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 |
|---|---|---|---|---|---|---|
Q8H6Q1 | DEF1_PETHY | PhD1 | Petunia | MARSICFFAVAILALMLFAAYDAEAATCKAECPTWDSVCINKKPCVACCKKAKFSDGHCSKILRRCLCTKECVFEKTEATQTETFTKDVNTLAEALLEADMMV | Plant defense peptide with antifungal activity against F.oxysporum and B.cinerea. | Q8H6Q1 |
Q2YWA3 | COPA_STAAB | Cu(+)-exporting ATPase | null | MANTKKTTLDITGMTCAACSNRIEKKLNKLDDVNAQVNLTTEKATVEYNPDQHDVQEFINTIQHLGYGVAVETVELDITGMTCAACSSRIEKVLNKMDGVQNATVNLTTEQAKVDYYPEETDADKLVTRIQKLGYDASIKDNNKDQTSRKAEALQHKLIKLIISAVLSLPLLMLMFVHLFNMHIPALFTNPWFQFILATPVQFIIGWQFYVGAYKNLRNGGANMDVLVAVGTSAAYFYSIYEMIRWLNGSTTQPHLYFETSAVLITLILFGKYLEARAKSQTTNALGELLSLQAKEARILKDGNELMIPLNEVHVGDTLIVKPGEKIPVDGKIIKGMTAIDESMLTGESIPVEKNVDDTVIGSTMNKNGTITMTATKVGGDTALANIIKVVEEAQSSKAPIQRLADIISGYFVPIVVGIALLTFIVWITLVTPGTFEPALVASISVLVIACPCALGLATPTSIMVGTGRAAENGILFKGGEFVERTHQIDTIVLDKTGTITNGRPVVTDYHGDDQTLQLLATAEKDSEHPLAEAIVNYAKEKQLTLTETTTFKAVPGHGIEATIDHHHILVGNRKLMADNDISLPKHISDDLTHYERDGKTAMLIAVNYSLTGIIAVADTLKNHAKDAIKQLHDMGIEVAMLTGDNKNTAQAIAKQVGIDTVIADILPEEKAAQIAKLQQQGKKVAMVGDGVNDAPALVKADIGIAIGTGTEVAIEAAGITILGGDLMLIPKAIYASKATIRNIRQNLFWAFGYNIAGIPIAALGLLAPWVAGAAMALSSVSVVTNALRLKKMRLEPRRKDA | Involved in copper export. | Q2YWA3 |
O80920 | PYL4_ARATH | Regulatory components of ABA receptor 10 | Arabidopsis | MLAVHRPSSAVSDGDSVQIPMMIASFQKRFPSLSRDSTAARFHTHEVGPNQCCSAVIQEISAPISTVWSVVRRFDNPQAYKHFLKSCSVIGGDGDNVGSLRQVHVVSGLPAASSTERLDILDDERHVISFSVVGGDHRLSNYRSVTTLHPSPISGTVVVESYVVDVPPGNTKEETCDFVDVIVRCNLQSLAKIAENTAAESKKKMSL | Receptor for abscisic acid (ABA) required for ABA-mediated responses such as stomatal closure and germination inhibition. Inhibits the activity of group-A protein phosphatases type 2C (PP2Cs) when activated by ABA . Can be activated by both (-)-ABA and (+)-ABA . | O80920 |
Q046I4 | XPT_LACGA | Xanthine phosphoribosyltransferase | Lactobacillus | MKLLEERIRKDGEVLDGDVLKINSFLNHQVDPELMMQVGEEFKRLFENEKITKVLTCEASGIAPGIMAAYQLGVPMVFARKKKPSTLNDAVYWADVFSYTKKVNNKICVEKKFLSSDDHLLIIDDFLAHGEAVKGMLNIAKQANAAVAGVGVVVAKEFQGGSDWVKEHGYRLEALARISNFENNQVHFVGEK | Converts the preformed base xanthine, a product of nucleic acid breakdown, to xanthosine 5'-monophosphate (XMP), so it can be reused for RNA or DNA synthesis. | Q046I4 |
P13106 | FER_BUMFI | Ferredoxin | Bumilleriopsis | ETYSVTLVNEEKNINAVIKCPDDQFILDAAEEQGIELPYSCRAGACSTCAGKVLSGTIDQSEQSFLDDDQMGAGFLLTCVAYPTSDCKVQTHAEDDLY | Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. | P13106 |
Q1XDN5 | RPOB_NEOYE | Plastid-encoded RNA polymerase subunit beta | Neopyropia | MVQRISLKNKLLPDLVEIQRASFKWFLLEGLTEVLEIFPKISDPTSRLELQLFGNEYKIKFPRYSVRQAKNRDKTYSAQIYVPAKLTRKDIDLPSKNQEKNIKSLDLSSTHLQLSAEKQIKNKKYKKRLVFIGDLPIMTNRGTFIVSGTERVIINQIIRSPGIYYKQEIDKNGKQIYSASLISNRGSWLKFEIDPKGEIWIRIDKTHKVNAYIFLRAIGLNKDEIEKGLSKYAFLISASQIYSVKELAKEIGKNNIEEVTDEEALLIVYSKLRPNEPATVAVAKQMLYSRFFDPKRYDLGEVGRYKINKKLGLNIPKTFRVLSPQDILSSIDYLINIKDKNSGNLDDIDHLGNRRVRSVGELLQNQFRVGLNRLERIIRERMMICDIDSLSLSNLINPKPLIASVREFFGSSQLSQFMDQTNPVAELTHKRRISALGPGGFNKDRAGFAVRDLHPSHYGRICPIETPEGPNAGLIGSLATCARVNVFGFIETPFYPVNQGQVIYHNSPVYLTADEEDDFRVAPGDVKVSKQHYIEGDIIPVRYRQEFITTTPTQVDYIAISPIQVISAATSLIPFLEHDDANRALMGSNMQRQAVPLLYPEKPIIGTGLETKIARDSGMVVISRTSGHVNYVSANKIGIQDNSGRTVHYRLKKYYRSNQDTCINQRPIVWVGEKIVVGQTLADGASTDGGEIALGRNILVAYMPWEGYNYEDAFLISERLVYDDLYTSIHIEKYEVECRQTKLGPEEITREIPNVSDNSLKDLDRNGIVVGGSWVEAGDILVGKITPKGEADQLPEGKLLRAIFGEKARDVRDTSLRLPNAAKGRVVKVRVFTRQKGDELPPGTNAMIRVYVAQKRKIQVGDKMAGRHGNKGIISRILPKQDMPYLSDGTPVDIVLNPLGVPSRMNVGQVFECLLGLAGGYLGKRFKIIPFDEMYGAEASRALVNRKLKEASLITSNKWLFNDQHPGKMQVFDGRTGEPFDNPVTVGRAYMLKLVHLVDDKIHARSTGPYSLVTQQPLGGRAQHGGQRLGEMEVWALEAFGAAYTLQELLTVKSDDMQARNEALNAIVKGKPIPKPGTPESFKVLMRELQSLGLDIAVHKLKLFEDGQRRTVEVDLMSDSKDNRVDRSNYDTPPVDDFEQFLY | DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | Q1XDN5 |
O76616 | PID3_CAEEL | piRNA-induced silencing defective protein 3 | Caenorhabditis | MVAHQKADFKSKWAMVVTVNNLNDKKRADLREFSEWFIETLRLEGAFIGHYFNYEAAPVTIVETLPGNFDSCTNAYQKIHKEHPQVVLVVHILPQSQSNEYEWMKVLASRYGFVRQGLLYDNCANRFQNVETDQNSVFRNMCQWIYRSGTAIVRNEGNACGILHGKDPKPTFDKVLFNSEDIKDSVFKVLHAEEEPRGADQENMLKISGYPGMLNTFGIAQLLTPYRVNGITITGAQSAVVALENKFQVYQAVQDFNGKKLDRNHKLQVSSLVVSSPAVPLEWPSLKKSKKLVEQVGKPIRLSKVSS | Component of the pid-1 and tost-1 variants of the PETISCO complexes, which have roles in the biogenesis of a class of 21 nucleotide PIWI-interacting RNAs (piRNAs) that possess a uracil residue at the 5'-end (also called 21U-RNAs) and embryogenesis, respectively . Within the pid-1 variant of the PETISCO complex may stabilize 21U-RNA precursor molecules . Promotes the biogenesis of 21U-RNAs . Required for chromosome segregation and cell division in early embryos . | O76616 |
B8GUJ5 | RUVA_THISH | Holliday junction ATP-dependent DNA helicase RuvA | Thioalkalivibrio | MIGRLRGELVSKQPPFLLLDVQGVGYEIEAPLSTFYDLPEPGGQVTLHTHLHVREDAHVLYGFASESERALFRSLIKVTGVGAKMALAILSGMTASEFSRCVMDGDVASLVRLPGIGRKTAERLVVEMRDRLGSLPAAVTLTGGKPAAAAARAPDPVSDAVSALVSLGYKPQEASRLISAVEGEAERSEDLIRLALKATLK | 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. | B8GUJ5 |
P0ADR2 | YGDD_ECOLI | UPF0382 inner membrane protein YgdD | Escherichia | MTSRFMLIFAAISGFIFVALGAFGAHVLSKTMGAVEMGWIQTGLEYQAFHTLAILGLAVAMQRRISIWFYWSSVFLALGTVLFSGSLYCLALSHLRLWAFVTPVGGVSFLAGWALMLVGAIRLKRKGVSHE | May be a peptide transporter or a protein that facilitates peptide internalization . | P0ADR2 |
B1L108 | LGT_CLOBM | Phosphatidylglycerol--prolipoprotein diacylglyceryl transferase | Clostridium | MNPIAFHVGNLAIRWYGVIISIGAALGLLLAMYNCKIREASYDEFINMFLIAFPSAIIGARLYYVIFEFEDYRDNLINIFNTRQGGLAIHGGIIFGVLAVYIYLKYRKENFFEYVDVAAPSIILGQAIGRWGNFFNSEAHGGPVTKEFISKFPQFIQKGMFIEGTYYHPTFLYESIWNFIVCIFLVYLLKKTKKKGIVFMAYIGLYSLGRFFIEGLRTDSLYLGSIRVAQLISVLGIILSIFFIYNIIKKEKRY | 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. | B1L108 |
Q8TS71 | MTBC2_METAC | Dimethylamine corrinoid protein 2 | Methanosarcina | MASKEELLQELSDAIVSCKKDRVIAAVEKAKEVMEPAEIIEKGLAAGMNQVGTLFERGKLFLPHVMMAADSMTAGVNILEAEMPAGTETKKLGVIVNGTVEGDVHDIGKSIVSTMLQSAGFEVHDIGRDVPIKNFVEKAKEVNADMIGLSALMTTTMQGQRDVIELLKEEGMRERVKVMVGGAPATQAWADKIGADCYAENASEAVAKAKELLLGK | Acts as a methyl group carrier between MtbB and MtbA. | Q8TS71 |
B3EFY2 | RL13_CHLL2 | 50S ribosomal protein L13 | Chlorobium | MSKTLSFKTYSAKPAEVERKWYVIDAEDQILGRMAAEIAKVLRGKHKPQFTPHIDTGDFIVVTNAEKVALSGKKIEYKTYFHHSNYPGGGKFDHVKDLLKKKPEKVIEHAVWGMLPHNNLGRQLFKKLKVYAGSEHPHTAQCPVELKVN | 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. | B3EFY2 |
A0A411PQN4 | AGN8_PAEDI | Agnestins biosynthesis cluster protein L8 | Paecilomyces | MAKDPTFEEVTGCQRALFEWADSYDTKDWERLKKCVAPTLRIDYRSFLDKLWEAMPSDEFILMASDPRFLGNPLLKTQHFVGLSTWQKISPDEIEGTHQLRVPHQRYTDSNMKEVAVKGHAHGIATMWYKRVEDEWKFAGVCPQIRWAEFDYDKVFAEGKDHFGENGGNGEHAV | Dehydratase; part of the gene cluster that mediates the biosynthesis of agnestins, dihydroxy-xanthone metabolites . The pathway begins with the assembly and cyclization of atrochrysone thioester by the non-reducing polyketide synthase Agnpks1 . The atrochrysone carboxyl ACP thioesterase AgnL7 then breaks the thioester bond and releases the atrochrysone carboxylic acid as the first enzyme-free intermediate . The decarboxylase AgnL1 then catalyzes the concerted decarboxylation-elimination required to convert atochrysone carboxylic acid into emodin anthrone, which is further oxidized to emodin by the anthrone oxygenase AgnL2 . Emodin then undergoes reduction catalyzed by the oxidoreductase AgnL4 to yield the dihydroquinone tautomer which is the substrate for reduction by the short chain dehydrogenase AgnL6 reduction to produce hydroxyketone, followed by AgnL8 dehydration and likely spontaneous autoxidation to chrysophanol . Baeyer-Villiger oxidation by the oxidase AgnL3 leads to monodictyphenone via cleavage of the C-10/C-10a bond of chrysophanol . Alternative cleavage at the C-4a/C-10 bond of chrysophanol leads also to the formation some cephalone F . Further conversion to agnestins A and B, requires reduction to dihydro-monodictyphenone, oxidation to agnestin C probably via an epoxide, and rearrangement to either agnestin A or agnestin B directly, although agnestin A or agnestin B can also interconvert . Within the cluster, AgnR1 is the only unassigned oxidoreductase present which could be involved in this conversion. However, AgnR1 seems not to be involved in this step, and thus genes involved in the proposed oxidation/reduction may be located elsewhere on the genome . Further agnestin A derivatives are probably formed by spontaneous decarboxylations, dehydrations and methanolysis reactions . | A0A411PQN4 |
A5F0H9 | ECTC_VIBC3 | N-acetyldiaminobutyrate dehydratase | Vibrio | MIVRTLEECRQSERRVVAENWESVRMLLKDDHMGFSFHITTIYANTQTHIHYRNHLESVYCMSGEGEIEVVGGKTYPIQPGTLYILDQHDEHYLRAFSSEMVMACVFNPPLTGHEIHDAEGVYPLDKSELISQCHKEK | Catalyzes the circularization of gamma-N-acetyl-alpha,gamma-diaminobutyric acid (ADABA) to ectoine (1,4,5,6-tetrahydro-2-methyl-4-pyrimidine carboxylic acid), which is an excellent osmoprotectant. | A5F0H9 |
B5YDV7 | RS8_DICT6 | 30S ribosomal protein S8 | Dictyoglomus | MTVTDPIADMLVRIKNASMRRHPTVDVPYSKMKEKILEILLREGYIARYEVIGEIPQKYIRVYLKYKGKTPVIQDVKRVSKPGRRYYVNKEEIPRVLGGLGIAILSTSKGIMTDKEARLLGVGGELICMVW | 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. | B5YDV7 |
Q18H64 | FLPA_HALWD | Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase | Haloquadratum | MKASSSLPDGVQRRQFDNRSRLTTHGTTVYGEPRDTDGWRLWDAGRSKLGAMFKLDIETGLTGGESILYLGAASGTTVSHVADFAGPTYAIEFAPRPVRDLLEVATTRPNLIPLLCDARQPETYAHVVETDIEYLIQDVATRGQATVALRNRQFLAPDGKLILMIKARSEDVLSDPEDVFDTIISTLREGYIIQTRQRLDRFHDDHLAVVATPNM | Involved in pre-rRNA and tRNA processing. Utilizes the methyl donor S-adenosyl-L-methionine to catalyze the site-specific 2'-hydroxyl methylation of ribose moieties in rRNA and tRNA. Site specificity is provided by a guide RNA that base pairs with the substrate. Methylation occurs at a characteristic distance from the sequence involved in base pairing with the guide RNA. | Q18H64 |
B2V847 | DXR_SULSY | 2-C-methyl-D-erythritol 4-phosphate synthase | unclassified Sulfurihydrogenibium | MLKVGILGSTGSVGSQALDVIRKYKDQIKVELLGASKLSENLINQIKEFKPSYVYVENAEEKSIDDIKVLVGEDGLRRAVNLDLDLFINAIAGIKGILPTYLLLKYNKTLATANKEAIICLGELLKDKYKKILPIDSEHSAIFQILKDSNQKEVRRIILTASGGPFVNMPAEDFENITVKQALIHPRWSMGKKITIDSATLMNKGLEVIEAHYLFSMPYEKIDVLIHPESIIHGMVEFVDGTVISNMSNPDMKIPISYALFYPERKFLSDNYLDFTKIKSLNFLKPDTEKFPLLKLAVECGKKGGVYPTVLTVADEIAVNYFLEERIKFTDIHKIILETLEKFDYNKLDSVDDIFYIIDKTINLATEIAKKYGST | Catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP). | B2V847 |
O80963 | ACCR2_ARATH | Protein CRINKLY 4 RELATED 2 | Arabidopsis | MQPNSHIFVIITISSLIITVSAYGSTGTIAAAFGENGFFCAIDASGKQEVICWDRGNTNRSLNRPPGEISGYSPPMTSLSGGEGFLCAITSNTSRAFCWNLEDPSENLVPRAFQYNSYLQIASGNNHVCAISGLYYSGPDYGPVHCWEYSDNTNFTSGLLWNSSFHNPYIDSLMFRKIVSGDGFSCGVTKDGDLVCWGPKSNLLNFSNNEEFEVLASGRNSVCGVSKDSGQLHCFGDETEFGSLPNRPRFIALSAGANHYCGIREDDHGVECWGRNLNSSSSSSAPNTSGFVAISSSDSTTCGVRELDLVLDCWRVHDSSKADYSPPLELCSPGMCSPRGNCGDGWFAFNASILKESELTSLCSFHNLNICLRCGISCLEGYFPSSTCNPNADRVCTPCSLCQNSSCYGICKIRATKSKEHEQKEQREVRRLVIIIGCSVLGFLVMLIGLSFIPKMTKGSKRDDEERSKMTCCFCFDKNSVEADPDPVPHQSVLLPTAVSLGETKIFRLSELKDATHGFKEFNELGRGSFGFVYKAVLSDGIHVAVKRANAATIIHSNNRGFESELEILCKIRHNNIVNLLGYCSEMGERLLVYEYMPHGTLHDHLHGDLSQLDWSMRLKIMLQAARGLDYLHNEVDPPIIHRDVKTSNILLDGEMCARIADFGLVSSNERDSSNSDREGDVYDFGIVLLEILSGRKAIDRESDPAGIAEWAVPLIRKGKAAAIIDRNICLPRNVEPLLKLAELAELAVRENSNERPNIRNILCFLDLIVKSGLTF | Serine/threonine-protein kinase with low activity. | O80963 |
B3QQD1 | APT_CHLP8 | Adenine phosphoribosyltransferase | Chlorobaculum | MPIKSRIRTVPDYPKKGIMFRDITTLIKDPVGFRLVIDNMTQHYLSNGIDFDVIVGIEARGFIIGGALSYTLGKGFVPVRKPGKLPADVVQLEYDLEYGSDKIEMHTDSLVKGQRVLLVDDLLATGGTALAAAALVEKLGGVVASMGFIVNLPDVGGEKKIRDKGYNIFSLTEFEGD | Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. | B3QQD1 |
A9IHE2 | SYDND_BORPD | Non-discriminating aspartyl-tRNA synthetase | Bordetella | MRTCYTGEVCRDHLGQTVTLYGWVNRRRDHGGVIFIDLRDRAGLAQIVFDPDNAAFATAERLRNEFCIRVTGLVRPRPEGTANPELASGEVEVLCKEVEILNASITPPFQLDDDNLSETTRLTHRVLDLRRPQMQRNLMLRYRVSIEVRKFLDQLGFIDIETPMLTKSTPEGARDYLVPSRVNAGHFFALPQSPQLFKQMLMVSGFDRYYQITKCFRDEDLRADRQPEFTQIDCETSFLNEVEIRQIFEDMIRHVFKTVQNVELPAPFPQMTWTEAMQRYGSDKPDLRVSLEFTDVTDVMRDVDFKVFAAAATAPGSRVVALRVPGGAELSRSEIDAYTQFVGIYGAKGLAYIKVNDASKGREGLQSPIVKNLHDAALAELLKRSGAQSGDIIFFGADRAKIVNDAIGALRVKIGHSEFGKKAGLASSDWKPLWVVDFPMFEYDEEDGRYTAAHHPFTSPKDGHEDFLESDPSKAFAKAYDMVLNGWEIGGGSVRIHREEVQSKVFRALKIGAEEAREKFGFLLDALQYGAPPHGGIAFGLDRIVTMMTGAESIRDVIAFPKTQRAQCLLTQAPSEVDEKQLRELHIRLRNVEVK | 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). | A9IHE2 |
Q4K6J1 | MURD_PSEF5 | UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase | Pseudomonas | MSLIASDHFRIVVGLGKSGMSLVRFLASRGVAFAVADTRENPPELATLRRDYPQVEVRCGELDVDFLCRADELYVSPGLALATPALQAAAARGVKLSGDIELFARNAKAPIVAISGSNAKSTVTTLVGEMAAAAGKRVAVGGNLGTPALDLLSDDVELYVMELSSFQLETTDQLGAEVATVLNISEDHMDRYSGLPAYHLAKHRIFRGARQVVFNRQDALTRPLIGEGLPCWTFGLSKPDFKAFGLREEDGEKYLAFEFQNLMPVRELKIRGAHNQSNALAALALGHAVGLPFDAMLAALRTFAGLEHRCQWVRDLDGVAYYNDSKATNVGAALAAIEGLGADIEGKIVLIAGGDGKGADFKDLRGPVAANCRAVILMGRDSDQIGEAIGDAVPLIRVGSLQEAVEQCRATAQPGDVVLLSPACASFDMFKNYEDRGHQFVRIVEELA | Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). | Q4K6J1 |
P9WMD2 | CHLER_MYCTO | HTH-type transcriptional repressor MT1396 | Mycobacterium tuberculosis complex | MQTTPGKRQRRQRGSINPEDIISGAFELAQQVSIDNLSMPLLGKHLGVGVTSIYWYFRKKDDLLNAMTDRALSKYVFATPYIEAGDWRETLRNHARSMRKTFADNPVLCDLILIRAALSPKTARLGAQEMEKAIANLVTAGLSLEDAFDIYSAVSVHVRGSVVLDRLSRKSQSAGSGPSAIEHPVAIDPATTPLLAHATGRGHRIGAPDETNFEYGLECILDHAGRLIEQSSKAAGEVAVRRPTATADAPTPGARAKAVAR | Negatively regulates the expression of the efflux pump MT0201 upon chloramphenicol exposure. Acts by binding to the MT0201 promoter region. | P9WMD2 |
A5CRA6 | HRCA_CLAM3 | Heat-inducible transcription repressor HrcA | Clavibacter | MVSERGLDVLRVIVQDYVSSREPVGSKSIVERHAFGVSAATIRNDMALLEEEELIAAPHTSSGRVPTDKGYRLFVDQLADVRPLTPAQRQAIHVFLGESVDLDDVLARTVRLLAQLTNQVALVQYPSLATSHVKHVELVALSTTRVLTVLITDTGRVEQRVVELAGDPDDAFLAVMRTRINQAVGGLGLAEAATRLETLSDEVEPAQRAAASVLAGTLVEQVLANRQERLLLAGSANLARTERDFPGSISPVLEAIEEQVVLLRLLGEMEADQHGVSVSIGRENAPFGLGETSVLTSGYSSSGGVLARLGVLGPTRMDYSTNMASVRAVARYLSRLLEER | Negative regulator of class I heat shock genes (grpE-dnaK-dnaJ and groELS operons). Prevents heat-shock induction of these operons. | A5CRA6 |
D3E3N9 | EF2_METRM | Elongation factor 2 | Methanobrevibacter | MSRRDKMIAKIKELMYKPEYIRNIGICAHIDHGKTTLSDNLLAGAGLISEDLAGEALGMDTKKDEQERGITIDAANASMVQEYEGEQYLINLIDTPGHVDFGGDVTRAMRAVDGAVVVVCAVDGVMPQTETVLKQALRENVKPVLFINKVDRLINELKLGPEELLKQLTSIIVEVNALIKSLAPKDKKNEWMVNVEEGSVAFGSAFKNWAINIPKMQETKFTFKDIIDYCNEGKEDELKQLLPLTEVLLNMVVKHLPSPNVAQVYRVPKIWDGDIESEVGQTMIKMSPDGPLAGMITNVAVDKHAGIVATCRIYGGTLEKSSEIYLVGSHGKARVQQAGIFMGAETIDTGKVPVGNIAYLTGVKGASAGETICSADCIIDEFEPIDHISEPVVTVAVEAKNTKDLPKLIEVLRQVSKEDPTIKVEINETTGEQLISGMGELHLEVVTNRIINDKKLEILVSEPIIVYKESVLGHSPVIEGKSPNKHNRFYIDVQPLDKPLYDALIEGDLKEGRIKTKETAQDFIELGMDKEEARRVWDVYNRSMFINMTRGIQYLDEVKELLLEGFEAALKDGPLANEEAVGLKFILSDAKLHEDAVHRGPAQVLPAIKKAIYASIMSANPCLLEPIQKVFISAPLEYMGNCNKDIQNRRGRIIGQETKGVIAEMDFEVPIAKMFGFAGDIRSATGGKGDFSTEMKGFETLPIYLQDDIVRQIRTRKGLSPEPYGPEHYSA | Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome. | D3E3N9 |
B3QQS6 | RL11_CHLP8 | 50S ribosomal protein L11 | Chlorobaculum | MAKKITGFIKLQIPAGGANPAPPVGPALGQKGVNIMEFCKQFNAKTQSEAGMIIPVVITVFSDKSFTFVTKTPPAAVLLLKEAKLQKGSGEPNRNKVGTVTMEQVRKIAELKKPDLNSVDIEGAAQMVMGTARSMGIVVEG | Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. | B3QQS6 |
A6LTK6 | ILVD_CLOB8 | Dihydroxy-acid dehydratase | Clostridium | MRSDVITKGSKSAPQRSLLSALGLTKEEMERPLVGIVSSQNDIVPGHMNLDKIVEAVKMGVSMAGGTPIVFPAIAVCDGIAMGHEGMKYSLVTRDLIADSTEAMAMAHAFDALVMVPNCDKNVPGLLMAAARVNIPTIFVSGGPMLAGKVDGCKTSLSSMFEAVGAYNAGKITAEKLDEYENNVCPTCGSCSGMYTANSMNCLTEVLGMGLQGNGTIPAVYSERIKLAKHAGMKIMELLEKNIRPRDIMTEDAFMNAMTMDMALGCSTNSMLHLPAIAHEVGFDLNVDIANEISSKTPNLCHLAPAGHTYIEDLNDAGGIYAVMNEINKLGLLKTNLITCTGKTVGENIEGCINKNPEVIRPVKNPYSQTGGIAVLKGNLAPDSCVVKRSAVVPKMLKHEGPAKVFDCEEDALEAINTGKIVAGDVVVIRYEGPKGGPGMREMLNPTSAIAGRGLGSSVALITDGRFSGASRGASIGHVSPEAAVGGNIALVEDGDMIQIDINANTINFLVSDEELARRKANWKPRKPKITTGYLARYAALVTSGNRGAILDIPKF | Functions in the biosynthesis of branched-chain amino acids. Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3-methylpentanoate (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3-methylpentanoate (2-oxo-3-methylvalerate) and of (2R)-2,3-dihydroxy-3-methylbutanoate (2,3-dihydroxyisovalerate) into 2-oxo-3-methylbutanoate (2-oxoisovalerate), the penultimate precursor to L-isoleucine and L-valine, respectively. | A6LTK6 |
C1DSX5 | KAD_AZOVD | Adenylate monophosphate kinase | Azotobacter | MRVILLGAPGAGKGTQARFITERFGIPQISTGDMLRAAVKAGSPLGLKVKGVMDSGGLVSDDIIIDLIRERIAQPDCARGFLFDGFPRTIPQAEALRDAGVSIDHVLEIAVDDEEIVSRMAGRRVHAASGRVYHDLHNPPKVAGKDDETGEDLIQREDDKEETVRHRLALYHSQTKPLVDFYQRLAATTGTPRYTRVEGIGSVSEITARVQAALA | Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. | C1DSX5 |
A3CRB1 | MNMG_STRSV | Glucose-inhibited division protein A | Streptococcus | MSHNFTESYDIIVIGAGHAGVEASLAASRMGCKVLLATINIEMLAFMPCNPSIGGSAKGIVVREVDALGGEMAKNIDKSYIQMKMLNTGKGPAVRALRAQADKELYSKEMRKTVENQENLTLRQTMINEILVEDGKVIGVKTATHQEYAAKAVIVTTGTALRGEIIIGDLKYSSGPNHSLAAIPLADNLRDLGFEIGRFKTGTPPRVKASSINYDVTEIQPGDEKANHFSYTSRDEDYVKDQVPCWLTYTNAESHEIIQNNLHRAPMFSGIVKGVGPRYCPSIEDKIVRFADKERHQLFLEPEGRDTEEVYVQGLSTSLPEDVQKDLVHSIKGLENAEMMRTGYAIEYDMIMPHQLRATLETKKISGLFTAGQTNGTSGYEEAAGQGIIAGINAALKIQGKQELILKRSDGYIGVMIDDLVTKGTVEPYRLLTSRAEYRLILRHDNADMRLTEMGREIGLVDDERWARFEIKKNQFDNEMKRLESIKLKPVKETNAKVEALGFKPLTDAVTAKEFMRRPEVSYQDVVQFIGPAAEELDEKIIELIETEIKYEGYISKALDQVEKMKRMEEKRIPANIDWDDIDSIATEARQKFKKINPETIGQASRISGVNPADISILMVYLEGKSRSISKNQAK | 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. | A3CRB1 |
B1A923 | ATPI_CARPA | F-ATPase subunit IV | Carica | MDVISCSSNTLKGLYDISGVEVGQHLYWQIGGLQVHAQVLITSWVVIAILLGSAIIAVRNPQTIPTAGQNFFEYVLEFIRDVSKTQIGEEYGPWVPFIGTMFLFIFVSNWSGALLPWKIIQLPHGELAAPTNDINTTVALALLTSVAYFYAGLTKKGLGYFSKYIQPTPILLPINILEDFTKPLSLSFRLFGNILADELVVVVLVSLVPLVVPIPVMFLGLFTSGIQALIFATLAAAYIGESMEGHH | Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. | B1A923 |
Q2K7G6 | COBT_RHIEC | N(1)-alpha-phosphoribosyltransferase | Rhizobium | MSVSGLPFDDFRTLLRELPGPDARALAAARERDAQLTKPPGALGRLEEIAFWLAAWTGRAPAVNRPLVAIFAGNHGVTRHGITPFPPAVTQQMVENFAAGGAAINQICVAHDLGLKVFDLALDYPTGDITEEAALSERDCAATMAFGMEAIAGGTDLLCIGEMGIGNTTIAAAINYALYGGSARDWVGPGTGSEGDMLERKIAAVEKAVALHSDHLDDPLEIMRRLGGREIAAMAGAILAARIERIPVLIDGYVATAAAAILKAANPAALDHCLIGHVSAEPGHLRSIEMLGKTPLLALGMRLGEGTGAALAAGIVKAAAACHSGMATFAQAGVSGKH | Catalyzes the synthesis of alpha-ribazole-5'-phosphate from nicotinate mononucleotide (NAMN) and 5,6-dimethylbenzimidazole (DMB). | Q2K7G6 |
A9IZA2 | TRMD_BART1 | tRNA [GM37] methyltransferase | Bartonella | MKFQARVLTLYPEMFPGFLGYSLAGHALERGIWSLETVQIRDFALDKHHSVDDTPAGGGAGMVMRADVLAAALDHCPQDSPRLLMSPRGRPFDQAYARRLADDSGITLVCGRFEGVDERVIEARELEEVSIGDYILSGGETAALVILDAIIRLLPGVMGNKASAKCESFENGLLEHPQYTRPSLFEGREIPPVLTSGHHKAIADWRQSQAELLTRQRRPDLYARYDKNRQKT | Specifically methylates guanosine-37 in various tRNAs. | A9IZA2 |
B0SXB0 | THIG_CAUSK | Thiazole synthase | unclassified Caulobacter | MNAHVPPESVSAAEDSWTVAGRTFRSRLIVGTGKYKDYATNAAAAKAAGAEIVTVAVRRVNLTDPTQPLLIDYVKPTEFTYLPNTAGCFTGEDAVRTLRLAREAGGWDLVKLEVLSDPKTLYPDMEETLRSLKLLVSEGFQVMVYCSDDPVYARKLEEAGAVAIMPLGAPIGSGLGIQNRVNLRIIVENAGVPVLVDAGVGTASDAAIGMELGCDAILMNTAIAEAKDPIRMARAMKHAVIAGREAYLAGRMQKRLYADPSSPLGGLI | Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is provided by the thiocarboxylate moiety of the carrier protein ThiS. In vitro, sulfur can be provided by H(2)S. | B0SXB0 |
Q93Z29 | ALMT5_ARATH | Aluminum-activated malate transporter 5 | Arabidopsis | MGGKMGSVPEQNTEKLLWQSSDVADSRDSKFRCCSWRALYEAPAKLYALGHSDRRKLYFSIKMGIALALCSFVIFLKEPLQDASKFAVWAILTVVLIFEYYVGATLVKGFNRALGTMLAGGLALGVAQLSVLAGEFEEVIIVICIFLAGFGASYLKLYASMKPYEYAFRVFKLTYCIVLVSGNNSRDFLSTAYYRILLIGLGATICLLVNVFLFPIWAGEDLHKLVAKNFKNVANSLEGCVNGYLQCVEYERIPSKILTYQASDDPLYSGYRSAVQSTSQEDSLLDFAIWEPPHGPYKTFNHPWKNYVKLSGAVRHCAFTVMAMHGCILSEIQASPEKRHVFSNELRRVGNEGAKVLRLFGEKVEKMEKLSLSLGEILKDVQRAAEALQMKIDSKSYLLVNSESWAAIKEQAEAEEARENDQEAKDDETKVIKSLSQIWDTNNNNNHQSNDQSQHWMSTESMMLKNREMWPSMSFIDGTVVNEIECKVYESASSLSLATFASLLIEFVARLQNIVNAFEELSTKAGFKDAVDQIPKV | Malate transporter. | Q93Z29 |
C6E4P3 | RS8_GEOSM | 30S ribosomal protein S8 | unclassified Geobacter | MCMTDPVADMLTRIRNAGMAKHQKVDIPSSNLKVSLATVLRAEGFIKNFKVIADNKQGILRVYLKFIDEKEPVINEIKRISKPGGRVYVNSDKIKQVKNGLGVAILSTSKGLVTDKTAREMGIGGEVLCTVW | 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. | C6E4P3 |
Q8DEC6 | OBG_VIBVU | GTP-binding protein Obg | Vibrio | MKFVDEAVIKVQAGDGGNGVVSFWREKFVTKGGPDGGDGGDGGDVYIQADENLNTLIDYRFQRFYEAERGQNGSGGNCTGKRGKDITLRVPVGTRAVDIHTNEIVAEVAEHGKKVMVAKGGWHGLGNTRFKSSVNRAPRQKTMGTKGEIRELRLELLLLADVGMLGLPNAGKSTFIRAVFAAKPKVADYPFTTLIPSLGVVSVVPEKSFVVADIPGLIEGAADGAGLGIRFLKHLERCRVLLHMIDIFPIDQSDPVQNALTIIDELEQYSEKLANKPRWLVFNKVDLVSEEQADEIIQEVIDALGWEEQYFKISAVNRQGTKELCYKLADFMEQLPREEQEVSEEEKVNFMWDYHPDANQGEVITEDDDDDWDDWDDEEDDGHVIYVRE | 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. | Q8DEC6 |
A9XFZ7 | DEF_COPTR | Defensin coprisin | Copris | MAKLIAFALVASLCLSMVLCNPLPEEVQEEGLVRQKRVTCDVLSFEAKGIAVNHSACALHCIALRKKGGSCQNGVCVCRN | Potent broad-spectrum antibacterial peptide against both Gram-positive (B.subtilis, S.epidermidis, and S.aureus) and Gram-negative bacteria (E.coli, S.typhimurium, and P.aeruginosa) . Is also active against all antibiotic-resistant bacterial strains tested . Induces apoptosis in C.albicans, but does not disrupt the fungal plasma membrane at all . Acts by permeabilizing the bacterial cell membrane, but not human membranes . Also shows potent anti-inflammatory activities, since it reduces both LPS-induced nitric oxide release and pro-inflammatory cytokine production . Anti-inflammatory activities are initiated by suppressing the binding of LPS to toll-like receptor 4 (TLR4), and subsequently inhibiting the phosphorylation of p38 mitogen-activated protein kinase (MAPK) and nuclear translocation of NF-kB (TNFRSF11A) . Does not show hemolytic activity against human erythrocytes . | A9XFZ7 |
Q8VUS8 | QADG_PARDE | Quinohemoprotein amine dehydrogenase catalytic subunit | Paracoccus | MNALVGCTTSFDPGWEVDAFGAVSNLCQPMEADLYGCADPCWWPAQVADTLNTYPNWSAGADDVMQDWRKLQSVFPETKGSS | Catalyzes the oxidative deamination of a wide range of primary aliphatic and aromatic amines . The physiological electron acceptor is the constitutive cytochrome c550 . | Q8VUS8 |
P19237 | TNNI1_HUMAN | Troponin I, slow-twitch isoform | Homo | MPEVERKPKITASRKLLLKSLMLAKAKECWEQEHEEREAEKVRYLAERIPTLQTRGLSLSALQDLCRELHAKVEVVDEERYDIEAKCLHNTREIKDLKLKVMDLRGKFKRPPLRRVRVSADAMLRALLGSKHKVSMDLRANLKSVKKEDTEKERPVEVGDWRKNVEAMSGMEGRKKMFDAAKSPTSQ | Troponin I is the inhibitory subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity. | P19237 |
A8AA22 | RNP1_IGNH4 | Rpp29 | Ignicoccus | MKHTPKNVIYHNLVGLRVEVLAHPDPSMKGLKGRIIDESKSFLTIEKDNGELVKVQKLGTFVLVLPSGRKVEVRGELLRGRPEERLKKFLKA | Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. | A8AA22 |
Q54K91 | ACH1_DICDI | Acetyl-CoA deacylase | Dictyostelium | MHKIVQQGSKSLIESRIKRKSLLSKVVTDVSQLIPYFQNGHYVSMGGFAGTGYPKVVPIALADHVEKNGLQGKLKMNLFVGASVGPETEDRWAMLDMIDKRYPHQNGHHIRNGINSGRIRFADQHLSTFASDLLAGYYTLDKPHGSKRTMDIAIVEATEITEDGCIVPGASVGITPEILQMADKIIIEINTSLPSFKGLHDMVKIALPPFSKPYQITRVDDRIGLEAFPVDPEKIIAIVESQLPDNTSVGAPEDETSSAIANNIVQFFIHEIEQGRFPKNLLPLQSGIGSIANAVIGGLSKGPFDNLSVWTEVIQDTFLDFFDNGKLKFASATSLRFSPPGFNRLFNNWENYKSKIILRNQAISNAAELISRVGCIALNTPCEVDIYGHVNSTNTMGSKMLNGLGGSGEFLRNSRISIVHTPSTRPTKTDPHGISCIVPFASHIDHTEHDIDIIVTEQGLADIRGLAPYERAKVIIQNCAHPIYKPILMEYLETSRQICLKNHMGHEPHQLDKAFKFYTNLSEKGTMKIDKW | Presumably involved in regulating the intracellular acetyl-CoA pool for fatty acid and cholesterol synthesis and fatty acid oxidation. | Q54K91 |
Q0CP15 | NST1_ASPTN | Stress response protein nst1 | Aspergillus subgen. Circumdati | MAPSQHPKSAAAPATTSDQMSTASSRPTNGTAHTSAETAYPSSMTDSKPTQSGPGSRASDEQDADEAYSNHSEQHMDHSNPDGHPSKPSGRKKKKKAKKGRAGSQTLGDESSTPLSTPSVSMSHPLPPPLPPHLGTRTILKSAKDRSIWNTSTQEERENIKTFWLELGEEERRQLVKVEKDAVLKKMKEQQKHSCSCTVCGRKRTAIEEELEVLYDAYYEELEQYANNNQGSFEKGSPIVPPPRLYQPPLRSPGQHTRTQGQFHPSRGRIHEITEDEEDLEEDYDDEEEDDDEPYSDDEFEDEETRAARADFFAFGNSLTVKDGILTVADDLLKNDGKHFIDMMEQLAERRMQREEDTQYNIAAAHQSLHSGHNHPPYDEEDYDDEEDEEYDSQEEDDYDEDEMDTMTEEQRMEEGRRMFQIFAARMFEQRVLTAYREKVAEQRQQKLIEELMEEQTRTEQKNAKKAREAEKRKEKKRLQKQAKEEEKARREAEKAAEEAAAKAEQEKKLEEQRRKREEQRKKREAERKAQEEERARKEAEKQRRLREERERQAEAERKHREQKEQEKKKREEARRKEREERELREKKAKEERERKAQEDQKKANQETPETKRTSHLGPVPIPANLQPQGSSSHLQSPHLQSASPAVPKAPTPAKARQPSQQGSHGSSPRSQQASTEPFHTSISPRSMAPSQSSGASSVASKQGYGQQPMLHHPQPSTPLSPLGSVNRSLPPGFASAGLPSNPPGLPGMVPRPPIGHELPTYPPHSGPLMNQLRGFPAPNGIPIPPGINGTRPLAPGRGFPLEAAPGLPFHTQQPIAGAFASHQGGMSHGHSRQPSGSFERSPLEPHAQPFPISRPSPIKRPPSTQQEQSDANRATQRDVDNLSAQLGSSALLDDTDIPFTSNLSQSLPGATAPGSLPGPTRASFGAPSLFPDPLASKPGGFPMGPGVGANTWGTQIPFVSSAFPGAPAWGTAHGSGWSNNAFGSGGHHRAHTSRPVAIRLLVIQACKQLDTMSSSKAGSGYHDVKIVLQQVEQLRPSNEPSIPLKEMLDICDTEGNTQNGGGSFSIKKDETGEFVKFEPDNNSAASGHRGSIVPGEIGSPVPSSSMPAFGGIGNTPSVLRQFSSPTGF | May act as a negative regulator of salt tolerance. | Q0CP15 |
A1C777 | EIF3D_ASPCL | Eukaryotic translation initiation factor 3 subunit D | Aspergillus subgen. Fumigati | MAPVSIADLVAALPSEDSWGPATPSDNMLEGVPYAPFSKGDKLGRMADWTSDSKDRDRAGRQAYNRNYRDQQVYGAGTSSLFNVQVAEDESSFSVVDNTRTTTKRTFGRGGGTVFRGRAQRGGAGQRGGRAGFQRVGAGRGQGGDRYYDNRGGRGNRGRRSGWKDYDKPQRTREPSVNVRPDWTMLEEVDFSRLSKLNLEAPEGEDLDSYGFLYYYDRSYDKAPVKNAERRLQALDRAAYNVTTTQDPIIQELAEKNEATVFATSDILSMLMCAPRSVYSWDIVIVHQGNKIYFDKREGASIDLVTVNENAADAPLEVTDSSGKQESLNTPSALALEATFINHNFALQTVVESEDSKVGFSHPNPFYNASEETEPLASKGYKYRRFDMSLQEDEEPLNLIVRTEVDAVMKNPVSGEEQQLVVKALNEFDSKAPGSGGALDWRSKLWSQRGAVVATEMKNNSIKLARWATQAILAKADAMKLGFVSRANPRSAAGHVVLGVVSYKPRDLAAQMNLNLGNGWGIVRTIVDRIQALDANEEEDKVTKYVLIKDPNRPVLRLYSVPANTFEEDDEAADEQEEKATEESEE | mRNA cap-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation. In the eIF-3 complex, eif3d specifically recognizes and binds the 7-methylguanosine cap of a subset of mRNAs. | A1C777 |
O94295 | PUS2_SCHPO | tRNA-uridine isomerase 2 | Schizosaccharomyces | MTSISKRKNQQEHIPAEDLETPKLPKREKIEGTKESNKVRIIILLGYSGYGYHGIQINNPLKTIEGDVVAVLKKLGYLKTNNIDAEHLCIARAARTDKGVHTLRNLISLNLFVDKPLDISLLKTELNEALCSQIRVWSVFPAPKYFNPRISCESRTYEYLIPSFALLPPKPSCPLFKKMQKNLSRKLDNELERNLVYSMNDLISFWNTVKLKQKEIQEMFDTNKDAFTNPFKGMFYEKPIPAGIVIPPQAKLKKALKQAEYYCYMNYRIKEDRLKVLQQLLKKYEGRHNFHNFTVTDDSTSPSNYRFIESVTCGTPFVYENWEWIPVTIKGNSFMLNQIRKMMAHVLMIIRSCAPTGLIDKAFDPNITMNISKSPGHVLLLKDIKFSSYNDSVTDGLEKIQFDCFEEDILSLKIKTIYPDIIKLEQKEKLFFSFLSYIDQHTGHQFDYLFG | Formation of pseudouridine at positions 27 and 28 in the anticodon stem and loop of transfer RNAs; at positions 34 and 36 of intron-containing precursor tRNA(Ile) and at position 35 in the intron-containing tRNA(Tyr). | O94295 |
O64896 | TPPA_ARATH | Trehalose 6-phosphate phosphatase | Arabidopsis | MDMKSGHSSPVMTDSPPISNSRLTIRQNRLPYSSAAATAISQNNNLLLTVPRKKTGILDDVKSNGWLDAMKSSSPPPTILNKDNLSNDATDMTYREWMQLKYPSALTSFEKIMSFAKGKRIALFLDYDGTLSPIVEEPDCAYMSSAMRSAVQNVAKYFPTAIISGRSRDKVYEFVNLSELYYAGSHGMDIMSPAGESLNHEHSRTVSVYEQGKDVNLFQPASEFLPMIDKVLCSLIESTKDIKGVKVEDNKFCISVHYRNVEEKNWTLVAQCVDDVIRTYPKLRLTHGRKVLEIRPVIDWDKGKAVTFLLESLGLNNCEDVLPIYVGDDRTDEDAFKVLRDGPNHGYGILVSAVPKDSNAFYSLRDPSEVMEFLKSLVTWKRSMG | Removes the phosphate from trehalose 6-phosphate to produce free trehalose. Trehalose accumulation in plant may improve abiotic stress tolerance. | O64896 |
Q11CM8 | DCUP_CHESB | Uroporphyrinogen decarboxylase | unclassified Chelativorans | MAERKLLEALNGRTVFPPPIWLMRQAGRYLPEYRETRKKAGSFLDLCYNPELAVEVTLQPIRRFGFDAAILFSDILVIPHALGRDLRFEEGAGPLMSPIQANEIPGLDPNLIHNRLQPVYETVRRLRSELSEETALIGFCGAPWTVATYMIAGRGTPDQAPARLFGYRHPKEFSELLDTISAASADYLIRQIDEGADAVQIFDSWAGILDETSFDQWCLRPVAEIVRRVRERHPNVPIIGFPKGAGWLYSRYRQQTGVTALGLDWTVPLSEASRLQAEGPVQGNLDPMRLVAGGQALSKGVEDILSALGGAPFIFNLGHGITPETPIGHVEAMIQQVREGRL | Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III. | Q11CM8 |
Q8AVR4 | PDC10_XENLA | Programmed cell death protein 10 | Xenopus | MRMTMEEMKNEAETTSMVSMPLYAVMYPVFNELERVNLSAAQTLRAAFIKAEKENPGLTQDIITKILEKKSVEVNFTESLLRMAADDVEEYMVERPEPEFQELNEKARALKQILSKIPDEINDRVRFLQTIKDIASAIKELLDTVNNVFKKYQYQNRRALEHQKKEFVKYSKSFSDTLKTYFKDGKALNVFISANRLIHQTNLILQTFKTVA | Promotes cell proliferation. Modulates apoptotic pathways. Increases mitogen-activated protein kinase activity. Important for cell migration, and for normal structure and assembly of the Golgi complex. Important for KDR/VEGFR2 signaling. Required for normal cardiovascular development. Required for normal angiogenesis, vasculogenesis and hematopoiesis during embryonic development. | Q8AVR4 |
Q92C06 | GCST_LISIN | Glycine cleavage system T protein | Listeria | MTELLKTPIHPLYAKYGAKTIDFGGWDLPVQFAGIKAEHEAVRTDAGLFDVSHMGEILVEGPDSTSYLQYLLSNDIEKIKIGKAQYNIMCYETGGTVDDLVVYKKSETEYILVVNAANTEKDYEWMVQNIVGDVTVKNASSEFGQLALQGPNAEKILSKLTDADLSSISFFGFIEDADVAGVKTIISRSGYTGEDGFEIYMQSADAGKVFEAILAEGVAPIGLGARDTLRLEAVLALYGQELSKDITPLEAGLNFAVKLKKEADFIGKQALIKQKEAGLTRKLVGIELIERGIPRHDYPVFLNDKEIGVITSGTQSPTLGTNIGLALIDTAYTELDQELEVGIRNKKVKAKVVQTPFYKRAK | The glycine cleavage system catalyzes the degradation of glycine. | Q92C06 |
O31149 | PT1_LISMO | Phosphotransferase system, enzyme I | Listeria | MAKELKGIAASDGIAIAKAYLLVEPDLSYEKTEVTDVESEVKRFESALEVSRTELSMIREKAAKDLGEDKAQIFDAHLLVLNDPELTGPIEESIKNSKTNAETALQETTDMFIGMFESMDNEYMRERAADIKDVRKRVLSHLLGVTIPNPALIDEEVVVVAADLTPSDTAQLNRNFVKGFVTDIGGRTSHSAIMARSLEIPAVVGTKEVTASVAKNDIVIIDGLEGNVIIHPTEEQIAHYEKIKSDFALQQAEWDKLKNEKTVSKDGVHVELAANIGTPNDLEGVISNGGEAVGLYRTEFLYMGRDNFPTEEEQFEAYKAVVSGMDGKSVVVRTLDIGGDKTLPYLELPEEMNPFLGFRAIRLCFANEELFRTQLRALLRASVYGNLKIMFPMIATVNEFRQARDILLDEKAKLKAAGTEVSDSIELGIMIEIPAAAVLADQFAKEVDFFSIGTNDLIQYTMAADRMNERVSYLYQPYNPSILRLVKMVIDASHKEGKWTGMCGEMAGDQTAVPLLLGLGLDEFSMSASSILKSRSLIKRLDQSEMVKLAEEALNKSTAEEVVELVEKYTAE | General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. Enzyme I transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein (HPr). | O31149 |
B0BQ46 | PURT_ACTPJ | Phosphoribosylglycinamide formyltransferase 2 | Actinobacillus | MTTIGTPLRPNATKVMMLGSGELGKEVVIELQRLGVEVIAVDRYENAPAQQVAHRAYTISMLDGAALRALAEKEKPDFIVPEVEAIATATLVELEQEGYNVVPTAKATQLTMNREGIRRLAAEELGLKTSPYRFVDNLEDFKQAVAEIGIPCVVKPIMSSSGHGQSVIKSEDQIQQAWDYSQEGGRAGGGRVIVEGFIKFDYEITQLTVRHVNGTSFLAPIGHRQEDGDYRESWQPQAMSDLALKRAQETAERITTALGGRGIFGVELFVCGDEIIFNEVSPRPHDTGMVTMASQELSQFALHARAILGLPISEIYQISPAASKAIVVEGKSNNMTFGNLDKVLEEIGTNIRLFGKGEVNGHRRLGVILARDENTEKALAKAERAYAKLAVQL | Involved in the de novo purine biosynthesis. Catalyzes the transfer of formate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR). Formate is provided by PurU via hydrolysis of 10-formyl-tetrahydrofolate. | B0BQ46 |
Q4UMR4 | RL6_RICFE | 50S ribosomal protein L6 | spotted fever group | MSRVGKLPITIPEGVKVGLNDLEVKISGPKGELSKTFKGNIAISLEENKLLVKPLAANKNARAMWGTARSIISNMVTGVKEGFKLKLEINGVGYRAMVKGKYLNLMLAKSHNTKIEIPSDIKIEVPKQNIIILEGTDKEKLGQFASIIIKQRPPEPYKGKGIKFENQFIPRKEGKKN | This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center. | Q4UMR4 |
Q9Z6T0 | DEGPL_CHLPN | Protease Do | Chlamydia | MITKQLRSWLAVLVGSSLLALPLSGQAVGKKESRVSELPQDVLLKEISGGFSKVATKATPAVVYIESFPKSQAVTHPSPGRRGPYENPFDYFNDEFFNRFFGLPSQREKPQSKEAVRGTGFLVSPDGYIVTNNHVVEDTGKIHVTLHDGQKYPATVIGLDPKTDLAVIKIKSQNLPYLSFGNSDHLKVGDWAIAIGNPFGLQATVTVGVISAKGRNQLHIADFEDFIQTDAAINPGNSGGPLLNIDGQVIGVNTAIVSGSGGYIGIGFAIPSLMANRIIDQLIRDGQVTRGFLGVTLQPIDAELAACYKLEKVYGALVTDVVKGSPADKAGLKQEDVIIAYNGKEVDSLSMFRNAVSLMNPDTRIVLKVVREGKVIEIPVTVSQAPKEDGMSALQRVGIRVQNLTPETAKKLGIAPETKGILIISVEPGSVAASSGIAPGQLILAVNRQKVSSIEDLNRTLKDSNNENILLMVSQGDVIRFIALKPEE | Might be efficient in the degradation of transiently denatured and unfolded proteins which accumulate in the periplasm following stress conditions. | Q9Z6T0 |
Q03QU1 | DNAK_LEVBA | Heat shock protein 70 | Levilactobacillus | MASNKIIGIDLGTTNSAVAVLEGSTPKIIANKEGARTTPSVVAFKDGETQVGEVAKRQAITNPNTISSIKSHMGEAGYKVSVDGKDYTPQQVSAMILQHLKAFAEDYIGDTVEKAVITVPAYFNDAQRQATKDAGKIAGLSVERIINEPTAAALAYGLDKQDKDEKVLVYDLGGGTFDVSVLELGDGVFDVLSTNGDTHLGGDDFDQKIMDWLVAGFKEENGVDLSKDKMALQRLKDAAEKAKKDLSGVTEAQISLPFISAGENGPLHLEKSLSRAKFNELTADLVEKTRIPVQNALKDADLQASDIDVVILNGGSTRIPAVQEAVKSWTGKEPNHSINPDEAVALGAAVQGGVITGDVKDVVLLDVTPLSLGIETMGGVFTKLIDRNTTIPTSKSQVFSTAADNQPAVDIHVLQGERPMAADNKTLGNFQLTDIPAAPRGVPQIQVTFDIDKNGIVNVSAKDMGTNKEQKITIKSSDGLSDEEIEKMMNEAKENEEADKKRKEEVDTKNEVDQLLFQTDKTLKDVKGKVSDDEIKKAEDARDALKKAQEANNLDDMKAKKDDLTKIIQDLSVKLYQQAQSEAGDGNAAGADGATADADKKDDNTVDGDFHEVNDDDKK | Acts as a chaperone. | Q03QU1 |
B2USG1 | ILVC_HELPS | Ketol-acid reductoisomerase type I | Helicobacter | MALPVYYDKDIDLGVIQSLQVGIIGYGAQGEAQALNLRDSKVKVRIGLYQGSLSVPKAKAEGFEVLEVKELVQQSDLIMALLPDELHKEVLEKEVIPFLKEGQIVGFAHGFSVHFNQVVLPKGVGAILVAPKGPGSALREEYLKNRGLYHLIAIEQESSKNNAKAVALSYAKAMGGGRMGVLETSFKEECESDLFGEQAVLCGGLEAIIRMGFETLIKAGYPEELAYFECVHEVKLVADLLHYKGVEGLRKHISNTAEFGAIKNREPMGNLLEKRMQKILKKIQNGSFAKDFLLEKSLNYPRLNTERKALKETKIEQIGEILRAPFNHKK | Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate. | B2USG1 |
A1SDP0 | ARAA_NOCSJ | L-arabinose isomerase | Nocardioides | MTHHPDELEIWFLTGSQHLYGPEVIDQVAEHAARIVAALDASPHLPVRVVSKPVLTETDSIRRALLDATATDSCVGVIAWMHTFSPAKMWITGLDALRKPLLHLHTQANQALPWAEIDMDFMNLNQAAHGDREFASVQTRMGVARKTVTGHVEDPEVARRIGLWARAALGRHALAGMRLARFGDNMRNVAVTEGDKVEAERRFGVSVNTWGVNDLVAVVDEVADADVDKLCEEYADSYDVAAELLPSGERHESLRYGARIELGLRSFLTEGGFTAFTSNFEDLGGLRQLPGLAVQRLMADGYGFGGEGDWKTSVLLRTLKVVADGLPGGTSFMEDYTYHLVPGEERILGAHMLEVCPSIAEGRPSLEIHPLSIGGREDPVRLVFDAAPGPAVLLGLADLGERFRFVGNEVEVVAPTEPLPNLPVARAVWRPAPDLRTSTEAWLMAGGPHHTVLSTALGAEHLDDLAEMTGTELVLVDADTTIRGLAKELRWSAAYHRLAQGL | Catalyzes the conversion of L-arabinose to L-ribulose. | A1SDP0 |
A6TM76 | TRPB_ALKMQ | Tryptophan synthase beta chain | Alkaliphilus | MMKVKELPKKFGKFGGQFVPETLMNALIELERQFIQTKEDDEFQEMYRYYVREYSGRPTPLYYAENLTKKLGGGKIYLKREDLNHTGAHKINNVIGQVLLARKMKKKRIIAETGAGQHGVATATICAMFDLECVVYMGAEDIERQALNVFKMEMLGAEVVSVTSGTATLKDATNEAIRDWVANVKDTYYVIGSVVGPHPYPTMVRDFQRIIGDEVKEQILEKEGRLPNYLVACVGGGSNAMGLFYPFYEDEAVALYGVEAAGLGVETDQHAATITKGSMGVIHGMMTYLLQDEQGQITPVHSISAGLDYPGIGPEHAYYHHTGRANYVAITDEEALEAFQLLTRLEGIIPALESAHAIAYLMKLAPKTKGDDIIVLNLSGRGDKDIHTISKLLGGNRDDK | The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. | A6TM76 |
Q0KBK6 | MNMC_CUPNH | FAD-dependent cmnm(5)s(2)U34 oxidoreductase | Cupriavidus | MPRALEPAEPILSAEGIPYSPRYDDVYHSTEGGLAQAAHVFLGGNGLPQAWAGQRQFVIVETGFGLGLNFLATWQAWRADPQRCGTLHFVSIEKHPFTREGLAQLHAGLDGLQPLAQALQAQWPLALPGLHRLAFDGGRVVLTLALGDIEQMLPRLAAGADAFYLDGFAPARNTEMWSPQVFRGLARLARPGARLATWAAAGFVRRGLKEVGFEVSRAPGFGGKWQMTVASFRPQWKARRHAPPLPAQWAERHAIVIGAGLAGCAVTERLAARGWRVTLFDGHDGPARQTSAHRAAAMHAHLSADDSLLSRLSRTGNQYALRAWAELAEAGHAVGWHGCGVLQIGEDEAEGEAQRAALAAMRLPEGFVRWMSAEEAAAAHHAGVPRGGLWFPQGGWVAPPDICSAQLAQAGAAVTARFGCRVAAIARVDGQWQALGQDGEVLASAPVLVLANAHEAQQLLPQQHWTMRRVRGQLTTLASAQVDALGGWPDCVVTGAGYLLPRTADGAGRVGSSYDADEGPLVEQPAVHAANLARLSGMLPRQADAVAAIDPATLSGYVGVRTVTHNRLPLVGQVPDEAAALAQAASLRGAHLRDLPRMPGLYAALAYGSRGLTWAALGAELLASQIEGEPLPLESDLADAMDPARLLLRALRHGHTG | Catalyzes the last two steps in the biosynthesis of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at the wobble position (U34) in tRNA. Catalyzes the FAD-dependent demodification of cmnm(5)s(2)U34 to nm(5)s(2)U34, followed by the transfer of a methyl group from S-adenosyl-L-methionine to nm(5)s(2)U34, to form mnm(5)s(2)U34. | Q0KBK6 |
Q5JHS5 | PAN_THEKO | Proteasome regulatory particle | Thermococcus | MSIENTDVHPEGYDDYVTFLKRRIRQLELQVRTLEADKERLERELSRLRMEMSRLRQPPAFAGNVIEVLDDERAIVQNYNGPRFVVRIAPWIERDKLKPGARVALDQRTMAIVELLPSEKDPSVLGFEVIERPKVTYNDIGGLEKQLQELREAIELPLKHPELFEQVGIEPPKGVLLYGPPGCGKTLMAKAVANHVNATFIRVVGSELVRKFIGEGARLVHELFELAKEKAPTIIFIDEIDAIGAKRMDETTGGEREVNRTLMQLLAEMDGFDPRGNVKVIAATNRPDILDPALLRPGRFDRLIEVPLPDYQGRLEILKVHTRKMNLKGVDLRVIAEITEGASGADLKAIATEAGMFAIRDRRTYVTQDDFLKAVDKVIGSEKRLAQQIAMHEVMYG | ATPase which is responsible for recognizing, binding, unfolding and translocation of substrate proteins into the archaeal 20S proteasome core particle. Is essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C-termini of the proteasomal ATPase function like a 'key in a lock' to induce gate opening and therefore regulate proteolysis. Unfolding activity requires energy from ATP hydrolysis, whereas ATP binding alone promotes ATPase-20S proteasome association which triggers gate opening, and supports translocation of unfolded substrates. | Q5JHS5 |
A9N514 | ULAF_SALPB | Phosphoribulose isomerase | Salmonella | MQKLKQQVFDANMDLPRYGLVTFTWGNVSAIDRERGLVVIKPSGVAYETMKVDDMVVVDMDGKVVEGRYRPSSDTATHLALYQRYPSLGGVVHTHSTHATAWAQAGMAIPALGTTHADYFFGDIPCTRALSEEEVQGEYELNTGKVIIETLGEVEPLHTPGIVVYQHGPFAWGKDAHDAVHNAVVMEEVARMAWIARGINPALNPIDDYLMNKHFMRKHGPNAYYGQK | Catalyzes the isomerization of L-ribulose 5-phosphate to D-xylulose 5-phosphate. Is involved in the anaerobic L-ascorbate utilization. | A9N514 |
Q7VKU5 | DUSC_HAEDU | tRNA-dihydrouridine synthase C | Haemophilus | MIKSIPRIMLAPMQGVLDPFMRKLLTAYNDYDLCVSEFVRVVDQRLPKKTFYRLAPELLQGGLTDSGTPIRVQLLGQYPQWLAENAQLAIELGSYGIDFNCGCPSKTVNGSHGGAALLKDPELIYCATKAIREAVPKAQPVSVKMRLGWDCASQCFEIADAIQQAGADEITVHGRTKQDGYRAERINWQAIGQIQQRLNIPVIANGEILDFNSAQKCREITACCGLMIGRGALNTPNLSKVIKYNVAKMAWSEVLQLLYEYVNMPNERDSGFYHVARIKQWLHYLDKAYPEAVDLFQIVKTEHSYDGVKAHIEKAVGRNEKTNFQ | 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 U16 in tRNAs. | Q7VKU5 |
C0R4Y2 | NUOB_WOLWR | NDH-1 subunit B | unclassified Wolbachia | MTNQILSNDDWGRYKKEGFLVTKFGDLTDYVMNWARSGSLWPMTFGLACCAVEMMHTASSRYDLDRYGIMFRASPRQSDVMIVAGTLTNKMAAALRKVYDQMADPKYVISMGSCANGGGYYHYSYSVVRGCDRIVPVDVYVPGCPPTAEALLYGMLCLQNKIKRTRNG | 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. | C0R4Y2 |
O13924 | HASP_SCHPO | Serine/threonine-protein kinase haspin homolog hrk1 | Schizosaccharomyces | MESRSKVKTYGKNRRYINKDIEIWASLDERPCALKPRNIENFNNQERSDLEHIHSKPKKDSLLSWNILLKKGSYKENELLAKRNQNLVPTVIIPASPRDNASKSVVSKKEVVNLSSSVALSGKPANNSKLDPLHRLLQIVAQEDALPFSQFVKSQTFEIQKIGEASYSEVYQASNADDVPVVWKVIPFGEDGQAQYADVLNEVQISQWIKVDGFANLHQVVVVKGTYPSLLLEEWDRYLMQNGSENDRPDSYSSTQLYCVLCLDHSGTDLEHFELRSWRECWSVFYETLKILSLVETRYEFEHRDLHWGNILIRKADRSEEEVSFLLNEISLDDIESVDFPGSQDKADDFDNILQVTLIDFTLARASYSQGIISYNEFNDPDLFNGVDDYQFDIYRLMSRVTKGRWAQFFPITNVLWLHYLIHQLLHKKNLSSPLTETETLMRSRLKQIFRLIDPVKTMQFQQAEDSIRSKSTVTSATSLLNWVRQKY | Serine/threonine haspin-like protein kinase involved in cell cycle regulation. Acts in chromosomal passenger complex (CPC) targeting to centromeres by phosphorylating histone H3 at 'Thr3' (H3T3ph). | O13924 |
B1IAU3 | RLMN_STRPI | tRNA m2A37 methyltransferase | Streptococcus | MKPSIHSLTHQTMQEWVLEQGEKKFRADQIWEWLYRKRVQSFEEMTNLSKDLIAKLNDQFVVNPLKQRIVQESADGTVKYLFELPDGMLIETVLMRQHYGLSVCVTTQVGCNIGCTFCASGLIKKQRDLNNGEIVAQIMLVQKYFDERGQDERVSHIVVMGIGEPFDNYNNVLNFFRTINDDKGMAIGARHITVSTLGLAHKIRDFADEGVQVNLAVSLHAPNNELRSSIMKINRAFPIEKLFAAIEYYIETTNRRVTFEYIMLNEVNDGVEQALELAELLKNIKKLSYVNLISYNPVSEHDQYSRSPKERVLAFYDTLKKKGGNCVVRQEHGTDIDAACGQLRSNTMKRDRQKAVAAVNP | Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. | B1IAU3 |
C3L062 | THIM1_CLOB6 | 4-methyl-5-beta-hydroxyethylthiazole kinase 1 | Clostridium | MENKNVIQKMREKTPLIHCITNYVTINDCANILLSFGASPAMCEAYDEVYDFVSISSALYINLGTLTKEQETAAVLASISAKNHNVPVVIDPVGCPAIKRKVEVINRMAEVGRIDIIKGNIGEIKFLAGMDSETRGVDSLDNGENALDACTQLAKKYNCIVAATGEKDFVSDGKRGSVIKNGTEMLTKVTGAGCMLGALCAATCANFEDKLVSTTAAILSMNIAGEKAYEKAQLPGSFRIALIDNIYMISDEEIWERGNVEWK | Catalyzes the phosphorylation of the hydroxyl group of 4-methyl-5-beta-hydroxyethylthiazole (THZ). | C3L062 |
A6TKT6 | HIS6_ALKMQ | ImGP synthase subunit HisF | Alkaliphilus | MITKRIIPCLDVRKGRVVKGVNFVDIKDAGDPVALARAYNDQGADEIVFLDITASHEERYILLDVVKKTSEEIFIPLTVGGGIRTVEDMRQIIKSGADKVSINSSAVKNPSMITDCARQFGSQAVVIAMDVKRGADGRYEVYVRGGREKTGLEAVDWARRVAQLGAGEILLTSMDRDGTKSGYDLEITKRISQAVNIPVIASGGAGSVQDFADAFIEGQADAALAASLFHYNEVSIPRLKQSLHEMDISMRR | IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit. | A6TKT6 |
Q5NQ50 | RL6_ZYMMO | 50S ribosomal protein L6 | Zymomonas | MSRIGKKPVAIPTGVTANIADGVLSVKGPKGELSMPLSSEVTYSLEDGQLSVQPVNDTKRARSFWGMQRTLVQNLIDGVTQGYSKTLQITGVGYRAASQGKTLKLQLGYSHDIDFAIPEGITIQTPEPTTVNISGIDKQKVGQVAAEIRRWRRPEPYKGKGIKYAGEFIFRKEGKKK | This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center. | Q5NQ50 |
Q64687 | SIA8A_MOUSE | Sialyltransferase St8Sia I | Mus | MSPCGRALHTSRGAMAMLARKFPRTRLPVGASALCVVVLCWLYIFPVYRLPNEKEIVQGVLAQRTAWRTNQTSASLFRRQMEDCCDPAHLFAMTKMNSPMGKSLWYDGELLYSFTIDNSTYSLFPQATPFQLPLKKCAVVGNGGILKMSGCGRQIDEANFVMRCNLPPLSSEYTRDVGSKTQLVTANPSIIRQRFENLLWSRKKFVDNMKIYNHSYIYMPAFSMKTGTEPSLRVYYTLKDVGANQTVLFANPNFLRNIGKFWKSRGIHAKRLSTGLFLVSAALGLCEEVSIYGFWPFSVNMQGDPISHHYYDNVLPFSGYHAMPEEFLQLWYLHKIGALRMQLDPCEEPSPQPTS | Catalyzes the addition of sialic acid in alpha 2,8-linkage to the sialic acid moiety of the ganglioside GM3 to form ganglioside GD3; gangliosides are a subfamily of complex glycosphinglolipds that contain one or more residues of sialic acid . Can catalyze the addition of a second alpha-2,8- sialic acid to GD3 to form GT3 . Can use GM1b, GD1a and GT1b as acceptor substrates to synthesize GD1c, GT1a and GQ1b respectively . | Q64687 |
Q65SS8 | NRDR_MANSM | Transcriptional repressor NrdR | Basfia | MHCPFCSTEETKVIDSRLVSDGYQVRRRRECTKCHERFTTFETAELVVPKIIKNNGMREPFNEDKLRRGIQHALEKRPVSADDVEKAISHITHQLRATGEREVPSKLVGSLVMEELKKLDKVAYIRFASVYLSFENINEFSNEIEKLKD | Negatively regulates transcription of bacterial ribonucleotide reductase nrd genes and operons by binding to NrdR-boxes. | Q65SS8 |
Q3ARQ5 | COBT_CHLCH | N(1)-alpha-phosphoribosyltransferase | Chlorobium | MKEKLETLLAAIQPADQTLRQAIQAHLDDLTKPQGSLGRLEEIAQQYILATGQIHPSLPKKKICCFAGDHGVAAEGVSAFPAEVTPQMVYNMLHGGAAINVLSRHVGAELSVVDVGVNHDFADAPNLVQCKVKRGSANMAVGAAMSETETLQAILAGAELAFQAADAGYGLLGTGEMGIANTTPATALYAVLLNLPVEAITGRGTGIDDARLHHKIAVIERAIAVNAERCATPFGTLAALGGFEIAAITGFILGAAARRIPVVVDGFISSSGALVAMKMVPSVVDYLFFSHLSAEQGHGAVMEALGVRPMLSLDLRLGEGTGAALAMQLVDAALKIYNEMATFSGAQVSEKIEG | Catalyzes the synthesis of alpha-ribazole-5'-phosphate from nicotinate mononucleotide (NAMN) and 5,6-dimethylbenzimidazole (DMB). | Q3ARQ5 |
Q43309 | 1A14_ARATH | S-adenosyl-L-methionine methylthioadenosine-lyase 4 | Arabidopsis | MVQLSRKATCNSHGQVSSYFLGWEEYEKNPYDVTKNPQGIIQMGLAENQLCFDLLESWLAQNTDAACFKRDGQSVFRELALFQDYHGLSSFKNAFADFMSENRGNRVSFDSNNLVLTAGATSANETLMFCLADPGDAFLLPTPYYPGFDRDLKWRTGVEIVPIQSSSTNGFRITKLALEEAYEQAKKLDLNVKGILITNPSNPLGTTTTQTELNILFDFITKNKNIHLVSDEIYSGTVFNSSEFISVMEILKNNQLENTDVLNRVHIVCSLSKDLGLPGFRVGAIYSNDKDVISAATKMSSFGLVSSQTQYLLSSLLSDKKFTKNYLRENQKRLKNRQRKLVLGLEAIGIKCLKSNAGLFCWVDMRPLLRSKTFEAEMDLWKKIVYEVKLNISPGSSCHCEEPGWFRVCFANMIDETLKLALKRLKMLVDDENSSRRCQKSKSERLNGSRKKTMSNVSNWVFRLSFHDREAEER | 1-aminocyclopropane-1-carboxylate synthase (ACS) enzymes catalyze the conversion of S-adenosyl-L-methionine (SAM) into 1-aminocyclopropane-1-carboxylate (ACC), a direct precursor of ethylene. | Q43309 |
B0U659 | FTSB_XYLFM | Cell division protein FtsB | Xylella | MRNWRWLLLVLAALLAWLQHRFWFGPGNSGEVRMLQVQIVQQHQENERLRQRNASLAAEVKNLKDGDAAIEERARSELGMIKPGEIFYRVVEDIPAPLPNDTSADHGVDLSQPRREKR | Essential cell division protein. May link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic. | B0U659 |
Q9EST2 | HNMT_CAVPO | Histamine N-methyltransferase | Cavia | MASSMRSLFSDHGRYFEAFRRFLNNSTEYQCMREFMDKQLPGIIARIGGSKSEIKVLSIGGGAGEMDLHILSKVKAQYPGVHIINEVVEPSAEQITKYKELVAKTSNLENIKFAWHKETSSEYQNRVMEQKEIQKWDFIHMIQMLYYVDDIPATLKFFHSLLATNAKILIILVSGKSGWLKFWKKYRSRLPQNDLCQYVTSFDIIQMLDSLGIKYQCYDLLSTMDITDCFIDGNENGELLWDFLTETCNFLTTAPPDLRAEIMKDLQGPEFIVRKEGKILFDNSLSFITIEA | Inactivates histamine by N-methylation. Plays an important role in degrading histamine and in regulating the airway response to histamine. | Q9EST2 |
A9B496 | DNAA_HERA2 | Chromosomal replication initiator protein DnaA | Herpetosiphon | MDTKQIWFTTLGTLQNQILRYDYDTWLKTTALVSVANDLAVIGAPNVTTKQVIEDRFMSVLRRALGEVLGYQVNVRVIISSATPAPSEPVAVTPSEPSPTTEVAEPSFASFNQAAPMLNQLPLGDPNRSSVLNPRYTFSSFIVGTSNRLAHAACMAVAEHPAQAYNPLFLYGGVGLGKTHLLQAIGNYALDRNPEVNVLYVSSEKFTNDLINAIRRQQTEEFRIRYRNIDILLIDDIQFIAGKEGTQEEFFHTFNTLHGAGKQIVLSSDRPPKAILTLEERLRSRFEWGLIVDVQNPDLETRTAILRAKGETLQVPVSSEVIDFLAQRIQSNIRELEGCLNRVIAYANLNRTPVTVEVASAALADLLDTSRRKRVTADDIFREVSQHYGIDQRAIRGRGRSRNVVLPRQVVMYLLREETDASLVEIGELLGGRDHTTVMHGYNKITDDLTSDARLRNDITSLRQRLYGENAR | Plays an important role in the initiation and regulation of chromosomal replication. Binds to the origin of replication; it binds specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'-TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids. | A9B496 |
P51142 | DVL2_XENLA | Xdsh | Xenopus | MAETKVIYHLDEEETPYLVKVPVPATDIRLRDFKAALGRGHAKYFFKAMDQDFGVVKEEISDDNAKLPCFNDRVVSWLASSEGSQPDSAPPAPATEVRPEPPPPVPPPIPPPPAERTSGIGDSRPPSFHPNVSGSTEQLDQDNESVISMRRDRVRRRESSEQAGVGRGVNGRTERHLSGYESSSTLLTSEIETSICDSEEDDTMSRFSSSTEQSSASRLLKRHRRRRKQRPPRLERTSSFSSVTDSTMSLNIITVTLNMEKYNFLGISIVGQSNERGDGGIYIGSIMKGGAVAADGRIEPGDMLLQVNDINFENMSNDDAVRVLRDIVHKPGPIVLTVAKCWDPSPQGYFTLPRNEPIHPIDPAAWVSHSAALSGSFPVYPGSASMSSMTSSTSVTETELSHALPPVSLFSLSVHTDLASVVKVMASPESGLEVRDRMWLKITIPNAFLGSDVVDWLYHHVEGFQDRREARKFASNLLKAGFIRHTVNKITFSEQCYYIFGDLTGCENYMTNLSLNDNDGSSGASDQDTLAPLPLPGASPWPLLPTFSYQYQAPHPYSTQPPAYHELSSYSYGMGSAGSQHSEGSRSSGSNRSDGGRGMQKDDRSGVAGVGGGDSKSGSGSESEYSTRSSIRRVGGGEAGPPSERSTSSRLPPHHPPSVHSYAAPGVPLSYNPMMLMMMPPPPLPPPGVCPPNSSVPPGAPPLVRDLASVPPELTATRQSFHMAMGNPSEFFVDVM | Involved in at least 2 independent signaling cascades, controlling cell fate via canonical Wnt signaling and cell polarity via a planar cell polarity (PCP) cascade. Acts synergistically with dal/dapple-like to activate Wnt signaling, stabilizing ctnnb1/beta-catenin and leading to dorsal axis formation. Also prevents degradation of ctnnb1/beta-catenin by displacing gsk3 from a complex with ARP/Axin-related protein. Has an additional role in anterior-posterior (A/P) axis formation, specifying different neuroectodermal cell fates along the A/P axis in a dose-dependent manner by activating several early patterning genes. In the PCP pathway, required at the cell membrane for PCP-mediated neural and mesodermal convergent extension during gastrulation and subsequent neural tube closure, acting to activate jnk. Also involved in blastopore closure and archenteron elongation during early, but not late, gastrulation. Associates with ephrin receptors and ligands and acts as part of a downstream PCP pathway to mediate ephrin-mediated cell repulsion via activation of rhoa. Required for efnb1/ephrin-B1-driven movement of non-retinal progenitor cells into the retina during eye field formation. Patterns the hindbrain. Required for ciliogenesis. Controls the docking of basal bodies to the apical plasma membrane; mediates the activation, but not localization of rhoa at the apical surface of ciliated cells during basal body docking. Furthermore, required for the association of basal bodies with membrane-bound vesicles and the vesicle-trafficking protein exoc4/sec8, and this association is in turn required for basal body docking. Once basal bodies are docked, required for the planar polarization of basal bodies that underlies ciliary beating and the directional fluid flow across ciliated epithelia. | P51142 |
A6WKM0 | ERPA_SHEB8 | Iron-sulfur cluster insertion protein ErpA | Shewanella | MTDQADTAMPIQFTDAAAAKVKGLLEEEQNPALKLRVYVTGGGCSGFQYGFTFDEKVNDGDFTIEKQGVLLVVDPMSLQYLVGGEVDYTSGLEGSRFFVKNPNATTTCGCGASFSV | Required for insertion of 4Fe-4S clusters for at least IspG. | A6WKM0 |
Q861R7 | KANL2_CAPHI | Non-specific lethal 2 homolog | Capra | MNRIRIHVLPTNRGRITPVPRSQEPLSCSFTHRPCSQPRLEGQEFCIKHILEDKNAPFKQCSYISTKNGKRCPSAAPKPEKKDGVSFCAEHARRNALALHAQMKKTNPGPVGETLLCQLSSYAKTELGSQTPESSRSEASRILDEDSWSDGEQEPITVDQTWRGDPDSEADSIDRDQEDPLKHAGVYTAEEVALIMREKLIRLQSLDIDQVKRLQHLLKEKKRRYLHNRKVEHEALGSSLLTGPEGLLARERENLKRLKCLRRYRQRYGVKALLHRQLKERRMLATDGAAQQAHTTRSSQRCLAFVDDVRCSNQSLPMTRHCLTHICQDTNRVLFKCCQGSEEVPCNKPVPVSLSEDPCCPLHFQLPPQMYKPEQVLSVPDDLEAGPMDLYLSAAELQPTESLPLEFSDDLDVVGDSMQCPPSPLLFDPSLTLEDHPVKEIAEGPVDILGQMQMAGDGCRSQGPRNSEKAPAPLSQSGIATANGKPEPTSVS | As part of the NSL complex it is involved in acetylation of nucleosomal histone H4 on several lysine residues and therefore may be involved in the regulation of transcription. | Q861R7 |
B7KU78 | DNLJ_METC4 | Polydeoxyribonucleotide synthase [NAD(+)] | Methylorubrum | MPSTPLSATVEALSEDAAQARHAELSRAIERANQLYYNEDAPELTDAEYDALRQELEAIEARFPALTGTTEASAGVGAKPSEKFAKVRHAVPMLSLGNAFADEDVDEFVARVRRFLNLPAEEAVAFTAEPKIDGLSLSLRYEAGRLVTAATRGDGEVGENVTANALTVDDIPETLSGEGIPEVLEVRGEIYLSHEDFAAINARQEAAGKPLFANPRNAAAGSLRQLDPAITASRPLRFFAYAWGEVSEPFTDTQSAVLERFRGWGLPVNPRTKLCRSAEEMIAHYRAIEAERAGLGYDIDGVVYKVDDLGFQRRLGFVSRAPRWALAHKFAAQEAITELLAIDINVGRTGSLNPLARLKPVTVGGVVVSNATLHNEGYVQGVGADGEPIREGRDIRVGDTVIVVRAGDVIPKVRDVVIEKRPADAVPYVFPDTCPACGSRAVRELNPRTKKLDAIRRCTGGLICPAQGVERLKHFVSRNGLDLEGFGQTYIEVLFEAGLVKQPADLFRLEFEPLKAAIVARREALSAQRRTEGEPAPKKPTKKKGEEEDKAIKNLLASLDARRTIPLNRFLFALGIPQIGESTAKALAKRFPDMPALMAALAAATREQAGRDWLELSALPRIGPGTRDRLFETLDPLPGEAMQDLSLGARLRGRLTPSQREAVLAHYGSEAEADAALERAASQRPGDAYRLFADDGEIGPVATDSLIQFFSEPHNDAAVRALLEEVGTEPLAATTSAAAFAGKTVVFTGSLEKMTRSEAKATAERLGAKVSGSVSAKTDLVVAGPGAGSKLKDAEKHGVKVVSEDDWLAMLAEA | DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA. | B7KU78 |
A1W445 | HIS3_ACISJ | Phosphoribosyl-AMP cyclohydrolase | unclassified Acidovorax | MDTMNWLDQVKWDAQGLVPVIAQEAATGDVLMFAWMNREALAKTAELGRAVYYSRSRGKLWFKGEESGHVQQVHDIRLDCDSDVVLLKVTQLGHEPGIACHTGRHSCFFNALQNGAWQAVDPVLKDPESIYK | Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP. | A1W445 |
Q0SN27 | RL23_BORAP | 50S ribosomal protein L23 | Borreliella | MKAYDIIVSPMLTEKTNTQRESINVYVFKVNKRANKKEVGAAIKELFNVTPVSCNLLNIKSKAKVVVSRKGYPIGKGKTSSWKKAYVYLKKEDKIDIF | One of the early assembly proteins it binds 23S rRNA. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the ribosome. Forms the main docking site for trigger factor binding to the ribosome. | Q0SN27 |
O52338 | RS3_MYCGA | 30S ribosomal protein S3 | Mycoplasma | MGQKVNSNGLRFGINKNWQSRWVAKTNQQTGDWIVQDEKIRNYLFKKFHSAFISNVDIERTQTSIRVFIYASQPGIILGKEAANIKVILLAINKIVGRHIKVDVDVLEVGNPSLSAKIVARELADAIENRTPLRTAMRQALKRVLKAGAKGIKVLVSGRLNGVEIARDKMYIEGNVTLSTLRTDIDYALEEAQMSYGVIGVKVWINRGEIFGKDFYKKQAHIVKPKGSEANHQRRNSNKSKDYRDNKNKQFNKNHQNQQPAKE | Binds the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation. | O52338 |
Q830Y9 | NADE_ENTFA | NH(3)-dependent NAD(+) synthetase | Enterococcus | MTTLQEKIIQELGVLPTIDPKEEVRKSIDFLKAYLTKHPFLKTFVLGISGGQDSTLAGRLAQLAMTEMREETGDMSYQFIAIRLPYGEQADEADAQAALAFIQPDVSLRVDIKPAVDAMVGSLENAGVQISDFNKGNMKARQRMITQYAVAGENAGAVIGTDHAAENVTAFFTKYGDGGADILPLFRLNKRQGKALLKELGAPEALYLKIPTADLEDDKPLVADEVALGVTYDAIDDYLEGKKVSETDQQTIENWYKKGQHKRHLPITIFDDFWK | Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source. | Q830Y9 |
P53685 | HST1_YEAST | Regulatory protein SIR2 homolog 1 | Saccharomyces | MNILLMQRIVSFILVVSQGRYFHVGELTMTMLKRPQEEESDNNATKKLKTRLTYPCILGKDKVTGKFIFPAITKDDVMNARLFLKDNDLKTFLEYFLPVEVNSIYIYFMIKLLGFDVKDKELFMALNSNITSNKERSSAELSSIHAKAEDEDELTDPLEKKHAVKLIKDLQKAINKVLSTRLRLPNFNTIDHFTATLRNAKKILVLTGAGVSTSLGIPDFRSSEGFYSKIRHLGLEDPQDVFNLDIFLQDPSVFYNIAHMVLPPENMYSPLHSFIKMLQDKGKLLRNYTQNIDNLESYAGIDPDKLVQCHGSFATASCVTCHWQIPGEKIFENIRNLELPLCPYCYQKRKQYFPMSNGNNTVQTNINFNSPILKSYGVLKPDMTFFGEALPSRFHKTIRKDILECDLLICIGTSLKVAPVSEIVNMVPSHVPQILINRDMVTHAEFDLNLLGFCDDVASLVAKKCHWDIPHKKWQDLKKIDYNCTEIDKGTYKIKKQPRKKQQ | NAD-dependent histone deacetylase involved in telomeric silencing. Histone deacetylase proteins act via the formation of large multiprotein complexes that are responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Restores silencing at HMR in SIR2 mutants when overexpressed. Required to repress middle sporulation genes during vegetative growth. Acts as a sensor of NAD(+) levels and regulator of NAD(+) biosynthesis. Regulates the gene expression of de novo NAD(+) biosynthesis genes. | P53685 |
O75578 | ITA10_HUMAN | Integrin alpha-10 | Homo | MELPFVTHLFLPLVFLTGLCSPFNLDEHHPRLFPGPPEAEFGYSVLQHVGGGQRWMLVGAPWDGPSGDRRGDVYRCPVGGAHNAPCAKGHLGDYQLGNSSHPAVNMHLGMSLLETDGDGGFMACAPLWSRACGSSVFSSGICARVDASFQPQGSLAPTAQRCPTYMDVVIVLDGSNSIYPWSEVQTFLRRLVGKLFIDPEQIQVGLVQYGESPVHEWSLGDFRTKEEVVRAAKNLSRREGRETKTAQAIMVACTEGFSQSHGGRPEAARLLVVVTDGESHDGEELPAALKACEAGRVTRYGIAVLGHYLRRQRDPSSFLREIRTIASDPDERFFFNVTDEAALTDIVDALGDRIFGLEGSHAENESSFGLEMSQIGFSTHRLKDGILFGMVGAYDWGGSVLWLEGGHRLFPPRMALEDEFPPALQNHAAYLGYSVSSMLLRGGRRLFLSGAPRFRHRGKVIAFQLKKDGAVRVAQSLQGEQIGSYFGSELCPLDTDRDGTTDVLLVAAPMFLGPQNKETGRVYVYLVGQQSLLTLQGTLQPEPPQDARFGFAMGALPDLNQDGFADVAVGAPLEDGHQGALYLYHGTQSGVRPHPAQRIAAASMPHALSYFGRSVDGRLDLDGDDLVDVAVGAQGAAILLSSRPIVHLTPSLEVTPQAISVVQRDCRRRGQEAVCLTAALCFQVTSRTPGRWDHQFYMRFTASLDEWTAGARAAFDGSGQRLSPRRLRLSVGNVTCEQLHFHVLDTSDYLRPVALTVTFALDNTTKPGPVLNEGSPTSIQKLVPFSKDCGPDNECVTDLVLQVNMDIRGSRKAPFVVRGGRRKVLVSTTLENRKENAYNTSLSLIFSRNLHLASLTPQRESPIKVECAAPSAHARLCSVGHPVFQTGAKVTFLLEFEFSCSSLLSQVFVKLTASSDSLERNGTLQDNTAQTSAYIQYEPHLLFSSESTLHRYEVHPYGTLPVGPGPEFKTTLRVQNLGCYVVSGLIISALLPAVAHGGNYFLSLSQVITNNASCIVQNLTEPPGPPVHPEELQHTNRLNGSNTQCQVVRCHLGQLAKGTEVSVGLLRLVHNEFFRRAKFKSLTVVSTFELGTEEGSVLQLTEASRWSESLLEVVQTRPILISLWILIGSVLGGLLLLALLVFCLWKLGFFAHKKIPEEEKREEKLEQ | Integrin alpha-10/beta-1 is a receptor for collagen. | O75578 |
Q7NGL0 | RF3_GLOVI | Peptide chain release factor 3 | Gloeobacter | MSNPTLAAEVGRRRTFAIISHPDAGKTTLTEKLLLYGGAIDMAGSVRARRNQRHATSDWMAMEQQRGISITSTVLQFVYRDCQINLLDTPGHQDFSEDTYRTLAAADNAAMLIDAAKGIEAQTRKLFDVCRMRGIPIFTFINKLDRPGREPLELLDEIEKVLGIDVYPVNWPIGMGDTFRGVFDRLEHTVHLFDRTTGGKKMAPVTVGAIGDERMRVLMDEGTYAQIVEEIELLDGVGVPFDIERVAQGKLTPVFFGSAANNFGVQLFLDAFIRFASRPGTRSANTGVISPVAEDFSGFVFKIQANMDPQHRDRVAFIRVCSGKFEKDMTVHHTRSGKKVRLSRSLKLFGQERETVEEAYAGDIVGVINPGTFAIGDTICLGKPLAFEGIPLFPPEHFATLRNPNPSKYKQFLKGVTQLREEGAVQVLFHQDEAKRDPILAAVGQLQFDVVRFRLESEYHVETILEPLPWTLARWITAKQLEDLETIDWYFDSLGLKDHEGRLVILFKTPWGFQQMSERNPHLQFHEIAPL | Increases the formation of ribosomal termination complexes and stimulates activities of RF-1 and RF-2. It binds guanine nucleotides and has strong preference for UGA stop codons. It may interact directly with the ribosome. The stimulation of RF-1 and RF-2 is significantly reduced by GTP and GDP, but not by GMP. | Q7NGL0 |
A9MFE4 | CEDA_SALAR | Cell division activator CedA | Salmonella | MMKPLRQQNRQIISYIPRVEPAPPEHAIKMDAFRDVWILRGKYVAFVLMGESFQRSPAFSVPESAQRWANQVRQENEIAD | Activates the cell division inhibited by chromosomal DNA over-replication. | A9MFE4 |
Q6MCT6 | RISB_PARUW | 6,7-dimethyl-8-ribityllumazine synthase | Candidatus Protochlamydia | MKEYKGKLNISKARIGIVISRFNETITKNLLEGSLDELERYGISTQNLPVAWVPGAFEIPLIAKQMALSGEFDAIICLGAIIRGTTPHFDYVASQSAAGILNVSLEINLPVVFGILTTDTVEQAMERSGVKMGNKGREAVQTAIEMIDLTDQLSLLRNHPHSSTANNTSVCK | 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. | Q6MCT6 |
Q00873 | CYT2_YEAST | Cytochrome c1 heme lyase | Saccharomyces | MMSSDQQGKCPVDEETKKLWLREHGNEAHPGATAPGNQLECSANPQDNDKTPEYHTTVDLSQSREVSTIPRTNSDRNWIYPSEKQFYEAMMKKNWDPNSDDMKVVVPLHNSINERVWNYIKSWEDKQGGEACGGIKLTNFKGDSKKLTPRAWFRSRILHLAKPFDRHDWQIDRCGKTVDYVIDFYSTDLNDANSQQQPLIYLDVRPKLNSFEGFRLRFWKSLGF | Lyase that catalyzes the covalent linking of the heme group to the cytochrome C1 apoprotein to produce the mature functional cytochrome. | Q00873 |
A8A4U6 | KBAZ_ECOHS | D-tagatose-1,6-bisphosphate aldolase subunit KbaZ | Escherichia | MKHLTEMVRQHKAGKTNAIYAVCSAHPLVLEAAIRYASANQTPLLIEATSNQVDQFGGYTGMTPADFRGFVCQLADSLNFPQDALILGGDHLGPNRWQNLPAAQAMANADDLIKSYVAAGFKKIHLDCSMSCQDDPIPLTDDIVAERAARLAKVAEETCLEHFGEADLEYVIGTEVPVPGGAHETLSELAVTTPDAARATLEAHRHAFEKQGLNAIWPRIIALVVQPGVEFDHTNVIDYQPAKASALSQMVENYETLIFEAHSTDYQTPQSLRQLVIDHFAILKVGPALTFALREALFSLAAIEEELVPAKVCSGLRQVLEDVMLDRPEYWQSHYHGDGNARRLARGYSYSDRVRYYWPDSQIDDAFAHLVRNLADSPIPLPLISQYLPLQYVKVRSGELQPTPRELIINHIQDILAQYHTACEGQ | Component of the tagatose-1,6-bisphosphate aldolase KbaYZ that is required for full activity and stability of the Y subunit. Could have a chaperone-like function for the proper and stable folding of KbaY. When expressed alone, KbaZ does not show any aldolase activity. | A8A4U6 |
Q8ECV2 | TRPD_SHEON | Anthranilate phosphoribosyltransferase | Shewanella | MSETSIQPLLDILFQGKALTREQTASLFSVLIQGEMNETVMAGMLMALKIRGETIEEISGAADAMRAAAKPFPYPESSRSQGVIDIVGTGGDGFNTINISTTAAFVAAAAGAKVAKHGNRSVSSKSGSSDLLAQFGIDLTMSPELASHCLEALNLCFLFAPHYHGGVKHAVPVRQTLKTRTLFNVLGPLINPARPEFMLLGVYSAELVTPIARVLQALGTQRAMVVHGSGLDEVALHGSTQVAELKDGEIIEYQLTPADFGVPQAHISELEGGEPAHNALITQQILQGHGCDAHTHAVAINAGCALYLCGLSESVKMGTALALSTIKTGKAYELLHKLATVSSQSQE | Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA). | Q8ECV2 |
A0RQM9 | RIMO_CAMFF | Ribosome maturation factor RimO | Campylobacter | MPNLYLVSLGCNKNLVDSEIMLGRLSSYNIVDKPNNADVMIVNTCGFIESAKEESVRTILELASYKKENSVLVVTGCLMQRYRDELMKELPEVDIFTGVGDYASIDEMILKKQNLFSPGVYLQKSDTKRVITGSSYHAYIKIAEGCNQKCSFCAIPTFKGKLKSRDINSIIKEVKELTKDGYSDFSFIAQDTSSFLRDAGINDGLIKLIDEVEKIEAVKSARILYLYPTTASMGLIDKIIASPKFVNYFDMPIQHINDDMLKIMRRGSSKERLKELLTKMRVAPKSFLRTGIIIGHPGETGERFDELCDFLTEFKFDRISAFAYSKEEGTLAYEMEQIPSKTITKRLNTIEKIIKKQIEGSFKSLVGEVIKVQINGSSSEGEMFFGAKSIIWDREIDGEILINDTQIKDPKVGEIYDCKINEFVKDKLIGEIICNS | Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein S12. | A0RQM9 |
Q3KI09 | Y854_PSEPF | Nucleotide-binding protein Pfl01_0854 | Pseudomonas | MRLIIVSGRSGSGKSTALDVLEDNGYYCIDNLPAGLLPELAERALIHTELAQPLVAVSIDARNLPSHLSRFPELLEDVRAKHIQCDVLYLDADEETLLKRFSETRRRHPLSNANRSLAEAIQDESALLGPIADLADLKINTTHLNLYQLRDTIKLRLLNQPEPGTAFLVESFGFKRGMPVDADLVFDVRCLPNPYWKPELRAQSGLDQPVAEYLAAQPEVEEMYQDIYTYLYKWLPRFAASNRAYVTIAIGCTGGHHRSVYLTERLGQALQKTLKNVQVRHRDLS | Displays ATPase and GTPase activities. | Q3KI09 |
Q8J0N2 | SODC_CORMI | Superoxide dismutase [Cu-Zn] | Cordyceps | MVKAVCVLRGDAKVAGTVTFEQESESAPTTITWDITGNDPNAERGFHIHTFGDNTNGCTSAGPHFNPHGKTHGAPTDAARHVGDLGNIKTDGQGNAKGSVQDSHVKLIGPHSVVGRTVVVHGGTDDLGKGGNEESLKTGNAGPRPACGVIGVAN | Destroys radicals which are normally produced within the cells and which are toxic to biological systems. | Q8J0N2 |
B7LN84 | MUKF_ESCF3 | Chromosome partition protein MukF | Escherichia | MSEFSQTVPELVAWARKNDFSISLPVDRLSFLLAVATLNGERLDGEMSEGELVDAFRHVSDAFEQTSETIGVRANNAINDMVRQRLLNRFTSEQAEGNAIYRLTPLGIGITDYYIRQREFSTLRLSMQLSIVAGELKRAADAAEEGGDEFHWHRNVYAPLKYSVAEIFDSIDLTQRLMDEQQQQVKDDIAQLLNKDWRAAISSCELLLSETSGTLRELQDTLEAAGDKLQANLLRIQDATMTHDDLHFVDRLVFDLQSKLDRIISWGQQSIDLWIGYDRHVHKFIRTAIDMDKNRVFAQRLRQSVQTYFDEPWALTYANADRLLDMRDEEMALRDEEVTGELPEDLEYEEFNEIREQLAAIIEEQLAVYKTRQVPLDLGLVVREYLAQYPRARHFDVARIVIDQAVRLGVAQADFTGLPAKWQPINDYGAKVQAHVIDKY | 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. Not required for mini-F plasmid partitioning. Probably acts via its interaction with MukB and MukE. Overexpression results in anucleate cells. It has a calcium binding activity. | B7LN84 |
B4LUA5 | EIF3I_DROVI | TRIP-1 homolog | Drosophila | MLQGHERSITQIKYNREGDLLFSSSKDQKPNVWYSLNGERLGTYDGHQGAVWCLDVDWESRKLITGAGDMTTKIWDVEYGTVIASIPTKSSVRTSNFSFSGNQAAYSTDKAMGQNCELFIIDVRNADSSLSEQEPTLRIPMVESKITSMLWGPLDETIITGHDNGNIAIWDIRKGQKVVDSGTDHTAGINDMQLSKDGTMFVTASRDTTAKLFDSESLMCLKTYKTERPVNSAAISPILDHVVLGGGQDAMEVTTTSTKAGKFDSRFFHLIYEEEFARLKGHFGPINSLAFHPDGKSYASGGEDGFVRVQSFDSTYFENIFE | Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation. | B4LUA5 |
Q39785 | CHI2_GOSHI | Endochitinase 2 | Gossypium | EQCGRQAGGALCPGGLCCSQFGWCGSTADYCTVPGCQSQCSGSGPAPGPGGLTNLISRETFNQMLLHRNDGACPARGFYTYDAFIAAARSFPAFATTGDQATRKREIAAFLAQTSHETTGGAGWAAPDGPYAWGYCYNRELNPPSSYCASDPNYPCAPGKQYFGRGPMQLSWNYNYGQCGRAIGVDLLNNPDLLSSDPTISFKSAFWFWMTPQSPKPSCHNVIIGAWSPSSSDRAAGRATGYGVITNIINGGLECGKGWNAQVEDRIGFYKRYCDILGVSYGNNLDCYNQSPFGNGVSVDSM | Defense against chitin-containing fungal pathogens. | Q39785 |
Q61754 | K1B24_MOUSE | Tissue kallikrein 24 | null | MWFLILFLALSLGGIDAAPPVQSRVVGGFKCEKNSQPWHVAVFRYNKYICGGVLLNPNWVLTAAHCYGNATSQYNVWLGKNKLFQREPSAQHRWVSKSFPHPDYNMSLLNDDIPQPKDKSNDLMLLRLSEPADITDAVKPIDLPTEEPKLGSTCLASGWGSITPTKWQKPNDLQCVFIKLLPNENCTKPYLHKVTDVMLCAGEMGGGKDTCAGDSGGPLICDGILHGITSWGPVPCGKPNAPAIYTKLIKFASWIKDTMAKNP | Glandular kallikreins cleave Met-Lys and Arg-Ser bonds in kininogen to release Lys-bradykinin. | Q61754 |
P57314 | MRAY_BUCAI | UDP-MurNAc-pentapeptide phosphotransferase | Buchnera | MLIFFNKYLHINLNILSYIPYRAIFSLLTSFFINLYIGPYFIYYFKKLQTYQIIRNNGPKTHYSKKNTPTMGGIFIIFSILFSTILYCNLSNIYIWYVISILIGYGLIGFIDDYKKIKYKNSQGLKLKWKYFFLSIIAFIFICMIKINNKDIISTELIIPFCIKNDFEINYLYIFLSYFVLVGTSNAVNLTDGLDGLAIMPVIFLTCGLTLISLFSDNINISHYLHVQYVKNSTELAILCMAIVGSGLGFLWFNSYPAKVFMGDVGSLALGGSLGAIAILLHQELLLIIMGGIFVFETISVILQIISFKIRKKRIFQMAPVHHHYEVKGILEPLIIVRFWIVSLILLLISLISLKVC | 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. | P57314 |
A6RC73 | NOP16_AJECN | Nucleolar protein 16 | unclassified Histoplasma | MGRILQKKKNRSGAPRVKQKSNRLKNGNKKINVLGNAIIAQNWDKKLTLTQNYRRLGLASQLNAPTGGAENKPDDPSNGRQEADSLHLLPSLASVKMIKPAEMRVERDPATGKILRVIHPENETEEVEIAGRKHRRANPLEDPLNEVGDDVLNNTALRIHGSSTSSAVVQALERQAALEEEALKKKQPRQQSKREEEWLERLVAKHGDNIIAMVRDTRLNPMQQTEGDIKRRLKKWREKRGNV | Involved in the biogenesis of the 60S ribosomal subunit. | A6RC73 |
Q9I4P4 | FLGJ_PSEAE | Muramidase FlgJ | Pseudomonas | MDSRLLSGIGAGPDSGSYTDLNRLNQLKVGKDRDGEANIRKVAQEFESLFLNEMLKSMRSANEALGDGNFMNSQTTKQYQDMYDQQLSVSLSKNAGGIGLADVLVRQLSKMKQGSRGNGENPFARVAENGAGRWPSNPSAQAGKALPMPEAGRDDSKLLNQRRLALPGKLAERMLAGIVPSASPAASQMQSLGQDSYLPAQSYPAASRRGFSTDGVDSQGSRRIAQPPLARGKSMFASADEFIATMLPMAQKAAERIGVDARYLVAQAALETGWGKSIIRQQDGGSSHNLFGIKTGSRWDGASARALTTEYEGGKAVKEIAAFRSYSSFEQSFHDYVSFLQGNDRYQNALDSAANPERFMQELQRAGYATDPQYARKVAQIARQMQTYQAVAAAGTPPLG | Flagellum-specific muramidase which hydrolyzes the peptidoglycan layer to assemble the rod structure in the periplasmic space. | Q9I4P4 |
Q1GCM3 | NTPP_RUEST | Nucleotide pyrophosphatase | unclassified Ruegeria | MSTHILLASGSEIRAKLLRQAGVDFRVEVARVDEDAIKTALEADGASPRDIADTLAEAKARKVSGKFPEEMVLGCDQVLDFEGTLLSKPKDKNQALQQLKAMRGKRHMLLSAAVIYCDAKPLWRHVGQVRLVMRMASDAYLESYVERNWESIRHAVGAYKLEEEGVRLFTTIDGSYFNVLGLPMLELMNYLGLQGIIEQ | Nucleoside triphosphate pyrophosphatase. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids. | Q1GCM3 |
A1SMA5 | DNLJ_NOCSJ | Polydeoxyribonucleotide synthase [NAD(+)] | Nocardioides | MKRNGFVPSNSVGRRGIPSNSTSSAIASAGGAVVWTGAGAGRVRARPEQVSVGPGTMSCVTDPREEHRLIAEEIEEARWRYYVLDSPTIDDADFDRRMRRLEALEEEFPELRTPDSPTQTVGGAVSTDFTSHPHLRRMESLDNAFSVEEVEAWYARLRRDGVEDPALLCELKVDGLAINLLYEEGRLVRALTRGDGTTGEDVTSNVKTITSVPHRLTGTDEFPVPALVEVRGEVFLPVEAFERLNESLLEAGKAPFANPRNSAAGSLRQKDPRITASRALGMVCHGIGERRGFEPQAQSHAYDALAAWGLPTSDQVRVVSTLKGVEGYIENAGARRHTIVPYEIDGVVVKVDDVALQRRLGSTSRAPRWAIAFKYPPEEVNAKLLEIRVNVGRTGRVTPYAVMEPTKVAGSTVENATLHNFYEVERKDVRPGGPGDPGDTVILRKAGDVIPEILGPVLALRPEGLQPWVPPTTCPSCGTPLVEQKEGDKDRRCPNHEKCPGQLRERVFFVASRNAFDIEGLGYEAAVALLDAEVIANEGDVFDLDAAALLRAPLFTRAPKKDEDGPQLSANGQRLLDNLDKAKQVPLWRVLVALSIRHVGPKAGRALATEFGSMAAIRAATEEQLAAAEGVGPTIAEAVIEWFKEPWHVEIVDKWERAGVTMADERDESTPRTLAGLTVVVTGSLVDFSRDSAKEAILSRGGKAAGSVSKKTDYVVVGENAGSKADKAEQLGVPVLDEAGFKTLLDGGPAAL | DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA. | A1SMA5 |
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