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
|
|---|---|---|---|---|---|---|
F1QHM7 | ZD23A_DANRE | Zinc finger DHHC domain-containing protein 23-A | Danio | MKRERFKPPEPDDPLCCCGDIDQQREYCCCDCEELDDACERLLRGEPDKPDVFSRFISRMADRLGVSCCTVGPLRLELSVLPPMVLIPGLLRVAAINCLLGVIILTALPLLVLWYYYMTHRRKRRTLFFLSLALFSLAYMYYLFLTEIVPRGDVTHLQVVTATTGMMLTLISLVRTKQGPGFVKSQSLALGINSSLATNRSTNLTLDTDLRNGVSHLKGEKDVKKKCPVCQLVRPPRAGHCRICGACVLRMDHHCVWINSCVGQANHRQFILTLLLFLLTSFYGISLVLRSICPKQSLFTAMLYCPGVYNQYSTALCFTCVWYSVIITGGLLHLFILQIINVSCNVTEREAQIALRNKTGRRRFCGLVVETGDHSRGFLQNWIQFLTMNMDEIGSSLNLTDMV | Palmitoyltransferase that could catalyze the addition of palmitate onto various protein substrates and be involved in a variety of cellular processes. | F1QHM7 |
P39109 | YCFI_YEAST | Yeast cadmium factor 1 | Saccharomyces | MAGNLVSWACKLCRSPEGFGPISFYGDFTQCFIDGVILNLSAIFMITFGIRDLVNLCKKKHSGIKYRRNWIIVSRMALVLLEIAFVSLASLNISKEEAENFTIVSQYASTMLSLFVALALHWIEYDRSVVANTVLLFYWLFETFGNFAKLINILIRHTYEGIWYSGQTGFILTLFQVITCASILLLEALPKKPLMPHQHIHQTLTRRKPNPYDSANIFSRITFSWMSGLMKTGYEKYLVEADLYKLPRNFSSEELSQKLEKNWENELKQKSNPSLSWAICRTFGSKMLLAAFFKAIHDVLAFTQPQLLRILIKFVTDYNSERQDDHSSLQGFENNHPQKLPIVRGFLIAFAMFLVGFTQTSVLHQYFLNVFNTGMYIKSALTALIYQKSLVLSNEASGLSSTGDIVNLMSVDVQKLQDLTQWLNLIWSGPFQIIICLYSLYKLLGNSMWVGVIILVIMMPLNSFLMRIQKKLQKSQMKYKDERTRVISEILNNIKSLKLYAWEKPYREKLEEVRNNKELKNLTKLGCYMAVTSFQFNIVPFLVSCCTFAVFVYTEDRALTTDLVFPALTLFNLLSFPLMIIPMVLNSFIEASVSIGRLFTFFTNEELQPDSVQRLPKVKNIGDVAINIGDDATFLWQRKPEYKVALKNINFQAKKGNLTCIVGKVGSGKTALLSCMLGDLFRVKGFATVHGSVAYVSQVPWIMNGTVKENILFGHRYDAEFYEKTIKACALTIDLAILMDGDKTLVGEKGISLSGGQKARLSLARAVYARADTYLLDDPLAAVDEHVARHLIEHVLGPNGLLHTKTKVLATNKVSALSIADSIALLDNGEITQQGTYDEITKDADSPLWKLLNNYGKKNNGKSNEFGDSSESSVRESSIPVEGELEQLQKLNDLDFGNSDAISLRRASDATLGSIDFGDDENIAKREHREQGKVKWNIYLEYAKACNPKSVCVFILFIVISMFLSVMGNVWLKHWSEVNSRYGSNPNAARYLAIYFALGIGSALATLIQTIVLWVFCTIHASKYLHNLMTNSVLRAPMTFFETTPIGRILNRFSNDIYKVDALLGRTFSQFFVNAVKVTFTITVICATTWQFIFIIIPLSVFYIYYQQYYLRTSRELRRLDSITRSPIYSHFQETLGGLATVRGYSQQKRFSHINQCRIDNNMSAFYPSINANRWLAYRLELIGSIIILGAATLSVFRLKQGTLTAGMVGLSLSYALQITQTLNWIVRMTVEVETNIVSVERIKEYADLKSEAPLIVEGHRPPKEWPSQGDIKFNNYSTRYRPELDLVLKHINIHIKPNEKVGIVGRTGAGKSSLTLALFRMIEASEGNIVIDNIAINEIGLYDLRHKLSIIPQDSQVFEGTVRENIDPINQYTDEAIWRALELSHLKEHVLSMSNDGLDAQLTEGGGNLSVGQRQLLCLARAMLVPSKILVLDEATAAVDVETDKVVQETIRTAFKDRTILTIAHRLNTIMDSDRIIVLDNGKVAEFDSPGQLLSDNKSLFYSLCMEAGLVNEN | Cooperates for the ATP-dependent vacuolar transport of bilirubin and glutathione conjugates. | P39109 |
Q9BTX7 | TTPAL_HUMAN | Alpha-tocopherol transfer protein-like | Homo | MSEESDSLRTSPSVASLSENELPPPPEPPGYVCSLTEDLVTKAREELQEKPEWRLRDVQALRDMVRKEYPNLSTSLDDAFLLRFLRARKFDYDRALQLLVNYHSCRRSWPEVFNNLKPSALKDVLASGFLTVLPHTDPRGCHVVCIRPDRWIPSNYPITENIRAIYLTLEKLIQSEETQVNGIVILADYKGVSLSKASHFGPFIAKKVIGILQDGFPIRIKAVHVVNEPRIFKGIFAIIKPFLKEKIANRFFLHGSDLNSLHTNLPRSILPKEYGGTAGELDTATWNAVLLASEDDFVKEFCQPVPACDSILGQTLLPEGLTSDAQCDDSLRAVKSQLYSCY | May act as a protein that binds a hydrophobic ligand. | Q9BTX7 |
Q12S25 | UBIB_SHEDO | Ubiquinone biosynthesis protein UbiB | Shewanella | MSISSLHRGYQVLRTLLHYGLDELLAKDKRPKLFPLIRGCFFWIRNQHKDKSAAERLKLAMQELGPVYIKLGQMLSTRRDLLDDEWAYQLAMLQDRVPPFDSALAREAIETELNASIDSLFDDFDDVPLASASIAQVHSATLKSNGKAVVLKVLRPNVEALILADLQLMSHCAALLERILGDGNRLRPAEVIEDYRLTILGELNLKLEALNAIKLRNNFLDSDALYVPYIYEDLSFTRLIVMERIYGIAVSDLSALKAQGTNLKLLAERGVELFFTQVFRDNFFHADMHPGNIFISRDHPDNPYYIGLDCGIMGTLTDVDKRYLAENFLAFFNRDYQRIAQLHLESGWVSEHTDIVAFEQAIKIVCEPMFNKPLAEISFGHVLLALFRTARQFNMVVQPQLVLLQKTLLYIEGLGRQLYPQLDLWQTAKPFLEQWMAKQVGPKALFDKFKSNAPFWAEKLPELPELVYDNLKLGRKLLGTQQQMLDKYLKYQHKAHKSNYLLITSAVFVICGTILFTQAVTLWASLLCLGTGAGLWLLGWQARPKNRKL | Is probably a protein kinase regulator of UbiI activity which is involved in aerobic coenzyme Q (ubiquinone) biosynthesis. | Q12S25 |
O23401 | U84A3_ARATH | Hydroxycinnamate glucosyltransferase 3 | Arabidopsis | MDPSRHTHVMLVSFPGQGHVNPLLRLGKLIASKGLLVTFVTTEKPWGKKMRQANKIQDGVLKPVGLGFIRFEFFSDGFADDDEKRFDFDAFRPHLEAVGKQEIKNLVKRYNKEPVTCLINNAFVPWVCDVAEELHIPSAVLWVQSCACLTAYYYYHHRLVKFPTKTEPDISVEIPCLPLLKHDEIPSFLHPSSPYTAFGDIILDQLKRFENHKSFYLFIDTFRELEKDIMDHMSQLCPQAIISPVGPLFKMAQTLSSDVKGDISEPASDCMEWLDSREPSSVVYISFGTIANLKQEQMEEIAHGVLSSGLSVLWVVRPPMEGTFVEPHVLPRELEEKGKIVEWCPQERVLAHPAIACFLSHCGWNSTMEALTAGVPVVCFPQWGDQVTDAVYLADVFKTGVRLGRGAAEEMIVSREVVAEKLLEATVGEKAVELRENARRWKAEAEAAVADGGSSDMNFKEFVDKLVTKHVTREDNGEH | UDP-glucosyltransferase that forms glucose esters with phenylpropanoids . Glucosylates 4-coumarate, ferulate, caffeate, sinapate and cinnamate . | O23401 |
Q9JKU1 | TR119_RAT | Taste receptor type 2 member 19 | Rattus | MMEGHILFFFLVVMVQFVTGVLANGLIVVVHAIDLIMWKKMAPLDLLLFCLATSRIILQLCILFAQLCLFSLVRHTLFEDNITFVFIINELSLWFATWLGVFYCAKIATIPHPLFLWLKMRISRLVPWLILGSVLYVIITTFIHSRETSAILKPIFISLFPKNATQVGTGHATLLSVLVLGLTLPLFIFTVAVLLLIYSLWNYSRQMRTMVGTREYSGHAHISAMLSILSFLILYLSHYMVAVLISTQVLYLGSRTFVFCLLVIGMYPSIHSIVLILGNPKLKRNAKMFIVHCKCCHCTRAWVTSRSPRLSDLPVPPTHPSANKTSCSEACIMPS | Gustducin-coupled receptor implicated in the perception of bitter compounds in the oral cavity and the gastrointestinal tract. Signals through PLCB2 and the calcium-regulated cation channel TRPM5. | Q9JKU1 |
Q8SR53 | TCPH_ENCCU | CCT-eta | Encephalitozoon | MNQLFVQTEKIVDPREGKLQVVSNVDVCTKIAEFLESTLGPYGMDKLFAGKEIVVTNDGATILKHMNIRHPVGRLLVALSESQDSEVGDGTTSVVILTTEILSCLKPLIKDNFDLGCIKGCLEELRMMCIEHLEKMGMELDDEVLYKLAGTCITSKNIRHEKEYFSRMIVDAVKQAKIDDAESIGVKKVQGGSIGDSVAVNGIAFEKCFTYAGYEQQPKRILNPRILCLNVELEWKSERDNAEIRVGGVEEYQRVVDAEWAIIRRKLDEIISSGANVVLSSLSIGDYATQYFAKHGIFCAGRVSKEDLGRVVGSCGGSILGATDYLEGSLGACALFEERQLGKFRYNYFEGGGTSACTMILRGPGQEVLEEIGRSVHDAVCVVRTALRTRKVVTGGGSVEMELSRIIREKSMKYDDKRMFVAKAVGQAFEKIPLLLARNFGLDTISTIQDLRKRHANGDSCEGISIDGARDMQKLGIYEPLEVKKNMVKASFSAAASIIMIDSTIMAEKSQ | Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. | Q8SR53 |
Q39PA6 | TYPH_BURL3 | TdRPase | Burkholderia cepacia complex | MFLPQEFIRQKRNRQALDRDGIAAFVRGVTDGSVTEGQVAAFAMAVYFNDLSTDERVALTLAQRDSGDVLDWHALELDGPVIDKHSTGGVGDVVSLMLGPMVAACGGYVPMISGRGLGHTGGTLDKLSAIPGYNVTPDTDAFRRAVRDVGVAIIGQTARLAPADMRIYAIRDVTATVESVAMITASILSKKLAAGLDGLVMDVKVGSGAFMPTAEQSAELARSIVDVGNGAGMKTTAILTDMNQSLAPCAGNALEVACAIDYLTGKSRPARLHDVTMALSAELLVTGGLAHDVADARAKLLRALDSGAAAERFARMVTALGGPADLIDAPARHLARAKVVVPVPARASGVVQRVDCRALGLAVVALGGGRTRAADAIDYSVGLTALAEIGQRVEADQPLGYVHARDAAAAAHAVDTIQRSYVLGEAGDAPPTIYQQIG | The enzymes which catalyze the reversible phosphorolysis of pyrimidine nucleosides are involved in the degradation of these compounds and in their utilization as carbon and energy sources, or in the rescue of pyrimidine bases for nucleotide synthesis. | Q39PA6 |
C4ZSI8 | THIM_ECOBW | 4-methyl-5-beta-hydroxyethylthiazole kinase | Escherichia | MQVDLLGSAQSAHALHLFHQHSPLVHCMTNDVVQTFTANTLLALGASPAMVIETEEASQFAAIASALLINVGTLTQPRAQAMRAAVEQAKSSQTPWTLDPVAVGALDYRRHFCHELLSFKPAAIRGNASEIMALAGIANGGRGVDTTDAAANAIPAAQTLARETGAIVVVTGEMDYVTDGHRIIGIHGGDPLMTKVVGTGCALSAVVAACCALPGDTLENVASACHWMKQAGERAVARSEGPGSFVPHFLDALWQLTQEVQA | Catalyzes the phosphorylation of the hydroxyl group of 4-methyl-5-beta-hydroxyethylthiazole (THZ). | C4ZSI8 |
P09642 | TBA3_CHICK | Tubulin alpha-3 chain | Gallus | ADQCSGLQGFLVFHSFGGGTGSGFTSLLMERLSVEYSKKSKLEFSVYPDRQVSTAVVEPYNSILTTHTTLEHSDCSFMVDNEAIYDICNRNLDIERPTYTNLNRLIGQIVSSVTASLRFNGALNVDLIEFQTNLVPYPRIHFPLTTYARIISAEKAYHEQLSVPEITNACFEFSNQMVKCDPRRGKYMACCLLYRGDVVPKDVNAAIAAIKTRRSIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDLAALEKDYEEVGRNSADGGEFEE | Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin. | P09642 |
B2IEW0 | TRUA_BEII9 | tRNA-uridine isomerase I | Beijerinckia | MPRYKLTVEYDGASFVGWQRQKNGLSVQEVIETALLAINGAPVGIRGAGRTDAGVHASAQVAHADLAREWRPDVLRDALNAHMRPALVAVVAAEPVPETFDARFSAIRRHYLYRIINRRAPLTFEAGRAWLVKRRLDARAMHEAAQVLTGRHDFSTFRAAECQAASPIRTLERLDVQAVGDLIEIRASARSFLHHQVRSMVGSLEMVGSGKWSAGDLRAALEACDRRRCGMVAPAAGLYLTGVDYPEEGEEKGAQPFFGE | Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs. | B2IEW0 |
A0QKY2 | Y4435_MYCA1 | Putative S-adenosyl-L-methionine-dependent methyltransferase MAV_4435 | Mycobacterium avium complex (MAC) | MTRTDQDSWDLASSVGATATMVAAARALASTGERPIINDPFAAPLVRAVGLDFFRRLVDGEVAPADPQRGERDLQLETDSIAVRTRFFDDFFTGAARDGIRQSVILAAGLDARAYRLDWPAGAVVYEVDQPKVVEFKTNTMAALDARPAAQLRTVSIDLREDWPEALRANGFDVTQATSWSAEGLLMYLPPEAQDRLFDNITALSAPGSRLATEYHPDATGTTMAQRAQEFNDRWARVGCDIDLSGLFFDGERSNVVEYLTGRGWRVSARPRRDLFDDYGLAYPEDDETAQFPNIVAVSAELG | Exhibits S-adenosyl-L-methionine-dependent methyltransferase activity. | A0QKY2 |
B6DCT4 | TX402_LYCSI | Toxin-like structure LSTX-C2 | Lycosa | MKVLVLFSVLFLTLFSYSSTEAIDEFDSDAEDDMLSLMANEQVRAKACTPRLHDCSHDRHSCCRGELSKDVCYCFYPEGEDKTEVCSCQQPKSHKYIEKVVDKAKTVVG | Enhances the high-affinity desensitization of human P2RX3 purinoceptors. | B6DCT4 |
P57751 | UGPA1_ARATH | UDP-glucose pyrophosphorylase 1 | Arabidopsis | MAATATEKLPQLKSAVDGLTEMSENEKSGFINLVSRYLSGEAQHIEWSKIQTPTDEIVVPYDKMANVSEDASETKYLLDKLVVLKLNGGLGTTMGCTGPKSVIEVRDGLTFLDLIVIQIENLNNKYNCKVPLVLMNSFNTHDDTQKIVEKYTKSNVDIHTFNQSKYPRVVADEFVPWPSKGKTDKDGWYPPGHGDVFPSLMNSGKLDAFLSQGKEYVFIANSDNLGAIVDLKILKHLIQNKNEYCMEVTPKTLADVKGGTLISYEGKVQLLEIAQVPDEHVNEFKSIEKFKIFNTNNLWVNLKAIKKLVEADALKMEIIPNPKEVDGVKVLQLETAAGAAIRFFDNAIGVNVPRSRFLPVKATSDLLLVQSDLYTLVDGFVTRNKARTNPTNPAIELGPEFKKVASFLSRFKSIPSIVELDSLKVSGDVWFGSGVVLKGKVTVKANAGTKLEIPDNAVLENKDINGPEDL | Converts glucose 1-phosphate to UDP-glucose, which is the major glycosyl donor for polysaccharides. Acts redundantly with UGP2 and is essential for the synthesis of sucrose, starch and cell wall, and callose deposition . Involved in the regulation of the programmed cell death (PCD) induced by the fungal toxin fumonisin B1 (FB1) . | P57751 |
Q9V1P5 | XERA_PYRAB | Tyrosine recombinase XerA | Pyrococcus | MEEREERVRDDTIEEFATYLELEGKSRNTVRMYTYYISKFFEEGHSPTARDALRFLAKLKRKGYSTRSLNLVIQALKAYFKFEGLDSEAEKLKTPKMPKTLPKSLTEEEVRRIINAAETLRDRLILLLLYGAGLRVSELCNLRVEDVNFEYGVIVVRGGKGGKDRVVPISESLLSEIKRYLESRNDDSPYLFVEMKRKRKDKLSPKTVWRLVKKYGRKAGVELTPHQLRHSFATHMLERGIDIRIIQELLGHSNLSTTQIYTKVSTKHLKEAVKKAKLVESIIGGS | Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. Probably involved in the resolution of chromosome dimers at the terminus of replication. Binds to the dif site. | Q9V1P5 |
A5FL65 | TATA_FLAJ1 | Sec-independent protein translocase protein TatA | Flavobacterium | MGRLGLTEILVIVGIVILLFGGKKIPELMKGLGSGIKEFKNAAKDDQPAPAKKQEEEQK | 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. | A5FL65 |
Q92117 | TBP_PROFL | Transcription initiation factor TFIID TBP subunit | Protobothrops | MDQNNSLPPYAQGLASPQSAMTPGIPIFSPMMPYGTGLTPQPAQSTNSLSILEEQQRQQQQAAAQQSTSQPTQAPSGQTPQLFHSQTLTTAPLPGTTPLYPSPMTPMTPITPATPASESSGIVPQLQNIVSTVNLGCKLDLKTIALRARNAEYNPKRFAAVIMRIREPRTTALIFSSGKMVCTGAKSEEQSRLAARKYARVVQKLGFPAKFLDFKIQNMVGSCDVKFPIRLEGLVLTHQQFSSYEPELFPGLIYRMIKPRIVLLIFVSGKVVLTGAKVRGEIYEAFENIYPILKGFRKTT | General transcription factor that functions at the core of the DNA-binding multiprotein factor TFIID. Binding of TFIID to the TATA box is the initial transcriptional step of the pre-initiation complex (PIC), playing a role in the activation of eukaryotic genes transcribed by RNA polymerase II. | Q92117 |
Q8D8S3 | TORA_VIBVU | Trimethylamine-N-oxide reductase | Vibrio | MAITRRSFLKGVATTSAASVIGPSLLASASANAVETTGTWKVSGSHWGAFRAHIYAGKVQEIKPIELDQNPTEMLNGIKGIIYSPSRVRYPMVRLDWLKKHKYSADTRGNNRFVRVTWDEALDLFYRELERVQKEYGPWALHAGQTGWNQTGSFNNCTAHMQRAVGMHGNYITKVGDYSTGAGQTILPYVLGSTEVYAQGTSWSEILENADNIILWANDPVKNLQVGWNCETHESYAYLAQLKEKVAKGEINVISVDPVKNKTQRYLENDHLYVNPMTDVPFMLAIAHVLYTENLYDKKFIETYCLGFEEFINYVQGKTKDKVEKTPEWAAPICGVKADKIREFARMLVKGRTQILMGWCIQRQEHGEQPYWAAAVVAAMIGQIGLPGGGISYGHHYSSIGVPSTGFAGPGGFPRNLDAGMKPKWDNNDFNGYSRTIPVARWIDCLLEPGKEINYNGGKVKLPDFKMMVISGCNPWHHHQDRNRMKQAFQKLQTVVTIDFAWTATCRFSDIVLPACTQWERNDIDVYGSYSSRGLIAMHRLVDPLFQSKPDFQIMKELTERFGRSEEYSRGMSEMDWIRSLYNDCKKSNEGKFEMPEFDEFWEKSVLDFGQGQPWVRHADFRQDPEINPLGTPSGFIEITSRKIGRYGYEHCQEHPMWFEKSERSHGGPGSDKHPFWLQSCHPDKRLHSQMCESEEFRATYAVKGREPVYINPLDAKAKGIKEGDLVRVFNDRGQLLAGAVLTDSYPRGVIRIEEGAWYGPLNEKVGAIDTYGDPNTLTQDIGSSELAQATSANTCIVDFEKFTGKVPPVTSFGGPIEVA | Reduces trimethylamine-N-oxide (TMAO) into trimethylamine; an anaerobic reaction coupled to energy-yielding reactions. | Q8D8S3 |
B1KR05 | UBIB_SHEWM | Ubiquinone biosynthesis protein UbiB | Shewanella | MTVTSIRRAYQVIKTALHYGLDELIPSKVKPWYFRLLRCTFFWLRNQHKDKVGGERLKLVMQELGPVYIKFGQMLSTRRDLLDDEWAEELAMLQDRVPPFDSSIAREMIELELGTSIDTYFDDFDNTPLASASISQVHTATLKSNGKAVVLKVLRPNVEAQVDADLHLMSQAANFLETVLGHGNRLRPAEVVEDYRTTIEGELNLKLEALNAVKLRNNFLDSGSLYIPYMYEELCFTRLIVMERIEGIPVSDMAALKAQGTNLKVLAERGVELFFTQVFRDNFFHADMHPGNIFVSREHPEDPYYIGLDCGIMGTLTEEDKRYLAENFLAFFNRDYHRIAQLYIESGWVSPDTDIAAFEQAVKVVCEPMFNKPLDEISFGHVLLELFRTARRFDMVVQPQLVLLEKTLLYIEGLGRQLYPQLDLWQTAKPFLEKWMSEQVGPKGMASKIKKEFPYWADKLPELPELVYDNLKMGRNFVKSQNQMLDRYLKQQQKAHKSNYLLITSAVLVICGTILFNQNATLWASYGSITVGVVLWLLGWRSRPKKRKF | Is probably a protein kinase regulator of UbiI activity which is involved in aerobic coenzyme Q (ubiquinone) biosynthesis. | B1KR05 |
D0U690 | XPT1_CRYNV | Xylosylphosphotransferase 1 | Cryptococcus neoformans species complex | MPSTALSPPSRPPAQSYDSYSSSLSPSSPRFHAAAGSHGRRSPSPSRLESLLDGPHVPPRSPSRKIRSALSRHIRPHITPRTLTPVFLWTLALWLIHHFLFPLSSPFAKLAKPKAEEHFLSTTFPPPAQRLGDDRLDSVDPRWRAYHPLPAPEPPFPRLRPTRFLPPQCLEQWFAEGETLCGAKEMGEEETLDATWLWVNGSDHRWRDSMVEWREKENVNSPERHYREQNELVHSMRSVLDALPGHLRTFHLILADYPFNYPEDLELVPSSIIPDLEVAASKSKGRRHPRELPGAPASLANLTERVTPESISPTLASHLQSEWRILQTPTWLDFSRRDPSDPSHPFHPYSVSKAGEIRQHYAEASYPTLRYASHWEVFHIPSVDRDGRQELMGEREWRENEWKKKALPSFNSMAIESRIGWLPGLADAIIALNDDFFLLRPHAVSDFHSPLYGSVIRFEHGYNQQVKPDVEKNHINDPGEMGGLYHANALLSRRFPRRLRPYFAHVPKVITRGLHHEASLMFQEALTESSTRRFREMKIGEGDVQMQWLLTSLRVERWREALLWTWTVANMGTLGGSQDHWDNDTRRAIKNLFGFTENDDDVVKIEVHRGERWTLEPGRMQRVFRQAGWEAPKATEFLFSSMDGIMPPLLRSGEDPAQNDRCIIDLNRCFGLFWTREEDVLSSDMMKRLTFQYPECGDCMIMALVTASGTLGLNAFFPPKETTITAPELGPGDAYPKFLPPPHLPLTPTWHEADFSLANILSTTALPGEQVDIRQYCMRLLSRYLYLDAKSVSHFHMMKSAEHARRVFRMIQGDPKVSILGMNDDIESDYDEVRGLMNEWFEMRWPRKAVWERDWDPVKDRYND | Xylosylphosphotransferase that is specific for UDP-xylose as a donor and mannose as an acceptor to form a xylose-alpha-1-phosphate-6-mannose linkage. Functions in the O-glycosylation of proteins en route through the secretory pathway. | D0U690 |
B4ECC9 | UREF_BURCJ | Urease accessory protein UreF | Burkholderia cepacia complex | MTTTELVALLHLASPALPIGAYSYSQGLEAALDANLIRDADSARDWIASGLTDVLAHGELPFLAHQLARWQTDDTHALAAENAWFVASRESAELRRETEQMGWSLAQLCASLEWGDAARRATLASLSPIALPTAFAYAAAAHDASADATLAAYAFGWVENQTSAALKAVPLGQLAGQRIIVALRGAIDAAVRRALATPPDAVNTFAPQLGILSARHETQYSRLFRS | Required for maturation of urease via the functional incorporation of the urease nickel metallocenter. | B4ECC9 |
B0T2Q1 | THIC_CAUSK | Thiamine biosynthesis protein ThiC | unclassified Caulobacter | MNVQLPIKDAIGAIPTGERPGSRKVYQAGSLFPDIRVPFREVAVHPSANEPPVTIYDPSGPYTDPHAKIDIEQGLERSREPWIIARGDCELVATPREVKPEDNGFAQGKHLAPQFTAKRPIFKGAQGKLVTQLEYARAGIVTAEMEYVAIRENLRREQDRPCVRDGEDFGASIPDFVTPEFVRQEVARGRAIIPANINHGELEPMAIGRNFLVKINANIGNSAVLSTVADEVDKLVWATRWGADTVMDLSTGRNIHNIRDWIIRNSPVPIGTVPIYQALEKVNGVAEDLNWEVFRDTLIEQAEQGVDYFTIHAGVRLPFIPLTAKRVTGIVSRGGSIMAKWCLAHHKENFLYERFEDICEIMRSYDVSFSLGDGLRPGSTADANDEAQFAELRTLGELTKVAWKHGVQVMIEGPGHVAMHKIKANMDEQLKHCHEAPFYTLGPLTTDIAPGYDHITSAIGAAMIGWFGTAMLCYVTPKEHLGLPDRDDVKTGVITYKLAAHAADLAKGHPGAAMWDDAISRARFEFRWEDQFNLGLDPETARAFHDETLPKEAHKTAHFCSMCGPKFCSMKISQEVREFAAGMAPNSIEQGMAEMSDKFREQGSEIYLKTE | 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. | B0T2Q1 |
A7MKI9 | TUSC_CROS8 | tRNA 2-thiouridine synthesizing protein C | Cronobacter | MKQVAFVFTQAPHGTSAGREGLDALLAMSALTEEIGVFFLSDGVFQILPGQHPQAVLSRDYISTFKVLPLYDIERCYICRESLQERGLSEEHAFVIDVEALDAAALRERLDDYDVVLTF | Part of a sulfur-relay system required for 2-thiolation of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at tRNA wobble positions. | A7MKI9 |
Q9UUH1 | VPS55_SCHPO | Vacuolar protein sorting-associated protein 55 | Schizosaccharomyces | MSDLRKIIGLSSVLAVGFMLVILSCALFKNWYPLLIVIPFILAPLPNLLTKKYSTSHDFLQEEDRNLLDFGRFTFGATICTGFALPIVFVNVGLIGTAAATMSCVGGSIIFLVITLYSQAFVQHEEEF | Involved in protein transport from endosomes to the vacuole. | Q9UUH1 |
Q68EQ9 | VMP1_XENTR | Vacuole membrane protein 1 | Silurana | MAENGTDCEQRRVGMAKEQNNGSFQDPSFLSDRKSRDREERQSIVLWRKPLITLQYFILEVLITLKDWSIRLWHRRMMVVSVLLLLAVLSVVYYIEGTHQQYVQYVEKKCLWCAYWVGLGILSSVGLGTGLHTFLLYLGPHIASVTIAAYECNSVNFPEPPYPDEIICPDEEGTEGAISLWTIISKVRLEACMWGAGTAIGELPPYFMARAARLSGVETDDEEYAEFEEMLEHAQTAQDFATRAKLAVQNLVQKVGFLGILACASIPNPLFDLAGITCGHFLVPFWTFFGATLIGKAIIKMHIQKLFVIITFSKHIVEQMVSLIGVIPSIGPSLQKPFQEYLEAQRKKLHHKEDSGAPQSENWLSWAFEKLVIIMVFYFILSIINSMAQSYAKRVQQRKLSVEKTK | 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. | Q68EQ9 |
Q06443 | WNT5B_AMBME | Protein Wnt-5b | Ambystoma | MPGIRLLLAAALLCCPPPAGATSWWSLAQNPVQRPEMYIIGAQPVCSQLSSLSPGQKKLCQLYQDHMMYIGEGAKTGIKECQYQFKQRRWNCSTVDNTSVFGRVMQIGSRETAFTYAVSAAGVVNAISRACREGELSTCGCSRTTRPKDLHRDWLWGGCGDNVDYGYRFAKEFVDAREREKNYPKGSEEQARTLMNLQNNEAGRRAVYKLADAACKCHGVSGSCSLKTCWLQLADFRKVGDHLKEKYDSAAAMRINRKGKLELVNNRFNLPTVEDLVYTDQSPDYCLRNESTGSLGTLGRLCNKTSEGMDGCELMCCGRGYDQFKTVQVERCHCKFHWCCFVKCKKCTEIVDQYVCK | Ligand for members of the frizzled family of seven transmembrane receptors. Probable developmental protein. May be a signaling molecule which affects the development of discrete regions of tissues. Is likely to signal over only few cell diameters. | Q06443 |
O87948 | TORA_SHEMA | Trimethylamine-N-oxide reductase | Shewanella | MNRRDFLKGIASSSFVVLGGSSVLTPLNALAKAGINEDEWLTTGSHFGAFKMKRKNGVIAEVKPFDLDKYPTDMINGIRGMVYNPSRVRYPMVRLDFLLKGHKSNTHQRGDFRFVRVTWDKALTLFKHSLDEVQTQYGPSGLHAGQTGWRATGQLHSSTSHMQRAVGMHGNYVKKIGDYSTGAGQTILPYVLGSTEVYAQGTSWPLILEHSDTIVLWSNDPYKNLQVGWNAETHESFAYLAQLKEKVKQGKIRVISIDPVVTKTQAYLGCEQLYVNPQTDVTLMLAIAHEMISKKLYDDKFIQGYSLGFEEFVPYVMGTKDGVAKTPEWAAPICGVEAHVIRDLAKTLVKGRTQFMMGWCIQRQQHGEQPYWMAAVLATMIGQIGLPGGGISYGHHYSSIGVPSSGAAAPGAFPRNLDENQKPLFDSSDFKGASSTIPVARWIDAILEPGKTIDANGSKVVYPDIKMMIFSGNNPWNHHQDRNRMKQAFHKLECVVTVDVNWTATCRFSDIVLPACTTYERNDIDVYGAYANRGILAMQKMVEPLFDSLSDFEIFTRFAAVLGKEKEYTRNMGEMEWLETLYNECKAANAGKFEMPDFATFWKQGYVHFGDGEVWTRHADFRNDPEINPLGTPSGLIEIFSRKIDQFGYDDCKGHPTWMEKTERSHGGPGSDKHPIWLQSCHPDKRLHSQMCESREYRETYAVNGREPVYISPVDAKARGIKDGDIVRVFNDRGQLLAGAVVSDNFPKGIVRIHEGAWYGPVGKDGSTEGGAEVGALCSYGDPNTLTLDIGTSKLAQACSAYTCLVEFEKYQGKVPKVSSFDGPIEVEI | Reduces trimethylamine-N-oxide (TMAO) into trimethylamine; an anaerobic reaction coupled to energy-yielding reactions. | O87948 |
A4F267 | TM40L_RAT | Protein TOMM40-like | Rattus | MGNTLGLAPMGTLPRWSHRREEPLPNPGSFDELHRLCKDVFPAQMEGVKLVVNKVLSSHFQVAHTVHMSALGLPGYHLHTAYAGDWQLSPTEVFPTVVGDMDSSGSLNAQVLLLLAERLRAKAVFQTQQAKFLTWQFDGEYRGDDYTATLTLGNPDLIGESVIMVAHFLQSITHRLVLGGELVYHRRPGEEGAILTLAGKYSALHWVATLNVGSGGAHASYYHKANEQVQVGVEFEANTRLQDTTFSFGYHLTLPQADMVFRGLVDSNWCVGAVLEKKMRPLPVTLALGAFLNHWRNRFHCGFSITVG | Potential channel-forming protein implicated in import of protein precursors into mitochondria. | A4F267 |
P0C296 | TX22_ANDCR | Toxin Acra II-2 | Androctonus | ADVPGNYPLNTNGNMYYCTILGENEFCRKVCKVHGVKYGYCFNSHCWCEYLEAKDVSVWNAAKNYCKNPVGK | Binds to sodium channels (Nav) and affects the channel activation process. | P0C296 |
Q2K3D7 | TSAD_RHIEC | tRNA threonylcarbamoyladenosine biosynthesis protein TsaD | Rhizobium | MVPFMRILGIETSCDETAAAVVERNAEGHCNVLSDVVLSQLDEHSAYGGVVPEIAARAHVEALDELIEQALKRANVSLADVDAIAATSGPGLIGGLLVGLMTGKAIARAAGKPLYAINHLEGHALTARLTHGLSFPYLVLLVSGGHTQLILVRGVGQYERWGTTIDDALGEAFDKTAKLLGLPYPGGPAVERMARDGNADRFDFPRPLVGEARLDFSFSGLKTAVRQAAQDIAPLSDQDVADICASFQRAISRTLKDRIGRGLQRFKREFPATGEKPALVVAGGVAANLELRATLQALCDKNGFRFIAPPLSLCTDNAVMIAWAGLERMATGVAPDTLDVQPRSRWPLDANAETLIGFGKRGAKA | 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. | Q2K3D7 |
A7FXK4 | YBEY_CLOB1 | Endoribonuclease YbeY | Clostridium | MIYIDNRQNKIKVNEELENKIKEIIDYALKEEKVNIDYEISVVFIDNNSIKEINKDYRNIDKATDVLSFPMLDYEDGEVFKDIYLNYEFDESDLDEGNLVLGDIALSLEKAEEQSKEFGHSFLRETCYLTIHSVLHLLGYDHMEEDEKVIMRQREEEILKSFNLHR | Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA. | A7FXK4 |
Q21VL5 | THIE_ALBFT | Thiamine-phosphate pyrophosphorylase | Rhodoferax | MVGASTLAHDVRLQALRLYLVTDQFCAGGRTLADVVAAAVQGGVTCVQLREKQLNTRDFLAQALALKDLLAPHGIPLVINDRIDVALACGAQGVHLGQSDMPVTQARRLLPPEVFIGWSVETLEDVARSAELPVDYLGVSPIFATPTKTDTLPPWGLEGLRQVRRATTVPLVAIGGIHVGNAREVLLAGADGLAVVSALCAAQDPCVAALRLRQLIDAV | 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). | Q21VL5 |
Q9KPL8 | TYPH_VIBCH | TdRPase | Vibrio | MSLSQAKYLPQEIIRRKRDGEVLTNDEINFFIQGVANNTVSEGQIAAFAMAIFFREMTMPERIALTCAMRDSGMVIDWSHMNFDGPIVDKHSTGGVGDVTSLMLGPMVAACGGYVPMISGRGLGHTGGTLDKLEAIPGYNITPTNDVFGKVTKQAGVAIIGQTGDLAPADKRVYATRDITATVDNISLITASILSKKLAAGLESLVMDVKVGSGAFMPTYEASEELAKSIVAVANGAGTNTTAILTDMNQVLASSAGNAVEVREAVRFLTGEYRNPRLLEVTMASCAEMLVLGKLAKDTAQAREKLQAVLDNGQAADRFGKMVAGLGGPSDFVENYDKYLAKAEIIRPVYAQQSGVISAMDTRAIGMAVVGMGGGRRVATDRIDYAVGFDQFIRLGEIADSNKPLAMIHARNEEQWQQAANALQSAIKVGGDYLPTPDVYRQIRAQDV | The enzymes which catalyze the reversible phosphorolysis of pyrimidine nucleosides are involved in the degradation of these compounds and in their utilization as carbon and energy sources, or in the rescue of pyrimidine bases for nucleotide synthesis. | Q9KPL8 |
P45312 | Y1677_HAEIN | Probable iron-sulfur cluster repair protein HI_1677 | Haemophilus | MSFAQQKLSELAVSIPGATKIFREYDLDFCCGGSVLLEVAAQQKNLNLAEIEKRLTDLQQSKAENNDKDWTSASYAEMIDHIITRFHNRHREQLPELITLAEKVENIHGDRDDCPIGVVAQLEKIYAELSQHLMKEEQILFPMIKMGNYAMASMPIRVMEMEHDEAGQDVEVIKSLTNNCTPPADACFSWKALYSGINEFIDDLMHHIHLENNILFPRVLNEK | Di-iron-containing protein involved in the repair of iron-sulfur clusters. | P45312 |
P00986 | VKT2_NAJNI | Venom basic protease inhibitor II | Naja | RPRFCELPAETGLCKARIRSFHYNRAAQQCLEFIYGGCGGNANRFKTIDECHRTCVG | Serine protease inhibitor. | P00986 |
Q2UUJ9 | TVP38_ASPOR | Golgi apparatus membrane protein tvp38 | Aspergillus subgen. Circumdati | MPADYTSTARALSLPTSPSESLSPADNDSYPPWSHLASGRSNPAHPSERPTLWKQVTHRLNETSQRMMAIWRRLSFWQKVGAAAAALLANLLGIGFLVFTGKVFIWLGPVAEQWEQSVVAYTVLWLCVFFVSFPPLVGWSTFGTISGYIFGVWKGWFLYASATVLGSTCSFVVSRTILSKFVNRMMERDKRFAALALTLKYDGLKLLCMIRLCPLPYSVCNGAVSTFPTVQPLMYGLATAIVTPKLLVPAFVGSRIRLLSEKGEEMSAGSKAVNIISIIVTVAIGIFTGWYIYKRTMARAKELEAQERADIRRSLQADHADRRPHHSFSEDPDVNTAATTLARDEEERLGFHDFDDDNVDLAIDDESGGENSPRLQSGGPYRDEFTDNDSDDVFKNGDGGEGETYGLHTHVRKS | Golgi membrane protein involved in vesicular trafficking and spindle migration. | Q2UUJ9 |
A1S3Z2 | TRMD_SHEAM | tRNA [GM37] methyltransferase | Shewanella | MWLGVITLFPEMFRAITDFGVTGRAIKNGLLELHTWNPRDFTHDRHRTVDDRPYGGGPGMLMMVQPLKDAIQAARTAAGDGAKVIYLSPQGRKLTQRGATELAETQKLILVCGRYEGIDERIIQTEVDEEWSIGDYVLSGGELPAMTLIDAVSRLVPGVLGKQASAEQDSFSDGLLDCPHYTRPESLDGLEVPAVLLGGNHEDIRRWRLKQSLGRTFLRRPELFENLALTDEQTRLLAQFVDEMDSPQKS | Specifically methylates guanosine-37 in various tRNAs. | A1S3Z2 |
A1UQZ7 | TSAD_BARBK | tRNA threonylcarbamoyladenosine biosynthesis protein TsaD | Bartonella | MRLLGIETSCDETATAVIEHNLKGKSHILSNIVWSQIEDHAPYGGVVPEIAARAHVEILDTLILEALAKAKTTLKEIDAIAVTGGPGLIGGLLVGLMSAKALAFATGKPFIAVNHLEGHALTAVLTHQVTFPYLLLLVSGGHTQMILVHGVGNYQRLGTTFDDALGEAFDKTAKLLGLPYPGGPALEKAALLGDKNRIPLPRPLKGNKQLNFSFSGLKTAVRQAATAMAPLSEQDVSDIAASFQAAVIDTLQDRVHLALQYFTSQYPSSHNQEHRPPAFVVAGGVAANQAIRLTLQNLAHQHSFEFIAPPPSLCTDNAAMIAFAGAERIARGQTSPLDIAPRSRWPLDENALPLIGTGRRGAKV | 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. | A1UQZ7 |
B5FDB4 | YCIB_ALIFM | Inner membrane-spanning protein YciB | Aliivibrio | MKQILDFIPLIIFFALYKMYDIYTATGALIIATAIQLVVTYALYKKVEKMQLITFIMVTVFGGMTIFLHDDNFIKWKVTIVYCVFAAGLIIAHILGKPVIKGMLGKEVTLPDDKWAKINHAWVLFFTVCAIANLYVAFEMPLDVWVNFKVFGLLGLTFLYTLFTGMYVYKHMPKEKKEEQE | Plays a role in cell envelope biogenesis, maintenance of cell envelope integrity and membrane homeostasis. | B5FDB4 |
B3PLP1 | TRPD_CELJU | Anthranilate phosphoribosyltransferase | Cellvibrio | MDIKQALKKLVASIDLSTEEMISVMRIVMTGGATPAQIGGFLVALRMKGETLDEITGAAMVMRELATPVNIDVDYLVDTCGTGGDGANLFNLSTASAFVVAAAGGRVAKHGNRSVSSSTGSADVLEAAGIKLDITAEQVARCVKEIGVGFMFAPSHHSAMKHAIGPRRELGMRTIFNMLGPLTNPANVKRQVIGVFNGELCKPMAEVLGRLGSEHVMVVHAKDGLDEISLATETQVAELKGGEIREYIIKPEDFGMQSKSLIGLSVSNAEDSLLLIRDALGNRRGQYAEKAADIIALNAGAAIYVSGVAGSLSDGVEMARDAIGSSLAGEKIRELAAFTQYLQ | Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA). | B3PLP1 |
Q8CFK2 | TF3B_MOUSE | B-related factor 1 | Mus | MTGRVCRGCGGTDIELDAARGDAVCTGCGSVLEDNIIVSEVQFVENSGGGSSAVGQFVSLDGAGKTPTLGGGFHVNLGKESRAQTLQNGRRHIHHLGSQLQLNQHCLDTAFNFFKMAVSKHLTRGRKMAHVIAACLYLVCRTEGTPHMLLDLSDLLQVNVYVLGKTFLLLARELCINAPAIDPCLYIPRFAHLLEFGEKNHEVSMTALRLLQRMKRDWMHTGRRPSGLCGAALLVAARMHDFRRTVKEVISVVKVCESTLRKRLTEFEDTPTSQLTIDEFMKIDLEEECDPPSYTAGQRKLRMKQLEQVLSKKLEEVEGEISSYQDAIEIELENSRPKAKGALANLSKDGSGEDATSSPRCEEDTEDEELEAAASHMNKDFYRELLGDDDGSEAAGDPDGGSRPLALESLLGPLPTAASLGISDSIRECISSPSGDPKDSSGDGELDLSGIDDLEIDRYILNESEARVKAELWMRENAEYLREQKEKEARIAKEKELGIYKEHKPKKSCKRREPILASTAGEAIEKMLEQKKISSKINYSVLRDLNSKGGGSPPRDDSQPPERASTKKLSRRKRATTRNSADPGTSTGKRLRPLLSAQPAKKAAVGEALLLSSPALGAEPVKPSAVLVESGPVPYHPEEDADEEDAEDEDGEPCVSALQMMGGNDYGCDGDEDDGY | General activator of RNA polymerase which utilizes different TFIIIB complexes at structurally distinct promoters. | Q8CFK2 |
P0A8Y6 | YIDA_ECOL6 | Sugar phosphatase YidA | Escherichia | MAIKLIAIDMDGTLLLPDHTISPAVKNAIAAARARGVNVVLTTGRPYAGVHNYLKELHMEQPGDYCITYNGALVQKAADGSTVAQTALSYDDYRFLEKLSREVGSHFHALDRTTLYTANRDISYYTVHESFVATIPLVFCEAEKMDPNTQFLKVMMIDEPAILDQAIARIPQEVKEKYTVLKSAPYFLEILDKRVNKGTGVKSLADVLGIKPEEIMAIGDQENDIAMIEYAGVGVAMDNAIPSVKEVANFVTKSNLEDGVAFAIEKYVLN | Catalyzes the dephosphorylation of different sugar phosphates. | P0A8Y6 |
V9QFG9 | TXAC_STEGR | Latrodectin | Steatoda | MNVLHFLILLMSVVSVFCINPEDIGCDDSITPEKFAENDAKCVQCKEQFEETNMLEQCREDCFKGKFFRSCVDHLSGAYDEKDDVEAPPPE | May increase the toxicity of alpha-latrotoxin and/or other venom components. Is non-toxic to mice and to the cockroach Periplaneta americana. | V9QFG9 |
Q7VKR0 | UVRC_HAEDU | Excinuclease ABC subunit C | Haemophilus | MSQFNAKAFLADVPHLPGVYRMYDANQAIIYVGKAKDLKKRLASYFRSQVASKKIEALVGNIHHIDTTITHSETEALLLEHNYIKQHQPKYNVLLRDDKSYPYLLLTKHQHPRLTAFRGSKKVAGEYFGPYPNVSAVRESLNLLQKIFPIRQCEDNYYKNRSRPCLQHQIGRCLAPCVTGYCSQQEYDNQVKWVRLFLQGKDSQVIDYLMQKMEIAASELDFETAARFRDQIQSVRAVQEKQFVANQRLDDLDIISIAYQSGLACAHILFIRQGKVLGNRAYFPKVPSHTDLTELADTFIGQFYLQLNQHRSIPNQIILDQPLTESNALAQLLTEQAGHKVTIITNHVRGDKSRYLALAQTNARAALSLQLKQSTTIHKRYDALKILLKLPTIKRMECFDISHTMGSQTVASCVVFDENGPLKSDYRRFNIEGITGGDDYAGMEQALVKRYDKPLPIEKIPDIIFIDGGKGQLNRALQVFEKLTVAWDKHKPLLIGVAKGAERKAGLETLIIGRLKKEIHLPIDSPALHLIQHIRDESHHHAISGHRKKRQKAFVESGLESIAGVGAKRRQALLKYLGGMQGVKSATLAEIESVPGISKTLAGVIFDTLHNS | 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. | Q7VKR0 |
P9WQ20 | TREY_MYCTO | (1,4)-alpha-D-glucan 1-alpha-D-glucosylmutase | Mycobacterium tuberculosis complex | MAFPVISTYRVQMRGRSNGFGFTFADAENLLDYLDDLGVSHLYLSPILTAVGGSTHGYDVTDPTTVSPELGGSDGLARLSAAARSRGMGLIVDIVPSHVGVGKPEQNAWWWDVLKFGRSSAYAEFFDIDWELGDGRIILPLLGSDSDVANLRVDGDLLRLGDLALPVAPGSGDGTGPAVHDRQHYRLVGWRHGLCGYRRFFSITSLAGLRQEDRAVFDASHAEVARWFTEGLVDGVRVDHLDGLSDPSGYLAQLRELLGPNAWIVVEKILAVDEALEPTLPVDGSTGYDVLREIGGVLVDPQGESPLTALVESAGVDYQEMPAMLADLKVHAAVHTLASELRRLRRCIAAAAGADHPLLPAAVAALLRHIGRYRCDYPGQAAVLPCALAETHSTTPQLAPGLQLIAAAVARGGEPAVRLQQLCGAVSAKAVEDCMFYRDARLVSLNEVGGEPRRFGVGAAEFHHRAATRARLWPRSMTTLSTHDTKRGEDVRARIGVLSQVPWLWAKFIGHAQAIAPAPDAVTGQFLWQNVFGVWPVSGEVSAALRGRLHTYAEKAIREAAWHTSWHNPNRAFEDDVHGWLDLVLDGPLASELTGLVAHLNSHAESDALAAKLLALTVPGVPDVYQGSELWDDSLVDPDNRRPVDYGTRRVALKALQHPKIRVLAAALRLRRTHPESFLGGAYHPVFAAGPAADHVVAFRRGDDILVAVTRWTVRLQQTGWDHTVLPLPDGSWTDALTGFTASGHTPAVELFADLPVVLLVRDNA | Catalyzes the conversion of maltooligosaccharide into the non-reducing saccharide, maltooligosyl trehalose (alpha-maltooligosyl alpha-D-glucoside) by intramolecular transglycosylation. | P9WQ20 |
A4XPW1 | THIC_PSEMY | Thiamine biosynthesis protein ThiC | Pseudomonas | MSAQQQKNLSESAQVDQQSVQPFPRSQKVYVQGSRPDIRVPMREISLDVTPTDFGGEINAPVTVYDTSGPYTDPNVTIDVRKGLSDVRSAWIEDRGDTEKLPGLSSEFGQRRLNDAELSAMRFAHVRNPRRARAGHNVSQMHYAKKGIITPEMEFVAIRENMKLAEAREAGLLNEQHAGHSFGASIPKEITPEFVRSEVARGRAIIPANINHVELEPMIIGRNFLVKINGNIGNSALGSSIEEEVAKLTWGIRWGSDTVMDLSTGKHIHETREWIIRNSPVPIGTVPIYQALEKVGGIAEDLTWELFRDTLIEQAEQGVDYFTIHAGVLLRYVPLTAKRVTGIVSRGGSIMAKWCLAHHKENFLYTHFEDICEIMKAYDVSFSLGDGLRPGSIADANDAAQFGELETLGELTKIAWKHDVQCMIEGPGHVPMQLIKENMDKQLECCDEAPFYTLGPLTTDIAPGYDHITSGIGAAMIGWFGCAMLCYVTPKEHLGLPNKDDVKTGIITYKIAAHAADLAKGHPGAQIRDNALSKARFEFRWEDQFNLGLDPDTARAFHDETLPKDSAKVAHFCSMCGPKFCSMKITQEVRDYAKEQRIDAVDLDAEQGMQAKAAEFKAQGSQLYQKV | 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. | A4XPW1 |
Q830K4 | THIM_ENTFA | 4-methyl-5-beta-hydroxyethylthiazole kinase | Enterococcus | MKTSVKFETIFPLTTAPLIQCITNEITCESMANALLYIDAKPIMADDPREFPQMFQQTSALVLNLGHLSQEREQSLLAASDYARQVNKLTVVDLVGYGASDIRNEVGEKLVHNQPTVVKGNLSEMRTFCQLVSHGRGVDGSPLDQSEEAIEELIQALRQQTQKFPQTVFLATGIQDVLVSQEQVIVLQNGVPELDCFTGTGDLVGALVAALLGEGNAPMTAAVAAVSYFNLCGEKAKTKSQGLADFRQNTLNQLSLLMKEKDWFEAVKGRVL | Catalyzes the phosphorylation of the hydroxyl group of 4-methyl-5-beta-hydroxyethylthiazole (THZ). | Q830K4 |
A3DHS8 | UPPP_ACET2 | Undecaprenyl pyrophosphate phosphatase | Acetivibrio | MLELIKAIFLGIVEGITEWLPISSTGHMILVEEFINMNLSDEFMEMFRVVIQLGAIMAVVVLYWNKLFPFSFEDRIQIKKDTFSLWIKVLAATLPAALIGVPFDDKIDELFYNYITVAITLIVYGVLFIIMENRNKSKIPAISTFEELGYKAVLLIGAFQVLALIPGTSRSGATILGAIMIGCSREIAAEFSFYLAIPVMFGASLLKLVKFGFAFSQTELIILLTGMIVAFAVSIFAIKFLMGYIKRNDFKAFGYYRIILGLIVVLYFLAVR | Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin. | A3DHS8 |
A1U501 | URED_MARN8 | Urease accessory protein UreD | Marinobacter | MTAYQAIDRHASGHRFDTERRWAAALELGFEARAESEPTPVTRLVRRRHHGPLRVQRPFYPEGKTGCCHVYLLHPPGGLVSGDELRIEATVAEGGHALLTTPAAAKLYKADSHGVAWGQHTRLQVAKDAILEYLPQETIAFDGSRGLQTTTIELATGARTLGWEVLALGRPASDLPFATGALEQRFHLSLDGQPLWLERQLLDPKHRRFNGPWGQGGATVQATLWAVGLDDEAAAIDVLRAQLPDHNRWAVTRRRGVLLLRYLGTERNEAWALCEQAWHLLRPMLASVPAHTPRIWLT | Required for maturation of urease via the functional incorporation of the urease nickel metallocenter. | A1U501 |
Q1GK93 | YBEY_RUEST | Endoribonuclease YbeY | unclassified Ruegeria | MILDVVIEDARWDAAALEKQAQEAVSATLAYLELEDEDWEVTVLGCDDARIADLNAEFREKPKPTNVLSWPAQELAAAQDGGQPTPPEVDFMGDAALGDIAISYDTCVKEANLAHKSREDHVRHLLVHGTLHLLGYDHIRDGDATIMETLEVGILGKLGIPDPYIIEDGP | Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA. | Q1GK93 |
P0C6A0 | ZGLP1_HUMAN | GATA-like protein 1 | Homo | MTEPQVGCVACPRVHKEPAQVGTPWPAKPRSHPRKRDPTALLPRSLWPACQESVTALCFLQETVERLGQSPAQDTPVLGPCWDPMALGTQGRLLLDRDSKDTQTRISQKGRRLQPPGTPSAPPQRRPRKQLNPCRGTERVDPGFEGVTLKFQIKPDSSLQIIPTYSLPCSSRSQESPADAVGGPAAHPGGTEAHSAGSEALEPRRCASCRTQRTPLWRDAEDGTPLCNACGIRYKKYGTRCSSCWLVPRKNVQPKRLCGRCGVSLDPIQEG | Transcriptional regulator that plays a key role in germ cell development. Determines the oogenic fate by activating key genes for the oogenic program and meiotic prophase entry. Acts downstream of bone morphogenetic protein (BMP) by regulating expression of genes required for the oogenic programs, which are repressed by Polycomb activities in sexually uncommitted germ cells. Regulates expression of STRA8, a central downstream effector for the meiotic program. Acts independently of retinoic acid (RA). In males, not required for germ-cell sex determination, but required to allow the spermatogonia to efficiently accomplish the meiotic prophase. | P0C6A0 |
Q9ZM59 | TATC_HELPJ | Sec-independent protein translocase protein TatC | Helicobacter | MFEDLKPHLQELRKRLMVSVGTILVAFLGCFHFWKNIFEFVKNSYKGTLIQLSPIEGVMVAVKISFSAAIVISMPIIFWQLWLFIAPGLYKNEKKVILPFVFFGSGMFLMGAAFSYYVVFPFIIEYLATFGSDVFAANISASSYVSFFTRLILGFGVAFELPVLAYFLAKVGLITDASLKAYFKYAIVVIFIVAAIITPPDVVSQIFMALPLVGLYGLSILIAKMVNPAPKDNENDHENDAKEHTKSES | 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. Together with TatB, TatC is part of a receptor directly interacting with Tat signal peptides. | Q9ZM59 |
A4WMQ7 | UPP_PYRAR | UPRTase | Pyrobaculum | MPVRIIDHVYAQYLLTRLRDKNTGSLDFRKGLVRLGRIIGYELVKTFPFRYVEVETPLGRAVGVDIIGLDKVVIVQILRAAMPLVEGLVKAFPNARLGVVAARRKEEEGYVDVEVFYSKMPSIGVEDTVIVADPMLATGTTMSKAIEEVYKTGTPGRLVVVSVIATPVGISRVLSRWPDTEIYTVAIDPELNDKAFIVPGLGDAGDRAFAT | Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate. | A4WMQ7 |
B1LN84 | THIM_ECOSM | 4-methyl-5-beta-hydroxyethylthiazole kinase | Escherichia | MQVDLLSSAQSAHALHLFHKHSPLVHCMTNDVVQTFTANTLLALGASPAMVIETEEASQFAAIASALLINVGTLTQPRAQAMRAAVEQAKRSQTPWTLDPVAVGALDYRRRFCLELLSHKPTAIRGNASEIMALAGVANGGRGVDTTDAAANAIPAAQTLARETGAIVVVTGEVDYVTDGHRIVGIHGGDPLMTKVVGTGCALSAVVAACCALPGDTLENIAFACHWMKQAGERAVARSEGPGSFVPHFLDALWQLTQEVQA | Catalyzes the phosphorylation of the hydroxyl group of 4-methyl-5-beta-hydroxyethylthiazole (THZ). | B1LN84 |
P56495 | TSHR_SHEEP | Thyroid-stimulating hormone receptor | Ovis | MRPTPLLRLALLLVLPSSLWGERCPSPPCECRQEDDFRVTCKDIQRIPSLPPSTQTLKFIETHLKTIPSRAFSNLPNISRIYLSIDATLQQLESHSFYNLSKVTHIEIRNTRSLTYIDSGALKELPLLKFLGIFNTGLRVFPDLTKIYSTDVFFILEITDNPYMTSVPANAFQGLSNETLTLKLYNNGFTSIQGHAFNGTKLDAVYLNKNKYLTVIDQDAFAGVYSGPTLLDISYTSVTALPSKGLEHLKELIARNTWTLKKLPLSLSFLHLTRADLSYPSHCCAFKNQKNIRGILQSLMCNESSIWGLRQRKSASALNGPFYQEYEEDLGDGSAGYKENSKFQDTHSNSHYYVFFEDQEDEIIGFGQELKNPQEETLQAFDNHYDYTVCGGSEEMVCTPKSDEFNPCEDIMGYKFLRIVVWFVSLLALLGNVFVLVILLTSHYKLTVPRFLMCNLAFADFCMGLYLLLIASVDLYTQSEYYNHAIDWQTGPGCNTAGFFTVFASELSVYTLTVITLERWYAITFAMHLDRKIRLWHAYVIMLGGWVCCFLLALLPLVGISSYAKVSICLPMDTETPLALAYIILVLLLNIIAFIIVCACYVKIYITVRNPHYNPGDKDTRIAKRMAVLIFTDFMCMAPISFYALSALMNKPLITVTNSKILLVLFYPLNSCANPFLYAIFTKAFQRDVFMLLSKFGICKRQAQAYRGQRVSSKNSTGIRVQKVPPDVRQSLPNVQDDYELLGNSHLTPKQQDQTSKEYKQTVL | Receptor for the thyroid-stimulating hormone (TSH) or thyrotropin. Also acts as a receptor for the heterodimeric glycoprotein hormone (GPHA2:GPHB5) or thyrostimulin. The activity of this receptor is mediated by G proteins which activate adenylate cyclase. Plays a central role in controlling thyroid cell metabolism. | P56495 |
P20352 | TF_MOUSE | Coagulation factor III | Mus | MAILVRPRLLAALAPTFLGCLLLQVIAGAGIPEKAFNLTWISTDFKTILEWQPKPTNYTYTVQISDRSRNWKNKCFSTTDTECDLTDEIVKDVTWAYEAKVLSVPRRNSVHGDGDQLVIHGEEPPFTNAPKFLPYRDTNLGQPVIQQFEQDGRKLNVVVKDSLTLVRKNGTFLTLRQVFGKDLGYIITYRKGSSTGKKTNITNTNEFSIDVEEGVSYCFFVQAMIFSRKTNQNSPGSSTVCTEQWKSFLGETLIIVGAVVLLATIFIILLSISLCKRRKNRAGQKGKNTPSRLA | Initiates blood coagulation by forming a complex with circulating factor VII or VIIa. The [TF:VIIa] complex activates factors IX or X by specific limited proteolysis. TF plays a role in normal hemostasis by initiating the cell-surface assembly and propagation of the coagulation protease cascade. | P20352 |
P0C1X4 | TUXA_POLAB | Turripeptide PaIAb | Polystira | RKRLFYRYYSHPGNYMYLGHYGRYYNMLHNCNAMLLAHQMQAMRRYQHRMRVKQMYRRIKMKQMYRHMKWMGMYRQAKAARLRCI | Is lethal to drosophila larvae. | P0C1X4 |
Q7XA86 | ZDH11_ARATH | Zinc finger DHHC domain-containing protein At3g51390 | Arabidopsis | MGVCCPFLQPWDRARDQCLLNLPCLSDPVRRSSLLLKLALVALHLVFIGFLFLFDAEFIEKTKRDPWYMGCYILLFSATLLQYFVTSGSSPGYVVDAMRDVCEASAMYRNPSTTSIQHASRKSESVVVNVEGGSASCPRRPPTPWGKLVLDLYPPGTSIRNLTCGYCHVEQPPRTKHCHDCDRCVLQFDHHCVWLGTCIGQKNHSKFWWYICEETTLCIWTLIMYVDYLSNVAKPWWKNAIIILLLVILAISLIFVLLLLIFHSYLILTNQSTYELVRRRRIPYMRNIPGRVHPFSRGIRRNLYNVCCGNYNLDSLPTAFELEDRSRPYTCIDMLKCRCC | S-acyltransferase involved in protein lipid modification. Catalyzes the palmitoylation of proteins peripheral or integral to the tonoplast. Required for the tonoplast localization of CBL2, CBL3 and CBL6, but not for the plasma membrane localization of CBL9, for the endosome localization of RABF1 or for the endomembrane localization of RABF2B. | Q7XA86 |
Q8I8A2 | TCTP_SCHHA | Translationally-controlled tumor protein homolog | Schistosoma | MNFREERYDTIMFTDSHCPRVVADFFYEVESRFTTASSKVDGRLIGANPSGEGEDDEDVDDTSERVIDLVHANGFISVPYDLKSYKAQLKSYLKAIKERLQKTVPDKLPLLESQVNKYRKDVFANFDQYECFTGPSTNPEAMVVLMNFVCGR | Involved in calcium binding and microtubule stabilization. | Q8I8A2 |
Q9I0D9 | TSI2_PSEAE | Anti-toxin protein Tsi2 | Pseudomonas | MNLKPQTLMVAIQCVAARTRELDAQLQNDDPQNAAELEQLLVGYDLAADDLKNAYEQALGQYSGLPPYDRLIEEPAS | Immunity protein that plays a role in preventing early activation of toxin Tse2. Binds to a large surface of Tse2 and thereby occludes the active site to specifically inhibits Tse2. | Q9I0D9 |
B1WR77 | TRMFO_CROS5 | Folate-dependent tRNA(M-5-U54)-methyltransferase | Crocosphaera subtropica | MTESTAKVQVIGGGLAGTEAAWQVAQAGIPVILHEMRPIRTSPAHHSQELAELVCSNSFGAMSSNRAAGLLHEELRRLNSIIIQTADKHAVPAGGALAVDRGVFSHQLTQTLQNHPLIELRRSEVQEIPSDGIVILATGPLTSPVLAEKLQQFTGMAYMSFFDAASPIIVGDSINRDIAFLASRYDKGEAAYLNCPLNPEQYLQFRDELCTAEQAELKEFERETAKFFEGCLPIEELAQRGEDTMRYGPLKPVGLFDARLGDFRDPENKEKRPYAVVQLRQEDKQGKLWNMVGFQTNLKWGEQKRVFRLIPGLENAEFVRMGVMHRNTFINSPQLLDPTLQFKSRPTLLAAGQLIGTEGYTAASAGGWLAGTNAARIALGLEPISLPSTTMMGALFEFISSASPKHFQPMPPNFGILPDLPVRIRNKRERYGKYRDRALADLNDCQTQLNNHQKNSVILV | Catalyzes the folate-dependent formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs. | B1WR77 |
Q4LCT0 | TXA8_ANDAU | Peptide AaF1CA8 | Androctonus | MMKLMLFSIIVILFSLIGSIHGADVPGNYPLDSSDDTYLCAPLGENPFCIKICRKHGVKYGYCYAFQCWCEYLEDKNVKI | Inhibits the vertebrate potassium channels Kv1.1/KCNA1 and Kv1.3/KCNA3 in vitro with an IC(50) of 5.3 nM and 50.0 nM respectively. | Q4LCT0 |
Q92MK1 | UBIG_RHIME | 3-demethylubiquinone 3-O-methyltransferase | Sinorhizobium | MSETARTTIDQSEVDRFSAMAAEWWDPTGKFRPLHKFNPVRLTYIRDRVSEHFGRDAKSRQPLEGLRVLDIGCGGGLLSEPMARMGADVVGADASEKNIGIARTHAAGSGVSVDYRAVTAEALAEAGESFDVVLNMEVVEHVADVEFFMTTCAHMVRPGGLMFVATINRTLKAAALAIFAAENVLRWLPRGTHQYDKLVRPDELERPLEASGMEIADRTGVFFNPLANQWNLSRDMDVNYMIVAKRPI | O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway. | Q92MK1 |
O60830 | TI17B_HUMAN | Mitochondrial import inner membrane translocase subunit Tim17-B | Homo | MEEYAREPCPWRIVDDCGGAFTMGVIGGGVFQAIKGFRNAPVGIRHRLRGSANAVRIRAPQIGGSFAVWGGLFSTIDCGLVRLRGKEDPWNSITSGALTGAVLAARSGPLAMVGSAMMGGILLALIEGVGILLTRYTAQQFRNAPPFLEDPSQLPPKDGTPAPGYPSYQQYH | Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane. | O60830 |
Q5RAM9 | ZN664_PONAB | Zinc finger protein 664 | Pongo | MIYKCPMCREFFSERADLFMHQKIHTAEKPHKCDKCDKGFFHISELHIHWRDHTGEKVYKCDDCGKDFSTTTKLNRHKKIHTVEKPYKCYECGKAFNWSSHLQIHMRVHTGEKPYVCSECGRGFSNSSNLCMHQRVHTGEKPFKCEECGKAFRHTSSLCMHQRVHTGEKLYKCYECGKAFSQSSSLCIHQRVHTGEKPYRCCGCGKAFSQSSSLCIHQRVHTGEKPFKCDECGKAFSQSTSLCIHQRVHTKERNHLKISVI | May be involved in transcriptional regulation. | Q5RAM9 |
A9VJW3 | TRPA_BACMK | Tryptophan synthase alpha chain | Bacillus cereus group | MGVEKIIAAFENGKKAFIPYVMGGDGGLEKLKERIRFLDEAGASIVEIGIPFSDPVADGPTIQRAGKRALDSGVTLKGIFQALIEVRQEVQIPFVLMTYLNPVLAFGKERFIESCLEAGVDGIIVPDLPYEEQDIIAPLLRVANIALIPLVTVTSPIERIEKITSESQGFVYAVTVAGVTGVRQNFKDEIRSYLEKVKEHVHLPVVAGFGISTREQIEEMITICDGVVVGSKVIELLENEKREEICELIHAVKETEEA | The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. | A9VJW3 |
Q1MND5 | TRPA_RHIL3 | Tryptophan synthase alpha chain | Rhizobium | MTARMDKRFAELKAEGRPALVTYFMGGDPDYDTSLGIMKALPEAGSDIIELGMPFSDPMADGPAIQLAGQRALKGGQTLKKTLQLAADFRKTNDATPIVMMGYYNPIYIYGVEKFLDDALLAGIDGLIVVDLPPEMDDELCIPAIRKGINFIRLATPTTDEKRLPKVLKNTSGFVYYVSMNGITGSALPDPSLVSGAVERIKQHTKLPVCVGFGVKTAEHAKVIGGSADGVVVGTAIVNQVATSLTHDGKATADTVQAVATLVRGLSTGTRSARLVAAE | The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. | Q1MND5 |
Q7NZD3 | UBIE_CHRVO | Demethylmenaquinone methyltransferase | Chromobacterium | MDKTTHFGYKTVAESEKAGKVAEVFHSVASKYDVMNDLMSGGLHRVWKHFTLTTSGVRAGDKVLDIAGGTGDLSRGWAKRVGKTGEVWLTDINSSMLTVGRDRLLDEGVILPVSLADAEKLPFPDNYFDAVSVAFGLRNMTHKDAALKEMCRVLKPGGKLFVLEFSKVWKPLSPFYDFYSFKALPIMGKLVANDADSYQYLAESIRMHPDQETLKQMMLDAGFGKVDYHNLTGGVVALHKGVKF | Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2) and the conversion of 2-polyprenyl-6-methoxy-1,4-benzoquinol (DDMQH2) to 2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinol (DMQH2). | Q7NZD3 |
Q9PI55 | THIC_CAMJE | Thiamine biosynthesis protein ThiC | Campylobacter | MKTQMNYAKEGIFTKEMQIVAQKENLSKDFLLENIACGKIIIPANINHKSLDPNGIGFGLRTKVNVNLGVSNDCVDYSEEMKKVELAHKFGIEAIMDLSNYGKTSRFRDELVNVSKAMIGTVPVYDAVGFLEKDLKQINAKDFLDVVYHHAKSGVDFMTIHAGINSRAAHIFKQSKRLTNIVSRGGSVLYAWMMMKDAENPFFEYYDDLLDICLKYDVTLSLGDALRPGSTHDASDGAQISELIELSLLTQRAWDVGIQVMIEGPGHMAINEIEANMQLEKRLCKGAPFYVLGPLVTDIGAGYDHISGAIGGAVAAASGADMLCYVTPAEHLRLPNLEDVREGIVATKIAAHAGDIAKLPKERARDDEMSKARQEIDWEKMFKLAIDGEKAKKMFNERRPDDLNSCSMCGKMCAMNTMNQILKGEDVSLA | 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. | Q9PI55 |
A1U1Q4 | TIG_MARN8 | PPIase | Marinobacter | MQVSVETTSNIERRMTIGVPAQEIDQAVQKRLQETARTVRLNGFRPGKVPMSVVKRRFGDSIRQEVVGEAMRDNYIKALQEQDINPAGWPKLEPKTMEEGKDLEFVATFEVLPEIELGDLSKINVEKPVSEVADKDIDNMIDNLRRQQATMKEVKRKSKNKDIVTIDFKGSIDGEEFEGGSAEGHRLTLGSGQMIPGFEKGIVGGKAGEELEIDVTFPEDYHNEDLAGKDAKFAITIHKVEEPQLPELDQEFFKRFGIEAEDEVAFREEVKKNMERELKQAVSNKVKNDVVDGLLETTELEVPAALVDQEIDRLRQDAVQRFGGQVDFQQLPKEIFEEQAKRRVKTGLLFQEVVKKNDLKADEAKVEEKIQEIASTYEQPDEVVAHFNSNPDQKAQVESSVLEDAVVDFVLGAAKVKEKKMKYEEAVQAGQPQR | 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. | A1U1Q4 |
Q17YL7 | UVRB_HELAH | Excinuclease ABC subunit B | Helicobacter | MPLFDLKSPYSLAGDQPQAIDTLTKSLKNKNHYQTLVGVTGSGKTYTMANIIAQTNKPTLIMSHNKTLCAQLYSEFKAFFPHNRVEYFISHFDYYQPESYIPRRDLFIEKDSSINDDLERLRLSATTSLLGYDDVIVIASVSANYGLGNPEEYLKVMEKIKVGEKRAYKSFLLKLVEMGYSRNEVVFDRGSFRAMGECVDIFPAYNDAEFIRIEFFGDEIERIAVFDALERNEIKRLDSVMLYAASQFAVGSERLNLAIKSIEDELALRLKFFKEQDKILEYNRLKQRTEHDLEMISATGVCKGIENYARHFTGKAPNETPFCLFDYLGIFEREFLVIVDESHVSLPQFGGMYAGDMSRKSVLVEYGFRLPSALDNRPLKFDEFIHKNCQFLFVSATPNKLELELSKKNVAEQIIRPTGLLDPKFEVRDSDKQVQDLFDEIKLVVARDERVLITTLTKKMAEELCKYYAEWGLKVRYMHSEIDAIERNHIIRSLRLKEFDVLIGINLLREGLDLPEVSLVAIMDADKEGFLRSETSLIQTMGRAARNANGKVLLYAKKITQSMQKAFETTTYRRAKQEEFNKLHNITPKTVTRALEEELKLRDDETKIAKALKKDKIPKSEREKIIKELDKKMRECAKNLDFEEAMHLRDEIAKLRTL | 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. | Q17YL7 |
Q9TSV6 | VATG2_PIG | Vacuolar proton pump subunit G 2 | Sus | MASQSQGIQQLLQAEKRAAEKVADARKRKARRLKQAKEEAQMEVEQYRREREQEFQSKQQAAMGSQGNLSAEVEQATRRQVQGMQSSQQRNRERVLAQLLGMVCDVRPQVHPNYRIAA | Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment. | Q9TSV6 |
Q6G9W1 | XERC_STAAS | Tyrosine recombinase XerC | Staphylococcus | MNHIQEAFLNTLKVERNFSEHTLKSYQDDLIQFNQFLEQEHLQLKTFEYRDARNYLSYLYSNHLKRTSVSRKISTLRTFYEYWMTLDENIINPFVQLVHPKKEKYLPQFFYEEEMEALFKTVEEDTSKSLRDRVILELLYATGIRVSELVNIKKQDIDFYANGVTVLGKGSKERFVPFGAYCRQSIENYLEHFKPIQSCNHDFLIVNMKGEAITERGVRYVLNDIVKRTAGVSEIHPHKLRHTFATHLLNQGADLRTVQSLLGHVNLSTTGKYTHVSNQQLRKVYLNAHPRAKKENET | 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. | Q6G9W1 |
B0RZV0 | THII_FINM2 | tRNA 4-thiouridine synthase | Finegoldia | MLDWYISVSFGELTLKGKNRHTFEKRAISKILDAISDYKIEEYYQEQGKLYIKADVNDFDEIIDHIKKVFGIVYISPCVKCEKTVESMQDGVLKIIEGKIIKDKLQTFKVDVHRVDKRFEPKSPELNPLLGGTILKKYGNYVKVDIKNPDFFIYVDIKDNCYVYTDRIKGWGGLPIGSSGRGLLLLSGGIDSPVAAFLMAKRGVRVDCLHFHSYPFTSQRGFEKVKQLAEEVSYYTGNINFYSVNLLPVYKAITKNCKERMMTIISRRFMMRIAERIANENKIDALITGESLGQVASQTIQGVSVINEVTSLPILRPLIASDKTEIIEIAREIGTYETSILPFEDCCTVFTPKRPVTKPRIYDVKREEENLDIEALVQECIDNMELIKIRQ | 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. | B0RZV0 |
Q2G6V6 | TYSY_NOVAD | Thymidylate synthase | Novosphingobium | MSILRDSGRHYEWQYLDLMRRIWEHGDERVDRTGVGTRSVFGAELRFDLSDGRMPLLTTKRVYWKTATREFLWFLTGNTNIRPLCAQGVEIWTDWPLDRYRKETGDDISRKDFSARIVADEAFALRWGDLGPVYGKQWVDWPVFEPVGDGLFRRREAGVNQVADVVDSLRHNPGSRRHIIEGWNVAEIDRMALPPCHKTYQFHVSGNRLNGLLYQRSCDVALGLPFNLWGAALLVRLLAQQCDLQPGELVWMGGDTHLYLNHADLVEAQLSREPEGDPRLAILRRPDSIFGYRIEDFEVTGYAPQGHLSAPVAV | 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. | Q2G6V6 |
Q40287 | UFOG5_MANES | UDP-glucose flavonoid 3-O-glucosyltransferase 5 | Manihot | MGSTDLNSKPHIVLLSSPGLGHLIPVLELGKRIVTLCNFDVTIFMVGSDTSAAEPQVLRSAMTPKLCEIIQLPPPNISCLIDPEATVCTRLFVLMREIRPAFRAAVSALKFRPAAIIVDLFGTESLEVAKELGIAKYVYIASNAWFLALTIYVPILDKEVEGEFVLQKEPMKIPGCRPVRTEEVVDPMLDRTNQQYSEYFRLGIEIPTADGILMNTWEALEPTTFGALRDVKFLGRVAKVPVFPIGPLRRQAGPCGSNCELLDWLDQQPKESVVYVSFGSGGTLSLEQMIELAWGLERSQQRFIWVVRQPTVKTGDAAFFTQGDGADDMSGYFPEGFLTRIQNVGLVVPQWSPQIHIMSHPSVGVFLSHCGWNSVLESITAGVPIIAWPIYAEQRMNATLLTEELGVAVRPKNLPAKEVVKREEIERMIRRIMVDEEGSEIRKRVRELKDSGEKALNEGGSSFNYMSALGNEWEKSWKTQRSERSLW | In the presence of other necessary color factors, this glycosylation reaction allows the accumulation of anthocyanin pigments. | Q40287 |
O74860 | YQ9A_SCHPO | Putative pyridoxal kinase C18.10 | Schizosaccharomyces | MTFPNVKFIGNKRVLSIQSSVSHGYVGNRSATFPLQLHEWEVDVVPTVHFSNHLGYGATRGSACIPEEVHDLLNALLQDNGIVYDAILTGFVPNHDIIQVIFDCVLAYKKDHPKVLWLLDPVMGDQGKMYVDTNVISTYKAMIPHAFAITPNAFEVEILTDIVIHTQMDAKRGLEKIYQLYGIQNAIITSFEVEESPGTLFCMGYSCEHGKPQLFLYQFPSLSGVFTGTGDLFSGLLLAKYREELDKRKHQQSDETKQTKRPTVLACAVGQVLSCMHTVLVNTKTYADEILLEDPKIASDEFLLSNARELRLIQSRTALLSKKSIYEAEFLPGFEEGEDV | Required for synthesis of pyridoxal-5-phosphate from vitamin B6. | O74860 |
Q2L002 | TSAD_BORA1 | tRNA threonylcarbamoyladenosine biosynthesis protein TsaD | Bordetella | MIILGFESSCDETGVAAVCTQRGLLAHALHSQIAMHQEYGGVVPELASRDHIRRIVPLTREVLAQAGLRREDVGAVAYTAGPGLAGALLVGASVAQSLAWSLGLPAIAIHHLEGHLLSPLLADPRPEFPFVALLVSGGHTQLMRVDGVGRYVLLGETLDDAAGEAFDKSAKLMGLGYPGGPALSRLAEQGDASRFDLPRPMLHSGDLDFSFSGLKTAVLTRVKAATREGALDEQARADLAAATQAAIIEVLAAKSICALKQTGLKRLVVAGGVGANSLLRQRLAEVLPRMKATAYFPPLSLCTDNGAMIAFAAAERVKAGLANLEQGDHAFTVRPRWDLAELERG | 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. | Q2L002 |
B0JNA9 | URED_MICAN | Urease accessory protein UreD | Microcystis | MWQGNLELIYKQKNLATEINHVYATAPLKVQRPFYPEGKNLCHTVILHTAGGIVGGDVLQQKIHLQAATNALITTASAGKVYQSNGQMAQQLIEIKIDDNASLEWLPQETIIFNGAAFRQHLRVDLGENSSWLGWEITRFGRSARGEKFLAGEWHSNWEIWRSGQPLWLDRSCLLGGKMIEGFSGLNDSALIGTLVYIGQPVGRNLIEKVRDFSLEGERGVTNTLGDGLLCRYRGNSSGEVRQWFQQVWQILRREMSDQEAIIPRVWLSW | Required for maturation of urease via the functional incorporation of the urease nickel metallocenter. | B0JNA9 |
Q9Z998 | TAL_CHLPN | Transaldolase | Chlamydia | MSNQFDQLKKLSTIVCDSGDPELVKASGSQDATTNPSLILKVAQEPKFQELLNEAVVWGIRQNGDDLQTLSFILDKIQVNFALEIIKNIPGRISLEIDARLSFNVEAMVQRAVFLSQLFEAMGGDKKRLLVKIPGTWEGIRAVEFLEAKGIACNVTLIFNLVQAIAAAKAKATLISPFVGRIYDWWIAAYGDEGYSIDADPGVASVSNIYAYYKKFGIPTQIMAASFRTKEQVLALAGCDLLTISPKLLDELKKSQHPVKKELDPAEAKKLDVQPIELTESFFRFLMNEDAMATEKLAEGIRIFAGDTQILETAITEFIKQIAAEGA | Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway. | Q9Z998 |
Q9K5W7 | TGL_HALH5 | Transglutaminase | Halalkalibacterium (ex Joshi et al. 2022) | MGNDMIQVAGRPFSLESTTDFGRVERAILQQMLDSSEWFSYSSMNELRFELNVRINIMESAKEMNASQVTFTIFEHASCNPEYWTLTSTGGFLVRSDVRPSDAILDIYRNGTLYGFECATAIIIIYYQAILKSIGQLRFDSIFQHLYLYSWHTHPGLELHTFHADRFLPGDVVYFNNPDFHPDTPWFRGENAVVLSDGTFFGHGFGIMTAEQMIQSLNSYRFPGSMQPAYLANLITRISPLTIRNLLTLQSDRTTYHYSKAVIHHNLCSISSMDYQYYLLSLNG | Probably plays a role in the assembly of the spore coat proteins by catalyzing epsilon-(gamma-glutamyl)lysine cross-links. | Q9K5W7 |
B7J5W3 | YCIB_ACIF2 | Inner membrane-spanning protein YciB | Acidithiobacillus | MKLLTDFLPIILFFVAYRIHGIYTATEVLIVAAILLMAWQWWRRGRVETMTWVSTLLILTFGGLTLYFHNDTFIKIKPSILYVLFAAALLFTHWREEPLLQRLMGGQLPAALPLSFWRRLNGYWIAFFLFGAVLNLIVAYAFSTGIWVDFKLFGMLAITVIFVLFQAVVISRALPQEAKDGDSSA | Plays a role in cell envelope biogenesis, maintenance of cell envelope integrity and membrane homeostasis. | B7J5W3 |
Q5GT66 | TSAD_WOLTR | tRNA threonylcarbamoyladenosine biosynthesis protein TsaD | unclassified Wolbachia | MKTILAVETSCDETAVAIVNSEKQVLAQEILSQTEHKKRGGVIPEIASRAHMEHLSSLIKNSIEKSNLNFCNLDATAATSGPGLIGGLIVGTMMAKAIAHVTQKPFIAVNHLEAHVLVIRLLYEVKFPFLVLLISGGHCQFLIAQNVGKYIKLGETLDDSLGEAFDKVARMLGLSYPGGPLIEKLAKKGNGTRFKLPRAMRKRPGCNFSFSGIKTAVKNLVQELEMSEQDVCDVCASFQECISEILLDRVKNAVIMAESLNIKINDFVVTGGVAANNFLRKKLKKHINLNILFPPINLCTDNAVMVGWTGIEILQKDYIDSLNFAPRPRWELGSY | 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. | Q5GT66 |
Q0K020 | TAUE_CUPNH | Probable sulfite/organosulfonate exporter TauE | Cupriavidus | MKAELLLPLLGLQALLGAGTYFQTVTGFGLGMIVMGVTSGLGLAPVATVAAVVSLVTLANSACALPGKLQHIDWRAVAAAAIGILPSVVVGVLVLEYLSSSAATLLQLLLGAVILYGGLSAALKPAPLAQRSGDGTFFVSGVFGGLLSGMFGVSGPPLIFQFYRQPMKPVEIRCALILVFTVTSTVRTLFSAWQGQLDAAVCVQAAIAVPVVVIATLLGRRFPPPFSPATTRRVAFGVLIGIGASLMLPAISAWVL | Could be a sulfite/organosulfonate exporter with a wide substrate range, including 3-sulfolactate and 3-sulfopyruvate. | Q0K020 |
Q18BF1 | YQGF_CLOD6 | Putative pre-16S rRNA nuclease | Clostridioides | MLDGRIMGLDVGDKTIGVAVSDLMGLTAQGVKTIKRVGKKKDIEELKAIIKEKQVNKIVSGLPKNMNGTLGPQGEKVIKFCELVKAETGIDVEFWDERLSTVAAERSLLEADVSRQKRKKVIDMLAAVIILQGYLDFKINS | Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA. | Q18BF1 |
A8AK17 | TIG_CITK8 | PPIase | Citrobacter | MQVSVETTQGLGRRVTITIAADSIETAVKSELVNVAKKVRIDGFRKGKVPMNVVAQRYGASVRQDVLGDLMSRNFVDAIIKEKINPAGAPNYVPGEYKLGEDFTYAVEFEVYPEVELTGLESIEVEKPVVEVTDADVDVMLDTLRKQQATWKDKDGAADAEDRVTIDFTGSVDGEEFEGGKASDFVLAMGQGRMIPGFEDGIKGHKAGEEFTIDVTFPEEYHAENLKGKAAKFAINLKKVEERELPELTEEFIKRFGVEDGSVAGLRTEVRKNMERELKGAVRNRVKSQAIEGLVKANDIDVPSALIDSEVDVLRRQAAQRFGGNEKQALELPRELFEEQAKRRVVVGLLLGEVIRTQELKADEERVKGLIEEMASAYEDPKEVIEFYSKNKELMDNMRNVALEEQAVEAVLAKAKVTEKATSFNELMNQQA | 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. | A8AK17 |
B9MFI6 | UPPP_ACIET | Undecaprenyl pyrophosphate phosphatase | Diaphorobacter | MDTLLLLKAAIMGVVEGLTEFLPISSTGHLILAGSLLGFDDAKAKVFDIAIQTGAIFAVILVYWQRIRATLVALPTERQARRFALNVLIGFLPAVLLGLLLGKAIKAHLFTPVVVASTFILGGFVILWAERRQQAAVRIHAVDDMTPLDALKVGLVQCLAMVPGTSRSGATIIGGMLLGLSRKAATDYSFFLAIPTLIGAGVYSLYKERALLSAADIPLFAVGLVFSFISAWLCVRWLLRYISSHSFVPFAWYRIAFGLVVLVTAWSGLVTWAE | Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin. | B9MFI6 |
Q2TBH5 | UBXN8_BOVIN | UBX domain-containing protein 6 | Bos | MASRGVVGIFLLSALPLLCLELRRGKPDLGIKDLILLCGRIFLLLALLTLIISVTTSWVNSFKPSQVYLKEEEEKNEKRQKLVRKKQQEAQGEKVSRYIENVLKPSQEMKLKKLEERFYQMTGETWKLSNGHKLGGDEDLELDSESQTSFETSNREAAKRRNLPNSVTNISPPAEQPTKKEVLDLPEEPPETAEEVVTVALRCPSGRVLRRRFFKSCSSQVLFDWMMKLGYRTSLYSLSTSFPRRPLEVEAGWSLQDIGITVDTVLNVEEKEQSS | May play a role in reproduction. | Q2TBH5 |
B8CLM6 | TRPB_SHEPW | Tryptophan synthase beta chain | Shewanella | MSKLNPYFGEYGGMYVPQILMPALKQLETAFIEAQQDEAFQKEFTDLLKNYAGRPTALTLTRNLSPNPLAKIYLKREDLLHGGAHKTNQVLGQALLAKRMGKKEIIAETGAGQHGVATALACALLDLKCKVYMGAKDVERQSPNVFRMKLMGAEVIPVTSGSATLKDACNEAMRDWSASYDKAHYLLGTAAGPHPFPTIVREFQRMIGAETKQQILEREGRLPDAVIACVGGGSNAIGMFADFIDEEEVALIGVEPAGKGIDTPMHGAPLKHGKTGIFFGMKAPLMQDSEGQIEESYSVSAGLDFPSVGPQHAHLAATGRATYESATDDEALETFQLLARSEGIIPALESAHALAYAVKLAKAATKETLLVVNLSGRGDKDIFTVADILEKQQADSSTTEESGNE | The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. | B8CLM6 |
Q6MTI1 | TRMD_MYCMS | tRNA [GM37] methyltransferase | Mycoplasma | MKFSIITLFPKIINSYIEESIIKRAINKQAIKIEIIDLRNFSTLSHNQVDDYQYGGGSGMVLMIEPLIKAIESVKTTKSIVLLTTPQGKTLNQSIVKTYANNYEHIIIVCGHYEGYDERVLDYIDDEISIGDYVITGGELASLILVDSISRLLPNVIKQESHENESFENNLLDHPVYTKPYEFRNKKVPDVLLSGHHQNIKKWREEQQVIKTLKKRPDLIDITKLNRHQLEIYKKMKGEQ | Specifically methylates guanosine-37 in various tRNAs. | Q6MTI1 |
Q45557 | TRUA_BACSV | tRNA-uridine isomerase I | Bacillus | MNNYKLMIQYDGGRYKGWQRLGNGENTIQGKIETVLSEMVGRKIEIIGSGRTDAGVHALGQVANVKLSENFTVKEVKEYLNRYLPHDISVTEVTLVPDRFHSRYNAKDKTYLYKIWNEDYTHPFMRKYSLHIEKKLHIDNMVKASQLFVGEHDFTAFSNAKSKKKTNTRTIHSITIQDNQGFIDIRVCGDGFLYNMVRKMVGTLIEVGLGEKEPEQVLTILESKDRSQAGFADATGLYLEGISF | Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs. | Q45557 |
A1A1Q5 | TSAD_BIFAA | tRNA threonylcarbamoyladenosine biosynthesis protein TsaD | Bifidobacterium | MSEPIVLGIESTCDETAAAVVQGRTLISNVVASSMDEHARYGGVIPEIASRAHAEAFVPCVSKALADANMTLSDVDAIAVSAGPGLAGCLAVGVSGAKSLAWAANKPIYGINHVIGHIAVTQLQFGPFPKDTLALIVSGGHTSLLHVEDVARHIDVVGTTLDDAAGECFDKVARLLGFPYPGGPHIDRHAQLGNPHAIKVPQGLTQGKAGQQHPYDFSFSGVKTAVARWIEQQQAEGNEIPIDDVCASLADSVATVLARKAMRGCEQYGSKTLIVGGGFSANSQLRAKLLEVGAKHGVEVRIPQIKLCTDNGAMVAMLGVNLVESGVKPSEPDFAIDSAMPLTKISM | 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. | A1A1Q5 |
Q04235 | TYW2_YEAST | tRNA(Phe) (4-demethylwyosine(37)-C(7)) aminocarboxypropyltransferase | Saccharomyces | MSDETMPVEFLVSDKRLLKTIKVKLETNGLFVTPIYSDNDNKVIKSSIEDLNHPLAVEINNIAGVKARFHESGNLERSEGHLKHQSNSITEFTKSFLKDHGLANDKIFLSHLLDHLPLKYTIYPPVVLFNNSTVRSFNHPIWQKAFQLKLFDPNEYYRELLCFLSPGKPSKGTSLHPNNRLLTHLAINNPITEADVLRRPFNIQPLYGKLIDDSILDDNDNTLWENPSQEQLNSSIWCKVIQNGVTQIWSPVFTMFSRGNIKEKKRVLTTFPDICNNDVVDLYAGIGYFTFSYLTKGARTLFAFELNPWSVEGLKRGLKANGFNKSGNCHVFQESNEMCVQRLTEFLSQNPGFRLRIRHINLGLLPSSKQGWPLAIKLIYLQGASLEKVTMHIHENVHIDAIEDGSFEKNVIVELDAINESIALIRNRGIKLQFVRSKLERIKTFAPDIWHVCVDVDVIVST | S-adenosyl-L-methionine-dependent transferase that acts as a component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of eukaryotic phenylalanine tRNA. Catalyzes the transfer of the alpha-amino-alpha-carboxypropyl (acp) group from S-adenosyl-L-methionine to the C-7 position of 4-demethylwyosine (imG-14) to produce wybutosine-86. | Q04235 |
P30961 | YCIB_BRADU | Inner membrane-spanning protein YciB | Bradyrhizobium | MDKTQPHPLFKLATELGPLLVFFFVNAKFNLFAATGAFMVAIVAAMIASYVVTRHIPIMAIVTGVIVLVFGTLTLVLHDETFIKVKPTIIYGLFAAILGGGLLFGRSFIAVMFDQMFNLTPQGWRILTLRWALFFAGMAVLNEIVWRTQSTDFWVNFKVFGVTPITMIFAIAQMPLTKRYHLEPVSLEASEADAGDVRKG | Plays a role in cell envelope biogenesis, maintenance of cell envelope integrity and membrane homeostasis. | P30961 |
Q8ES61 | Y782_OCEIH | Putative metal-dependent hydrolase OB0782 | Oceanobacillus | MNEKYPIGEFQFDGEITNIIINEWINEIEDLPRLLKNTVIDLNNEQLDTSYRSGGWTVRQVIHHLADSHMNAYIRLKLAITEENPVIKPYDEKEWAELYDYNLPIEISLSLIEALHKRWCSLLRDLSPTDMERTFKHPESGSISIGKNIGIYAWHGKHHLAHITSLCKRKDW | Possible metal-dependent hydrolase. | Q8ES61 |
B4L1K2 | UBA5_DROMO | Ubiquitin-like modifier-activating enzyme 5 | Drosophila | MSTAIDELQAIIAELKTELEEQKTSTRIARERIERMSAEVVDSNPYSRLMALQRMNIVKDYERIRDKAVAIVGVGGVGSVTADMLTRCGIGKLILFDYDKVELANMNRLFFTPDQAGLSKVEAAARTLSFINPDVVIETHNYNITTVENFDKFLTTISESGLQKGQPVDLVLSCVDNFEARMAINAACNENNLNWFESGVSENAVSGHIQFIRPGETACFACAPPLVVAENIDERTLKREGVCAASLPTTMGITAGLLVQNALKYLLNFGEVSDYLGYNALNDFFPKMTLKPNAECDDRYCLQRQKEFQARPQPKEQQIDEVVSNEPLHASNDWGIELVAEDAPVEQQTTNTTNVASGLRLAYEAPDKVDVNQSESAAVVNAGLPETSLDDLMAQMKSM | E1-like enzyme which activates UFM1. | B4L1K2 |
A7MEN2 | XGPT_CROS8 | Xanthine phosphoribosyltransferase | Cronobacter | MSEKYVVTWDMLQIHARKLASRLLPAEQWKGIIAVSRGGLVPGALLARELGIRHVDTVCISSYDHDNQRELKVIKRAEGDGEGFIVVDDLVDTGGTAVAIREMYPKARFVTIFAKPAGQPLVDDYVIDIPQDTWIEQPWDMGVVFVPPLSGR | 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. | A7MEN2 |
A0JRH6 | UREF_ARTS2 | Urease accessory protein UreF | Arthrobacter | MAAAGSYQLALQQLTDSALPTGAFAHSLGFETYIERGLVHDEASFGVWLSAFVGQQLSYSDGLAIRFLYEGVSFAELDALLTAQLLPRQLREASTKMGTRLLEIGTEVFPSPELAEYRALVGAGRAAGHQPLAFAVVARSLGVPLTESLAAYLFAAVTSLTQNAVRAIPLGQNAGQRLLRKASDDVAAAVERIGRLAPDDFGAVSPGLEISQMRHERQRARMFMS | Required for maturation of urease via the functional incorporation of the urease nickel metallocenter. | A0JRH6 |
Q55624 | Y755_SYNY3 | Thioredoxin reductase | unclassified Synechocystis | MTEVLRVGQPAPDFTATAIVDQSFQTVKLSTYRGKYLVLFFYPLDFTFVCPTEIIAFSDRHSEFTALDTEVVGISVDSEFSHLAWIQTERKMGGIGNINYPLVSDLKKEISQAYNVLEPDAGIALRGLFIIDREGILQYATVNNLSFGRSVDETLRVLKAIRHVQSHPNEVCPVDWQEGDKTMIPDPEKAKTYFETVAEP | 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. | Q55624 |
P0AED5 | UVRY_ECOLI | Response regulator UvrY | Escherichia | MINVLLVDDHELVRAGIRRILEDIKGIKVVGEASCGEDAVKWCRTNAVDVVLMDMSMPGIGGLEATRKIARSTADVKIIMLTVHTENPLPAKVMQAGAAGYLSKGAAPQEVVSAIRSVYSGQRYIASDIAQQMALSQIEPEKTESPFASLSERELQIMLMITKGQKVNEISEQLNLSPKTVNSYRYRMFSKLNIHGDVELTHLAIRHGLCNAETLSSQ | Member of the two-component regulatory system UvrY/BarA involved in the regulation of carbon metabolism via the CsrA/CsrB regulatory system . UvrY activates the transcription of the untranslated csrB RNA and of barA, in an autoregulatory loop. Mediates the effects of CsrA on csrB RNA by BarA-dependent and BarA-independent mechanisms . | P0AED5 |