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
|
|---|---|---|---|---|---|---|
C6DYS1 | YIDC_GEOSM | Membrane protein YidC | unclassified Geobacter | MEKRLIIAVVLSIGVLYAYSFIFPTPKPVPTPGGKQAAMSSATAPAPSVAALPIAGTTPVAAPAPQAGQAPAVAKDVTVDTDLYTAVFSTQGGGLKKFVLKKYKETAGPQGKDIVLVNETAANRYALLSDSREFGISPNALYSASTGEVKVTDGGKGSLELTTTTSQGITFRKVYTFSGDAYRIGLTEEVQNVGNVALTGAVHLLQTSRVVDAKKEGRYEVYSPSTLAEGKVKLDDLEDLQKTPVQYGKDIAWSAFADKYFVDGIIADKGSISQVRITRPANDAILRDVASPTVSVAPGQRSAINYAIYYGPKDLDILKLQGSRFEEVIDYGWFGPIAKPLIYSLKFLYKYTGNYGIAIIIITFILKLVFFPLTHKSYKSMKDMQKLQPKMTELKEKFKNDRDAMNRAVMELYKTHKVNPLGGCLPMLVQIPVFFGLYRALMYSIELRHAPFYLWITDLSAKDPYYVTPIIMGATMFIQQKMTPTNMDPVQAKMMLMLPIVFTFMFLNFPSGLVIYWLVNNVLTIAQQMYINKTVE | 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 membrane proteins. | C6DYS1 |
Q4QPI7 | UVRC_HAEI8 | Excinuclease ABC subunit C | Haemophilus | MFDAKKFLADVSHEPGVYRMYDDKDQVIYVGKAKDLKKRLSSYFRKNLSSKKTEALVASIHHIDTMLTSSETEALLLEHNFIKLYQPRYNVLLRDDKSYPFILLTKERHPRITSYRGSKKFAGEYFGPYPHAGAVRETLSLLQKLFPVRQCENSVYSNRSRPCLQYQIGRCSAPCVQGYVSDEEYNQQVELARLFLQGKDQQVLDYLIGKMEQASRNLDFEQAARYRDQIQAVRSVIEKQFVSNERLDDMDIMSIAYQHGLACVQVMFIRQGKVLGNRSYFPKVPANTDLSELTETFVGQFYLQGHQGRSIPNSIIVDRQLAEKSELEQLLTEQAGRKVTIQESVKGDKSKYLQLAQVNAKAALNVQLKQSSRMSERYQALCDLLNLPEIKRMECFDISHTMGNQTVASCVVFNQEGPLKSDYRRFNIEGITGGDDYAAMEQALQKRYERDLEEDKIPDIIFIDGGKGQLNRALNVFQHLQVKWDKNRPHLIGVAKGVDRRAGQEVLIISKQDREIHLPDDSLALHLIQHIRDESHNHAISGHRKKRQKAFTQSGLETIEGVGAKRRQALLKYLGGLQGVKKATLDEIASVPGISLKLAETIFETLKND | The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision. | Q4QPI7 |
Q755J9 | VPS27_ASHGO | Vacuolar protein sorting-associated protein 27 | Eremothecium | MNTEIQTVAALGECIQRATSESIPNGEIDLALALDVSDAVRSRRLGARDSMRALKKRVLQTKSNPNTQLAAWRLVEVCVKNGGTHFLKEVCSREFMDCMEHVAAQEKTVDNEDLVQLCRRIIFELYTAFKNDSQLSYVSQVHQRLQARGVEFPQAAPGYLVNTMAMFDSKAPADWVDSDACMICSNAFTFLNRKHHCRSCGGIFCNEHSSHQLPLPEMGITEPVRVCDNCYDEYEIKKHSSRRLRRQSQRRARPKAEREDEDDDLRRAIELSLRESKTQDNLVPTVTRLENSDATKDDEDPEFLAAVQASLREHQLEQERQAAAAAAAAKHPSQPERAVQLPSLMDSRQAPVAQQRYSTLTNQEEDDIYLFANLVEKMKGQPMNAVLEDTQLQMLYQKVLGTRPRLNHSLNDTFHKYNTLVDMNAKISDIMSIYDTMLERQLRNINLSQQYSMPHLPSDPYTYQMHRQPESSPANTVPYEKTQPEPTYRSYARSSSNAAELTPAILHTTQSSPMENRQSQSVTGFEPQVSEPDIKKTLLSSPSEPLYPPEESIPDKEKEAQVPITQFEFPSVPAQKIKMATPQNERVTEDAGTTPQEETLLIEL | Component of the ESCRT-0 complex which is the sorting receptor for ubiquitinated cargo proteins at the multivesicular body (MVB) and recruits ESCRT-I to the MVB outer membrane. | Q755J9 |
P45125 | UVRB_HAEIN | Excinuclease ABC subunit B | Haemophilus | MSEKINTKPFILHSDFRPSGDQPQAIEKLAENLTDGLAHQTLLGVTGSGKTFTIANVIAQLNRPAMLLAPNKTLAAQLYAEMKAFFPENAVEYFVSYYDYYQPEAYVPSSDTFIEKDASINDQIEQMRLSATKSFLERRDTIVVASVSAIYGLGDPDSYLQMMLHLQQGAIIDQRQILAKLAELQYTRNDQAFQRGTFRVRGEIIDIFPAESDDRAVRIELFDDEIERLSLFDPLTGSSFGAVPRFTIYPKTHYVTPRERILDAIENIKKELVSRREYFIKEHKLLEEQRISQRTQFDIEMMNELGYCSGIENYSRYLSGRNEGEPPPTLFDYMPPDAILIIDESHVTVPQIGGMYRGDRSRKETLVEYGFRLPSALDNRPLRFEEFERLAPQTIYVSATPGAYELEKSGSEIIDQVVRPTGLLDPLIEIRPVSIQVDDLLSEARQRADKNERVLVTTLTKKMAEDLTDYLDEHGIRVRYLHSDIDTVERVEIIRDLRLGEFDVLVGINLLREGLDIPEVSLVAILDADKEGFLRSERSLIQTIGRAARNLNGKAILYADSITKSMEKAITETNRRREKQTKYNEEHGIVPQALNKKVGELLDIGQGANQKAKANKQRGKMAAEPTALYNAPKNAKEYQQQIKKLEQQMYKFAQDLEFEKAAAIRDQLHQLREQFVFDN | 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. | P45125 |
Q97CP8 | VATD_THEVO | V-ATPase subunit D | Thermoplasma | MEIRPTRIELIRTRRRIKLARKGLDLLKMKRSALIYEFLQISRTIRGMRENLRREVEDALNTIRTAEILEGQVALERIANMSSDSTINVDSRNVMGVVIPTLNLTYNLSILSDVYRTISVPVAINDAIDRFQRLFLNLIQILEKENALRNLLIEIDKTKRRSNAIENILIPRLEYQAKMIKMMLDERERDTFTTLKTIKKKIEAGKDEE | Produces ATP from ADP in the presence of a proton gradient across the membrane. | Q97CP8 |
B9DM01 | XPT_STACT | Xanthine phosphoribosyltransferase | Staphylococcus | MEALRQKVKEDGVVIGEKILKVDGFLNHQIDAQLMYDIGETFYEQFKDQKVTKILTVEASGIAPAIMVAYKFGVPCLFAKKAKPNTLNKGFYQTDIHSFTKDKTNSVIISEEFLDEHDRVLIIDDFLANGDASLGLNRLVHQAGAETVGVGIVVEKSFQQGRTRLEEAGLKVSSLCEVASLSGNKVTLVGEE | Converts the preformed base xanthine, a product of nucleic acid breakdown, to xanthosine 5'-monophosphate (XMP), so it can be reused for RNA or DNA synthesis. | B9DM01 |
Q9K9G7 | THIZ_HALH5 | Formylaminopyrimidine import ATP-binding protein ThiZ | Halalkalibacterium (ex Joshi et al. 2022) | MVKELLTFEEVSFAYSSSSPVIERLSFTVFENEIVAILAKSGSGKSTLFRLITRLESPDQGTIVCHAQGKIGYMPQQDLLLPWLTILENVSLPLEIQGKDKKEAKIIAASFFNRFGLVGTESLYPDALSGGMRQRAAFLRATLTSETLLLLDEPFASLDSLTKTSMHHWLVSMWEKEKRTLLLVTHDIEEALLLSDRLFIFTNQPLHGFTEVQVPPDLRRKMETTEKMEQQRSSLKKDIRALLIEESLR | Participates in a thiamine pyrimidine salvage pathway as part of the ABC transporter complex ThiXYZ involved in the import of thiamine degradation products such as the formylaminopyrimidine N-formyl-4-amino-5-aminomethyl-2-methylpyrimidine (FAMP). Is likely responsible for energy coupling to the transport system. | Q9K9G7 |
S7UQV8 | UGO_TOXGG | Unique GC organizer UGO | Toxoplasma | MRMQWFLLRHAYFIKGEDFAVAVALLDLALYVLIGTNSLQFLDQSPEKALFGMITSALIFIIALCGFVIVRMFRTSKYKIETYIMPVLIICNIASVFYMQLINKLVGFMTLQLPVLTFLITGYPYVWLVAFVLIGMGGGLIAQSVVCSVSLGSSCPPSVWVDVGLYALQLISGSVAYFTVYELGILIVRYKRHPARYLDAFSDLTALDTIVFSPVFGLGGETARQVQVNQLMAPEKPNLDGLTFLRSASQVSQTTNRIVSRAFYHANTPPHSSSRDALPADKALGAERSDRAGSAVFSPNTLGPLGAPSAGLRDFGPGRPVPGASVVVPKSLKQHAAALHAGANSPHGSPPLQPHGALPGAPRSNTLRGCSGQVSLVPREEESDPACGSLRASVESKATHRSAATLSACESKSRSGRVAGLFRGLSKRPGGPDCEEAAPAEPATSLGSKELGRKKTAGSKAQSSVPILLPRPQSIEETTWRGLASGDLSKDTPVASLASRRNLRMDEQSGDADKASSDVSRDPAKKGAGPFVAEAPVHTAVLPSSSFHSEFPLSRRDSGKELLSDLRESRERTARAASHDTHAAADDSGLQGDPALAAEARVRTALHYHRRWFFSQLFHFRRARRRHRRGAGARDGELVFERGEPDEVESEESCDDSRSRPRETASLSHFSRLSRSRRHKTRTYRRGRSSDGTTAGTSDSDSHGESLEDEGSDSGQESESEESRRRRMRSSRNRRRETSSEDSSSGTSVRSEGRHCREGRANSSVFSSGIRRYFSFFSAATRCAHAASSEEERPVRPARHSWRRGSGDSRECSASTSGVSEACEHSSDASWASSSSLCGSCEKRSIRMSRRRRREGKSRPHASSVSRAERHRGHVSVDLAPLLPSRLFFDTFLNSVRRAERLSKEGRLPASVSRQSSETRGSRTAFLNGDKGCSPTSEAPERSFPASANEVSFRRNEGWERYYDMLLPSLPPFPSARPLYVKPRKNSQAFQNVAVSVSRNETEMTASSPATSFDGPRAVSLSPEGRGARESSDGGGATAPSDLHSRPARAKSLVAAMLHTYPTCPQPPSDLSLFTTPPASPSSLNEVQASRSSSARITSVELGALGKQQGEAAPAGTDAVEEDRDATEDARGSLSSPTGASRRGDRCRRSWSSCEARSSVEMKPNLSIRDARASESPLQSAAPLLSEEKKSRKAQSCAQCRRCGRSRTRLQPSGRLGSSSREDLVGEADSHVSPEKEVFVSSRREKREEQVPRSRREERRDRRGRRWRRGRRRRKARECSETEERRDSSSEWSGTQYSSQERRSHEAVGGVAQLTPICVDDECGKGDAGLSPLLRSEAEESEGEGDMRERQIYETHSDGDVEELSEEEREDRGRSWLRWLFPWGAGEGQGGEKNRRKRSRSEGRREREFISAERRYLEHHRRSRVSSVADSRWGSGSEASADAYPALRRRKGSRVYPVSKPQWFQPSGLTACSSKNSWLAVPPDISLVSAAPALPTPSPSSLSFSGLDQELDCDANSSTAVSSSLPDSTAWQGSGAAASASSPSLRASVDAHFAEAELHAAEHSDGVSVSPRNSPGALSARPMSAAGMPNPDSGIATQTPQTPQTPHTQRPLLLAQSLVAASGKPLPPTRADFEAQRSQGLGDLSQKTPRVFSPQGLGRSQGYGPGGSSYALDSSREAGPSGRLSATPSTRLQGSGGPAFPHSSFPQAIGAAGTPTAPSRDSRTFFGDTGAARASRAGLSGRLASRGTALAPKGTRRLKSGYSVGAADAKDKQKGKVLRYQLVQKFHDRLPWWVARIIVYTDAALENCRRRRRLMQRATWKTKVAMPVRNMLGLFSDEKIETWYVQWLNAFNAKYYPRVAWLLFLICFYATAFHGLLRLRGFIENYPLCIDAVRASPLGEAGFLILVAVRFASQPILSFLLLLPLLRHSGSRLIDFLFCSRAPATPLKSYKLYRWMLALSFLQFVYAVFDNTWHLIAEPGSRHVNPLTIIPASPSLEIAAVQTVYILAVRTPTINLIFLLYIITYIIIFFVALPPGVQQVQLFTISMAGWLFTCVGGQLFYTRAFEVNRRRLFCKYVLPYMLYLEEIAAILYSNPQGEYPLDEGSEDEVSMGSGHLVGDRSA | In tachyzoites, required for the cellular trafficking of guanylate cyclase GC to the cell membrane and for GC guanylate cyclase activity. | S7UQV8 |
Q5HR05 | Y390_STAEQ | Putative lipid kinase SERP0390 | Staphylococcus | MKQPYNHGVLFYHEHSGLKDIHNGIGEVAKSLSSMCKHLSLQLSENKGDIIKYCKSIKNENYSSDVDVLFILGGDGTLNELVNGVMQYQLNLPIGVIPGGTFNDFTKTLQLHPNFKTASEQLLTSHAESYDVLKVNDLYVLNFVGLGLIVQNAENVQDGSKDIFGKFSYIGSTVKTLLNPVKFDFSLTVDGETKEGNTSMMLIANGPNIGGGQIPLTDLSPQDGRANTFVFNDQTLNILNDILKKRDSMNWNEITQGIDHISGKHITLSTNPSMKVDIDGEINLETPIEIQVLPKAIQLLTATEQNN | May catalyze the ATP-dependent phosphorylation of lipids other than diacylglycerol (DAG). | Q5HR05 |
B0CA92 | YCF3_ACAM1 | Photosystem I assembly protein Ycf3 | Acaryochloris | MPSDNFIDKAFSAMSDVVMKVIPTDQKSKDAFKYYRSGMAAQVDGNYAKALGNYTEALALEEDPFDKSYILYNMGLIFANNGDHEKALDYYHQSLELNPNLVQALYNTGVILHYKGEQAEEAAELDEAERFFDLAADFWKRAIKIAPNNYSEVQNWLKTTGRVGVG | Essential for the assembly of the photosystem I (PSI) complex. May act as a chaperone-like factor to guide the assembly of the PSI subunits. | B0CA92 |
A1L167 | U2QL1_HUMAN | E2Q-like ubiquitin-conjugating enzyme 1 | Homo | MKELQDIARLSDRFISVELVDESLFDWNVKLHQVDKDSVLWQDMKETNTEFILLNLTFPDNFPFSPPFMRVLSPRLENGYVLDGGAICMELLTPRGWSSAYTVEAVMRQFAASLVKGQGRICRKAGKSKKSFSRKEAEATFKSLVKTHEKYGWVTPPVSDG | Probable E2 ubiquitin-protein ligase that catalyzes the covalent attachment of ubiquitin to target proteins. May facilitate the monoubiquitination and degradation of MTOR and CCNE1 through interaction with FBXW7. | A1L167 |
C5BYK3 | TILS_BEUC1 | tRNA(Ile)-lysidine synthetase | Beutenbergia | MSGPHPSVAAARNAVRALLAELEPARGVLVACSGGADSLALAAATAFVAPRAGRAAGAVVVDHALQAGSAEVAARAADQCRGLGLEARVVRVDVDIALGGPEGAARAARYAALEAASREAGDAVVLLGHTLDDQAETVLLRLARGSGARSLAGMPRRRGVFARPFLHLERARLREVVDAVGLTPWEDPTNAVDGPARRADGGPLPRSAIRGRVLPALTEALGPGVPASLARSADLLREDADALDAFAADLLSTARGEDGSLDVEILAAAPPAVRRRALRRAALDAGSPAGDLAHVHVEALDALVTGYHGQAGVDLPGGRRAVRACGRLTL | Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine. | C5BYK3 |
P45359 | THLA_CLOAB | CaTHL | Clostridium | MKEVVIASAVRTAIGSYGKSLKDVPAVDLGATAIKEAVKKAGIKPEDVNEVILGNVLQAGLGQNPARQASFKAGLPVEIPAMTINKVCGSGLRTVSLAAQIIKAGDADVIIAGGMENMSRAPYLANNARWGYRMGNAKFVDEMITDGLWDAFNDYHMGITAENIAERWNISREEQDEFALASQKKAEEAIKSGQFKDEIVPVVIKGRKGETVVDTDEHPRFGSTIEGLAKLKPAFKKDGTVTAGNASGLNDCAAVLVIMSAEKAKELGVKPLAKIVSYGSAGVDPAIMGYGPFYATKAAIEKAGWTVDELDLIESNEAFAAQSLAVAKDLKFDMNKVNVNGGAIALGHPIGASGARILVTLVHAMQKRDAKKGLATLCIGGGQGTAILLEKC | Catalyzes the condensation of two molecules of acetyl-CoA to produce acetoacetyl-CoA . Involved in solvent production . | P45359 |
B7JN72 | THIE_BACC0 | Thiamine-phosphate pyrophosphorylase | Bacillus cereus group | MSRISKAEMSKLLSVYFIMGSNNCTKDPLQVLREALEGGITIFQFREKGEGALTGEERICFAKELQAICKEYGVPFIVNDDVELALELDADGVHVGQDDEGITSVREKMGDKIVGVSTHTIEEARWAIENGADYLGVGPIFPTSTKKDTKAVQGTKGLAHFREQGITIPIVGIGGISIENTASVIEAGADGVSVISAISLAESAYESTKKLVEEVSRSL | 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). | B7JN72 |
Q4KJA1 | THIC_PSEF5 | Thiamine biosynthesis protein ThiC | Pseudomonas | MTTKLKNASNLSESAQVDQQSVQPFTRSQKVYVQGSRPDIRVPMREITLDVTPTDFGGEINAPVTVYDTSGPYTDPNVVIDVRKGLGDVRSAWIEDRGDTERLAGLSSNFGQQRLADPELTKLRFAHVNNPRRAKAGANVSQMHYARKGIITAEMEYVAIRENMKLQEARAAGLLKQQHAGHSFGASIPKEITPEFVREEIARGRAIIPANINHVELEPMIIGRNFLVKINGNIGNSALGSSIEEEVAKLTWGIRWGSDTVMDLSTGKHIHETREWIIRNSPVPIGTVPIYQALEKVNGVAEDLTWELFRDTLIEQAEQGVDYFTIHAGVLLRYVPLTAKRVTGIVSRGGSIMAKWCLAHHKENFLYTHFDEICEIMKAYDVSFSLGDGLRPGSIADANDEAQFGELETLGELTKIAWKHDVQCMIEGPGHVPMQLIKENMDKQLECCDEAPFYTLGPLTTDIAPGYDHITSGIGAAMIGWFGCAMLCYVTPKEHLGLPNKDDVKTGIITYKIAAHAADLAKGHPGAQIRDNALSKARFEFRWEDQFNLGLDPDTARSYHDETLPKDSAKVAHFCSMCGPKFCSMKITQEVREYAANQRIEAVDVDVAKGLAEQAERFKQEGSQLYKKV | Catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction. | Q4KJA1 |
P21798 | TNNC2_BALNU | Troponin C, isoform 2 | Balanus | MMDELDKDQIAMLKKAFDGFDHEKKGAINCDVVATILRMMGQAYNAQTLKELIDEVDADGSGMLEFEEFVTLAAKFIIDDDAEAMAKELKEAFRLYDKAGKGYIPTSALKDILKELDETLNAEDLDNIIGEIDTDGSGTVDFDEFMEMMTG | Troponin is the central regulatory protein of striated muscle contraction. Tn consists of three components: Tn-I which is the inhibitor of actomyosin ATPase, Tn-T which contains the binding site for tropomyosin and Tn-C. The binding of calcium to Tn-C abolishes the inhibitory action of Tn on actin filaments. | P21798 |
Q8Y832 | TARI_LISMO | Ribitol-5-phosphate cytidylyltransferase | Listeria | MIYAEILAGGKGTRMGNVNMPKQYLPLKGKPIIVHTIEKFILNDRFEKIIIATPKDWINHTQDIIKKYIFDSRVIVIEGGTDRNETIMNGIRYVEKEFGLNEDDIIVTHDAVRPFITHRIIEENIDMALEFGSVDTVIPAVDTIVESTNHDFITDIPVRGNIYQGQTPQSFNMKTIQKHYNNLTDDEKQILTDACKICLLAGEKVKLVNGGISNIKITTPYDLKVANAIVQERINS | Catalyzes the transfer of the cytidylyl group of CTP to D-ribitol 5-phosphate. | Q8Y832 |
Q73H71 | TSAD_WOLPM | tRNA threonylcarbamoyladenosine biosynthesis protein TsaD | unclassified Wolbachia | MKTILAVETSCDETAVAIVNSDKQVLAHEILSQAEHKKRGGVIPEIASRAHMEHLSGLIKSAVEKSNLNFCDLNAIAATSGPGLIGGLIVGTMMAKAIAHVAQKPFIAVNHLEAHALVIRLLHEVKFPFLVLLISGGHCQFLIAQDVGKYIKLGETLDDSLGEAFDKVAKMLGLSYPGGPLIEKLAKKGNGTRFKLPRAMIKRSGCNFSFSGIKTAVKNLVQELKMSEQDVCDVCASFQECISDILLDRVSNAIIMAESLNIKINDFVITGGVAANNFLREKLKQHINLNIFFPPNDLCTDNAIMVGWTGIERLQKNYIDPLNFAPRPKWELESY | Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction. | Q73H71 |
Q3KKY7 | TIG_CHLTA | PPIase | Chlamydia | MSSRDFSNDLFSINIEENAGCVVSAKVQANPLVTQKCHKEALKTVKKNVVLPGFRKGKAPDNIVESRYSTQVEQELRRLFLRASFEALSQMCDRKPLSPKAVRSSAIDTCNPVNGGSVSFLYEAFPVIPSLPWEQLSLPDPEPVKEISEEDLENGLKNVAYFFATKTPVTRPSQEGDFISLSLYVSKRGDENSTPVAIFENKYFKISEEDMTDSFKARFLNVSTGHRVEEEIGSEDIQSFLNGDLLTFTVNAVIEISSPEMDDEKARQLQAESLEDLKKKLRIQLENQAKEAQHQKRFSDAEDALAQLIDFDLPESLLQEREELLSREKLLNARLVKYCSDSELEEQKQALLEEAKADARKAVKLLFLTQKVFSEKGLSISREELQYMMDVCSRERFGGYPPKDISNEMIQELVLVARDRLTYRKAIEAISSEKKDLEVVPS | 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. | Q3KKY7 |
Q67ES1 | TR113_RAT | Taste receptor type 2 member 30 | Rattus | MVAVLQSTFAIIFSMEFIVGTLGNGFIILMTCIDWVRRRKISLVDQILTALAITRITLILLVFIDWWVSVLFPALHETGKILRMYFISWTVINHCNLWLTASLSIIYFLKIASFSSIIFLYLKFRVKNVVFVTLLVSLFFLFINTAIVNVYFDVCFDGVQRNVSQVSRLYNHEQICKFLSFTNPMFAFIPFVTSMATFFLLIFSLWRHLKNMKHNAEGCRDVSTIVHIRALQTIIVSVVLYSTFFLSFFVKVWSSGSPERYLIFLFVWALGNAVLPAHTFVLIWGNCRLRWASLSLMLWLRYRFKNIDV | Putative taste receptor which may play a role in the perception of bitterness. | Q67ES1 |
Q9PG67 | TSAD_XYLFA | tRNA threonylcarbamoyladenosine biosynthesis protein TsaD | Xylella | MKIIGIESSCDETGVAVYDTALSGFAALRAHSVYSQVALHAEYGGVVPELASRDHVRKLLPLLRQTLAEAKLSVEELDGVAYTAGPGLVGALLVGAGVARALAWALEVPAIGVHHMEGHLLSPLLEDDPPEVPFVALLVSGGHTQLVAVDAIGDYRLLGETLDDAAGEAFDKVAKLMGLPYPGGPQLAALAEQGIPGRFCFTRPMVDRPGLDFSFSGLKTQVLLAWRNSDQSDAIRVDVARGFEDAVVDTLAIKCERALDTVACQTLVVAGGVGANKCLRARLQAMCRQRGGRACFPRPALCTDNGAMIAFAGALRLQAGQQSDIAVRVTPRWDMAALPPLVSRSCRR | Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction. | Q9PG67 |
B5F7D6 | YDIB_SALA4 | NAD-dependent shikimate 5-dehydrogenase | Salmonella | MDVTAKYELIGLMAYPIRHSLSPEMQNKALEKAGLPYTYMAFEVDNTTFASAIEGLKALKMRGTGVSMPNKQLACEYVDELTPAAKLVGAINTIVNDDGYLRGYNTDGTGHIRAIKESGFDIRGKTMVLLGAGGAATAIGAQAAIEGIKEIKLFNRKDDFFEKAVAFAKRVNENTDCVVTVTDLADQHAFTEALASADILTNGTKVGMKPLENESLIGDVSLLRPELLVTECVYNPHMTKLLQQAQQAGCKTIDGYGMLLWQGAEQFELWTGKAFPLDYVKQVMGFTA | The actual biological function of YdiB remains unclear, nor is it known whether 3-dehydroshikimate or quinate represents the natural substrate. Catalyzes the reversible NAD-dependent reduction of both 3-dehydroshikimate (DHSA) and 3-dehydroquinate to yield shikimate (SA) and quinate, respectively. It can use both NAD or NADP for catalysis, however it has higher catalytic efficiency with NAD. | B5F7D6 |
A4WB03 | TRPA_ENT38 | Tryptophan synthase alpha chain | Enterobacter | MERYDNAFTELKARKEGAFVPFVTLGDPGPEQSLKIIDTLIAAGADALELGIPFSDPLADGPTIQSATLRAFASGVTPTQCFEMLATVRQKYPTIPIGLLMYANLVFNRGIDEFYAECARVGVDSVLIADVPIEESAPFRQAAMRHNIAPIFICPPNADDELLRQIASHGRGYTYLLSRAGVTGAENKAAVPLHHLVEKLAEYHAAPPLQGFGISSPEQVTAAIEANAAGAISGSAIVKIIEKNVDKPDQMLTELRDFVTVMKAATRHA | The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. | A4WB03 |
A7H4T0 | THIC_CAMJD | Thiamine biosynthesis protein ThiC | Campylobacter | MKTQMNYAKEGVFTKEMQIVAQKENLSKDFLLENIACGKIIIPANINHKSLDPNGIGFGLRTKVNVNLGVSNDCVDYSEEMKKVELAHKFGIEAIMDLSNYGKTSRFRDELVNVSKAMIGTVPVYDAVGFLEKDLKQIGAKDFLDVVYHHAKSGVDFMTIHAGINSRATHIFKQSKRLTNIVSRGGSVLYAWMMMKDAENPFFEYYDDLLDICLKYDVTLSLGDALRPGSTHDASDGAQISELIELSLLTQRAWDVGVQVMIEGPGHMAINEIEANMQLEKRLCKGAPFYVLGPLVTDIGAGYDHISGAIGGAVAAASGADMLCYVTPAEHLRLPNLEDVREGIVATKIAAHAGDIAKLPKERARDDEMSKARQEIDWEKMFKLAIDGEKAKKMFNERRPDDLNSCSMCGKMCAMNTMNQILKGEDVSLV | Catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction. | A7H4T0 |
P18726 | ZG5A_XENLA | Gastrula zinc finger protein XlCGF51.1A | Xenopus | TGEKPFSCSDCGARFTYRSLLRRHNKIHAEGKSLICSECGKPFTSESALTAHQRSHGGEKPFSCTDCEKCFAQRMHLIEHQRTHTGEKPFSCTVCGEMFTYRAQFSKHMLKHKRKRTEGESLDCSHCGKHFTSRSDLTVHRKSHKGKSPLQCSDCGKCFKYQSQLASHQRVH | May be involved in transcriptional regulation. | P18726 |
Q255B1 | TRMD_CHLFF | tRNA [GM37] methyltransferase | Chlamydia | MEIDILSLFPDYFDSPLRSSILGRAIKNGLLKIQSRDIREFGLGKWKQVDDAPFNNDGMLLMAEPVVQAIRYVKRRESRVIHLSPQGVPLTAQKSRELAKCSHLIFLCGHYEGIDERALEIEVDEEISIGDYVLTNGGIAALVVIDALSRFIPGVLGNQESAEKDSLENGLLEGPQYTRPRVFEGREVPQVLLQGDHQAIARWRKQVSLDRTRERRPDLYVRYLYDRESEDVPQMEADPKQSAFEGECAVVLDVENINRSKRFYSKVFKSNQPIGDKLYIPGKTQMVLHLQEVGLKNKNTAVLSLRLDCENDFYSFLGRWKMLGGTLEQADDRGAVRLVRDFDGHLWAISCKKAK | Specifically methylates guanosine-37 in various tRNAs. | Q255B1 |
C5CQK5 | TATA_VARPS | Sec-independent protein translocase protein TatA | Variovorax | MGSFSIWHWLIVLLVVVMIFGTKKLRNMGSDLGGAVKGFKDGMKDGSTTDAPAASSAPAAQVTGQPANSDKSTIDVEARQKS | 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. | C5CQK5 |
Q9RPX3 | YU58_BRUSU | Type IV secretion system putative outer membrane lipoprotein BRA0058/BS1330_II0058 | Brucella | MRTLVMVACAVSLAACSSPPKPPTVSGRHRIPINSPAAQEELRLQVFPQEPTAQATMWPARPPKQTVSVYFPQDVTVFRPTSAQINQLHTLLWPVPKHINVRGLTDNNCPPPGDTQVARVRALAIYNWLINQGVSASRITISYAPVKDYASNAPLSPGRVLNRRVDIEILRK | The VirB system could be required for the establishment of the replication niche in the host. | Q9RPX3 |
Q5FC64 | ZDHCS_CAEEL | Defective spermatogenesis protein 10 | Caenorhabditis | MSWYSKIYVAVREYRAKHKITGWILTRCLNVLLFIQLILLWWSLYMYVTVTIGYYVQSTIQATIYLIVGSFLFVMSMWSLAKTLFTRVGRVPERYRPSKELEDRLKAVTPMEKNRYVVEKSTPEQLAQQNTILEEMCTYCKVVVAECDQVGRLKYCYECGHIKPDRARHCSSCGKCCIKYDHHCPWINMCVTHVNYKYFLLYIIYTSFLVYWYLLTSLEGAVRYFINQQWTDELGKFLFYLFSFIVGGVFGYYPLGELIIFHYQLISLNETTVEQTKPALLRFDNAADYNMGKYNNFQSVFGWGLWLCPIDSSTQDGLHFDIRYVNTQQRNRFVRIEEEPSSTQSSQSSIQ | Involved in spermatogenesis, specifically in the morphogenesis of fibrous body-membranous organelles (FB-MO), which are Golgi-derived organelles used for transporting sperm-specific components, in spermatocytes and in their localization into budding spermatids . Required for the proper formation of spermatids and spermatozoa . | Q5FC64 |
Q02115 | TAGU_BACSU | Membrane-bound protein LytR | Bacillus | MRNERRKKKKTLLLTILTIIGLLVLGTGGYAYYLWHKAASTVASIHESIDKSKKRDKEVSINKKDPFSVLIMGVDERDGDKGRADTLIYMTVNPKTNTTDMVSIPRDTYTKIIGKGTMDKINHSYAFGGTQMTVDTVENFLDVPVDYFVKVNMESFRDVVDTLGGITVNSTFAFSYDGYSFGKGEITLNGKEALAYTRMRKEDPRGDFGRQDRQRQVIQGIINKGANISSITKFGDMFKVVENNVKTNLTFDNMWDIQSDYKGARKHIKQHELKGTGTKINGIYYYQADESALSDITKELKESLEK | May catalyze the final step in cell wall teichoic acid biosynthesis, the transfer of the anionic cell wall polymers (APs) from their lipid-linked precursor to the cell wall peptidoglycan (PG). | Q02115 |
P76499 | YFCP_ECOLI | Uncharacterized fimbrial-like protein YfcP | Escherichia | MNKSMIQSGGYVLLAGLILAMSSTLFAADNNLHFSGNLLSKSCALVVDGQYLAEVRFPTVSRQDLNVAGQSARVPVVFKLKDCKGPAGYNVKVTLTGVEDSEQPGFLALDTSSTAQGVGIGMEKTDGMQVAINNTNGATFALTNGNNDINFRAWLQAKSGRDVTIGEFTASLTATFEYI | Part of the yfcOPQRSUV fimbrial operon. Could contribute to adhesion to various surfaces in specific environmental niches. Increases adhesion to eukaryotic T24 bladder epithelial cells in the absence of fim genes. | P76499 |
A9KYL6 | UBIB_SHEB9 | Ubiquinone biosynthesis protein UbiB | Shewanella | MTLASIRRGYHVIKTLLQYGLDDVLPPKMTPWYFKLARNSLFWIRNKHKNKPGGERLKLAMQELGPVYIKLGQMLSTRRDLLSDEWASELAMLQDKVPPFDGALARQAIEAELKAPIESLFDDFNETPLASASISQVHTATLKSNGKDVVLKVLRPNVETKIQADLQLMSQTAKLIEYLLGEGNRLRPAEVIEDYRVTILGELNLKLEALNAVKLRNNFLDSDALYVPYVYEEFCYPRLMVMERIYGISVSDIAALKAQGTNFKLLAERGVELFFTQVFRDNFFHADMHPGNIFISRDHPENPYYIGLDCGIMGTLSEVDKRYLAENFLAFFNRDYHRIAQLYIESGWVSEKTDLQAFEQAIKVVCEPMFNKPLDEISFGHVLLELFRTARHFDIVVQPQLVLLEKTLLYIEGLGRQLYPQLDLWQTAKPFLEQWMADQVGPKAMFKKVSTKLPYWADKLPEFPELIYDNLKLGRKLLSSQQQMLDKYLKYQQQAHKSNYLLITSAVLLICGTLLINRDATLWTPYVCLVSGIILWFVGWRSRPKNRKF | Is probably a protein kinase regulator of UbiI activity which is involved in aerobic coenzyme Q (ubiquinone) biosynthesis. | A9KYL6 |
P84017 | TX24_PHONI | Neurotoxin PNTx24A0C3 | Phoneutria | VFCRFNGQQCTSDGQCCYGKCRTAFMGKICM | Acts as a neurotoxin. | P84017 |
B2KIQ4 | WDR76_RHIFE | WD repeat-containing protein 76 | Rhinolophus | MSGSCAAAEEKEGSRQRLQMKVNEYKENQNMSSVSLRSIQKTVLEKTVKVCLVPFSLSNYKSGQFKLPKSLLDKNSKNEVACKKYKKTEIKKACTRILTSKMEATASSKAESTLQKSSIDVHTENNQRQHKSTSDTVSLGVDTESSQDGDSDEDTTSSLDDFSGLSPYERKRLKNISENANFFASLQLSESAARLREMIEKRQPPETKRKKPKKKENETGCRRSMRLLNVDPSGVSLPVTPTEPTLVADENPLLPPGPLEMIPENRDDNSELFKEFLQTWAEVSKTSSKNIEKELSSLKTYKANLSGMVISEDTVYKVTKGAIFSIAFHPSEIKTLVAAGAKSGQVGLWDLTHQPKEDGVYVFQPHSQPVSCLYFSPANPAHMLSLSYDGTLRCGDISSAVFEEVYRNERSSLSSFDFLAEDASTFIVGHWDGSISLVDRRTPGASYEKLISSSLRKIRTVHVHPVQRQYFITAGLRDTHIYDARRLTPSGSQPLISLTEHTKSIASAYFSPLTGNRIVTTCADCKLRFFDSSCISSQIPLLTTIRHNTITGRWLTRLRAVWDPKQEDCVIIGSMAHPRQVEIFHETGEQVHSFLGGECLVSVCSINAVHPTRYILAGGNSSGKIHVFMN | Specifically binds 5-hydroxymethylcytosine (5hmC), suggesting that it acts as a specific reader of 5hmC. | B2KIQ4 |
Q182C6 | YBEY_CLOD6 | Endoribonuclease YbeY | Clostridioides | MDLILDDRQDKLEVSEELIEKIKDIIIECLDYEGYDDNYEVSLSFVDNKEIHELNREYRGVDRVTDVLSFPLLSDDFEDVELEEESLGDIVVSLERALEQSIEYNHSFEREVCFLICHSMFHLLGYDHDTDENTKEMREKEEHILNKLNITRE | Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA. | Q182C6 |
Q9HM64 | VATB_THEAC | V-ATPase subunit B | Thermoplasma | MPKLAYKSVSQISGPLLFVENVPNAAYNEMVDIELENGETRQGQVLDTRKGLAIVQIFGATTGIGTQGTTVKFRGETARLPISEDMLGRVFNGIGEPIDGGPEIIAKERMEITSNAINPYSREEPSEFIETGISAIDGMNTLVRGQKLPIFSGSGLPHNQLAAQIARQAKVLDSSENFAVVFGAMGITSEEANYFTNQFRETGALSRSVMFLNLSSDPSMERIILPRIALTTAEYLAFQKGMHILVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLSTIYERAGKLKGNNGSITQIPILTMPGDDITHPVPDLTGYITEGQIVISRDLNRKDMYPGIDVLLSLSRLMNQGIGKGRTREDHRGLADQLYAAYASGKDLRSLTAIVGEEALSQNDRKYLHFADTFESRYIKQGFFEDRSIEDTLGLGWDLLADLPVQDMKRVKPDHIQKYGRWKKE | Produces ATP from ADP in the presence of a proton gradient across the membrane. The archaeal beta chain is a regulatory subunit. | Q9HM64 |
B7LY16 | TRPA_ECO8A | Tryptophan synthase alpha chain | Escherichia | MERYESLFAQLKERKEGAFVPFVTLGDPGIEQSLKIIDTLIEAGADALELGIPFSDPLADGPTIQNATLRAFAAGVTPAQCFEMLALIRQKHPTIPIGLLMYANLVFNKGIDEFYAQCEKVGVDSVLVADVPIEESAPFRQAALRHNVAPIFICPPNADDDLLRQIASYGRGYTYLLSRAGVTGAENRAALPLNHLVAKLKEYNAAPPLQGFGISAPDQVKAAIDAGAAGAISGSAIVKIIEQHINEPEKMLAALKVFVQPMKAATRS | The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. | B7LY16 |
Q12GB2 | TGT_POLSJ | tRNA-guanine transglycosylase | unclassified Polaromonas | MLEFEVLKTDARTGEGANAHPGSHARRGQLTLTHGVVQTPIFMPVGTYGTVKGVMPQSLHEMGAQIILGNTFHLWMRPGLDVMKQFGGLHRFESWDKPILTDSGGFQVWSLGDMRKISEEGVKFASPVNGDKLFLTPEISMQIQTVLNSDIVMQFDECTPYDTKGHITTESEARSSMELSLRWAKRCVAEFDKLENPNALFGIVQGGMYQNLRHESLEALVELDLPGYAVGGVSVGEPKEEMQRIMAHTPHRLPADKPRYLMGVGTPEDLVEGVGAGIDMFDCVMPTRNARNGHLFTRFGDLKIRNARHKADEQPLDTTCTCYTCKGRTMPDGSTSGGFSRAYLHHLDRCGEMLGPMLASIHNLHYYLNLMQEIRDALDAGRFGEFAARFRTDRLRGV | Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine). | Q12GB2 |
Q1MAQ8 | TSAD_RHIL3 | tRNA threonylcarbamoyladenosine biosynthesis protein TsaD | Rhizobium | MVPFLRILGIETSCDETAAAVVERDAEGHSNVLSDVVLSQLDEHSAYGGVVPEIAARAHVEALDELIEEALKRANVSLNDVDAIAATSGPGLIGGLLVGLMTGKAIARAAGKPLYAINHLEGHALTARLTDGLSFPYLMLLVSGGHTQLILVRGVGQYERWGTTIDDALGEAFDKTAKLLGLPYPGGPAVERMARDGNPDRFDFPRPLVGEARLDFSFSGLKTAVRQAAQDIAPLSDQDVADICASFQKAVSRTLKDRIGRGLQRFKTEFPATGEKPALVVAGGVAANLELRGTLQALCNKNGFRFIAPPLHLCTDNAVMIAWAGLERMATGAAPDTLDVQPRSRWPLDSNAETLIGFGKRGAKA | Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction. | Q1MAQ8 |
P36598 | THI1_SCHPO | Transcription factor ntf1 | Schizosaccharomyces | MNEEIGFLKNQLFADVKDLERKKKRRVPPEQRRRVFRACKHCRQKKIKCNGGQPCISCKTLNIECVYAQKSQNKTLSREYLEELSERQLCLEYIFSRMCPNFNLETKNLISISKKLSENENLPVSKIAEVTNELDTLVRINDQLSRNHISGTTEEMQSSSSLIAGEVQPGISFRDQLKVGKLEDTLYLGPTTSEAFIERLQNELELESISEDDLYSKRLSPSVSYSEFDEQLLLHARSLIPSKAVVEFLINSFFINVQTNLFVYHPHFFKCRLEIFLAMENQIDAGFLCILLMVLAFGNQYTAEQQEDVSKSNFHASNIGNRLFSAALSIFPLVLLQSDVSAVQSSLLIGLYLQSTIYEKSSFAYFGLAIKFAVALGLHKNSDDPSLTQNSKELRNRLLWSVFCIDRFVSMTTGRRPSIPLECISIPYPVILPDLEIPGSQSIVENMRAVINLAKLTNEICDSLYWNPSPSFESQVNSVRRIYARLELWKSDLHSSVVFDESAVQHPLFRSNAHVQMIYDNAIMLTTRVIMVKKLKDKDLTAENRRYIQLCVESATRVINIAHLLLTHKCLSSLSFFGLHVPFASAPILLLSLHYENSQDIQAVVTKLWQVLEFLSSRCEFARESLNYLKSFNKQLSRRNAPDINNPIADFQNSFQNWQSWVGDMSHGDMLSTFKLTGESSNGSNSTPNEAFQPFDQTSSLYNVPGLNKSYVSNQPSLLTPETFLPDPVLNLEVDKQWTAPTFLSWTELLGPTNVSEQSSHTAEQTSNLTLEKNG | Transcription factor that activates the nmt1 promoter. Regulation of thiamine repressible genes. Positively regulates conjugation during meiosis. | P36598 |
A8AKT3 | THIG_CITK8 | Thiazole synthase | Citrobacter | MLRIADKTFDSHLFTGTGKFASSQLMVEAIRASGSQLVTLAMKRVDLRQHNDAILAPLIDAGVTLLPNTSGAKTAEEAIFAAQLAREALGTHWLKLEIHPDARWLLPDPVETLKAAEALVKQGFVVLPYCGADPVLCKRLEEVGCAAVMPLGAPIGSNQGLETRAMLEIIIQQATVPVVVDAGIGVPSHATQALEMGADAVLVNTAIAVADDPVMMAQAFRLAVEAGVMARRAVPGTRSSYAQATSPLTGFLEASA | Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is provided by the thiocarboxylate moiety of the carrier protein ThiS. In vitro, sulfur can be provided by H(2)S. | A8AKT3 |
Q97LP3 | Y511_CLOAB | Nucleotide-binding protein CA_C0511 | Clostridium | MRFVIVTGLSGAGKTQAIRSLEDLGYFCIDNLPPALIPKFAQVCYESESKINKIALVIDIRGGEFFDNLFESLKYLKEAGYKYEILFLDADNEVLIKRFKESRRKHPLAPNGRILNGIQMERKKLKTLYNMANNVIDTSKLATRELREKINSIYQEEGQIESKLIVTVVSFGFKYGIPVDSDLVFDVRFLPNPFYIPELKRFSGIEKPVKDYVMSFDQTKEFVNKIEQLLKFLIPNYLKEGKRQLIVSIGCTGGRHRSVTIANEIYERLKNDGETVNIDHRDIEEDINKGGKKL | Displays ATPase and GTPase activities. | Q97LP3 |
Q9BXA7 | TSSK1_HUMAN | Serine/threonine-protein kinase 22A | Homo | MDDAAVLKRRGYLLGINLGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLPREIEILAMLNHCSIIKTYEIFETSHGKVYIVMELAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDSGRMALSKTFCGSPAYAAPEVLQGIPYQPKVYDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRVNFPRSKHLTGECKDLIYHMLQPDVNRRLHIDEILSHCWMQPKARGSPSVAINKEGESSRGTEPLWTPEPGSDKKSATKLEPEGEAQPQAQPETKPEGTAMQMSRQSEILGFPSKPSTMETEEGPPQQPPETRAQ | Testis-specific serine/threonine-protein kinase required during spermatid development. Phosphorylates 'Ser-288' of TSKS. Involved in the late stages of spermatogenesis, during the reconstruction of the cytoplasm. During spermatogenesis, required for the transformation of a ring-shaped structure around the base of the flagellum originating from the chromatoid body. | Q9BXA7 |
Q8Z996 | TILS_SALTI | tRNA(Ile)-lysidine synthetase | Salmonella | MTTLTLNTSLLSSRRILAAFSGGLDSTVLLHQLVLWRERHPDVTLRAIHIHHGLSPHADSWVRHCETVCERWQVPLVVERVTLADNGLGIEAHAREARYRAFAQTLLPGEVLATAQHLDDQCETFLLALKRGSGPAGLSAMGERSPFAGTLLLRPLLRETRKTLEQWAVRHGLCWIEDESNQDDAYDRNFLRLRALPLLQQRWPHFPAAVARSATLCAEQERLLDELLASDLTDCITTEGTLRLSPLMSMSDVRRAAILRRWLAMRNAPMPSRDALERIWQEVALARDDASPCLRFGDHEIRRYQSQLWWIKTVAGQHETTVAWPVWQTPLALPAGLGTVQLVPGGELRRPREEESVSIRFKAPGLLHIVGRHGGRKLKKIWQEQGIPPWRRDTTPLLFYGETLIAAAGVFVTREGAAEDKEGVSLVWHA | Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine. | Q8Z996 |
B2U6Y7 | TRPA_RALPJ | Tryptophan synthase alpha chain | Ralstonia | MSRIAQTFSQLSAQGRKGLIPFITAGDPYPEMTVDLMHALVKGGSNVIELGVPFSDPMADGPVIQRASERALAKKVGLRTVLEYVRAFRATDLTTPVVLMGYANPIERMGVDAFAKAASEAGVDGVLVVDYPPEECEAFAKTMRAAGIDPIFLLAPTSTEARIAQIARVASGYIYYVSLKGVTGAATIDLDAVAARIPQIRQHARLPVGVGFGIRDAATARAISGVADAVVIGSRIVQLLEEAPREQAVQYLTDFIAEIRQALDA | The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. | B2U6Y7 |
B3DR08 | TILS_BIFLD | tRNA(Ile)-lysidine synthetase | Bifidobacterium | MAYSARLRKAVGAVRTTLSAVELCDVQAPEFAQHGDHAVASDAPLVLVACSGGRDSMALAAVSHIVCTSMGVRCGVVIVDHGLQEGSEQVAGEAANRCRALGLGPVIVRNATVQARGEGLEAAARQARYNELCAAARESGAIAVLLAHTMDDQAETVLIGLLRSRGVDALAGMPQVFTRSGVTFARPLLTLTRAETTGICEDLGVEYWDDPTNGDAVDGELPNDYPLRSRVRHDLLPAIERFAGFNVTRHFAESARLARMDKEYLDQRSDEVMGEAVTTVDWPASSAAVSTDTPRACAAGDTNDSSHGVGLMISVRRIAREPEAIRLRVIAHALSQAGVNASAAQIAAIDRLVVDWHGQGGVSLPRGYSANRKKHVIRVCQDGAHANR | Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine. | B3DR08 |
P85800 | VARI_AMBVA | Variegin | Amblyomma | SDQGDVAEPKMHKTAPPFDFEAIPEEYLDDES | Thrombin inhibitor. Does not inhibit other serine proteases. | P85800 |
Q9JT57 | TYSY_NEIMA | Thymidylate synthase | Neisseria | MKAYLDLMRHVLDNGTDKSDRTGTGTRSVFGYQMRFDLGKGFPLLTTKKLHLRSIIHELLWFLKGDTNIKYLKDNNVSIWDEWADENGDLGPVYGYQWRNWPAPDGRHIDQIANVLEQIKKNPDSRRLIVSAWNPALVDEMALPPCHALFQFYVADGKLSCQLYQRSADIFLGVPFNIASYALLTMMMAQVCGLEAGEFVHTFGDAHLYRNHFEQAALQLEREPRALPVMKINPEVKDLFAFKFEDFELEGYDPHPHIKAAVSV | Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. | Q9JT57 |
Q63EC6 | TRPA_BACCZ | Tryptophan synthase alpha chain | Bacillus cereus group | MGVERIQAAFENGKKAFIPYVMGGDGGLEILKERIRFLDEAGASIVEIGIPFSDPVADGPTIQRAGKRALDSGVTVKGIFQALIEARKEVQIPFVLMTYLNPVLAFGKERFIENCMEAGVDGIIVPDLPYEEQDIIAPLLREANIALIPLVTVTSPIERIKKITSESEGFVYAVTVAGVTGVRQNFKDEIHSYLEKVKSHTHLPVVAGFGISTKEHVEEMVTICDGVVVGSKVIELLENEKREEICEFIQATKQKEEA | The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. | Q63EC6 |
Q7VRL0 | TPIS_BLOFL | Triose-phosphate isomerase | Candidatus Blochmannia | MKNLSIIANWKLNGNKNTITNSLINLTTQLTNIPQYIKIAIAPPILYIDMVKNHLTSYNNKTIELCSQNVDIHLSGAFTGDISASMLKDLSVKYVLIGHSERRIYHKENNSLIAQKFSIIKQTELIPILCIGENKEERDSGSTQSICIQQIDSIIKLVGIKAFENTIIAYEPVWAIGSGSSASPRNVQSIHQFIRNYIAQYDKTIANQISIQYGGSITTDNVLEFITQKDIDGVLVGSASLDIRNLIKIINLSSNLIKKTYQ | Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P). | Q7VRL0 |
Q6HLU3 | TRPA_BACHK | Tryptophan synthase alpha chain | Bacillus cereus group | MGVERIKAAFENGKKAFIPYVMGGDGGLEILKERIRFLDEAGASIVEIGIPFSDPVADGPTIQRAGKRALDSGVTVKGIFQALIEVREEVQIPFVLMTYLNPVLAFGKERFIENCMEAGVDGIIVPDLPYEEQDIIAPLLREANIALIPLVTVTSPIERIKKITSESEGFVYAVTVAGVTGVRQNFKDEIHSYLEKVKSHTHLPVVAGFGISTKEHVEEMVTICDGVVVGSKVIELLENEKREEICEFIQATKQKEEA | The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. | Q6HLU3 |
Q896K7 | VATE1_CLOTE | V-ATPase subunit E 1 | Clostridium | MSRLENLTSKIIKDSEEKAKIILDEAKREEEKIMLGQKQEGESIKSKIIEKAYLESKNRKERIISNSHLFVRNRKLEAKQEVIDKVYKEALNKLAKLNKEEYLNFIKDSILALEIYGDEEIILSQDEKYINKETIEEINKELKSKGKKGEIKISDKKRDFRGGFILNKDGIEINNTFEALILSLKDDLEPVIIDTLFS | Produces ATP from ADP in the presence of a proton gradient across the membrane. | Q896K7 |
C5BSX6 | Y3824_TERTT | Nucleotide-binding protein TERTU_3824 | Teredinibacter | MRLLIISGRSGSGKTTALHLLEDEGYTCIDNLPVDLLPALIEQLSTSDRPSPRVAIGIDARNINNDLSRLMAMIEVGPLPRESYQVIYLDSSREVLLKRYSETRRKHPLSDGLTDLNEAIERERIILEPISNAADVTIDTSQLNLHELRSAIKYLVVGSDREGMAVLFKSFGFKYGLPVDADFVFDVRCLPNPYWDAGLRKLSGLSPEVIAFLNGEEQVEEMYNDILTFMRKWIPRFENNNRSYLTIAIGCTGGFHRSVYMSERLAKALKADYKNVQTRHRQIPDSSAPKHS | Displays ATPase and GTPase activities. | C5BSX6 |
Q5WSX6 | TRHO_LEGPL | tRNA hydroxylation protein O | Legionella | MKDIIIASFYKFIPLNDFESLREPILTKMHEIGIKGTIILAHEGVNGGFAGNREQMYIFYDYLRSDSRFADLHFKETYDNKNPFDKAKVKLRKEIVTMGVQKVDPSYNAGTYLSPEEWHQFIQDPNVILLDTRNDYEYELGTFKNAINPDIENFREFPDYVQRNLIDKKDKKIAMFCTGGIRCEKTTAYMKELGFQHVYQLHDGILNYLESIPEGESLWEGKCFVFDDRVAVDQKLDRVYPQLPQDYKYEREQK | Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs. | Q5WSX6 |
A6U170 | XERC_STAA2 | Tyrosine recombinase XerC | Staphylococcus | MNHIQEAFLNTLKVERNFSEHTLKSYQDDLIQFNQFLEQEHLQLKTFEYRDARNYLSYLYSNHLKRTSVSRKISTLRTFYEYWMTLDENIINPFVQLVHPKKEKYLPQFFYEEEMEALFKTVEEDTSKNLRDRVILELLYATGIRVSELVNIKKQDIDFYANGVTVLGKGSKERFVPFGAYCRQSIENYLEHFKPIQSCNHDFLILNMKGEAITERGVRYVLNDIVKRTAGVSEIHPHKLRHTFATHLLNQGADLRTVQSLLGHVNLSTTGKYTHVSNQQLRKVYLNAHPRAKKENEI | Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. The XerC-XerD complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids. | A6U170 |
G3Y423 | YANE_ASPNA | Yanuthone D biosynthesis cluster protein E | Aspergillus subgen. Circumdati | MAPCKPRTFTAGEDPLTKFDGAISVATMPRPADRQFLFHGIMRPSRGIYAKLVATGKKPPTHFHPSQWEFFRVLRGNLTVDINGVPVHRTVDDGEMAVPPYTHHVIYGTPGTEMNEVEFLVSATDEEEGATAMDQEFFENWYGYQEDIFQRGEKIDLIQVLAMFDAGGTYLSPPWWVPFRAWVGLILGIVIGRWIGGLLGYAPFYPEWTTNWDAACDRMEQSWFQRRYADRGAQQRAREKFQVQKGQGTVAKGEKSE | Part of the gene cluster that mediates the biosynthesis of yanuthone D, a fungal isoprenoid epoxycyclohexenone that acts as an antibiotic against fungi and bacteria . The first step of the pathway is the synthesis of 6-methylsalicylic acid (6-MSA) by the polyketide synthase yanA . 6-MSA is then converted to m-cresol by the decarboxylase yanB . The cytochrome P450 monooxygenase yanC then catalyzes the oxidation of m-cresol to toluquinol . Epoxidation of toluquinol is then performed by the short chain dehydrogenase yanD, with the help of yanE, and a further prenylation by yanG leads to 7-deacetoxyyanuthone A . The next step is the hydroxylation of C-22 of 7-deacetoxyyanuthone A by the cytochrome P450 monooxygenase yanH to yield 22-deacetylyanuthone A . O-Mevalon transferase yanI then attaches mevalon to the hydroxyl group of 22-deacetylyanuthone A to produce yanuthone E . Finally, the FAD-dependent monooxygenase yanF oxidizes the hydroxyl group at C15 of yanuthone E to form yanuthone D . Furthermore, several branching points in the pathway lead to the production of yanuthones F and G from 7-deacetoxyyanuthone A; yanuthones H and I from 22-deacetylyanuthone A; and yanuthone J from yanuthone E . YanE is also involved in the synthesis of yanuthone X1 which does not have 6-methylsalicylic acid (6-MSA) as precursor . | G3Y423 |
P17795 | VIRB5_AGRFC | Protein virB5 | Agrobacterium tumefaciens complex | MKIMQLVAAAMAVSLLSVGPARAQFVVSDPATEAETLATALETAANLEQTITMVAMLTSAYGVTGLLTSLNQKNQYPSTRDLDTEMFSPRMPMSTTARAITTDTDRAVVGGDAEADLLRSQITGSANSAGIAADNLETMDKRLTANAETSTQLSRSRNIMQATVTNGLLLKQIHDAMIQNVQATSLLTMTTAQAGLHEAEEAAAQRKEHQKTAVIFGAVP | VirB proteins are suggested to act at the bacterial surface and there play an important role in directing T-DNA transfer to plant cells. | P17795 |
A7ZX76 | THII_ECOHS | tRNA 4-thiouridine synthase | Escherichia | MKFIIKLFPEITIKSQSVRLRFIKILTGNIRNVLKHYDETLAVVRHWDNIEVRAKDENQRLAIRDALTRIPGIHHILEVEDVPFTDMHDIFEKALVQYRDQLEGKTFCVRVKRRGKHDFSSIDVERYVGGGLNQHIESARVKLTNPEVTVHLEVEDDRLLLIKGRYEGIGGFPIGTQEDVLSLISGGFDSGVSSYMLMRRGCRVHYCFFNLGGAAHEIGVRQVAHYLWNRFGSSHRVRFVAINFEPVVGEILEKIDDGQMGVILKRMMVRAASKVAERYGVQALVTGEALGQVSSQTLTNLRLIDNVSDTLILRPLISYDKEHIINLARQIGTEDFARTMPEYCGVISKSPTVKAVKSKIEAEEEKFDFSILDKVVEEANNVDIREIAQQTEQEVVEVETVNGFGPNDVILDIRSVDEQEDKPLKVEGIDVVSLPFYKLSTKFGDLDQNRTWLLWCERGVMSRLQALYLREQGFNNVKVYRP | Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiamine biosynthesis pathway. The sulfur is donated as persulfide by IscS. | A7ZX76 |
P38709 | UGPA2_YEAST | UDP-glucose pyrophosphorylase | Saccharomyces | MTVFSGVNKIEFEGTFEGIGKDVVMSQMIRALQKHFPSIRDKNYEFSLFLHIFQRYVLENTSITHDLVCDKIRLPIIDEVVELDDIKNYGLLEGKLLSKLAILKLTGKANPIIGKESPLFEVKNGMSSLDVIVRQTQNLNVRYNSDVPLIFMTSLETESQVSNFLEEHYSSSKVRWKTVVQSSFPQIDKDRLLPIDLQINSHENDFWYPCGTGNLTDTLYFSGELDKLIAQGKEILFVSNVDNLGATGDLNILNFIINEKIEYLVEVVERTANVSNTGVLATYKGKLRSVYYNCLSNESASTCRIVNTNNIWIDLKKLKVLIESNSLNLPIHSSESKITHKNEEIECLQFKTQLVDCIAFFPNSRVLKVSRDRFLPLRTCKDLFLLKSTLYDLDSNGTFNLYPLKFGLLPSIDLGDEFATYETFKIGVPDIPNILELEHLTVMGNVFFGRNITLKGTVIIICDENDVITVPDGSILENVTIWHKSQLEDMNGY | Plays a central role as a glucosyl donor in cellular metabolic pathways. | P38709 |
A4QJH4 | TI214_AETCO | Translocon at the inner envelope membrane of chloroplasts 214 | Aethionema | MMVFQSFILGNLVSLCMKIINSVVVVGLYYGFLTTFSIGPSYLFLLRARVMDEGEEGTEKKVSATTGFIAGQLMMFISIYYAPLHLALGRPHTITVLALPYLLFHFFWNNHKHFFDYGSTTRNEMRNLRIQCVFLNNLIFQLFNHFILPSSMLARLVNIYMFRCNNKMLFVTSSFVGWLIGHILFMKWVGLVLVWIQQNHSIRSNVLIRSNKYKFLVSELRNSMARIFSILLFITCVYYLGRIPSPIFTKKLKGTSETEERGGTKQDQEVSTEEAPFPSLFSEEREDLDQIDEIDEIRVNAKEQINKDDEFHIRTYYNYKKVSENLDGNKENSNLEFLKIKKKEDSVLWFEKPFVTLVFDYKRWNRPNRYIKNDQIENAVRNEMSQYFFSACQSDGKDRISFSYPRNISTFFDMIQKKIPSFRREKTPSDKFSTCWSLINEEKKENLKKEFLHRIEALDKEWSVEHILEKTTRFCHNETRKEYLPKIYDPFLQGISRGRIQRLVPFQIITETYIKNNIGRSWINKIHGILLNINYQKFEQTIEKFNRKSSAIEKKLSYFFDPQEEKLNSEEEIKIFKFLFDVVLTDSNDQMLSKNFLDVHEIHKKVPRWSYKLRSDLEELEGENEETIPMEPGIRARKAKRVVIFTDTEPHNEIYTNLKNNQNYDQNDEMVLIRYSQQSDFRREIIQGSMRPQRRKTVIWEFCQANMHSPFFFDKIGKFFFFSFDIRGLTKKILRNFMWKNGKKKLDKKYEDKSKRKEKRRLEIAEVWDSFLFAQILRSSLLVTQSILRKYIILPLLIIIKNSVRMLLFQIPEWSEDLKDWKREMHVKCTYNGVQLSETEFPRKWLTDGIQIKILFPFYLKPWHKSKFHSSQKGRLKKTKDKNDFCFLTVWGMETELPFGSAQKQPSFFEPFFKEFKKKMKKYKTKSLLVLRFFKERDKIFAKEIKNGILKNFIFIKGKRNDLSKGNRIPLFDLREIYELTETKNDSITSNPIIHELSVQNRSMEWKNSSFSENKIKNLIDRINTIRNQIEAISKEKKKITNSSNKTPYESKIIESSKKKWQIVKRINTRLIRKIFYFVKFCLEQLSLGIVVGIMNIPRMTTQFFFESTKKILDKSIYKNEETEDKITKKKNTIYLISTIKKLISNKKKMSYDICSLSQAYVFYKLSQLQVSNFSKLRAVLEYNICGTSLFVTNQIKDFFQKHGIFHYKLKEKTFLNSEINPWKNWLRSHYQYNLPEIVWARLVTEKWKNQINQNSLVLNKSLNKEDSYEKNKFDNYKKLNYLKADSLLNPKQKQNFKKDSIYNIFCYKSINSKEKSFDMPLEIIIDNFLVSSFRGKSNIRDIGEFRTRKYLEWRIIPFWFIKKVNIESAVDTKSQKIYIKTQVQNSEKIDKITKMGLANQKSLFFDWMGMNEEILNYPIANLEFLFFPEFFLFSSTYKIKPWVIPIKLLLFNFNEKKNLNKIITRNKNGFIPSNEKKYLRFYNLTNDEKEKQRNPQLALPNQEKNIEENYAESKIKKRQNKKQYKSNTEVELDLFLTRYSRFQLRWNFFLNKKILNNVKIYCLLVRLKNPNKIAISSIERGEMSLDILMIEKNLTFAKLMKKGILIIEPLRSSVKNDGQLIIYRTIGISLVHKNNHQISQRDKKKIEKSITQLKKKTVNRKKNNYDFFVPEKILSPKRRREFRILICSKLKKKSTRYRNSRFDKNIQNCGQVLNQTKYLDNDKTNLINLKFFLWPNFRLEDLACMNRYWFNTNNGNHFSMIRIHMYTRLKINS | Involved in protein precursor import into chloroplasts. May be part of an intermediate translocation complex acting as a protein-conducting channel at the inner envelope. | A4QJH4 |
D6PXE8 | VM3B_NAJAT | Snake venom metalloproteinase | Naja | MIQALLVIICLAVFPHQGSSIILESGNVNDYEVVYPQKVPALLKGGVQNPQPETKYEDTMRYEFQVNGEPVVLHLERNKGLFSEDYTETHYAPDGREITTSPPVQDHCYYHGYIQNEADSSAVISACDGLKGHFEHQGETYFIEPLKISNSEAHAIYKDENVENEDETPEICGVTETTWESDESIEKTSQLTNTPEQDRYLQDKKYIEFYVIVDNRMYRYYNNDKPAIKIRVYEMINAVNTKFRPLKIHIALIGLEIWSNKDKFEVKPAASVTLKSFGEWRETVLLPRKRNDNAQLLTGIDFNGNTVGRAYIGSLCKTNESVAIVQDYNRRISLVASTMTHELGHNLGIHHDKASCICIPGPCIMLKKRTAPAFQFSSCSIREYREYLLRDRPQCILNKPLSTDIVSPPICGNYFVEVGEECDCGSPQACQSACCNAATCQFKGAETECRVAKDDCDLPELCTGQSAECPTDSLQRNGHPCQNNQGYCYNRTCPTLTNQCITLLGPHFTVSPKGCFDLNMRGDDGSFCGMEDGTKIPCAAKDVKCGRLYCTEKNTMSCLIPPNPDGIMAEPGTKCGDGMVCSKGQCVDVQTAY | Snake venom zinc protease that inhibits the classical and alternative pathways of complement by cleaving factor B, C6, C7, and C8. Also slowly and selectively degrades alpha-chain of fibrinogen (FGA), and shows edema-inducing activity. | D6PXE8 |
Q9Z7W2 | YIDD_CHLPN | Putative membrane protein insertion efficiency factor | Chlamydia | MSFKRFLQQIPVRICLLIIYLYQWLISPLLGSCCRFFPSCSHYAEQALKSHGFLMGCWLSIKRIGKCGPWHPGGIDMVPKTALQEVLEPYQEIDGGDSSHFSE | Could be involved in insertion of integral membrane proteins into the membrane. | Q9Z7W2 |
B2HNX5 | TAM_MYCMM | Trans-aconitate 2-methyltransferase | Mycobacterium | MWDPDVYLAFADHRGRPFYDLVSRIGAKRARRVVDLGCGPGNLTRYLARRWPEAIIEAWDSSPQMVAAARERGIDATTGDLRTWKPKPDTDVVISSAALHWVPEHADLMVQWATELPHGSWIAVQVPGNFETPSHAVVRALARREPYAKLMRDIPFRVGAVVGSPASYAGLLMDAGCKVDAWETTYLHQLTGKNPVLEWITGTALVPVRERLDDVSWEQFRQELIPLLDDAYPPRSDGTTMFPFRRLFIVAEVGGARRSADVS | Catalyzes the S-adenosylmethionine monomethyl esterification of trans-aconitate. | B2HNX5 |
Q8Z7A8 | TPX_SALTI | Thioredoxin-dependent peroxiredoxin | Salmonella | MSQTVHFQDNPVTVANVIPQAGSKAQAFTLVAKDLSDVSLSQYAGKRKVLNIFPSIDTGVCAASVRKFNQLATEVENTVVLCVSADLPFAQSRFCGAEGLSNVITLSTLRNNEFLKNYGVEIVDGPLKGLAARAVIVLDENDNVIFSQLVDEITHEPDYDAALNVLKA | Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. | Q8Z7A8 |
Q8U0I8 | UPPS_PYRFU | Undecaprenyl pyrophosphate synthase | Pyrococcus | MIYRIISHIPSIFFKPAYDLYERYLLEKVKAGVIPKHVAIIMDGNRRWARKREKPPWYGHFFGSKKLEEIVEWCHELGIRILTVYAFSTENFKRSKEEVDRLMKLFEEKFRELVTDRRVHEYGIRVNVMGRKELLPKNVREAAEEAERVTRKYNNYFLNIALAYGGRSEIVDAIKDIVNDVLEGRLKLEDINEEIVRKYLYVPNMPDPDIVIRTGGEVRISNFLLYQIAYSELFFVDVYFPEFRKIDFLRIIREFQKRERRFGR | Catalyzes the sequential condensation of isopentenyl diphosphate (IPP) with geranylgeranyl diphosphate (GGPP) to yield (2Z,6Z,10Z,14Z,18Z,22Z,26Z,30E,34E,38E)-undecaprenyl diphosphate (tritrans,heptacis-UPP). It is probably the precursor of glycosyl carrier lipids. | Q8U0I8 |
Q8E471 | UVRB_STRA3 | Excinuclease ABC subunit B | Streptococcus | MIDRKDTNRFKLVSKYSPSGDQPQAIETLVDNIEGGEKAQILKGATGTGKTYTMSQVIAQVNKPTLVIAHNKTLAGQLYGEFKEFFPDNAVEYFVSYYDYYQPEAYVPSSDTYIEKDSSVNDEIDKLRHSATSSLLERNDVIVVASVSCIYGLGSPKEYADSVVSLRPGQEISRDQLLNNLVDIQFERNDIDFQRGKFRVRGDVVEVFPASRDEHAFRIEFFGDEIDRIREIESLTGRVLGEVEHLAIFPATHFMTNDEHMEEAISKIQAEMENQVELFEKEGKLIEAQRIRQRTEYDIEMLREMGYTNGVENYSRHMDGRSEGEPPFTLLDFFPEDFLIMIDESHMTMGQIKGMYNGDRSRKEMLVNYGFRLPSALDNRPLRREEFESHVHQIVYVSATPGDYEMEQTDTVVEQIIRPTGLLDPEVEVRPSMGQMDDLLGEINLRTEKGERTFITTLTKRMAEDLTDYLKEMGVKVKYMHSDIKTLERTEIIRDLRLGVFDVLIGINLLREGIDVPEVSLVAILDADKEGFLRNERGLIQTIGRAARNSNGHVIMYADKITDSMQRAMDETARRRRLQMDYNEKHGIVPQTIKKEIRDLIAITKSNDSDKPEKVVDYSSLSKKERQAEIKALQQQMQEAAELLDFELAAQIRDVILELKAID | 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. | Q8E471 |
A8AKQ0 | XGPT_CITK8 | Xanthine phosphoribosyltransferase | Citrobacter | MSEKYVVTWDMLQIHARKLASRLMPSEQWKGIIAVSRGGLVPGALLARELGIRHVDTVCISSYDHDNQRELKVLKRAEGDGEGFIVIDDLVDTGGTAVAIREMYPKAHFVTIFAKPAGRPLVDDYVIDIPQDTWIEQPWDMGVVFVPPISGR | Purine salvage pathway enzyme that catalyzes the transfer of the ribosyl-5-phosphate group from 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to the N9 position of the 6-oxopurines guanine and xanthine to form the corresponding ribonucleotides GMP (guanosine 5'-monophosphate) and XMP (xanthosine 5'-monophosphate), with the release of PPi. To a lesser extent, also acts on hypoxanthine. | A8AKQ0 |
B5RMW0 | TSAD_BORDL | tRNA threonylcarbamoyladenosine biosynthesis protein TsaD | Borrelia | MKVLGIESSCDDCCAAIVENGNTILSNIKLSQKEHKKYYGIVPEIASRLHTEFIMYVCQQAIISAQINISEIDLIAVTSQPGLIGSLIVGVNFAKGLSIALKKPLICIDHILGHLYAPLLNHTIEYPFLSLVLSGGHTILAKQNNFDDIEILGRTLDDACGEAFDKIAKHYKMGFPGGPNIEKLAIDGNQYAFNFPITIFDKKENRYDFSYSGLKTACIHQLEKFKNNNAQITNNNIAASFQRAAFENLIIPIKRAIKDTNIKKLIISGGVASNLYLREKIKNLEIETYYPPIDLCTDNAAMIAGIGYLMYLKYGASSIETNANSRIENYKYTKGVKL | Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction. | B5RMW0 |
P39603 | YWCE_BACSU | Spore morphogenesis and germination protein YwcE | Bacillus | MMDMFFAYLLVASATPLFIWLDNKKVALSAIPPIILMWVFFFFYATESLSPLGHTLMIILFAVNVIVAHIAAFIIYGLPYLRRKRSS | Required for proper spore morphogenesis. Important for spore germination. | P39603 |
A1K7B7 | TRUB_AZOSB | tRNA-uridine isomerase | Azoarcus | MQRKIPRRIVDGVLLLDKPSGMTSNGALQTARRLLNAAKAGHTGTLDPMASGLLPLTFGEATKFSQILLDADKTYEAGVKLGTTTDTGDADGNVVAEHPVSVTREALEEVLSRFRGEIDQLPPMYSALKRDGKPLYEYARAGIEIEREVRRVTIHDLELIAFSGEHFSMRVRCSKGTYIRTLAMDIGAALGCGAYLDALRRTAIGDFDAARAVTLEALEASPAAMRDGLLEPVDALVAHFPKVELQPAEAAAILQGRELRKPEDGQGSVRLFCGGRFLGVGEWQSGSLRPKRLIATQTGQ | Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs. | A1K7B7 |
Q6NYY9 | VMP1_DANRE | Vacuole membrane protein 1 | Danio | MAANGAECEQPQKRLGPKDKQNGSSTDSSLRERKQLDREERLSLVLWKRPFITLQYFFLETAITLKEWTWKLWQRRGVVFLTVVLFSLFSLAYSIEGAHQEYVQHLEKKFLWCAYWVGLGILSSVGLGTGLHTFLLYLGPHIASVTLAAYECGSVNFPEPPYPAQIVCPEDEALQESISLWTIMSKVRLEACMWGAGTAIGELPPYFMARAARMSGADPDDEDYEEFEEMLEHSQSAQDFASRAKLAVQNMVQKVGFFGILACASIPNPLFDLAGITCGHFLIPFWTFFGATLIGKAIIKMHIQKLFVIITFSKHIVEQMVSLIGVIPGVGASLQKPFREYLEAQRTKLHNPAGDGAAAGESWLSWVFEKVVLVMVCYFILSIINSMAQSYAKRLQQKKYSEEKTK | Phospholipid scramblase involved in lipid homeostasis and membrane dynamics processes. Has phospholipid scramblase activity toward cholesterol and phosphatidylserine, as well as phosphatidylethanolamine and phosphatidylcholine. Required for autophagosome formation: participates in early stages of autophagosome biogenesis at the endoplasmic reticulum (ER) membrane by reequilibrating the leaflets of the ER as lipids are extracted by atg2 (atg2a or atg2b) to mediate autophagosome assembly. In addition to autophagy, involved in other processes in which phospholipid scramblase activity is required. Modulates ER contacts with lipid droplets, mitochondria and endosomes. | Q6NYY9 |
Q9C040 | TRIM2_HUMAN | RING-type E3 ubiquitin transferase TRIM2 | Homo | MASEGTNIPSPVVRQIDKQFLICSICLERYKNPKVLPCLHTFCERCLQNYIPAHSLTLSCPVCRQTSILPEKGVAALQNNFFITNLMDVLQRTPGSNAEESSILETVTAVAAGKPLSCPNHDGNVMEFYCQSCETAMCRECTEGEHAEHPTVPLKDVVEQHKASLQVQLDAVNKRLPEIDSALQFISEIIHQLTNQKASIVDDIHSTFDELQKTLNVRKSVLLMELEVNYGLKHKVLQSQLDTLLQGQESIKSCSNFTAQALNHGTETEVLLVKKQMSEKLNELADQDFPLHPRENDQLDFIVETEGLKKSIHNLGTILTTNAVASETVATGEGLRQTIIGQPMSVTITTKDKDGELCKTGNAYLTAELSTPDGSVADGEILDNKNGTYEFLYTVQKEGDFTLSLRLYDQHIRGSPFKLKVIRSADVSPTTEGVKRRVKSPGSGHVKQKAVKRPASMYSTGKRKENPIEDDLIFRVGTKGRNKGEFTNLQGVAASTNGKILIADSNNQCVQIFSNDGQFKSRFGIRGRSPGQLQRPTGVAVHPSGDIIIADYDNKWVSIFSSDGKFKTKIGSGKLMGPKGVSVDRNGHIIVVDNKACCVFIFQPNGKIVTRFGSRGNGDRQFAGPHFAAVNSNNEIIITDFHNHSVKVFNQEGEFMLKFGSNGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDGSGSFLSYINTSADPLYGPQGLALTSDGHVVVADSGNHCFKVYRYLQ | UBE2D1-dependent E3 ubiquitin-protein ligase that mediates the ubiquitination of NEFL and of phosphorylated BCL2L11. Plays a neuroprotective function. May play a role in neuronal rapid ischemic tolerance. | Q9C040 |
Q5D7I6 | TRIM5_ALOSA | TRIM5alpha | Alouatta | MASKILVNIKEEVTCPICLELLTEPLSLDCGHSFCQACITANHKESRERSCPLCRVSYHSENLRPNRHLANIAERLREVMLSPEEGQKVDRCARHGEKLLLFCQQHGNVICWLCERSEEHRGHRTSLVEEVAQKYREKLQAALEMMRQKEQDAEMLEADVREEQASWKIQIENDKTSTLAEFKQLRDILDCEESNELQKLEKEEENLLKRLVQSENDMVLQTQSIRVLIADLERRLQGSVMELLQGVEGVIKRIKNVTLQKPETFLNEKRRVFQAPDLKGMLQVFKELKEVQCYWAHVTLIPNHPSCTVISEDKREVRYQEQIHHHPSMEVKYFYGILGSPSITSGKHYWEVDVSNKSAWILGVCVSLKCIGNFPGIENYQPQNGYWVIGLRNADNYSAFQDAVPETENYQPKNRNRFTGLQNADNCSAFQNAFPGIQSYQPKKSHLFTGLQNLSNYNAFQNKVQYNYIDFQDDSLSTPSAPLIVPLFMTICPKRVGVFLDYEACTVSFFNVTSNGYLIYKFSNCQFSYPVFPYFSPMTCELPMTLCSPSS | Capsid-specific restriction factor that prevents infection from non-host-adapted retroviruses. Blocks viral replication early in the life cycle, after viral entry but before reverse transcription. In addition to acting as a capsid-specific restriction factor, also acts as a pattern recognition receptor that activates innate immune signaling in response to the retroviral capsid lattice. Binding to the viral capsid triggers its E3 ubiquitin ligase activity, and in concert with the heterodimeric ubiquitin conjugating enzyme complex UBE2V1-UBE2N (also known as UBC13-UEV1A complex) generates 'Lys-63'-linked polyubiquitin chains, which in turn are catalysts in the autophosphorylation of the MAP3K7/TAK1 complex (includes TAK1, TAB2, and TAB3). Activation of the MAP3K7/TAK1 complex by autophosphorylation results in the induction and expression of NF-kappa-B and MAPK-responsive inflammatory genes, thereby leading to an innate immune response in the infected cell. Plays a role in regulating autophagy through activation of autophagy regulator BECN1 by causing its dissociation from its inhibitors BCL2 and TAB2. | Q5D7I6 |
Q6F7W2 | XPT_ACIAD | Xanthine phosphoribosyltransferase | Acinetobacter | MYALEQKILNEGIVLSDQVLKVDAFLNHQIDPVLMQQIGKEFAARFKDTGITKIVTIEASGIAPAVMAGLELGVPVIFARKYQSLTLKDDLYRSKVFSFTKQVESTIAISNKHINAEDKVLVIDDFLANGQAALGLIDLIHQANADIVGVGIVIEKSFQPGRDLLLEKGYRVESLARVASLTNGQVTFVIE | Converts the preformed base xanthine, a product of nucleic acid breakdown, to xanthosine 5'-monophosphate (XMP), so it can be reused for RNA or DNA synthesis. | Q6F7W2 |
Q04TG5 | YBEY_LEPBJ | Endoribonuclease YbeY | Leptospira | MIFNCGILFRKELKDFPCELGLLLVGDSDMRKINRLRRGKDKTTDVLSFPLEFDSAPLQNVLQKRTGFDSNSLPPIALGEIVISVDTLEKQAVEIGHSVKDEFYRLLVHGFLHLLGYDHERGEEEERIMKLKEDECLEILQEL | Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA. | Q04TG5 |
Q9PGJ7 | TPIS_XYLFA | Triose-phosphate isomerase | Xylella | MRPKIVAGNWKLHGSHAFAQALVAQVAAGLPLLGVSVIILPPLLYLSDLAQRFKGEGLAFGAQNVSHHDKGAYTGEVSAAMVADVGAHYTLVGHSERREYHHEDSELVARKFAAALSAGLRPILCVGESLPQREAGQAEVAIAMQLAPVLALVGPQGVARGLIAYEPVWAIGTGRHADPSQVQAMHAFIRGEIARQDARIGDSLLILYGGGIKPCNAAELFSQQDVDGGLIGGASLVADDFLAIARATV | Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P). | Q9PGJ7 |
C1CHZ8 | TRHO_STRZP | tRNA hydroxylation protein O | Streptococcus | MAKDIRVLLYYLYTPIENAEQFAADHLAFCKSIGLKGRILVADEGINGTVSGDYETTQKYMDYVHSLPGMEELWFKIDEESEQAFKKMFVRYKKEIVHLGLEDNDFDNDINPLETTGAYLSPKEFKEALLDKDTVVLDTRNDYEYDLGHFRGAIRPDIRNFRELPQWVRDNKEKFMDKRVVVYCTGGVRCEKFSGWMVREGYKDVGQLHGGIATYGKDPEVQGELWDGKMYVFDERIAVDVNHVNPTIVGKDWFDGTPCERYVNCGNPFCNRRILTSEENEDKYLRGCSHECRVHPRNRYVSKNELTQAEVIERLAAIGESLDQAATV | Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs. | C1CHZ8 |
A9VKK9 | TRMB_BACMK | tRNA(m7G46)-methyltransferase | Bacillus cereus group | MRLRHKPYAMDRINEYSHIVIGNPEESAGNWKEIFGNEQPIHIEVGTGRGRFMYDMAKANPHINYIGIEKFTSVVVDALDKLIEEEVPNLKLINKDAEDLTVFFAKGEIDRVYLNFSDPWPKNRHTKRRLTYKTFLRNYEEVLVDGGEIHFKTDNQGLFEYSIMSMAEYGMLLTYLSLDLHNSDYEGNIMTEYEEKFSSKGHRIYRVEAKYRTEPMQ | Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. | A9VKK9 |
Q80WQ2 | VAC14_MOUSE | Protein VAC14 homolog | Mus | MNPEKDFAPLTPNIVRALNDKLYEKRKVAALEIEKLVRDFVAQNNTMQIKHVIQTLSQEFALSQHPHSRKGGLIGLAACSIALGKDSGLYLKELIEPVLTCFNDADSRLRYYACEALYNIVKVARGAVLPHFNVLFDGLSKLAADPDPNVKSGSELLDRLLKDIVTESSKFDLVSFIPLLRERIYSNNQYARQFIISWILVLVSVPDINLLDYLPEILDGLFQILGDNGKEIRKMCEVVLGEFLKEIKKNPSSVKFAEMANILVIHCQTTDDLIQLTAMCWMREFIQLAGRVMLPYSSGILTAVLPCLAYDDRKKSIKEVANVCNQSLMKLVTPEDDEPDEPKSVAQKQTEPNPEDSLPKQEGTASGGPGSCDSSFGSGINVFTSANTDRAPVTLHLDGIVQVLNCHLSDTTIGMMTRIAVLKWLYHLYIKTPRKMFRHTDSLFPILLQTLSDESDEVVLKDLEVLAEIASSPAGQTDDPGAPDGPDLRVNHSELQVPTSGRANLLNPPSTKGLEGSPSTPTMNSYFYKFMINLLQTFSSERKLLEARGPFIIRQLCLLLNAENIFHSMADILLREEDLKFASTMVHTLNTILLTSTELFQLRNQLKDLQTPESQNLFCCLYRSWCHNPVTTVSLCFLTQNYRHAYDLIQKFGDLEVTVDFLTEVDKLVQLIECPIFTYLRLQLLDVKNNPYLIKALYGLLMLLPQSSAFQLLSHRLQCVPNPELLQTEDCLKAAPKSQKGDSPSIDYTELLQHFEKVQKQHLEVRHQRSGRGDHLDRRVIL | Scaffold protein component of the PI(3,5)P2 regulatory complex which regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Pentamerizes into a star-shaped structure and nucleates the assembly of the complex. The pentamer binds a single copy each of PIKFYVE and FIG4 and coordinates both PIKfyve kinase activity and FIG4 phosphatase activity, being required to maintain normal levels of phosphatidylinositol 3-phosphate (PtdIns(3)P) and phosphatidylinositol 5-phosphate (PtdIns(5)P). Plays a role in the biogenesis of endosome carrier vesicles (ECV) / multivesicular bodies (MVB) transport intermediates from early endosomes. | Q80WQ2 |
Q6KHL5 | TRMD_MYCMO | tRNA [GM37] methyltransferase | Mesomycoplasma | MINIEIIDFRNFAYGKQKKVDDEIYGGGSGMLLKIEPIDLALENTKGKRILLSPQGKPFTQDDALKLSKEENLTFICGRYEGFDERIRNLIDEEYSIGDYVLTGGELASMVIADSTIRLIPGVIKEESYKNDSFQNNLLDYPQYTRPATYKNMNVPEVLLNGNHKEIKQWREQKAYEKTLKNRPDLIERKNNAK | Specifically methylates guanosine-37 in various tRNAs. | Q6KHL5 |
O32126 | YUTE_BACSU | Putative toxin HepT | Bacillus | MYFVDRSKIEKTLGFFEHQLALFDSQTDWQSEIGELALQRIGHLLIECILDTGNDMIDGFIMRDPGSYDDIMDILVDEKVVTEKEGDELKKLIAYRKTLVQQYLLADSGELYRLIKAHQTALQDFPKRIRSYLETELGPVSAFK | Probable toxic component of a putative type VII toxin-antitoxin (TA) system, probably an RNase. Probably neutralized by cognate antitoxin YutD. | O32126 |
A4WE62 | ZAPA_ENT38 | Z ring-associated protein ZapA | Enterobacter | MSAQPVDLQIFGRSLRVNCPPEQRDALSQAADDLNQRLQDLKERTRVTNTEQLVFIAALNISYELTQEKAKTRDYAASMEQRIKMLQQTIEQALLDQGRTPERPGQKFE | Activator of cell division through the inhibition of FtsZ GTPase activity, therefore promoting FtsZ assembly into bundles of protofilaments necessary for the formation of the division Z ring. It is recruited early at mid-cell but it is not essential for cell division. | A4WE62 |
Q7M711 | TR113_MOUSE | Taste receptor type 2 member 113 | Mus | MVAVLQSTLPIIFSMEFIMGTLGNGFIFLIVCIDWVQRRKISLVDQIRTALAISRIALIWLIFLDWWVSVHYPALHETGKMLSTYLISWTVINHCNFWLTANLSILYFLKIANFSNIIFLYLKFRSKNVVLVTLLVSLFFLFLNTVIIKIFSDVCFDSVQRNVSQIFIMYNHEQICKFLSFTNPMFTFIPFVMSTVMFSLLIFSLWRHLKNMQHTAKGCRDISTTVHIRALQTIIVSVVLYTIFFLSFFVKVWSFVSPERYLIFLFVWALGNAVFSAHPFVMILVNRRLRLASLSLIFWLWYRFKNIEV | Putative taste receptor which may play a role in the perception of bitterness. | Q7M711 |
P42244 | YCBL_BACSU | Uncharacterized transcriptional regulatory protein YcbL | Bacillus | MLVEDDHSISEMVDHYLTKEGFGIVHAFDGEEGIRLFQQGSYDLVLLDIMLPKLNGMDFLKIIREKSNIPVLMISAKDGDVDKALGLGFGADDYIAKPFSMIELTARVKAAIRRATQYSAEEPAVNKVIRIHQLAIDIDNVSVLKNGEPLQLTSTEWQLLCLFASNPKKVFTKEQIYRSVWNEEYFDDQNIINVHMRRLREKIEDDPSSPQYIKTLWGIGYKLGEF | Member of the two-component regulatory system YcbM/YcbL. | P42244 |
P07871 | THIKB_RAT | Peroxisomal 3-oxoacyl-CoA thiolase B | Rattus | MHRLQVVLGHLAGRSESSSALQAAPCSAGFPQASASDVVVVHGRRTPIGRAGRGGFKDTTPDELLSAVLTAVLQDVKLKPECLGDISVGNVLQPGAGAAMARIAQFLSGIPETVPLSAVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTLSERGNPGNISSRLLENEKARDCLIPMGITSENVAERFGISRQKQDAFALASQQKAASAQSKGCFRAEIVPVTTTVLDDKGDRKTITVSQDEGVRPSTTMEGLAKLKPAFKDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDIMGIGPAYAIPAALQKAGLTVNDIDIFEINEAFASQALYCVEKLGIPAEKVNPLGGAIALGHPLGCTGARQVVTLLNELKRRGRRAYGVVSMCIGTGMGAAAVFEYPGN | Responsible for the thiolytic cleavage of straight chain 3-keto fatty acyl-CoAs (3-oxoacyl-CoAs) . Plays an important role in fatty acid peroxisomal beta-oxidation . Catalyzes the cleavage of short, medium, long, and very long straight chain 3-oxoacyl-CoAs . Medium chain straight 3-oxoacyl-CoAs are preferred substrates . | P07871 |
Q3SI71 | TATA_THIDA | Sec-independent protein translocase protein TatA | Thiobacillus | MGSFSIWHWLIVLVVVLLIFGTKKLRNIGSDLGGAVKGFKEGMKDDAPKISESDKGGHTIDAEVKDKQNS | 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. | Q3SI71 |
Q9YE67 | TOP6A_AERPE | Type II DNA topoisomerase VI subunit A | Aeropyrum | MSGEMFGDEVDIKARLRAAEVMYKKFHRLISDVIKGRPPKLEIPKRTLSNTIFDPERGILVIGEEKLEREFLNVGESRRFMQTLLMASIIYQSLIENEYPTIRDLYYKGKHTIVYRDYSGRKREENTWDEQKESDSVIQDIEVYTGLFREDMLILSKEKGKVVGNMRIRSGGDVIDLSKLGHGAYAIEPTPDLIEFLDVDAEFVLVVEKDAVFQQLHRAGFWKKYKALLVTGSGQPDRATRRFVRRLHEELKLPVYIITDSDPYGWYIYSVYKVGSITLSYESERLATPKAKFLGVQMTDIFGYRGKKPYLSEAERKKFMIKATDKDIKRAKELLNYSWIGKNRRWNVEIRLFLKHLVKLEIEAIASKGLKFFAYQYIPEKIETGDWID | Relaxes both positive and negative superturns and exhibits a strong decatenase activity. | Q9YE67 |
A4Y2Q3 | UBIB_SHEPC | Ubiquinone biosynthesis protein UbiB | Shewanella | MTLTSIRRGYHVIKTLLQYGLDEVLPPKMTPWYFTLARSSLFWIRNKHKSKPGGERLKLAMQELGPVYIKLGQMLSTRRDLLSDEWAIELAMLQDKVPPFDGVLARKAIEAELKASIESLFDDFDETPLASASISQVHTATLKSNGKAVVLKVLRPNVEAKILADLQLMSQTANLLEYFLGEGNRLRPAEVIEDYRVTILGELNLKLEALNAIKLRNNFLNSDALYVPYVYEEFCYPRLMVMERIYGIPVSDIAALKAQGTNFKLLAERGVELFFTQVFRDNFFHADMHPGNIFISRDHPENPYYIGLDCGIMGTLSEVDKRYLAENFLAFFNRDYHRIAQLYIESGWVSEKTDLQAFEQAIKVVCEPMFNKPLDEISFGHVLLELFRTARSFDIVVQPQLVLLEKTLLYIEGLGRQLYPQLDLWQTAKPFLEQWMAEQVGPKAMFKKVSTKLPYWSDKLPEFPELIYDNLKLGRKLLSSQQQMLDKYLKHQQQAHKSNYMLITSAVLLICGTLLFNQDATLWSPYVCLTSGVLMWFIGWRSRPKNRKF | Is probably a protein kinase regulator of UbiI activity which is involved in aerobic coenzyme Q (ubiquinone) biosynthesis. | A4Y2Q3 |
A5FWG2 | UPPP_ACICJ | Undecaprenyl pyrophosphate phosphatase | Acidiphilium | MTPLIAVLFAILQGATELFPVSSLGHVVIVPALLHWPIDQASPSFLPFVVMLHVGTATALLLYFWREWWAMLAGLLGRGEPGEVDAQRGLLLRLVVATLPAVLIGFALKKPIQHLFASPEIAAAFLIANGAVLIIGERLRRRRAGNGFGIGQLTLRDSLVIGLFQCLAFLPGLSRSGSAIVGGLTRGLDHEAAARFAFLMATPVIAGAAVIEVPHLLHHAAAARGMFGTALLAAVVAGVVAYLSTAFLMRYFRNHDRWALGPFAAYCALFGALSLILIPFGA | Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin. | A5FWG2 |
S0DHV6 | VEA_GIBF5 | Velvet complex subunit 1 | Fusarium fujikuroi species complex | MATPSSIPAEPKRDVVNRIHRVTRGNRSLWYQMTVLQQPERARACGSGSKANSDRRPVDPPPVVELRIIEGPSVEEGKDITFDYNANFFLYASLEHARPLARGRVNTPAAGNPPILTGVPASGMAYLDRPTEAGYFIFPDLSVRHEGLYILTFSLFETTKEERDFDLEPADGDLPPGVDYRMEIKTDPFSVYSAKKFPGLMESTQLSKTVADQGCQVRIRRDVRMRKRESKPGAGNSNSGGNGFERREEDFGRRRTITPASEDPHSIRNRSHSNSSEQRTPYTDASRRPSMVDSYPPPPPPPSYEPAPSASRHLDFGDSSAAQYPTPRQYAHQPGLQITPGPPSGSYAPTAQSPYSKTDAPYGYVNRNIPPSCPSPAPSVKHDLYDRRQSTSSYVPPSPSVYSTEGHHRRDSRPSYPPTPVAAPRPRPMHSQTSLPALKIDQLVSPVSPLPPIEPQTGPAPELPPINVGGKRKHESVFAQSTRPLHNGQRQVDPHYGRSHRGYSPDHDQGWYSRADGQISSVQFNRYYDE | Component of the velvet transcription factor complex that controls sexual/asexual developmental ratio in response to light, promoting sexual development in the darkness while stimulating asexual sporulation under illumination . The velvet complex hat acts as a global regulator for secondary metabolite gene expression . Controls positively the expression of the gibberellins, fumonisins and fusarin C gene clusters . Controls the expression of the fusaric acid gene cluster . Controls negatively the expression of the bikaverin gene cluster . Regulates the expression of laeA . Plays a crucial role in virulence . | S0DHV6 |
Q66EN1 | THIQ_YERPS | Thiamine import ATP-binding protein ThiQ | Yersinia | MLKLEKITYLYDHLPMCFDLHIQPGERVAILGPSGAGKSTLLSLIAGFLAPTSGHMLLNNQDHTASPPAQRPVSMLFQENNLFAHLTVEQNIGLGLHPGLKLSGEQRLLLQHIAQQVGLESCLDRLPAQLSGGQRQRAALARCLVRSQPILLLDEPFSALDPALRNEMLQLVDQVCINRQLTLLMVSHNLDDAARIAQRTLLIVEGRIDYDGPTQALVDGSAAKASVLGIKSAVIS | Part of the ABC transporter complex ThiBPQ involved in thiamine import. Responsible for energy coupling to the transport system. | Q66EN1 |
A5UF28 | TRUB_HAEIG | tRNA-uridine isomerase | Haemophilus | MSRPRKRWRDVDGVFLLDKPQGMSSNDIMQKVKRLFQANKAGHTGALDPLATGMLPICLGEATKFSQFLLDADKRYLVTAKLGERTDTSDAEGQVVETREVHVETPQILTALEQFRGDILQVPTMFSALKHNGKPLYEYARQGITVEREARPITIFELNFIEYHAPFLTLEVHCSKGTYIRTLVDDLGEVLGCGAHVTMLRRTAVADYPVAEMMLINELELLAESFPLSELDRLLLPTDTAVSKLPALHLDVEQSKAIGFGQRVKFANEQQLSGQVRLFSAENLFLGVALIDGNIIRPQRLITQSA | Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs. | A5UF28 |
C0JRZ9 | TSRM_STRLU | Tryptophan 2-C-methyltransferase | Streptomyces | MLRKGTVALINPNQIHPPIAPYALDVLTTALEASGFEAHVLDLTFHLDDWRQTLRDYFRAERPLLVGVTCRNTDTVYALEQRPFVDGYKAVIDEVRRLTAAPVVAGGVGFSTMPFALVDYFGIEYGVKGPGEKIICDLARALAEGRSADRIHIPGLLVNRGPGNVTRVAPPALDPRAAPAPSSSPSPSPAPSSSSAPVPVPLSFAAVGHHESRAWQAETELPYTRRSGEPYKVDNLRYYREGGLGSILTKNGCVYKCSFCVEPDAKGTQFARRGITAVVDEMEALTAQGIHDLHTTDSEFNLSIAHSKNLLREIVRRRDHDATSPLRDLRLWVYCQPSPFDEEFAELLAAAGCAGVNIGADHTRPEMLDGWKVTAKGTRYYDFADTERLVQLCHRNGMLTMVEALFGMPGETLETMRDCVDRMMELDATVTGFSLGLRLLPYMGLAKSLAEQCDGVRTVRGLQSNNASGPIVLKQLHQCDGPIEYERQFMFDESGDFRLVCYFSPDLPEAPGTADSPDGIWRASVDFLWDRIPKSEQYRVMLPTLSGSSENDNNYADNPFLTSLNRKGYTGAFWAHWRDREAIMSGATLPLGELAEAVR | Involved in the biosynthetic pathway of the antibiotic thiostrepton A. First, TsrM catalyzes the transfer of a methyl group from S-adenosyl methionine (SAM) to cobalamin, leading to the formation of methylcobalamin (CH3-cobalamin) and S-adenosyl-L-homocysteine (SAH). Then the methyl group is transferred to the C2 position of tryptophan (Trp) with the concerted action of the radical SAM [4Fe-4S] center, leading to the production of methyltryptophan. | C0JRZ9 |
Q1ACJ2 | YCF4_CHAVU | Photosystem I assembly protein Ycf4 | Chara | MKIKPCKSQVFRLEPIIGSRKYINYFWSFSIFFGAFGFLIVGICSYLKKELFFFSAENIIFIPQGAVMCFYGIAGIFLSFYLWFTMILGVGSGFNEFNKNEGIVNIFRWGFPGQNRRIKICCLIKDIKSIRIYIRDGISPRSALYLKIRGMPDIPLDVIEDRFNLNEIEKRATELASFLRVPIEGLE | Seems to be required for the assembly of the photosystem I complex. | Q1ACJ2 |
B1B1U3 | ZSS1_ZINZE | Alpha-humulene synthase | Zingiber | MERQSMALVGDKEEIIRKSFEYHPTVWGDYFIRNYSCLPLEKECMIKRVEELKDRVRNLFEETHDVLQIMILVDSIQLLGLDYHFEKEITAALRLIYEADVENYGLYEVSLRFRLLRQHGYNLSPDVFNKFKDDKGRFLPTLNGDAKGLLNLYNAAYLGTHEETILDEAISFTKCQLESLLGELEQPLAIEVSLFLETPLYRRTRRLLVRKYIPIYQEKVMRNDTILELAKLDFNLLQSLHQEEVKKITIWWNDLALTKSLKFARDRVVECYYWIVAVYFEPQYSRARVITSKAISLMSIMDDIYDNYSTLEESRLLTEAIERWEPQAVDCVPEYLKDFYLKLLKTYKDFEDELEPNEKYRIPYLQEEIKVLSRAYFQEAKWGVERYVPALEEHLLVSLITAGYFAVACASYVGLGEDATKETFEWVASSPKILKSCSIHCRLMDDITSHQREQERDHFASTVESYMKEHGTSAKVACEKLQVMVEQKWKDLNEECLRPTQVARPLIEIILNLSRAMEDIYKHKDTYTNSNTRMKDNVSLIFVESFLI | Catalyzes the formation of alpha-humulene in the first step of zerumbone biosynthesis, a highly promising multi-anticancer agent. Also mediates formation of beta-caryophyllene at a much lower level. | B1B1U3 |
P0AFQ7 | YCFH_ECOLI | Uncharacterized metal-dependent hydrolase YcfH | Escherichia | MFLVDSHCHLDGLDYESLHKDVDDVLAKAAARDVKFCLAVATTLPGYLHMRDLVGERDNVVFSCGVHPLNQNDPYDVEDLRRLAAEEGVVALGETGLDYYYTPETKVRQQESFIHHIQIGRELNKPVIVHTRDARADTLAILREEKVTDCGGVLHCFTEDRETAGKLLDLGFYISFSGIVTFRNAEQLRDAARYVPLDRLLVETDSPYLAPVPHRGKENQPAMVRDVAEYMAVLKGVAVEELAQVTTDNFARLFHIDASRLQSIR | Has D-tyrosyl-tRNA deacylase activity in vitro. | P0AFQ7 |
Q9V1F9 | TYW1_PYRAB | tRNA wyosine derivatives biosynthesis protein Taw1 | Pyrococcus | MREMITIKPGKITVQANPNMPEEVANLFRKQHYEIVGRHSGVKLCHWLKKSLTEGRFCYKQKFYGIHSHRCLQMTPVLAWCTHNCIFCWRPMETFLGTELPQPWDDPEFIVEESIKAQRKLLIGYKGNPKVDKKKFEEAWEPKHAAISLSGEPMLYPYMGDLVEEFHKRGFTTFIVTNGTVPERLEEMIKEDKLPTQLYVSITAPDIETYNSVNIPMIPDGWERIMRFLELMRDLPTRTVVRLTLVKGENMHSPEKYAKLILKARPMFVEAKAYMFVGYSRNRLTINNMPSHQDIREFAEALVKHLPGYHIEDEYEPSRVVLIMRDDVDPQGTGVNGRFIKH | Component of the wyosine derivatives biosynthesis pathway that catalyzes the condensation of N-methylguanine with 2 carbon atoms from pyruvate to form the tricyclic 4-demethylwyosine (imG-14) on guanosine-37 of tRNA(Phe). | Q9V1F9 |
Q1AU89 | TRPD_RUBXD | Anthranilate phosphoribosyltransferase | Rubrobacter | MLREALRKAAAGEPLSEGEAERALETIMEGGASPEATAALLTALRVRGESVQEIVGFARAMRRFAARVRAPEGVVDTCGTGGDAKGTINVSTAAAFVARGAGVVIAKHGNRAATSRAGSADVLEALGAAIELSPEQVSRCIEEAGIGFMFARTHHPAMRHVAPVRAELPFRTVFNLLGPLTNPAGARRQLVGVFSAGYVRPMAEALEGLGAERALVVHGRDGMDEITVTGPTLVAEVGGGGVEEYEISPEDFGLSRHAPDGLLGGDAHLNARILRDVLSGEERGASRDVIVLNAGAAIYVAGKAPSIEEGVRLAEGSLESGAALAALERFVRVSRRLAGRGA | Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA). | Q1AU89 |
Q9GZ70 | TPM_PERVI | Tropomyosin | Perna | MDAIKKKMVAMKMEKKNALDRAEQLEQKLRETEEAKAKIEDDYNSLVKKNIQTENDYDNCNTQLQDVQAKYERAEKQIQEHEQEIQSLTRKISLLEEGIMKAEERFTTASGKLEEASKAADESERNRKVLENLNSGNDERIDQLEKQLTEAKWIAEEADKKYEEAARKLAITEVDLERAEARLEAAEAKVIDLEEQLTVVGANIKTLQVQNDQASQREDSYEETIRDLTNRLKDAENRATEAERTVSKLQKEVDRLEDELLTEKEKYKAISDELDATFAELAGY | Tropomyosin, in association with the troponin complex, plays a central role in the calcium dependent regulation of muscle contraction. | Q9GZ70 |
P80318 | TCPG_MOUSE | mTRiC-P5 | Mus | MMGHRPVLVLSQNTKRESGRKVQSGNINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAKSMIEISRTQDEEVGDGTTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRMALDDMISTLKKISTPVDVNNREMMLSIINSSITTKVISRWSSLACNIALDAVKTVQFEENGRKEIDIKKYARVEKIPGGIIEDSCVLRGVMINKDVTHPRMRRYIKNPRIVLLDSSLEYKKGESQTDIEITREEDFTRILQMEEEYIHQLCEDIIQLKPDVVITEKGISDLAQHYLMRANVTAIRRVRKTDNNRIARACGARIVSRPEELREDDVGTGAGLLEIKKIGDEYFTFITDCKDPKACTILLRGASKEILSEVERNLQDAMQVCRNVLLDPQLVPGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHTQESCETWGVNGETGTLVDMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIVSGHKKKGDDQNRQTGAPDAGQE | Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin. | P80318 |