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 |
|---|---|---|---|---|---|---|
Q2NTI8 | RUVB_SODGM | Holliday junction ATP-dependent DNA helicase RuvB | Sodalis | MIEADRLMSAAAVTGEEVIDRAIRPKKLEDYIGQPHVLEQMEIFIQAAKMRGDALDHLLISGPPGLGKTTLANIVANEMGVNLRTTSGPVLEKAGDLAAMLTSLEPHDVLFIDEIHRLSPVVEEVLYPAMEDYQLDIMIGEGPAGRSIKIELPPFTLVGATTRAGSLTPPLRDRFGIVQRLEFYQTGDLQHIVSRSAVCLALNITEGGAREIARRARGTPRIANRLLRRVRDFAEVRAAGHITDDVAVSALNMLNVDTEGFDFMDRKLLLAIIDKFVGGPVGLDNLAAAIGEERETIEDVLEPFLIQQGFIQRTPRGRIA... | 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. | Q2NTI8 |
B0T2D7 | RL6_CAUSK | 50S ribosomal protein L6 | unclassified Caulobacter | MSRIGKKAVAIPSGVNITLDGQTVTVKGPKGQLSWTIAEEITISQEGSDLLLVARDDSKRAKSMWGLSRTLVANMVQGVTTGFEETLELVGVGYRAAMKGDALSIQLGFSHDVNVEAPAGVTFAVPKQTEIKIAGADKQAVGEIAAKIRRIRPPEPYKGKGVRYAGEKVRRKEGKKK | 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. | B0T2D7 |
P01190 | COLI_BOVIN | Met-enkephalin | Bos | MPRLCSSRSGALLLALLLQASMEVRGWCLESSQCQDLTTESNLLACIRACKPDLSAETPVFPGNGDEQPLTENPRKYVMGHFRWDRFGRRNGSSSSGVGGAAQKREEEVAVGEGPGPRGDDAETGPREDKRSYSMEHFRWGKPVGKKRRPVKVYPNGAEDESAQAFPLEFKRELTGERLEQARGPEAQAESAAARAELEYGLVAEAEAEAAEKKDSGPYKMEHFRWGSPPKDKRYGGFMTSEKSQTPLVTLFKNAIIKNAHKKGQ | Endogenous opiate. | P01190 |
A8F5H5 | GATB_PSELT | Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B | Pseudothermotoga | MSFKTIVGLEIHVQLMTKTKAFCSCRADVFDLPPNTAICPVCTGQPGALPTVNSTMIDYAIKIALALNCNIHEYSRFDRKNYFYPDLPKGYQITQYFYPIATSGYMDIDVDGQTKRIRIRRLHIEEDAGKLIHEGDSITQAQYSLVDMNRCGVPLVEIVTEPDLSSPKEARIFVEKLRSILRYLEVSSGDMEKGALRCDANISIYDESAHLQSNRVEVKNMNSFRFIEKALEYEQQRIIEALKNNEDVEKETRGWDIATKMTVSMRGKEEESDYRYFPEPDIPPVIVPVERIEEIKRSLVELPDEKIERFVSVYGIPKYD... | Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated ... | A8F5H5 |
O04921 | HEMH2_ARATH | Protoheme ferro-lyase 2 | Arabidopsis | MNCPAMTASPSSSSSSSYSTFRPPPPLLPQLSNDSQRSVVMHCTRLPFEAFAATSSNRLLGKHSLPLRAALVTSNPLNISSSSVISDAISSSSVITDDAKIGVLLLNLGGPETLDDVQPFLFNLFADPDIIRLPPVFQFLQKPLAQFISVARAPKSKEGYASIGGGSPLRHITDAQAEELRKCLWEKNVPAKVYVGMRYWHPFTEEAIEQIKRDGITKLVVLPLYPQFSISTSGSSLRLLERIFREDEYLVNMQHTVIPSWYQREGYIKAMANLIQSELGKFGSPNQVVIFFSAHGVPLAYVEEAGDPYKAEMEECVDLI... | Catalyzes the last step of heme biosynthesis by inserting ferrous iron into protoporphyrin IX to produce protoheme. Produces heme for photosynthetic cytochromes, and for proteins involved in abiotic and biotic stress responses . May play a role in the quality control of individual chloroplasts during photo-oxidative st... | O04921 |
P29174 | CSDE1_CAVPO | Protein UNR | Cavia | FGFINYEVGDSKKLFFHVKEVQDGIELQAGDEVEFSVILNQRTGKCSACNVWRVCEGPKAVAAPRPDRLVNRLKNITLDDASAPRLMVLRQPRGPDNSMGFGAERKIRQAGVID | RNA-binding protein involved in translationally coupled mRNA turnover. Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain. Required for efficient formation of stress gr... | P29174 |
Q38JA7 | KDM5C_CANLF | [histone H3]-trimethyl-L-lysine(4) demethylase 5C | Canis | MEPGSDDFLPPPECPVFEPSWAEFRDPLGYIAKIRPIAEKSGICKIRPPADWQPPFAVEVDNFRFTPRIQRLNELEAQTRVKLNYLDQIAKFWEIQGSSLKIPNVERRILDLYSLSKIVVEEGGYEAICKDRRWARVAQRLNYPPGKNIGSLLRSHYERIVYPYEMYQSGANLVQCNTRPFDNEEKDKEYKPHSIPLRQSVQPSKFNSYGRRAKRLQPDPEPTEEDIEKNPELKKLQIYGAGPKMMGLGLMAKDKTLRKKDKEGPECPPTVVVKEESGGDVKVESTSPKTFLESKEELSHSPEPCTKMTMRLRRNHSNAQ... | Histone demethylase that specifically demethylates 'Lys-4' of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-9', H3 'Lys-27', H3 'Lys-36', H3 'Lys-79' or H4 'Lys-20'. Demethylates trimethylated and dimethylated but not monomethylated H3 'Lys-4'. Participates in transcri... | Q38JA7 |
Q034T9 | ALR_LACP3 | Alanine racemase | Lacticaseibacillus | MTIGNFRPATVLIDETAILHNIQHEVARLKKQTQLFAVVKADAYGHGMLRVARVAKAAGATGFCVAILDEALGLRKADYSEPVLVLGIVPSQYAAIAAAQTISLPVSSTEWLEQALPVLEAQPELPPLRIHLALDTGMGRIGFTEDQALKTAVAFVEAHPKQFVIEGVFTHFATADAPDDTYFKQQVDKFNHLVNLLPSRPRYVHVSNSATSLWHAACNGNMIRYGVAIYGLNPSGDAIPTTPFPLEPALSLKSELTYCKQVHAGDGISYGVTYRAKGDEFIGTVPIGYADGWLRRLQGFHVLVDGQYCEIVGRICMDQF... | Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids. | Q034T9 |
B1VAC7 | KAD_PHYAS | Adenylate monophosphate kinase | 16SrXII (Stolbur group) | MILILLGPPGIGKGTQAAVLSDLLKLQHVATGDIFRKNFQENTPLGKESKKFINKGLLVPDEITNQMIADYLSQIVPHSNFLLDGFPRNVFQAQFLETFFTKSNLHLNKVIYFNAFKQDLMKRIEGRRICSHCGKVYHLDNLPPKIEGICDKDQKKLIQREDDKPNTFLKRLKVFNQETLHLVEYYRSKKQLFEVDGMQNIQQVTQKILKVLETEQK | 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. | B1VAC7 |
A4WEK3 | MUG_ENT38 | Mismatch-specific uracil DNA-glycosylase | Enterobacter | MINDILAPGLRVVFCGINPGKSSAHTGFHFAHPGNRFWKVIHQAGFTDKLLKPEEEQHLLDTRCGITMLVERPTVQANEVNLHELRSGGRELVKKIEDYQPAALAILGKQAYEQAFSQRGAQWGKQRITIGMTQVWVLPNPSGLNRATLDKLVEAYRELDEALVVRGR | Excises ethenocytosine and uracil, which can arise by alkylation or deamination of cytosine, respectively, from the corresponding mispairs with guanine in ds-DNA. It is capable of hydrolyzing the carbon-nitrogen bond between the sugar-phosphate backbone of the DNA and the mispaired base. The complementary strand guanin... | A4WEK3 |
Q9KNV2 | AROB_VIBCH | 3-dehydroquinate synthase | Vibrio | MERITVNLGERSYPISIGAGLFANPALLSLSAKQKVVIVTNHTVAPLYAPAIISLLDHIGCQHALLELPDGEQYKTLETFNTVMSFLLEHNYSRDVVVIALGGGVIGDLVGFAAACYQRGVDFIQIPTTLLSQVDSSVGGKTAVNHPLGKNMIGAFYQPKAVVIDTDCLTTLPAREFAAGMAEVIKYGIIYDSAFFDWLEAQMEALYALDEQALTYAIARCCQIKAEVVAQDEKESGIRALLNLGHTFGHAIEAHMGYGNWLHGEAVSAGTVMAAKTAQLQGLIDASQFERILAILKKAHLPVRTPENMTFADFMQHMMR... | Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ). | Q9KNV2 |
E7Q3U9 | MPS2_YEASB | Monopolar spindle protein 2 | Saccharomyces | MSNGAFDAIFEYAWGQIDKPISGDFIYGKDLPKLIEIIENIFQKAQKSGSYELRLPLFSEINKDLFRTFSNTKTFFKIHKEEFDDIFFNLVNHPLREILENAFIGVDSIPSDFIVSMNLNSPSKFLVENKNKNTEGAGISTPRKKLTESPIKLLSRKNIGKALEVQVEELKRELTAKQSLLQENERQVSELKIRLETYQEKYASIQQRFSDLQKARQVEDNQNSSRTSDPGSPLVTGIDQKAILEEFRRRLQRQTDTISFLKDQIRRERGLNCSNDKVSHSKRKHATTDGDGTFKNFISAVPSNIWVKATIRIIVCFALL... | Component of the spindle pole body (SPB) required for insertion of the nascent SPB into the nuclear envelope and for the proper execution of spindle pole body (SPB) duplication. | E7Q3U9 |
B8I5M9 | RL1_RUMCH | 50S ribosomal protein L1 | Ruminiclostridium | MFRGKKYQESSKLIDRLKLYEPSEALELAQKTAKAKFDETIEVHIKLGVDSRHADQQVRGAVVLPHGTGKKVRVLVFAKGDKAKEAEQAGADFVGGEELISKIQNENWFDYDVVVATPDMMGVVGRLGKVLGPKGLMPNPKAGTVSMDVAKAIADIKAGKIEYRLDKTNIIHCPIGKASFGNEKLMDNFRTLLGAIIKAKPAAAKGQYLKSVVVTSTMGPGIKINPLRVE | Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA. | B8I5M9 |
Q030J2 | FABZ_LACLS | Beta-hydroxyacyl-ACP dehydratase | Lactococcus cremoris subsp. cremoris | MTEVNINVTEIMEALPHRYPFLLVDRVIDIADDEITAIKNVTINEEFFQGHFPQYPVMPGVLIMEALAQAAGVLELSKPENKGKLVFYAGMDNVKYKKQVTPGDQLVLHAKFIKRRGPIAVVEAEATVDGKLAAKGTLTFALGK | Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs. | Q030J2 |
C1C5D8 | TIG_STRP7 | PPIase | Streptococcus | MSVSFENKETNRGVLTFTISQDQIKPELDRVFKSVKKSLNVPGFRKGHLPRPIFDKKFGEESLYQDVMNALLPNAYEAAVKEAGLEVVAQPKIDVTSMEKGQDWVITAEVVTKPEVKLGDYKNLEVSVDVEKEVTDADVEERIERERNNLAELVIKEAAAENGDTVVIDFVGSIDGVEFDGGKGENFSLGLGSGQFIPGFEDQLVGHSAGETVDVIVTFPEDYQAEDLAGKEAKFVTTIHEVKAKEVPALDDELAKDIDEEVETLADLKEKYRKELATAKEEAYKDAVEGAAIDTAVENAEIVELPEEMIHEEVHRSVNE... | Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase. | C1C5D8 |
P39652 | DEXT_ARTSD | Endodextranase | Arthrobacter | MPGTGLGRLAKRMTAAAAVFFISTSAVLPAQAATAPAAAPPGVPAALKAERAITTVDNGNLHTWWHDNGVFSPATPTQSSEVRRSSFYDVQVAQANQPQKLYDAFSYMSIPRSGKGKIGYTEEDGAEFSSDARLTMSWSSFEYAKDVWVEVSLRTGQTISSADQVQIRPSSYNFEKQLVDADTVRIKVPYSDAGYRFSVEFEPQLYTAYNDMSGDSGKLTTEAAGNRPIHTEPRNSMMVFAEPKLRGEQKERLVPTEESGSIHYPEPGEVRNLNSVSEEIIYFRPGTYSMGPDYHAVLPANVKWVYLAPGAYVKGAFRFL... | Efficiently decomposes water-insoluble glucan as well as dextran. | P39652 |
Q8NCD3 | HJURP_HUMAN | Up-regulated in lung cancer 9 | Homo | MLGTLRAMEGEDVEDDQLLQKLRASRRRFQRRMQRLIEKYNQPFEDTPVVQMATLTYETPQGLRIWGGRLIKERNEGEIQDSSMKPADRTDGSVQAAAWGPELPSHRTVLGADSKSGEVDATSDQEESVAWALAPAVPQSPLKNELRRKYLTQVDILLQGAEYFECAGNRAGRDVRVTPLPSLASPAVPAPGYCSRISRKSPGDPAKPASSPREWDPLHPSSTDMALVPRNDSLSLQETSSSSFLSSQPFEDDDICNVTISDLYAGMLHSMSRLLSTKPSSIISTKTFIMQNWNSRRRHRYKSRMNKTYCKGARRSQRSS... | Centromeric protein that plays a central role in the incorporation and maintenance of histone H3-like variant CENPA at centromeres. Acts as a specific chaperone for CENPA and is required for the incorporation of newly synthesized CENPA molecules into nucleosomes at replicated centromeres. Prevents CENPA-H4 tetramerizat... | Q8NCD3 |
Q9FFQ5 | FLS3_ARATH | Flavonol synthase 3 | Arabidopsis | MEMEKNQHISSLDIPVIDLSNPDEELVASAVVKASQEWGIFQVVNHGIPTELILRLLQVGMEFFELPETEKEAVAKPEDSLDIEGYRTKYQKDLEGRNAWVDHLFHRIWPPSRVNHKFWPKNPPEYIEVNEEYASHIKKLSEKIMEWLSEGLGLRHEALKEGLGGETIEYLMKINYYPPCPDPELVVGAPDHTDVNGITLLVANEALGLQAFKDNQWIDAEYTTSGIIVIIGDQFLRMSNGKYKSVEHRAKMDKEKTRISWPVFVESSLDQVFGPLPELITGDENVPKFKPYVYKDYKFRKLKKLLLD | Catalyzes the formation of flavonols from dihydroflavonols. Possesses low activity in vitro towards dihydrokaempferol and dihydroquercetin producing kaempferol and quercitin, respectively. | Q9FFQ5 |
B5ZS16 | ATP6_RHILW | F-ATPase subunit 6 | Rhizobium | MSNDPTHQFQIFKIVPIEIGGIDFSFTNASLFMAASAAVAVGFLYFATSNRAIVPGRSQSVAEMSYEFIANMLKEGAGKQGMKFFPLVFSLFMFVLTANLLGMFPYFFTITSQIIVTFALAILVIGTVLVYGFYKHGFHFLNVFVPSGVPGILLPLVVSIEIISFLSRPISLSVRLFANMLAGHITLKVFAGFVASLGALGAVGVGGAVLPLIMTVALTGLEFLVAFLQAYVFAVLTCMYLNDAIHPGGH | Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. | B5ZS16 |
Q494C4 | ATPG_BLOPB | F-ATPase gamma subunit | Candidatus Blochmannia | MSGLKEIRGKIDSIRNIQKIAKAMEMISVAKIYQTQRRMLISKPYAETIRKVIDHISSGTLEYKHSYFLERKIQSVGYWVVSTDRGLAGGLNINLLKTLLYDFNKWSNEGITIRLAIIGSKGASFLRSIKQTEIVSCVYGIGDAPKMSALIGSVRVMLQLYDNNQIDRLYLAYNKFINTLTQSPQILQILPIISSKNSILQTKYWDYLYEPDSKVLLNSLLQRYIESQVYQGVVENLASEQSARMMAMKTASDNGEVIINDLKLFYNKARQTKITEELTEIVSGASVI | 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. | Q494C4 |
Q8N5K1 | CISD2_HUMAN | Nutrient-deprivation autophagy factor-1 | Homo | MVLESVARIVKVQLPAYLKRLPVPESITGFARLTVSEWLRLLPFLGVLALLGYLAVRPFLPKKKQQKDSLINLKIQKENPKVVNEINIEDLCLTKAAYCRCWRSKTFPACDGSHNKHNELTGDNVGPLILKKKEV | Regulator of autophagy that contributes to antagonize BECN1-mediated cellular autophagy at the endoplasmic reticulum. Participates in the interaction of BCL2 with BECN1 and is required for BCL2-mediated depression of endoplasmic reticulum Ca(2+) stores during autophagy. Contributes to BIK-initiated autophagy, while it ... | Q8N5K1 |
Q4WJW8 | MCR1_ASPFU | Mitochondrial cytochrome b reductase | Aspergillus subgen. Fumigati | MFARQSLRVAQPLKQGFRKYSTEAPSKGKSSLAPIYLGVGLIGLGVGLYRYNSASAEAPPAERPKVFTGGDQGWVDLKLAQIENLSPNTKRLRFEFPDKEAVSGLHVASALLTKFKPQGAEKPVIRPYTPVSDEEQPGYLDLVVKVYPNGPMSEHLHSMNVDQRLEFKGPIPKYPWEANKHKHICLIAGGTGITPMYQLARKIFKDPEDQTKVTLVFGNVREEDILLKKELEELENTYPRRFRAFYLLDHPPKEWTGGKGYITKELLKTVLPEPKEENIKIFVCGPPGMYKSISGPKVSPTDQGELTGILAELGYSKDQV... | May mediate the reduction of outer membrane cytochrome b5. | Q4WJW8 |
Q8MR37 | KLFL_DROME | Krueppel-like factor luna | Sophophora | MDILPSGNIFSELERICTTGYYSSQPSIEDQWQQTCYELERYLRDEPKLQKKMHSNLDNPWDIFSTPARLLEELKIKEQHLDTISTTSSVSSNCSGTSWDSNGSQALSCSVLVKQERIDEEDDDVGCDDKLSVLLAAPPSAISPNPSIGSAGNMTPTSISNSSSISSSNSHSNSNGNTTGSSNIIASPLSSLGSGSTITVSSRNSSAPGIKVRVVQAKNHPGSNARMHLGHVQDFVLPTLTPPSSPESNLRSHNYAQQLEANDLAALIQQQQQQQQQQQQQQQQQQLNPQPGNSTPATAILRFTSQSNPTMTQLQQQQQQ... | Probable transcription factor that is required for cell differentiation . Essential for proper separation of the sister chromatids during early nuclear division cycles in the syncytial pre-blastoderm embryo . | Q8MR37 |
B5E5S7 | NADE_STRP4 | NH(3)-dependent NAD(+) synthetase | Streptococcus | MSLQETIIQELGVKPVIDAQEEIRRSIDFLKRYLKKHPFLKTFVLGISGGQDSTLAGRLAQLAMEELRAETGDDSYKFIAVRLPYGVQADEADAQKALAFIQPDVSLVVNIKESADAMTAAVEATGSPVSDFNKGNIKARCRMIAQYALAGFHSGAVIGTDHAAENITGFFTKFGDGGADILPLYRLNKRQGKQLLQKLGAEPALYEKIPTADLEEDKPGLADEVALGVTYAEIDDYLEGKTISPEAQATIENWWHKGQHKRHLPITVFDDFWE | Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source. | B5E5S7 |
Q8YAD1 | PTH_LISMO | Peptidyl-tRNA hydrolase | Listeria | MKLIAGLGNPGKKYERTRHNVGFMVVDELSFRHQTPWKKSKFNGMTSEIIVGGEKMILVKPLTFMNASGECIRPLMDYYNIPIEDVVIVYDDLDLPVGKIRLRQKGSAGGHNGMKSIIQHVKTQEFNRIRVGVSRPLKGEVINYVLGDFPKAEQPDIIAAIQKSADAIEDFAQTPFIEVMNKYNQK | The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis. | Q8YAD1 |
A8GQX8 | GATC_RICRS | Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit C | spotted fever group | MITKEAAQKIAKLARLKFEEDTVEKFFTQLSTIMDMIDILNEIDCKDIEPLTSVCNMNARMREDAVTSSDLSSELFDNVSGNSTQLAKEVKYFITPKVVE | Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated ... | A8GQX8 |
F1Q930 | T237A_DANRE | Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 4 protein homolog A | Danio | MCVTSRADKMPSVKPKKKKIKKEINEVEEPEAGPEPAIEMEGLESRRQSESREPLTPEPHDNPPLKKKKKKKTHTFENEGEQQDHPNGDVQESPTDGEEVTKKSKKKRKNKMMENQSHNELGVEEDDIITDVHAPISQRSLFSAPLSHSHPIGKVFVEKNRRFQATDLSHDHLEEYMEVRPMWNTRDVAMRVHSGFRIIGLFSHGFLAGYAVWNIIVVYVLAGEQMTTLPNLLQQYHSLAYPAQSLLYLLLAISTVSAFDRVNLAKASMALRGFLTLDPAALASFLYFAALILSLSQQMTSDRIHLYPTANETLWPPGLE... | Component of the transition zone in primary cilia. Required for ciliogenesis. | F1Q930 |
Q6N5A3 | RS18_RHOPA | RRP-S18 | Rhodopseudomonas | MAEAGARRPFFRRRKTCPFTGANAPKIDYKDSKLLMRYVSERGKIVPSRITAVSAKKQRELARAIKRARFLGLLPYVIR | 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. | Q6N5A3 |
B1J201 | YBEY_PSEPW | Endoribonuclease YbeY | Pseudomonas | MLELDLQRATDAATPDDAALRAWCELALRQRSADSEMTIRLVDEAEGRELNHTYRHKDYATNVLSFPADVPDELLDIPLLGDLVICVPVVEREAAEQGKSLQAHWAHLVIHGCLHLLGYDHIEDDEAEEMEALERELLAELGHPDPYADDENDSITH | Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA. | B1J201 |
Q13107 | UBP4_HUMAN | Ubiquitous nuclear protein homolog | Homo | MAEGGGCRERPDAETQKSELGPLMRTTLQRGAQWYLIDSRWFKQWKKYVGFDSWDMYNVGEHNLFPGPIDNSGLFSDPESQTLKEHLIDELDYVLVPTEAWNKLLNWYGCVEGQQPIVRKVVEHGLFVKHCKVEVYLLELKLCENSDPTNVLSCHFSKADTIATIEKEMRKLFNIPAERETRLWNKYMSNTYEQLSKLDNTVQDAGLYQGQVLVIEPQNEDGTWPRQTLQSKSSTAPSRNFTTSPKSSASPYSSVSASLIANGDSTSTCGMHSSGVSRGGSGFSASYNCQEPPSSHIQPGLCGLGNLGNTCFMNSALQCL... | Deubiquitinating enzyme that removes conjugated ubiquitin from target proteins . Deubiquitinates PDPK1 . Deubiquitinates TRIM21 . Deubiquitinates receptor ADORA2A which increases the amount of functional receptor at the cell surface . Deubiquitinates HAS2 . May regulate mRNA splicing through deubiquitination of the U4 ... | Q13107 |
Q6C7U1 | CCPR3_YARLI | Putative heme-binding peroxidase | Yarrowia | MNYPSVSEQKHRVFIIYSAYLRVQFRESARLAVSVRNKNYNLVRADLHNILPQKNTTVFKDGTLAPLLIRLAWHSCATYDKYTRTGGSNGATMRYHLEASDEGNVGLEVARLSLEPIKRKHPWITYADLWILAGVVSIEACKGPSIKWRDGRVDYEDDLLVPPNGRLPLGGGDASHVRTIFSRMGFNDQETVALIGAHSLGRLHHHRSGFDGPWTSNPAKCDNEFYKLLLGNVWTLVDSPTGRKQYVNSTGQVMMPSDMSLIEDANFRFWVDQYAVSEELWRDHFALAFEKLTELGR | Destroys radicals which are normally produced within the cells and which are toxic to biological systems. | Q6C7U1 |
P11415 | QOR_CAVPO | Zeta-crystallin | Cavia | MATGQKLMRAIRVFEFGGPEVLKVQSDVAVPIPKDHQVLIKVHACGINPVETYIRSGTYTRIPLLPYTPGTDVAGVVESIGNDVSAFKKGDRVFTTSTISGGYAEYALASDHTVYRLPEKLDFRQGAAIGIPYFTACRALFHSARAKAGESVLVHGASGGVGLAACQIARAYGLKVLGTAGTEEGQKVVLQNGAHEVFNHRDAHYIDEIKKSIGEKGVDVIIEMLANVNLSNDLKLLSCGGRVIIVGCRGSIEINPRDTMAKESTISGVSLFSSTKEEFQQFASTIQAGMELGWVKPVIGSQYPLEKASQAHENIIHSSG... | Does not have alcohol dehydrogenase activity. Binds NADP and acts through a one-electron transfer process. Orthoquinones, such as 1,2-naphthoquinone or 9,10-phenanthrenequinone, are the best substrates (in vitro). May act in the detoxification of xenobiotics. Interacts with (AU)-rich elements (ARE) in the 3'-UTR of tar... | P11415 |
Q62GY9 | ARAG_BURMA | Arabinose import ATP-binding protein AraG | pseudomallei group | MAAALRFDNIGKVFPGVRALDGISFDVQAGQVHGLMGENGAGKSTLLKILGGEYQLDSGSVLVDGRAMRFPSAAASIAAGVAVIHQELQYVPDLTVAENLLLGRLPSALGWVRKRDAQRFVRERLAAMGVDLDAQAKLRRLSIAQRQMVEICKALLRNARVIALDEPTSSLSHRETEVLFKLVDDLRRDGRALIYISHRMDEIYRLCDACTIFRDGRQVASHASLANVPRETLVRQMVGREISDIYHYAPRALGDVRLSARALEGDALRAGASFDVRAGEIVGFFGLVGAGRSELMRVIYGAQRRTGGALMLDGEPLDIR... | Part of the ABC transporter complex AraFGH involved in arabinose import. Responsible for energy coupling to the transport system. | Q62GY9 |
Q9VFP2 | RDX_DROME | Hh-induced MATH and BTB domain-containing protein | Sophophora | MFEPYVKIKKKRSVNEIYENENLEQQQHHLQQQQQQPATSDNCCCENGEPQNAPEVATATVAATSVAATSAAATVATGAAASSSSSGNCSRLQQLISTPPVLLRRSSLQQQQHQQQQHHPHTPAATATPPQQQQQQQAAPSVLQQHLGHLNYESGATAAAAATAAAAAATVATSRSGSATLAQHLATPSNILQAAFGSSNLQHILTRSAPSPSSSAISSNNCSSACAGNTHYNGGNSNSGSSSSNSNHHSNSIIASRLFGAASSSSSSSSSSASASSSSVAASSSSSSHHLHSHHSALTNSITNRINQSIRRHLNQQQHH... | Involved in segment polarity. In complex with gft/CUL3, promotes ubiquitination of ci and its subsequent degradation by the proteasome, which results in hh signaling attenuation. This regulation may be important during eye formation for proper packing of ommatidia into a hexagonal array. | Q9VFP2 |
Q5N8J3 | BBD1_ORYSJ | Bifunctional nuclease 1 | Oryza sativa | MEIINGPVLPRYAAPATGALTSDAKISGQLLRRVHLRRRACGLQGDHYRAARRFFGFPSERHARSGWVWPVCCSYGSSSDGDGAAAADYDASGEEFVNSSVMEAVELRSVSDGFVIKMRDGKNLRCVQNNPRVLRLRDSAPHHAIVLKMEDGSDLLLPIIVMETPSIMLLAALRNIRIPRPTIYNVVKEMTERMGYAVRLVRITEMVHDAYYSRLYLAKIGNEEETISLDLKPSDAINIAFRCKVPIQVNRRIAYNNGLKVVQPTPSESYVSSDQFQYTRLDRPDDQPCFEAQEFDLVRNMLVAAVEERYKDAAQYRDQL... | Bifunctional nuclease with both RNase and DNase activities. Involved in basal defense response. Participates in abscisic acid-derived callose deposition following infection by a necrotrophic pathogen. | Q5N8J3 |
C3PMV5 | CTAA_RICAE | Cytochrome aa3-controlling protein | spotted fever group | MQKSLITKWLCISCIMVIATIVIGGITRLTGSGLSIVEWRPVTGILPPFSFESWQSEFAKYKAFPEYNSVNYGITLSQFKFIYLLEFIHRLLGRITALIYIVPLIYFYFKDVIKNRDMLPYIIALLLFCIQGFIGWYMVKSGLLNSPYVSHFRLAFHLIIAVIIYHILFYQLIKNRCDILLILSQTDFKLPLIFSGIAITVVYVQIFLGALVAGLDAGLIYNSFPLMDDRFIPMEIKDNFFDLKNWYDPVFIQFIHRLVGYSVFLVVVVLIICLLKIEHPKLNKIAYFLMIVLFMQVSTGIITLLYSVPIIIASIHQLFA... | Catalyzes the conversion of heme O to heme A by two successive hydroxylations of the methyl group at C8. The first hydroxylation forms heme I, the second hydroxylation results in an unstable dihydroxymethyl group, which spontaneously dehydrates, resulting in the formyl group of heme A. | C3PMV5 |
Q04WF5 | RECF_LEPBJ | DNA replication and repair protein RecF | Leptospira | MFLKHLTLQNFRSYEELSLDFNSRLIFFVGDNGEGKTNLLEAICMLSWLKSFRESEDSNLIRWGSENYFLRGKIKGDQKESVLEVGFTAKPTVKRKLKFNQEEVKKRTDLIGKFITVLLTPMDLKIIEGGPAERRKFIDAFISSFDPFYLECLLEYNKILKHRNALLKTGISDASHLSIWDRKLIEKGVLILNKRKEIVFGLNSFYQPNLNKLSGGKDELEMIYGPNVKDKDEFVEKLGRNLGKDLRLGYTSVGIHRDDLFIGADKRDITEFGSQGQKRSTVIALKAATFNYYRNVLDTMPVLLIDDVIRELDVKRREYF... | The RecF protein is involved in DNA metabolism; it is required for DNA replication and normal SOS inducibility. RecF binds preferentially to single-stranded, linear DNA. It also seems to bind ATP. | Q04WF5 |
D0EL35 | CTC1_ARATH | Protein CONSERVED TELOMERE MAINTENANCE COMPONENT 1 | Arabidopsis | MENTTILTVKDLVNEGIAVTGASSLFSSAASHSSSESTSTNPKSHPGAVDSDFSRKFLTPLNYPTVIFGTVALPSETLKCPNRYCFRFTDGDLTICCDILGFEFRAIGSKICVLSWNFLPMNHSGGFLEIINWKFVDSGSLLSRCSGISSFPLIPSLYSSQNGDRKSRYSVCGVLESISPVSVVPCMDGVSSDSVNLPGFLVHVMACECKVYSRDAIDCGHAFERSVFVYFCGLEAASWHPVVMKLVGRNVALSGLKRKLVYVRGDSLLVFVTTENSVLHPPWLSKKGTVSKTVVDRRGNCGSYRGYVRGLYLKGKLVEM... | Component of the CST complex, a complex that binds to single-stranded DNA and is required to protect telomeres from DNA degradation. The CST complex binds single-stranded DNA with high affinity in a sequence-independent manner, while isolated subunits bind DNA with low affinity by themselves . Associates with enzymatic... | D0EL35 |
Q31TK2 | AMPA_SHIBS | Leucyl aminopeptidase | Shigella | MEFSVKSGSPEKQRSACIVVGVFEPRRLSPIAEQLDKISDGYISALLRRGELEGKPGQTLLLHHVPNVLSERILLIGCGKERELDERQYKQVIQKTINTLNDTGSMEAVCFLTELHVKGRNNYWKVRQAVETAKETLYSFDQLKTNKSEPRRPLRKMVFNVPTRRELTSGERAILHGLAIAAGIKAAKDLGNMPPNICNAAYLASQARQLADSYSKNVITRVIGEQQMKELGMHSYLAVGQGSQNESLMSVIEYKGNASEDARPIVLVGKGLTFDSGGISIKPSEGMDEMKYDMCGAAAVYGVMRMVAELQLPINVIGVL... | Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. | Q31TK2 |
B0SB37 | RL9_LEPBA | 50S ribosomal protein L9 | Leptospira | MKVVLQKDVLNLGDAGDVKEVADGYARNFLIPRRLAVRANDGNTKAAIHQKRLAELKRDKRVKVMKELSASIDGKTYEIKVKVGENDKLFGSVTANDIALAIKNTGVELDKRKLDLGEPIKSVGEFKIKVRLAEGVVPGIIVKVVGQA | Binds to the 23S rRNA. | B0SB37 |
Q7AHS5 | DJLA_ECO57 | Co-chaperone protein DjlA | Escherichia | MQYWGKIIGVAVALLMGGGFWGVVLGLLIGHMFDKARSRKMAWFANQRERQALFFATTFEVMGHLTKSKGRVTEADIHIASQLMDRMNLHGASRTAAQNAFRVGKSDNYPLREKMRQFRSVCFGRFDLIRMFLEIQIQAAFADGSLHPNERAVLYVIAEELGISRAQFDQFLRMMQGGAQFGGGYQQQSGGGNWQQAQRGPTLEDACNVLGVKPTDDATTIKRAYRKLMSEHHPDKLVAKGLPPEMMEMAKQKAQEIQQAYELIKQQKGFK | Regulatory DnaK co-chaperone. Direct interaction between DnaK and DjlA is needed for the induction of the wcaABCDE operon, involved in the synthesis of a colanic acid polysaccharide capsule, possibly through activation of the RcsB/RcsC phosphotransfer signaling pathway. The colanic acid capsule may help the bacterium s... | Q7AHS5 |
Q9HM60 | PDXT_THEAC | Pyridoxal 5'-phosphate synthase glutaminase subunit | Thermoplasma | MNIGVLGFQGDVQEHMDMLKKLSRKNRDLTLTHVKRVIDLEHVDALIIPGGESTTIYKLTLEYGLYDAIVKRSAEGMPIMATCAGLILVSKNTNDERVRGMGLLDVTIRRNAYGRQVMSFETDIEINGIGMFPAVFIRAPVIEDSGKTEVLGTLDGKPVIVKQGNVIGMTFHPELTGDTRLHEYFINMVRGRGGYISTADVKR | Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS. | Q9HM60 |
Q3SSS2 | IHFA_NITWN | Integration host factor subunit alpha | Nitrobacter | MTGTGKTVTRVDLCEAVYKKVGLSRTESSAFVELVLKEITDCLEKGETVKLSSFGSFMVRKKGQRIGRNPKTGTEVPISPRRVMVFKPSAILKQRINSNGAGGKTD | This protein is one of the two subunits of integration host factor, a specific DNA-binding protein that functions in genetic recombination as well as in transcriptional and translational control. | Q3SSS2 |
A0A0N9E2K8 | MMP21_DANRE | Matrix metallopeptidase-21 | Danio | MLTVIRRIFIIQTFIFITAEKIFHSRDHSDVLNNIHQAELITDTDTAQRFLSKYGFIKAAGSEESQLSESSGDLDFSLSLDLHEGGTTSGSSSSDLQFVSALRDFQRLSDLPVTGVFDDATKAAMNKPRCGVMDDDQELKDVTGSNSTRNHIRTSTNTSHNHEHQAPVRKKRHLSALLKNTSLQKRDVSKWTGHMAFSKSVLKWRLIGEGYSSQLSIQEQKYIFRLAFRMWSEISPLQFIEDLHSPLENIDIRLGFGTGRHLGCSQRFDGAGREFAHAWFLGDIHFDDDEHFTVPNTGSGISLLKVAVHEIGHVLGLPHI... | Plays a specialized role in the generation of left-right asymmetry during embryogenesis. May act as a negative regulator of the NOTCH-signaling pathway. | A0A0N9E2K8 |
P33256 | ATPF_MYCGA | F-type ATPase subunit b | Mycoplasma | MWSTRVKKLLLLSFNFLIISAIVSSCSIPEELQAKTIVNEFFPNFWVFVAHTIALSIIILLGIFLLWKPTKRFLAKRSELIQAEINNANEIKKQAQFLLDNAKKQKQNAELQAREIINLATNQAYRLKNDLETDAKRKANRIIENAHAEIIKQESILKRELEGRIVDVALEATSTLIQKNVAKEDHERLVNELLRNLD | Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0). | P33256 |
Q12SD4 | RSMH_SHEDO | rRNA (cytosine-N(4)-)-methyltransferase RsmH | Shewanella | MSQEFAHLSVLLKETVDGLNIQPDGIYIDGTFGRGGHSRHVLSHLGPNGRLIAIDRDPQAIEAAKQFADDPRFQIVHGGFGQLADYVAELGLVGKIDGVLLDLGVSSPQLDDAERGFSFLRDGPLDMRMDNSQGQTAAQWIARAEIEDMAWVFKTYGEEKNSRHIARCIAADREKTPFLRTKDLADLIARITKNKERNKHPATRVFQAIRIYINSELEQIDQALEGAVNVLAPHGRMSIISFHSLEDRMVKRFMRRHSQGESVPHGLPITEAEINKSKKLKTLGKAMKPSEIEVEQNPRARSSVLRVAERLDY | Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA. | Q12SD4 |
Q1J0B6 | RSMH_DEIGD | rRNA (cytosine-N(4)-)-methyltransferase RsmH | Deinococcus | MNTAPSPSDRPLSHALSHTPVLAAEVVAALAPAPGRVIVDGTLGGAGHTRLLLEAGASVIGIDQDPYALNRAREAQLPQLTVLEGNYRDMRELLAGIGVTQVDGVLLDIGVSSFQLDDAARGFSYHTDAPLDMRMAQSGESAAEVVNGYPEEELAAIIYEYGEERHSRRIARAIVQARTQAPIQSTVQLAEIIKRAYPGFSKGIHPARRTFQALRIHVNDELGALRDGLRAAEALLTPGGRLAVIAFHSLEDRIVKRFLRASPTLKSLTKRPVEASEEERGRNPRARSAKLRAAEKVAAPEGLPEVEV | Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA. | Q1J0B6 |
Q9RU19 | QUEA_DEIRA | Queuosine biosynthesis protein QueA | Deinococcus | MPDSTADPSTADEVLARLHFDLPEDRIAQTGAEPRDTSRLMVVGEQIKHRMFRDLPDLLRPSDLLVFNESRVIPARVLARKPVVNGFGGGQVEVLLLREEFDVGANVWSAYLKPAKRAGHELWLGENEATGHRAEVVGVLDDGARLLRFDHDIKPHLDEIGRLPLPPYINAGDSDETWRERYQTVYAKTPGSVAAPTAGLHFTPELLARLDEMGVERASVTLHVGAGTFKPIQGPVADHVMHAERYEVSETNAAAITRAKAEGRRVVAVGTTTVRTLESAWDGAAVRAGAGETRIFITPGTRVEVPDLLITNLHLPGSTL... | Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA). | Q9RU19 |
Q3B286 | HIS5_CHLL3 | ImGP synthase subunit HisH | Pelodictyon | MVFIADYGAGNLRSVQKAFDYLGIPATVSSDPAKMAGCRKVVLPGVGAFGQAIEALDRLGFTDALSEHVDKGGHLFGICLGMQLMLSDSEEMGSHRGLGLIPGSVRHFQSDSDKIPQIGWNSIDLKQESVLFRGIADHSFFYFVHSYYCDPLEASSIASTTWFAGKNFCSAIEKNGIFAVQFHPEKSSEAGLQVLRNFAEC | IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisH subunit catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the synthesis of IGP and AICAR. The resulting ammonia molecule is channeled to the active site of HisF. | Q3B286 |
A4QLI0 | ATPF_LOBMA | ATPase subunit I | Lobularia | MKNLTDSFVYLGHWPAAGSFGFNTDILATNPINLSVVFGVLIFFGKGVLNDLLDNRKQRILNTIRNSEELREGAIQQLENARARLRKVEAEADQFRVNGYSEIEREKLNLINSTSKTLKQLENYKNETILVEQQRTINQVRERIFQQALQGAIGTLNSCLSNELHLRTINANIGMFGTMKKITD | Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0). | A4QLI0 |
Q7VBM8 | SYT_PROMA | Threonyl-tRNA synthetase | Prochlorococcus | MPIITLPDGAQRTYSTPVTIAEIAAEIGPGLAKAAIAGEVNGELVDTCIPISVNANINIITSKNKEGIDIIRHSFAHLLGHAIKQLYPDAKMAIGPVIENGFYYDIAYKDTFSLDDLNQIELRIKELIKQDYDVVVEEVSKEKARKTFLDRDEAYKVQIIDEIPDNETIKLYKHQEYIDMCRGPHVPNTKHLRAFSLMKVSGAYWRGDSNNEMLQRIYGTAWGSTKELEAYLLKIEEAEKRDHRKIGKKLDLFHTQEEAPGMIFWHPKGWSIYQVLESFIRETLILNDYKEIKTPQTVDRSLWEKSGHWDKFKEDMFTTT... | Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr). | Q7VBM8 |
Q9BYR6 | KRA33_HUMAN | Keratin-associated protein 3.3 | Homo | MDCCASRGCSVPTGPATTICSSDKSCRCGVCLPSTCPHTVWLLEPTCCDNCPPPCHIPQPCVPTCFLLNSCQPTPGLETLNLTTFTQPCCEPCLPRGC | In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of ha... | Q9BYR6 |
A2BW66 | CCSA_PROM5 | Cytochrome c biogenesis protein CcsA | Prochlorococcus | MIFDGFIKNLIYDPVSTLGILIFYFLLINLPISLLALFNKKSSSFVRFFTILINLFIALQLIFRWILSGHFPISNLYESLYFLVWGISLGQLLVEKEYPNPIIPVIAIPIELLTIAFACFVLPDDLKLSSNLVPALRSSWLIMHVSVVMLSYAALIIGSLLSASVLFINNRQPLQLRSSSTGIGGFRMSNEYSGNNFNEPINFTHTEELDTLSYRSILVGFVLLTLGLITGAIWANEAWGTWWSWDPKETWAFISWLFYAAYLHMRISRGWQGRRPALFATSGFFVVLICYLGVNFLGIGLHSYGWIFGILN | Required during biogenesis of c-type cytochromes (cytochrome c6 and cytochrome f) at the step of heme attachment. | A2BW66 |
Q87TN7 | TRKH_VIBPA | Trk system potassium uptake protein TrkH | Vibrio | MQFRSIIRIVGLLLALFSVTMLAPALVALLYRDGAGVPFVTTFFVLLFCGAMCWFPNRRHKHELKSRDGFLIVVLFWTVLGSAGSLPFLIADNPNISVTDAFFESFSALTTTGATVIVGLDELPKAILFYRQFLQWFGGMGIIVLAVAILPVLGIGGMQLYRAEIPGPVKDTKMTPRIAETAKALWYIYLSLTIACAVAFWLAGMTPFDAISHSFSTIAIGGFSTHDASMGYFDSYAINLITVVFLLISACNFTLHFAAFASGGVHPKYYWKDPEFRAFIFIQVLLFLVCFLLLLKHHSYTSPYDAFDQALFQTVSISTT... | Low-affinity potassium transport system. Interacts with trk system potassium uptake protein TrkA and requires TrkE for transport activity. Selective for permeation of potassium ion and rubidium ion over smaller ions such as natrium or litium. | Q87TN7 |
Q8ES79 | GATC_OCEIH | Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit C | Oceanobacillus | MAEISKDQVKHVAHLARLELDDEAVEKMSDELSAIIDFAEQLNELDTDSVEPTTHVLNLKNVMRKDEPKKWISQEDALRNAPDHKDGQIRVPSILE | Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated ... | Q8ES79 |
Q63TW1 | SSUB_BURPS | Aliphatic sulfonates import ATP-binding protein SsuB | pseudomallei group | MTGTTLAATYGPISGADLEAELAQPRIADGDAQDAAVYERDGGAHAPPDGDRADVRRAAGAGDASVRLTRVSKRYGERAVLADVDLSIGRGSFVSIVGRSGCGKSTLLRLVAELETPSAGTLVKRGDGGGALDTRIMYQEARLLPWKTVLQNVMLGLGRRAKDDARAVLDEVGLLARANDWPAQLSGGQRQRVALARALVHRPQLLLLDEPLGALDALTRIEMHALIERLWREHRFTALLVTHDVQEAVALADRVLLIEAGRIAFDQRVPLDRPRARASAAFAALEDRVLQRVLTGSDAAPAAPNAAGPEGASRGRAAPA... | Part of the ABC transporter complex SsuABC involved in aliphatic sulfonates import. Responsible for energy coupling to the transport system. | Q63TW1 |
A3PV34 | RL1_MYCSJ | 50S ribosomal protein L1 | unclassified Mycobacterium | MSKNSKAYREAAEKVDKTKLYSPLEAAKLAKETSSKKQDATVEVAIRLGVDPRKADQMVRGTVNLPHGTGKTARVAVFAVGDKAEQAAAAGADIVGSDDLIEQIQGGMLDFDAAIATPDQMAKVGRIARILGPRGLMPNPKTGTVTADVAKAVSDIKGGKINFRVDKQANLHIVIGKASFDEKKLAENYGAALDEILRAKPSASKGRYLKKIVVSTTTGPGIPVDPQVTRNFAEA | Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA. | A3PV34 |
P68283 | CRYAA_PEDCA | Alpha-crystallin A chain | Pedetes | MDVTIQHPWFKRALGPFYPSRLFDQFFGEGLFEYDLLPFLSSTISPYYRQSLFRTVLDSGISEVRSDRDKFVIFLDVKHFSPEDLTVKVQEDFVEIHGKHNERQDDHGYISREFHRRYRLPSNVDQSALSCSLSADGMLTFSGPKVQSGLDAGHSERAIPVSREEKPSSAPSS | Contributes to the transparency and refractive index of the lens. Acts as a chaperone, preventing aggregation of various proteins under a wide range of stress conditions. Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA. | P68283 |
O25340 | MURC_HELPY | UDP-N-acetylmuramoyl-L-alanine synthetase | Helicobacter | MLETPKVLLKNLQDCKIHFIGIGGIGISGLAKYLKAQGATISGSDIAISPSVKYLKALGVEINIPHDPKAINNQDVIIHSAIIKEDNKEIQRAKELEIPILSRKDALYSILKDKRVFSVCGAHGKSSITAMLSAICPSFGAIIGAHSKEFDSNVRESANDSLVFEADESDSSFLFSNPYAAIVPNTEPEHLEHYGHDLERFFFAYEYFLDHAQKRVIYKEDPFLKNYSKNAIVLEKKDIYNIQYILKDGEPYTSFELKDLGAFLVWGLGEHNATNASLAILSALDELHLEEIRNNLLNFKGIKKRFDILQKNALILIDDY... | Cell wall formation. | O25340 |
W5QJZ5 | DIOX4_RUTGR | 2-oxoglutarate-dependent dioxygenase 4 | Ruta | MAPTKDSVIHMGAESWDEISEFVTKKGHGVKGLSELGIKTLPKQFHQPLEERFSEKKILERASIPLIDMSKWDSPEVVKSICDAAEHWGFFQIVNHGVPLETLQRVKEATHRFFALPAEEKNKYSKENSPINNVRFGSSFVPHVEKALEWKDFLSMFYVSEEETNTYWPPICRDEMLEYMRSSEVLIKRLMEVLVVKGLKVKQIDEIREPMLVGSRRINLNYYPKCPNPELTLGVGRHSDISTFTILLQDEIGGLHVRKLDDTGNTWVHVTPISGSLIINIGDALQIMSNGRYKSIEHMVVANGTQDRISVPLFVNPKPQ... | 2-oxoglutarate (OG)- and Fe(II)-dependent dioxygenase (2OGD) involved in scopoletin and umbelliferone biosynthesis . Converts feruloyl CoA into 6'-hydroxyferuloyl CoA, and p-coumaroyl CoA into 2,4-dihydroxycinnamoyl-CoA . Has no activity with cinnamic acid, caffeic acid, p-coumaric acid, ferulic acid, cinnamoyl-CoA and... | W5QJZ5 |
Q8CG03 | PDE5A_MOUSE | cGMP-binding cGMP-specific phosphodiesterase | Mus | MERAGPNSVRSQQQRDPDWVEAWLDDHRDFTFSYFIRKATRDMVNAWFSERVHNIPVCKEGIRAHTESCSCSLQQSPHADNTTPGAPARKISASEFDRPLRPIVVKDSEGTVSFLSDSGKKEQMPLTPPRFDSDEGDQCSRLLELVKDISSHLDVTALCHKIFLHIHGLISADRYSLFLVCEDSSKDKFLISRLFDVAEGSTLEEASNNCIRLEWNKGIVGHVAAFGEPLNIKDAYEDPRFNAEVDQITGYKTQSILCMPIKNHREEVVGVAQAINKKSGNGGTFTEKDEKDFAAYLAFCGIVLHNAQLYETSLLENKRN... | Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides. This phosphodiesterase catalyzes the specific hydrolysis of cGMP to 5'-GMP. Specifically regulates nitric-oxide-generated cGMP. | Q8CG03 |
A1WPV4 | DCTP_VEREI | Solute-binding protein Veis_3954 | Verminephrobacter | MPSTRPLPRPSSRSLRRLALGLGLAFGLGATAAAQTTMRINISTAQNSHQGVAIDTFAKEVEKRTGGRYKVQTFYNAALGAERESVEAVQLGTHELTFSSSGPIPNFVPETKILDVPFLFRDKAHARAVLDGPIGQELLTRFDGKGFKALAWAENGFRHMSNSKRAVKEPGDLKGLKMRTMENPVHIAAYKGFGIVTTPMAFSEVFTALQQGTVDGQENPLSVIISAKFDQVQKHLTLTGHVYSPALFLMNKALFDKLPAADQQAFIDAARQGAKLNRARVDEDDAKGVADLRAKGMTVIDNIDKARFVAALAPVNAQFE... | Solute-binding protein that binds (R)-pantoate and D-erythronate (in vitro) . Probably part of a tripartite ATP-independent periplasmic (TRAP) transport system that mediates solute transport into the cytoplasm. | A1WPV4 |
B2IJ38 | HYPA_BEII9 | Hydrogenase maturation factor HypA | Beijerinckia | MHELSLCESVIETIMDNVRTHHFSQVRRVRLTVGRFAGVETEALRFSFDVVARGTLVEGAELELLEEPGAAWCFDCSETVPLMDRLDPCPRCGGTRLHPTAGTDVMIKDLEVI | Involved in the maturation of [NiFe] hydrogenases. Required for nickel insertion into the metal center of the hydrogenase. | B2IJ38 |
Q5VJ50 | CYB_LEPRU | Ubiquinol-cytochrome-c reductase complex cytochrome b subunit | Lepilemur | MTNTRKNHPLMKIINNSFIDLPTPPNISSLWNFGSLLGACLTIQVITGLFLAMHYTADTTTAFSSVTHICRDVNYGWTIRYLHANGASMFFMCLFIHVGRGLYYGSFALLETWNIGIMLLFSVMATAFMGYVLPWGQMSFWGATVITNLLSAIPYVGTNLVEWIWGGFSVGKPTLTRFFALHFILPFIISALAMIHLLFLHETGSNNPLGMSSNSDKIPFHPYYTTKDFLGLLLLILLLMTLTLFYPDLLGDPDNYTPANPLNTPPHIKPEWYFLFAYAILRSIPNKPGGVVALILSILILAIIPFLQPSKQQTMMFRPL... | 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... | Q5VJ50 |
P56193 | LAC1_THACU | Urishiol oxidase 1 | Thanatephorus | MARTTFLVSVSLFVSAVLARTVEYGLKISDGEIAPDGVKRNATLVNGGYPGPLIFANKGDTLKVKVQNKLTNPEMYRTTSIHWHGLLQHRNADDDGPSFVTQCPIVPRESYTYTIPLDDQTGTYWYHSHLSSQYVDGLRGPLVIYDPKDPHRRLYDVDDEKTVLIIGDWYHESSKAILASGNITRQRPVSATINGKGRFDPDNTPANPDTLYTLKVKRGKRYRLRVINSSEIASFRFSVEGHKVTVIAADGVSTKPYQVDAFDILAGQRIDCVVEANQEPDTYWINAPLTNVPNKTAQALLVYEEDRRPYHPPKGPYRKW... | Lignin degradation and detoxification of lignin-derived products. | P56193 |
Q91274 | ALBU_PETMA | Serum albumin SDS-1 | Petromyzon | MGKAMLKLCITLMVLVFSGTAESKGVMRREDESFPHLKSRLCGGLNGLGEDAYRSHCVVYYTKRMGVVSLDHVEELANHCLRIVKQCCAEGAADDCLQTELAAVQEQVCTRMSEAKDVPLVGRCCALAGSERHDCFHHAGGVAEGEGAWPHALPVTSPPEYDSVTVCALHATANARLYDTLLWEFSRRYPSASDSHLIALANEFITGLTTCCLVEEEHGACLATLREDFKHKLTEASHKSQNLCKALKSLGKEKFEDRIIVRFTQRAPQAPFELIQKLAHRFEVLAEKCCELGHSDRCLVEERYTVDDELCLEQSFVATC... | Serum albumin, the main protein of plasma, has a good binding capacity for water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood. | Q91274 |
B1MHQ0 | MSHA_MYCA9 | N-acetylglucosamine-inositol-phosphate N-acetylglucosaminyltransferase | Mycobacteroides abscessus | MLSGDEFARRAVAALKPRRIAVLSVHTSPLAQPGTGDAGGMNVYVLQTALQLARRGVAVDIFTRATSSSDEPVVSVTDGVTVRNIVAGPFEGLDKYDLPTQLCAFTAGVLRAEAVHEPGYYNLVHSHYWLSGQAGWLARDRWGVPLVHTAHTLAAVKNQTLAEGDRPEPALRGVGEQQVVDEADRLIVNTKDEADQLVSIHNADPARIDIVHPGVDLDVFTPGDKAAARAEFGLRADEQVVAFVGRIQPLKAPDLLVRAAERLPGVRVLIVGGPSGSGLDEPTALQDLAVDLGIADRVTFLPPQTRERLAQVYRAADIVA... | Catalyzes the transfer of a N-acetyl-glucosamine moiety to 1D-myo-inositol 3-phosphate to produce 1D-myo-inositol 2-acetamido-2-deoxy-glucopyranoside 3-phosphate in the mycothiol biosynthesis pathway. | B1MHQ0 |
B2JD95 | GLPK_PARP8 | Glycerokinase | Paraburkholderia | MQDQYILALDQGTTSSRAMLFDRNGNVVSVAQKEFRQIYPHPGWVEHDPLEIWATQAGVAAEAVTHAGLNGTSIAAIGITNQRETTIVWDRQTGHPIYNAIVWQDRRTADFCDQLKAQGLEDEVRAKTGLPVDSYFSATKIRWILDNVEGAREKAKQGKLAFGTVDSWLVWNFTKHELHITDVTNASRTMLFNIHTLQWDDALLDALDIPRSMLPEVRPSSEVYGPTKTTVFASKIPLAGIAGDQHAALFGQMCTRSGMVKNTYGTGCFLVMNTGTKPIESKNNLVTTIAWQIGDQINYALEGSIFIAGAVVQWLRDGLG... | Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate. | B2JD95 |
O58708 | MOBA_PYRHO | Molybdopterin-guanine dinucleotide synthase | Pyrococcus | MKLIAAVLAGGKSRRFGEDKLLFEINGKPLILHTIDRLEKCNLIKRVVIVASSHNEKVMREFGYEVIVDELEIGPISGLYSALSLGEVLVVGGDMPSLIPEFIDYIIKEFNNSRKIACVPRWSNGYLEPLHAAYSREFREILGERIRKGKYKLGDAIREIPNVCYISIEKLPVEWRESFFNVNRKEDLHIIT | Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor. | O58708 |
Q7W418 | UREE_BORPA | Urease accessory protein UreE | Bordetella | MKIANTFIKRGAAGGLDLSQAPGVTLTLAERRRSRQRLDLDEGRGELGMAIERGQTLRDGDVLVAEDGTYVVVRAALEDVARVTAATPWQLARAAYHLGNRHVLLEIAEQHLQFEYDAVLIDMLAQLGGVTAMRLRAVFEPDVGAYGGGHRHGHDESFGDDYALAQAAYHAHEAHPHAHSHAGGHGHVHSGHGHGGKHGEHDAES | Involved in urease metallocenter assembly. Binds nickel. Probably functions as a nickel donor during metallocenter assembly. | Q7W418 |
Q3B2D5 | RUVC_CHLL3 | Holliday junction resolvase RuvC | Pelodictyon | MIVLGIDPGSLSTGYGVVSTDDGRYRLLECGVLRLNPGKSHPARIGEIFEALDCLISRVQPGRLSIETAFVGRNVQSALKLGQVRGAVIALGVHRGLMLHEYAPREVKLAVTGRGGASKEQVAGMVTAMLGLGSVPKPLDVTDAIALALCDMLRNEGNVSLPKAKGSSRRGNGWAEFVKASPDLVVEPLKH | Nuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves the cruciform structure in supercoiled DNA by nicking to strands with the same polarity at sites symmetrically opposed at the junction in the homologous arms and leaves a 5'-terminal phosphate and a 3'-terminal hydroxyl group. | Q3B2D5 |
B8CWY9 | DER_HALOH | GTP-binding protein EngA | Halothermothrix | MAKPVVAIVGRPNVGKSTLFNRLAGYRISIVEGEPNVTRDRIYADVNWLDRSFIIVDTGGIDPYDRDQIKNMVKYQAQMAIDEASLILFVVDGRNGLTATDEEVAAFLRKSNKKVILVVNKVDDFKNMEEDCWEFYTLGFDKLIPISAEHGKNTGDLLDEIVNMLPEKGPEDSDDDAIDVAIIGKPNVGKSSLVNYIVGQERVIVSDIPGTTRDAIDTLVEKNGHRYNLIDTAGLRKKSRVKEATEYYSALRTIKAIDRSDGVIMMIDALEGVTEQDKKIAGYAHEAGKAIVLAVNKWDLVEKDTHTMENYKEEIYYNLK... | GTPase that plays an essential role in the late steps of ribosome biogenesis. | B8CWY9 |
Q1ISF4 | RECO_KORVE | Recombination protein O | Candidatus Koribacter | MLKQSEAIVLRTYPMREADLLVTLFTRAEGKIKGVAKAAKKSRRRFGGALEPLTHVRVYYEDRERQELTRLDSCDVLASPMSAEVDYPRALALGHVAEVIDDLLPDREPNDAVFRLSLAVLGQLVPGAVWMPLTYFDLWMVRLAGFLPDLMHCVVCGEELDDRAFFHPLVDGLVCANDKRLASTELTVESRAIADLMFRAPLENFAGAPWPRQRCADLRRFLVQILERHLEKKLVTVTMLDKLD | Involved in DNA repair and RecF pathway recombination. | Q1ISF4 |
Q10156 | LKH1_SCHPO | Dual specificity protein kinase lkh1 | Schizosaccharomyces | MHSLKRRRNHAPDWQDFYKNGVPQEVIVIEDSASPRLTPNLPPPFSVHQLQSFVPPQPPSSSSPSTTGTVAVPINGANAVYPSTNSVSLPQSYDPWLDANGVVPLPHDVASHPSYMVQSPTSYHACSNNQSPFPHSHHPPLHNPLPVSCQPVLRPPPVPQVPSHWYPVSLPSPNLPHQPISKPPVIPNLPKLQVHPNRLPHPIHNHPYSSPTSYPPPLCPATYCPSNPPQLAPATAIAPSSQSSQHKSVNYSVTPSSINNHTAVPLSPTLAVWLPMTQPTFQPPSANVYQPASNANQVITPVSISDYRPPKKRKRAAWPP... | Protein kinase that may act as a negative regulator of filamentous growth and flocculation. Appears to have a role in normal cell wall and septum formation and in cell separation. May have antagonistic function in the regulation of beta-glucan distribution between the sites for cell wall and septum assembly. | Q10156 |
Q7VNY2 | TUSA_HAEDU | Sulfur carrier protein TusA | Haemophilus | MTDLPVDKILDTLGLRCPEPVMLTRKTIRHMQQGEILFILADDPATTRDIPSFCEFMDHQLLKSKTDTPPYEYWIKKGI | Sulfur carrier protein which probably makes part of a sulfur-relay system. | Q7VNY2 |
O82798 | ARR4_ARATH | Response regulator 1 | Arabidopsis | MARDGGVSCLRRSEMMSVGGIGGIESAPLDLDEVHVLAVDDSLVDRIVIERLLRITSCKVTAVDSGWRALEFLGLDNEKASAEFDRLKVDLIITDYCMPGMTGYELLKKIKESSNFREVPVVIMSSENVLTRIDRCLEEGAQDFLLKPVKLADVKRLRSHLTKDVKLSNGNKRKLPEDSSSVNSSLPPPSPPLTISPESSPPLTVSTESSDSSPPLSPVEIFSTSPLSSPIDDEDDDVLTSSSEESPIRRQKMRSPGLD | Functions as response regulator involved in His-to-Asp phosphorelay signal transduction system. Phosphorylation of the Asp residue in the receiver domain activates the ability of the protein to promote the transcription of target genes. Type-A response regulators seem to act as negative regulators of the cytokinin sign... | O82798 |
A4SIG6 | HLDE_AERS4 | D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase | Aeromonas | MKITLPEFGKARVLVVGDVMLDRYWHGPTGRISPEAPVPVVKVEHIEERPGGAANVALNSAALGAHAVLLGLTGQDEAADALAGQMAGVKVACDFVRLADYPTITKLRVLSRNQQLLRLDFEEAFHDVDSTLLMNKVEQALPSSDVMILSDYGKGALNDVPGMIQRARAAGIPVLVDPKGTEFEKYRGATLLTPNMSEFEAVVGKVKGEEDLVAKGLALVKRFELEALLVTRSENGMTLIREGQPELHLPAQAHEVYDVTGAGDTVISTLATSLAAGMSLDEACALANTAAGIVVGKLGTSTVSPVELANALYTEQETGF... | Catalyzes the ADP transfer from ATP to D-glycero-beta-D-manno-heptose 1-phosphate, yielding ADP-D-glycero-beta-D-manno-heptose. | A4SIG6 |
Q98F85 | PAL_RHILO | Outer membrane lipoprotein Omp16 homolog | Mesorhizobium | MGRIAALTRNPVMIALVAMLAIAGCASKKTPNNAADLGLNGAGAATPGSAQDFTVNIGDRIFFDTDSSSIRADAQTTLARQAQWLNQYKQYAIVVEGHADERGTREYNLALGARRAAAARDFLVSKGVASSRLKTISYGKERPVAVCDDISCWSQNRRAVTTLSGAGS | Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity. | Q98F85 |
Q113W0 | TRMD_TRIEI | tRNA [GM37] methyltransferase | Trichodesmium | MRFDVITLFPDFFTTPLNSGLLGRAFNKNIAKVNLVNPRNYTTDKYKKVDDESYGGGVGMVLKPEPIFAAVESLPTLSKREVILLTPQGKRMHQGLFRELATDYEQLILICGHYEGIDERVQYLVSREVSLGDFVLTGGEIPALALINGVVRLLPGTVGKAESLECESFESGLLDYPQYTRPANFRGWKVPEVLLSGHHAEIARWRYQQQLQRTKSRRPDLLKNDDN | Specifically methylates guanosine-37 in various tRNAs. | Q113W0 |
P23988 | PAGC_SALTY | Virulence membrane protein PagC | Salmonella | MKNIILSTLVITTSVLVVNVAQADTNAFSVGYAQSKVQDFKNIRGVNVKYRYEDDSPVSFISSLSYLYGDRQASGSVEPEGIHYHDKFEVKYGSLMVGPAYRLSDNFSLYALAGVGTVKATFKEHSTQDGDSFSNKISSRKTGFAWGAGVQMNPLENIVVDVGYEGSNISSTKINGFNVGVGYRF | Essential for full virulence and survival within macrophages. | P23988 |
Q255L3 | RS15_CHLFF | 30S ribosomal protein S15 | Chlamydia | MSLDKGTKEEITKKFQLHEKDTGSADVQIAILTEHITELKQHLKRSPKDQNSRLALLKLVGQRRKLLEYLNSTDTERYKNLITRLNLRK | Forms an intersubunit bridge (bridge B4) with the 23S rRNA of the 50S subunit in the ribosome. | Q255L3 |
P29764 | RLA0_OXYRB | Light-induced 34 kDa protein | Oxybasis | MAVKPTKAEKKIAYDQKLCQLLDEYSQVLIASADNVGSNQLQAIRIGLRGDSIVLMGKNTMMKRSIRLHAENTGNENLRNVEQLFLPNVGLIFTKGDLNQVREEISKYKVGAPARFGLVAPIDVVVPPGNTGLDPSQTSFFQVLNIPTKINKGTVEIITAVELIKKGEKVGSSEAALLAKLGIRPFSYGLNVESVYDDGSVFSPEVLDLTEDDLLARFATGVSMVTSLSLAISYPTLAAAPHSSSMGATMFLLLLLQPTMTSLRPRKLRSISRILAVASCSCSSAGTAPTGGGAAAAAVEEKKEEPEEESDDDIGFSLFD... | Ribosomal protein P0 is the functional equivalent of E.coli protein L10. | P29764 |
Q87Q74 | HUTI_VIBPA | Imidazolone-5-propionate hydrolase | Vibrio | MDLLIENARLVSMERGEAGYLPTPPARVGIQAGKIAAISAHPVGRDTPQIEALLSPQHYSQTIDLQGQLLTPGLIDCHTHLIYAGNRANEFEMRLNGVPYQEIAKQGGGILSSVKATRAATEEQLIELALPRLDGLLASGVTSVEVKSGYGLTLKDELKMLRAAKALEQERNVKITTTLLAAHALPPEFEGRADDYIEHVCQEIIPIVAEENLATSVDVFCESIGFNLEQTEKVFATAKLYGLHVKGHTEQLSNLGGTELTARYKGLSADHIEYLDEDGVVALSKSDTVATLLPGAFYFLRETQLPPIELLRKYHVPMAI... | Catalyzes the hydrolytic cleavage of the carbon-nitrogen bond in imidazolone-5-propanoate to yield N-formimidoyl-L-glutamate. It is the third step in the universal histidine degradation pathway. | Q87Q74 |
Q6LZ92 | ASPD_METMP | L-aspartate dehydrogenase | Methanococcus | MLKIGLVGCGAIASLITKALMSDRLNKAEVLAFYDGNLEKAEKLAMETGADFCKSLDELVSKDLDLIVECASVNAVEDTVIKSLNNDKDVIIMSVGAFADKDLFVKLYKLAEKLGKKIYVPSGAVAGIDAVKSGSLGKISEVSLTTTKPVHGLKSALEEQGLNTDEIKEPKIVFEGTVFDAISKFPQNINVSVVLSLASRYPAKVKIIADPNAVVNRHEILVKGSIGTIKTCVENNPCRDNPKTSALAAYSVIRLIKDLSEPVRIGT | Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate. | Q6LZ92 |
P0CN92 | ALG3_CRYNJ | Dolichyl-P-Man:Man(5)GlcNAc(2)-PP-dolichyl mannosyltransferase | Cryptococcus neoformans species complex | MSRQSLFTPALGQRKGLISHTVDLVRALLFDRRYFWHTAFLLFLGEVALSLLVIWKIPYTKIDWPAYMQQVDMFLAGERDYSKIEGETGPLVYPALHLYIYTAFHRLLPSIENVRPAQFVFLGFYLATYLAISTIYYLAGRPSNGGHHFPQVLLIPLTLSKRAHSIFLLRLFNDPIAMLIFYLSVIAFQIGGRKGWRLGCVLFSLALGVKMNILNFLPGLLVLLFQYRGIVGTVEGLSIIGLIQFLLPAPFFFSKSNPYLIRAYFTSAFDFSRQFLYEWTVNWRFISEETFLSRERAVTLLAGHLTVLGLFAAFKWSPVP... | Adds the first Dol-P-Man derived mannose in an alpha-1,3 linkage to Man(5)GlcNAc(2)-PP-Dol. | P0CN92 |
B0TQH1 | YIDC_SHEHH | Membrane protein YidC | Shewanella | MESQRNILLIGLLFVSFLLWQQWQADQAPQPVAAAQTQSSIPASTVADSHSSDVPDADSAVPEAITASKELITVFTDQLEIKIDPVGGDIVYSALLSHKLEENGDDPFVLLEQTNDIYYIAQSGLIGRDGIDSSVKGRAHFDSASREYKLADGQDTLSVPLTYVSDKGVTYTKSFVFTRGKYNIAVDYKINNTSDASLQVQMYGQIKHSIKKSESSMMMPTYLGGAFSTDDIRYEKYSFDDMADKNLDDSTLGGWVAMLQHYFVSAWVPPATEKNIIFSSMKNGLANIGFRGELHDIAPGSEQVIKSEFYVGPKDQKALS... | Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispanning memb... | B0TQH1 |
Q3J771 | UREE_NITOC | Urease accessory protein UreE | Nitrosococcus | MLCFERRLPSDTPADLEMAFTFEQRERSRLRFPLPDGREAAFLIERGAPLVEGERLGTAEGLVLAIQAKPELLMEVRTSDPLTLVRAAYHLGNRHVRLEIGAHWLRLPPDYVLRDMLMRLGVEVFEVTAPYQPESGAYGGGHHHSHSHHEGDEFHSKPRLHHFGGSQ | Involved in urease metallocenter assembly. Binds nickel. Probably functions as a nickel donor during metallocenter assembly. | Q3J771 |
Q7UE01 | LEPA2_RHOBA | Ribosomal back-translocase LepA 2 | Rhodopirellula | MKHIRNFCIIAHIDHGKSTLADRLIQSCGGVTQREFHDQMLDSMDIERERGITIKSNTVTLNYTAKDGEAYQLNLIDTPGHVDFSHEVRRSLMACEGALMVVDASQGVEAQTVANLYLALEYDLELLPVINKIDLPAADVDRVRGEIDEDLGLDPFVAIPVSAKTGQGIEDVLEGIVKNLPAPKGDPKAPLKALVFDAFFDKYRGVILQCRVMEGTLKPKDEIHFMHADRDFTVDELGYNQFKLVPKKELTAGEVGYIVAGVKTVQDIEIGDTITLANRPADEPIPGYQPARQVVFSSVYPMSTDEYQDLTKALEKLSIN... | Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre-t... | Q7UE01 |
Q9U4X5 | SODC_DROOR | Superoxide dismutase 1 | Sophophora | MVVKAVCVINGDAKGTVFFEQESSETPVKVSGEVCGLAKGLHGFHVHEFGDNTNGCMSSGPHFNPYGKEHGAPVDENRHLGDLGNIEATGDCPTKVSITDSRITLFGADSIIGRTVVVHADADDLGKGGHELSKSTGNAGARIGCGVIGIAKV | Destroys radicals which are normally produced within the cells and which are toxic to biological systems. | Q9U4X5 |
Q80US8 | MAD3_MOUSE | Max-associated protein 3 | Mus | MEPVASNIQVLLQAAEFLERREREAEHGYASLCPHHSPGTVCRRRKPPLQAPGALNSGRSVHNELEKRRRAQLKRCLEQLRQQMPLGVDCTRYTTLSLLRRARVHIQKLEEQEQQARRLKEKLRSKQQSLQQQLEQLQGLPGARERERLRADSLDSSGLSSERSDSDQEDLEVDVESLVFGTETELLQSFSAGREHSYSHSTCAWL | Transcriptional repressor. Binds with MAX to form a sequence-specific DNA-binding protein complex which recognizes the core sequence 5'-CAC[GA]TG-3'. Antagonizes MYC transcriptional activity by competing for MAX and suppresses MYC dependent cell transformation. | Q80US8 |
Q6KZK4 | RNH2_PICTO | Ribonuclease HII | Picrophilus | MCVCGIDEAGRGPVIGPMVMAMVCADDINFYVNDSKLLTRNKRSLIFNDVSGLYHKYYIINPAEIDDAVKKHSLNNLEEQYAEKLILKAECEKIYIDCFDVNESRLERILKDRTGKEVICRHHADRDIKIVSAASIIAKVLRDNEIEKLKSIYGDFGSGYPSDPKTLRFLEHSIINHDNIDNIVRKEWKTYKNLVQGHI | Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. | Q6KZK4 |
Q9MTL6 | PSBK_OENEH | Photosystem II reaction center protein K | Oenothera | MLNIFSLICLNSDLYSSRFFLAKLPEAYAFLNPIVDVMPVIPLFFLLLAFVWQAAVSFR | One of the components of the core complex of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, a... | Q9MTL6 |
Q13TR5 | TATA_PARXL | Sec-independent protein translocase protein TatA | Paraburkholderia | MGSLSIWHWLIVLLIVALVFGTKKLRNIGTDLGGAVKGFKEGMKEAETPAGEAQQRELPRNGAVDVDAKEKAPRSGDYR | Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system. | Q13TR5 |
D7Y2H2 | CDNC_ECOM1 | c-di-AMP synthase | Escherichia | MSTEHVDHKTIARFAEDKVNLPKVKADDFREQAKRLQNKLEGYLSDHPDFSLKRMIPSGSLAKGTALRSLNDIDVAVYISGSDAPQDLRGLLDYLADRLRKAFPNFSPDQVKPQTYSVTVSFRGSGLDVDIVPVLYSGLPDWRGHLISQEDGSFLETSIPLHLDFIKARKRAAPKHFAQVVRLAKYWARLMKQERPNFRFKSFMIELILAKLLDNGVDFSNYPEALQAFFSYLVSTELRERIVFEDNYPASKIGTLSDLVQIIDPVNPVNNVARLYTQSNVDAIIDAAMDAGDAIDAAFYAPTKQLTVTYWQKVFGSSFQ... | Protects E.coli strain JP313 against bacteriophage lambda cI- infection. When the cdnC-cap7-cap6-nucC operon is transformed into a susceptible strain it confers bacteriophage immunity. Mutations in the sensor (Cap7 also called HORMA) or effector proteins (CdnC, NucC) but not the disassembly protein (Cap6 also called Tr... | D7Y2H2 |
B0CAE7 | RUVA_ACAM1 | Holliday junction ATP-dependent DNA helicase RuvA | Acaryochloris | MIGFLQGYVVSLQQTSTHRTLLTLDVNQVGYDLYVPSRIRQHLPPDQEQMRVFTHLQVREDQMVLFGFAVVAERDLFRQLIAVSGIGPQLALALIDTLGLQDLVQAIVNSNTKMLVKTPGVGAKTAERIALELRSKLAEWRDQAGLKTLPSAGPIDSVQEDVEMTLLALGYTSQEVMRALQAVGQNTALAKNSDTEAWIREAIAWLSQ | 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... | B0CAE7 |
Q9Y871 | FAEB_PIREQ | Ferulic acid esterase B | unclassified Piromyces | MKTSIVLSIVALFLTSKASADCWSERLGWPCCSDSNAEVIYVDDDGDWGVENNDWCGIQKEEENNNSWDMGDWNQGGNQGGGMPWGDFGGNQGGGMQWGDFGGNQGGGMPWGDFGGNQGGGMPWGDFGGNQGGNQGGGMPWGDFGGNQGGNQGGGMPWGDFGGNQGGGMQWGDFGGNQGGNQGGGMPWGDFGGNQGGGMQWGDFGGNQGGNQGGGMPWGDFGGNQGGGMQWGDFGGNQGGGMQWGDFGGNQGGNQDWGNQGGNSGPTVEYSTDVDCSGKTLKSNTNLNINGRKVIVKFPSGFTGDKAAPLLINYHPIMGS... | Involved in degradation of plant cell walls. Hydrolyzes of the feruloyl-arabinose ester bond in arabinoxylans as well as the feruloyl-galactose and feruloyl-arabinose ester bonds in pectin. | Q9Y871 |
Q12200 | NPC1_YEAST | Niemann-Pick type C-related protein 1 | Saccharomyces | MNVLWIIALVGQLMRLVQGTATCAMYGNCGKKSVFGNELPCPVPRSFEPPVLSDETSKLLVEVCGEEWKEVRYACCTKDQVVALRDNLQKAQPLISSCPACLKNFNNLFCHFTCAADQGRFVNITKVEKSKEDKDIVAELDVFMNSSWASEFYDSCKNIKFSATNGYAMDLIGGGAKNYSQFLKFLGDAKPMLGGSPFQINYKYDLANEEKEWQEFNDEVYACDDAQYKCACSDCQESCPHLKPLKDGVCKVGPLPCFSLSVLIFYTICALFAFMWYYLCKRKKNGAMIVDDDIVPESGSLDESETNVFESFNNETNFFN... | Involved in sphingolipid trafficking. May recycle sphingolipids between cellular membranous compartments. | Q12200 |
A7FW89 | DER_CLOB1 | GTP-binding protein EngA | Clostridium | MAKPIVAIVGRPNVGKSTLFNKLAGKRISIVQDTPGVTRDRIYAEAEWLNYKFTMIDTGGIEPKSEDIIVSQMRRQAQIAIEMANVIIFLVDGKEGLAPADKEVAQMLRKSKKPVVLVVNKIDKLKDENNAYEFYNLGIGDPVTISSSQALGLGDMLDRVVEYFKDDESAGEDDERINIAFIGKPNVGKSSLINKLLGEERLIVSDIPGTTRDSIDSYVDTDFGEFTLIDTAGLRRKSKVKEEIERYSVIRTYASIERADVCILMIDATEGISEQDQKIIGYAHDINKAILVIVNKWDLVEKDDKTMDKFKKELKVNLSF... | GTPase that plays an essential role in the late steps of ribosome biogenesis. | A7FW89 |
P23774 | FAPR_ECOLX | 987P fimbrial operon positive regulatory protein FapR | Escherichia | MKLKNIHLYNYVVIYTKNCEIYINKGNEQVYIPPRMVAIFEKNISFNIETIRKGDGVLYESFDMKHELLTSLRRVIEPSVKFAAESYTNKRSFKERIFKVKSCSIVIDLFKRLKDNGSPEFTAIYELAFLVSKCENPSMFAISLFSSVAVTFSERIVTLLFSDLTRKWKLSDIAEEMHISEISVRKRLEQECLNFNQLILDVRMNQAAKFIIRSDHQIGMIASLVGYTSVSYFIKTFKEYYGVTPKKFEIGIKENLRCNR | Positive regulator of the expression of the 987P operon for the fimbrial protein in enterotoxygenic E.coli. | P23774 |
B1AIB9 | ATPG_UREP2 | F-ATPase gamma subunit | Ureaplasma | MSLDAMKRKINSVQTTAKITNAMKLVATAKLKRQRDRLAAIKEYCHDYYDVIGLLLSVVDDVEFLKIPNAKDRTLYITINSTMGLAGSYNYNVNKLISKIVNETDITFTIGKKGHDFMRLSGRVDQVNTYLNLNDNDLTFDMSLQIAREALELYSQGEVNKICIIYTKFINAITFEVSVIDVLPFDKTALIKDHLAETIELAKDNIIFKPNKFELVKKILPTYIATVLYGSLIESKISENASRRNAMDAATKNAKALAENYKLIYNTLRQGKITREITEIVAGSDD | 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. | B1AIB9 |
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