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 |
|---|---|---|---|---|---|---|
A7MWH3 | RS8_VIBC1 | 30S ribosomal protein S8 | Vibrio | MSMQDPISDMLTRVRNGQAANKVAVKMPSSKLKVAIAALLKAEGYIVDFAVEGEAKPELEVTLKYFQAKPVIEQLKRVSRPGLRVYKKKDQLPSVMGGLGIAIVSTSKGLMSDRAARKAGLGGEIICYVA | 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. | A7MWH3 |
A8GN90 | SYP_RICAH | Prolyl-tRNA synthetase | spotted fever group | MLLSQYFLPVLKEEPSEAQVTSHKLMLRSGMIRQQAAGIYTWLPLGLKVLKNIENIVSLNMNKAGALEVLMPCIQPAHLWMESGRFNNYGKEMLKFQDRHDNTLLFGPTNEDMITDIFRHNIKSYKDLPKNLYHIQWKFRDEIRPRFGVMRGREFLMKDAYSFDINEENAVKTYNQMYKAYINTFRDLGVFAIPVIADNGPIGGKLSHEFHIIAETGESTIYYDKRFKTLKDNPDIDVDEIKSWYAAAEEKHDINKLPISEQEITSSKGIEVGHIFYIGSKYSVNMKALINDEHGKLAPVEMSSYGIGISRLVAAIIEANCDEKGIIWPFSVAPFKVSLINLNIHDSKCVELAAKAYKDLSDKNIEVLYDDTEARPGSKFATHDLIGSPHQIIIGPKKAANNIVELKDRKSGNIEDIEVENLINYIK | Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). | A8GN90 |
A4YSL4 | RS13_BRASO | 30S ribosomal protein S13 | unclassified Bradyrhizobium | MARIAGVNIPTNKRVLIALQYIHGIGPKIAGEIIEKVKIAEDRRVNQLSDQEVLQIREIIDRDYVVEGDLRRETGINIKRLMDLGCYRGLRHRRGLPVRGQRTHTNARTRKGPAKAIAGKKK | Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA. In the 70S ribosome it contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit (bridge B1b), connecting the 2 subunits; these bridges are implicated in subunit movement. Contacts the tRNAs in the A and P-sites. | A4YSL4 |
O66188 | SCNC_THITI | Thiocyanate hydrolase subunit gamma | Thiobacillus | MSADHDHDHDHDHDHKPAPMVEEVSDFEILEMAVRELAIEKGLFSAEDHRVWKDYVHTLGPLPAARLVAKAWLDPEYKKLCIEDGVEASKAVGVNWVTSPPTQFGTPSDYCNLRVLADSPTLKHVVVCTLCSCYPRPILGQSPEWYRSPNYRRRLVRWPRQVLAEFGLQLPSEVQIRVADSNQKTRYIVMPVRPEGTDGWTEDQLAEIVTRDCLIGVAVPKPGITVNAKRPVLKANRPVHHDH | Involved in the degradation of thiocyanate. | O66188 |
Q17Z55 | NUOD_HELAH | NDH-1 subunit D | Helicobacter | MAQNFTKLNPQFENIIFEHDDNQMVLNFGPQHPSSHGQLRLILELEGERIIKATPEIGYLHRGCEKLGENMTYNEYMPTTDRLDYTSSASNNYAYAHAVETLLNLEIPRRAQVIRTILLELNRMISHIFFISVHALDVGAMSVFLYAFKTREHGLDLMEDYCGARLTHNAIRIGGVPLDLPPNWLEGLKKFLGEMRECKKLIQGLLDKNRIWRMRLENVGVVTPKMAQSWGMSGIMLRGTGIAYDIRKEEPYELYRELDFDVPVGNYGDSYDRYCLYMLEIDESIRIIEQLIPMYAKTDTPIMAQNPHYISAPKEDIMTQNYALMQHFVLVAQGMRPPIGEVYAPTESPKGELGFFIHSEGESYPHRLKIRAPSFYHIGSLGDILVGQYLADAVTVIGSTNAVFGEVDR | 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. | Q17Z55 |
Q8PC63 | KPRS_XANCP | Phosphoribosyl pyrophosphate synthase | Xanthomonas | MQDQRNLLVFSGNANKPLAQSICKELGVRMGKALVTRFSDGEVQVEIEESVRRQEVFVIQPTCAPSAENLMELLVLIDALKRASAASVTAVIPYFGYSRQDRRMRSSRVPITAKVAAKMICAMEADRVLTVDLHADQIQGFFDVPIDNVYASPLLLADIWRAYGTDNLIVVSPDVGGVVRARAVAKRLDDADLAIIDKRRPRANVATVMNIIGDVQGKTCVLVDDLVDTAGTLCAAAAALKQRGALKVVAYITHPVLSGPAVDNINNSQLDELVVTDTIPLSAAARTCPKIRQLSVAELLAETIHRIAFGESVSSLYVD | Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib-5-P). | Q8PC63 |
A8FEH6 | PANC_BACP2 | Pantoate-activating enzyme | Bacillus | MNVVTHIHELKELIKQHQEKQHSIGFVPTMGFLHEGHLTLAKEARDQNDLVVMSIFVNPLQFGPNEDFESYPRDMERDQRLAKEAGVDILFTPDVKEMYANEPSITMTVRKRTDVLCGKKRPGHFDGVVTVLTKLFHLVAPTNAYFGLKDAQQVAVIDAMIKDFFFDLHLVSVPTVREEDGLAKSSRNVYLSDKERQEAPALYRALKKGQSAIENGERDVSRIYQLVEEDILQTSGEIDYIEIYSYPELEPLQQLAGQVIIAIAVKFSRARLIDNVIFHVPESGEKHV | Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. | A8FEH6 |
A1RXN7 | FAU1_THEPD | RNA-binding protein FAU-1 | Thermofilum | MIRVRGIHSTAIAGLLDEAGFRFADLSQELLARIPQLRVEERVLVTVKDTDDRSGVVVLGDRAVVEKVAYLLRAVIPGALVSYVGEGPYTTYAVRLLSRVEGDVYEAEYSPGKRTTVKLRRPHVEGEVIMAHVIRASPEAPLLKEGVAITGSLVRLVQFDRHSVSEHIRDENLRLQLLTLAMTSAPTGWGVHFRSASKRASIVDVMAEIKALSEKAEKILKEVAPKEPGVVVPGEAIAIVEIPADASIRMDALRSRYYPTLPLHHLLKRLGDDELSRAVDFSERLLAGCEKCLSSTGAIEVFLERLSSLKGRQVSVLHRKVAGAGHVWSAEVESVKRMTVVLKRVVSSPGLYDGFEGLKREPGDVIRSYTWLFGRAVVHFYTSARGELKGVYVNINAPVFFAGNANTLGYVDLGVDVTRAADEEPKVVDLAEFLDLVERGVLDKQLAGSYLEFAESVKHLLEKDIGEDLPARIMQAQKSIFSFETDKLLAV | Probable RNase involved in rRNA stability through maturation and/or degradation of precursor rRNAs. Binds to RNA in loop regions with AU-rich sequences. | A1RXN7 |
A1VBA3 | SYE_DESVV | Glutamyl-tRNA synthetase | Desulfovibrio | MSNVVTRFAPSPTGHLHIGGARTAIFNWLLARHFGGRFVLRIEDTDTERSKQEYTDSILASMKWLGLDWDGDLIYQSERFDIYNSYIDRLLESGHAYWCECPPDEVEKMREEARAKGLKPRYNGRCRSRDLGPGDGRVVRLKAPAEGRIVFDDLVKGTVAFDVAELDDMVLRRSDGAPTYNLAVVVDDATMGVTHVLRGDDHLSNTPKQILLYQALGFDLPRFGHVPMILGPDRKKLSKRHGAKAVIEYEQYGLLPQALVNYLVRLGWSHGDQEIFALEELVEKFGTENLNSSAAGFDPDKLEWLNGHYLRETSPEELARLVLPFVAAEGFDVDASRLAQLVPLFRERANNLVELARVMRFMLVPAAEVEYDAAAVAKALTEEGRRHVAGVREALAVLGIFDREGCEKAIHDYVEGNGLKFKQVAPAVRVAVVGAMGGPGLPDMMALLGRDDVLARLDRAVAL | 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). | A1VBA3 |
P80685 | CUG1A_TENMO | TM-PCP G1A | Tenebrio | GLLGAPAVATYAAAPAVAYSAAPAVSTAYINQAAPVLAHAGPVAVAHAAPYAVHAPAVGASHQAIVRSLGGNQAVSHYSKAVDSAFSSVRKFDTRITNDALLHAPVAVAHAAPVVSTYAAHAPVVSSYAHAPLVSSYAAHAPLVSSYAAHAPLVSSYAAHAPVLSTAYAAHAPVVSSYAAPVVARTAAVGYSPAAVVSHTSFTGLGASYAW | Component of the cuticle of the pupa of Tenebrio molitor. | P80685 |
A6TWH6 | RS3_ALKMQ | 30S ribosomal protein S3 | Alkaliphilus | MGQKVNPHGLRVGVIKDWDAKWYANKRDFSDYLIEDHSIRKFVKKKLFLSGINKIETERAANNRVKINVHTAKPGMVIGKGGIGVEELRKELEKMTKKTVIVNVVEVKRPEVESQLVAENIAFSLERRVSFRRAMKQAMQRAMRAGAKGIKVSTAGRLGGADMARTEGYSEGNVPLHTLRADIDYGFAEADTTYGKLGIKVWIYKGEILPTKGKNEETNNETADNSRGRRREAK | Binds the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation. | A6TWH6 |
Q1MPQ6 | RL16_LAWIP | 50S ribosomal protein L16 | Lawsonia | MLAPKKVKFRKWQKGRLRGPALRGISIAYGDIALKSTEHGKLTSQQIEAARIAMMRHIKRGGKVWIRVFPDHPITAKPLETRQGSGKGSPVGWCAPVKPGRILYEIKGVNIDLAREALIRAAHKLPVKTVIVLKERL | Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs. | Q1MPQ6 |
A8ZZT5 | MNTP_DESOH | Putative manganese efflux pump MntP | Desulfosudis | MNTLTIFGIAVALAMDAFAVSIAAGVFLRSIGLRHYFRLAWHFGLFQALMPIVGWYAGLSVRGLIERYDHWIAFFLLAFVSFNMIRESFDAGENHTKADPTRGLRLVLLSIATSIDALAVGLSLSVLNVSVWMPATVIGITAAVFTVGGLMMGSRAGDIPWLRRYADRVGAGVLLFIGLRILYAHGVFY | Probably functions as a manganese efflux pump. | A8ZZT5 |
Q1GB17 | POTA_LACDA | Spermidine/putrescine import ATP-binding protein PotA | Lactobacillus | MEIIKLDHITKQYDDGFVALKDINLELESGKFYSLLGPSGSGKTTILRIIAGFTEASAGKVYFDGQDITNLDASKRHINTVFQNYALFPHLNVYENVAFALKLRQRPESEIREKVKDALHTVRLDGYANREISELSGGQQQRVAIARAIINEPKVLLLDECLSALDKRLRKEMQFELRAIQKKLGITFIFVTHDQEEALAMSDEIFVLNDGEIKQSGSPVDIYDEPVNDFVARFIGDSNILSGRMIRDFAVEFAGKDFECADAGITPGEKVEVVLRPEDLDITAPAAGKLLVTVQSQLFLGDHFEIKAIGQDGFEWLIHSTNGVQIGQEVGIFFDPEDIHVMRLGETEEEFDARLETYEGED | Part of the ABC transporter complex PotABCD involved in spermidine/putrescine import. Responsible for energy coupling to the transport system. | Q1GB17 |
B7KL53 | PYRF_GLOC7 | OMP decarboxylase | Gloeothece citriformis | MINDRVIVPLDVPTLEEAIALLDLLPRVSFWKVGLELFVSAGPSILEILKEREKRIFLDLKFHDIPNTVAGACRSATKYGVDLLTLHATAGRKALSQAVEAISTGDKPPKLLAISLLTSINSRELAFDLKIPLELPEYALQMALLAQETGIDGAVCSPQEVSQLRQVCGSDFLLVCPGVRPTWAEAGDQRRVMTPVSAIKAGADYLVIGRPITTASNPVEAWEKVCQELAEV | Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP). | B7KL53 |
E5A7T3 | PEPA_LEPMJ | Aspartic protease pepA | Leptosphaeria maculans species complex | MPSIVSLTAALTFVGAVIASPVEKRSAFSVEQVPHTTYLKNGPAQKVKTLRKYGKPVPQSLLDAAESRDAVGETFTASAVGDGSDPAVPSDQYDSSYLSPVTVGSTTVELDFDTGSADLWVFSSLQASSQLSGHQYYQADASKLKSGYSWKISYGDGSGASGKVYADKVVVGGVTATSQAVEAATSVSAQFSRDSNTDGLLGLAFSSINTVSPEPQKTFFDTVKPQLAEPLFAVNLKYHAAGTYDFGYIDKSKYTGPITYVNVDDSQGFWGISATAYGVGGTTTQRAISGILDTGTTLVYTDTAIVKAYYAKVSGAKLDNIQGGYVFPCSATLPNFSITVGGVAQVVPGKHINYSPVDSSGTTCFGGIQTNDGLGMSIFGDIFLKSKYVVHEAAPDSPPRIGLAQSASV | Secreted aspartic endopeptidase that allows assimilation of proteinaceous substrates. The scissile peptide bond is attacked by a nucleophilic water molecule activated by two aspartic residues in the active site. Shows a broad primary substrate specificity. Favors hydrophobic residues at the P1 and P1' positions. | E5A7T3 |
C3PKL1 | MENG_CORA7 | Demethylmenaquinone methyltransferase | Corynebacterium | MSKADLEKKPFDVARMFDAVGKKYDITNTVLSFGQDARWRRLTRERLNPQPGEKVLDLAAGTAVSTEELSKSGAWCVACDFSLGMLAAGAERDVPKVAGDGMRLPFADNTFDAVTISYGLRNIHDFELGLREMARVTKPGGRLAVAEFSKPVIPVFGTVYKEYLTRLLPPIAKVVSSNPEAYIYLAESIRAWPEQHELAAAINRNGWEQAGWRNLTFGIVALHSAVKPA | Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2). | C3PKL1 |
A7FQI8 | METK_CLOB1 | Methionine adenosyltransferase | Clostridium | MRKLFTSESVTEGHPDKICDQISDAVLDAILDKDPNGRVACETAVTTGMVMVMGEISTKCYVDIPKLVRETIRGIGYDRAKYGFDCETCSVITSIDEQSVDIAMGVDEALESKKGEMDKLDAVGAGDQGMMFGFATNETKEYMPMPIEMAHKLSRRLSEVRKNGTLPYLRPDGKTQVTVEYENGKPVRIDAIVISTQHGPEVYLEQIEKDIKEHVIKVIVPSELLDENTKYFINPTGRFVVGGPQGDSGLTGRKIIVDTYGGYGRHGGGAFSGKDPTKVDRSAAYAARWVAKNLVAAGVADKLEIQLAYAIGVAKPVSISVDTFGTGKMTDEEIVSIVNKVFDLRPGAIIRDLDLRRPIYKQVAAYGHFGRTDIDVPWERLDKVEEIKKHI | Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. | A7FQI8 |
P96744 | TPIS_CHLAA | Triose-phosphate isomerase | Chloroflexus | MRIPLIAGNWKMYKTVGEATTLVRDLLAGLGELSDREAIVCPPFTALAAVAALVADSPLGLGAQNLYPEAQGAFTGEVSPPMLVDIGCRYVIIGHSERRQYFGESDAFVNRKLRAALAHGLRPIVCVGESKPQRDAGQAEPIVTAQVRAALLEVPPDQMANVVIAYEPIWAIGTGDTATPADAQAMHAAIRATLAELYGSEIAATVRIQYGGSVKPDNIDELMAQPDIDGALVGGASLQAASFLRIIHYQ | Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P). | P96744 |
Q8VYB5 | AMSH1_ARATH | Deubiquitinating enzyme AMSH1 | Arabidopsis | MGSSFETIDIATSARRIGVDNRISLKFYFRIADNILKQANIFRAEKNVIDLYVMLLRFSSLALETIPSHRDYRTSLKSNKEYLRMRLLDVLTELEKLKPVVQQRIDELYPKLKPRYNVQAHPANGSLGWSSAVKPSFNSYDHAKVRNPPGHNSGYMGSRGQQFLNAAPLEERFRKMSVNFRPNEETLSKHSILGPGGLSAQWQPPKYDTKVQYPSNIDFSPVVIPSFQQLVDSKPMITNGSNDEPEKPIVEPSVASNEKIQKNYTEELSSMISFEEPESVNENNLIRQPSPPPVLAEVQDLVPALCPEVREPECMIENSLPDESLRSESPLELHIATSMMDTFMRLAKSNTKKNLETCGILAGSLKNRKFYITALIIPKQESTSDSCQATNEEEIFEVQDKQSLFPLGWIHTHPTQSCFMSSIDVHTHYSYQIMLPEAVAIVMAPQDSSRNHGIFRLTTPGGMTVIRNCDRRGFHAHSSPEDGGPIYNTCKEVYMNPNLKFDVIDLR | Zinc metalloprotease that cleaves 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. | Q8VYB5 |
P19439 | GLRK_CHICK | Kainate-binding protein | Gallus | MDKGLHFIFCVVTAVLLLRESSQTGAMRNDDAMIKPNDLRGPEENLPSLTVTTILEDPYVMVRSAELEGYCIDLLKALASMLHFSYKVKVVGDGKYGAISPSGNWTGMIGEILRQEADIAVAPLTVTSAREEVVSFTTPFLQTGIGILLRKETISQEMSFFHFLAPFSKETWTGLLFAYVLTCVCLFLVARLSPCEWNEPKNEENHFTFLNSLWFGAGALTLQGVTPRPKAFSVRVIAAIWWLFTIALLAAYIANFTALLSSGSEQLSIQTFEDLVKQRKLEFGTLDGSSTFYFFKNSKNPIHRMVYEYMDKRRDHVLVKTYQEAVQRVMESNYAFIGESISQDLAAARHCNLIRAPEVIGARGFGIATAQASPWTKKLSVAVLKLRETGDLDYLRNKWWESSCLHKSREGWSPLQPQALGGLFLTLAIGLALGVIAAMVELSNKSRHAAGHIKKSCCSIFTEEMCTRLRIKENTRQTQETSGRANA | Receptor for glutamate. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. The postsynaptic actions of Glu are mediated by a variety of receptors that are named according to their selective agonists. | P19439 |
Q72JK8 | SPEBH_THET2 | Protein SpeB homolog | Thermus | MRLVFGEKDAPYEEARVVVLPVPYDLSLSFLPGARRGPEAILLASRELEPFLLELGAAPEEVGIHAAEPVPWVAGMAEESHRLIREEALKHLRAGKWLVALGGDHSVTHPLVQAHREALGEFSLLHVDAHADLYPEWQGSVYSHASPFYRLLTEGFPLVQVGIRAMDRDSLRLARKRGVALFPAHRIHREGLPLDEILEALGKRVYISLDFDALDPSLMPSVGTPLPGGLSYRQVVDLLEAVFREKEVVGMDFVELSPNGQFHAEMTAAQLVYHAIGLKGLQAGWLSREVDHI | Involved in the biosynthesis of polyamines which are thought to support the growth of thermophilic microorganisms under high-temperature conditions. It seems that long-chain and branched-chain of polyamines effectively stabilize DNA and RNA, respectively. Catalyzes the decarboxylation of N1-(3-aminopropyl)agmatine to yield spermidine and urea. Does not act on agmatine. | Q72JK8 |
Q5HBH7 | RS15_EHRRW | 30S ribosomal protein S15 | Ehrlichia | MSVTPERKSELISEYCLKKGDTGSSFVQCAILSERIRNLTEHLKIHKKDFHCRRGLMVLVCRRRNELQYIRRKYGNDRYLALVKQLGIRDVFH | Forms an intersubunit bridge (bridge B4) with the 23S rRNA of the 50S subunit in the ribosome. | Q5HBH7 |
Q36368 | CYB_ERIEU | Ubiquinol-cytochrome-c reductase complex cytochrome b subunit | Erinaceus | MMNMRKTHPLMKIINNSFIDLPTPSNISSWWNFGSLLGLCLITQIITGLFLAMHYTSDTLTAFSSITHICRDVNYGWLIRYTHANGASMFFMCLFLHIGRGLYYGSYLFYETWNIGIILLIITMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTDLVQWIWGSFSVDKATLTRFFAFHFIFPFIIVAMVMIHLLFLHEAGSNNPTGITSESDKISFHPYYTLKDMLGMMFMFLILMSLVLFYPDLLGDPDNYTPANPLSTPPHIKPEWYFLFAYAILRSIPNKLGGVLALFMSILILFLLPYLHTSKHRSMVFRPVSQCIFWLLVSDLLILTWIGSQPVENPFITIGQLASIYYFLSILILIPLAGLIENYMFKW | Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis. | Q36368 |
Q15YN2 | RL16_PSEA6 | 50S ribosomal protein L16 | Pseudoalteromonas | MLQPKRMKFRKMHKGRNRGYAAGDSVSFGTFGLKSVGRGRMTARQIEAARRAMTRAVKRQGKIWIRVFPDKPITEKPLEVRQGKGKGNVEYWVCQIQPGRVLYEMEGVPESVAREAFELAASKLPFKTTFVTRTVM | Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs. | Q15YN2 |
E1WAB5 | ORGA_SALTS | Oxygen-regulated invasion protein OrgA | Salmonella | MIRRNRQMNRQPLPIIWQRIIFDPLSYIHPQRLQIAPEMIVRPAARAAANELILAAWRLKNGEKECIQNSLTQLWLRQWRRLPQVAYLLGCHKLRADLARQGALLGLPDWAQAFLAMHQGTSLSVCNKAPNHRFLLSVGYAQLNALNEFLPESLAQRFPLLFPPFIEEALKQDAVEMSILLLALQYAQKYPNTVPAFAC | Oxygen-regulated protein required for bacterial internalization. | E1WAB5 |
Q9VXX8 | RL371_DROME | Probable 60S ribosomal protein L37-A | Sophophora | MTKGTSSFGKRHNKTHTLCRRCGRSSYHIQKSTCAQCGYPAAKLRSYNWSVKAKRRKTTGTGRMQHLKVVRRRFRNGFREGTQAKPKKAVASK | Binds to the 23S rRNA. | Q9VXX8 |
Q8DEL1 | MURC_VIBVU | UDP-N-acetylmuramoyl-L-alanine synthetase | Vibrio | MTIQHKQDLAQIRAMVPEMRRVKSIHFIGIGGAGMSGIAEVLLNEGYQITGSDIAENAVTERLAQKGAKVYIGHQATNVAEASVVVVSTAINEANPEVKAAREARIPVVRRAEMLAELMRFRHGIAVAGTHGKTTTTALVTQIYSEAGLDPTFVNGGLVKSAGTNARLGSSRILIAEADESDASFLHLQPMVCIVTNIEADHMDTYGGDFETLKQTFIDFLHNLPFYGQAIVCIDDPVIRELIPRISRQVITYGFSEDADVRIENYRQEGQQGKFTVVRKDCEALDITLNIPGRHNALNAAAAIAVATEDEIGDDAILAAMVGTQGTGRRFEHLGEFETGNGNVMLVDDYGHHPTEVDVTIQAARNGWQEKRLVMIFQPHRYSRTRDLYDDFANVLEQVDVLVMLDVYAAGEKAIAGADSRSLCRTIRSRGKIDPIFVADTQQLPEVLANILQEGDLLLAQGAGDIGKVARQLAALELNISNMKAK | Cell wall formation. | Q8DEL1 |
A7H773 | DAPA_ANADF | 4-hydroxy-tetrahydrodipicolinate synthase | unclassified Anaeromyxobacter | MPRLEGSMVAIVTPMKDGAVDLRALRELTEWQIAEGTDGIVPCGTTGEGATLTAAERAEVIRAVVEVARGRALVVAGAGSNATHEAIEGVKAAKALGADAALVVTPYYNKPTPEGLYRHYTAIWEATRFPVVAYNVPGRTAVDMGPDTVARLAKAGAIVGIKEATASMDRQVQLVERIGKDAIAYLSGDDFTVVPYIACGGHGVISVISNIAPRAMKDLVVAARLGDFARALDLQVRMAELNRVMFVETSPGPVKAAVALLGRAGPELRLPLAPVSEASLSKVREAMTRFGLKLA | Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA). | A7H773 |
Q8VFK2 | O1002_MOUSE | Olfactory receptor 175-2 | Mus | MMHRNQTVVTEFFFTGLTSSFHLQIVLFLTFLCVYLATLLGNLGMIILIHQDTRLHIPMYFFLSHLSFVDACSSSVISPKMLSDIFVDKKVISFLGCAIQFCLFSQFVVTECFLLASMAYDRYVAICKPLLYTLIMSQRVCVQLVIGPYSIGLISTVVHTTSAFILPYCGPNLINHFFCDLLPVLSLACADTQMNKHLLFIMAGILGVFSGIIILVSYVYIAITILKINSADGRRKAFSTCSSHLTAVSILYGTLFFIYVRPSSSFSLDINKVVSLFYTAVIPMLNPFIYSLRNKEVKDALIRTFEKKFCYSLQDKIL | Potential odorant receptor. | Q8VFK2 |
A4FM22 | PNP_SACEN | Polynucleotide phosphorylase | Saccharopolyspora | MTDVQSLDEGVYEATAVLDNGAFGTRTVRFETGRLAKQAAGSVVAYLDDDTMLLSATTASKQPKEHFDFFPLTVDVEERMYAAGRIPGSFFRREGRPSTDAILTCRLIDRPLRPSFVDGLRNEVQVVVTVMSLDPQDPYDVLAINGASASTQLSGLPFSGPVGGTRMALIDGQWVAFPTYEQLERAVFDMVVAGRIVGDDVAIMMVEAEATEKTAGLVSAGAQAPTEEVVAAGLEAAKPFIRTLCQAQQQLAQAAGKATEEFPVFPAYADDAFTAVEQAASAELAEALKIASKQERENRLDEIKAAVLEKVGTGEGEQFEGREKEVGAAFRSLTKKLVRQRIIRDQVRIDGRGLTDIRSLSAEVGVIPRAHGSALFERGETQILGVSTLNMLRLEQTIDSLSPETTKRYMHHYNFPPYSTGETGRVGSPKRREIGHGALAERALIPVLPTREEFPYALRQVSEALGSNGSTSMGSVCASTLSLLNAGVPLKAPVAGIAMGLVSDEIDGKTHYVALTDILGAEDAFGDMDFKVAGTKEFVTALQLDTKLDGIPSEVLAQALGQARDARFTILEVMAEAIGKPDEMSPHAPRVTSISIPVDKIGEVIGPKGKMINSITEETGAEITIEDDGTIYVGAADGPSAEAAIDKINAIANPQLPKVGERFLGTVVKTAAFGAFVSLLPGKDGLVHISKLGNGKRIGKVEDVVNVGDKLRVEIADIDSRGKISLVVVDDEAENADKGGESEETSEQGA | Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction. | A4FM22 |
Q42093 | AB2C_ARATH | Multidrug resistance-associated protein 2 | Arabidopsis | MGFEFIEWYCKPVPNGVWTKQVANAFGAYTPCATDSFVLGISQLVLLVLCLYRIWLALKDHKVERFCLRSRLYNYFLALLAAYATAEPLFRLIMGISVLDFDGPGLPPFEAFGLGVKAFAWGAVMVMILMETKIYIRELRWYVRFAVIYALVGDMVLLNLVLSVKEYYSSYVLYLYTSEVGAQVLFGILLFMHLPNLDTYPGYMPVRSETVDDYEYEEISDGQQICPEKHANIFDKIFFSWMNPLMTLGSKRPLTEKDVWYLDTWDQTETLFTSFQHSWDKELQKPQPWLLRALNNSLGGRFWWGGFWKIGNDCSQFVGPLLLNQLLKSMQEDAPAWMGYIYAFSIFVGVVFGVLCEAQYFQNVMRVGYRLRSALIAAVFRKSLRLTNEGRRKFQTGKITNLMTTDAESLQQICQSLHTMWSAPFRIIIALILLYQQLGVASLIGALLLVLMFPLQTVIISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDELSWFRKSQLLGALNMFILNSIPVLVTIVSFGVFTLLGGDLTPARAFTSLSLFAVLRFPLFMLPNIITQVVNANVSLKRLEEVLATEERILLPNPPIEPGEPAISIRNGYFSWDSKGDRPTLSNINLDVPLGSLVAVVGSTGEGKTSLISAILGELPATSDAIVTLRGSVAYVPQVSWIFNATVRDNILFGSPFDREKYERAIDVTSLKHDLELLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGQQVFEKCIKRELGQKTRVLVTNQLHFLSQVDRIVLVHEGTVKEEGTYEELSSNGPLFQRLMENAGKVEEYSEENGEAEADQTAEQPVANGNTNGLQMDGSDDKKSKEGNKKGGKSVLIKQEERETGVVSWRVLKRYQDALGGAWVVMMLLLCYVLTEVFRVTSSTWLSEWTDAGTPKSHGPLFYNLIYALLSFGQVLVTLTNSYWLIMSSLYAAKKLHDNMLHSILRAPMSFFHTNPLGRIINRFAKDLGDIDRTVAVFVNMFMGQVSQLLSTVVLIGIVSTLSLWAIMPLLVLFYGAYLYYQNTAREVKRMDSISRSPVYAQFGEALNGLSTIRAYKAYDRMADINGRSMDNNIRFTLVNMGANRWLGIRLETLGGLMIWLTASFAVMQNGRAENQQAFASTMGLLLSYALNITSLLTGVLRLASLAENSLNAVERVGNYIEIPPEAPPVIENNRPPPGWPSSGSIKFEDVVLRYRPQLPPVLHGVSFFIHPTDKVGIVGRTGAGKSSLLNALFRIVEVEKGRILIDDCDVGKFGLMDLRKVLGIIPQSPVLFSGTVRFNLDPFGEHNDADLWESLERAHLKDTIRRNPLGLDAEVSEAGENFSVGQRQLLSLSRALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDKILVLDSGRVQEFSSPENLLSNEGSSFSKMVQSTGAANAEYLRSLVLDNKRAKDDSHHLQGQRKWLASSRWAAAAQFALAASLTSSHNDLQSLEIEDDSSILKRTNDAVVTLRSVLEGKHDKEIAESLEEHNISREGWLSSLYRMVEGLAVMSRLARNRMQQPDYNFEGNTFDWDNVEM | Pump for glutathione S-conjugates. Mediates the transport of S-conjugates such as GSH, S-(2,4-dinitrophenyl)-glutathione (DNP-GS), GSSG, cyanidin 3-glucoside-GS (C3G-GS) and metolachlor-GS (MOC-GS), glucuronides such as 17-beta-estradiol 17-(beta-D-glucuronide) (E(2)17betaG), and of the chlorophyll catabolite such as B.napus nonfluorescent chlorophyll catabolite (Bn-NCC-1). | Q42093 |
Q56108 | NRDH_SALTY | Glutaredoxin-like protein NrdH | Salmonella | MSITIYTRNNCVQCHATKRAMESRGFEFEMVNVDLVPDAADTLRAQGFRQLPVVMAGDLSWSGFRPDMINRLHPTPHAANA | Electron transport system for the ribonucleotide reductase system NrdEF. | Q56108 |
O05779 | FTSE_MYCTU | Cell division ATP-binding protein FtsE | Mycobacterium tuberculosis complex | MMITLDHVTKQYKSSARPALDDINVKIDKGEFVFLIGPSGSGKSTFMRLLLAAETPTSGDVRVSKFHVNKLRGRHVPKLRQVIGCVFQDFRLLQQKTVYDNVAFALEVIGKRTDAINRVVPEVLETVGLSGKANRLPDELSGGEQQRVAIARAFVNRPLVLLADEPTGNLDPETSRDIMDLLERINRTGTTVLMATHDHHIVDSMRQRVVELSLGRLVRDEQRGVYGMDR | Part of the ABC transporter FtsEX involved in cellular division. Has ATPase activity. | O05779 |
A4Y1B7 | PEPQ_SHEPC | Proline dipeptidase | Shewanella | MDQLAHHYRAHIAELNRRVAEILSREALSGLVIHSGQPHRMFLDDINYPFKANPHFKAWLPVLDNPNCWLVVNGRDKPQLIFYRPVDFWHKVSDVPDMFWTEHFDIKLLTKADKVAELLPKDTVNWAYLGEHLDVAEVLGFTSRNPDAVMSYLHYHRTTKTEYELECMRRANQIAVQGHLAAKNAFYNGASEFEIQQHYLSAVGQSENEVPYGNIIALNQNAAILHYTALEHQSPAKRLSFLIDAGASYFGYASDITRTYAFEKNRFDELIAAMNKAQLELIDMMRPGVRYPDLHLATHAKVAQMLLDFDLATGDAQGLVDQGITSAFFPHGLGHMLGLQVHDVGGFSHDERGTHIAAPEAHPFLRCTRILAPNQVLTMEPGLYIIDTLLNELKQDSRGLQINWQTVDELRPFGGIRIEDNVIVHQDRNENMTRELGLAD | Splits dipeptides with a prolyl residue in the C-terminal position. | A4Y1B7 |
P23126 | SM25_SCHMA | Antigen Sm25 | Schistosoma | MFSFHERMKKKHVTIRVYKHERILVFLFVLFISTTDFSTEIIMIQTINWIVWKLFIIYISLDLFSLKLVNSEENSNSIITDEDYDHYNSSLDSSNNVKHSQEAFHRNSDPDGFPEYEFLNETSIEIKEELGQELHQLQLILDELSRRIRATPNSANKYMKNEFLMSSCIVITLNLFIFMYKS | Major antigen in the surface tegument. | P23126 |
P55884 | EIF3B_HUMAN | eIF3 p116 | Homo | MQDAENVAVPEAAEERAEPGQQQPAAEPPPAEGLLRPAGPGAPEAAGTEASSEEVGIAEAGPESEVRTEPAAEAEAASGPSESPSPPAAEELPGSHAEPPVPAQGEAPGEQARDERSDSRAQAVSEDAGGNEGRAAEAEPRALENGDADEPSFSDPEDFVDDVSEEELLGDVLKDRPQEADGIDSVIVVDNVPQVGPDRLEKLKNVIHKIFSKFGKITNDFYPEEDGKTKGYIFLEYASPAHAVDAVKNADGYKLDKQHTFRVNLFTDFDKYMTISDEWDIPEKQPFKDLGNLRYWLEEAECRDQYSVIFESGDRTSIFWNDVKDPVSIEERARWTETYVRWSPKGTYLATFHQRGIALWGGEKFKQIQRFSHQGVQLIDFSPCERYLVTFSPLMDTQDDPQAIIIWDILTGHKKRGFHCESSAHWPIFKWSHDGKFFARMTLDTLSIYETPSMGLLDKKSLKISGIKDFSWSPGGNIIAFWVPEDKDIPARVTLMQLPTRQEIRVRNLFNVVDCKLHWQKNGDYLCVKVDRTPKGTQGVVTNFEIFRMREKQVPVDVVEMKETIIAFAWEPNGSKFAVLHGEAPRISVSFYHVKNNGKIELIKMFDKQQANTIFWSPQGQFVVLAGLRSMNGALAFVDTSDCTVMNIAEHYMASDVEWDPTGRYVVTSVSWWSHKVDNAYWLWTFQGRLLQKNNKDRFCQLLWRPRPPTLLSQEQIKQIKKDLKKYSKIFEQKDRLSQSKASKELVERRRTMMEDFRKYRKMAQELYMEQKNERLELRGGVDTDELDSNVDDWEEETIEFFVTEEIIPLGNQE | (Microbial infection) In case of FCV infection, plays a role in the ribosomal termination-reinitiation event leading to the translation of VP2 . | P55884 |
Q57616 | ACDB1_METJA | ACDS complex acyltransferase 1 | Methanocaldococcus | MKIRLYGETMVVGNIIEGGKTVLNLTKEILEKEDENLKVSYPGTNYNLPIIYGLLGKKIETVKDLKELINSLEIKDEETLENALDAGVVTLICAEAIEALKYAKSEKPYKEPYVGFIPDEILRGLGVPLVEGKIPAILVVIGKVGDKEKLKKLIDDIKKRNILALLVGDIVKEMDEADIEYGLDKLLVPVGNEITSAIHAANLAIRAPLIFGGIEPGKTEEIIDYLKNRVPAVVVALGELDNITLAAGAGCIKAGVPVITNNEVPVIKGALESSDIDNIVENALKMKGVKVKVVEFDIPVSVGPMNEGERVRGPDMYVELAGPKSYGFELVKVVNKAEDKVEIIGKDIDEMEEGSRNPFAIIVEVSGSNLEEDLEGVLERRIHEFLNYIEGVMHLNQRDQVWIRINKNSFNKGLRLKHIGEVVKQLFKEHFPIVEKCNVIIITDPDKVKEELEKAKEIYKKRDEKTKSIREEDVDVFYGCVMCQSFAPTHVCIITPDRPSLCGSINYLDARAAAKIDPNGPIFEIPKGECLDEKLGIYTGVNEVVRERSQGSVEEMALHSALTNPCTSCGCFEAIVFYIPEVDGFGVAHRNFRGETPFGLPFSTLAGQCSGGKQVPGFVGISISYMKSPKFLQGDGGWERVVWLPKELKERVKDAIPEELYDKIATEEDVKTTDELIKFLKEKGHPIVKKTEEEVVEEVEEEKEEVKATEEEKEGIEVGELITKLAKEGGIQIIMKNVKIVINLNVKR | Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing autotrophic growth from CO(2). The alpha-epsilon complex generates CO from CO(2), while the beta subunit (this protein) combines the CO with CoA and a methyl group to form acetyl-CoA. The methyl group, which is incorporated into acetyl-CoA, is transferred to the beta subunit by a corrinoid iron-sulfur protein (the gamma-delta complex). | Q57616 |
D2RWE9 | COFC_HALTV | 2-phospho-L-lactate guanylyltransferase | Haloterrigena | MQVVVPFAATEPKTRLADVLTPAERTAFARAMLADVLTAVVEAGHEPTVLATAPLDLETLDLEAAVRDAGSVAVDDRPLTEAVNARLPERGDGGDDGTHIDPVAVVMADLALATADALEALFSAAADVAVVPGRGAGTNALVVDHPEFRVDYHGASYLDHREIAHDVGATLETVDSFRLGTDIDEPADLVEVLVHGTETDRAPARLREFGFELERTDGRVTVARLEESRPK | Guanylyltransferase that catalyzes the activation of (2S)-2-phospholactate (2-PL) as (2S)-lactyl-2-diphospho-5'-guanosine, via the condensation of 2-PL with GTP. It is involved in the biosynthesis of coenzyme F420, a hydride carrier cofactor. | D2RWE9 |
Q99969 | RARR2_HUMAN | Tazarotene-induced gene 2 protein | Homo | MRRLLIPLALWLGAVGVGVAELTEAQRRGLQVALEEFHKHPPVQWAFQETSVESAVDTPFPAGIFVRLEFKLQQTSCRKRDWKKPECKVRPNGRKRKCLACIKLGSEDKVLGRLVHCPIETQVLREAEEHQETQCLRVQRAGEDPHSFYFPGQFAFSKALPRS | Adipocyte-secreted protein (adipokine) that regulates adipogenesis, metabolism and inflammation through activation of the chemokine-like receptor 1 (CMKLR1). Acts also as a ligand for CMKLR2. Can also bind to C-C chemokine receptor-like 2 (CCRL2), but with a lower affinity than it does to CMKLR1 or CMKLR2 . Positively regulates adipocyte differentiation, modulates the expression of adipocyte genes involved in lipid and glucose metabolism and might play a role in angiogenesis, a process essential for the expansion of white adipose tissue. Also acts as a pro-inflammatory adipokine, causing an increase in secretion of pro-inflammatory and prodiabetic adipokines, which further impair adipose tissue metabolic function and have negative systemic effects including impaired insulin sensitivity, altered glucose and lipid metabolism, and a decrease in vascular function in other tissues. Can have both pro- and anti-inflammatory properties depending on the modality of enzymatic cleavage by different classes of proteases. Acts as a chemotactic factor for leukocyte populations expressing CMKLR1, particularly immature plasmacytoid dendritic cells, but also immature myeloid DCs, macrophages and natural killer cells. Exerts an anti-inflammatory role by preventing TNF/TNFA-induced VCAM1 expression and monocytes adhesion in vascular endothelial cells. The effect is mediated via inhibiting activation of NF-kappa-B and CRK/p38 through stimulation of AKT1/NOS3 signaling and nitric oxide production. Its dual role in inflammation and metabolism might provide a link between chronic inflammation and obesity, as well as obesity-related disorders such as type 2 diabetes and cardiovascular disease. Exhibits an antimicrobial function in the skin. | Q99969 |
A8L175 | PCKG_FRASN | Phosphoenolpyruvate carboxykinase [GTP] | unclassified Frankia | MTTAAQIPGLDAAPTKHARLLAWVREIAELTQPDRIEWCDGSESEFDRLTSLLIDKGTLVQLDDEKRPNSFYAASDPSDVARVEDRTYICSEKAEDAGPTNNWLDPAEMRTKLGKLFSGCMRGRTMYVVPFCMGPLGSHISALGVEITDSPYVVISMRTMTRMGTPALDQLGDDGFFVPAVHSLGAPLEPGATDVPWPCNSTKYITHFPETREIWSYGSGYGGNALLGKKCYALRIASVMARDQGWLAEHMLILKLTSPAGKVHFIAAAFPSACGKTNLAMLIPTLPGWKAETVGDDIAWMRFGDDGRLYAVNPEAGLFGVAPGTGEETNPNAVKTLWGNAVFTNVARTDDGDVWWEGLTPDKPAHLIDWKGRDWTPDSTEPAAHPNARFTVPASQCPTMAPEWENPAGVPISAILFGGRRATAVPLVTEAPDWQRGVFFGSIVSSETTAAAAGAIGKLRRDPFAMLPFCGYNMADYFAHWLEIGNKADPDKLPRIYYVNWFRKSPEGRYLWPGFGENSRVLAWVASRLDGEAKGTETPLGILPAPGELPTEGLDVSEADLETLLSVDTEVWRQEAELIPEHYNTFGDRLPAQLWAEHEALTKRLNG | Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle. | A8L175 |
Q9FMM7 | AI5L8_ARATH | bZIP transcription factor 15 | Arabidopsis | MDSYWRLKNLVNDLPVSTSLSRQGSIYSWTVDQFQTSLGLDCGSMNMDELVKHISSAEETQEGSQRQGSTTLPPTLSKQNVGEVWKSITEEKHTNNNGGVTNITHLQGQQTLGEITLEEFFIRAGARGGNTNGGSIHDSSSSISGNPHTSLGVQIQPKAMVSDFMNNMVPRSHDSYLHQNVNGSMSTYQPQQSIMSMPNGYSYGKQIRFSNGSLGSGNQSLQDTKRSLVPSVATIPSEAITCSPVTPFPTLNGKQKINGESSLLSPSPYISNGSTSTRGGKINSEITAEKQFVDKKLRRKIKNRESAARSRARKQAQTMEVEVELENLKKDYEELLKQHVELRKRQMEPGMISLHERPERKLRRTKSDIK | Could participate in abscisic acid-regulated gene expression. | Q9FMM7 |
C1DXS9 | RIMP_SULAA | Ribosome maturation factor RimP | Sulfurihydrogenibium | MKLEEKVKELLSPILEDRGLKLVDIEYITGKRPVLRIYIYNPEGTSIDDCEYVSQRIGSILDVEDLIKTSYTLEVSSPGLDRKFKNIEEYNIFKGKDVVVKTKEPIEDKKIFKGILEGLEDGIVKLKQDNIVVEIPLDKISQTKLDF | Required for maturation of 30S ribosomal subunits. | C1DXS9 |
Q03222 | RHO_BACSU | ATP-dependent helicase Rho | Bacillus | MKDVSISSLENMKLKELYELARHYKISYYSKLTKKELIFAILKANAEQEDLLFMEGVLEIIQSEGFGFLRPINYSPSSEDIYISASQIRRFDLRNGDKVSGKVRPPKENERYYGLLHVEAVNGDDPESAKERVHFPALTPLYPDRQMVLETKPNFLSTRIMDMMAPVGFGQRGLIVAPPKAGKTMLLKEIANSITANQPEAELIVLLIDERPEEVTDIERSVAGDVVSSTFDEVPENHIKVAELVLERAMRLVEHKKDVIILMDSITRLARAYNLVIPPSGRTLSGGIDPAAFHRPKRFFGAARNIEEGGSLTILATALVDTGSRMDDVIYEEFKGTGNMELHLDRSLAERRIFPAIDIRRSGTRKEELLVPKEHLDRLWSIRKTMSDSPDFAEKFMRKMKKTKTNQEFFDILNQEWKQANLSSARR | Facilitates transcription termination by a mechanism that involves Rho binding to the nascent RNA, activation of Rho's RNA-dependent ATPase activity, and release of the mRNA from the DNA template. | Q03222 |
Q03709 | LYS7_ECOLX | Lysis protein for colicin E7 | Escherichia | MKKITGIILLLLAAIILAACQANYIRDVQGGTVSPSSTAELTGVETQ | Lysis proteins are required for both colicin release and partial cell lysis. | Q03709 |
A0M5W6 | SAHH_GRAFK | S-adenosyl-L-homocysteine hydrolase | Gramella | MSTKTVPYTAYKVKDIELAEYGRREIELAEAEMPGLMALRKEYGASKPLKGARIAGCLHMTIQTAVLIETLVELGANVTWSSCNIFSTQDHAAAAIAAAGIPVYAWKGLTEEEFNWCIEQTLFFGEDRKPLNMILDDGGDLTNMVLDEYPELAEGIKGLSEETTTGVHRLYERMKKGTLPMPAINVNDSVTKSKFDNKYGCRESAVDAIRRATDVMLAGKRVVVCGYGDVGKGTAQSFKGAGSIVTVTEIDPICALQAAMDGFEVKQLETVLPKADIVITTTGNKDIVRPEHFEAMKDKTIVANIGHFDNEIAVSWLNEKHGDSKVEIKPQVDKYTINGKDIILLAEGRLVNLGCATGHPSFVMSNSFTNQTLAQIELWKNTDEYKNEVYMLPKHLDEKVAKLHLERIGVELTELKQDQAEYIGVTVEGPYKPEYYRY | May play a key role in the regulation of the intracellular concentration of adenosylhomocysteine. | A0M5W6 |
P0ACS6 | ZNTR_ECO57 | Zn(II)-responsive regulator of zntA | Escherichia | MYRIGELAKMAEVTPDTIRYYEKQQMMEHEVRTEGGFRLYTESDLQRLKFIRHARQLGFSLESIRELLSIRIDPEHHTCQESKGIVQERLQEVEARIAELQSMQRSLQRLNDACCGTAHSSVYCSILEALEQGASGVKSGC | Zinc-responsive transcriptional regulator of zntA. | P0ACS6 |
B6J2F3 | DAPB_COXB2 | 4-hydroxy-tetrahydrodipicolinate reductase | Coxiella | MAINVIINGINGKIGRVVKENITAQSDLELVSGTGRQDDLAKTIQTTHADVVIDFTTPQSVFHNAEIIIQSGARPVIGTTGLTLEQIALLDKQCRNKKLGAIVAPNFSVGAVLMMKYAKEAAHYFPDVEIIEMHHSQKIDAPSGTAIKTAQMIGEMRSSKKDEPFKDRARGEIKNGIPIHSIRLPGLFSHQSVIFGSNGETLTIRHDGMDRNCTMPGIFMACRKVMELDYLVYGLENLL | Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate. | B6J2F3 |
Q24WW7 | ADDB_DESHY | ATP-dependent helicase/nuclease AddB | Desulfitobacterium | MSMRFIVGRAGTGKSTLCRQEIHKESQEHPEGLPLILLVPEQATHQMEMSLAHDPQSGGILRAQVLSFRRLGWRVFSEVGGGGKAVIGEVGKRMLLRRLLLNHRSDLRVFARSATRPGMADLLAQAIAEFKIYRITPDQLRGIEDADELLLQKTHELAFLYEELNKSLGTAARDPDDELNLVAGKISQAPFLQGAKIWVDGFKGFTPQELYVIQAMLGTAAEITVSLPLDPELLKAGTPRFKPGEELFYEPRQTYQGLVDLAREAKASISHVFLTETHRFEKAGLKHLERFYNAYPTQTFPGGDDSTAPDPLGIALFPAANKRAEVEGVARELRRLAREEGRTWRDCSVVTRDLPGYQGIIEQVFNAHEIPYFLDHKRPVIHHPLLELLLSAIETVQKDWAYEPLFRCLKTDFFPCSKDRIDRLENYCLAYGIHGSAWKGNRSWSYYPDPNHKEETAGLNETRQIIYDLFSPFDQAIRPHPEAGGPSVTVAQITEAIYELLIRLKVPEHLQEWAEAAHSRGDLAEAQLQNQIWDAVIQVLDELVAGLGEEVMDLSDFAMILTSGLENLQLGLIPPGYDQVLVGSLDRSRNPETAVLFLLGANDGILPGKPSDEGVFDELERLRLESKGIMLAPKGKVQVYEEQYFIYTALTRAREQLYISYPLTDEEGRGLTVSPVIHRLKMIFPGLPEKYLSLDEEEPGALPHPYALLPAYALHLQKLRQGSSLSPLWQAIRLWFLSQTAAFPQVQLLEKGLRDQNEEGKLPQPLARQLYGKRLVTSVSRLELFARCPFAHFAQYGLKLKERSNYRLSPPDMGQFFHAVLHDYAIALRERGLDWGELSKEQSWQLVNETAEPIALQLQNKILLSNARYRYLTHKLKRTVHHAVRVLGEHARQGVFLPMELEVKFGPQEALPPLEVPLSGGNSLLLRGQIDRIDGAVLGHEIYLRIFDYKSREAHVSLNQIYHGLDLQLLAYLDAALQGAQILVSSSGLAEGSKGSEGSEGSEDSEDSTIHPAGFLYFPVLEPQLKSKTLLYPEQLEKDRIKAVKVKGYLLADRQVLLAMDRDLENSSLLGIKLTKSGEFKKGSPILTEEQFALLRKHLQHFLRCSGEALLEGDISITPYRQGKHTACQFCSYKPLCHFDPYLPENNYRNLPVIQDEEFWQRVQSQDSEQYPEQHPPTSVPGETSRRALQKDGGNSPRGQELIWLGEDEAGAGKEDDGHE | The heterodimer acts as both an ATP-dependent DNA helicase and an ATP-dependent, dual-direction single-stranded exonuclease. Recognizes the chi site generating a DNA molecule suitable for the initiation of homologous recombination. The AddB nuclease domain is not required for chi fragment generation; this subunit has 5' -> 3' nuclease activity. | Q24WW7 |
A6UDM2 | ATPG_SINMW | F-ATPase gamma subunit | Sinorhizobium | MPSLKDLKNRIASVKATQKITKAMKMVAAAKLRRAQEAAEAARPYSQRMAAVLSNIAQAVGADDSAPRLMTGTGKDDTHLLVVCTAERGLCGGFNSQIARHARDHVRKLLAQGKTVKIICVGKKGFDILRREFASLIIDRVDLREVKKIGFENADRIGHKVIELFDNGEFDVCTLFYSEFKSVISQIPTAQQLIPASAGEAVAEGASAIYEYEPDAAAILSDLIPRNISVQIFRALLENVAGEMGAKMSAMDNATRNAGEMINKLTLNYNRQRQAQITKELIEIISGAEAL | 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. | A6UDM2 |
A8ACY4 | UBIB_CITK8 | Ubiquinone biosynthesis protein UbiB | Citrobacter | MTPGEVRRLYFIIRTFLSYGLDELIPKMRITLPLRLWRYSLFWMPNRHKDKPLGERLRLALQELGPVWIKFGQMLSTRRDLFPPQIADQLALLQDKVAPFDGALAKAQIEEAMGGLPVEEWFDDFDIQPLASASIAQVHTARLKSNGKEVVIKVIRPDILPVIKADLKLIYRLARWVPRLLPDGRRLRPTEVVREYEKTLIDELNLLRESANAIQLRRNFENSPMLYVPEVYSDYCSQDMMVMERIYGIPVSDVATLEKNGTNMKLLAERGVQVFFTQVFRDSFFHADMHPGNIFVSYEHPENPKYIGIDCGIVGSLNKEDKRYLAENFIAFFNRDYRKVAELHVDSGWVPPDTNVEEFEFAIRTVCEPIFEKPLAEISFGHVLLNLFNTARRFNMEVQPQLVLLQKTLLYVEGVGRQLYPQLDLWKTAKPFLESWIKDQVGIPALTRALKEKAPFWVEKMPEIPELVYDSLRQGKYLQHSVDKIARELQENHVRQGQSRYLLGIGATLLLSGTFLLVSRPEWGLMPCWLMAGGLVAWLIGWRKTR | Is probably a protein kinase regulator of UbiI activity which is involved in aerobic coenzyme Q (ubiquinone) biosynthesis. | A8ACY4 |
C5J887 | NDB4T_OPICY | OcyC2f | Opisthacanthus | MKTQFAILMIAVVLMQMLVQTEGGILGKIWEGVKSLIGKRGLKKLDQLDDTFDSDLSDADVKLLREMFK | Amphipathic peptide with antimicrobial activity . Shows antifungal activity with MIC values ranging from 25 to 200 uM . | C5J887 |
Q2YAY0 | RS5_NITMU | 30S ribosomal protein S5 | Nitrosospira | MAKMQGRMQGKVAPGDDRGDGLKEKMVAINRVTKVVKGGRILGFAALTVVGNGDGGVGMGKGKSREVPVAVQKAMDEARRKMIKVSLKNGTLQHPVIGRHGAAKVYMQPASEGTGIIAGGPMRAIFEVMGVHNILAKCIGSTNPYNVVRATLNGLQAMSNPAEIAAKRGKSVEEILGLEK | Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body. | Q2YAY0 |
B7MQ21 | GLO2_ECO81 | Glyoxalase II | Escherichia | MNLNSIPAFDDNYIWVLNDEAGRCLIVDPGDAEPVLNAISANNWQPEAIFLTHHHHDHVGGVKELVEKFPQIVVYGPQETQDKGTTQVVKDGETAFVLGHEFSVIATPGHTLGHICYFSKPYLFCGDTLFSGGCGRLFEGTPSQMYQSLKKLSALPDDTLVCCAHEYTLSNMKFALSILPHDLSINDYYRKVKELRAKNQITLPVILKNERQINVFLRTENIDLINVINEETLLQQPEERFAWLRSKKDRF | Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid. | B7MQ21 |
C0HKK0 | CYVIA_VIODI | Cyclotide vdif-A | Viola | GIPCGESCVFIPCISSVVGCSCKSKVCYRN | Probably participates in a plant defense mechanism. | C0HKK0 |
Q2FM63 | THIE_METHJ | Thiamine-phosphate pyrophosphorylase | Methanospirillum | MDCGLYIITDEILAPGCSHIQIAKESLSGGAKIIQLRDKRRNAAELYAIAQEIRSLCTQHHARFIVNDRLDIALAVQADGVHLGQDDLPLSAARLLAPRPFIIGVSVGTVEEAVLAEKGGADYLGVGPVYPTGTKADAGPAVGPGLIRSIRERVAIPIIAIGGINLTNAGDVLAAGADGIAVISAVICSPDIAAASRKFADLMIHS | Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP). | Q2FM63 |
Q57JH3 | GLMM_SALCH | Phosphoglucosamine mutase | Salmonella | MSNRKYFGTDGIRGRVGNAPITPDFVLKLGWAAGKVLARHGSRKIIIGKDTRISGYMLESALEAGLAAAGLSASFTGPMPTPAVAYLTRTFRAEAGIVISASHNPFYDNGIKFFSIDGTKLPDDVEEAIEAEMEKEITCVDSAELGKASRIVDAAGRYIEFCKGTFPNELSLNGLKVVVDCANGATYHIAPNVLRELGATVIAIGCEPNGVNINEEVGATDVRALQARVLAEKADLGIALDGDGDRVIMVDHEGNKVDGDQIMYIIAREGLRQGQLRGGAVGTLMSNMGLELALKQLGIPFSRAKVGDRYVLEKLQEKGWRIGAENSGHVILLDKTTTGDGIVAGLQVLAAMVRNHMSLHDLCSGMKMFPQILVNVRYTAGSGDPLENEAVKAVTADVEATLGNRGRVLLRKSGTEPLIRVMVEGEDEAQVTAFAHRIADAVKAV | Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate. | Q57JH3 |
Q89AJ6 | ODO2_BUCBP | Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex | Buchnera | MNIINIFIPDLPESVTDATIIKWHKKKGDKVQEDTILVDIETDKVILEIPSPSDGILNSIIADKGKIVLPGQVIGTLLKIGIKNEEKIIKTTNNVVNTDNNQNINLKLLEKTYSPTVRRLISMHDLRDVDIIQGTGTKNRLTRKDILNYLKNIRSNTNKKINNYDLNAYNFNTTHKNHRSIKRVKMTRLRKKISERLLSTKNNTASLTTFNEVNMQSILNLRRKYGELFKQKHGIKLGLMSFYVKAVIEALKIFPEINASIDNDEIIYYNYFDISIAISTPRGLVTPVLKNADLMSMAEIEIKIKDFSEKGKNSKLTIDDLIGGNFTITNGGVFGSLFSTPLINPPQSAILGMHAIHKRPVIVDENIEVHPMMYLALSYDHRLIDGKESVGFLLKIKEFLEDFSRIVLNI | E2 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the second step in the conversion of 2-oxoglutarate to succinyl-CoA and CO(2). | Q89AJ6 |
Q73TF1 | RS182_MYCPA | 30S ribosomal protein S18 2 | Mycobacterium avium complex (MAC) | MPKKPARTRRPAPLAGRARKKNLLDSLGLRTVDYKDTATLRVFISERGKIRSRQVTGLSVQQQRQVATAIKNAREMALLPYPGQGIKP | Binds as a heterodimer with protein S6 to the central domain of the 16S rRNA, where it helps stabilize the platform of the 30S subunit. | Q73TF1 |
Q9LK39 | AAE16_ARATH | Probable acyl-activating enzyme 16, chloroplastic | Arabidopsis | MASTSLGASILVSHCSSAPEFQVSGMRLVFGYKAFGCRTSRRGFRVRCESKIQEKELRRCSPFLERLSLPREAALSSNEWKSVPDIWRSSVEKYGDRVAVVDPYHDPPSTFTYRQLEQEILDFVEGLRVVGVKADEKIALFADNSCRWLVADQGIMATGAVNVVRGSRSSVEELLQIYCHSESVALVVDNPEFFNRIAESFSYKAAPKFVILLWGEKSSLVTAGRHTPVYSYNEIKKFGQERRAKFARSNDSGKYEYEYIDPDDIATIMYTSGTTGNPKGVMLTHQNLLHQIRNLSDFVPAEAGERFLSMLPSWHAYERACEYFIFTCGVEQKYTSIRFLKDDLKRYQPHYLISVPLVYETLYSGIQKQISASSPARKFLALTLIKVSLAYTEMKRVYEGLCLTKNQKPPMYIVSLVDWLWARVVAFFLWPLHMLAEKLVHRKIRSSIGITKAGVSGGGSLPMHVDKFFEAIGVNVQNGYGLTETSPVVSARRLRCNVLGSVGHPIKDTEFKIVDHETGTVLPPGSKGIVKVRGPPVMKGYYKNPLATKQVIDDDGWFNTGDMGWITPQHSTGRSRSCGGVIVLEGRAKDTIVLSTGENVEPLEIEEAAMRSNLIQQIVVIGQDQRRLGAIVIPNKEAAEGAAKQKISPVDSEVNELSKETITSMVYEELRKWTSQCSFQVGPVLIVDEPFTIDNGLMTPTMKIRRDKVVDQYKNEIERLYK | May be involved in the activation of fatty acids to acyl-carrier-protein. | Q9LK39 |
P53444 | ALF_NEUCR | Fructose-1,6-bisphosphate aldolase | Neurospora | MGIFDELNLPAGVLYGDDVLKLFQYAREKQFAIPACNVTSSSTAVAALEAARDQKAPIILQTSQGGAAFFAGKGIKDSAEKREASVAGAIAAAHYIRSIAPIYGIPVVLHTDHCAKKLLPWLDGMLEEDEKFFKANGVPLFSSHMIDLSEEPVEENISTCVKYLKRMAPMKQWLEMEIGITGGEEDGVDNSEVDNASLYTQPEDIWQIEEAFRPISPYFSIAAGFGNVHGVYAPGNVKLHPELLGKHQAYVSEKLGGKDKKPVFFVFHGGSGSSKEEYREAISNGVVKVNVDTDLQWSYLVGIRDYILNNIDYLRSQVGNPEGPNKPNKKKYDPRVWIREGEKTMKARVEEALKDFNAAGTV | Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis. | P53444 |
A1RID4 | YCIB_SHESW | Inner membrane-spanning protein YciB | Shewanella | MKQLLDFLPLVIFFAVYKFFDIYIASGALIAATALQLIVTYALYKKLEKMHLITFAMVTVFGTLTLVFHDDAFIKWKVTIIYALFALALGISQLLNKSILKSMLGKEMQVADKIWAHITWYWVIFFATCGLVNIYVAFSLPLETWVNFKVFGLTALTLVNTVITVFYLYKHLPEDQRKELK | Plays a role in cell envelope biogenesis, maintenance of cell envelope integrity and membrane homeostasis. | A1RID4 |
Q8R8M4 | UVRB_CALS4 | Excinuclease ABC subunit B | Caldanaerobacter | MGGFKLVSNFKPTGDQPQAIEKLVEGVRRGYRYQTLLGVTGSGKTFTMANIIARLNRPTLVIAHNKTLAAQLYSEFKEFFPENAVEYFVSYYDYYQPEAYVPETDTYIEKDASINEEIDKLRHSATAALFERRDVIIVASVSCIYGLGDPIDYENLMLSLRPGMVKDRDEIIRKLVEIQYERNDINFTRGKFRVRGDVIEVFPASFSNKAIRIELFGDEIDRIAEIDVLTGEVLGYRKHVAIFPASHYATSRDKLERAIKSIREELEERYKELKEMGKIVEAERLWQRTNYDLEMLQEMGYCKGIENYSRHISGRPPGSPPYTLLDYFPEDFLIFIDESHVTIPQLRGMYNGDRSRKEALVEYGFRLPSAYDNRPLTFEEFEQRVNQVIFVSATPGPYEMEHSEQVVEQLIRPTGLVDPEVIVRPVKGQVDDLIAEIRKTVAKGYRVLVTTLTKKMAEDLSDYLKEMGIRVRYLHSDIETIERVEIIRDLRLGKFDVLIGINLLREGLDIPEVALVAILDADKEGFLRSETSLIQTIGRAARNAEGRVIMYADTITNSMRRAIDETNRRRKIQMEYNEKHGIVPKTVVKGVRDVIQATQVAEKEEKYEKTANFYDPDVIKSTIEQLEKEMRQAAIELQFEKAAKLRDMILELRKQLEEVSLR | The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and the UvrB-DNA preincision complex is formed. This complex is subsequently bound by UvrC and the second UvrB is released. If no lesion is found, the DNA wraps around the other UvrB subunit that will check the other stand for damage. | Q8R8M4 |
P10112 | CRYGS_CYPCA | Gamma-S-crystallin | Cyprinus | MGRIIFYEDKNFQGRRYECDSDCSDFHAFLNRCNSIRVESGAWVIYERPNFMGYQYVLTRGEYPDYQRWMGLNDRLCSCKMIHFVSGSEYKIQLYDKGDFTGQVYESTEDCPSVVDRFRTREVHSCKVLDGIWIFYEHPNYRGRQYLLEKGEYRKPVDWGAVCPTVQSFKRLME | Crystallins are the dominant structural components of the vertebrate eye lens. | P10112 |
Q8TIN7 | FTSY_METAC | Signal recognition particle receptor FtsY | Methanosarcina | MFNKFKEKLGSFKKALSKTIDEKAVEVEPVVVEQMPQSEESLEEEIEPIVEEEALEAALEAESSEAETEAASPAIAHVPIEDLKKAEYRKKLKDLKKVGEKKVEEEKPPEEKKSFFKKVVPKVGFAQKAKALVFNREVYLDNKDLEEPLWELEMGLLESDLALSVSEAIVESVKNQLTGTTKRIGSNTGEIVEAALKKAILEVVSANTFDFDEYVKNREKPVHIVFVGINGTGKTTSISKITNRLLKSGYSVVLAAGDTFRAGAIDQLGIHANRLGVKMIKHQAGADPAAVIYDAVQYAKAHKIDFVLSDTAGRMHTNMNLMAQMEKICRVSTPDLIIFVDEAVAGNDAVERAAQFNEAVPIDGSILTKIDADAKGGAAISIAYITGKPILFFGIGQGYEDLKKFDPEWFVDQLFNQ | Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Acts as a receptor for the complex formed by the signal recognition particle (SRP) and the ribosome-nascent chain (RNC). | Q8TIN7 |
A3MZB7 | RSMA_ACTP2 | S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase | Actinobacillus | MSNQNSKKHLGHTARKRFGQNFLHDMNVIHNIVSAINPKNGQFLLEIGPGLGALTEPVAEQVDKLTVVELDRDLAERLRHHPFLNHKLTIIEQDALRFNFREYFESLELREGEGVRVFGNLPYNISTPLMFHLFKFHDLIQDMHFMLQKEVVKRLCAAPNSKAYGRLTIMAQYYCQVMPVLEVPPTAFKPAPKVDSAVVRLMPHKVLPHPVKDVYWLNRVTTQAFNQRRKTLRNALSTLFSPEQLEALNIDLNARAENLSIADYARLANWLYDNPPAVDNQEEIIDEDI | Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits. | A3MZB7 |
O85467 | GERIA_BACCE | Spore germination protein GerIA | Bacillus cereus group | MIWNWLRKKKKSNTSKLNETDNQEQHSNNQEDDNKEQTRSMKHNKGKNNEQKDSSQDKQQSAKQGDSSQDKQQNPKQEDSSQDKQQNPKQGDSSQDKQQSAKQKDPSQDKQQNPKQEDSSQDKQQSAKQGDSSQDKQQSAKQGDSSQDKQQNAKQDEPSQSKQQSSGGNSIYDFTKPEKDRIHSLQNLIEKLKKSSDFVNYHTSDDETMPYWISYYRPSLDGEKLQKYLMPTLLERPNASLEELKEHIPMSGITITNDLQKIEDMVLKGHAIIQLNQQDQKCMLANIAIDNYRAPTPPLNESTVIGPQEGFVEDIDTNINLVRKRLPVLDLQTKEMIIGEFSKTKVVMMYLDNLAEKDNVDFLEESLRALEYDQINDSAYLQELMGEKSIFPLYINTERTDRVTKALIDGKIAIFVDGSPSVLLTPVSYFDFFISPEDYNVSWMYATFSRILRLIAVLFSICATPLYVAVLNYHYELIPSDLLETLILSRAQVPFPPLIEALFLELAIDLLREAGARLPMKVGQTLGIVGGIVIGQASVQAGLTSNILLIIVALSALASFITPIYKMGNAVRLLRFPFLAFAEIGGLFGISLGFIFLFTHLFRLTSLRKPYALFYPTRQQSVKDSWIRFPLTMIDTRDVQARPQHVKKAAKGISTKHRSDFDD | Required for inosine germination. | O85467 |
Q2NG79 | DTD_METST | Gly-tRNA(Ala) deacylase | Methanosphaera | MKLVVQRVTSAKVEVNNNIVGKIGKGYLVLLGIKKTDTKKEADYMINKLMKLRVFEDEENKMNLSIQDIDGEILLIPQFTLYGDVTHNNRPSFSNAMKPTDAKKLFEYCCNECEKKVHTQKGEFGAFMDVNLVNNGPVTIIIEKEYNS | An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo and helps enforce protein L-homochirality. | Q2NG79 |
Q089P0 | RS8_SHEFN | 30S ribosomal protein S8 | Shewanella | MSMQDPIADMLTRIRNGQAANHVSVKMPSAKLKVAIAKLLKDEGFITEYAVADEAKPELEITLKYFQGKPVVETIQRVSRPGLRIYKGKDELPKVMGGLGIAIVSTSQGLMTDRAARQNGTGGEVICYVA | 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. | Q089P0 |
Q99MZ7 | PECR_MOUSE | Peroxisomal trans-2-enoyl-CoA reductase | Mus | MGSWKTGQSYLAAGLLKNQVAVVTGGGTGIGKAVSRELLHLGCNVVIASRKLDRLTAAVDELRASLPPSSSAEVSAIQCNIRKEEEVSNLVKSTLAKYGKINFLVNNGGGQFMAPVEDITAKGWHAVIETNLTGTFYMCKEVYNSWMREHGGSIVNIIVLLNNGFPTAAHTGAAREGVYNLTKSMALAWASSGVRINCVAPGTIYSQTAVDNYGEMGQTLFEMAFDSIPAKRLGVPEEISPLVCFLLSPAASYITGQLINVDGGQALYTHAFSIPDHDNWPVGAGDLSIVKRIKESFKKKAKL | Participates in chain elongation of fatty acids. Catalyzes the reduction of trans-2-enoyl-CoAs of varying chain lengths from 6:1 to 16:1, having maximum activity with 10:1 CoA. Has no 2,4-dienoyl-CoA reductase activity. | Q99MZ7 |
C3MB76 | SECB_SINFN | Protein-export protein SecB | Sinorhizobium | MTTDTASNGNGAQQAPSLNILAQYVKDLSFENPGAPRSLQARDQAPSININVNVNANPLAENDFDVVLSLNAQAQDGDKVLFNVELAYGGVFRVSGFPQEHMLPLLFIECPRLLFPFARQIVADATRNGGFPPLMIDPIDFAQMFAQRMAEEKVRAQVANSNTTTN | One of the proteins required for the normal export of preproteins out of the cell cytoplasm. It is a molecular chaperone that binds to a subset of precursor proteins, maintaining them in a translocation-competent state. It also specifically binds to its receptor SecA. | C3MB76 |
A6NI72 | NCF1B_HUMAN | Putative SH3 and PX domain-containing protein 1B | Homo | MGDTFIRHIALLGFEKRFVPSQHYVRYMFLVKWQDLSEKVVYRRFTEIYEFHKTLKEMFPIEAGAINPENRIIPHLPAPKWFDGQRAAENHQGTLTEYCGTLMSLPTKISRCPHLLDFFKVRPDDLKLPTDNQTKKPETYLMPKDGKSTATDITGPIILQTYRAIANYEKTSGSEMALSTGDVVEVVEKSESGWWFCQMKAKRGWIPASFLEPLDSPDETEDPEPNYAGEPYVAIKAYTAVEGDEVSLLEGEAVEVIHKLLDGWWVIRKDDVTGYFPSMYLQKSGQDVSQAQRQIKRGAPPRRSSIRNVHSIHQRSRKRLSQDAYRRNSVRFLQQRRRQARPGPQSPGSPLEEERQTQRSKPQPAVPPRPSADLILNRCSESTKRKLASAV | May be required for activation of the latent NADPH oxidase (necessary for superoxide production). | A6NI72 |
P10575 | GLRX1_BOVIN | Thioltransferase | Bos | MAQAFVNSKIQPGKVVVFIKPTCPYCRKTQELLSQLPFKQGLLEFVDITAAGNISEIQDYLQQLTGARTVPRVFIGQECIGGCTDLVNMHERGELLTRLKQMGALQ | Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins. | P10575 |
P36572 | BIOD_SERMA | Dethiobiotin synthase | Serratia | MSKRWFVTGTDTEVGKSVASSALLQAANRAGYPSAGYKPVASGSEMTAEGLRNGDALALQANSGVALDYDEVNPYVFAEPTSPHIVSADEGRPIDAARLSDGLRRLEQRADWVLVEGAGGWFTPLSAEYTFADWVRQEQLPVILVVGIKLGCINHAVLTAQAVQQAGLTLAGWIANDVGGAPGRRHQEYLATLRRMLPRRCWAKSRTCRRPERAPLGQYLDISLLAQ | Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring. | P36572 |
P0CH90 | NA237_NEMVE | Neurotoxin Nv3-3 | Nematostella | MASFKIVIVCLALLVAVASARRRDMMSDDELDYHYSKRGIPCACDSDGPDIRSASLSGIVWMGSCPSGWKKCKSYYSIVADCCNQ | Binds to site 3 of voltage-gated sodium channels and inhibits the inactivation process . Is highly active on DmNav1/TipE (drosophila) and is only extremely weakly active on rat Nav1.4-beta-1/SCN4A-SCN1B, and on human Nav1.5-beta-1/SCN5A-beta-1 . This reveals high specificity for arthropod over mammalian channels . In vivo, when released into the medium, this recombinant toxin induces impaired swimming, paralysis and death of the crustacean A.nauplii within several hours . Also causes paralysis of cherry shrimps immediately after injection at very low doses . Its effect on zebrafish (D.rerio) larvae is also rapid, since it induces tail twitching accompanied by impaired swimming after 20 minutes and complete paralysis within 45 minutes . It has also been observed to cause death of zebrafish larvae within 1 hour . | P0CH90 |
Q8ABI8 | FABH1_BACTN | 3-oxoacyl-[acyl-carrier-protein] synthase III 1 | Bacteroides | MDKINAVITGVGGYVPDYVLTNDEISKMVDTTDEWIMGRIGIKERHILNEEGLGTSYMARKAAKQLMQRTKSRPDDIDLVIVATTTSDYRFPSTASILCERLGLKNAFAFDMQAVCSGFLYAMETGANFIRSGKYKKIIIVGADKMSSVIDYTDRATCPIFGDGAAAFMLEPTTEEVGIMDSVLRTDGKGLPFLHIKAGGSVCPPSYYSLDHHLHYIYQEGRTVFKYAVANMSDSCEAIIARNHLTKEEVDWVIPHQANQRIITAVAQRLEVPSEKVMVNIERYGNTSAGTLPLCIWDFEKKLKKGDNLIFTAFGAGFAWGAVYVKWGYDPKEDA | Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids. | Q8ABI8 |
A6WSV3 | MIAA_SHEB8 | Isopentenyl-diphosphate:tRNA isopentenyltransferase | Shewanella | MNKELQPKVIFLMGPTASGKTALALELAEKHNCEIISVDSALIYRGMDIGSAKPSADELARGPHRLIDIRDPSESYSAADFRADAITEIEQIISMGKTPVLVGGTMMYFKALLEGLSPLPSADEAIRAEIQAEADEKGWEALHDQLREIDPVSAERIHPNDPQRLSRALEVYRISGKSMTELTQTKSAPLPYDVVQFAIAPRERKVLHDLIAQRFAIMLKQGFLEEVTELKARGDLHLDLPSMRCVGYRQCWQYLDGEFDYDTMVEKAVAATRQLAKRQLTWLRSWPELNWLESGAEGNLVTLMRQCR | Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A). | A6WSV3 |
Q2P7N0 | FABA_XANOM | Trans-2-decenoyl-[acyl-carrier-protein] isomerase | Xanthomonas | MTRQSAYSRDQLLASARGELFAPDSGRLPNDPMLMFDRITEISDTGGAHGKGVIRAELDIRPDLWFFGCHFIGDPVMPGCLGLDAMWQLTGFFLTWIGAQGRGRALGCGEVKFTGQVLPSAQLVRYEIDVSRVINRKLVMAQTDARMLVDGREIYVAKDLRVGMFTSTENF | Necessary for the introduction of cis unsaturation into fatty acids. Catalyzes the dehydration of (3R)-3-hydroxydecanoyl-ACP to E-(2)-decenoyl-ACP and then its isomerization to Z-(3)-decenoyl-ACP. Can catalyze the dehydratase reaction for beta-hydroxyacyl-ACPs with saturated chain lengths up to 16:0, being most active on intermediate chain length. | Q2P7N0 |
A0A2P1BT06 | FCS1_UNKP | Trans-feruloyl-CoA synthetase | environmental samples | MGERRFSNQQIDRLLRPKSVAVIGASDRKGALGATLLNNLVQYEFSGDIYPVNPKRDELLGLKVYHEVAELPEGIDCAVLAIPRPFVIDTVRQLAQRGCGAVVIYSAGFSEAGEEGMKDQLELAAIAAEYGMVIEGPNCLGCTNYVERVPLTFVETNMQTPPKGTRAVGIASQSGALAAVLATALHPRGLYVSSSVSTGNEAASGVEDYVEWLVDDEDTHVIAMYVESLRRPKAFIAAARRAHAAGKPIVMLHPGKSNKAQESAATHTGAMAGDYALMKTKLAREGVIFADTLEELADITEIALRCRALPGANMAVLGESGALRGLAFDIAEDIGLDLIHLDDDNSPALRAILPDFVPVSNPTDITALGLSEPEIYTKVLTALLEDERIGSVVASIIQSDPITSGIKFPHIIKVLDGGTFAKPLVFAGVDEGATVPKEYIDGLRKVGIPWFPSTERAYRAIARLADLSKRDLADNSGDPIVVPGLDAVSGVVPEYKAKELLRPLGIAFPPSQFAANAEAAAAAARAIGYPVVMKAQAAALGHKSDAGGVILNLKTDDEVRDAFARIYGNVEAYDRSIALDGVLIEKMGKMGTEMIVGAKNDPQWGPVVLAGFGGVTAEILKDVKLFTPEMDAAAVQRGLLELKQAPILKGYRGAPALDVAALAELIVQIGRVMAGNPSIREIDLNPVIIHPAGEGVAALDALMLVER | Catalyzes the formation of feruloyl-CoA, ADP and phosphate from ferulate, CoA and ATP. | A0A2P1BT06 |
A4RAE9 | AMPP3_MAGO7 | Aminoacylproline aminopeptidase | Pyricularia | MASKNYDDVLKGKYPAKEHARRVVEVIRSSQPDVSGVLYLEGQKTKMIEDNDSEEHFRQRRYFYYLTGCELPDCYLTYDIATSRSTLYIPPVDPESVIWSGLPMSALEALQKYDVDEVRYTHEVNAALTSLAEAAPSSTVYAIPNQVSDSITFLGFGAKNFDVLKPAIERARVVKSDYEIALIAKANDISGAAHLAVLKRVRHVSNERELYATFLAECISRGAPHMAYHSIVAAGRAAATLHYVKNDEPTAGKLNLLLDAACELNCYASDITRTFPISGSFTPESRAIYDTVLRMQLETLAMLKEGVRWDDVHIHAHRVAIEGLLAAGIFKKGFSVDEILESRTSVAFFPHGLGHYLGMDTHDTGGNANYQDKDSMFRYLRVRGTLPAGSVITVEPGIYFCNFIIEPYLKDEKHSKYIDAAVLDKYWDVGGVRIEDNVVITKDGYDNLTTAVKDAKEMEKIISSS | Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides. | A4RAE9 |
Q09812 | ATG22_SCHPO | Autophagy-related protein 22 | Schizosaccharomyces | MNSPIQLHKKFSTTVWHVLSWILYAVGAGPTAIISMGVYVPLIVMKNAHDHGFLRTDHTIPCSLYPEEPCSLNIVGPLWIDVSSIVFAASAISTFLQMAMMVSLGVICDYGNNRRYILFSCVIIGSISGIILSWSPSSFLLGKIVFLILVDLNFIISQSCYDSFLPIFLRFYPITRGPITLESALQDETDDLDSYITNTTIDSSEEEPYLLEHSLILNESAPPADVEDEHKAKIAARLSSVGFGSFFGAAILFQIIFTPILYKTNNNPIILPITVTVCSCWWLILSTPLCTIVTLPVENHSSDAILTLLYNSVKESYHSFKHAMSISSIRLFLFSRLFINCGIQTSLSSAVIFGKARLNLSNFQLTLLGMGISSFALLGTVIIPYLTEYFQLNSLQVVMIISILLPMAPLYGLLGYIPGFENAGIRTSADVFRATLFFGFFLGGAHSYCRSVYAQLVPSGKETRFFALYALISQTGVLFSHISLTLISNYTSDLRAVYIFVIVVMTLPLSSLWIMYQHSKTPNLHRSSS | Vacuolar effluxer which mediate the efflux of amino acids resulting from autophagic degradation. The release of autophagic amino acids allows the maintenance of protein synthesis and viability during nitrogen starvation. | Q09812 |
P45494 | PEPV_LACDL | Peptidase V | Lactobacillus | MDLNFKELAEAKKDAILKDLEELIAIDSSEDLENATEEYPVGKGPVDAMTKFLSFAKRDGFDTENFANYAGRVNFGAGDKRLGIIGHMDVVPAGEGWTRDPFKMEIDEEGRIYGRGSADDKGPSLTAYYGMLLLKEAGFKPKKKIDFVLGTNEETNWVGIDYYLKHEPTPDIVFSPDAEYPIINGEQGIFTLEFSFKNDDTKGDYVLDKFKAGIATNVTPQVTRATISGPDLEAVKLAYESFLADKELDGSFEINDESADIVLIGQGAHASAPQVGKNSATFLALFLDQYAFAGRDKNFLHFLAEVEHEDFYGKKLGIFHHDDLMGDLASSPSMFDYEHAGKASLLNNVRYPQGTDPDTMIKQVLDKFSGILDVTYNGFEEPHYVPGSDPMVQTLLKVYEKQTGKPGHEVVIGGGTYGRLFERGVAFGAQPENGPMVMHAANEFMMLDDLILSIAIYAEAIYELTKDEEL | Is a relatively unspecific dipeptidase cleaving a variety of dipeptides, notably those with an N-terminal beta-Ala or D-Ala residue, e.g. carnosine (beta-Ala-His). To a lesser extent, also shows aminopeptidase activity, since it is able to catalyze the removal of the N-terminal amino acid from a few distinct tripeptides. | P45494 |
Q45594 | YYDH_BACSU | Putative peptide zinc metalloprotease protein YydH | Bacillus | MKILKYEDEKYEVLVQNNVFIKDKKSGEYYKNSLNSLSDKQLLRFKMYKEKVSPKFFYLFLSFTALMFILNYIHLIKLQNGLSSVFYGWKMWIIIVIYFIMNIVLHELGHIYSLKFFGKNFDKVGFKLNFYVFPAFYVQLNETYMLSRNEKIIVHLFGLFINYLLINTLELINQFTFSSEALTMAFMLFSSTLLWNLIPILNSDGYKILLAFLSLDEYSRFKTNHWLVLTIQIIGIGLAVNSVVHWILYIVN | Required for production of the modified peptide YydF (Probable). May process the precursor form of YydF to release the active peptide (Potential). | Q45594 |
Q8RDK2 | LEUC_CALS4 | Isopropylmalate isomerase | Caldanaerobacter | MGLTLTQKILSAKAGREVKPGELIEIDVDMVLGNDITAPVAIKEFEKIGVDKVFDNTKIALVPDHFVPSKDIKSAEQVNVMRKFAKKYNIVNFFEVGRMGIEHALLPEQGLVLPGDVVIGADSHTCTYGALTCFATGVGSTDMAAAMATGKAWFKVPEAIKFVLKGNLGKWVSGKDVILYIIGKIGVDGALYKSMEFTGNIKALSIDDRFTIANMAIEAGAKNGIFDFDEITEAYVKKRAKREYKVFERDEDAEYSEVIEINLDDIRPQVAFPHLPENTRSIDEVGKVKIDQVVIGSCTNGRLSDMEIAYRILKGKKVHPDVRLIIFPATQEIYLECVKRGYIEEFIKAGAAVSTPTCGPCLGGHMGVLAKGERALATTNRNFVGRMGHPESEVYLASPAVAAASAIAGYIVSPEEVE | Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate. | Q8RDK2 |
Q3AA35 | ADDA_CARHZ | ATP-dependent helicase/nuclease AddA | Carboxydothermus | MKNWTAEQMRAITSRGNALLVSAAAGAGKTSVLVERVLSRVLTDTPPVDIDRLLVVTFTEAAAGEMKERLGTELLKRLNEDPGNSRILEQLELLPVADISTLHSFCHKIIRKYGRVCGYETKFAILEGPRETYLKNKVLEEILEERYEKGDRELFALLEYLNDEKNDRNLKELILNLYHFSRSNPEPEKWLLDSLNLFNGNWERFEDTFWYREIKSSTEMWLEYILELLGRAKSVAEKYGQARAFSLLAEDMEKVRGLYAKLNEGYEAAKQYLSQVKFGTFSWGRGVGGKDEAKDLRDKAKEQFETIKKRYFSWEAGNFREELRTLTSYLDPLVKLVREFSRKYQEEKRKHGFADFSDLEHWALDILKSGVYRELREKYVEILVDEYQDINGLQEEILTYVSRDGQNLFMVGDVKQSIYRFRWARPEIFLKKYEDFTDEKKIELSLNFRSREEIIATVNFIFKQIMKKRVAELSYDEKAFLKKGADYLPNANCFAELHLIEGKPEEDINSNGEPEEDLTAVHREARLVAAKILKLKEEGFKVFDRETKEFRPLQYRDIVILSRSLSNSSNIWQEELTRAGIPVYVEGAGSFLNSKEILLMTSFLKVIDNPCQDVPLAAVLCSPVAGLTYEELWQVRKEYPEGLLYDALKNKSLGKDELSVKSQKFLELLVEFQKLSRQISLAELVNEIYRKTNLPEIFGAYPGGEVRQANLKLLHDLAVDFAEINGGGIYNFLTFLSQAAESEDFSPAKLIGEADDVVRVMSVHKSKGLEFPVVFVVGLGKRFKFDYSNTVFLHSDLGFGPKFFDPEKRIRRHSIASQILSERMRRETLAEEMRILYVALTRAREKLILVGTVKNLAKKMAGWQSQTEALKDTLSDGQIARAGNFLDWIGPVVFREGSDLPDCLKVEVHPQQEKIEGEQWELPEVLRVKLLTKTPFTEETDYTGQFRAGLEFNYPGLKIAKLPAKMSVSDLKEVFSTDDVISLEDEDEVFLPGVYFEDGAMLGIVYHEFLRRIDFQGDLSASGLKAQGETLVAEGVLPPESREMLDFTKIARIFATPLGQRILRAREIYPEFPFTLGVKAGEIYPEATGFSEKILVRGVIDLLALEEDGFFIVDWKTDRVTGDILNERLKEYAGQLNLYARAVEEITGKKVKEKYLYFINLEKEVRV | The heterodimer acts as both an ATP-dependent DNA helicase and an ATP-dependent, dual-direction single-stranded exonuclease. Recognizes the chi site generating a DNA molecule suitable for the initiation of homologous recombination. The AddA nuclease domain is required for chi fragment generation; this subunit has the helicase and 3' -> 5' nuclease activities. | Q3AA35 |
Q9ES08 | KCNK9_RAT | Two pore potassium channel KT3.2 | Rattus | MKRQNVRTLSLIACTFTYLLVGAAVFDALESDHEMREEEKLKAEEVRLRGKYNISSDDYQQLELVILQSEPHRAGVQWKFAGSFYFAITVITTIGYGHAAPGTDAGKAFCMFYAVLGIPLTLVMFQSLGERMNTFVRYLLKRIKKCCGMRNTEVSMENMVTVGFFSCMGTLCLGAAAFSQCEDWSFFHAYYYCFITLTTIGFGDFVALQSKGALQRKPFYVAFSFMYILVGLTVIGAFLNLVVLRFLTMNTDEDLLEGEVAQILAGNPRRVVVRVPQSRKRHHPMYFLRKYGRTLCYLCFPGANWGDDDDDDDDAVENVVVTTPVPPAVAAAAAAATPGPSTRNVRATVHSVSCRVEEIPPDVLRNTYFRSPFGAIPPGMHTCGENHRLHIRRKSI | pH-dependent, voltage-insensitive, background potassium channel protein. | Q9ES08 |
Q3HKH9 | ATPA2_CERS4 | F-ATPase subunit alpha 2 | Cereibacter | MSGDPGLEALKARVAEVPLGPEIEETGRIATLADGLVEVEGLPGARLGEVVRFAGGAEGLVLTLDPETVQVALLDPGAALGSGTEVRRTGQLLSVPVGQGLLGRVVDPLGRPLDGLPAILPEARLEIERPAPGIVDRDMVAEPVETGLLVVDALFAVGRGQRELIIGERATGKTSLAVDAIVNQAASDIVCFYVAIGQRTTAVRRVIETVREKGAFARTVFVVAPATASPGLRWIAPFAATSMAEWVRDRGGHALIVYDDLTKHAAVHRELALLARQPPGREAYPGDIFYLHARLLERSAKLSAVNGGGSLTALPIAEIEAGNLSAYIPTNLISIADGQIVTSAALFAANQRPAVDIGLSVSRVGGKAQRGALKAVAGRVRLDYAQYLEMKMFSRFGGFGDAALRARLARGERIGALLAQPRTTPLSTPVQVALLAALAEGALDDVPLEDLARLKAALGPVLAADASLGPFRAAPDRLEPETRAALLACVRRAREAP | Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. | Q3HKH9 |
A0JM49 | LTN1_XENTR | RING-type E3 ubiquitin transferase listerin | Silurana | MQEFGFMCKEREMETVRGVLPYWPRIYCKISLDLDRRVREATQQAFEQLILKVKKYLAPHLKSLMGFWLIAQCDTYSPAASSARVAFEAAFPAHKQPEALAFCKEEIMNVLLDHLLKETPDTLSDTQAVPIEDRESKYFRVVTCSLLALKRLLCMLPRSENSSLQERLAHLLSQSKFWKYSKHSTSSIRSAFFELMSALCQCSPDVLRAEASRLCPAVLLSIDDSDAVVCPALWEAVLYTITTIEDCWEHVNAQKGVLPKLWSVLREGGRGLATVIFPNLLPFISRVPTNIIKTPTDFYSNFFNSLGQGLSSERAVASPAECSAIISAYMECLRFAMQENAGEEEENKKVQQILISDQLMPLIDSSLKDPKLQNSPLFSQVEETLYSWEKKAESQGLDDKLSRIHATLLREFWENLAHICVSHVDVIEAGEKNLAGVSGLLQVLQNPNCLLKVNKKKKAKIRFKGEGDDESDAVSHVSESQPMSKFIMETCSSSGRDPGIAQLRQERLEDLVCKLAELSMVYISEQRSQQHLMFLAALLSTFPSIRVFQVLLQQSSEEDPKNLNSPDHDVTPRHKNPAVQFLYAKLIFWFNDKSLEESDFLVDILYSVLFCCTDSSERKHLLDDMTKMNFKWSVFLYIIQKACTDPEKYSLASDWLKGEVLGERLICLANDLCTSGLMDKATPSEAYCSKKWALLSLVLSEHVHNEYLIADAYVEKIINKLHSALMKARNLSKAGHLEQSVSFICDVGSNFFSSIKGCLQMPSAEDLLLTIFQLCAQASDTSHMSESLLLKLKNTWLAGLHSLVCQYKNMPQGSNFLKQSAQWVKDQIQTSHLNVKSLQSLICTVDDLYSTILDSSLSGFSLLAEHTASMMPSAETWQKMRHALSSQWLSKPLLEGRLSMNTETSGTDLKSFPKTWLPSHLCTASLLSKMALRLLEKEKSLKEEEIGVKINITVAEMLYSLQWCEELEKPPTLIGECCEMLCSLGVSHEKVMDLSVHLPGLLELLYNRSKEDGSLWSLTANRFIHKRGAGPSELLPLTEDTEKYFPVTLGSLHTIQSLSAFLCPELKEELVIQCTARLMTCSASAVSCTDGGFGYLAIINSCLGSDSDLCQEILPGVLKVMLSWKDDQEDIFLFSSNVQDSSQSLIGLNVEMIRFLSILLKYLASSVSSLVDVDWDFIMCSMLAWLESACESSAAYHIPLVRLFACASCDLATEISHYFESVATSTTMSLPANLMSEWKEFFSEGIYSLMLPMLVRIAEEYKASETSHMSHVLKSLGRTLGYISKEQLLNHKLPAKFVAGQKTNLTDSLQSLLNTLAPLLLYRERSVQITVYHLLDKIMADLPGFDDEDLKSYGDEDEEPALSPPAALMSVLAIQEDLVESILKEIPVGEFAVIEPLKEEFCFVLGYLLTWKLILTFFKAASSQLRALYSQYLRKTKSLNKLLYNLFKLMPHNPVLPGQASDMPSKEPKTFFTEELQLAVKGTATVQQEVPHLACCVYHMTLKDLPAMVRLWWNGCEKRIFNVVDRFTTKYVSSVLSSQEISSVQLSTQVFDGMTVKARSTTREVIATYSVDDICIELIIQLPQNYPLGSITVESGRRVGVAVQQWRNWMLQLNTYLTHQNGSIMEGLALWKNNVDKRFEGVEDCMICFSVIHGSNYSLPKKACRTCKKKFHSECLYKWFTSSNKSTCPLCRETFF | E3 ubiquitin-protein ligase. Component of the ribosome quality control complex (RQC), a ribosome-associated complex that mediates ubiquitination and extraction of incompletely synthesized nascent chains for proteasomal degradation. Ubiquitination leads to vcp/p97 recruitment for extraction and degradation of the incomplete translation product. | A0JM49 |
P92846 | CYB_BOTAT | Ubiquinol-cytochrome-c reductase complex cytochrome b subunit | Bothrops | YINYKNMSHQHLLTLFNLLPVGSNISTWWNFGSMLLACLMIQIITGFFLAIHYTANINLAFSSIIHLSRDVPYGWIMQNTHAISASLFFICIYIHIARGFYYGSYLNKEVWLSGTTLLIILMATAFFGYVLPWGQMSFWAATVITNLLTAIPYLGTTLTTWLWGGFAINDPTLTRFFALHFILPFIIISMSSIHILLLHNEGSNNPLGTNSDID | Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis. | P92846 |
B9MDZ8 | PROB_ACIET | Gamma-glutamyl kinase | Diaphorobacter | MVSSVLRDARRIVVKVGSSLVTNEGRGLDEVAIGEWCRQLAALVRGQGGEPREVIMVSSGAIAEGMKRLGWSSRPGEIHELQAAAAVGQMGLAQMYETKLREQSMGSAQVLLTHADLADRERYLNARSTLLTLLRLGVVPVINENDTVVTDEIKFGDNDTLGALVANLVEADALVILTDQKGLYTADPRRDPQAQFVHEAQAGDAALEAMAGGAGSSIGKGGMITKILAAKRAAGSGASTVIAWGREPDVLLRLARGESIGTLLVAQTQKNQARKQWMVDHLQLRGSVTVDAGAAAKLREDGKSLLPIGMVAVEGDFVRGDVIAVRDAGGTEIARGLANYASAEARLLCRKPSAEFERLLGYAAEPEMVHRDNMVVLGAR | Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate. | B9MDZ8 |
B4SCV5 | FTSH_PELPB | ATP-dependent zinc metalloprotease FtsH | Pelodictyon | MSENPVKRPGKDGSRNKFKPVQEEGGTPGWFRSKGESPQGKFPGFLLFLMAGLLMLFVFLRFFSGTDAPEITYNEYKSVLSRALVTEVTVKTYEDKSAILSGKLNAPAQLQLIDKTTLQTNRFAVRVPSFTLEQADMLTEKGVRLKVEKGSSDLNTFLALFAPWIIFAALYFFLFRRMSGQNGAQAKNIFSFGKSRAKMVSEFEVKTTFKDVAGVDEAIEELQETVEFLTNPEKFQKIGGKIPKGVLLLGPPGTGKTLLAKAIAGEAKVPFFSISGADFVEMFVGVGAARVRDLFEQAKKNAPCIIFIDEIDAVGRSRGAGLGGGHDEREQTLNQLLVEMDGFTTNENVILIAATNRPDVLDSALLRPGRFDRQITIDKPDIRGREAILKIHTRNTPLDGDVDITVLAKSSPGFSGADLANLVNEAALLAARHEQVLITAVNFEQARDKILMGPERRSMFISDEQKKLTAYHEAGHVLVSIHTKGSDPIHKVTIIPRGRSLGLTAYLPLEDRYTHNREYLLAMITYALGGRVAEELVFQECSTGAANDIEKATDIARRMVRQWGMSESLGPINYGDSHKEVFLGKDYSHIREYSEETALQIDVEVRNIIMGCMENAKTVLSEQLAVLHRLAGILIEKESLNAREIQEITGPGQGALPNPVTA | Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins. | B4SCV5 |
Q9PT43 | LDHA_TRASE | L-lactate dehydrogenase A chain | Trachemys | MSVKELLIQNVHKEEHSHAHNKITVVGVGAVGMACAISILMKDLADELALVDVIEDKLRGEMLDLQHGSLFLRTPKIVSGKDYSVTAHSKLVIITAGARQQEGESRLNLVQRNVNIFKFIIPNVVKHSPDCTLLVVSNPVDILTYVAWKISGFPKHRVIGSGCNLDSARFRYLMGGKLGIHSLSCHGWIIGEHGDSSVPVWSGVNVAGVSLKALYPDLGTDADKEHWKEVHKQVVDSAYEVIKLKGYTSWAIGLSVADLAETIMRNLRRVHPISTMVKGMYGIHDDVFLSVPCVLGYSGITDVVKMTLKSEEEEKLRKSADTLWGIQKELQF | Interconverts simultaneously and stereospecifically pyruvate and lactate with concomitant interconversion of NADH and NAD(+). | Q9PT43 |
Q2W4Q8 | ISPDF_MAGSA | null | Magnetospirillum | MAKTVVLVVAAGRGRRFGGDLPKQYHDLAGRMVLRHTLAAFATNPEIGAVRAVIHPDDRQLYDMAAAGLNLLEPVHGGATRQDSVRLGLDSLKDLNPDKVLIHDGARPFIDHGTIGRVIRALDRHPGALPVVPVADTLKRGQDGFVADTVDRANLFRAQTPQGFRYAEIVAAHHAVIGNELTDDAAVAEKAGLAVELVNGAEDNVKITTGADLERARCLFDGPGEVRSASGYDVHRFDPAKDACWLCGVPVPHEAGLLGHSDADVGLHALTDAVLGAISAGDIGHHFPPTDARWKGAASDQFLAHAGSLVTAKGGRIVNVDVTIICERPKVGPHRAAMAARVAEILGISQDRVSVKATTTEGLGFTGRKEGIAAQAMASVWLPR | Bifunctional enzyme that catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP) (IspD), and catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP) (IspF). | Q2W4Q8 |
Q8E8K8 | CYSA2_SHEON | Sulfate-transporting ATPase 2 | Shewanella | MSIHIQQVNKHFGNFVAVDSVNLEIKTGELTALLGPSGSGKTTLLRIIAGLEQADSGIVKFNGEDITTQHVSERGVGFVFQHYALFKHMTVFENVAYGLTVRPRKTRPSKAEIAEKVHSLLKLVQLDWTADRYPSQLSGGQRQRIALARALAVEPKVLLLDEPFGALDAKVRAELRRWLRRLHDEINVTTVFVTHDQEEALEVADKIVVMNKGRIEQQGTPEEVYDTPSNPFVYEFLGNVNLFHARVKHGHSTIGNIHIPSPEHAGGEEQQGLAYVRPHEIEVLTQPTENAIKVNLDLVTIVGPVARLEVLTEIDEQLIHVELSKVQFKQLGISKGDNAWIQPRYSKVFLGEGI | Part of the ABC transporter complex CysAWTP involved in sulfate/thiosulfate import. Responsible for energy coupling to the transport system. | Q8E8K8 |
Q9PQT8 | RNC_UREPA | Ribonuclease III | Ureaplasma | MDNKKFLDFLKQNRIEPKNLSIYLEALTHKSYANEHKLTKNYQRLEFLGDACVEWVISNFIFNYKIKDNEKMRSLDEGEMTRARSNMVRSEILSYAAKDLGLTDFLMIGVGLEQDQSARMEKIYEDIFEAFIGAVAQDQGIKKVSLILEKTLIKYFREGQINYQKDYKTIFQEQAQRINKKPIMYKLVRNEGDKKEVHLVWNDLIYGIGIASTRKEAEILAAKNAILKLDDYTKKA | Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the organism. | Q9PQT8 |
B5F101 | RLMC_SALA4 | 23S rRNA(m5U747)-methyltransferase | Salmonella | MQCALYDAGRCRSCQWITQSVNEQLSAKTADLHRLLAGLPVEQWCAPTGGPEQRFRNKAKMVVSGSVEKPLFGMLHRDGTPVDLCGCPLYPASFAPVFSALKPFIARAGLTPYNVARKRGELKYLLLTESQFDGGMMLRFVLRSETKLTQLRAALPWLRAQLPQLKVITANIQPVHMAIMEGETEIYLTDQQALAERFNDVPLWIRPQSFFQTNPTVASRLYATARDWVGQLPVRHMWDLFCGVGGFGLHCATPQMQLTGIEIAPEAIACAKQSAAELGLTRLHFQALDSTQFATAQGETPDLVLVNPPRRGIGKPLCDYLAQMAPRFIIYSSCNAQTMAQDIRHLPNYRIQRVQLFDMFPHTAHYEVLTLLCRL | Catalyzes the formation of 5-methyl-uridine at position 747 (m5U747) in 23S rRNA. | B5F101 |
Q8X560 | USPC_ECO57 | Universal stress protein C | Escherichia | MSYSNILVAVAVTPESQQLLAKAVSIARPVKGHISLITLASDPEMYNQLAAPMLEDLRSVMQEETQSFLDKLIQDAGYPVDKTFIAYGELSEHILEVCRKYHFDLVICGNHNHSFFSRASCSAKRVIASSEVDVLLVPLTGD | Required for resistance to DNA-damaging agents. | Q8X560 |
C4ZRY8 | OPGC_ECOBW | Glucans biosynthesis protein C | Escherichia | MNPVPAQREYFLDSIRAWLMLLGIPFHISLIYSSHTWHVNSAESSLWLTLFNDFIHSFRMQVFFVISGYFSYMLFLRYPLKKWWKVRVERVGIPMLTAIPLLTLPQFIMLQYVKGKAESWPGLSLYDKYNTLAWELISHLWFLLVLVVMTTLCVWIFKRIRNNLENSDKTNKKFSMVKLSVIFLCLGIGYAVIRRTIFIVYPPILSNGMFNFIVMQTLFYLPFFILGALAFIFPHLKALFTTPSRGCTLAAALAFVAYLLNQRYGSGDAWMYETESVITMVLGLWMVNVVFSFGHRLLNFQSARVTYFVNASLFIYLVHHPLTLFFGAYITPHITSNWLGFLCGLIFVVGIAIILYEIHLRIPLLKFLFSGKPVVKRENDKAPAR | Necessary for the succinyl substitution of periplasmic glucans. Could catalyze the transfer of succinyl residues from the cytoplasmic side of the membrane to the nascent glucan backbones on the periplasmic side of the membrane. | C4ZRY8 |
Q8EST0 | IDI2_OCEIH | Type 2 isopentenyl diphosphate isomerase | Oceanobacillus | MEKGINQRKTEHIRLCLTGNVEGVNKSTGLEGINFIHNALPEIDFADISLESSFLGKQLKAPFLVSSMTGGSELATKINQNLAIAAEEKGWALAIGSTRAFLESDQHKESFLIRNQAPTAPLIVNIGAVQLNYGYGPEECQRIIDKTNADSIVLHLNSLQEAVQDGGDLNFKDLLPKIEQVCKQVKAPVGVKEVGFGIDGEVARRLYDAGISYIDVAGAGGTSWSQVEKLRSKDPLNKAAAEAFNNWGTPTKDCLVSVRGELPEAPLVASGGMKTGVDAAKAITIGADVVGFARHLLKAAMETPEDVIRTMEQLELELKMTMFGIGAVNLEELKNTSRVSIMGQSLMDK | Involved in the biosynthesis of isoprenoids. Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its allylic isomer, dimethylallyl diphosphate (DMAPP). | Q8EST0 |
Q0HXU9 | RLMH_SHESR | rRNA (pseudouridine-N3-)-methyltransferase RlmH | Shewanella | MKLQLIAVGTRMPDWVTRGFEEYQRRFPRDMALELIEIPAGKRGKNADIVRILQKEGEQMLAAIPKGNHIVTLDLPGKNWTTPELATAMNKWQLDGRDVSLLVGGPEGLAPACKEAAHQSWCLSALTLPHPLVRIVVAESLYRAWSVNNNHPYHRE | Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA. | Q0HXU9 |
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.