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 |
|---|---|---|---|---|---|---|
B0K1T5 | CODY_THEPX | GTP-sensing transcriptional pleiotropic repressor CodY | unclassified Thermoanaerobacter | MSTLLEKTRKVNRILQKTGIQPVDFNEMASILKDVIEANVYILSRKGKVLGYSILKDYGNDIFAQSKIIPEEYNDKLLRVTETLANDKGNLFKEDKILSDLILTIVPVNGGGDRLGTLVLSRGVKEFTDDDLILAEYGATVVGLEILRSKNEEIEDEARKRAVVQMALGTLSYSELEAIKNIFEELNGKEGLLVASKIADKVGITRSVIVNALRKFESAGIIESRSLGMKGTHIRVLNDKLLEELEKMKR | 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... | B0K1T5 |
Q4L837 | GLMM_STAHJ | Phosphoglucosamine mutase | Staphylococcus | MVKYFGTDGVRGIANKELTPELAFKLGRYGGYVLAHNEGADRPKVLVGRDTRVSGEMLESALISGLASIGAEVMRLGVISTPGVAYLTREMGAELGVMISASHNPVADNGIKFFGADGFKLSDAQEEEIETLLDQDNPDLPRPVGTDIVHFSDYFEGAQKYLSYLKSTIDVNLEGLKITLDGANGSTSALAPFLFGDLEADTETIGCSPDGYNINDNCGSTHPELLAEKVLETESDFGLAFDGDGDRLIAVDEKGNIIDGDQIMFVIGQEMHKNQELNNDMIVSTVMSNLGFYKALENEGIKSNKTKVGDRYVVEEMRKG... | Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate. | Q4L837 |
Q03VW4 | GLMM_LEUMM | Phosphoglucosamine mutase | Leuconostoc | MSEFNLKYFGTDGVRGVANKTLTPELAFRLGRTGGAILTRHANDENKKPVVIVGRDTRISGEMLQQAIIAGFLSVGIDVLRLGVITTPAVAFLVQNLEADAGVQITASHNPAADNGIKFFGNDGFKLSDQLEYEIEQLLDESEDTLPRPSADGLGVVNNYPEGVQKYLEFLQKTIPTDLNGMRIALDGANGATSGLLARLFADLGTDFVTLGTEPNGLNINDGVGSTNPAALAELVKENDVQAGLAFDGDGDRLIAVDENGEIVDGDKIMFITGKFLNEQGRLKHNAVVSTVMSNIGFYKALAENDMTSIKTAVGDRYVM... | Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate. | Q03VW4 |
T1SFR8 | PPR3C_CLABA | Protein phosphatase 1 regulatory subunit 3C | Clarias | MPVDMAVQLYITSSPPLHHRFLSSYKDYRVRNLISVNCKPLRPCINTKNTHNTSLNPPCSVWKAPEPKAKKKVVFADSKGMSLTAVRVFSPCENKKSDSQVQFQLPKLEVALKPVQSRILAFRQPATEYMEFRKRLMKNSVCLESCTLQGHTLTGTIKVRNVSFEKSVQVRITFDSWENHRDIECTFLNDVCGCRDTDTFSFIIEIPACVLPQDSVEFCVSYTCGGKTHWDNNNGKNYALVTTHDEKKDKTKETDLLDPFRNQQKRNRFTADWNSLMIGIRGPTW | Acts as a glycogen-targeting subunit for PP1 and regulates its activity. Activates glycogen synthase, reduces glycogen phosphorylase activity and limits glycogen breakdown. | T1SFR8 |
B3PMB4 | RSMH_META1 | rRNA (cytosine-N(4)-)-methyltransferase RsmH | Metamycoplasma | MEIKSDGTYVDLTLGRAGHSLEILKKLINGRLICFDKDNEAIKESYKKLQKISPNFTLIQNDFRFLKAELEKLGINEVDGILADLGVSSPQIDDPTRGFSYSQEGPLDMRMNQQNSFSAKDIIDNFDESELTKILIKNADVKLANLVAKAIVAKRPIKSTSELVEIIKNALPAKIVREKNPAKAVFQALRIEVNDELGALTAMLADATQLLKKDGKILIITFHSKEDSIVKNFFQKQNYVDPRLNKLPINIQKIWKQKIIFPSEDEKLQNNRSRSAKLRVVKKLSI | Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA. | B3PMB4 |
Q1J652 | OBG_STRPF | GTP-binding protein Obg | Streptococcus | MSMFLDTAKISVQAGRGGDGMVAFRREKYVPNGGPWGGDGGKGGSVIFRVDEGLRTLMDFRYNRKFKAKSGEKGMTKGMHGRGAEDLIVFVPQGTTVRDAETGKVITDLVEHGQEVVIAKGGRGGRGNIRFATPRNPAPEIAENGEPGEERQLELELKILADVGLVGFPSVGKSTLLSVVSSAKPKIGAYHFTTIVPNLGMVRTKSGDSFAMADLPGLIEGASQGIGLGTQFLRHIERTRVILHVIDMSASEGRDPYEDYVSINNELETYNLRLMERPQIIVANKMDMPEAQENLKAFKKKLAAQYDEFDDLPMIFPISS... | An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis control. | Q1J652 |
Q6H3C9 | PA2AC_TRIST | Phosphatidylcholine 2-acylhydrolase | Trimeresurus | MRTLWIMAVLLLGVEGSLIQFETLIMKVAKKSGMFSYSAYGCYCGWGGQGQPQDATDRCCFVHDCCYGKVTGCDPKMDIYTYSEENGDIVCGGDDPCRKAVCECDKAAAICFRDNKDTYDWKKYWRFPTKNCQESVPC | Snake venom phospholipase A2 (PLA2) that shows a moderate inhibition of ADP-induced human platelet aggregation when tested on platelet rich plasma. Exhibits high hydrolytic activities and prefers the anionic micelles (dPPC with deoxycholate) to the zwitterionic micelles (dPPC with Triton X-100). PLA2 catalyzes the calc... | Q6H3C9 |
A6WXC3 | ACCA_BRUA4 | Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha | Brucella | MYNYLDFEKPVADLEGQILELKKLAQEQGSVEMSDEIRRLEKRSADALKDIYRKLTPWQKTQIARHPDRPHCLEYIDRLFTEFTPLAGDRKFANDEALQTGFGRFNGQAVAIIGQEKGSDTKTRLKHNFGSARPEGYRKAVRIMEMADRFQLPLITFVDTAGAYPGVSAEERGQAEAIARSTAECLRLRVPVISIIIGEGGSGGAIAIAVANRVYMLEHSIYSVISPEGAASILWHDSTRAKDAASSMRITAQDLFDLKVIDGVIPEPMGGAHRGKEAVIDAAGDIITASLRSMKDIDGETLKQERRQKFLEIGRNI | 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. | A6WXC3 |
Q48JS3 | SYT_PSE14 | Threonyl-tRNA synthetase | Pseudomonas | MPTITLPDGSQRSFDHVVSVADVALSIGAGLAKATVAGKVDGKLVDACDLIENDASLQIITPKDQEGLEIIRHSCAHLVGHAVKQLYPTAKMVIGPVIDDGFYYDIAYERPFTPDDMAAIEQRMQQLIEKDYDVIKKVTPRAEVIEVFTARHEDYKLRLVEDMPNEQAMGLYYHEEYVDMCRGPHVPNTRFLKSFKLTKLSGAYWRGDAKNEQLQRVYGTAWADKKQLAAYIQRIEEAEKRDHRKIGKRLGLFHTQEEAPGMVFWHPQGWTLYQVLEQYMRKVQRENGYLEIKTPQVVDRSLWEKSGHWANYADNMFTTE... | 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). | Q48JS3 |
Q01497 | PEX3_PICAN | Peroxisomal membrane protein PER9 | Ogataea | MFQYCRDLVSRHKKKLLFGTGVIAVSYAVSSFVSNKLAELNERLKEENFAKEQIKRRFKQTQNDCYMTFLSLLPVLTEPIYEALKVEEITRELQNKRFERQKAKNAPVGNSTDPALSTVLSDDFSVHNEKENPMHTGVQQTKSKTQLWNELRNQSITRFLTLLYCESLLIVFLHLQLNILSRRSYLETAIKLASKTKGIKLENESNVDLDPANLFLENDEELAMGSSRQDENLAEQAFLSYSWWLLNKGWIDIKNQVESSVEDIFGDINPRQELSIEEFATLINKTQQIIDKQIYAEKESEPLTAPGHSSSTVITSLLPP... | Involved in peroxisome proliferation and/or membrane biosynthesis. Plays a role in the maintenance of the peroxisomal membrane in vivo. | Q01497 |
A0Q060 | MRAY_CLONN | UDP-MurNAc-pentapeptide phosphotransferase | Clostridium | MSLMIYSVLVAFVVSLIQGPILIPLLHKFKFGQNIRSEGPESHKKKSGTPTMGGVIFIISSVITVFVVSRHPSFETKLAIFAFVAFGIIGLIDDSLKIIHKENEGLKAYQKMILLLIVSSIIGFYAYNNPRIGSEIIVPFVHKTWNLGMFYIPFIIFYFAATTNAVNLTDGLDGLATSITLLVMTFFAVVSYATGNYNLAVFCSIVAGALLGFLKYNAYPAQVFMGDTGSLALGGVVGAVAMMLKLPLIVIIVGGIYLAEALSVILQVGSFKLRGKRIFKMSPIHHHFELSGWHETKIVSIFSIITVILCLIGFLSLIKM... | Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I... | A0Q060 |
Q7VLK1 | USPA_HAEDU | Universal stress protein A homolog | Haemophilus | MYKHILVAVDLSEESLILLRKGAGLAEKCGAKLSLIHVDVNFSDLYTGLIDINMSSVQDGVIEETTKALDELALKIDYPVSQRLNGTGDFSQVLEEAVAKYQIDLLITGHHQDFWSKFMSSTRQVMNNVTVDMLVVPLIDE | Required for resistance to DNA-damaging agents. | Q7VLK1 |
A5F2H3 | BIOB_VIBC3 | Biotin synthase | Vibrio | MEVRHNWTVAEVKALLDKPFMDLLFEAQQVHRLHHPHNHVQVSTLLSIKTGACPEDCKYCPQSAHYRTDVDKERLMEVERVLDAAQKAKNSGSTRFCMGAAWKNPKERDMPLLKEMIRGVKDMGLETCMTLGMLTPDQAQQLAQAGLDYYNHNLDTSPEFYGNIITTRTYQDRLDTLSHVRDAGMKICSGGIIGMGESTNDRAGLLVELANLPTHPESVPINMLVKVKGTPLEQVDDVEPFDFVRLIAVARIMMPKSAVRLSAGREKMNEQMQALCFMAGANSIFYGCKLLTTPNPAEDSDMLLFKKLGINREQVAQKPD... | Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism. | A5F2H3 |
P46217 | RPO11_SULAC | DNA-directed RNA polymerase subunit L | Sulfolobus | MEIKVIKEEQNYLELQIDGEEHTIGNLLKGMLLKVPGVKFAAYSLPHPLITSITIKILTDGSISAREALIKAIELAENYANLFIDEVKKI | DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | P46217 |
Q82TC0 | AROK_NITEU | Shikimate kinase | Nitrosomonas | MHFRYNYRMQRSKTPNTKNSDTGSIPGNIILIGMMGSGKTTVGKLLANLVGKTFIDIDHEIQRRTGVGIPVIFEIEGEAGFRKRESEVLRDIVRQQNIVLATGGGAILHPDNRALLRQHGTVVYLCAPVTELRRRTYLDKNRPLLQTGNVHAKLIELFTQRDPLYRETAHIIMDSGRQSARAFVQKLIQKLRQSNQEFTAAGSPPCVKPSE | Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate. | Q82TC0 |
P61666 | MUTS_DESVH | DNA mismatch repair protein MutS | Desulfovibrio | MTNPSPKLTPMFEQYLRIKEDYPDALLFYRMGDFYELFFDDAETTARELQIALTCRNPNAELKAPMCGVPYHAVEGYISQLLDKGYRVAICEQIEDPKEAKGLVKRAVTRVLTPGTVIDDANLDAKEHNYLGALFWNQDAEAGAFAWVDVSTGEWSGLYSRKLAELWQWAQKMAPRELLLPEGVDTPAMATLGTTQTVRVPARSHFDLKSGTERVMRAQGVADLGSLGLEGKPELVRACAALLAYLAQTQKQELSHLAPFKPLNLGRHLIIDEVTERNLELFHRLDGRKGPGTLWHILDRTLTPMGGRLLEERMHHPWRE... | This protein is involved in the repair of mismatches in DNA. It is possible that it carries out the mismatch recognition step. This protein has a weak ATPase activity. | P61666 |
M1VV66 | TCPD_CLAP2 | Tyrosine O-prenyltransferase tcpD | Claviceps | MPFMFETILSRVKWTANTLVARLTTLYEYEYPRTAKEETGIDKEYHIKLWDEDIGAMLVSMMRLAGYSEQSQKTHRIFFKEQVARSLGLYPTTYPHQSAWESFMTDDHTPVEMSWSWSGNTPTPVVRYAAEPISWHAGTASDPLNSEATTECLASTAPLAPSLDLRWYRHFLKHLVADDSDGQHDTTDHLSQEFIAFDLDKDSMTVKYYFLPTLKSLACGKTNLELMEESILSLPEADEAVRSSLKVLTTYIRAYPQDEQPQAEIFAVDCVNPANSRLKIYVRSRKTTFDSMLEMMTLGGQTPDLTRDAIDSLRELWCAC... | 4-O-dimethylallyl-L-tyrosine synthase; part of the gene cluster that mediates the biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) lacking the reactive thiol group important for toxicity . Firstly, L-tyrosine is prenylated by tcpD, before undergoing condensation with L-glycine in a reaction cataly... | M1VV66 |
Q6D7L7 | LPTE_PECAS | LPS-assembly lipoprotein LptE | Pectobacterium | MRHRLFTLVLGLAVLITAGCGFHLRGTTQVPAQLQTLVLDSSDPYGPLTRAVREQLRLSDVKIVDDATRQDIPSLRVLSSSETRDTVSIFQDGKTAEYQMVLTLQAQVLMPGEDIYPLSVTVFRTFFDNPLAALAKDAEQDIVRQEMREQAAQQLVRKLLTINGSQEVKNRLQSTDSPTAAKRS | Together with LptD, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane. Required for the proper assembly of LptD. Binds LPS and may serve as the LPS recognition site at the outer membrane. | Q6D7L7 |
Q71SG7 | GCNT4_DANRE | Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase 4 | Danio | MRRCAVLHRLRCKFYVFVVSLFVVVKLVYLKISMDNSIYIEPYGVTRRSLKPQPLDGINCTAIYDLEPVEIGKSLEMRRKKIVEVDDGRIASFTADCKSYIEQRRYNEVLVTDEECNFPIAYSLVVHKNSAMVERILRAIYAPQNIYCIHYDQKSTKDFIAAMKNLESCFPNVFIASKIESVQYAHITRLKADLNCLSDLLSSEVKWKYVINLCGQDFPLKSNYELVTELRKLNGANMLETSRPSKVKKQRFQFRYQLKDVSYEYQKMPVKTSIAKDPPPHNIEMFVGSAYFVLSRDFVTYVMNNQLAKDFLQWSVDTYS... | Glycosyltransferase that mediates core 2 O-glycan branching, an important step in mucin-type biosynthesis. | Q71SG7 |
Q8MJK1 | CBY1_BOVIN | PKD2 interactor, Golgi and endoplasmic reticulum-associated 1 | Bos | MPLFGSTFSPKKTPPRKSASLSNLHNLDRSTREVELGLDYGTPTMNLAGQSLKFENGQWIAETGISGGVDRREAQRLRRRNQQLEEENNLLRLKVDILLDMLSETTAESHLMEKELDELKSVSRRRK | Inhibits the Wnt/Wingless pathway by binding to CTNNB1/beta-catenin and inhibiting beta-catenin-mediated transcriptional activation through competition with TCF/LEF transcription factors. Has also been shown to play a role in regulating the intracellular trafficking of polycystin-2/PKD2 and possibly of other intracellu... | Q8MJK1 |
Q5NNW5 | ADE_ZYMMO | Adenine aminohydrolase | Zymomonas | MNNLIKFIAALPKAELHLHIEGSLEPELMFELAKRNKVTLPFPDVESVKAAYNFNNLQEFLDIYYQGTNVLKTEEDFCDLAMAYFYRAHRDNVLHSEIFFDPQSHTERGIPFNVVMNGLLAAITKAEAELGMSVQLIMCFLRHLDEESAFATLRMAEPFLDKIAGVGLDSSEVGNPPSKFRHVFAEARQKGLKLVAHAGEEGDASYIKEALDILNIDRIDHGNRITEDRLLMTRAARSAIALTICPLSNQKLQVVPDLRNHPLPYLLRQGLRVTINSDDPAYFGGYVNDNYKALAEYCGLKAADFVEIARNSFLGSFLPD... | Catalyzes the hydrolytic deamination of adenine to hypoxanthine. Plays an important role in the purine salvage pathway and in nitrogen catabolism. | Q5NNW5 |
B5YG33 | RS8_THEYD | 30S ribosomal protein S8 | Thermodesulfovibrio | MITDPISDMLTRIRNAIKVKADKVDIPASRMKIEISKILKEEGFIKSYKIIKDKKQGIIRINLKYTSEGDSVISNLQRISKPGRRVYVSKDEIPHVMGGLGVAILTTSQGVMTDKECRHKGVGGEVICYIW | 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. | B5YG33 |
Q9D9H3 | MB3L1_MOUSE | Methyl-CpG-binding domain protein 3-like 1 | Mus | MGKTSQRKQCDCENPSKPCLSTSIPLRMSSYTFKRPVTKITSHLGNEVRYYQWEETLEKPEQACWQKRLQGLQAYSSAGELLSTSDLAKTLKDLTSTDTVASASDTQATSIDITSVPTLESSSHLANMIPEAGPQILCKEFLVTEQDIINQERKVKIARERLAVALIAHKLASEMETVRGSRKANL | Transcriptional repressor. | Q9D9H3 |
Q7S2H8 | TPC1_NEUCR | Mitochondrial thiamine pyrophosphate carrier 1 | Neurospora | MSGKAERLKDEGSRLQVTAAGATAGLISRFVIAPLDVVKIRLQLQHHSLSDPLLHQRRAEIIGGGPVYKGTLPTIRHILRTEGLTGLWKGNIPAELLYVSYAAVQFTTYRSITQFLQAAFPKDQNKQLPPSVESFIAGASAGGVATAVTYPLDLLRTRFAAQGVERVYPSLVQALKTIYASEGVTGYFRGLGPGLAQIIPYMGTFFCVYETLRPRLSKLELPYSSGSAVAGVLASVMAKTGTFPLDLVRKRIQVQGPTRGMYVHKNIPVYDGGMVKTVATIVRREGVRGLYRGLTVSLFKAAPASAVTMWTYERALKLYI... | Mitochondrial transporter that mediates uptake of thiamine pyrophosphate (ThPP) into mitochondria. | Q7S2H8 |
B4F0D8 | MNMG_PROMH | Glucose-inhibited division protein A | Proteus | MFYPEHFDVIVIGGGHAGTEAAMAAARMGRQTLLLTHNIDTLGQMSCNPAIGGIGKGHLVKEIDAMGGLMATAIDHAGIQFRTLNASKGPAVRATRAQADRVLYRQAIRTTLENQPNLMIFQQPVEDLIVENDQVTGAVTRMGLKFRAKAVVLTVGTFLDGKIHIGLENYSGGRAGDPPSVSLSHRLRELPLRVGRLKTGTPPRIDARTIDFSQLAPQLGDNPMPVFSFLGNVDQHPEQMPCHITHTNEQTHEIIRNNLERSPMYAGVIEGIGPRYCPSIEDKVMRFADRNSHQIFLEPEGLTSNEIYPNGISTSLPFDV... | 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. | B4F0D8 |
B2IU73 | GLMU_NOSP7 | Glucosamine-1-phosphate N-acetyltransferase | Nostoc | MVVVAILAAGRGTRMKSRLPKVLHSLGGQSLVERVIESVEPLSPSRRIVIVGYQSEEVQTAMHSIPNLEFVEQTVQLGTGHAIQQLLPHLKDYTGDLLILNGDLPLIRSETLKQMLQTHAQNQNAATILTSHLPDPTGYGRVFCNNENIVQQMVEHKDCTAAQRQNQRINAGVYCFRWPDLAKVLPHLQANNAQKEYYLTDAVTQVGQVMAVDVEDNQEILGINDRLQLATAYEILQKRVKEKWMLAGVTLIDPASITIDETVELQPDVIIEPQTHLRGNTVIQTGSHIGPGSLIENSQLAENVTVQYSVVIDSTIQAGS... | Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted ... | B2IU73 |
Q9KDX6 | GLGA_HALH5 | Starch [bacterial glycogen] synthase | Halalkalibacterium (ex Joshi et al. 2022) | MNVLHVASECNPFFKTGGLADVLGSLPKALIKQGINVSVILPKYGHLSDEWQNQLTLKKSFTVSVTWRNQYCGLEQFVDQGVTYYFIDNEYYFKRERLYGYLDEAERFTFFNHAVLSSLPFLDESPDLIHCHDWQSGLIPAYMKTGSVENPVPTVFTIHNLRYQGAFPPDVFRELLHFAPEHFAGLEMDGAINFLKGALVHSDRVTTVSPTYAQEIQTPAFGEGLHGLLHQERGKTRGILNGIDLEDFDPKTDPHVTYPYKHNQMEKRKNKQVIQRLFELPERKDIPLIAMVSRLVEEKGVPLLTQIAGELVTTENVQLA... | Synthesizes alpha-1,4-glucan chains using ADP-glucose. | Q9KDX6 |
A6GWB6 | SYD_FLAPJ | Aspartyl-tRNA synthetase | Flavobacterium | MYRSHNCGELNATHINKEVTLAGWVQKSRDKGFMNWVDLRDRYGITQLMFDESRSDKTVFELAKTLGREFVIQVKGTVIEREAKNKNISTGEIEILVTQMTILNSSLTPPFTIEDETDGGEDIRMKYRYLDIRRNPVKNSLLFRHKVAMEVRKYLSDLDFCEVETPYLIKSTPEGARDFVVPSRMNEGQFYALPQSPQTFKQLLMVGGMDKYFQIVKCFRDEDLRADRQPEFTQIDCEMAFVEQEDILNIFEGLTRHLLKELKGIEVEKFPRMTYNHAMKTYGNDKPDIRFGMEFGELNEYAKHKDFPVFNAAELVVAIA... | Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp). | A6GWB6 |
Q2S8W2 | PANC_HAHCH | Pantoate-activating enzyme | Hahella | MITIHRVKDLRAAIRQQRTQGKRIGLVPTMGNLHAGHVSLVKQAKELCDYVVTSIFVNPLQFGANEDLDKYPRTLDADKEKLVAAGNHLLFTPEVSQLYPEGLERHTKVITPGLSELHCGASRPSHFTGVTTVVSMLFNMVQPDVAIFGEKDFQQLAVIRKMTRDLYLPIVIESGPTLRETDGLAMSSRNGYLSAEQRQTAPLLYKLLQESAEQIENGDKDFAAISAEANNRLTKAGFVPDYFNIVNSDTLSPAVPSDSDITILAAAYLGTTRLIDNISVHLG | Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. | Q2S8W2 |
B2I3A5 | LGT_ACIBC | Phosphatidylglycerol--prolipoprotein diacylglyceryl transferase | Acinetobacter calcoaceticus/baumannii complex | MLTYPNIDPVAIHLGPLQVHWYGLMYLLAFLCAWGLASYRAKQRDGWTSDMVSDLVFYGALGVVLGGRIGYVLFYEFDKFLENPIWLFQVWTGGMSFHGGFLGVMIAMLFWCKKYQKTWFQTLDFIAPCVPTGLMFGRIGNFIGGELYGRAVTDPNYPFGMIFPTDPLHLVRHPSQIYQALCEGLLLFIILWWFSSKPRPRMAVSALFLMGYGVARFVMEFFRQPDADQGFILFGWMTKGQILTVPMLLIGLWMMWYAYQKKIYDWGPQKNS | Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins. | B2I3A5 |
Q8ZST5 | PSB2_PYRAE | Proteasome core protein PsmB 2 | Pyrobaculum | MGEEVQIGATAVGIKAKDGVVLAAEKRVSYGFYTLSSAGKKVFVIDDKLAIASAGIIADMQTLAKILKLNAKAYELEMKRKPSTHSMARLLSVIMFSRRFMPFFAEVLVGGIDEEGPHLIVMDPLGSLIEDNYAALGTGAKLAVAVLDTGYRPDITVEEAKKLAVQALKAAIERDPVSGGGIDLAIVDKNGAREEEVRVQLLI | Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. | Q8ZST5 |
A4TBE2 | SEPF_MYCGI | Cell division protein SepF | Mycolicibacterium | MSTLHKVKAYFGMAPMDEYEDDYYEDDDRGPAPRGYRRPREDRFEDEGYAPRGYDGHPEDRRRDYDEPPAYRAGLAGGMPGGFDDARFEARMRAPREFDRTPPRFGAMRGSTRGALAMDPRGMAELFEAGSPLAKITTLRPKDYSEARTIGERFRDGTPVIMDLVSMDNADAKRLVDFAAGLAFALRGSFDKVATKVFLLSPADVDVTAEQRRRIAEAGFYSYQ | Cell division protein that is part of the divisome complex and is recruited early to the Z-ring. Probably stimulates Z-ring formation, perhaps through the cross-linking of FtsZ protofilaments. Its function overlaps with FtsA. | A4TBE2 |
Q4QK57 | POTA_HAEI8 | Spermidine/putrescine import ATP-binding protein PotA | Haemophilus | MENQPQNKPIIELRSIKKSYGSNTIINDFNLAINNGEFVTILGPSGCGKTTVLRLLAGLEELDSGSIILDGEDITNVPAEKRHINTVFQSYALFPHMTIFENVAFGLRMQKVPNEEIKPRVLEALRMVQLEEMADRKPTQLSGGQQQRIAIARAVVNKPKVLLLDESLSALDYKLRKQMQQELKMLQRQLGITFIFVTHDQEEAITMSDRIVLLRKGKIAQDGSPREIYEDPANLFVARFIGEINVFEATVIERKSEQVVLANVEGRICDIYTDMPVEKDQKLQVLLRPEDIVIEELDENEHSKAIIGHIIDRTYKGMTL... | Part of the ABC transporter complex PotABCD involved in spermidine/putrescine import. Responsible for energy coupling to the transport system. | Q4QK57 |
Q5WTA1 | MIAA_LEGPL | Isopentenyl-diphosphate:tRNA isopentenyltransferase | Legionella | MNKLVFCLMGPTASGKTGLACELLTHFPFEIISVDSAMIYRDMNIGTAKPSIHELQSAPHYLIDIKDPVESYSAAQFCTDALSLCAAIIKRGNIPLLVGGTMMYFNALQKGLATLPEADEAVRKRLEEEALSQGWDFLYQKLSQLDPVTAARIHAHDTQRIQRALEVYYLTGSTLSTYLTGPHEQPDYCFVNLALFPEQRSWLHERIAQRFDAMLSEGFIEEVQQLQAKWPIQINLPSMRCVGYRQILEYLAGHYDYETMREKGIAATRQLAKRQLTWLRHWEGALFYDSQNVGFNTDIIAKIREILDNTVSN | 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). | Q5WTA1 |
Q8MY85 | FGFR2_DUGJA | DjPTK1 | Dugesia | MLNKFIVIVTMLAMWNYAQDCNFELSKNETVQFTSFLPLILNCASISKFDTDLCETINDERPYNWYFQNKKIGNETKGKIKLVSSSQQMIIFNGSASDEGNYMCETINNNKEFISKTFDARMIEPSMTQMELLLNSFPNDHQEEINGRIYWLPEMILNHIRDVVIINQGAESDLHSFYYVSGSDSQISTFDVQWYFHYQPKSEDKTIIDHNIKTFYSSCNDLDLLPRKVNGSCYSSRLYLYNVEIKDQGFYSVEATLRMKNGSSHGLNFTYELKINIANILDPDKTNSILSTPQISFNLNSRVCINDRFDWICKVTPVVS... | Receptor for basic fibroblast growth factor. | Q8MY85 |
Q7N870 | PANC_PHOLL | Pantoate-activating enzyme | Photorhabdus | MLIVETVPILRREIRRWRQEGKRIALVPTMGNLHDGHMTLVDTAKGQADIVIVSIFVNPMQFNRPDDLAKYPRTLQEDCEKLHQHGVNLVFAPADKEIYPDGMEHQTYVDVPELSTMLEGASRPGHFRGVSTVVSKLFNLVQPDLTYFGEKDFQQLQLIRKMIADLAYDITLVSVPTVRDQNGLALSSRNNNLTADEHRIAPELSKIMRSIAEKMAQGERHTEQLLTQASSQLHEAGFVPDELFIRDAETLAPLNTESKKAVILMAAWLGQTRMIDNQQVDLTQ | Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. | Q7N870 |
Q96A58 | RERG_HUMAN | Ras-related and estrogen-regulated growth inhibitor | Homo | MAKSAEVKLAIFGRAGVGKSALVVRFLTKRFIWEYDPTLESTYRHQATIDDEVVSMEILDTAGQEDTIQREGHMRWGEGFVLVYDITDRGSFEEVLPLKNILDEIKKPKNVTLILVGNKADLDHSRQVSTEEGEKLATELACAFYECSACTGEGNITEIFYELCREVRRRRMVQGKTRRRSSTTHVKQAINKMLTKISS | Binds GDP/GTP and possesses intrinsic GTPase activity. Has higher affinity for GDP than for GTP. In cell lines overexpression leads to a reduction in the rate of proliferation, colony formation and in tumorigenic potential. | Q96A58 |
O48665 | LGB5_PEA | Leghemoglobin Lb120-29 | Pisum | MGFTDKQEALVNSSWELFKQNPGYSVLFYNIILKKAPATKGMFSFLKDSAGVVDSPKLQAHAEKVFGMVHDSAVQLRVSGEVVLGDATLGAIHIQKGVVDSHFVVVKEALLETIKEASGEKWSEELSTAWEVAYEGLASAIKKAMS | Provides oxygen to the bacteroids. This role is essential for symbiotic nitrogen fixation. | O48665 |
O45526 | LSY27_CAEEL | Zinc finger protein lsy-27 | Caenorhabditis | MTSIHSPVTRKEDTELKRPDLRGKFVCSSCSQNFQHSASLNRHRQLMHSNEHTCMMCERALNQKETIREHMRNEHNLAQVFTCGCCNWTFASKRQLTEHTKCIQGTGAPGDTIPIAKSINAPGSLIQSTIQGTPPVVKTGRKRPMGGSLSPSSSVSTSISSRDASGSPPPTEEEAERKVLFDNAVDTILQSKFFTYQQITEVDTWVKIIESANTLADTLQRIKKSQKVKAEGPAVESKMIPEKHVKQEIE | Involved in regulating left/right asymmetric differentiation of the gustatory ASE neurons . Plays a role in modulating expression of LIM/homeobox protein lim-6 . | O45526 |
Q331Q7 | GERKI_STRSQ | dTDP-4-keto-6-deoxyallose reductase | Streptomyces | MTADRWAGRTVLVTGALGFIGSHFVRQLDARGAEVLALYRTERPEIQAELAALNRVRLVRTELRDESDVRGAFKYLAPSIDTVVHCAAMDGNAQFKLERSAEILDSNQRTISNLLNCVRDFGVGEVVVMSSSELYSASPTVAAREEDDFRRSMRYTDNGYVLSKTYGEILARLHREQFGTNVFLVRPGNVYGPGDGFDCSRGRVIPSMLAKADAGEEIEIWGDGSQTRSFVHVADLVRASLRLLETGKYPEMNVAGAEQVSILELAGMVMAVLGRPERIRLDPSRPVGAPSRLLDLSRMSEVIDFDPQPLRAGLEETARW... | Catalyzes the stereospecific reduction of the C-4 keto group of dTDP-4-dehydro-6-deoxy-D-allose, leading to dTDP-6-deoxy-D-allose, an intermediate in the biosynthesis of the mycinose moiety of dihydrochalcomycin (GERI-155) antibiotic. Cannot directly reduce dTDP-4-dehydro-6-deoxyglucose, and thus acts after the epimeri... | Q331Q7 |
Q94JG1 | NRT23_ORYSJ | High-affinity nitrate transporter 2.3 | Oryza sativa | MEAKPVAMEVEGVEAAGGKPRFRMPVDSDLKATEFWLFSFARPHMASFHMAWFSFFCCFVSTFAAPPLLPLIRDTLGLTATDIGNAGIASVSGAVFARLAMGTACDLVGPRLASASLILLTTPAVYCSSIIQSPSGYLLVRFFTGISLASFVSAQFWMSSMFSAPKVGLANGVAGGWGNLGGGAVQLLMPLVYEAIHKIGSTPFTAWRIAFFIPGLMQTFSAIAVLAFGQDMPGGNYGKLHKTGDMHKDSFGNVLRHALTNYRGWILALTYGYSFGVELTIDNVVHQYFYDRFDVNLQTAGLIAASFGMANIISRPGGGL... | Involved in nitrate transport, but does not seem to be able to mediate transport by its own. Acts as a dual component transporter with NAR2.1. Imports nitrate with high affinity when expressed with NAR2.1 in a heterologous system (Xenopus oocytes). Plays a key role in long-distance nitrate transport from root to shoot ... | Q94JG1 |
Q8DKQ1 | HSLO_THEVB | Heat shock protein 33 homolog | Thermosynechococcus | MADFLLRATAAAEGIRAVGVITTQLTDEARKRHQLSYVATAALGRTMAAGLILASSFKQPQARVNVRIQGNGPLGTIFADAGADGTVRGYVQYPSVELPPNAKGKLDVGAAVGHQGYLYVIHDLGYGYPYSSTVELVSGEIAEDITYYLATSEQTPSALMLGVFVEESGVTAAGGLMLQVLPKAANDEHLIATLEQRVANLKGFTPLLQAGRTLPDIFQELLGDMDLQILPQRQMVRFHCGCSHERMLAALKLLGEAELRDILATEAKAEATCQFCNAVYWADQPMLEQLIAELATASV | Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. | Q8DKQ1 |
B3E7T5 | RL3_TRIL1 | 50S ribosomal protein L3 | Trichlorobacter | MNKGIIGKKLGMTQIFLEDGTRVPVTVVQAGPCVVLQKKTAEVDGYSAVQVGFETVNAAKANSADRGHCVKAGKGVFRHLRELKLEQEAELNIGDELTVQQFEPGDLIDVTGTSIGKGFQGVIKRHNFKGGRASHGSRFHRAPGSIGCSATPSRVFKNKKMPGQMGNERVTVQRLQVVRVDADQNLILIKGAIPDSKNNVVVIKDSVKATK | One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit. | B3E7T5 |
A5VR14 | RPOC_BRUO2 | Transcriptase subunit beta' | Brucella | MNQEVMNLFNPQAPAQTFDSIRISIASPEKILSWSYGEIKKPETINYRTFKPERDGLFCARIFGPIKDYECLCGKYKRMKYKGIICEKCGVEVTLSRVRRERMGHIELAAPVAHIWFLKSLPSRIGTLLDMTLKDIERVLYFENYIVTEPGLTSLKEHQLLSEEEYMIAVDEFGEDQFTALIGAEAIYELLASMELEKIAADLRVDLAETTSDLKQKKLMKRLKIVENFLESGNRPEWMIMKIVPVIPPDLRPLVPLDGGRFATSDLNDLYRRVINRNNRLKRLIELRAPGIIIRNEKRMLQEAVDALFDNGRRGRVITG... | DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | A5VR14 |
C4XTD0 | SYP_SOLM1 | Prolyl-tRNA synthetase | Solidesulfovibrio | MRLSRYYAPTLKETPAEAEVISHKLLLRAGMIRKLTAGIYTYLPLGLKALNNVAKIVREEMDRAGALEILMPAVQPADLWKESGRWDFYGRELLRFVDRHDRESCLGPTHEEVVTDLVRHEIRSYRQLPVNLYQIQTKFRDEIRPRFGLMRGREFVMKDAYSFDKDDSGADASYWGMYEAYARIFKRLGLKFRAVAADSGAIGGSFSHEFMVLADTGEDTIVACPACDYGANVEKAEAICPPAGDLAPCPAAEKIATPGQHTVEELAAFLKVPVASVIKTLLYVADGKTVAALVRGDRELNEVKFKNLLDAKEDLRLATP... | 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... | C4XTD0 |
P45186 | MUKE_HAEIN | Chromosome partition protein MukE | Haemophilus | MTDIQDVISPKLAVAIANPIFPAVDSLLRSGRHISTEHLDNHAFLMDFQNELDGFYRRYNVELIRAPEGFFYLRPKATTLIARSVLSELEMLVGKVLCYLYLSPERLAQQGIFSTQEVYDELLNLADEGKLLKAVNQRSSGSDLDKQKLAEKVRAAIGRLRRLGMIQTVGEQNSGKFTISESVFRFGAEVRSGDDPLESQARLIRDGEAATPDSLALEKQAQLMENDTKSADEIDEEFDGEQE | Involved in chromosome condensation, segregation and cell cycle progression. May participate in facilitating chromosome segregation by condensation DNA from both sides of a centrally located replisome during cell division. Probably acts via its interaction with MukB and MukF. | P45186 |
Q89AF2 | FTSH_BUCBP | ATP-dependent zinc metalloprotease FtsH | Buchnera | MAKNLMLWLVIAVVLMSIFQNFSANNINNRKIDYSTFLSDVNQDQVREVHISGREMNIIRKDNGRYITYIPISDPKLLDNLLVKNVKIIGAAPEEQSFFTAIFISWFPMLLLIGVWVFFMRQMQVGGGKGAMSFGKSKARMLPEDQVKITFSDVAGCDEAKEEVQELVEYLKEPSRFQKLGGKIPKGILMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFEHSRKVAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQMLVEMDGFDGNEGIILIAATNRPDVLDPALLRPGRFDRQIFVA... | Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins. | Q89AF2 |
Q760S6 | RBS_NEODN | Ribulose bisphosphate carboxylase small subunit | Neoporphyra | MRLTQGTFSFLPDLTDEQINKQLTYIVSKGLSANVEYTDDPHPRNSYWELWGLPLFDVKDASAVMYEISSCRKAKPNYYVKVNAFDNTRGIESCVMSFIVNRPANEPGFLLQRQDFEGRTMKYSLHSYATEKPEGARY | RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site. Although the s... | Q760S6 |
Q59YD8 | NOP16_CANAL | Nucleolar protein 16 | Candida | MTSVRKRKMARSSVKKNTRRTKDKQRNINIHSNPIIEANWDKSLTLKQNYKRLGLRAKLGRSAGGDERKVESLSELQAKREKNQKNQSKHVPTVSEIENLDDPSRIPEGEARLIRDPETNEVIKVIYGTMKVDDKDESEEEIENPSVIKQLEEYAEKNSKIKKERHQSERENDWIKSLYEKYGDDYDKMKWDKKLNIYQQSAGDLKRRIIKWKKANGI | Involved in the biogenesis of the 60S ribosomal subunit. | Q59YD8 |
L7WRQ4 | NOTA_ASPVE | Notoamide biosynthesis cluster protein A' | Aspergillus subgen. Nidulantes | MTNTNRRTITVYGATGAQGGPVVRSLLKNNAFKVRAITRKPESEAAKALADLGAEIVQGDGWKKEQMVAAFSGSWAAFVNTNSDDPCFWDANHPTEFDLGKIIIDGIIQAGTVKHLVYSSFVDTSSFTNGQAIIEAADEKSKIERYAASSGHFDTVCPLYQGWYMDVFRGQEYAHALGGFPYFEDEDKFRTLRLPRWGTHTDMPLPWISLEDDFGDIVHGIFLTPEDYNGRVVPTVSDIRTYPEMIDAFQSGMPSLFWFLVCRLTSVHALATGQKARYIPVTDWEAHFGDSHHGKESLAIFKFGKFTNGKYFGDEPISTD... | NmrA-like family domain-containing oxidoreductase; part of the gene cluster that mediates the biosynthesis of notoamide, a fungal indole alkaloid that belongs to a family of natural products containing a characteristic bicyclo[2.2.2]diazaoctane core . The first step of notoamide biosynthesis involves coupling of L-prol... | L7WRQ4 |
B2FQ14 | RF1_STRMK | Peptide chain release factor 1 | Stenotrophomonas maltophilia group | MTPTLRRKLEALAERREELERLLAEPDVVADNTRFRDLSREFAQLEPIAIALADESRAKADLAAAEGMRADPDLRELADEEIAAAQARLLELEQELALLLVPRDPRDEGNLFLEVRAGTGGDEAAIFAGDLFRMYARYAERQGWKVEIESDNPGEHGGYKEVVARVVGRGAFSRLKFESGTHRVQRVPATESQGRIHTSAATVAIIPEADEVDDIVINPADLKVDTFRSSGAGGQHVNKTESAIRITHVPTGVVVECQTERSQHANRDKAMKRLKAQLLDAERQRQDAAQAESRRLQVGSGDRSQRIRTYNFPQGRITDH... | Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA. | B2FQ14 |
P0C8J5 | SL2C2_VIPAA | Snaclec factor X-activator 2 light chain 2 | Vipera | AFCCPSGWSAYDQNCY | Regulatory subunit of the blood coagulation factor X-activating enzyme. Activates coagulation factor X (F10) in a calcium-dependent manner by cleaving the Arg-Ile bond at position 234. Weakly hydrolyzes insulin B chain, fibrinogen and some components of the extracellular matrix in vitro, but does not activate prothromb... | P0C8J5 |
P21909 | EDD_ZYMMO | 6-phosphogluconate dehydratase | Zymomonas | MTDLHSTVEKVTARVIERSRETRKAYLDLIQYEREKGVDRPNLSCSNLAHGFAAMNGDKPALRDFNRMNIGVVTSYNDMLSAHEPYYRYPEQMKVFAREVGATVQVAGGVPAMCDGVTQGQPGMEESLFSRDVIALATSVSLSHGMFEGAALLGICDKIVPGLLMGALRFGHLPTILVPSGPMTTGIPNKEKIRIRQLYAQGKIGQKELLDMEAACYHAEGTCTFYGTANTNQMVMEVLGLHMPGSAFVTPGTPLRQALTRAAVHRVAELGWKGDDYRPLGKIIDEKSIVNAIVGLLATGGSTNHTMHIPAIARAAGVIV... | Catalyzes the dehydration of 6-phospho-D-gluconate to 2-dehydro-3-deoxy-6-phospho-D-gluconate. | P21909 |
A0T0K0 | RPOA_PHATC | Plastid-encoded RNA polymerase subunit alpha | Phaeodactylum | MNNISIKCLKSEKIQSGACHGQFLINSLNPGQGITIGNQLRRVLLGDLGGVAISAVRIAGITHEFSTIPGVREDILEILLNLKGIICTSQIQDTQFGHLKVQGPSVVTADLIQLPPGVEIINPNHYIATISTSNILEIEFKFEYGSGYHLASQNFVEEDENYLQLDTIFMPVQKVDFKIENIYDATNNISERLFLDIWTNGSISPNDALESAAQVIIDLFTLLINNKNINNNNRLELKPETISIEPYTNIAIEELQLSVRAYNCLKKAQINTVGDLLQYSPEKLQELKNFGRKSADEVFSTLKNKLGIILK | DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | A0T0K0 |
A2Q7V4 | MEP_ASPNC | Fungalysin mep | Aspergillus subgen. Circumdati | MHGLRLVCSIGTLPLVILAYPAASLHTTSAAVDLDSLRLTSNSEYVNSVHVDTNRSVAVSAEEHYTDTAARLVQNIVPGASFRLIDDHFVGDNGVAHVYFRQTLHGIDIDNADFNVNIGKDGLVLSFGHSFFTGALPSSHLDNTNVLSPEAALRGARDAIQLPLTIDNVSTEAAEGRNEYIFREAVGAVSDPKAKLVYLVKPEGTLALTWRIETDMYEHWLLTYIDAETTTVHGVVDYVADATYQVYPWGTNDPAEGHRTIVTDPWDLSASAYTWISDGRDNYTTTRGNNAIAHWNPTGGGSYLYNLRPSDPNLNFQWPY... | Secreted metalloproteinase that allows assimilation of proteinaceous substrates. | A2Q7V4 |
Q98QL0 | RNR_MYCPU | VacB protein homolog | Mycoplasmopsis | MKNLVLQNLKSNKAYSFLEIARINKINPNFNSQLSKALFSLLDQGLIVKNNDGNFIKVNEIKKIQGIFKQSNRNFAFIETADEQSYFVAKAHFNGAINSFEVEAIVYESPFEKDKKYAVVKKILKNTHPEIIGFIKISNGIKYFNAFEESFRSYKFFVDQNIDVEEDDVILVVVEKIVDQKIYVNFVKKVSTLKSNFYQIDIVLEKSKTIIDFPEDVLDESALIEDHVIEKDYQNRKDLRDKLIITIDGEDTKDFDDAIYVEKNKDHFLLSVHIADVAHYVKENSAIDKEALRRATSIYLPHMVIPMLPEKLSNGICSLN... | 3'-5' exoribonuclease that releases 5'-nucleoside monophosphates and is involved in maturation of structured RNAs. | Q98QL0 |
A9HRJ3 | YQGF_GLUDA | Putative pre-16S rRNA nuclease | Gluconacetobacter | MPLFNMHQIRGQLGRDQRLLGLDPGQKTIGLALSDVSLMLASPYGALRRGKLSVVAAEIRRIAAREGVGGLVSGLPLSMDGSFGPAAQAARDWMISLSEQVGLPAAMWDERLSSSAVNRMLIQDADMTRQRRAELVDKLAASYMLQGALDATAE | Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA. | A9HRJ3 |
Q5WEP5 | HEM3_ALKCK | Pre-uroporphyrinogen synthase | Alkalihalobacillus | MRKIVIGTRRSKLALTQTNWVIDQLKQLGVPYEFEVKEIVTKGDRILDVTLSKVGGKGLFVKEIEAALRSGEIDVAVHSMKDVPSELLEEFTLAAITEREDPRDVLVSENGHTLDELPAGAIVGTSSLRRSAQILHRRPDVQVKWIRGNVETRLRKLKEEDFSAIVLAAAGLKRLGYGEDVITEYLDKDVCLPAIGQGALGLECRVDDVETTELLAKLHHEETGKAVLAERAFLKEMNGGCQVPIGGYATVLEDGAVFLTGLVGSPDGKTILKEGKCGMVADELGKEVSSLLTAQGAGAILEKVRSELEGS | Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps. | Q5WEP5 |
E3QDQ4 | MAP21_COLGM | Peptidase M | Colletotrichum graminicola species complex | MGSKTPEEQIPGGNGGPPSTGPSSSGGEPRGTHLSRDGDGSLGDHGDDDDADEDDVSSRPLRADVEEKKKKKRPKKKKKPAAAKEQSSPPRVPLSDLFPLGEYPAGEDLVYDRVPQPDANTARTTTAELRYQSRKHLEDPALLNDYRKAAEVHRQVRHWVQEAVKPGWTLLDIATGIEDGVRSLLANQGIEPGDNLRSGMGFPTGLCLNHETAHYTPNPGQRDVVLQHGDVMKVDYGVQVNGWIVDSAFTMSFDPTYDNLLAAARDATNSGIKAAGIDVRICDVSAEIQEAMESYEVEIRGKTYPVKAVRNICAHDIKRY... | Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). | E3QDQ4 |
A4XHM5 | RISB_CALS8 | 6,7-dimethyl-8-ribityllumazine synthase | Caldicellulosiruptor | MRTFEGSFCGKDLKLAIVVSRFNSFITDELLKGCLDGLSRHDVDSENIDVYYVPGAFEIPLVAKKLAKSKKYNAIIALGAVIRGSTPHFEYVSAEVSKGIANVSLEQEVPVIFGVLTCDTVDQAIERAGTKAGNKGFDAALSALEMANLMKNISES | Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin. | A4XHM5 |
Q65Q27 | RHAT_MANSM | L-rhamnose-H(+) transport protein | Basfia | MGGSILLGIFWHFVGATSAACFYAPMKKVTNWSWETMWAIAGIFSWILLPWGISYWLLPDFGSYYSFFGSDILLPVFLFGAMWGIGNIGYGLTMRYLGMSMGIGIAIGITLIVGTLMTPIIQGRFGELLASTGGQMTLIGVVIAVVGVAVVSYAGLLKEKAIGVTAEEFNLKKGLALAVMCGIFSAGMSFAMSAATPMHEEAARLGVDPLYVALPSYVVIMGGGAIINLGFCIIRLITRPELSFKADMSVVKGLLISNILFSALGGIMWYFQFFFYAWGHANIPANYGFMSWMLHMSFYVLCGGIVGLLLHEWKDTGKKP... | Uptake of L-rhamnose across the cytoplasmic membrane with the concomitant transport of protons into the cell (symport system). | Q65Q27 |
Q7N486 | TRPB_PHOLL | Tryptophan synthase beta chain | Photorhabdus | MSKLNPYFGDFGGQFVPQILIPALEQLEAAFIAAQQDPEFQQEFQDLLKNYAGRPTALTLCRNLTKGTKTRLYLKREDLLHGGAHKTNQVLGQALLAKRMGKNEIIAETGAGQHGVATALTCALLNMKCRIYMGAKDVERQSPNVFRMRLMGAEVIPVHSGSATLKDACNEALRDWSGSYDKAHYLLGTAAGPHPYPTMVREFQRMIGEEAKSQILAREGRLPDAVLACVGGGSNAIGMFAEFIPETSVRLIGIEPAGLGIETGKHGAPLKHGKLGIYFGMKSPMMQTDEGQIEESYSISAGLDFPSVGPQHAYLNSIGR... | The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. | Q7N486 |
Q8U0K5 | IF1A_PYRFU | Translation initiation factor 1A | Pyrococcus | MLMPKKERKVEGEEVIRVPLPEGNQLFGVVEQALGAGWMDVRCEDGKVRRCRIPGRLRRRVWIKVGDLVIVEPWPVQSDKRGDIVYRYTQTQVEWLLRKGKISQEFLTGGSLLLE | Seems to be required for maximal rate of protein biosynthesis. Enhances ribosome dissociation into subunits and stabilizes the binding of the initiator Met-tRNA(I) to 40 S ribosomal subunits. | Q8U0K5 |
B8E2A8 | RS20_DICTD | 30S ribosomal protein S20 | Dictyoglomus | MANTKSAIKRIKISERNRIRNRVRLGKIKFYTKQFLKFLNENNIEEAKKILPEVISAIDKAAQKGTLHKNTAARKKSKLMKLLNQKLSANLSS | Binds directly to 16S ribosomal RNA. | B8E2A8 |
A1USL0 | RS7_BARBK | 30S ribosomal protein S7 | Bartonella | MSRRHRAEKREINPDPKFGDVVITKFMNAIMFDGKKSVAERIVYGALDVVEGKVKTDPVALFHQALENVAPHIEVRSRRVGGATYQVPVDVRPDRRQALAIRWLIKAARGRNETAMIDRLSGELVDAANNRGTAVKKREDVHRMAEANRAFSHYRW | 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. | A1USL0 |
Q6D4A2 | RUVB_PECAS | Holliday junction ATP-dependent DNA helicase RuvB | Pectobacterium | MIEADRLISADAVPEEEFLDRAMRPKLLKEYVGQPQVREQMEIFIQAARKRGDALDHLLIFGPPGLGKTTLANIVANEMGVNMRTTSGPVLEKAGDLAALLTNLEPHDVLFIDEIHRLSPVVEEVLYPAMEDYQLDIMIGEGPAARSIKLDLPPFTLIGATTRAGSLTSPLRDRFGIVQRLEFYNVADLQYIVGRSAQCLGLDLTQEGSLEVARRARGTPRIANRLLRRVRDFSEVKSEGAITGTVATQALDMLAVDTEGFDYMDRKLLLAIIDKFMGGPVGLDNLAAAIGEERETIEDVLEPFLIQQGFIQRTPRGRMA... | 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. | Q6D4A2 |
P56823 | HCYG_HELPO | Hemocyanin, beta-C chain unit G | Helix | DIHTTAVAGVGVRKDVTRLTVSETENLREALRRIKADNGSDGFQSIASFHGSPPGCEHENHSVACCIHGMANFPQWHRLYVKQWEDALTAQGAKIGIPYWDWTTAFTELPALVTEEVDNPFHHGTIYNGEITTRAPRDKLFNDPEFGKESFFYRQVLLALEQTDYCDFEVQYEISHNAIHSWTGGQSPYGMSTLEYTAYDPLFLLHHSNVDRQFAIWQALQKFRGLPYNSANCAIQLLHQPMRPFSDADNVNPVTRTNSRARDVFNYDRLNYQYDDLNFHGLSISELNDVLERRKEKARIFAEFLLHGIGASADVTFDLC... | Hemocyanins are copper-containing oxygen carriers occurring freely dissolved in the hemolymph of many mollusks and arthropods. | P56823 |
P28495 | CAPZA_YEAST | F-actin-capping protein subunit alpha | Saccharomyces | MSSSKFEEVINKIINDSPPGELREVYDDLIKITSENSKNTILDAIENYNVQNCIPIEVNGNSVIISKYNKEGAKFFDPVNSVIFSVNHLERKGLDIEPYEFTHAKIEKGQLKELHDKLHEYLLQSFPGDVSFAVYPVPEEISKISIIIVSTKYNPNNFWNGHWRSSYIYDLETRELSGQISTQVHYYEDGNVSFQSGKDINQSNVDDVVCTIRDIETNFENDLDLSFFDLNEKQFKALRRRLPVTRSKINWGSAIGSYRLGKNAAEGK | F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. | P28495 |
B7NDQ3 | AROE_ECOLU | Shikimate dehydrogenase (NADP(+)) | Escherichia | METYAVFGNPIAHSKSPFIHQQFAQQLNIEHPYGRVLAPINDFINTLNAFFSAGGKGANVTVPFKEEAFARADELTERAALAGAVNTLKRLEDGRLLGDNTDGIGLLSDLERLSFIRPGLRILLIGAGGASRGVLLPLLSLDCAVTITNRTVSRAEELTKLFAHTGSIQALGMDELEGHEFDLIINATSSGISGDIPAIPSSLIHPGIYCYDMFYQKGKTPFLAWCEQRGSKRNADGLGMLVAQAAHAFLLWHGVLPDVEPVIKLLQQELSA | Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA). | B7NDQ3 |
A6TVI5 | HPRK_ALKMQ | HPr(Ser) kinase/phosphorylase | Alkaliphilus | MKSITVEKLMKDLNMEELNSIEATALLISTTDLNRPGMQLAGFFDYFAYERIQIIGKVEHRYLETLDTKTRKERLDRMMSYDIPCLIISRGLEVPEELLCTANKYQRKILRSHKNTTKLISKVINYLEDTLAPTITLHGVLMDIYGVGVLITGKSGIGKSETAVELIKRGHLLVADDAVEIKRIGHEVLQGCAPEIIRHMIEVRGIGILDVKSLFGVGAIKIKTDIDLIIDLEEWDSTKSYDRLGLDDNHREILGMKIDEVTIPIKPARNIALIIEVAARNHRQKKMGYHAAQEFNDRLMKSLEEKSQQ | Catalyzes the ATP- as well as the pyrophosphate-dependent phosphorylation of a specific serine residue in HPr, a phosphocarrier protein of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS). HprK/P also catalyzes the pyrophosphate-producing, inorganic phosphate-dependent dephosphorylation (phosphor... | A6TVI5 |
Q2W2J1 | RL3_MAGSA | 50S ribosomal protein L3 | Magnetospirillum | MRSGLIAQKVGMTRIFTEDGTHVPVTVLKVDTCQVVSTRSVEKDGYVAVQLGAGTAKVKNVSKPARANFAKAKVEPKKKLVEFRVAPENLLEVGTELSAAHFIPGQYVDVTGTTIGKGFAGGMKRWNFRGLEATHGVSVSHRSHGSTGQRQDPGKVFKGKKMAGHMGDEQVTTQNLTVVSTDADRGLILVKGSVPGHEGSWVLVRDAVKRKLPDGVPFPAGVKAAASAE | One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit. | Q2W2J1 |
P59048 | PDRG1_MOUSE | p53 and DNA damage-regulated protein 1 | Mus | MLSPEAERVLRYLVEVEELAEAVLSDKRQIVDLDTKRNQNREGLRALQKDLSVSEDVMVCFGNMFIKMPHPKTKEMIQKDQEHLDKEIERLRSQLKVKVNRLFEAQGKPELKGFNLNPLSPDEVKALKVILKG | May play a role in chaperone-mediated protein folding. | P59048 |
Q57TL5 | SYI_SALCH | Isoleucyl-tRNA synthetase | Salmonella | MSDYKSTLNLPETGFPMRGDLAKREPGMLARWTDDDLYGIIRAAKKGKKTFILHDGPPYANGSIHIGHSVNKILKDIIVKSKGLSGFDSPYVPGWDCHGLPIELKVEQEFGKPGEKFTAAEFRAKCREYAATQVDGQRKDFIRLGVLGDWSHPYLTMDFKTEANIIRALGRIIKNGHLHKGAKPVHWCVDCRSALAEAEVEYYDKTSPSIDVAFRAVDQDAVKAKFGLPGVSGPVSLVIWTTTPWTLPANRAISLAPDFDYALVQIDGQAVILAKDLVESVMQRIGAAEYTILGTVKGAELELLRFTHPFMGFDVPAILG... | Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrol... | Q57TL5 |
Q60336 | ARTE_METJA | Probable archaeosortase E | Methanocaldococcus | MGSLLMERNFMVEDTFTNGKLSKKEKILFLIKFYIIFLVVFFILSYFGKYLIGIVTYLSYIFTKIIISDARLADNFIYLPNNTVEVVEECTGSFLIAGLLALIIVYSKNIKEFIIGIFFVLLAFFVNIFRIVLICYLVNMHPESSYLYHEIAGYGVILTLVPVLVIGYLKIIEKYRHSSNKSHL | Transpeptidase that recognizes and modifies its substrate by proteolytic cleavage of a sorting signal. Following cleavage, a covalent intermediate is formed via a thioester bond between the archaeosortase and its substrate, which is then transferred and covalently attached to the cell membrane. | Q60336 |
Q8DT23 | METK_STRMU | Methionine adenosyltransferase | Streptococcus | MSERKLFTSESVSEGHPDKIADQISDAILDAVLVQDPDAHVAAETAVYTGSVHVFGEISTTAYVDINRVVRDTIAEIGYTDTAYGFSAETVGVHPSLVEQSPDIAQGVNEALEVRGHHEQDDLDLIGAGDQGLMFGFAVDETPELMPLPISLAHRLVRKLAELRKSGEIAYLRPDAKSQVTVEYDENDKPVRVDTVVISTQHDPEATNEQIHRDVIEKVIKAVIPAEYLDAKTKYLINPTGRFVIGGPQGDSGLTGRKIIVDTYGGYARHGGGAFSGKDATKVDRSASYAARYIAKNIVAAGLAKKAEVQLAYAIGVAQP... | Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. | Q8DT23 |
Q28571 | THB_SHEEP | Nuclear receptor subfamily 1 group A member 2 | Ovis | MTPNSMTENGLPAWDKPKPCPDGEPEWKLVGMSEACLHRKSHPERRGPLKHEQSPLIQASWTSSIFHLDHDDVSDQSAPSAQAFQTEEKKCKGYIPSYLDKDELCVVCGDKATGYHYRCITCEGCKGFFRRTIQKNLHPSYSCKYEGKCVIDKVTRNQCQECRFKKCIYVGMATDLVLDDSKRLAKRKLIEENREKRRREELQRSMGHKPEPTDQEWELIKTVTEAHVATNAQGSHWKQKRKFLPEDIGQAPIVNAPEGGKVDLEAFSHFTKIITPAITRVVDFAKKLPMFCELPCEDQIILLKGCCMEIMSLRAAVRYD... | Nuclear hormone receptor that can act as a repressor or activator of transcription. High affinity receptor for thyroid hormones, including triiodothyronine and thyroxine. | Q28571 |
Q9U1H0 | CIC_DROME | Protein fettucine | Sophophora | MNAFQDFELGAKLYLQCLLSLSSSRSATPSYTSPVNHAGASPLNAIAHSPVNVSATHRQNFFTPIANQSQQQQQQQPVAVPLDSKWKTTPSPVLYNANNNSSNNNTSSSNNNNNSNWEVGSNSNTHVAATAAATSTVGAQPLPPQTTPVSLVMHAPPPQQQPLQQQHHHHQPPPPPPASLPAPSAPPTSGSSSSHNSVGHATSVIRISSSQQQHQQQQQHQQQAHPHVVVSGGQTFHPVIVDATQLSVPLPPTTVSFHQPNTPTSTAASVASMSQDKMLAKNGYNAPWFKLLPHMTPMSKASPAPVTPTLTTSASSYNVV... | Transcriptional repressor required for the specification of numerous cell types during embryonic development. Required for terminal patterning of early embryos. May associate with gro to repress tll and hkb, restricting their expression to embryonic terminal poles where they initiate correct development of head and tai... | Q9U1H0 |
C4LDB2 | TIG_TOLAT | PPIase | Tolumonas | MQVSVETTQGLERRLTITVPADKIEKEYNSRLNQVAKTRRIDGFRPGKAPKALIQKMYGESIVADVADAVMQRHFVEALVAEKLNPVGAPTLEPNQLVPGSDFTFTVSFEVYPEFKVQNLDAIKVEKPVATVSDADLDKMLTTLRKQHASWVDADEAAANDLRVNMDFVGSVDGEEFEGGKAEGFALVLGAGRMIPGFEAGILGKKAGESFDIEVTFPEDYHAENLKGKAAKFAIKLNKVEKQDLPELDAEFIKRFGVEDGSVESLKAEIRKNMERELTQALKGQVKEQILSGLLEQNLIDVPKAAVTREVEALRQQALQ... | Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase. | C4LDB2 |
Q7N8V7 | RSMA_PHOLL | S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase | Photorhabdus | MNNRVHQGHFARKRFGQNFLTDQFVIDSIAAAINPQPGQAVLEIGPGLGALTEPVGERMDKMTVVELDRDLAARLQVHPQLKDKLTIIQQDAMTVNFGELSQQRGKPLRVFGNLPYNISTPLMFHLFSYTDAIADMHFMLQKEVVNRLVAGPGSKTFGRLSVMAQYYCQVIPVLEVPPTAFTPAPKVDSAVVRLVPHKSIPHPVKNIRMLSRITTQAFNQRRKTIRNSLGDLFTVEQLTELGIDPSTRAENISVEQYCKMANWLSEQPEMQS | 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. | Q7N8V7 |
B1XIE7 | NDK_SYNP2 | Nucleoside-2-P kinase | unclassified Synechococcus | MERTFVMVKPDGVQRGLVGDVIRRFEAKGFKLVGLKLVSVSRELAEQHYGVHRERPFFGSLVEFIISVPVVAMVWEGKGAIAAARKIIGATNPLEAEPGTIRGDFGVDIGRNLIHGSDGPDTAASEIALWFSESELANWEPATKAWLYE | (Microbial infection) Catalyzes the phosphorylation of dZDP to dZTP, when the bacterium is infected by a phage that produces the substrate for the synthesis of dZTP (2- amino-2'-deoxyadenosine 5'-triphosphate), which is then used by the phage as a DNA polymerase substrate. | B1XIE7 |
Q6G401 | LIPA_BARHE | Sulfur insertion protein LipA | Bartonella | MVTVVDRVTDRRLRHPEKAHRPDTSVQKKPDWIRVKAPTSQVYKETHGIVRAHKLVTVCEEAGCPNIGECWSQRHASFMILGEICTRACAFCNVATGIPFAVDENEPERVADAVARMELKHVVITSVDRDDLADGGAEHFAKVIYAIRRKAPKTTIEVLTPDFRHKDGALEIVVAAKPDVFNHNLETVPSKYLKVRPGARYFHSIRLLQRVKELDPTIFTKSGIMVGLGEERNEILQLMDDLRSADVDFMTIGQYLQPTRKHHPVIRFVPPEEFESFAKIGKVKGFLHMASNPLTRSSHHAGDDFAILQKARDEKFALQR | Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives. | Q6G401 |
Q9X7R6 | RNH_STRCO | Ribonuclease HI | Streptomyces albidoflavus group | MRERAVAACDGASKGNPGPAGWAWVVADASENPVRWEAGPLGKATNNIAELTALERLLASTDPDVPLEVRMDSQYAMKAVTTWLPGWKRNGWKTAAGKPVANRELVVRIDELLDGRSVEFRYVPAHQVDGDRLNDFADRAASQAAVVQEAAGSALGSPEPPPAPDVPAARRAPRRGSSGAARKGGGGSSARTIKAKFPGRCLCGRPYAAGEPIAKNDQGWGHPECRTVAAG | Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. | Q9X7R6 |
A6WPJ2 | PEPE_SHEB8 | Dipeptidase E | Shewanella | MTINALLLSSSRVGDTPYLAHAIPFIKPLTTNAQKWIFIPYAGVSMSYDNYLASVVTGLSELELDISGIHQHPDPQQAIKDADGILIGGGNTFHLLHQLYRYDLVTLIGEQVALGKPYIGWSAGSNVSGQSIRTTNDMPIIEPPSFKALNLLPFQLNPHYSNYQAPGHNGETRAQRLLEFTKVDPLTPVVGIVEGSALWRQGDKLSLLGDQPAYLFCGEQQEIPIPVGSDLSHLLKA | Hydrolyzes dipeptides containing N-terminal aspartate residues. May play a role in allowing the cell to use peptide aspartate to spare carbon otherwise required for the synthesis of the aspartate family of amino acids. | A6WPJ2 |
Q5YP21 | LEXA1_NOCFA | LexA repressor 1 | Nocardia | MTDYDFEHLDTSALPVRQRRILEVIRDWVVEHGYAPSTRQIGAAVGLRSMSSVARHLRSLEERGFLRRGEGVARPIDVRLFLHGTAAAAPSEDAVTVPVVGDIAAGAPILAEEHTDDLLTLPRELVGRGTVFALRVRGDSMIDAAICDGDTVVVRSQREANSGDIVAAMIGEEATVKVFRRRNGHVLLEPRNPAYDVIDGDEAVILGKVVSVLRRI | 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... | Q5YP21 |
Q5LSS5 | RL13_RUEPO | 50S ribosomal protein L13 | Ruegeria | MKTFSATPADIDKKWILIDAEGVVLGRLASIVAMRLRGKHKASFTPHMDMGDNVIVINADKVQITGKKREEHFYWHTGHPGGIKSRTKQQILEGAHPERVVYQAVKRMLPGNRLSRQQMTNLRIYAGTEHPHEAQAPEVLDVKSMNKKNTRS | 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. | Q5LSS5 |
Q03WG9 | RS14_LEUMM | 30S ribosomal protein S14 | Leuconostoc | MAKKSKIAKAQKREALVAKYADKRAALKAAGDYIGLAALPKDSSPVRVHNRDWIDGRPHAYMREFGMSRLNFRQLAHKGQIPGVRKASW | Binds 16S rRNA, required for the assembly of 30S particles and may also be responsible for determining the conformation of the 16S rRNA at the A site. | Q03WG9 |
Q9N0T1 | STC1_BOVIN | Stanniocalcin-1 | Bos | MLQNSAVLLVLVISASATHEAEQNDSVSLRKSRVAAQNSAEVIRCLNSALQVGCGAFACLENSTCDTDGMYDICKSFLYSAAKFDTQGKAFVKESLKCIANGVTSKVFLAIRRCSTFQRMIAEVQEECYTKLNVCSVAKRNPEAITEVVQLPNHFSNRYYNRLVRSLLDCDEDTVSTIRDSLMEKIGPNMASLFHILQTDHCAHTQQRADFNRRRANEPQKLKVLLRNLRGEVASPSHIKRTSQESA | Stimulates renal phosphate reabsorption, and could therefore prevent hypercalcemia. | Q9N0T1 |
Q65S74 | SOTB_MANSM | Probable sugar efflux transporter | Basfia | MLNRKLVNRVEYFRVIVMAFAAFVFNTTEFVPVALLSDIADSFQMPVSNTGLMITIYAWIVSLCSLPCMLMTARLERRRLLISLFILFIASHILSAFAWNYEVLLIARAGVALTHSIFWSITAALTIRIAPKNKKTQALGLLALGSSLAMVLGLPLGRIIGQAFGWRTTFTLIGVFAALILILIVRLLPKIPSQNAGSLKSLPVLARRPMLITLYIFTILVISAHFTAYSYIEPFMIQIGRVSANKATAVLLIFGVSGVVASVLFSRLYRIAPIKFLLSSVAILTLALICLYGVSGISGAIFALVFIWGVAISALSLAMQ... | Involved in the efflux of sugars. The physiological role may be the reduction of the intracellular concentration of toxic sugars or sugar metabolites. | Q65S74 |
Q7UDU1 | DNAJ_SHIFL | Chaperone protein DnaJ | Shigella | MAKQDYYEILGVSKTAEEREIRKAYKRLAMKYHPDRNQGDKEAEAKFKEIKEAYEVLTDSQKRAAYDQYGHAAFEQGGMGGGGFGGGADFSDIFGDVFGDIFGGGRGRQRAARGADLRYNMELTLEEAVRGVTKEIRIPTLEECDVCHGSGAKPGTQPQTCPTCHGSGQVQMRQGFFAVQQTCPHCQGRGTLIKDPCNKCHGHGRVERSKTLSVKIPAGVDTGDRIRLAGEGEAGEHGAPAGDLYVQVQVKQHPIFEREGNNLYCEVPINFAMAALGGEIEVPTLDGRVKLKVPGETQTGKLFRMRGKGVKSVRGGAQGD... | 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... | Q7UDU1 |
A5VQP4 | ISPDF_BRUO2 | 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase | Brucella | MQAQSLAEVTVISKAAAVIVAAGRGERAGQSAEGPKQYRLIGAEAVLARTLRAFTDCPLIGTIAVVIHPDDHALYRRAVPEKHENVILVTGGPTRQESTRLGLLALKDEAPQYVLIHDGVRPFIGQDLLERIIANLTPDNGVLPALAVSDTLKRAAADGMVETTISRTGLFAAQTPQAFPYAPILDAHEKAFAINRTDFTDDAAIAEWQEIAVRIIEGSADNTKLTWAKDIEMADKRLRQDHAVFPDIRTGNGYDVHSFEPGDHVTLCGVKIPHEAKLNGHSDADVALHALTDALLATRGAGDIGTHFPPSDPQWKGAAS... | Bifunctional enzyme that catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP) (IspD), and catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a ... | A5VQP4 |
P07262 | DHE4_YEAST | NADP-dependent glutamate dehydrogenase 1 | Saccharomyces | MSEPEFQQAYEEVVSSLEDSTLFEQHPEYRKVLPIVSVPERIIQFRVTWENDKGEQEVAQGYRVQYNSAKGPYKGGLRFHPSVNLSILKFLGFEQIFKNSLTGLDMGGGKGGLCVDLKGRSNNEIRRICYAFMRELSRHIGQDTDVPAGDIGVGGREIGYLFGAYRSYKNSWEGVLTGKGLNWGGSLIRPEATGYGLVYYTQAMIDYATNGKESFEGKRVTISGSGNVAQYAALKVIELGGTVVSLSDSKGCIISETGITSEQVADISSAKVNFKSLEQIVNEYSTFSENKVQYIAGARPWTHVQKVDIALPCATQNEVS... | Catalyzes the incorporation of an ammonium ion into alpha-ketoglutarate to form L-glutamate, the major route of assimilation of ammonia into an organic form in yeast. | P07262 |
B8AW64 | NAP1B_ORYSI | Nucleosome assembly protein 1-like 2 | Oryza sativa | MSDGKDSLDLSGLGAAVPNAKELSAEDKANLVESIKNTLQGLAARHTDVLESLEPKVRKRVEVLREIQSQHDDLEAKFFEERAALEAKYQKMYEPLYSKRYEIVNGVVEVDGVTKEAADETPAEQKEEKGVPEFWLNAMKNHEILSEEIQERDEEALKYLKDIKWYRISEPKGFKLEFYFDTNPFFKNSVLTKTYHMIDEDEPILEKAIGTEIEWFPGKCLTQKVLKKKPKKGSKNTKPITKTENCESFFNFFSPPQVPDDDEEIDEDTAEQLQNQMEQDYDIGSTIRDKIIPHAVSWFTGEAAQDEDFEGIMDDEDDDD... | May modulate chromatin structure by regulation of nucleosome assembly/disassembly. | B8AW64 |
A6V720 | TIG_PSEA7 | PPIase | Pseudomonas | MQVSVESTSALERRMTVGVPAERIETEVNKRLQQTARRAKIPGFRPGKVPMSVIRQRYEASARQEAMGDLIQETFYEAVVEQKLNPAGSPSVEPKSFEKGKDLEYIATFEVFPEFTVSGLEGIKIERLQAEVADADVDNMLDVLRKQNTRFEVVERAAQNDDQLNIDFVGKIDGEAFAGGSAKGTLLVLGSGRMIAGFEEGLVGAKAGEERVLNLTFPEDYQNLDLANKPAEFTVTVNSVAEPKLPELNEEFFALFGVKETGLDGFRAEVQKNMERELRQAIKSKVKNQVMEGLLQANPIEVPKALIGNEVNRLRVQAVQ... | Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase. | A6V720 |
A9IN82 | MUTL_BART1 | DNA mismatch repair protein MutL | Bartonella | MIIRHLSENIINQIAAGEVIERPANVVKELVENAIDAGATRIEIITANGGKNFIKVSDNGCGIPADQLTLAVSRHCTSKITDDVHNICFLGFRGEALPSIGSVAKLKLISRTKEAENAAEISVTAGKIVGPKPAAANLGTIVEVRDLFFVTPARLKFMKTDRAETNAISDMIKRIAIAFPHIRFSLSGLDRTSMELSATENNTQGQLQRITQIMGKEFAPNSIALDAERESVRLTGFACLPSFNRNNSLHQFAYVNGRPVRDKFLWGAIRGAYADVMTRDRYPVAILFIDLPPAEVDVNVHPAKADVRFRDPGLIRGLIV... | 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 ... | A9IN82 |
A1WIF0 | PSD_VEREI | Phosphatidylserine decarboxylase beta chain | Verminephrobacter | MPDRLAVLAQYALPKRALTTWAGKWASARLGGLTTALIRRFVARYDVNMAEAANPDMAGYASFNDFFTRALQPGARPLARADLICPVDGAISQFGRIGKDRIFQAKGHAYSTTALLGGDAAMAARFDDGHFATLYLSPRDYHRVHMPCAGELTRMVHVPGELFSVNPATACVVPGLFARNERVVCVFESAPGPGGPFALVLIGAAIVGSMATVWHGQVNPPRPGTLRQWDYAKGQVRLQQGQEMGRFLLGSTVVLLLPRGPLQFNPQWAPARPIMLGQAMAQRCAD | Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). | A1WIF0 |
F4K2F0 | EML3_ARATH | Protein EMSY-LIKE 3 | Arabidopsis | MDYRPSDSSGTDDDLPPSHQGRYQRNARPTGNGRPSVLNSAPLSRVHNEMETQIHLIEQEAYSSILRAFKAQSDAITWEKESLITELRKELRVSDEEHRELLSRVNADEMIRRIREWRKANSLQSSVPQLVHDAPSPAVSGSRKKQKTSQSIASLAMGPPSPSLHPSMQPSSSALRRGGPPPGPKTKKPKTSMQYPSTGIAGRPQAGALTNEPGESGSYDPLVGRKVWTKWPDDNQYYEAVITDYNPVEGRHALVYDINSANETWEWVNLKEISPGDIRWEGEDPGISRKGGHPGQGRGTKTMARGGPASNAGGRGRGSM... | Probably involved in the regulation of chromatin states (Probable). Contributes to basal immunity . | F4K2F0 |
P22636 | PCYB_SPHSK | 4,5-PCD | Sphingobium | MARVTTGITSSHIPALGAAIQTGTSDNDYWGPVFKGYQPIRDWIKQPGNMPDVVILVYNDHASAFDMNIIPTFAIGCAETFKPADEGWGPRPVPDVKGHPDLAWHIAQSLILDEFDMTIMNQMDVDHGCTVPLSMIFGEPEEWPCKVIPFPVNVVTYPPPSGKRCFALGDSIRAAVESFPEDLNVHVWGTGGMSHQLQGPRAGLINKEFDLNFIDKLISDPEELSKMPHIQYLRESGSEGVELVMWLIMRGALPEKVRDLYTFYHIPASNTALGAMILQPEETAGTPLEPRKVMSGHSLAQA | Responsible for the aromatic ring fission of protocatechuate. | P22636 |
Q38XF6 | ACCD_LATSS | Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta | Latilactobacillus | MQLFNAVRNIGKAHLKYNQEARQKVPDGLWVACPKCQQSIYHKDLGYYRTCPVCQYGFRTRAKVRLDWLVDSFEPAGDLAQTPNPLHFPKYPQKLRKAQQITGLEDSILTGVATIKQQKFALGIMDPYFIMGSMGSATGEKITRLFELATEKGLPVILIAASGGARMQEGIFSLMQMAKTSAAVKQHAEQGLLYISLLTDPTTGGVTASFATEADIILAEPKAVIGFAGRRVIEQTMHEQIAPDLQDAETVLKNGFIDQIVARQDQKKVLHQLLKLHERGAHY | Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA. | Q38XF6 |
Q9SA47 | MYB58_ARATH | Myb-related protein 58 | Arabidopsis | MGKGRAPCCDKTKVKRGPWSHDEDLKLISFIHKNGHENWRSLPKQAGLLRCGKSCRLRWINYLRPDVKRGNFSAEEEDTIIKLHQSFGNKWSKIASKLPGRTDNEIKNVWHTHLKKRLSSETNLNADEAGSKGSLNEEENSQESSPNASMSFAGSNISSKDDDAQISQMFEHILTYSEFTGMLQEVDKPELLEMPFDLDPDIWSFIDGSDSFQQPENRALQESEEDEVDKWFKHLESELGLEENDNQQQQQQHKQGTEDEHSSSLLESYELLIH | Transcriptional activator that binds DNA to the AC cis-elements 5'-ACCTACC-3', 5'-ACCAACC-3' and 5'-ACCTAAC-3' of promoters and specifically activates lignin biosynthetic genes during secondary wall formation mediated by SND1. | Q9SA47 |
Q13BT8 | ISPE_RHOPS | 4-(cytidine-5'-diphospho)-2-C-methyl-D-erythritol kinase | Rhodopseudomonas | MTALSEQARAKVNLTLRVVGRRVDGYHDLESVVAFADCADRLTLHPGAELSLVMSGPGAQDCGDTSDNLVLKATRLLAERVPNLRTGGFVLDKHLPVAAGIGGGSADAAAALRLLARANELSADDPRVVEAARLTGADVPVCLPSKPCVMTGVGENLSPLQLPRLPAVMVNPRVPVATKDVFAALGLRAGQLNVGVVDLLKSTGWPTDGSSAADWIAAVKRGTNDLEAPALKVESVVGDVLRALAALPGVRLSRMSGSGATCFALFANDDDAQAGAQLLKAAQPGWWVHAGALS | Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol. | Q13BT8 |
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