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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B4S3W8 | RISB_PROA2 | 6,7-dimethyl-8-ribityllumazine synthase | Prosthecochloris | MTIKTIEGTLDARNSRFALVVSRFNDFIGQKLVEGAVDCIVRHGGSEEQIALYKCPGAFELPSVAKKVAVSGRYDAVITLGAIIRGATSHYDVIAAEATKGVAQVGLDTMIPVTFGVLTTDNLEQAIERAGTKAGNKGFDAALAAIEMVNLYQQV | 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. | B4S3W8 |
Q2NS03 | UNG_SODGM | Uracil-DNA glycosylase | Sodalis | MTQMLTWRDALAQEKTLPYFQETLAFVARERAAGMTVYPPAKDVFNAFRFTELNAVKVVILGQDPYHGPNQAHGLSFSVKPGVPAPPSLVNIYKELASDIPGFVIPNHGCLQSWAQQGVMLLNTVLTVEAGKAHSHASLGWETFTDKVIKVLNAQREGIVFLLWGSHAQKKGTIIDPKRHHVLKAPHPSPLSAHRGFLGCRHFSRANALLEQQGQQPIDWTPTLPAA | Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine. | Q2NS03 |
Q7VNA7 | PSD_HAEDU | Phosphatidylserine decarboxylase beta chain | Haemophilus | MSLKSYSTPTYWQRVKVACQYLFPQLPITRLAGWLAEQKWGMVTHFIIRIFAKQYNVNLAEAEKTNPADYTTFNEFFLRPLKENARPINQDDQAVCLPADGKISELGQINENRLLQAKGHYFTLETLLANDEEMAESFKNGSFITTYLSPRDYHRVHMPCDATLKKMIYVPGDLFSVNSFLAEHIPNLFARNERVICEFETAFGPMVQILVGATITASISTVWAGIINPPRSKDVVEYNYQTTGETAIHLKKGDEMGAFRLGSTVINLFPQATVELVSHLQAGVETRMGERFAKIIK | Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). | Q7VNA7 |
A7N0H8 | RPOA_VIBC1 | Transcriptase subunit alpha | Vibrio | MQGSVTEFLKPRLVDIEQISSTHAKVTLEPLERGFGHTLGNALRRILLSSMPGCAVIEVEIEGVLHEYSTKEGVQEDILEILLNLKGLAVRVAEGKDEVFITLNKSGSGPVVAGDITHDGDVEIANPEHVICHLTDDNAEIAMRIKVERGRGYVPASARIHNEEDERPIGRLLVDATYSPVDKIAYAVEAARVEQRTDLDKLVIDMETNGTLEPEEAIRRAATILAEQLDAFVDLRDVRVPEEKEEKPEFDPILLRPVDDLELTVRSANCLKAEAIHYIGDLVQRTEVELLKTPNLGKKSLTEIKDVLASRGLSLGMRLENWPPASIAED | DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | A7N0H8 |
O15205 | UBD_HUMAN | Ubiquitin-like protein FAT10 | Homo | MAPNASCLCVHVRSEEWDLMTFDANPYDSVKKIKEHVRSKTKVPVQDQVLLLGSKILKPRRSLSSYGIDKEKTIHLTLKVVKPSDEELPLFLVESGDEAKRHLLQVRRSSSVAQVKAMIETKTGIIPETQIVTCNGKRLEDGKMMADYGIRKGNLLFLACYCIGG | Ubiquitin-like protein modifier which can be covalently attached to target protein and subsequently leads to their degradation by the 26S proteasome, in a NUB1-dependent manner. Probably functions as a survival factor. Conjugation ability activated by UBA6. Promotes the expression of the proteasome subunit beta type-9 (PSMB9/LMP2). Regulates TNF-alpha-induced and LPS-mediated activation of the central mediator of innate immunity NF-kappa-B by promoting TNF-alpha-mediated proteasomal degradation of ubiquitinated-I-kappa-B-alpha. Required for TNF-alpha-induced p65 nuclear translocation in renal tubular epithelial cells (RTECs). May be involved in dendritic cell (DC) maturation, the process by which immature dendritic cells differentiate into fully competent antigen-presenting cells that initiate T-cell responses. Mediates mitotic non-disjunction and chromosome instability, in long-term in vitro culture and cancers, by abbreviating mitotic phase and impairing the kinetochore localization of MAD2L1 during the prometaphase stage of the cell cycle. May be involved in the formation of aggresomes when proteasome is saturated or impaired. Mediates apoptosis in a caspase-dependent manner, especially in renal epithelium and tubular cells during renal diseases such as polycystic kidney disease and Human immunodeficiency virus (HIV)-associated nephropathy (HIVAN). | O15205 |
A3MWZ8 | RL24_PYRCJ | 50S ribosomal protein L24 | Pyrobaculum | MPFTASAQPRKQRLSLYAAPLHLRRKLLNAKLSPELQKKLGVKRLPVRRGDTVLIMRGDFKGVTGKVVKVDLKRVRIFVEGATRTNSRGQTVYYPIHPSKVMIVDVDLSDKARQKLIERRKRGQHGSS | Located at the polypeptide exit tunnel on the outside of the subunit. | A3MWZ8 |
Q7VAP4 | AMPA_PROMA | Leucyl aminopeptidase | Prochlorococcus | MQISLYQKNLADWTGSIIAVGLLEGQIQEQLSLLEEICDYDSLLTHVEEKDFSAKAGELIKLEILGKSLEKIILIGLGKPEALSIDDLREGAALASRASIGSKGKIGILFPWEPFNPISASKAVAEAMRLSIFKDLRFQSEPKPQNNPQSIDLIGLPESNHNIIKEVDPICSGVELARELVAAPPNELTPAALAEKAVEIAKKFKWNYKILNRKECEKEGMGAYLAVSQGSDLEPQFIHLTYKPNGQIKRRIAMVGKGLTFDSGGYNLKVGASQIEMMKYDMGGSAAVIGAARAIGELAPVDTEVHFIVAACENMVNGSAVHPGDIIKASNGTTIEINNTDAEGRLTLADALIYACKLEPDAIVDLATLTGACVIALGEEIAGLWVESDELANELKDASSACGEKLWRMPLQASYKEGLKSMLADIKNTGPRSGGSITAALFLKEFISNGIKWAHIDIAGTCWTDKDRGIDPAGATGFGVRTLVNWACKSNPDIEK | Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. | Q7VAP4 |
Q2GJ82 | PDXH_ANAPZ | Pyridoxal 5'-phosphate synthase | phagocytophilum group | MTINKEGLRVDACSGDPMSIFGLWYEEVLRVKSVREPSAMVLATCDSENRPSARVVLLKRYSDAGFEFYTNLESRKAREIALNPCVSLVFDWRPIYKQVRVEGIAEFMDASESDAYFASRSRESQIGAWCSRQSMILEDRDVLLSKIELMEREYEGREIPRPKFWGGIRVVPNVIEFWMDGKHRLHDRRQYSKNIDGTWTSVYLYP | Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP). | Q2GJ82 |
Q8WVZ9 | KBTB7_HUMAN | Kelch repeat and BTB domain-containing protein 7 | Homo | MQSREDVPRSRRLASPRGGRRPKRISKPSVSAFFTGPEELKDTAHSAALLAQLKSFYDARLLCDVTIEVVTPGSGPGTGRLFSCNRNVLAAACPYFKSMFTGGMYESQQASVTMHDVDAESFEVLVDYCYTGRVSLSEANVQRLYAASDMLQLEYVREACASFLARRLDLTNCTAILKFADAFDHHKLRSQAQSYIAHNFKQLSRMGSIREETLADLTLAQLLAVLRLDSLDIESERTVCHVAVQWLEAAAKERGPSAAEVFKCVRWMHFTEEDQDYLEGLLTKPIVKKYCLDVIEGALQMRYGDLLYKSLVPVPNSSSSSSSSNSLVSAAENPPQRLGMCAKEMVIFFGHPRDPFLCYDPYSGDIYTMPSPLTSFAHTKTVTSSAVCVSPDHDIYLAAQPRKDLWVYKPAQNSWQQLADRLLCREGMDVAYLNGYIYILGGRDPITGVKLKEVECYSVQRNQWALVAPVPHSFYSFELIVVQNYLYAVNSKRMLCYDPSHNMWLNCASLKRSDFQEACVFNDEIYCICDIPVMKVYNPARGEWRRISNIPLDSETHNYQIVNHDQKLLLITSTTPQWKKNRVTVYEYDTREDQWINIGTMLGLLQFDSGFICLCARVYPSCLEPGQSFITEEDDARSESSTEWDLDGFSELDSESGSSSSFSDDEVWVQVAPQRNAQDQQGSL | As part of the CUL3(KBTBD6/7) E3 ubiquitin ligase complex functions as a substrate adapter for the RAC1 guanine exchange factor (GEF) TIAM1, mediating its 'Lys-48' ubiquitination and proteasomal degradation . By controlling this ubiquitination, regulates RAC1 signal transduction and downstream biological processes including the organization of the cytoskeleton, cell migration and cell proliferation . Ubiquitination of TIAM1 requires the membrane-associated protein GABARAP which may restrict locally the activity of the complex . | Q8WVZ9 |
P10613 | CP51_CANAL | Sterol 14-alpha demethylase | Candida | MAIVETVIDGINYFLSLSVTQQISILLGVPFVYNLVWQYLYSLRKDRAPLVFYWIPWFGSAASYGQQPYEFFESCRQKYGDVFSFMLLGKIMTVYLGPKGHEFVFNAKLSDVSAEDAYKHLTTPVFGKGVIYDCPNSRLMEQKKFAKFALTTDSFKRYVPKIREEILNYFVTDESFKLKEKTHGVANVMKTQPEITIFTASRSLFGDEMRRIFDRSFAQLYSDLDKGFTPINFVFPNLPLPHYWRRDAAQKKISATYMKEIKSRRERGDIDPNRDLIDSLLIHSTYKDGVKMTDQEIANLLIGILMGGQHTSASTSAWFLLHLGEKPHLQDVIYQEVVELLKEKGGDLNDLTYEDLQKLPSVNNTIKETLRMHMPLHSIFRKVTNPLRIPETNYIVPKGHYVLVSPGYAHTSERYFDNPEDFDPTRWDTAAAKANSVSFNSSDEVDYGFGKVSKGVSSPYLPFGGGRHRCIGEQFAYVQLGTILTTFVYNLRWTIDGYKVPDPDYSSMVVLPTEPAEIIWEKRETCMF | Lanosterol 14-alpha demethylase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway . The lanosterol 14-alpha-demethylase ERG11 (also known as CYP51) catalyzes C14-demethylation of lanosterol to produce 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol, which is critical for ergosterol biosynthesis . The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase ERG9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Squalene synthase is crucial for balancing the incorporation of farnesyl diphosphate (FPP) into sterol and nonsterol isoprene synthesis. Secondly, the squalene epoxidase ERG1 catalyzes the stereospecific oxidation of squalene to (S)-2,3-epoxysqualene, which is considered to be a rate-limiting enzyme in steroid biosynthesis. Then, the lanosterol synthase ERG7 catalyzes the cyclization of (S)-2,3 oxidosqualene to lanosterol, a reaction that forms the sterol core. In the next steps, lanosterol is transformed to zymosterol through a complex process involving various demethylation, reduction and desaturation reactions. The lanosterol 14-alpha-demethylase ERG11 (also known as CYP51) catalyzes C14-demethylation of lanosterol to produce 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol, which is critical for ergosterol biosynthesis. The C-14 reductase ERG24 reduces the C14=C15 double bond of 4,4-dimethyl-cholesta-8,14,24-trienol to produce 4,4-dimethyl-cholesta-8,24-dienol. 4,4-dimethyl-cholesta-8,24-dienol is substrate of the C-4 demethylation complex ERG25-ERG26-ERG27 in which ERG25 catalyzes the three-step monooxygenation required for the demethylation of 4,4-dimethyl and 4alpha-methylsterols, ERG26 catalyzes the oxidative decarboxylation that results in a reduction of the 3-beta-hydroxy group at the C-3 carbon to an oxo group, and ERG27 is responsible for the reduction of the keto group on the C-3. ERG28 has a role as a scaffold to help anchor ERG25, ERG26 and ERG27 to the endoplasmic reticulum and ERG29 regulates the activity of the iron-containing C4-methylsterol oxidase ERG25. Then, the sterol 24-C-methyltransferase ERG6 catalyzes the methyl transfer from S-adenosyl-methionine to the C-24 of zymosterol to form fecosterol. The C-8 sterol isomerase ERG2 catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol. The sterol-C5-desaturase ERG3 then catalyzes the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol. The C-22 sterol desaturase ERG5 further converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen-3beta-ol is substrate of the C-24(28) sterol reductase ERG4 to produce ergosterol (Probable). | P10613 |
Q56063 | PRPC_SALTY | Citrate synthase | Salmonella | MTDTTILQNNTHVIKPKKSVALSGVPAGNTALCTVGKSGNDLHYRGYDILDLAEHCEFEEVAHLLIHGKLPTRDELNAYKSKLKALRGLPANVRTVLEALPAASHPMDVMRTGVSALGCTLPEKEGHTVSGARDIADKLLASLSSILLYWYHYSHNGERIQPETDDDSIGGHFLHLLHGEKPTQSWEKAMHISLVLYAEHEFNASTFTSRVIAGTGSDVYSAIIGAIGALRGPKHGGANEVSLEIQQRYETPDEAEADIRKRVENKEVVIGFGHPVYTIADPRHQVIKRVAKQLSEEGGSLKMYHIADRLETVMWETKKMFPNLDWFSAVSYNMMGVPTEMFTPLFVIARVTGWAAHIIEQRQDNKIIRPSANYTGPEDRPFVSIDDRC | Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and via the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the Claisen condensation of propionyl-CoA and oxaloacetate (OAA) to yield 2-methylcitrate (2-MC) and CoA. Also catalyzes the condensation of oxaloacetate with acetyl-CoA or butyryl-CoA but with a lower specificity. | Q56063 |
D4GZM5 | DACZ_HALVD | Cyclic-di-AMP synthase | Haloferax | MAALSELLGDLVADVDGLFLFTPSSSHYEQFAETDVPTVVIAPENTVEAETFVELPLQFQNVKDRIRFGVEGAMEQSIVEAGDTIACNVGTFGGDPDSLVRVRVEENMRSGIYDLFANSRADPGVIRDVFEVAIELGKKGQKGEPVGALFIVGDAGKVMNKSRPLSYNPFEKSHVYVGDPIVNVMLKEFSRLDGAFVISDSGKIVSAYRYLEPSAEGVDIPKGLGARHMAGGAITRDTNATAIVLSESDGLVRAFKGGKMILEIDPEAY | Diadenylate cyclase that catalyzes the condensation of 2 ATP molecules into cyclic di-AMP (c-di-AMP). c-di-AMP is a second messenger for intracellular signal transduction involved in the control of important regulatory processes such as osmoregulation. Is essential for H.volcanii. Overexpression of DacZ leads to cell death, suggesting the need for tight regulation of c-di-AMP levels. Cannot use GTP as substrate. | D4GZM5 |
B8ABC2 | LRR1_ORYSI | Leucine-rich repeat protein 1 | Oryza sativa | MGAGALGVVAMVAAAVVVAMAGANSEGDALSALRRSLRDPGGVLQSWDPTLVNPCTWFHVTCDRDNRVTRLDLGNLNLSGHLVPELGKLDHLQYLELYKNNIQGTIPSELGNLKNLISLDLYKNNISGTIPPTLGKLTSLVFLRLNGNRLTGPIPRELAGISSLKVVDVSSNDLCGTIPTSGPFEHIPLSNFEKNPRLEGPELQGLAVYDTNC | Involved in plant defense response. | B8ABC2 |
Q2SPF8 | HSLO_HAHCH | Heat shock protein 33 homolog | Hahella | MKADLLQRFIFDELDIRGELLVLKKTVQDALSRHDYPQAIQSLLGQALSAGLLLSATLKIKGDTTLQATGEGELRLLMAEATHRRTARGIARWEGAPDSTSLKQLLGNRAALAITIAPQNGQRYQGIVPLSSDSLSACLEEYFERSEQLATRIWLYESNGCWGGLLLQQLPAARGGEYSAENWERIVALSATLTADELFSLPAEEVLHRLFHEESVRVLQEEPASFWCSCSEERTLEVVKSLGREEAFSILDESGEIEMNCQFCLQRYSFGRERIEQLFDSPTLH | 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. | Q2SPF8 |
A7MEB1 | CMOA_CROS8 | Carboxy-S-adenosyl-L-methionine synthase | Cronobacter | MSNRDTLFSAPIARLGDWTFDERVAEVFPDMIQRSVPGYSNIISMIGMLAERFVQPASQVYDLGCSLGAATLSVRRNVHHDGCKIIAVDNSPAMVERCRRHIDAFKAQTPVEVIEDDIRNITIENASMVVLNFTLQFLNPDDRQLLLNKIFQGLNPGGALVLSEKFSFEDSVVGELLFNMHHDFKRANGYSELEISQKRSMLENVMLTDSVETHKARLRKAGFEHSELWFQCFNFGSLVAVKGGSAT | Catalyzes the conversion of S-adenosyl-L-methionine (SAM) to carboxy-S-adenosyl-L-methionine (Cx-SAM). | A7MEB1 |
Q083S7 | CDD_SHEFN | Cytidine aminohydrolase | Shewanella | MQNRFLESITQLDKPLANALVPLLHDQFCGHIDASQFAGLVKASGKTEQQVLMDLLPIAAALANPPISEFYVGAIAKGSSGDLYMGANLELPGEALFHSVHAEQSAISHAWLSGETEIVDIIVNFSPCGHCRQFMNELVNGSKINIHLPNQETQTLAHYLPYAFGPSDLDVTVPLLCKREQEFNCDSDDPMIIEAIDQMGLSYAPYTNNNAAVVLETNDGATFCGRYAESAAFNPSMQPMQMALSNLIRNNRQYSEIKRAVLVESSVGKITLVGAAMDALHAIAPIELQHMVVEPLLG | This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis. | Q083S7 |
D4DB32 | UTP25_TRIVH | U three protein 25 | Trichophyton | MAIQHKKGGGHRGRGSKTGRSRGRKFETSRLKDVREDESSGGEEDVDGQPTEDMNDSEGTDVSSESGLDEPPKENSYSTLLKLLNTDAKSNEPARKKRKIKANEPDANPVEVSIPTADDTEQMDEVADTEASASEDENMDDEDIPDEDYAEDIGTDGRNDMFELHFGNPDETELSHKIQACSKAWKSTKADLIDGLYSVVSMPDAGGISSASLPTTPSPADLKLKQKLARNAVSFDRLNSCLTPYIFGYHDTLFCSRTTQNSAKLRDLYCLHALNHVLKTRDRVIKNSAILSRENNGDVELRDQGFTRPKVLIILPTRQACVRVINSFTKIYPMEQQENKKRFMDSFSAADSDEWAHKPDDFKELFGGNDDDMFRLGFKFTRKSLKFFSKFYSSDIILASPLGLRTAIEKEGGKKNENDFLSSIEMVIVDHADALMMQNWDHVEYIFSNLNLQPKEAHGCDFSRVRQWYLDGHGKFLRQTLVFSAFNTPELNALYNTQMQNVFGKAKIMSKYEGAMLNLRLPISVKQTFSRFDSASPLKDPEARFQYFTRTVLASLARGWTESSPRKKSGGTLIFIPSYLDFVRVRNHFANSSQTENISFGLISEYTSVRDSSRARSHFMNGRHSVLLYTERAHHFRRYNIRGVTNIVMYGLPDNPIFWGDLIEYLGSAAGGTSTPTVRVLFSKWDALKLERIVGTARVRSMLLEKGGDTFTFV | DEAD-box RNA helicase-like protein required for pre-18S rRNA processing, specifically at sites A0, A1, and A2. | D4DB32 |
O08349 | MDH_ARCFU | Malate dehydrogenase | Archaeoglobus | MKLGFVGAGRVGSTSAFTCLLNLDVDEIALVDIAEDLAVGEAMDLAHAAAGIDKYPKIVGGADYSLLKGSEIIVVTAGLARKPGMTRLDLAHKNAGIIKDIAKKIVENAPESKILVVTNPMDVMTYIMWKESGKPRNEVFGMGNQLDSQRLKERLYNAGARNIRRAWIIGEHGDSMFVAKSLADFDGEVDWEAVENDVRFVAAEVIKRKGATIFGPAVAIYRMVKAVVEDTGEIIPTSMILQGEYGIENVAVGVPAKLGKNGAEVADIKLSDEEIEKLRNSAKILRERLEELGY | Catalyzes the reversible oxidation of malate to oxaloacetate. Can also oxidize tartrate. | O08349 |
B1A990 | NDHH_CARPA | NADH-plastoquinone oxidoreductase subunit H | Carica | MNIPATGKDFMIVNMGPHHPSMHGVLRLIVTLDGEDVIDCEPILGYLHRGMEKIAENRTIIQYLPYVTRWDYLATMFTEAITVNGPEQLGNIQVPKRASYIRVIMLELSRIASHLLWLGPFMADIGAQTPFFYIFRERELVYDLFEAATGMRMMHNYFRIGGIAADLPHGWIDKCLDFCDYFLTGVAEYQKLITRNPIFLERVEGVGIIGGEEAINWGLSGPMLRASGIEWDLRKVDHYECYDEFDWEVQWQKEGDSLARYLVRISEMTESIKIIQQALEGIPGGPYENLEIRCFDRKKDPEWNDFDYRFISKKPSPTFELPKQELYVRVEAPKGELGIFLIGDQSGFPWRWKIRPPGFINLQILPQLVKRMKLADIMTILGSIDIIMGEVDR | NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. | B1A990 |
A7HYC4 | SYDND_PARL1 | Non-discriminating aspartyl-tRNA synthetase | Parvibaculum | MSSFRSHTSGELRKSHVGETVRLAGWVHRKRDHGGLLFIDLRDNYGLTQLVFDPDRAEAFALAEKLRAEYVVAIEGKVVARSAETINANLPTGDIEIAVSSMEVLSEAQDLPLPVFGEPDYPEDIRLTYRFLDLRRETLHRNILLRSKIIADIRRRMTEVGFNEFQTPILTASSPEGARDFLVPSRMHPGKFYALPQAPQQFKQLIMVAGFDRYFQIAPCFRDEDARADRSPGEFYQLDVEMSFVTQDDVFAAIEPVLHGLFEKFAEGKKVSSYPFTRIPYAEAIRKYGSDKPDLRNPIVMESVTDHFRGSGFKVFAGLIEKDSKVEVWAIPAPGGGNRAFCDRMNSWAQGEGQPGLGYIFFREEGGALEGAGPVAKNIGPERTEAIRTQLGLKAGDAVFFVAGVPAKTASFAGLARTRVGTELGLIEEDIFKFCWIVDFPMFEWNEDEKKIDFSHNPFSMPNYPLDKFLKLDKDNADEILGMTAFQYDIVCNGVELSSGAIRNHKPDVMYKAFEIAGYDKSVVETKFGGMLNAFKYGAPPHGGLAPGIDRMVMLLAGVENLREVTMFPMNQQAQDLLMQAPSEVEPKQLKELHIRVVPPLEKKKEG | Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn). | A7HYC4 |
Q14213 | IL27B_HUMAN | Epstein-Barr virus-induced gene 3 protein | Homo | MTPQLLLALVLWASCPPCSGRKGPPAALTLPRVQCRASRYPIAVDCSWTLPPAPNSTSPVSFIATYRLGMAARGHSWPCLQQTPTSTSCTITDVQLFSMAPYVLNVTAVHPWGSSSSFVPFITEHIIKPDPPEGVRLSPLAERQLQVQWEPPGSWPFPEIFSLKYWIRYKRQGAARFHRVGPIEATSFILRAVRPRARYYVQVAAQDLTDYGELSDWSLPATATMSLGK | Associates with IL27 to form the IL-27 interleukin, a heterodimeric cytokine which functions in innate immunity. IL-27 has pro- and anti-inflammatory properties, that can regulate T-helper cell development, suppress T-cell proliferation, stimulate cytotoxic T-cell activity, induce isotype switching in B-cells, and that has diverse effects on innate immune cells. Among its target cells are CD4 T-helper cells which can differentiate in type 1 effector cells (TH1), type 2 effector cells (TH2) and IL17 producing helper T-cells (TH17). It drives rapid clonal expansion of naive but not memory CD4 T-cells. It also strongly synergizes with IL-12 to trigger interferon-gamma/IFN-gamma production of naive CD4 T-cells, binds to the cytokine receptor WSX-1/TCCR. Another important role of IL-27 is its antitumor activity as well as its antiangiogenic activity with activation of production of antiangiogenic chemokines. | Q14213 |
A4FN28 | ATPG_SACEN | F-ATPase gamma subunit | Saccharopolyspora | MAQLRELRNRIRSVKSTRKITKAQELIATSRIMKAQARVEASRPYADEITNVLTALADASTLDHPLLTERENPKRAGVLVVTSDRGFCGGYNANVLRAAEELQTLLREQGKTPVLYVVGRKGEAYYRFRQREIAKSWTGFTDRPDYSDAADIGETLVKAFLAGADDYLDDGGPDGTLGVDELHLVHTEFVSMITQKPSVKRVAPLEVEYSEEPQKTLRPVYDFEPDADTLFKALLPKYINTRLFAGLLDAAASEHAARRTAMKSATDNADEIIRTLSREANQARQAQITQEISEIVGGVEALSSAGSE | Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex. | A4FN28 |
Q8TI26 | TBP1_METAC | TATA-box factor 1 | Methanosarcina | MSESSIKIENVVASTKLAEEFDLTVIESEFEGAEYNKQKFPGLVYRVSDPKAAFLVFTSGKVVCTGAKNVADVHTVIGNMAKKLNSIGIKTMENPQITVQNIVASADLHTILNLNAIAIGLGLENIEYEPEQFPGLVYRIDEPKVVVLIFSSGKLVVTGGKSPEDCERGVEVVRQQLDNMGLL | General factor that plays a role in the activation of archaeal genes transcribed by RNA polymerase. Binds specifically to the TATA box promoter element which lies close to the position of transcription initiation. | Q8TI26 |
Q0VF58 | COJA1_MOUSE | Collagen alpha-1(Y) chain | Mus | MRHTGSWKLWTWVTTFLLPACTCLTVRDKPETTCPTLRTERYQDDRNKSELSGFDLGESFALRHAFCEGDKTCFKLGSVLLIRDTVKIFPKGLPEEYAIAVMFRVRRSTKKERWFLWKILNQQNMAQISVVIDGTKKVVEFMFRGAEGDLLNYVFKNRELRPLFDRQWHKLGIGVQSRVLSLYMDCNLIASRHTEEKNSVDFQGRTIIAARASDGKPVDIELHQLRIYCNANFLAEESCCNLSPTKCPEQDDFGSTTSSWGTSNTGKMSSYLPGKQELKDTCQCIPNKEEAGLPGTLRSIGHKGDKGEPGEHGLDGTPGLPGQKGEQGLEGIKGEIGEKGEPGAKGDSGLDGLNGQDGLKGDSGPQGPPGPKGDKGDMGPPGPPALTGSIGIQGPQGPPGKEGQRGRRGKTGPPGNPGPPGPPGPPGLQGLQQPFGGYFNKGTGEHGASGPKGEKGDTGLPGFPGSVGPKGHKGEPGEPLTKGEKGDRGEPGLLGPQGIKGEPGDPGPPGLLGSPGLKGQQGPAGSMGPRGPPGDVGLPGEHGIPGKQGVKGEKGDPGGRLGPPGLPGLKGDAGPPGISLPGKPGLDGNPGSPGPRGPKGERGLPGLHGSPGDTGPPGVGIPGRTGSQGPAGEPGIQGPRGLPGLPGTPGMPGNDGAPGKDGKPGLPGPPGDPIALPLLGDIGALLKNFCGNCQANVPGLKSIKGDDGSTGEPGKYDPAARKGDVGPRGPPGFPGREGPKGSKGERGYPGIHGEKGDEGLQGIPGLSGAPGPTGPPGLTGRTGHPGPTGAKGDKGSEGPPGKPGPPGPPGVPLNEGNGMSSLYKIQGGVNVPGYPGPPGPPGPKGDPGPVGEPGAMGLPGLEGFPGVKGDRGPAGPPGIAGISGKPGAPGPPGVPGEQGERGPIGDTGFPGPEGPSGKPGINGKDGLPGAQGIMGKPGDRGPKGERGDQGIPGDRGPQGERGKPGLTGMKGAIGPVGPAGSKGSTGPPGHQGPPGNPGIPGTPADAVSFEEIKHYINQEVLRIFEERMAVFLSQLKLPAAMLSAQAHGRPGPPGKDGLPGPPGDPGPQGYRGQKGERGEPGIGLPGSPGLPGSSAVGLPGSPGAPGPQGPPGPSGRCNPEDCLYPAPPPHQQAGGK | May act as a cross-bridge between fibrils and other extracellular matrix molecules. Involved in skeletal myogenesis in the developing esophagus. May play a role in organization of the pericellular matrix or the sphinteric smooth muscle. | Q0VF58 |
Q0C604 | YBEY_HYPNA | Endoribonuclease YbeY | Hyphomonas | MISFDLIVEDDSWAALGDLEALCRKAFDAAEYVAPVEEGNIALLLADNHVLHQLNLDFRSKDKPTDVLSFPSLPMDRPFLGDIAVAWGVSASDAKIQGKPLDAHLVHLLIHGYLHLLGFDHETDDEAAEMEALEIKALASLDIANPYRND | Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA. | Q0C604 |
Q2JS37 | PSBJ_SYNJA | Photosystem II reaction center protein J | unclassified Synechococcus | MTSQARIPLWIVAVVVGLGVVTVVGLFFYGSYTGLGAPV | One of the components of the core complex of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. | Q2JS37 |
B0TZ23 | SUCC_FRAP2 | Succinyl-CoA synthetase subunit beta | Francisella | MNLHEYQAKDLLESYGLKVQKGIVAHNPNEAAQAFDQLGGKFAVVKAQVHAGGRGKAGGVKVVKSSQEAREVAESLIGTNLVTFQTDAEGQPVNSVGVFEDVYPVTRELYLGAVVDRSSRKVTFMASTEGGVDIEEVAHNTPEKILKVEVDPLVGLQPFQAREVAFKLGLEGKQINDFVKTMLGAYKAFVECDFALFEINPLAVRENGEIVCVDGKINLDSNALYRHPKLLALRDKSQENAKELKASEHELNYVALEGNIGCMVNGAGLAMATMDIIQLYGGKPANFLDVGGGATKERVIEAFKLILDDENVKAVLINIFGGIVRCDMIAEAIIEAVKEVNVTVPVVVRLEGNNAEKGAKILADSGLTLIPADGLADAADKVVKSLG | Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit. | B0TZ23 |
Q8N7E2 | CBLL2_HUMAN | c-Cbl-like protein 2 | Homo | MNKMPAGEQECEYNKEGKYYSKGVKLVRKKKKIPGYRWGDIKINIIGEKDDLPIHFCDKCDLPIKIYGRIIPCKHAFCYHCANLYDKVGYKVCPRCRYPVLRIEAHKRGSVFMCSIVQQCKRTYLSQKSLQAHIKRRHKRARKQVTSASLEKVRPHIAPPQTEISDIPKRLQDRDHLSYIPPEQHTMVSLPSVQHMLQEQHNQPHKDIQAPPPELSLSLPFPIQWETVSIFTRKHGNLTVDHIQNNSDSGAKKPTPPDYYPECQSQPAVSSPHHIIPQKQHYAPPPSPSSPVNHQMPYPPQDVVTPNSVRSQVPALTTTYDPSSGYIIVKVPPDMNSPPLRAPQSQNGNPSASEFASHHYNLNILPQFTENQETLSPQFTQTDAMDHRRWPAWKRLSPCPPTRSPPPSTLHGRSHHSHQRRHRRY | E3 ubiquitin ligase catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins . May operate on tyrosine-phosphorylated SRC substrates . | Q8N7E2 |
Q1IG22 | APAH_PSEE4 | Diadenosine tetraphosphatase | Pseudomonas | MATYAVGDLQGCLQPLKCLLERAHFNPAVDRLWLVGDLVNRGPESLETLRYLYSIRDSLVCVLGNHDLHLLAAWHNVERLKKSDTLREIIEAPDADQLFDWLRRQKLLHYDEPRGIAMVHAGIPPQWTLGKALELAAEVEEVLRDDGRLKLYLDGMYGNEPNKWSKDLAGVERLRVITNYFTRMRFCTATGKLDLKSKEGLESAPKGYKPWFDHPDRRSRHVKIIFGHWAALEGRVDVPGVIALDTGCVWGGAMTLYNVDSGEYHRCDCTREGTPRPAALNNDQP | Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield ADP. | Q1IG22 |
Q3AZA2 | RPOC2_SYNS9 | Transcriptase subunit beta' | unclassified Synechococcus | MTTSKPRKPSKAKAAKAAKAAKAALEKISKPLSKTPPPFRNHIIDKKALKNLVAWSFKHHGTAVTSSMADDLKDLGFKYATQAAVSISVDDLKVPAAKKDLLGQAEEQITATEERYRLGEITEVERHTKVIDTWTETNERLVDAVKKNFDENAPLNSVWMMANSGARGNMSQVRQLVGMRGLMANPQGEIIDLPIRTNFREGLTVTEYVISSYGARKGLVDTALRTADSGYLTRRLVDVAQDVIVREDDCGTMRHIVVEAEDSKFAKRLVGRLTAAQVVSAEGEVLAERDTEIDPALSSKIEKAGITAVSIRSPLTCEANRSVCRKCYGWALAHNELVDLGEAVGIIAAQSIGEPGTQLTMRTFHTGGVSTAESGVVRSKVAGDVEFGSKARVRPYRTPHGVEAQQAEVDFTLTIKPSGKGRPQKIDITLGSLLFVDNGQAIESDVTVVQIAAGAVQKSVEKATKDVICDLAGQVHYEDKIQPREVTDRQGNITLKAQRLGRMWVLAGDVYNLPPNALPVVDGKSTVTEGQVLAEASQRSEFGGDVRLRDSIGDSREVQIVTTAMTLKDFKLLEESNHSGELWNLEAKDGTRYRLNTIPGSKIGNGEVIAELADDRFRTGTGGLVKFAPGLAIKKARSAKNGYEVNKGGTLLWVPQETHEINKDISLLMITDGQWIEAGTEVVKDIFSQTAGVVTVTQKNDILREIIVRGGDLRLISDNKALERFEGDGQMVNPGDDVAKGVSVDTMKFVQTVETPEGKGLLLRPVEEYTIPNEAQLPELSHLKQANGPHLGIKATQRLAFKDNELIKSVEGVELLKTQLLLETFDTTPQMTVDVERAPDKRAKTISRLRLVILESILVRRDTMSDSSHGSTHTDLQVEDGISVKAGDVVATTQILCKQEGVVQLPEATEAEPVRRLIVERPEDTTTISTSGKPSVAVGDRVVDGDLLASGQPSDCCGEVEAVDGSSVTLRLGRPYMVSPDSLLHVRDGDLVQRGDGLALLVFERQKTGDIVQGLPRIEELLEARRPRDSAILCRKPGTVEIKQGEDDDSLSVNVIESDDAIGEYPILLGRNVMVNDGQQVTAGELLTDGPINPHELLECFFEDFRSRKPLMDAAQEAIANLQHRLVTEVQNVYKSQGVSIDDKHIEVIVRQMTSKVRVEDAGDTTLLPGELIELRQVEDTNQAMAITGGAPSEFTPVLLGITKASLNTDSFISAASFQETTRVLTEAAIEGKSDWLRGLKENVIIGRLIPAGTGFSGFEEELQKEAGPHPDILSEDPAGYRRMQNLRPDYTVDMPPAASSSALLADPSDADLEATRTRHNIDPSASTNAAFTRPDVDNELKEEQVVDAEAVEGLQEEGLLSDD | DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | Q3AZA2 |
B4SHL3 | GLNE_STRM5 | Adenylyl transferase | Stenotrophomonas maltophilia group | MTLAPADLPASLQPLVDRALARLAQVLPEPIPANLLPLLTRLAVTSDFALDTLVRQPALLAQLAAPGCPPIPAPVLDPLQPSDWPAQIRRWRTAMSTRLIWRDLTGLDDVAQTLAGATALAEDCLRLALDALQQEFAQRHGVIADEHGIPQQLVVFGLGKLGGGELNFSSDVDLVYAYPQGGESDGPRPLAAEEYFARLGQRLAKLLDETTVDGFSHRVDLRLRPFGSAGRVALSFAAMDQYFQREGRDWERYAWLKARAVAGDIEAGEAWLQTLRPFVYRRYLDFTALDGLREMKAAITAEVARRELHDDIKRGAGGIREIEFLCQALQLIRGGREPALRERRLLVALDALVAAGQIAPEDGSALREAYLFLRRLENRLQMLRDAQTHVLPSDALDRERIAVGLGYPDWEVLRAALAVQQQRVSTEFAALLAPRKGQAAPDALANYWRSLPEGSNAPLLAEAGFLDANGADQSLRDFAQGTGVKSLSDAARARLDRVLPALLHAATRSPQPDAALKRVLGLLQAVLRRTSYLALLDEQPSALARLVDVLARSALLAERLAAYPLLLDELLDVRVSGPMPDAAGMLAECQQVLAVEDPESALRWLNETRLALSFRMAMATLDGRQGAVDSTRQLAELAQAVVVTVLAMAEADMHAAHGEIPGGRFAIIGYGSLGGLELGFGSDLDLVFLHDNPAGVDASDGARPLEPGRWYARLAQKVMALLGAVTAAGRLYDIDVRLRPDGGKGSLVSSLASYTEYQRERAWTWEHQALVRARGVAGDASLLADFEQVRAQTLGRERDTGVLYADVLKMRGRMRTELDRSDAARLDLKQGAGGVVDLEFLLQTGVLARSARHAALLQPRDTPSLIDALAVAEFLPEDTAQALHGAHATLLDVGLACTLDRRPRLAPTTPAIEEACAAITAACIAAELPFA | Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of GlnE binds the signal transduction protein PII (GlnB) which indicates the nitrogen status of the cell. | B4SHL3 |
P54005 | DIA1_YEAST | Digs into agar protein 1 | Saccharomyces | MGSISRYLLKKAADGLKDEQRLKIEMSDSKSVPECFHFNRERRMPIAEINGEDGFFMFPSQQSLENFENTKKYSNELSPDAIGIPLFQIINCTLPFGKRGHSNTVVGNVPYYKIFKFILRTADEPPPYTVAKIVCSNNGLILYKVPLYDIYKNVSQANVTYSFVGTTSTEPNLLAMAHREGHRDLDTKVNNLNLRWHVTYSPVVTNDHYKLILLADYEVNRLDEDVIRAAKNKMSIDQKDQKVQRFVAAHYTREFETSLFRWVAQEGHLILGEYSTDQGSFGLNNIPPLTEELGCQSLLIHYIEYMKRQRKKIAKEARRQNKRNVANTTNMNMNLM | Involved in regulation of invasive growth. | P54005 |
P83437 | COG5_BOVIN | Component of oligomeric Golgi complex 5 | Bos | IGALQGAVDRVLTQPTQSIVRNVAVVNSLYK | Required for normal Golgi function. | P83437 |
Q8MA72 | MATK_BYBLI | Intron maturase | Byblis | MEEIQIYLQLERSQQHDFLYPLIFQEYIYAFAHDRGFNRSISSENLGYDNKFSFLIVKRLISRMYQQNHFFISLNDSNKNLFCARNKNFDSQIISEVFACIVEIPFSIPYINLEWKKKKIVKPQNLRSIHSTFPFLEDNFSHLNLLVDILIPYPIHAEILVQTLRYWIKDASSLHLLRFFLHEYCILNSFIIPKKASSSFSNFSKRNPKLFLFLYNSHVCEYESVFLFLRNQSSHLRSTSSGVLLERIYFYRKIERLVNTFVKLKYFQPNLWFVKEPYIHYVSYQKIASLASKGTSLLMKKWKCYFVTFWQWYFSLWFHPKRIYIKQLSNQSFYFLGYLSSVRMNFSVVRSQILGKSFLINNVIKKFDTLVPTIPMIASLAKAKFCNVLGHPISKPVWADLSDSHIIDRFWRICRNISHYHSGSSKKKSLYRIKYILRLSCARTLARKHKSTVRTFLKKLGSELLKEFFRSEEDVFSLTFHKASPAFWEVYRSRIWYLDIICLNDLGNPKSQF | Usually encoded in the trnK tRNA gene intron. Probably assists in splicing its own and other chloroplast group II introns. | Q8MA72 |
A3MYL1 | LEUC_ACTP2 | Isopropylmalate isomerase | Actinobacillus | MAKTLYEKLFDAHVVYEAAGETPILYINRHLIHEVTSPQAFDGLRVAGRQVRQIGKTFGTMDHSISTQVRDVNKLEGQAKIQVLELAKNCEANGISLFDMQTKEQGIVHVMGPEQGLTLPGMTIVCGDSHTATHGAFGALAFGIGTSEVEHVLATQTLKQARAKSMKVEVRGKVNPGITAKDIVLAIIGKTTMAGGTGHVVEFCGEAIRNLSMEGRMTVCNMAIEFGAKAGLVAPDETTFAYLKDRPHAPKGKDWDDAVEYWTTLKSDDDAVFDSVVVLEAKDIAPQVTWGTNPGQVIGIDQVVPNPQEMADPVTKASAEKALAYIGLDANTDMKNIPVDQVFIGSCTNSRIEDLRAAAAVMKGRKKADNVKRVLVVPGSGLVKEQAEKEGLDKIFIEAGAEWRNPGCSMCLGMNDDRLGEWERCASTSNRNFEGRQGRNGRTHLVSPAMAAAAAMFGKFVDIRHVELN | Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate. | A3MYL1 |
Q81EP4 | LDH1_BACCR | L-lactate dehydrogenase 1 | Bacillus cereus group | MKKGINRVVLVGTGAVGCSYAYCMINQAVAEEFVLVDVNEAKAEGEAMDLSHAVPFAPAPTRVWKGSYEDCKDADLVVITAGLPQKPGETRLDLVEKNAKIFKQIVRSIMDSGFDGIFLIATNPVDILTYVTWKESGLPKERVIGSGTTLDSARFRYMLGEYFDIGPHNIHAYIIGEHGDTELPVWSHVSVGIQKLQTLLEKDNTYNQEDLDKIFINVRDAAYHIIERKGATYYGIGMSLLRVTKAILNDENSVLTVSAYLEGQYGQKDVYIGVPAVLNRGGVREILEVELSEDEELKFDHSVQVLKETMAPVL | Catalyzes the conversion of lactate to pyruvate. | Q81EP4 |
P0CE00 | MPH3_YEAST | Maltose transport protein 3 | Saccharomyces | MKNLSFLINRRKENTSDSNVYPGKAKSHEPSWIEMDDQTKKDGLDIVHVEFSPDTRAPSDSNKVITEIFDATEDAKEADESERGMPLATALNTYPKAAAWSLLVSTTLIMEGYDTAILGAFYALPIFQRKFGSQNDKTGEWEISASWQIGLTLCYMAGEIVGLQLTGPSVDLVGNRYTLIIALFFLAAFTFILYFCNSLGMIAVGQALCGMPWGCFQCLTVSYASEICPLALRYYLTTYSNLCWLFGQLFAAGIMKNSQKKYADSELGYKLPFALQWILPVPLALGIFFAPESPWWLVKKGRFDEARRSLRRTLSGKGPEKEILVTLEVDKIKVTIDKEKRLTSKEGSYSDCFEDKINRRRTRITCLCWAGQATCGSILIGYSTYFYEKAGVSTEMSFTFSIIQYCLGICATFLSWWASKYFGRYDLYAFGLAFQTIVFFIIGGLGCSSTHGSKMGSGSLLMAVAFFYNLGIAPVVFCLVSEMPSSRLRTKTIILARNTYNVVSIICSVLILYQLNSKKWNWGAKSGFFWGVLCFCTLIWAVVDLPETAGKTFVEINELFKLGVSARKFKSTKVDPFVVKTPPKDVSHNDPKGDIEASIAEE | High-affinity uptake of maltose and maltotriose. Also transports alpha-methylglucoside, glucose and turanose but not melezitose or trehalose. | P0CE00 |
P9WIW7 | NUOA_MYCTU | NUO1 | Mycobacterium tuberculosis complex | MNVYIPILVLAALAAAFAVVSVVIASLVGPSRFNRSKQAAYECGIEPASTGARTSIGPGAASGQRFPIKYYLTAMLFIVFDIEIVFLYPWAVSYDSLGTFALVEMAIFMLTVFVAYAYVWRRGGLTWD | 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 a menaquinone. 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. | P9WIW7 |
A0RBG1 | QUEC_BACAH | Queuosine biosynthesis protein QueC | Bacillus cereus group | MKKEKAVVVFSGGQDSTTCLFWAIEQFAEVEAVTFNYNQRHKLEIDCAAEIAKELGIKHTVLDMSLLNQLAPNALTRTDMEITHEEGELPSTFVDGRNLLFLSFAAVLAKQVGARHIVTGVCETDFSGYPDCRDVFVKSLNVTLNLSMDYPFVIHTPLMWIDKAETWKLSDELGAFEFVREKTLTCYNGIIGDGCGECPACQLRKAGLDTYLQEREGASN | Catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)). | A0RBG1 |
A8F7D4 | NUSB_PSELT | Antitermination factor NusB | Pseudothermotoga | MTRRSKMRDLVFKVIFQNEFRNDSIETVLEDILHISKSGLMKADITRYVKGIYENLPSIDEKISLCLENWSLQRLSLVDRSILRLATYELLYESDVPIEVTLDEAVEIAKKYGTENSSKFVNGVLDKVAKSFAPEEKRYI | 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. | A8F7D4 |
A7E559 | MMM1_SCLS1 | Maintenance of mitochondrial morphology protein 1 | Sclerotinia | MWLDDVASELSFTQGLLLGQLSIVILIGAFIKFFIFGDPPSPDVSAALRATERRSRTLAHKRSLLTLRSSTPRHASQSLNRKRSSVLRNPAPLTTNAILSKTYYNVDSHQPESLDWFNVLIAQTIAQFRADAQHDDAILTSLTKALNGGNRPDFLDEIKVTELSLGEDFPIFSNCRVIPVDEDGITLGREGGAAGREHGRLQARMDVDLSDFITLAVETKLLLNYPKPLVAVLPVALAVSVMRFSGTLSISFVPGSPLNGSPTTLAFCFLDDYRLDLSIRSLVGSRSRLQDVPKIAQLIEARLHTWFDERCVEPRFQQIELPSLWPRKKNTRGGEDLDTGSEAGGIGRARSRDVERDLREEARKEVEAETGVRVGRSKLGVSLDVPDVGLDGGSEEGLRFRRRSRGRGDEYAMPGSMPGLSMA | Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondria. The mdm12-mmm1 subcomplex functions in the major beta-barrel assembly pathway that is responsible for biogenesis of all outer membrane beta-barrel proteins, and acts in a late step after the SAM complex. The mdm10-mdm12-mmm1 subcomplex further acts in the TOM40-specific pathway after the action of the mdm12-mmm1 complex. Essential for establishing and maintaining the structure of mitochondria and maintenance of mtDNA nucleoids. | A7E559 |
B7IFW4 | SYS_THEAB | Seryl-tRNA(Ser/Sec) synthetase | Thermosipho | MIDVKLLRKNPEIFYDAIKKRNMDTEIIDKILEVDKEWRELVAKVNELKAKRNEFSKLVAKAKVEKDNEKASKLIEESKKIGEEIKKIEEQEKKLEEEMQNLALNIPNIPAEDVPFGKDESENIEIRRWGEPRKFDFEPKAHWDLGPELSMMDFERGAKLSGSRFTVLYSYLARLERALIQFMLDVHTKEHGYTEVWVPQLVKRDAMLWTGKLPKFEEDAYCIEKDDMFLIPTAEVPLVALHAQEILSEKDLPIKYTAYSACYRREAGSYGKDVRGMIRQHQFDKVELVWITTPERSFEDLERLTQDAERILQLLELPYRVVSLCSGDLGFVSAKTYDIEVWLPSYNSYKEISSCSNTTDFQTRRSNIRYRGSDNKLHYAHALNGSGLAVGRTLVAIVENYQNEDGSITVPKVLVPYMGVEKIEVK | Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec). | B7IFW4 |
Q28LT2 | RISB_JANSC | 6,7-dimethyl-8-ribityllumazine synthase | unclassified Jannaschia | MAGHSDNDLGLPSFDKPVKVAIVIAPYYTSISEAQLAAARGVLDAADVAHETIEVPGSLEVPTAIGIAHRMSNFDGFVALGCVIRGATSHYDVVVNESSRALTMLGLQGICIGNGIITVETRDQAEERADGGRLNTAGGAAEAALHLIALTRSYGAPKGALGFKPRGTIEIADGSSQA | 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. | Q28LT2 |
B4S113 | CH10_ALTMD | Chaperonin-10 | Alteromonas | MAIRPLHDRVILKRAEQESKSAGGIVLTGSAAEKSTRGEVIAVGNGRILENGEVKALDVKVGDTVIFNDGYGVKTEKLDGEEVLILSESDILAIVE | 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. | B4S113 |
Q8ZKH4 | DUSA_SALTY | tRNA-dihydrouridine synthase A | Salmonella | MQPETQSSALPAYRFSIAPMLDWTDRHCRYFLRLLSRQTQLYTEMVTTGAIIHGKGDYLAYSEEEHPVALQLGGSDPAQLAHCAKLAEARGYDEINLNVGCPSDRVQNGMFGACLMGNAQLVADCVKAMRDVVSIPVTVKTRIGIDDQDSYAFLCDFIDTVSGQGECEMFIIHARKAWLSGLSPKENREIPPLDYPRVYQLKRDFPHLTMSINGGIKSLEEAKEHLRHMDGVMVGREAYQNPGILAAVDREIFGADTTDADPVAVVRAMYPYIERELSQGAYLGHITRHMLGLFQGIPGARQWRRYLSENAHKAGADVAVLEQALKLVADKR | Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines. Specifically modifies U20 and U20a in tRNAs. | Q8ZKH4 |
Q90965 | RAB2A_CHICK | Ras-related protein Rab-2A | Gallus | MAYAYLFKYIIIGDTGVGKSCLLLQFTDKRFQPVHDLTIGVEFGARMITIDGKQIKLQIWDTAGQESFRSITRSYYRGAAGALLVYDITRRDTFNHLTTWLEDARQHSNSNMVIMLIGNKSDLESRREVKKEEGEAFAREHGLIFMETSAKTASNVEEAFINTAKEIYEKIQEGVFDINNEANGIKIGPQHAATNATLAGNQGGQQAGGGCC | The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between active GTP-bound and inactive GDP-bound states. In their active state, drive transport of vesicular carriers from donor organelles to acceptor organelles to regulate the membrane traffic that maintains organelle identity and morphology. | Q90965 |
P35828 | SLAP_CAUVC | Paracrystalline surface layer protein | Caulobacter | MAYTTAQLVTAYTNANLGKAPDAATTLTLDAYATQTQTGGLSDAAALTNTLKLVNSTTAVAIQTYQFFTGVAPSAAGLDFLVDSTTNTNDLNDAYYSKFAQENRFINFSINLATGAGAGATAFAAAYTGVSYAQTVATAYDKIIGNAVATAAGVDVAAAVAFLSRQANIDYLTAFVRANTPFTAAADIDLAVKAALIGTILNAATVSGIGGYATATAAMINDLSDGALSTDNAAGVNLFTAYPSSGVSGSTLSLTTGTDTLTGTANNDTFVAGEVAGAATLTVGDTLSGGAGTDVLNWVQAAAVTALPTGVTISGIETMNVTSGAAITLNTSSGVTGLTALNTNTSGAAQTVTAGAGQNLTATTAAQAANNVAVDGGANVTVASTGVTSGTTTVGANSAASGTVSVSVANSSTTTTGAIAVTGGTAVTVAQTAGNAVNTTLTQADVTVTGNSSTTAVTVTQTAAATAGATVAGRVNGAVTITDSAAASATTAGKIATVTLGSFGAATIDSSALTTVNLSGTGTSLGIGRGALTATPTANTLTLNVNGLTTTGAITDSEAAADDGFTTINIAGSTASSTIASLVAADATTLNISGDARVTITSHTAAALTGITVTNSVGATLGAELATGLVFTGGAGADSILLGATTKAIVMGAGDDTVTVSSATLGAGGSVNGGDGTDVLVANVNGSSFSADPAFGGFETLRVAGAAAQGSHNANGFTALQLGATAGATTFTNVAVNVGLTVLAAPTGTTTVTLANATGTSDVFNLTLSSSAALAAGTVALAGVETVNIAATDTNTTAHVDTLTLQATSAKSIVVTGNAGLNLTNTGNTAVTSFDASAVTGTGSAVTFVSANTTVGEVVTIRGGAGADSLTGSATANDTIIGGAGADTLVYTGGTDTFTGGTGADIFDINAIGTSTAFVTITDAAVGDKLDLVGISTNGAIADGAFGAAVTLGAAATLAQYLDAAAAGDGSGTSVAKWFQFGGDTYVVVDSSAGATFVSGADAVIKLTGLVTLTTSAFATEVLTLA | The S-layer is a paracrystalline mono-layered assembly of proteins which coats the surface of bacteria. Probably acts as a physical barrier to parasites and lytic enzymes. | P35828 |
Q9SKB7 | IP5PE_ARATH | Type II inositol polyphosphate 5-phosphatase 14 | Arabidopsis | MDSVIIEPDEREALASLVPAHPLPPRKTHSYVEQCEQKPHHPIRKYSLDEGSRSVTSDSEAVYFDSSDGEFSTEGVAIVDGRTSGERGNGEECGFVTPPSKPASQGGGNDGGREDDIESLPEFIGAGGGLDVFKVPVRAAVNPGRPPCLELRPHPLRETQTGKFLRNIACTESQLWAGQENGVRFWNLEEAYEVGCGLGGQVRRGDEDTAPFHESVPTSPALCLLVDHGNRLVWTGHKDGKIRAWKMNQPNTTTADDSKPFKERLSWQAHRGPVNYIVISSYGDMWSCSDGGVIKIWTLDSLEKSLVLKLEEKHMAALLVERSGIDLRSQVTVNGTCSISSSDVKFLLVDTVKAKVWAVQHLSFSLWDAQNKELLKVFNIDGQVENRVDMPPTQGQQVEDTKAKFFSAPKKEKSQGFLQRSRHAIMGAAGAVRRAATRSAGAFAEDTRKVEAIAIAADGSIWTGSMNGVIAQWDGNGSRLREVNHHQQAVLCFCTFGDRIYVGYSSGYIQVLDLGGKLIASWVSHNEPVIKLAAGGGFIFSLATHGGVRGWYVTSPGPLDSLIRTELSQKEMAYARQDSVKILIGTWNVGEGRASRGALVSWLGSAVSDVGIVAIGLQEVDMGAGFLAMSTAKETVGVEGSAVGQWWLDAIGNALDERNTFERMGSRQLAGLLISLWVRKSIRTHVGDLDVAAVPCGFGRAIGNKGGVGLRIRVYDRIMCFVNCHLAAHLEAVTRRNADFNHIYRSMVFSKGQSVYTAAAAGASTSAQALKNNPNTNNSTEEEKSHLASADLVAFFGDFNYRLFGITYDEARDFISHRSFDWLREKDQLRQEMNEGKVFQGMREALITFPPTYKFEKNKPGLGGYDSGEKKRIPAWCDRVIYRDNQSISYTECSLKCPVVSSTIMYEACMDVTESDHKPVRCKLHANIAHTDKSVRRQELGKIVKSNEKLRAMFEELKSVPETSVSTNNILLHSQDTFIFTIRNTSNSSRAIFNIVCKGQTLVREDGEEPDNHSRGTFGLPRWLEVSPGAGIIKPDASLQVKVHHEDSHNSEEFIDGIQQNSLSEESSDKEVTLIIIVQGSCSTRTISHSIKVRHCSSAAKSLSLVHSKTTTMTKNLEGSTRYQTDANRGGSTRHRTDDSTRRG | Has phosphatase activity toward PtdIns(4,5)P2, PtdIns(3,4,5)P3 and Ins(1,4,5)P3. | Q9SKB7 |
Q1IWK0 | TRMB_DEIGD | tRNA(m7G46)-methyltransferase | Deinococcus | MIFRLADFHFPDSAARLYPDTPQRPWILEVGFGDGRFWPHYAATFPEAPNYLGVEISGVSLLKAERRLREAGLSNAVLTKLPATPLIREVVPAGSLDAIVVNFPDPWPKAGHAEHRLLRAPFFRLAASRLKPGGAVLLTTDHDEYFEFACREAEASGVMRAELTDPPPAALETKYARKWRELGLEVQHARFVPTHHPHVPHGTVARFPDSEDAPAVPHAILTLPAAFDPGAFHKHTARGGQTREDPVGWTVVLLELYRSLKQDGWVMLAHVVEGELTQEVLIGISARGDGSHLVRLASFGGPIITPGVKAAVGVVTDWLEEQGAAVRHRGY | Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. | Q1IWK0 |
B8F870 | ERPA_GLAP5 | Iron-sulfur cluster insertion protein ErpA | Glaesserella | MSDILVPLIFTDAAAKKVKFLIEGEENPELRLRVYITGGGCSGFQYGFTFDDKLNEGDLTIENLDVALVIDPMSLQYLIGATIDYVEGLDGSRFVVQNPNASSTCGCGASFSI | Required for insertion of 4Fe-4S clusters for at least IspG. | B8F870 |
A9AB23 | RNP4_METM6 | Rpp21 | Methanococcus | MKLKKKFLEKSKKIAEERIDVLMNLAEKESKDGKADRSKNYVLLGKKIAMRMRMPYPKEWKRRICKNCGSFLIYGKNARVRTKAKNYPHVVITCLECNSITRIPIKTEKK | Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. | A9AB23 |
C0HJV6 | CTX4_LACTA | Cytoinsectotoxin-4 | Lachesana | MKCFILAAALVLAFACIAASEPAETENEDLDDLSDLEDEEWLDELEEAAEYLESLREFEESRGYKDYMSKAKDLYKDIKKDKRVKAVMKSSYMKEAKKLYKDNPVRDAYQVYKGVKAGGKLLFG | Insecticidal and antimicrobial peptide. Has insecticidal activity against larvae of flesh fly S.carnaria. Has antibacterial activity against Gram-positive bacterium B.subtilis B-501 (MIC=2.5 uM) and Gram-negative bacterium E.coli DH5alpha (MIC=10 uM). | C0HJV6 |
D2Y207 | H2A04_CYRHA | Peptide F8-20.15 | Haplopelma | MKMTLIAILTCAAVLVLHITAAEELEAESQLMEVGMPDTELEAVDEERLFECSVSCEIEKEGNKDCKKKKCKGGWKCKFNMCVKV | Neurotoxin active on both insects and mammals. | D2Y207 |
C5D5E9 | RUVA_GEOSW | Holliday junction ATP-dependent DNA helicase RuvA | unclassified Geobacillus | MIEFVRGYVDYVCPEYIVIDNNGIGYQIFTPNPFSFQESRDTIVTVYTYQYVREDTLALYGFRTREERTLFAKLLQVSGIGPKGGLAILAAGQPEQLVEAIEQENETFLCKFPGVGKKTARQMILDLKGKLTAVTAKTFPDLFHLQEESARPHLSALEEAIEALKALGYAEREIQKVVPSLMKENLSTDQYVKRALQQLLK | The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. RuvA stimulates, in the presence of DNA, the weak ATPase activity of RuvB. | C5D5E9 |
C0QTL3 | EFTS_PERMH | Elongation factor Ts | Persephonella | MATDAKLVKTLREMTGAGILECKKALEETGGNLEEAVELLRKRGIAKAAKKAGRETKEGIIHSYIHAGGRVGVLLELNCETDFVARNEVFKELANEIALQIAAMKPQYVSREDIPREVIEKEGEIAREAAIAEGKPEHIAEKIAEGKLEKFFKEVCLLEQPYIKDDKKTIEDLIKEYIAKLGENIKVSRFCRYEIGE | Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome. | C0QTL3 |
Q2NEH4 | HEM1_METST | Glutamyl-tRNA reductase | Methanosphaera | MLVNIRIDFKIADIETMEKSYAKLDMINAELHEKLDILEEVTLKTCNRYEIYLLIDEEVNIPTTTFIVEKNDMAINHLLRLASGLESMIMGEDQILGQIKTARKNAIKNKTIGPKLEKVFTKAIHVGQTIRKNTHINEGGVSVGSGAVELIEEKYGSLKGKNVLIIGAGEMGTVVSKALLEKETNTIVVANRTYDKARQLAQELDGEAIKFDEMNNELVNIDIVISSTGAPHSIISKERIAFLPEEHLHDMIMLDLANPHDIENDVQELGVKLYNLDDLRYVTDKNKERRNKEAIKAEAIIEDETLLLKESLKQMEITPILSSLNIEAEKIRKQELDKTLHMLDLDKKSSKKVDYLTRSITDKLLYNIINNLKEAAANNDKDTIRNAKKILLEYN | Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA). | Q2NEH4 |
Q4H186 | MATK_PILTE | Intron maturase | Pillansia | MEELQGYFEKDRSRQQPFLYPLLFQEYIYALAHDRGLNRNGSIFYEPLEVFGYDSKSSLALVKRLITRIYQQHFFLSSVNDSNQNQFVGHHHTNFFYSRFYSQMISEGFAIIVEIPFSLQLVSYLKEKEIPKSHNLRSIHSIFPFLEDKLLHFNYVSDILIPHPIHMEILVQILQCWIQDVPLLHFLRFFLHEYHNWNSFFITQNKSIYLFSKETKRLFRFLYNSYVYECEFVFVFLRKYSSYLRFTSFRTFLERRYFYGKMEHLQTEHLIIVCCDYFNGTLWSFKDPFMHYARCQGKAILVSKGTHLLMKKWKYNFVNLWQYYFHFWYQSYRIHINQLSKHSFHFLGYLSSLLKNSSTVRNQMLDNSFLIDTLTTKFDTAVPVIFLIVSLSKAQFCTVSGHPISKPIWTDLSDSGIIERFGRICRNLSHYHSGSSKKQGLYRIKYILRLSCARTLARKHKSTVRTFLQRLGSRLLEEFFTEGEQDLSLILPKAIPFPFQGSHRERIWYLDIIRINDLVNRL | Usually encoded in the trnK tRNA gene intron. Probably assists in splicing its own and other chloroplast group II introns. | Q4H186 |
Q9ZBR6 | THID_STRCO | Hydroxymethylpyrimidine phosphate kinase | Streptomyces albidoflavus group | MTAPTPPVTPPLVLTVAGSDSGGGAGIQADLKTMLALGTHGMSVLTAVTAQNSRGVQGAWELPVEAVRAQYRSVVDDIGVQAVKTGMLSSAELVETVAELLAGTDAPAVVDPVGVSKHGDALLASSALESVRTRLLPVATVATPNLDEVAQLTGVRVDDETDLRRAAAAVLAFGPRWALIKGGHLAGDAVDLLTDGSEEHWLRAPRLDNRHTHGTGCTLASAVACGLAKGQSVPVAVRAAKEYVTGAITAGFPLGGGIGPVDHGWALGE | Catalyzes the phosphorylation of hydroxymethylpyrimidine phosphate (HMP-P) to HMP-PP, and of HMP to HMP-P. | Q9ZBR6 |
A6TGP0 | RPOB_KLEP7 | Transcriptase subunit beta | Klebsiella | MVYSYTEKKRIRKDFGKRPQVLDVPYLLSIQLDSFQKFIEQDPEGQYGLEAAFRSVFPIQSYSGNSELQYVSYRLGEPVFDVKECQIRGVTYSAPLRVKLRLVIYEREAPEGTVKDIKEQEVYMGEIPLMTDNGTFVINGTERVIVSQLHRSPGVFFDSDKGKTHSSGKVLYNARIIPYRGSWLDFEFDPKDNLFVRIDRRRKLPATIILRALNYTTEQILDLFFEKVVFEIRDNKLQMELIPERLRGETASFDIEANGKVYVEKGRRITARHIRQLEKDDIKHIEVPVEYIAGKVAAKDYIDEATGELICPANMELSLDLLAKLSQSGHKRIETLFTNDLDHGPYISETVRVDPTNDRLSALVEIYRMMRPGEPPTREAAESLFENLFFSEDRYDLSAVGRMKFNRSLLRDEIEGSGILSKDDIIEVMKKLIDIRNGKGEVDDIDHLGNRRIRSVGEMAENQFRVGLVRVERAVKERLSLGDLDTLMPQDMINAKPISAAVKEFFGSSQLSQFMDQNNPLSEITHKRRISALGPGGLTRERAGFEVRDVHPTHYGRVCPIETPEGPNIGLINSLSVYAQTNEYGFLETPYRKVTDGVVTDEIHYLSAIEEGNYVIAQANSNLDENGHFVEDLVTCRSKGESSLFSRDQVDYMDVSTQQVVSVGASLIPFLEHDDANRALMGANMQRQAVPTLRADKPLVGTGMERAVAVDSGVTAVAKRGGTVQYVDASRIVIKVNEDEMYPGEAGIDIYNLTKYTRSNQNTCINQMPCVSLGEPIERGDVLADGPSTDLGELALGQNMRVAFMPWNGYNFEDSILVSERVVQEDRFTTIHIQELACVSRDTKLGPEEITADIPNVGEAALSKLDESGIVYIGAEVTGGDILVGKVTPKGETQLTPEEKLLRAIFGEKASDVKDSSLRVPNGVSGTVIDVQVFTRDGVEKDKRALEIEEMQLKQAKKDLSEELQILEAGLFSRIYAVLVSGGVEAEKLDKLPRDRWLELGLTDEEKQNQLEQLAEQYDELKHEFEKKLEAKRRKITQGDDLAPGVLKIVKVYLAVKRRIQPGDKMAGRHGNKGVISKINPIEDMPHDANGTPVDIVLNPLGVPSRMNIGQILETHLGMAAKGIGDKINAMLKQQQEVAKLREFIQRAYDLGADVRQKVDLNTFSDEEVLRLAENLRKGMPIATPVFDGAKEAEIKELLQLGDLPTSGQITLFDGRTGEQFERPVTVGYMYMLKLNHLVDDKMHARSTGSYSLVTQQPLGGKAQFGGQRFGEMEVWALEAYGAAYTLQEMLTVKSDDVNGRTKMYKNIVDGNHQMEPGMPESFNVLLKEIRSLGINIELEDE | DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | A6TGP0 |
O89117 | DEFB1_RAT | Defensin, beta 1 | Rattus | MKTHYFLLVMLFFLFSQMELGAGILTSLGRRTDQYRCLQNGGFCLRSSCPSHTKLQGTCKPDKPNCCRS | Has bactericidal activity. May act as a ligand for C-C chemokine receptor CCR6. Positively regulates the sperm motility and bactericidal activity in a CCR6-dependent manner. Binds to CCR6 and triggers Ca2+ mobilization in the sperm which is important for its motility. | O89117 |
A7H1L5 | IF2_CAMJD | Translation initiation factor IF-2 | Campylobacter | MAKIRIHEIAKELGYDSKEIIEKANELGLGIKTASNAVEPDIAVAIYEYIQTREIPEAFKKNIKTPTAKKPKKENAKDQEKLNESEKKEPKKEESKEQEKQEIIDTHKPQSLASATLAKRRGLVIVKKKKDEEEIQVKKEEIKNSNDISINNEERLSLKTMFSNADESLKKKKKEKKSFVASKKESTEKMNFLDEHDFGDISLDDEDEVVLPDFSVKEQEKPQNINKKQPNFIRQAVGNSAGFGLEGGIQRRSRKKPPKKIEKKEVEEVSSVSISKEIRVYEFADKIGKSTSEVISKLFMLGMMTTKNDFLDEDAIEILAAEFGIEINIINEADEFDYVKDYEEETDEKDLVTRAPVITIMGHVDHGKTSLLDYIRKSRVASGEAGGITQHVGAYMVEKNGRKITFIDTPGHEAFTAMRARGASITDIVIIVVAADDGVKPQTKEAINHAKAAGVPIIIAINKMDKEAANPDMVKTQLAEMEIMPVEWGGSYEFVGVSAKTGMGIEDLLEIVLLQADILELKANPKSFAKASIIESSVQKGRGAVATIIVQNGTLAVGSTVVAGEAYGKVRAMSDDQGKALKEIKPGECGVIVGLSEVADAGEILIAVKTDKEAREYANKRHEYNRQKELSKSTKVSIDELGAKIKEGNLKALPVILKADVQGSLEALKASLEKLRNDEIKVNIIYSGVGGITQSDIELASASENSIVLGFNIRPTGEVKERAKDKGVEIKTYNVIYNLLDDVKALLGGMMSPIISEEQLGQAEIRQVINVPKIGQIAGCMVTEGVINRGAKIRLIRDGVVVYEGNVSSLKRFKDDAKEVAKGYECGVGIEGCDDMRVGDYIESYKEVEEQASL | One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex. | A7H1L5 |
A8YUK5 | YIDD_LACH4 | Putative membrane protein insertion efficiency factor | Lactobacillus | MRKILIFIVRIYQTLISPLFPPSCRYYPTCSNYMIDALKKHGPILGLIMGISRTLRCNPFVRGGVDPVPDNFTVFRNPHPERYEDEIIASKFHSNSK | Could be involved in insertion of integral membrane proteins into the membrane. | A8YUK5 |
P68285 | CRYAA_HIPAM | Alpha-crystallin A chain | Hippopotamus | MDIAIQHPWFKRALGPFYPSRLFDQFFGEGLFEYDLLPFLSSTISPYYRQSLFRTVLDSGISEVRSDRDKFVIFLDVKHFSPEDLTVKVQEDFVEIHGKHNERQDDHGYISREFHRRYRLPSNVDQSALSCSLSADGMLTFSGPKIPSGVDAGHSERAIPVSREEKPSSAPSS | Contributes to the transparency and refractive index of the lens. Acts as a chaperone, preventing aggregation of various proteins under a wide range of stress conditions. Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA. | P68285 |
C6BUG6 | KTHY_MARSD | dTMP kinase | Maridesulfovibrio | MFITFEGIEGTGKTTQIKKLTAFLEESGHNVDVTLEPGGSRIGKELRKILLNMDSTDITGECELFLYLADRAQHVGQVIKPAVEAGKIIISDRFADSTIVYQGYGRGLDPKLLRELNDVAVSGNWPDLTILLDIDPEIGLKRAMTRNLQENKMQEEGRFEAESLEFHNRVREGYLTWAALNNDRIVVVNADQTPDEIFKEIKAKVVERIKGDFVTNG | Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis. | C6BUG6 |
Q9KQ30 | 5NTD_VIBCH | 5'-nucleotidase | Vibrio | MKQGLILKSVLSAAIIASLAGCATAPAQQWEADKTYKLTILHTNDHHGRFWQNQYGEYGMAARKTLIDQLRADIEAQGGSVLLLSGGDINTGVPESDLQDAEPDFKGMSKIGYDAMALGNHEFDNPLEVLFKQKEWANFPMLSANIYDKATGKRLFEPYHIFDKQGIKIAVIGLTTEDTAKIGNPEYIGGIDFRDPKEEAKKVIAELKKKEKPDLIIAVTHMGHYQNGEHGVNAPGDVALARYLPAGELDMIVGGHSQEPVCMEGPNLVKKNFKPGDECKPDIQNGTYIVQAYEWGKYVGRADYEFRNGELNMVSYNLIPVNLKKKVEVNGETQRVFATSEIKEDSAMLEFLRPFQEKGQEQLSIKIAHSNGKLEGDRNVVRFEQTNLGRMIAMAHMQRAKADFAVMNSGGVRDSIQAGDITYKDVLKVQPFGNIVSYVDMNGQEVLDYLNVVATKPVDSGAYAQFAGISMTVADGKVSNVVIGGKQLRLDATYRFTVPSFNAAGGDGYPKITDHPGYVNTGFVDAEVLKDYLEANSPIDVNRFAPAGEIVYR | Degradation of extracellular 5'-nucleotides for nutritional needs. | Q9KQ30 |
Q5AJU7 | AP1_CANAL | AP-1-like transcription factor CAP1 | Candida | MTDIKRNFSDIASPANLDDTKKLHVDSTATTKVGRKPIDTEPKSKRTAQNRAAQRAYRERKERKMKELEDKVRLLEDANVRALTETDFLRAQVDVLKNELAKYTGGSDFSDLNLPTKVGHLSHPNNHHSNVSTGTPHGSMSSSNSVASLDNDKPSSASSVSNNSPGFAFDNPWSKDNIQKLKHQHQQQQQKVPQGVPDLVSGSSSSSTPLNDNLLVTPESLTGLSTSSKYTGQNNVPTNLDFTNQFDEQVDPFCVKLNEACGTKSNPVPKFKRSGSKANTSVTNNSPLAHLVSPESQQYTNSSNIDFMNDPFFNGVGTDYNFNFDSKNGSIQDPLSFLQDDNFDLALAFGDPSPTGNEAEADPISLLTTEESIYDPLTNNSDKLCSTVKADDVNTDFNFNDFVKNSLPEKQEKGKYEPPSTSKTTNNNEEEDKDEVVPAPPQTLKCSEIWDRITSHPKYTELDIDGLCNELKSKAKCSEKGVVINTADVNQLLERSIKH | Transcription activator involved in multidrug resistance, oxidative stress response, and redox homeostasis. Preferentially binds to promoters with the core binding site 5'-TTA[CG]TAA-3'. Involved in the oxidative stress response in via multiple pathways, including the cellular antioxidant defense system, carbohydrate metabolism and energy metabolism, protein degradation, ATP-dependent RNA helicase, and resistance pathways. The ability of the major systemic fungal pathogen of humans to sense and respond to reactive oxygen species, such as H(2)O(2) generated by the host immune system, is required for survival in the host and therefore virulence. Regulates the transcription of COR33, GLR1, GTO1, GTT1, GTT1, TRR1, TRX1, SOD1, CAT1, and the transcription regulator TSA1. Participates in the apoptosis by regulating the expression of the glutathione reductase gene and glutathione content. Also plays a role in the peroxide-mediated induction of MDR1 and other drug response genes such as PDR16, MDR1, FLU1, YCF1, and FCR1. Regulates trehalose accumulation which is important for the oxidative stress tolerance. Recruits ADA2 to its target promoters. Activity of CAP1 is controlled through oxidation of specific cysteine residues resulting in the alteration of its subcellular location. Oxidative stress induces nuclear accumulation and as a result CAP1 transcriptional activity. Nuclear export is restored when disulfide bonds are reduced by thioredoxin, whose expression is controlled by CAP1, providing a mechanism for negative autoregulation. | Q5AJU7 |
B1LTD9 | DAPA_METRJ | 4-hydroxy-tetrahydrodipicolinate synthase | Methylobacterium | MTEMTGSRLRGSLTALVTPFRDGAFDEAAFRKFVRWQIEQGSHGLVPTGTTGESPTLTHSEHDRVVEACIDEAGGRVPVVAGAGSNSTAEAVERAQHAERAGADAVLVVTPYYNKPTQAGLYAHFKAVNDAVGIPIIIYNIPPRSVIDMSVETMARLFELKNIAGVKDATAKIDRVSQQRQAMGDSFIQLSGEDATALGYNAHGGHGCISVVANVAPRLCADLQEATLAGDYAKALTLQDRLFPLQTGLFAEANPAPVKYALSRLGHMTDELRLPLVPVTEPTKRIVDDALRHAGLLVD | Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA). | B1LTD9 |
A7H185 | RNH_CAMC5 | Ribonuclease H | Campylobacter | MKTVTLFSDGSCLNNPGAGGWAYILEFNGAVKKDSGGAAMTTNNQMELTAVIEGLKALKEPCEVRLFTDSSYVANAVNSWLDGWVKKNFIGSDKKPVKNIELWQEYLRVSRPHKVTASWIKAHNGHPQNEECDTMAREKATKFQNEADI | Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. | A7H185 |
A5DNL9 | SDS23_PICGU | Protein SDS23 | Meyerozyma | MPNPFSRTPQSPSQASRKPSVVELLSSPPPLPSPDHDDVHSFSLSRHTSMSSVATGATGDRSRGSVSAGTTSGGVDWSDIKLSELTEPQKLISINSGYTVQEAFKTLVTHNLTSVPVSLSKTDSSDLENCLSFDYSDLNTYLLLLFGRARLDALSVDEINVEGSMSKLEYAQQMVNKAKHGGEVPVDFILRLHPKNPFIKFPEQETLYPAMEALGNGVHRVAITKDSSPHAPITGILSQRRLIKYMWENARRFPSLDFLINSTIQDLNIGSSNPLTIHGDQPLIDALQKMFTERVSSLAVIDRSRCLMGNISIVDVKHVSSSKNQDLLFKSVLNFISYNLSQKGIEAGQDQYPIFHVSNQSSLGRVIAKLVATQSHRLWVVESRQVKHHASSSGGFGSISGTRSGSISGASSAGPVEAALSPQSSSNNSAAAAAAAAASNPSTGSGSVSGSVSGTNSASGTGAGDSGLPGKLIGVVTLTDILGLFAESKYGKKIDPGLARRQRRRSSTSTRSSIDTTQGEIFRKSYTKQEGVFGKE | Involved in DNA replication and cell separation. | A5DNL9 |
Q46J16 | RIMP_PROMT | Ribosome maturation factor RimP | Prochlorococcus | MSNQTVSELKVLTAKSATNYGFDVTDFKMFTHLNPLSIQVNIRHKNPDKKVTIDDCSILSQYIDEAIQGSSILDQPFNLEISSEGIGDFLTEEKDFQTFKGFPVEVSYQDLKKIEQQINGLLLKRTDNELHINQKGKTQRIPVEDVIQVRLATPSG | Required for maturation of 30S ribosomal subunits. | Q46J16 |
A9EX55 | NUON1_SORC5 | NDH-1 subunit N 1 | Sorangium | MILGPYIAVSPLIVISLGGALLMLAEAFSHRREESHDRRSGPSSDMALGTAITLLAGAVFSGAVGFVGPETLEGFDSLAPYLVMDRFTLFFSFVLCLGGALAALLAGGYLPEHRLDRGEFYPLLTFSTVGAIILAGAGDLLTLFLGLETMSLGAYALTGFRRTSPRSTEAAIKYFLLGSFAAALLLYGGALIYGATGHTDLAGIGEAIAGAKGAAAPNPALLLIGAALVLVGLAFKVSAVPFHMWTPDAYEGAPTPATTFMAVAVKGAAFATLLRVLLGAFGSPALSSWAAGWPPAVAVMALLTMTVANLIAGRQESVKRMLAYSSIAHAGYLLVGVAATVRASEDAQASVMFYLLAYTVSTVGAFGTLILCGSRGAEAVSYEDLSGIGKRHPVAALAFSLFLLSLAGVPPTAGFFGKLYIVKAAMGAELYTLSVALLLNSVLSAYYYLRVLVYMYMREPAPGAPIARPMRSGYVNAALVVSAVLVMVLGIWPTTSLGIAVRAVLASR | 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. | A9EX55 |
P29445 | THIO1_DICDI | Thioredoxin-1 | Dictyostelium | MSNRVIHVSSCEELDKHLRDERVVVDFSAVWCGPCRAISPVFEKLSNEFITFTFLHVDIDKLNVHPIVSKIKSVPTFHFYRNGSKVSEFSGASESILRSTLEANK | Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. | P29445 |
A6W5W1 | IF1_KINRD | Translation initiation factor IF-1 | Kineococcus | MPKKDGVIEIEGTVIEALPNAMFRVELSNGHKVLAHISGKMRQHYIRILPEDRVVVELSPYDLSRGRIVYRYK | One of the essential components for the initiation of protein synthesis. Stabilizes the binding of IF-2 and IF-3 on the 30S subunit to which N-formylmethionyl-tRNA(fMet) subsequently binds. Helps modulate mRNA selection, yielding the 30S pre-initiation complex (PIC). Upon addition of the 50S ribosomal subunit IF-1, IF-2 and IF-3 are released leaving the mature 70S translation initiation complex. | A6W5W1 |
B8F3R8 | EFTS_GLAP5 | Elongation factor Ts | Glaesserella | MAEITAALVKELRERTGAGMMECKKALVEANGDIELAIDNMRKSGQAKAAKKAGRVAAEGVILARIGAGFGVLVEMNCETDFVAKDAGFVGLANEVADYALANKGTSIEALQAQFEEKRAALVAKIGENMNIRRVQYLEGQVIAQYLHGAKIGVLVAGQGAEEELKKVAMHVAASKPDFVNPEDVSAEVVAKEREIQIEIAMNSGKPKEIAEKMVEGRMAKFTGEVSLTGQPFVMDPSQTVGAYLKSVNASVTNFVRLEVGEGIEKVEEDFAAEVAKITGGNA | Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome. | B8F3R8 |
Q74CR0 | GPMA_GEOSL | 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase | Geobacter | MRTLVLIRHGESVWNRENRFTGWTDVGLTDKGAAEALRAGRTLKNEGFAFDEAFTSVLKRAIKTLWIVLEEMDQMWIPEHRHWRLNERHYGALQGLNKAETAERHGMEQVHVWRRSYDIPPPPLAAGDPRNPARDPRYAELDPADIPLTESLKDTVARFLPYWHETIAPRILAGRRLLIAAHGNSLRALVKYLDGIGDDAIAGLNIPTGIPLVYELEDDLHPIRSYYLGDPDEVARATQSVADQVKR | Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate. | Q74CR0 |
B1A4P2 | PLIAB_BOTJR | Phospholipase A2 inhibitor | Bothrops | MRLILLSGLLLLGIFLANGDEVDPDRKLLNSLIDALMHLQREFANLKGSFLIVHKARSFGSGSERMYVTNKEIKNFEALRQICEQADGHIPSPQLENQNKAFANVLERHGKEAYLVVGDSANFTNWAAGEPNKAAGACVKADTHGSWHSASCDDNLLVVCEFYFML | This phospholipase A2 inhibitor binds directly phospholipase A2 in the presence or absence of calcium. | B1A4P2 |
Q6IE14 | TM11L_RAT | Transmembrane protease serine 11B | Rattus | MTVSKLRPVIASRKSFPPWMIILGVLGVLAILGLIIGLLVHFLAVENKIYYYQGSFKVLNIPYDRNYERETSLESNYLSKILEIKMVDAFESSNIYKQYINSQIITLVPENNSVTAHIWLVFKDPWSNKENLRRRIESILHQMLENNSGSLTTDPGSLKLTEITKVDAEKIINNRCGRRPRMSATYDRITGGSTAQKGEWPWQASLRVNGKHHCGASLIGERFLLTAAHCFLRTNNPKNLTVSFGTRVTPAYMQHYVEEVIIHEDYVKGQHHDDVAIIKLTEKVSFRNDVHRVCLPEATQVFPPGEGVVVTGWGSLSYNGKSPLLLQKASIKIIDTNACNSEEAYGGRIMDTMLCAGYMEGYVDACQGDSGGPLVHPNSRDIWYLVGIVSWGHECGRVNKPGVYMRVTSYRDWIASKTGI | Serine protease. | Q6IE14 |
Q9MUM3 | CCSA_MESVI | Cytochrome c biogenesis protein CcsA | Mesostigma | MNLIEIETYLANASFALLLITMLIYGMKAIFTKNNILQLFGTLGILFSNFLVALLLSIRWFDSHHFPLSNMYESLMFLCWCFTFFHLLIEKYIQINFIGFITVPIAMLVNAFATFFLPLDMQHSTPLVPALKSNWLIMHVTIMMASYAALILGSLLSIAFLFLTYNKQIELQGNSIGNINDEMNSYITIDIEFQKNESIELAKLIDNLSYRTIGIGFPLLTIGIISGAVWANDAWGSYWSWDPKETWALITWIIFAIYLHTRITKGWQGRRPAIVAFIGFVIVWVCYLGVNLLGQGLHSYGWFTK | Required during biogenesis of c-type cytochromes (cytochrome c6 and cytochrome f) at the step of heme attachment. | Q9MUM3 |
Q75BV4 | LYS1_ASHGO | Lysine--2-oxoglutarate reductase | Eremothecium | MSAILHLRAETKPMEARAALTPTTVRTLVSHGFKIYVEESAQSVFEAAEYAAAGAEVVATGSWRGAPRERIIVGLKELPEEDTFPLEHTHIQFAHCYKNQSGWREVLGRFQSGGGLLYDLEFLQDDRGRRVAAFGYYAGFAGAALGLRDWAWKQTHTDAEDLPAVAPYENEQALVSEVAAACEEAYKKGARKPRVLVIGALGRCGSGAVELLRQCGLHDKHIIRWDIAETARGGPFPEIAAADIFINCIYLSQPIAPFINMELLDRPDRKLRTIVDVSADTTNPHNPVPVYNVATVFSSPTVVVPTSQGPKLSVISIDHLPSLLPREASEAFASDLLPSLLQLPERDTAPVWLRAKELFQQHCERLSKEARL | Catalyzes the NAD(+)-dependent cleavage of saccharopine to L-lysine and 2-oxoglutarate, the final step in the alpha-aminoadipate (AAA) pathway for lysin biosynthesis. | Q75BV4 |
B5FAF3 | PIMT_ALIFM | Protein-beta-aspartate methyltransferase | Aliivibrio | MLNSRSELLDQFLRQQGIRNEAILAAIRELPRERFIPEALSHQAYQNNALPIGEGQTISQPYIVAKMTELLELTPTSNVLEVGTGSGYQTAVLAKLVEHVNSIERIKSLQWNAKRLLKQLDIYNVSTKHGDGWKGWESKGPFDAIIVTAAAESIPNDLLFQLKDNGHLVIPVGEESQQLLRIIRQGEEFFSEVIEEVRFVPLVAGELA | Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins. | B5FAF3 |
O05306 | LOGH_MYCTU | Protein LONELY GUY homolog | Mycobacterium tuberculosis complex | MSAKIDITGDWTVAVYCAASPTHAELLELAAEVGAAIAGRGWTLVWGGGHVSAMGAVASAARACGGWTVGVIPKMLVYRELADHDADELIVTDTMWERKQIMEDRSDAFIVLPGGVGTLDELFDAWTDGYLGTHDKPIVMVDPWGHFDGLRAWLNGLLDTGYVSPTAMERLVVVDNVKDALRACAPS | Catalyzes the hydrolytic removal of ribose 5'-monophosphate from nitrogen N6-modified adenosines, the final step of bioactive cytokinin synthesis. Is involved in the synthesis of isopentenyladenine (iP) and 2-methylthio-iP (2MeS-iP), the most abundant cytokinins detected in M.tuberculosis lysates and supernatants. Is also able to convert trans-zeatin-riboside monophosphate (tZRMP) to trans-zeatin (tZ) in vitro; however, it may not be involved in the biosynthesis of this minor cytokinin in vivo. Accumulation of Rv1205 sensitizes M.tuberculosis to nitric oxide since cytokinin breakdown products synergize with NO to kill M.tuberculosis. Shows a slow AMP hydrolase activity, but is not able to hydrolyze ATP. Displays no lysine decarboxylase (LDC) activity (L-lysine conversion to cadaverine). | O05306 |
Q976K0 | LYSJ_SULTO | [LysW]-aminoadipate semialdehyde/glutamate semialdehyde transaminase | Sulfurisphaera | MKFIQLYGDRGLTIVKGEGQYVWDISGTKYLDLHTGIGVAFLGHRNRRVIEYLSRQMENIMTLSTSFSTPIRDEMLKELDPLKPDKMDNIILLNSGTEAVEAALKTARKITGRKKIIAFKNSFHGRTAGSLSVTWNKRYREPFEPLMSPVQFLTYNNIDELKNIDEQTAAVIVEPIQGESGVIPANEDFMKALREQTQKVGALLVVDEVQTGFGRTGKVWAYQHYGIIPDLLTAGKAIGGGFPVSALFLPDWIAEKLEEGDHGSTYGGNPMAMAAVTAASKVLKEDNVVEQASIKGEIFKKILREKLSDLKSVREIRGKGLMIGIEIRFPPAIALKVMQDERVLALKAGSTVIRFLAPYMITQSDMEEASNAARKGIIETENKRAIT | Involved in both the arginine and lysine biosynthetic pathways. | Q976K0 |
A0KGL0 | CH10_AERHH | Chaperonin-10 | Aeromonas | MKIRPLHDRVIIKRIEAEAKSAGGIVLTGTAAQKSTRGEVLAVGTGRILDNGDVKALAVKVGDKVIFNEGYGVKTEKLDGQDVLILSETDILAIVEE | 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. | A0KGL0 |
Q0AK63 | RS15_MARMM | 30S ribosomal protein S15 | Maricaulis | MSITQERKSALIAEHARGKTDTGSPEVQVAILTTRIANLTEHFKTHKKDNHSRRGLLKMVSQRRRLLDYVKNKDVARYQAIIEKLGLRR | Forms an intersubunit bridge (bridge B4) with the 23S rRNA of the 50S subunit in the ribosome. | Q0AK63 |
A3PF22 | RL13_PROM0 | 50S ribosomal protein L13 | Prochlorococcus | MNKTITPSLETIERNWFLVDAKDKTLGRLATEIATVLRGKNKPTFTPHLDTGDFVIVVNAEKVEVTGKKASQKLYRRHSGRPGGMKIEKFESLQERIPERIIEQAVKGMLPHNSLGRQQFKKLKVYKGADHPHAAQNPVLLNS | 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. | A3PF22 |
C4Z5N8 | RBFA_LACE2 | Ribosome-binding factor A | Lachnospira | MRKNSVKNTRINGEVLKELSNIIRSEIKDPRINPMTSVVAVEVAPDLKTCKAYISVLGDEKSQKDTITGLKSAEGYIRRQLARTVNLRNTPEIRFILDQSIEYGINMSKLIDEVTEHDNKMHVEVEDETE | One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Associates with free 30S ribosomal subunits (but not with 30S subunits that are part of 70S ribosomes or polysomes). Required for efficient processing of 16S rRNA. May interact with the 5'-terminal helix region of 16S rRNA. | C4Z5N8 |
C0M6G7 | SYY_STRE4 | Tyrosyl-tRNA synthetase | Streptococcus | MNIFEELKARGLVFQTTDEEALVKALTEGQVSYYTGYDPTADSLHLGHLVAILTSRRLQLAGHKPYALVGGATGLIGDPSFKDAERILQTKETVLDWSQKIKEQLSCFLDFDNGENKAELVNNYDWFSQISFIDFLRDVGKHFTINYMMSKDSVKKRIETGISYTEFAYQVMQGYDFYELNAKHNVTLQIGGSDQWGNMTAGTELLRKKADKTGHVMTVPLITDATGKKFGKSEGNAIWLDAKKTSPYEMYQFWLNVMDDDAVRFLKIFTFLSLDEIAAIEEQFNAARHERLAQKTLAREVVTLVHGEAAYQQALNITEQLFAGAIKNLSAAELKQGLSNVPNYQVQAEDSLNIVDMLVTAGISPSKRQAREDLQNGAIYLNGERLQDLDYSLSTADRIDNQLTVIRRGKKKYAVLTY | Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr). | C0M6G7 |
Q21XH1 | MDH1_ALBFT | Malate dehydrogenase 1 | Rhodoferax | MSKKPVRVAVTGAAGQIGYAILFRIASGEMLGKDQPVILQLLEVPVEKAQQALQGVMMELQDCAFPLLAGMEAHSDPMTAFKDVDYALLIGSRPRGPGMERAELLAVNGAIFTAQGKALNAVASRNVKVLVVGNPANTNAYIAMKSAPDLPAKNFTAMLRLDHNRALSQLASKTGKAVADIEKMAVWGNHSPTMYADYRFATINGESVKDMINDQDWNANTFLPTVGKRGAAIIAARGVSSAASAANAAIDHMRDWALGTNGKWVTMGIPSDGQYGIPKETMFGFPVTCEGGEYKVVQNLPIDAFSQECINKTLKELQDEQAGVAHLL | Catalyzes the reversible oxidation of malate to oxaloacetate. | Q21XH1 |
Q0S4S5 | UREG_RHOJR | Urease accessory protein UreG | Rhodococcus | MPPHFIDGEPHDHQHDRPRRVRVAGEPVRIGIGGPVGSGKTALVAALCRQLREELSLAVLTNDIYTTEDADFLRRHAVLPDERIAAVQTGGCPHTAIRDDITANLDAIDDLIAANPPLDLILVESGGDNLTATFSSGLIDVQIFVVDVAGGDKVPRKGGPGVTFSDLLVINKTDLAPMVGADLGVMRRDAERVREGRPTALISLTEDPSSGPALEWVREQVRTLADVHQ | Facilitates the functional incorporation of the urease nickel metallocenter. This process requires GTP hydrolysis, probably effectuated by UreG. | Q0S4S5 |
A5W7K1 | MINE_PSEP1 | Cell division topological specificity factor | Pseudomonas | MNLFDFFRGRQKQTSASVAKERLQIIVAHERGQRSEPDYLPALQKELLEVIRKYVNIGNDDVHIELENQGSCSILELNITLPDR | Prevents the cell division inhibition by proteins MinC and MinD at internal division sites while permitting inhibition at polar sites. This ensures cell division at the proper site by restricting the formation of a division septum at the midpoint of the long axis of the cell. | A5W7K1 |
P47718 | CDD_MYCPI | Cytidine aminohydrolase | Mycoplasma | MKEKDIYFQKLNELISNAYVPYSNFRVSCLLLTDGGWFAGVNIENSAYSPTICAERSAVSSMITSGFKQIFKVYILTDTIVKDIGTPCGVCRQVLSEFAKPETPIITYNLKGEKFFYTLEQLLPFAFNKDALK | This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis. | P47718 |
A5GIT4 | RL24_SYNPW | 50S ribosomal protein L24 | unclassified Synechococcus | MATATSQSAPTQRIKMRLRKGDTVQVIAGKDKGKTGEVLRTLPNENRVIVEGVNMRTRHVKPTQEGESGRIVTEEASLHASNVMLYSTAKKVASRVELITEKDGSKKRRLKKTGEVID | One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit. | A5GIT4 |
B0KS83 | DAPE_PSEPG | N-succinyl-LL-2,6-diaminoheptanedioate amidohydrolase | Pseudomonas | MTAPAELSPTLQLACDLIRRPSVTPVDADCQAQMMNRLGAVGFELEPMRIEDVDNFWATHGSQDGPVLCFAGHTDVVPTGPVQQWQHEPFEALIDADGMLCGRGAADMKGSLASMVIASERFVQDYPNHRGKVAFLITSDEEGPAHHGTKAVVERLKARNERLDWCIVGEPSSTTLLGDVVKNGRRGSLGAKLTVRGKQGHVAYPHLARNPIHLAAPALAELAAEHWDEGNAFFPPTSFQISNLNSGTGATNVVPGELTALFNFRFSTESTVEGLQARVSAILDKHELDWSIDWALSGLPFLTEPGELLDAVASSIKGVTGRDTQPSTSGGTSDGRFIATMGTQVVELGPVNATIHQVDERILASDLDLLTEIYYQTLVRLLA | Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls. | B0KS83 |
O26157 | SYE_METTH | Glutamyl-tRNA synthetase | Methanothermobacter | MVPVEDLVYRYALLNAVKHRGRANPGAVMGAVMSNEPELRKMAPQVKEAVEAAVERVNSLSPEEQQQEMERLGLEITERKQKKRKGLRELAGVKGEVVLRFAPNPSGPLHIGHARAAILNHEYARKYDGRLILRIEDTDPRRVDPEAYDMIPADLEWLGVEWDETVIQSDRMETYYEYTEKLIERGGAYVCTCRPEEFRELKNRGEACHCRSLGFRENLQRWREMFEMKEGSAVVRVKTDLNHPNPAIRDWVSMRIVEAEHPRTGTRYRVYPMMNFSVAVDDHLLGVTHVLRGKDHLANREKQEYLYRHLGWEPPEFIHYGRLKMDDVALSTSGAREGILRGEYSGWDDPRLGTLRAIARRGIRPEAIRKLMVEIGVKIADSTMSWKKIYGLNRSILEEEARRYFFAADPVKLEVVGLPGPVRVERPLHPDHPEIGNRVLELRGEVYLPGDDLGEGPLRLIDAVNVIYSGGELRYHSEGIEEARELGASMIHWVPAESALEAEVIMPDASRVRGVIEADASELEVDDVVQLERFGFARLDSAGPGMVFYYAHK | 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). | O26157 |
Q3M7F0 | MINE_TRIV2 | Cell division topological specificity factor | Trichormus | MILELLDKLFLRTPDTSRSHVKRRLQLVIAHDRAGLDPETLEKMRKEILDIVCRYVEVESDGLEFALESNQRTTALIANLPIRRVKPELPAFDETSQ | Prevents the cell division inhibition by proteins MinC and MinD at internal division sites while permitting inhibition at polar sites. This ensures cell division at the proper site by restricting the formation of a division septum at the midpoint of the long axis of the cell. | Q3M7F0 |
Q652K1 | SGR_ORYSJ | Protein STAYGREEN | Oryza sativa | MAAATSTMSLLPPITQQQRWHAADSLVVLASRCHNSRRRRRCRYVVPRARLFGPAIFEASKLKVLFLGVDEEKHQHPGKLPRTYTLTHSDVTARLTLAVSHTINRAQLQGWYNKLQRDEVVAEWKKVQGHMSLHVHCHISGGHVLLDLIAGLRYYIFRKELPVVLKAFVHGDGNLFSRHPELEEATVWVYFHSNLPRFNRVECWGPLRDAGAPPEEDDAVAAAAAEEAAAEQMPAAGEWPRRCPGQCDCCFPPYSLIPWPHQHDVAAADGQPQQ | Involved in the disassembling mechanism of the intact light-harvesting complex of photosystem II (LHCII) in the thylakoid membranes. Required to trigger chlorophyll degradation during natural and dark-induced leaf senescence. | Q652K1 |
B1YD10 | ARGDC_PYRNV | Arginine decarboxylase alpha chain | Pyrobaculum | MQTTTQVKTPVVGKHVYGELYGVDEELLRDQEKLRKIVIEAAHIAKMHLVEVNSWKFKGGDKEGVSVIALVLESHIAIHTWPTYNYATVDVYTCGEHSDPMAAFRYIVSQLAPKRFTVNYSDRSYR | Specifically catalyzes the decarboxylation of L-arginine to agmatine. Has no S-adenosylmethionine decarboxylase (AdoMetDC) activity. | B1YD10 |
Q9B1U9 | MATK_LILLO | Intron maturase | Lilium | MEELQGYLKKDRSPQQHFLYPLLLQEYIYTLAHDDSLNGSIFYEPIEFIGYDNKFSLVLVKRLIIRMYQQNFLIYLVNDSNQNRFGGHTNSFYSHFFYSQMVSKGFSVIVEIPFSLRLVSSSEEKEIPKSQNLGSIHSIFPFLEDKLSHLNNVSDILIPHPIHFEILVQILQCWIQDVPSLHLLRFFLHKYQNLNKTIQSNKTIYVFSKENKRLFWFLYNSYVSECEFLLVFFHKQSCYLRSTSSGTFLERSHFYGKMEHIIIVCCNNFHKTLWPIKDPLIHYVRYQGKAILASRGTHLLMKKWRYYFVNFWQYYFHFWSQPYRMHINSLLNYSFYFMGYLLRVLINPYAVKNQMLENSFLIDTVIKKFDTIIPIIPLIGSLSKAKFCTFSGHPISKPIWADLSDFDIIDRFGRICRNLSHYYSGSSKKQSLYRIKYILRLSCARTLARKHKSTARALLQRLGLGFLEEFFTEEEQVLSFIFPKTTLFTLHGSHRERIWSLDIIRINDLVNN | Usually encoded in the trnK tRNA gene intron. Probably assists in splicing its own and other chloroplast group II introns. | Q9B1U9 |
Q97W02 | DPO4_SACS2 | DNA polymerase IV | Saccharolobus | MIVLFVDFDYFYAQVEEVLNPSLKGKPVVVCVFSGRFEDSGAVATANYEARKFGVKAGIPIVEAKKILPNAVYLPMRKEVYQQVSSRIMNLLREYSEKIEIASIDEAYLDISDKVRDYREAYNLGLEIKNKILEKEKITVTVGISKNKVFAKIAADMAKPNGIKVIDDEEVKRLIRELDIADVPGIGNITAEKLKKLGINKLVDTLSIEFDKLKGMIGEAKAKYLISLARDEYNEPIRTRVRKSIGRIVTMKRNSRNLEEIKPYLFRAIEESYYKLDKRIPKAIHVVAVTEDLDIVSRGRTFPHGISKETAYSESVKLLQKILEEDERKIRRIGVRFSKFIEAIGLDKFFDT | 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. It is involved in translesional synthesis. | Q97W02 |
A2R9P4 | GMT_ASPNC | GDP-mannose transporter | Aspergillus subgen. Circumdati | MAEGKKTDDYTIQMDSIDQGNKSFEAPPPPQPRSPPSGSLSNNPILPVLAYCGSSILMTVMNKYVLSGTDFNLNFFLLCIQSLVCIIAIQTCKSCGLITYRDFSADEARKWFPITLLLIGMIYTGSKALQFLSIPVYTIFKNLTIILIAYGEVLWFGGSVTGLTLFSFGLMVLSSIIAAWADIKHAVESNGDATAKVSTLNAGYIWMLVNCLCTSSYVLGMRKRIKLTNFKDFDTMFYNNLLSIPVLIVLSAFLEDWSSTNVNRNFPPMDRNSIVFAMILSGLSSVFISYTSAWCVRVTSSTTYSMVGALNKLPIAISGLIFFDAPVTFPSVSAIVVGFVSGIVYAVAKIKQNAKPRTGVLPTANPPVSASSQSMRDSLRS | Involved in the import of GDP-mannose from the cytoplasm into the Golgi lumen. | A2R9P4 |