFAKFRGGKAVATSAGVLLCYSPVVFAILAVVFFSLLFTTRYVSLSSMVTAVVAVIASIVSGDKIFIIAMCLLAGMVIYKHRANIGRIINKTEPKANFSKKQK | Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP. | Q733N4 |
Q74FK2 | ALR_GEOSL | Alanine racemase | Geobacter | MDSRPTIAEVDLAALRHNYDLVVRTIPRGCGILAVVKADAYGHGFMDIARELETLGVTAFGVAFLAEGIQLRKSGIDRPVLILGGVYPGQERKCVGFNLSTALFSLEQARVLDDAAGRLYRRARVHAKIDTGMGRLGIPHEEASAFFSALRELKHLDLEGIISHFASADELDEDGRRYSDLQASRFAAAVAAARHEGFEPRYVHIANSAAAFGMDLPFCNLVRPGIVLYGALPSGDFEGKMALKPIMRLRSSIAMLKWVEPGTSISYARRFTAPDRRLVASIPVGYADGYSRSLTNRGEVVVRGRRAPVVGTVCMDWIMADVTHVSGVTVGDEVTLLGCDQEGNCVRAEELAEWAGTIPYEIFCGISKRVPRVYLNPSIRHR | Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids. | Q74FK2 |
O61704 | PSP1_CHRIL | Plasmatocyte-spreading peptide | Chrysodeixis | MKLTINILFCLILISQYNSANGNLRDLFNNVRGSISSSANKIRQDVKTLFHPSDKSGNKESSNIVFVEDKDEGAVGPARDNKPVAVTPAPVVSTTTQASAPTVATNGTATGGKDDKGRENFNGGCLAGYMRTADGRCKPTF | Mediates the spreading of plasmatocytes to foreign surfaces. Plasmocytes are a class of hemocytes involved in insect cellular immunity. | O61704 |
Q5M7R9 | GRHL2_XENTR | Transcription factor CP2-like 3 | Silurana | MSQETDNKRLVVLVPNDAVFNPRRAYTSEDEAWKSYLENPLTAATKAMMSINGDEESAAAIGLLYDYYKVPREKRLLSLNKINEGHEDQDKRNCLPANETPSNLSTGENRVQVLKTVPVNLSLNNDTVESSNREKYTTSLSESPQPAPASAVTVVKAEEFTPVFMAPSVPYRSDGEEPRGVIFEQTHFGVHSITTHSDYLKDDQRSTPDSTYNESFKETTEKYRTPSVGTEEFLYEQTASSTFQYTLEATKSLRQKQGEGPMTYLNKGQFYAITLSETGANKCFRHPISKVRSVIMVVFSEDKNRDEQLKYWKYWHSRQHTAKQRVLDIADYKESFNTIGNIEEIAYNAVSFTWDVNEEAKIFITVNCLSTDFSSQKGVKGLPLMIQIDTYSYNNRSNKPIHRAYCQIKVFCDKGAERKIRDEERKQNRKKGKSQAAQAQCNNSADGKLSAVPLQKKSDITFFKTMTDLDVQPVLFIPDVHFGNLQRTGQVFYNTDDDIEGGVLVKRLLRPVDEDYGPPAPKQMKEGSRKVLLYVRKETDEVFDALMLKYPTVKGLLEAISEKYGIPVEKIVKIYKKSKKGILVNMDDNIIEHYSNEDTFILNVESLAEQGYKITLTEI | Transcription factor playing an important role in primary neurulation and in epithelial development. Binds directly to the consensus DNA sequence 5'-AACCGGTT-3' acting as an activator and repressor on distinct target genes. | Q5M7R9 |
A8GV61 | NUSB_RICB8 | Antitermination factor NusB | belli group | MSSNKINKKSIARIAAIQAIYQHMLRNNDNIDDIIENVLSFYRNDTSMTDSPIKISLTISHFKMLVKLVFENIDKIDEIISNHLVNDKNQNHIPILLQALLRSGICELLFFPDIPTKVIINEYTDIANDMLNDHEIGFVNSILDKIAHENKRFYDK | Involved in transcription antitermination. Required for transcription of ribosomal RNA (rRNA) genes. Binds specifically to the boxA antiterminator sequence of the ribosomal RNA (rrn) operons. | A8GV61 |
P41791 | EUTM_SALTY | Ethanolamine utilization protein EutM | Salmonella | MEALGMIETRGLVALIEASDAMVKAARVKLVGVKQIGGGLCTAMVRGDVAACKAATDAGAAAAQRIGELVSVHVIPRPHGDLEEVFPISFKGDSNI | Expression of the eut operon allows this bacteria to use ethanolamine as a carbon, nitrogen and energy source. It relies on cobalamin (vitamin B12) both as a cofactor for the ethanolamine ammonia-lyase (EAL) activity and to induce the operon . EA enhances bacterial survival in macrophages in a concentration-dependent manner, suggesting it is an important nutrient during infection . | P41791 |
B3PB33 | RNFD_CELJU | Rnf electron transport complex subunit D | Cellvibrio | MALLNITSPHAQGANRTSRLMLLVVYATIPGMFTMTWFFGPGVLVNVLLASISCMLFEALAIKARQRPVGFYLRDFSALVTGVLIGVSLPPYCPWWLLISGSFIAIILAKQLYGGMGFNPFNPAMVAYALLLVSFPVEMTQWAQPKPLWVDGQLPGLMDTLAKVFSGAPIDGYSGATALDIIKQNKGLVLGDLYQQQPLLAEGRWASAGWEWVNIAFLFGGLYLLYKKVYTWHAPVSMLLALALMAALFYDSGSSSSSGSPLFHLLTGATMLGAFFIVTDPVSSTVSTKGRVIYGALIGMLVYVIRTWGSSYPDGVAFAVLLMNFAAPFIDYYTTPRTYGHKKPRRATDSTPRNGH | Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane. | B3PB33 |
Q5L6T4 | SYE_CHLAB | Glutamyl-tRNA synthetase | Chlamydia | MAWENVRVRVAPSPTGDPHVGTAYMALFNAIFAKRFNGKMILRIEDTDQTRSRDDYEKNIFSALQWCGIQWDEGPDIGGPYGPYRQSERTEIYRKYAELLLKTDYAYKCFATPKELEEMRAVATTLGYRGGYDRRYRYLSSEEVDARTREGQPYTIRLKVPLTGECVLDDYCKGRVVFPWADVDDQVLIKSDGFPTYHFANVVDDHLMGITHVLRGEEWLSSTPKHLLLYQAFGWKAPTFLHMPLLLNPDGTKLSKRKNPTSIFYYRDAGYIKEAFMNFLTLMGYSMEGDEEIYSLEKLIANFDPRRIGKSGAVFDTRKLDWMNKHYLTHERSSESLLAKLKDWLINDEFFLKILPLCQSRITTLAEFIGFTGFFFSVLPEYSKEELLPTTISQEKAAILLYSYVKYLEKSDLWVKDQFYQGSKWLSSAFQVHHKKVVIPLLYVAITGKKQGLPLFDSMELLGKPRTRARLVHAQNLLGGVPKKIQTTIDKVLKEEDLESKIFEF | 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). | Q5L6T4 |
P37569 | MCSA_BACSU | Protein-arginine kinase activator protein | Bacillus | MICQECHERPATFHFTKVVNGEKIEVHICEQCAKENSDSYGISANQGFSIHNLLSGLLNMDSSFQNAGTQMFSHSEQISACPKCGMTFQQFRKIGRFGCSECYKTFHSNITPILRKVHSGNTVHAGKIPKRIGGNLHVRRQIDMLKKELESLIHQEEFENAAHVRDQIRLLEQSLKSTDSEEEQE | Activates the phosphorylation activity of the protein-arginine kinase McsB. Is required for the delocalization of competence proteins from the cell poles. | P37569 |
P0A347 | CH10_THEVB | null | Thermosynechococcus | MAAVSLSVSTVKPLGDRIFVKVAESEERTAGGILLPDNAREKPQVGEVTAVGPGKLTEDGKRQPMDVKVGDKVLYSKYAGTEVKLAGEDYVLLSEKDILAIVG | 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 the GroEL ring, thereby capping the opening of the GroEL channel. | P0A347 |
A8F4R2 | RL4_PSELT | 50S ribosomal protein L4 | Pseudothermotoga | MAVVDLYNMKGEKVGTQELKDDIFNIEPNFDVMWRYVDYQLSLRRAGTVSTKTRSEVSGGGRKPWIQKHTGRARHGSIRSPIWRHGGVAHGPKPRDWSKKLPKKMKKLALKSALSQRFKEGNIIVVDDIGFDSSKTKNMRQLIKAFGFEGKKILFVLPWKRSEYENVKLSCKNIPGLKAIIADNPGATRENESIMRIDGLNVFDILNHEKLVLTRDMVMKIEEVLG | Forms part of the polypeptide exit tunnel. | A8F4R2 |
A4RD36 | YPI1_MAGO7 | Type 1 phosphatases regulator YPI1 | Pyricularia | MASRQSRQQHTTSAPAASRTQTETSTPSQEQPPQDPTPEVRSQPAILRLRGVRASSGPSVRWAEGVVDNEGLGRKSSKVCCIYHPTKPVGESSDESSSDSSSDSGTDSDDSTRGKGKRKHRSGGGGGGKKHGEGDCHGHNHGHDHGSSSSSGGGGGARKKKKKRTPSPNAYEKMPKVKPRAPAPEGAPGASGQ | Regulator of type 1 phosphatases which maintains protein phosphatase activity under strict control. | A4RD36 |
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