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
|
|---|---|---|---|---|---|---|
A5UE25 | TRUD_HAEIE | tRNA-uridine isomerase D | Haemophilus | MLEQLPYLALKTPPKTTALLKAECADFIVKEHLGYEMSGDGEFVALYVRKTDCNTLFVGEKLAKFAGVSERNMGYAGLKDRRAVTEQWFCLQMPGMETPDFSQFELDGVEILTVTRHNRKIRTGSLEGNYFDILLRGAEESDELKVRLDFVANFGFPNYFTEQRFGREGHNLTQALRWAQGEIKVKDRKKRSFYLSAARSEIFNLVVAARIAKGATNQVLPNDIVQLAGSHSWFKADEKEDLNALQVRLENQDILLTAPLIGEDILAASDIENEIVNQHSVFDPLMKQERMKAARRPLLMKAKGFSWAFELEGLRLKFYLPAGSYATALVRELVNYTEE | Responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs. | A5UE25 |
Q2V338 | WNK9_ARATH | Protein kinase with no lysine 9 | Arabidopsis | MMNNLSHLESDYSEYVEVDPTGRYGRYNEVLGKGSSKTVYRGFDEYQGIEVAWNQVKLYDFLQSPQELERLYCEIHLLKTLKHKSIMKFYASWVDTDNRNINFVTEMFTSGTLRQYRLKHKRVNIRAVKNWCRQILRGLNYLHTHDPPVIHRDLKCDNIFINGNQGEVKIGDLGLAACLQHSHAAHCVGTPEFMAPEVYKEEYNQLVDIYSFGMCVLEMVTFDYPYSECSHPAQIYKRVISGKKPDGLDKVKDPEVRGFIEKCLATVSLRLSACELLDDHFLCIDESDMRRVESEKGLIDEAGTPLRHSYHIPHYSNGYYSLYNQNQWDYNGDETVESHEIDLLEFQNDDDEEEEDKRFGSVDISIKGKRRDNGDGLFLRLKTVNKEGCVRNIYFPFDIETDTAISVAREMVEELEMDDRDVTKIANMIDGEIASLVPNWSIFCSSESNRSSVGSVMDFNEMQCGRDGCEEKHGRFEEITFEITVNDSDEED | May regulate flowering time by modulating the photoperiod pathway. | Q2V338 |
Q73BQ6 | TRPA_BACC1 | Tryptophan synthase alpha chain | Bacillus cereus group | MGVEKIKAAFENGKKAFIPYVMGGDGGLEKLKERIRFLDEAGASIVEIGIPFSDPVADGPTIQRAGKRALDSGVTVKGIFQALIEVRKEVQIPFVLMTYLNPVLAFGKEQFIENCIEAGVDGIIVPDLPYEEQDIIAPLLRTANIALIPLVTVTSPIERIEKITSESEGFVYAVTVAGVTGVRQNFKEEIHSYLEKVKSHTHLPVVAGFGISTKEHVEEMITICDGVVVGSKVIELLENEKREEICELIQATKQKEEA | The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. | Q73BQ6 |
A8FKN8 | THIC_CAMJ8 | null | Campylobacter | MKTQMNYAKEGVFTKEMQIVAQKENLSKDFLLENIACGKIIIPANINHKSLDPNGIGFGLRTKVNVNLGVSNDCVDYSEEMKKVELAHKFDIEAIMDLSNYGKTSRFRDELVNVSKAMIGTVPVYDAVGFLEKDLKQIGAKDFLDVVYHHAKSGVDFMTIHAGINSRAAHIFKQSKRLTNIVSRGGSVLYAWMMMKDAENPFFEYYDDLLDICLKYDVTLSLGDALRPGSTHDASDGAQISELIELSLLTQRAWDVGVQVMIEGPGHMAINEIEVNMQLEKRLCKGAPFYVLGPLVTDIGAGYDHISGAIGGAVAAASGADMLCYVTPAEHLRLPNLEDVREGIVATKIAAHAGDIAKLPKERARDDEMSKARQEIDWEKMFKLAIDGEKAKKMFNERRPDDLNSCSMCGKMCAMNTMNQILKGEDVSLA | 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. | A8FKN8 |
P31495 | URE2_YEREN | Urea amidohydrolase subunit beta | Yersinia | MSTKTNSTKATSEKTDSLKTNRGTKSSAGYSDQNIPLGGCILADTPITFNENKPVTKVKVRNTGDRPIQVGSHFHFFEANRALEFDRAAAYGKRLNISSTTAIRFEPGDETEVPLIPFGGKQTLYGFNNLVDGWTGEGVVPNSERPDKLEAIRRAAERGFKSSK | Expression of the urease operon increases the likelihood of bacterial survival by contibuting to acid resistance in vitro and in vivo in BALB/c mice. Y.enterocolitica enters the body via an oral path and must survive the acidic stomach before being able to colonize the intestinal mucosa . | P31495 |
A1YEX3 | ZBT25_GORGO | Zinc finger and BTB domain-containing protein 25 | Gorilla | MDTASHSLVLLQQLNMQREFGFLCDCTVAIGDVYFKAHRAVLAAFSNYFKMIFIHQTSECIKIQPTDIQPDIFSYLLHIMYTGKGPKQIVDHSRLEEGIRFLHADYLSHIATEMNQVFSPETVQSSNLYGIQISTTQKTVVKQGLEVKEAPSSNSGNRAAVQGDHPQLQLSLAIGLDDGTADQQRACPATQALEEHQKPPVSIKQERCDPESVISQSHPSPSSEVTGPTFTENSIKIHLCHYCGERFDSRSNLRQHLHTHVSGSLPFGVPASILESNDLGEVHPLNENSEALECRRLSSFIVKENEQQPDHTNRGTTEPLQISQVSLISKDTEPVELNCNFSFSRKRKMSCTICGHKFPRKSQLLEHMYTHKGKSYRYNRCQRFGNALAQRFQPYCDSWSDVSLKSSRLSQEHLDLPCALESELTQENVDTILVE | May be involved in transcriptional regulation. | A1YEX3 |
O65555 | Y4094_ARATH | BTB/POZ domain-containing protein At4g30940 | Arabidopsis | MGLSNDRIKFNVGGRIFETTATTLANAGRDSFFGALFDENWNLSQPGDLFIDRNPDCFAVLLDLLRTGDLNIPPNIPERLLHKEAMFYGLIDHLRTAKWGPFDGNRLHLSRSVTGIAPGDGTAIRAGPDGGCCIAHGSVVHVFDWMLEEHPTINLDYQRVNDVGWIDSGNIVLSACERLGRGDGGMGLFSSSSGELRYKFQVSHDNQVKSYSAGALSFSPDSKIFTSCKGRSNEYGIGVWDQSTGKQVDFFYESPGWSLGDADKLQWLSGKNCLLVATLFPRKDNCYISLLDFREKNMVWSWSDIGFLTMAEEKRVRDAIAMEESNSICVVNEFEDLGFIDLRMDGGGSSVRWSSRSRLMKSKMPDEPCYPKLALHEGQLFSSMNDSISVFCGSDWVLTSRLKRSYGGSICDFSIGGDRLFALHSEENVFDVWETLPPPII | May act as a substrate-specific adapter of an E3 ubiquitin-protein ligase complex (CUL3-RBX1-BTB) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. | O65555 |
P29417 | XYNA_PENCH | 1,4-beta-D-xylan xylanohydrolase | Penicillium chrysogenum species complex | MIPNITQLKTAALVMLFAGQALSGPVESRQASESIDAKFKAHGKKYLGNIADQGTLNGNPKTPAIIKANFGQLSPENSMKWDATEPSQGQFSFAGSDYFVEFAETNGKLIRGHTLVWHSQLPSWVSSITDKTTLTDVMKNHITTVMKQYKGKLYAWDVVNEIFEEDGTLRDSVFSRVLGEDFVRIAFETAREADPEAKLYINDYNLDSATSAKLQGMVSHVKKWIAAGVPIDGIGSQTHLGAGAGAAASGALNALASAGTEEVAVTELDIAGATSTDYVDVVNACLDQPKCVGITVWGVADPDSWRADESPLLFDASYNPKEAYNVSQLLSRQHAFDLYLKLGNLLLSRLHSD | Hydrolyzes oat spelt and birchwood xylan randomly, yielding xylose and xylobiose as major end products. | P29417 |
Q7WML9 | UBID_BORBR | Polyprenyl p-hydroxybenzoate decarboxylase | Bordetella | MKYRDLRDFLAQLERQGELKRITAPVSTRLEMTEIADRVLRAGGPALLFENARHNDAPADMPVLANLFGTPRRVAWGMGADDVGALRETGELLASLREPEAPKGLRDALAKVSMLKAALWDMSPKTVRSAACQEIVWEGADVDLGRLPIQTCWPGDVAPLLAWGLVITRGPNARRQNLGIYRQQPLGPNKLIMRWLSHRGGALDFRDHAQAHPGKPFPIAVALGADPATILGAVTPVPDTLSEYQFAGLLRGSRTEVVKALGSDLSVPASAEIVLEGHLLPADDPRAVAAAVPEGANPPPATGYEMALEGPYGDHTGYYNEQDWFPVFTVDRITMRRNPIYHSTYTGKPPDEPAVLGVALNEVFVPLLRRQLPEIVDFYLPPEGCSYRLAVVSIRKQYAGHAKRVMFGLWSVLRQFMYTKFIVVVDEDIDPRDWTEVVWAMTTRMDPVRDTVLVENTPIDYLDFASPVSGLGGKMGLDATNKWPGETSREWGTPIHMDEAVKRRVDAMWDTLGL | Catalyzes the decarboxylation of 3-octaprenyl-4-hydroxy benzoate to 2-octaprenylphenol, an intermediate step in ubiquinone biosynthesis. | Q7WML9 |
P77269 | YPHF_ECOLI | ABC transporter periplasmic-binding protein YphF | Escherichia | MPTKMRTTRNLLLMATLLGSALFARAAEKEMTIGAIYLDTQGYYAGVRQGVQDAAKDSSVQVQLIETNAQGDISKESTFVDTLVARNVDAIILSAVSENGSSRTVRRASEAGIPVICYNTCINQKGVDKYVSAYLVGDPLEFGKKLGNAAADYFIANKIDQPKIAVINCEAFEVCVQRRKGFEEVLKSRVPGAQIVANQEGTVLDKAISVGEKLIISTPDLNAIMGESGGATLGAVKAVRNQNQAGKIAVFGSDMTTEIAQELENNQVLKAVVDISGKKMGNAVFAQTLKVINKQADGEKVIQVPIDLYTKTEDGKQWLATHVDGLP | Probably part of the binding-protein-dependent transport system YphDEF. | P77269 |
Q62AJ2 | TRUA_BURMA | tRNA-uridine isomerase I | pseudomallei group | MRIALGIQYDGAAFCGWQSQPHGKTVQDALERSLAEFAQTSLHTTVAGRTDTGVHGLGQVVHFDTDLDRADFSWVRGTNAFLPPTVAVQWAKPMPDTFHARFAAFERTYYYALYVHPVRSPMLAGRAGWVHTPLDVDAMREAAAHLVGEHDFSAFRSSECQAKSPVKHLYQIGIRPDGDFIHFRFRANAFLHHMVRNLMGCLVAVGRGRYPSSWLAEVLESRDRDCAAPTFMPEGLYLAHVGYPAEFAVPPAQLGSVPWSSVWADLDGRT | Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs. | Q62AJ2 |
Q980D9 | XERA_SACS2 | Tyrosine recombinase XerA | Saccharolobus | MKLDLGSPPESGDLYNAFINALIIAGAGNGTIKLYSTAVRDFLDFINKDPRKVTSEDLNRWISSLLNREGKVKGDEVEKKRAKSVTIRYYIIAVRRFLKWINVSVRPPIPKVRRKEVKALDEIQIQKVLNACKRTKDKLIIRLLLDTGLRANELLSVLVKDIDLENNMIRVRNTKNGEERIVFFTDETKLLLRKYIKGKKAEDKLFDLKYDTLYRKLKRLGKKVGIDLRPHILRHTFATLSLKRGINVITLQKLLGHKDIKTTQIYTHLVLDDLRNEYLKAMSSSSSKTPP | 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. Binds to the dif site. | Q980D9 |
A6WUU9 | Y022_BRUA4 | Nucleoid-associated protein Oant_0022 | Brucella | MRDMMGMMKQAKELQAKMKAMQDEIATMEASASSGGGLVTITLSGKGTLSALKIDPSLMKEEEVEILEDLIIAAHNDAKAKLEAAMAEKTQSLTAGLPIPPGFKLPF | Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection. | A6WUU9 |
Q5ABD9 | VPS27_CANAL | Vacuolar protein sorting-associated protein 27 | Candida | MSWFGRATSDAPVATISQVELDNKIVEATSESIPNGEIDLSIAFEITDLIRSKKISNKIAMRSLKKRLTLIYLNPNLLLSSLKLIDLCIKNCGFGFLIEISSKEFMDYLIDFIFKIHYNTKELTYGHGGGDVGNKIKIGEMILKYLQNWKIIFENQQQLQYVEKKYQELKNQGFEFPDNNNNSGENDDFNDQVTQLNSKFVVDSEVPPDWVDNEECMICYSPFSMLNRKHHCRACGGVFCQTHSSNNIPLVNLGIMEPVRVCDNCFAKYDKSKKHSRNTSSSGDYNHQSRSIQNDYGGTHGSRRQGNNNDDDNDEEEQIRKAIELSLKESGAGGSGSGGPNSIPSQSRPSAQPPIDREPESETGNADDDEDAEMKAAIAASLKEYETEKSRQSQYQQIQPVQSTQSTQPESDLYNISFPTFSSTSNYPQPQFTASQPPPQQQQQQQAQQQAPSQDLSQAEEEQINLFITLMNSIKNDSRKQKDIMYDTNLNELYGKVIKLRPKLNKSLRNSIEKYETFLEMNNKISTITRLYDQFLEQKLNMAYGNHHISTQFTGVPQQQQEGQFTGSQQQQQQQQPHLPAQGTGYPRYGGSDTNVAQQQQQPPISPNEFYNNLPQHTGFQNYPSYPQNQGTAPDNSYLSQQPSGASTRQKQQQPPIQTYPNQLQPSEPDFEDDDNEEPVNTPQIRVAHNRTSSGSCPLYPTNDIIPDPYSANTNKSTTPNSDDHNYVAVSLPHYPPPEDLSNELPPQQHYVRRASSSLPPNAYEDASLKYPTLENVEHDYDKKKNQEQQQSVNESDFPDVSKVSQFNNRGEEDEGRRNSGASGASSNKKFVVEPEPLIEL | 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. | Q5ABD9 |
B6DCT8 | TX406_LYCSI | Toxin-like structure LSTX-C6 | Lycosa | MKVLVLFSVLFLTLFSYSSTEAIDELDSDAEEDMLSLMANEQVRAKACTPRLHDCSHDRHSCCRGELFKDVCYCFYPEGEDKTEVCSCQQPKSHKYIEKVVDKAKTVVG | Enhances the high-affinity desensitization of human P2RX3 purinoceptors. | B6DCT8 |
P39890 | TCMI_STRGA | Tetracenomycin polyketide synthesis protein TcmI | Streptomyces | MAYRALMVLRMDPADAEHVAAAFAEHDTTELPLEIGVRRRVLFRFHDLYMHLIEADDDIMERLYQARSHPLFQEVNERVGQYLTPYAQDWEELKDSKAEVFYSWTAPDS | Catalyzing the conversion of tetracenomycin F2 to tetracenomycin F1. | P39890 |
Q9C519 | WRKY6_ARATH | WRKY DNA-binding protein 6 | Arabidopsis | MDRGWSGLTLDSSSLDLLNPNRISHKNHRRFSNPLAMSRIDEEDDQKTRISTNGSEFRFPVSLSGIRDREDEDFSSGVAGDNDREVPGEVDFFSDKKSRVCREDDEGFRVKKEEQDDRTDVNTGLNLRTTGNTKSDESMIDDGESSEMEDKRAKNELVKLQDELKKMTMDNQKLRELLTQVSNSYTSLQMHLVSLMQQQQQQNNKVIEAAEKPEETIVPRQFIDLGPTRAVGEAEDVSNSSSEDRTRSGGSSAAERRSNGKRLGREESPETESNKIQKVNSTTPTTFDQTAEATMRKARVSVRARSEAPMISDGCQWRKYGQKMAKGNPCPRAYYRCTMATGCPVRKQVQRCAEDRSILITTYEGNHNHPLPPAAVAMASTTTAAANMLLSGSMSSHDGMMNPTNLLARAVLPCSTSMATISASAPFPTVTLDLTHSPPPPNGSNPSSSAATNNNHNSLMQRPQQQQQQMTNLPPGMLPHVIGQALYNQSKFSGLQFSGGSPSTAAFSQSHAVADTITALTADPNFTAALAAVISSMINGTNHHDGEGNNKNQ | Transcription factor involved in the control of processes related to senescence and pathogen defense . Interacts specifically with the W box (5'-(T)TGAC[CT]-3'), a frequently occurring elicitor-responsive cis-acting element . Activates the transcription of the SIRK gene and represses its own expression and that of the WRKY42 genes . Modulates phosphate homeostasis and Pi translocation by regulating PHO1 expression . | Q9C519 |
C4KZE2 | THIM_EXISA | 4-methyl-5-beta-hydroxyethylthiazole kinase | unclassified Exiguobacterium | MRHEIWNEIRQQAPLIHNITNTVVANFSANGLLAIGASPVMADAIEEVAEMTFVSDALVLNIGTLGTMTEATMIRAGQAANEAGCPIVLDPVGVGATSFRRDVVERIMRHVRVSVIRGNAGEIATLIGVDWAARGVDAGDGACEPRQLALEAAKRYGCVVAVTGKEDMVSDGHVVMEVRGGTKRMTETTGTGCLLSAVVGACLAVEKNALKATVTAMSGYAYCGELASERAEGPGDFPIHFLNALHQLTQYTIPTNRIEVSTS | Catalyzes the phosphorylation of the hydroxyl group of 4-methyl-5-beta-hydroxyethylthiazole (THZ). | C4KZE2 |
Q6X784 | ZPBP2_HUMAN | ZPBP-like protein | Homo | MMRTCVLLSAVLWCLTGVQCPRFTLFNKKGFIYGKTGQPDKIYVELHQNSPVLICMDFKLSKKEIVDPTYLWIGPNEKTLTGNNRINITETGQLMVKDFLEPLSGLYTCTLSYKTVKAETQEEKTVKKRYDFMVFAYREPDYSYQMAVRFTTRSCIGRYNDVFFRVLKKILDSLISDLSCHVIEPSYKCHSVEIPEHGLIHELFIAFQVNPFAPGWKGACNGSVDCEDTTNHNILQARDRIEDFFRSQAYIFYHNFNKTLPAMHFVDHSLQVVRLDSCRPGFGKNERLHSNCASCCVVCSPATFSPDVNVTCQTCVSVLTYGAKSCPQTSNKNQQYED | Is implicated in sperm-oocyte interaction during fertilization. | Q6X784 |
P47183 | THI11_YEAST | Thiamine pyrimidine synthase | Saccharomyces | MSTDKITFLLNWQPTPYHIPIFLAQTKGYFKEQGLDIAILEPTNPSDVTELIGSGKVDMGLKAMIHTLAAKARGFPVTSVASLLDEPFTGVLYLKGSGITEDFQSLKGKKIGYVGEFGKIQIDELTKHYGMKPEDYTAVRCGMNVAKYIIEDKIDAGIGIECMQQVELEEYLAKQGRPASDAKMLRIDKLACLGCCCFCTVLYICNDEFLKKNPEKVRKFLKAIKKATDYVLADPVKAWKEYIDFKPQLNNDLSYKQYQRCYAYFSSSLYNVHRDWKKVTGYGKRLAILPPDYVSNYTNEYLSWPEPEEVSDPLEAQRLMAIHQEKCRQEGTFKRLALPA | Responsible for the formation of the pyrimidine heterocycle in the thiamine biosynthesis pathway. Catalyzes the formation of hydroxymethylpyrimidine phosphate (HMP-P) from histidine and pyridoxal phosphate (PLP). The protein uses PLP and the active site histidine to form HMP-P, generating an inactive enzyme. The enzyme can only undergo a single turnover, which suggests it is a suicide enzyme. | P47183 |
Q1QWF3 | TOLB_CHRSD | Tol-Pal system protein TolB | Chromohalobacter | MKRLNLWAASLLLMLCAGMAHAELTIEITKGSDQAIPIAIVPMANGDDLPENVSRIVSNDLERSGRFEPLPRESLISRPSSSEEVHYQDWQQLDSDYLVVGKIDNQGGEYRIQYELLNVNGQNRMLGEVVTSSRDQLRDSAHYISDQIFEEITGIRGAFSTSIAYVTASGVGDDIDYALSVADADGHNSQQILSSDEPILSPAWSPDGGKLAYVSFETGRPGIYVQNLATGQRVRLTSFEGINGAPAWSPDGRKLAMSLSKDGQPEIYVMDIASRDLRRLTQSDAIDTEPEWAPNGRSLIFTSDRSGNPQIYRYDLGSGRAERLTFTGSYNSRGRFSPDGDAIFMVTRDDSGYHVARQDLDTDRMTILTDSDWDESPSVAPNGTMVIFATQEGTRGVLGAVSADGSASFRLPSPQGDVREPAWSPFLD | Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity. | Q1QWF3 |
Q811F1 | ZBT41_MOUSE | Zinc finger and BTB domain-containing protein 41 | Mus | MKKRRKVTSNLDEKIHLGYHKDSSEENAAVECGQVTYTQAPERPTPEAAQRCQELPPSPDQRKLLSSLQYNKNLLKYLNDDRQKQPSFCDLLIIVEGKEFSAHKVVVAVGSSYFHACLSKNPSTDVVTLDHVTHSVFQHLLEFLYTSEFFVYKYEIPLVLEAAKFLDIIDAVKLLNNENVAAFQAELTEKSSPEETLNELTGRLSSSHQCKFCSRHFCYKKSLENHLAKTHRSLLLGKKHGLKMLERSFSTRRSKRNRKCPVKFEDTSDDEQESGDGSDNLHQESSEKERSDRNDSEDPGSEYNAEDEELEEEVSDEDSDTEQSDKDNDAEEEPEAGDSAGSIHEGLAPVIIQNSNKKILQCPKCDKTFDRIGKYESHTRVHTGEKPFECDICHQRYSTKSNLTVHRKKHSNEVEFHRKEHKCPYCNKLHASKKTLAKHVKRFHPENAQEFISIKKTKSESWKCDICKKSFTRRPHLEEHMILHSQDKPFKCTYCEEHFKSRFARLKHQEKFHLGPFPCDICGRQFNDTGNLKRHIECTHGGKRKWTCFICGKSVRERTTLKEHLRIHSGEKPHLCSICGQSFRHGSSYRLHLRVHHDDKRYECDECGKTFIRHDHLTKHKKIHSGEKAHQCEECGKCFGRRDHLTVHYKSVHLGEKVWQKYKATFHQCDVCKKIFKGKSSLEMHFRTHSGEKPYKCQICNQSFRIKKTLTKHLVIHSDARPFNCQHCNATFKRKDKLKYHIDHVHGIKSPDDSLSTSEEKLMSLPMEYSSDDKIFQAETKQYLDQPKVYQSEAKTMLQNVSAEVCVPVTLVPVQMPDTSSDLVPHTTTLPTSSHEMLPPQPQSTDYPRAADLAFLEKYTLTPQPANIVHPVRPEQMLDPREPSYLGTLLGLDSTAAVQNMCSSEHRS | May be involved in transcriptional regulation. | Q811F1 |
Q9LFE2 | TOZ_ARATH | Protein TORMOZ EMBRYO DEFECTIVE | Arabidopsis | MAPHSLKKNYRCSRSLKQFYGGGPFIVSSDGSFIACACGDVINIVDSTDSSVKSTIEGESDTLTALALSPDDKLLFSAGHSRQIRVWDLETLKCIRSWKGHEGPVMGMACHASGGLLATAGADRKVLVWDVDGGFCTHYFRGHKGVVSSILFHPDSNKNILISGSDDATVRVWDLNAKNTEKKCLAIMEKHFSAVTSIALSEDGLTLFSAGRDKVVNLWDLHDYSCKATVATYEVLEAVTTVSSGTPFASFVASLDQKKSKKKESDSQATYFITVGERGVVRIWKSEGSICLYEQKSSDITVSSDDEESKRGFTAAAMLPSDHGLLCVTADQQFFFYSVVENVEETELVLSKRLVGYNEEIADMKFLGDEEQFLAVATNLEEVRVYDVATMSCSYVLAGHKEVVLSLDTCVSSSGNVLIVTGSKDKTVRLWNATSKSCIGVGTGHNGDILAVAFAKKSFSFFVSGSGDRTLKVWSLDGISEDSEEPINLKTRSVVAAHDKDINSVAVARNDSLVCTGSEDRTASIWRLPDLVHVVTLKGHKRRIFSVEFSTVDQCVMTASGDKTVKIWAISDGSCLKTFEGHTSSVLRASFITDGTQFVSCGADGLLKLWNVNTSECIATYDQHEDKVWALAVGKKTEMIATGGGDAVINLWHDSTASDKEDDFRKEEEAILRGQELENAVLDAEYTKAIRLAFELCRPHKVFELFSGLCRKRDSDEQIVKALQGLEKEEFRLLFEYVREWNTKPKLCHIAQFVLYKTFNILPPTEIVQVKGIGELLEGLIPYSQRHFSRIDRFVRSSFLLDYTLGEMSVIDPETVETEYPKDEKKKEKDVIAAMEQDTDELKQETPSRKRKSQKSKGKSNKKRLIAEAQGSVIAV | Essential protein involved in the regulation of cell division planes during embryogenesis which defines cell patterning, especially longitudinal division planes of the proembryo, probably via the regulation of embryo patterning genes expression patterns. | Q9LFE2 |
Q2NWE3 | UPPP_SODGM | Undecaprenyl pyrophosphate phosphatase | Sodalis | MADMHEWVIAFILGGVEGLTEFLPVSSTGHMILVGSLLGFTDDKAKTFEVIIQLGSILAVVVVFWRRLFGLIGIHFGQVPHEGIGSGRLRLGHILLGMIPAVVLGLVFHEQIKAIFAPIYVMYALVVGGVLLLAGEWLKPKVPRAAGIDDLTYLQAFLIGCFQCLALWPGFSRSGATISGGLLVGVSRYAASEFSFILAVPMMLGATVLDLYKSLPFLSWQDLPMFAIGFVTAFVVALLAIKFFLQIIKRISFVPFAIYRFILAVVVYWILIG | Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin. | Q2NWE3 |
O75795 | UDB17_HUMAN | C19-steroid-specific UDP-glucuronosyltransferase | Homo | MSLKWMSVFLLMQLSCYFSSGSCGKVLVWPTEYSHWINMKTILEELVQRGHEVIVLTSSASILVNASKSSAIKLEVYPTSLTKNDLEDFFMKMFDRWTYSISKNTFWSYFSQLQELCWEYSDYNIKLCEDAVLNKKLMRKLQESKFDVLLADAVNPCGELLAELLNIPFLYSLRFSVGYTVEKNGGGFLFPPSYVPVVMSELSDQMIFMERIKNMIYMLYFDFWFQAYDLKKWDQFYSEVLGRPTTLFETMGKAEMWLIRTYWDFEFPRPFLPNVDFVGGLHCKPAKPLPKEMEEFVQSSGENGIVVFSLGSMISNMSEESANMIASALAQIPQKVLWRFDGKKPNTLGSNTRLYKWLPQNDLLGHPKTKAFITHGGTNGIYEAIYHGIPMVGIPLFADQHDNIAHMKAKGAALSVDIRTMSSRDLLNALKSVINDPIYKENIMKLSRIHHDQPVKPLDRAVFWIEFVMRHKGAKHLRVAAHNLTWIQYHSLDVIAFLLACVATMIFMITKCCLFCFRKLAKTGKKKKRD | UDP-glucuronosyltransferase (UGT) that catalyzes phase II biotransformation reactions in which lipophilic substrates are conjugated with glucuronic acid to increase the metabolite's water solubility, thereby facilitating excretion into either the urine or bile . Catalyzes the glucuronidation of endogenous steroid hormones such as androgens (epitestosterone, androsterone) and estrogens (estradiol, epiestradiol) . | O75795 |
Q07130 | UGPA_BOVIN | UDP-glucose pyrophosphorylase | Bos | MSRFVQDLSKAMSQDGASQFQEVIRQELELSVKKELEKILTTAPSHEFEHTKKDLDGFRKLFHRFLQEKGPSVDWGKIQRPPEDSIQPYEKIKARGLPDNVSSVLNKLVVVKLNGGLGTSMGCKGPKSLIGVRNENTFLDLTVQQIEHLNKTYDTDVPLVLMNSFNTDEDTKKILQKYNHCRVKIYTFNQSRYPRINKESLLPVAKNVSYSGENTEAWYPPGHGDIYASFYNSGLLDTFIGEGKEYIFVSNIDNLGATVDLYILNHLMNPPNGKPCEFVMEVTNKTRADVKGGTLTQYEGKLRLVEIAQVPKAHVDEFKSVSKFKIFNTNNLWISLAAVKRLQEQNAIDMEIIVNPKTLDGGLNVIQLETAVGAAIKSFENSLGINVPRSRFLPVKTTSDLLLVMSNLYSLNAGSLTMSEKREFPTVPLVKLGSSFTKVQDYLRRFESIPDMLELDHLTVSGDVTFGKNVSLKGTVIIIANHGDRIDIPPGAVLENKIVSGNLRILDH | UTP--glucose-1-phosphate uridylyltransferase catalyzing the conversion of glucose-1-phosphate into UDP-glucose, a crucial precursor for the production of glycogen. | Q07130 |
Q65RF4 | TIG_MANSM | PPIase | Basfia | MTTIETTQGLERRVSITVPAETVTTAVRDELKRVAKNARVDGFRKGKVPAQIIEKRFGASVRQDVLNDLLPRHFFDLAFKEKVNLAGRPTFAVENYEEGKDLQFTATFEVYPEIQLQGLENIKVEKPVVEITDADVDNMVEVLRKQQATWAETDNAATKDDRVTIDFVGSIDGEEFQGGKANDFVLAMGQGRMIPGFEDGILGHKAGEQFDIEVTFPEDYHVENLKAKPAKFAITVKKVEVMVLPELTADFIAKFGPNTKTVDDLRAEIRKNMQRELKNALTARVKNQVIDGLIEQNQIDVPFAAVDQEIEVLRNQAAQRFGGNGEQAAQLPRELFEEQAKRRVQVGLLLAEVISSNELKADEEKAKAMIEDIASAYEQPAEVVEYYSKNNELMNNIRNVVLEEQAIDAVLAKAQVTEKASSFDEVMNPQA | 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. | Q65RF4 |
A8AVP7 | TRMB_STRGC | tRNA(m7G46)-methyltransferase | Streptococcus | MRVRNRKGATELLEANPQYVVLNPADAKGKWQELFGNDHPIHIEVGSGKGAFITGMAKANPNINYIGIDIQKSVLSYALDKVLATDVPNIKLLWVDGSDLTNYFADGEIERLYLNFSDPWPKKRHEKRRLTYKSFLDTFKQILPEKGEVHFKTDNRGLFEYSLVSFSQYGMKLKGVWLDLHASDFEGNVLTEYEQKFSSKGQVIYRVEAVFQ | Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. | A8AVP7 |
B2AMJ3 | TVP38_PODAN | Golgi apparatus membrane protein TVP38 | Podospora anserina | MGPDEIEMVPPKTPRGLPPSETDYQPVNWKRLFLRPKYLAMWVVLVIIIILTAIITIYHDKVVEVGDIRHFDNVCGGKQEILTAHPLQHLRPFAEQVRHLPGGWLIPIVILIVISFPPLFGHEIIALLCGVVYGLWIGFGIVAAGTFLGEVGTWFAFKYLFRQKSEKLERTSLSYGALARITRDGGFWIVLIIRFSAIPTHFSTAVFSTCGVNFWIFAIATFLTLPKQIFLVYLGVLLLQDKPDDAPKNIVFGIAFVLTIVMAGYIGFKMRFVKKILIEEQEERRKALAMPTMDDTVNTGDGVLDTERSEYEALSQNDFSIAMPGPAAGNHTPLGEPSKGPSTAPSGWTTEAVNTPDSPGTPPNEYFGQQPAKGFQWV | Golgi membrane protein involved in vesicular trafficking and spindle migration. | B2AMJ3 |
Q9C0U7 | VPS5_SCHPO | Vacuolar protein sorting-associated protein vps5 | Schizosaccharomyces | MLGHNIYEEDDAFNPFADSVSPLNPPKTDQEPSAEGVEEESPNVQASPPKTHIYTSPRKRSVNLKSLPFETLTLDSAPLGPLQFSDAPSMAPENNRLEVGLNTKINPLKGSSPALNADFSANKPWISEVNSFSPSPIGATENPTIPNSEQTVDTLDAASSSAPNFTHTVSSASSQKQGSTSLTDTENQKAHPAAAPQSLTPFYIQVHDPHTVKEITKSHTVYSVSTRLEEHNQPSVSNVTVQRRYNDFAFLYQLLSNNHPGCIIPPIPEKQVVGRFDDEFIEQRRAALEVMLRKISAHPVLRDDYSFKLFLEAETFDPRMTHRTTLIESSSSPLRSGPSTSGLLDSFTSAFHTSGSSKFSEQDPILIEAKDTLDSLETQLKSVYHALLLSIDQRIQFASAIHDFGEAVGNLSLVDLEPTLSSKFDGLSQLQVELRFVQERKVAQDNLTLGTTLEEYIRYVESAKNAFTTRQKLWQTWQSSVQAVSRAKTQLEKCKKQAKSQQKSLPYLEEQYEKYRAKAADLEKEFSESTTLLKRDLSSLTTSRVDDLKASVETWLESAIESQKEIIERWESFLDQ | Plays a role in vesicular protein sorting. Required for the endosome-to-Golgi retrieval of the vacuolar protein sorting receptor pep1/vps10. Component of the membrane-associated retromer complex which is essential in endosome-to-Golgi retrograde transport. The vps29-vps26-vps35 subcomplex may be involved in cargo selection. | Q9C0U7 |
Q56839 | XECC_XANP2 | NADPH:2-ketopropyl-CoM oxidoreductase/carboxylase | Xanthobacter | MKVWNARNDHLTINQWATRIDEILEAPDGGEVIYNVDENDPREYDAIFIGGGAAGRFGSAYLRAMGGRQLIVDRWPFLGGSCPHNACVPHHLFSDCAAELMLARTFSGQYWFPDMTEKVVGIKEVVDLFRAGRNGPHGIMNFQSKEQLNLEYILNCPAKVIDNHTVEAAGKVFKAKNLILAVGAGPGTLDVPGVNAKGVFDHATLVEELDYEPGSTVVVVGGSKTAVEYGCFFNATGRRTVMLVRTEPLKLIKDNETRAYVLDRMKEQGMEIISGSNVTRIEEDANGRVQAVVAMTPNGEMRIETDFVFLGLGEQPRSAELAKILGLDLGPKGEVLVNEYLQTSVPNVYAVGDLIGGPMEMFKARKSGCYAARNVMGEKISYTPKNYPDFLHTHYEVSFLGMGEEEARAAGHEIVTIKMPPDTENGLNVALPASDRTMLYAFGKGTAHMSGFQKIVIDAKTRKVLGAHHVGYGAKDAFQYLNVLIKQGLTVDELGDMDELFLNPTHFIQLSRLRAGSKNLVSL | Involved in aliphatic epoxide carboxylation . Catalyzes the reductive cleavage of the thioether bond of 2-oxopropyl-coenzyme M (2-KPC), and the subsequent carboxylation of the ketopropyl cleavage product, yielding the products acetoacetate and free coenzyme M . | Q56839 |
Q8VZC0 | UXS1_ARATH | UDP-glucuronate decarboxylase 1 | Arabidopsis | MKQLHKQMSSKRDEETIPMSQSSPYSPKTLKHPRSLPRSLHYLFREQRLLFILVGILIGSTFFILQPSLSRLGAAESTSLITRSVSYAVTDSPPSRSTFNSGGGGGRTGRVPVGIGRKRLRIVVTGGAGFVGSHLVDKLIGRGDEVIVIDNFFTGRKENLVHLFSNPRFELIRHDVVEPILLEVDQIYHLACPASPVHYKYNPVKTIKTNVMGTLNMLGLAKRVGARFLLTSTSEVYGDPLEHPQKETYWGNVNPIGERSCYDEGKRTAETLAMDYHRGAGVEVRIARIFNTYGPRMCLDDGRVVSNFVAQTIRKHPMTVYGDGKQTRSFQYVSDLVEGLVALMENDHVGPFNLGNPGEFTMLELAEVVKEVIDPSATIEFKPNTADDPHKRKPDISKAKEQLNWEPKISLREGLPRMVSDFRNRILNEDEGKGL | Catalyzes the NAD-dependent decarboxylation of UDP-glucuronic acid to UDP-xylose. Necessary for the biosynthesis of the core tetrasaccharide in glycosaminoglycan biosynthesis. | Q8VZC0 |
A5WDP0 | THIE_PSYWF | Thiamine-phosphate pyrophosphorylase | Psychrobacter | MNKHNKSADALSLYLVTDSALCADKGLIETVLAAIDGGVTLVQLRDKHASDEALYTTACELKEAIAGRVPLVINDKVQIAHKAKLDGAHIGQGDLSVKQARNILGHDAWLGLSINTLAQLQQTHHHHLDLLDYVGLGPVFATATKQDHAEPIGLEGLSTLSKASVLPTVAIGGINHANARQVYQTGCHGIAVVSAICAADDPKQAAELLIAQR | 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). | A5WDP0 |
B1VM97 | Y3378_STRGG | Nucleoid-associated protein SGR_3378 | Streptomyces | MIPGGGQPNMQQLLQQAQKMQQDLAAAQEELARTEVDGQAGGGLVKATVTGSGELRALVIDPKAVDPEDTETLADLVVAAVQAANENAQALQQEKLGPLAQGLGGGGGIPGLPF | Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection. | B1VM97 |
A4FBM6 | TPIS_SACEN | Triose-phosphate isomerase | Saccharopolyspora | MARQPLIAGNWKMNLNHLEAIALVQKIAFSLPEKYFAKVEVAVIPPFTDIRSVQTLIDGDKLLLKHGAQDVSEHESGAYTGEVSGPMLAKLGCSYVVVGHSERREHHAETDEVVNRKVRAVLKHGMSPILCVGEPLEVREAGGHVEHSTTQLINALKGLKTEQIRQVVVAYEPVWAIGTGKVATAADAQEVCAALRTALADKYGKEIADEVRVLYGGSVKSSNIGELIGQNDVDGALVGGASLNGDEFTKLSAMAAGGPLP | Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P). | A4FBM6 |
Q03EL7 | YIDD_PEDPA | Putative membrane protein insertion efficiency factor | Pediococcus | MKQILLLIIRGYQKFISPMFPPSCRYYPTCSNYSLQAIKRFGAIKGGLMGVARILRCHPFVRGGYDPVPDNFSLKRNQKNSKPRN | Could be involved in insertion of integral membrane proteins into the membrane. | Q03EL7 |
A6TVF5 | Y4092_ALKMQ | Nucleotide-binding protein Amet_4092 | Alkaliphilus | MKFVIITGLSGAGKSQTVKSMEDFGFYCVDNLPPALIPKFAELCHQSQGVISRAALVIDIRGGMFFDDLFESLKELEHLGHQYEILFLDADDEVLMKRFKETRRSHPLNVDGSIENGITRERELLQELKDRASHIIHTTKLIPAQLKEELRNIYVEGNQMNNLMISIASFGFKHGIPLDSDLVFDVRFLPNPFYIEELKDFTGNDVKVRNYVMNSPISVEFSNKLHDIVSFLIPHYVQEGKNQLVISIGCTGGRHRSVTIAHVLYHQLKDKGHRVTLSHRDSGETRERKKES | Displays ATPase and GTPase activities. | A6TVF5 |
Q2NIZ2 | TRUB_AYWBP | tRNA-uridine isomerase | Candidatus Phytoplasma asteris | MNGFFLVNKPEKMTSHDVVFQIKKKFHFDKVGHTGTLDPLASGLLIVCVGKATKLAFLFDKLSKTYQGTFLFNKHYDTLDVKGKLLDTKNIPLNDFAIQTSFASFHQKKYWQIPPMFSAVKIKGQKMYRLARQNQVVDIPPREVFIHHFEKKSLFCHDQVDFLVHVSKGTYIRSLARDLALQLNTYGALLRLQRTAIGTHLLQNAKTIENLELNDLILDSIFFASYDELILNDYLIKLVKNGTYLDQRQIITQKPFIVKDSNKNFVAYYDILDENKYYPRYFF | Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs. | Q2NIZ2 |
Q0I3P3 | TRUB_HAES1 | tRNA-uridine isomerase | Histophilus | MSKPRKKGRDINGIFLLDKSQGMSSNDIMQKVKRLFQANKAGHTGALDPLATGMLPICLGEATKFSQYLLDADKRYQVIAKLGERTDTSDADGQVVQKREVNIDLAKILTALEQFRGEIMQVPTMFSALKYQGKALYEYARAGITIEREARPISIFELKFIDYQIPYLTLEVHCSKGTYIRTLVDDLGEVLGCGAHVTRLRRIAVADYPYNKMMTLEQLQQFSEQEDLDLLDQHLLPMESAVIRLPGLHLTKEQARAVGFGQRIKFLNEQGIQGQVRLISPENLFLGVAVIDENSIVHPQRMVVIKPE | Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs. | Q0I3P3 |
Q3Z652 | TATA_DEHM1 | Sec-independent protein translocase protein TatA | Dehalococcoides | MPKIGPMEILIIVLLVVVVFGIGKLPQVGDAIGKGIRNFRKASSGEEEKEEVETKEETKTIEKSE | 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. | Q3Z652 |
A0AKX3 | YHAM_LISW6 | 3'-5' exoribonuclease YhaM | Listeria | MEKRLLDFEVGETVELFLLIKSSIKGTASNGKPFLSLVLQDKSGELEAKLWDVKESDEVNYGVQQIVHLIGDIQNYRGRKQLKIRQIRQATPLDGVNASEFMETAPINKEEMADEITQYIFEMKNANLQRITRALLKKYQDDFYDYPAAMRHHHEFVSGLSFHVVSMLRLAKAVSDLYPTVNRDLLYAGVILHDLGKVIELSGPVSTTYTLEGNLIGHISIVVEEVSKIADELSIDDEEVVVLKHVLLSHHGKGEWGSPKPPLVREAEILHQIDLMDASINMMDKVLKHTKPGEFSERVFGLDNRSFYNPTFE | Shows a 3'-5' exoribonuclease activity. | A0AKX3 |
Q8ER61 | TMCAL_OCEIH | tRNA(Met) cytidine acetate ligase | Oceanobacillus | MDSCGLIVEYNPFHNGHQYHINQARNVSNSTCIIAIMSGNFLQRGEPAIIDKFHRTKAALHGGADIVIELPYTFAVQNSDRFANGAIQTLNKFGVSSVCFGSESGSMDPFFQAYKTIKNSSEAFDNLLKDNLSDGLSFPDAATAVYETLGLTEGNLDLSKPNNILGFSYVKAIQEYAPTIKPLTIQRKNNDFHDESINGSIASATSIRKQILQSDSMDDDVHNAIPIETLHQLQSYKDKTAIWHDFEQYFPLLRYRVLTMSIKELQNIQGVVEGLEYRIQQTASDALSFVDWMHKIKTKRYTWTRIQRIFIHILTNTKKDENYVDESPSYIRILGMNKQGQQYLNYHKKNFDVPIITSIANTTHSMLAIEERATKAYYSIIPAKLQRKMFKQELQGPIII | Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of elongator tRNA(Met), using acetate and ATP as substrates. First activates an acetate ion to form acetyladenylate (Ac-AMP) and then transfers the acetyl group to tRNA to form ac(4)C34. | Q8ER61 |
B6IAS2 | TAM_ECOSE | Trans-aconitate 2-methyltransferase | Escherichia | MSDWNPSLYLHFAAERSRPAVELLARVPLENIKYVADLGCGPGNSTALLHQRWPAARITGIDSSPAMIAEARSALPDCQFVEADIRNWQPEQALDLIFANASLQWLPDHYELFPHLVSLLNPQGVLAVQMPDNWLEPTHVLMREVAWEQNYPDRGREPLAGVHAYYDILSEAGCEVDIWRTTYYHQMPSHQAIIDWVTATGLRPWLQDLTESEQQLFLTRYHQMLEEQYPLQENEQILLAFPRLFIVARRTE | Catalyzes the S-adenosylmethionine monomethyl esterification of trans-aconitate. | B6IAS2 |
Q8Y0H3 | UVRC_RALSO | Excinuclease ABC subunit C | Ralstonia | MPPPGAQTPPAPAVDPSEAAFDAKAHIARLPSLPGVYRYFDAQGSVLYVGKARDLKKRVSSYFTKTLLSPRIAMMVAKIAHIETTVVRSEAEALLLENNLIKALAPRYNILFRDDKSYPYLKLTQHAYPRMAYYRGATDRKHQYFGPFPSAHAVRESMQILQKVFQLRTCEDTVFNNRTRPCLLHQIHRCTAPCVQAISAEDYARDVANAAGFLLGRQDEVMQTLQDKMQRHAAALEFEQAATVRDQIGALSTVLTRQSVEEVGQASDIDILAVAIKGGHACVNLAMVRGGRHLGDKAYFPTHVEEGAAIVGVDVEADVPEGAETQPEPARDPERMARDILEAFVAQHYLDQFVPPVLVVSHPIRAAGLIEALAAQAGRRVSVVRQPQGARRAWLEMAEKGAELSLARRLSEQGSQQARTRALAETIGVDLEDLAALRVECFDISHTAGEATQASCVVFHSHAMQNGEYRRYNIQDIIPGDDYAAMRQVLTRRYQKVVEQAAEDAPDMPRVVLIDGGKGQVEVARQVFEELGLDIGLLVGVAKGEGRKVGLETLVFADGRPSLELGQGSAALMLVAQIRDEAHRFAITGMRAKRAKARNTSRLEEIEGIGAKRRQRLLARFGGLRGVMAASVEELATVEGISQTLAEEIYRQLH | 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. | Q8Y0H3 |
Q10410 | YD85_SCHPO | Probable ADP-ribosylation factor-binding protein C1F3.05 | Schizosaccharomyces | MRSSQTLSKYIDKATDQFNLEPNLALNIEIADLINEKKGNTPREAALLILKRVNSANPTVSYLALHLLDICVKNCGYPFHFQIASEEFLNGFVSRFPNHPISRMNKIQSKMLEMLEEWNYMLCKNNRHREDFSRIHDIRELMAFRGYKFPAVDEDSIAVMKPNNSLRSAQELAREDLEAHKAKLQELLRRGTPMDLAEANALMKVIAGYDEENTEDYSALAAADLESIRSKALRVKQFLVNQTVSLEEGTLADAVESLKVYQTKIARILREENEDEYYVQKLLSLNDLLINVIEECSNSDLIHSGTNVVSSQPNVVESHVPPSSNDTKQESSLIDLMKLTEEPAVPSPSLPTNVPANQSLSMLSSLSNSMSSTSNGALNSPSYSQAAIPNTNSSLTSILQSDSLMISTQLTSVQKSSGFASYSVQFSNCSLTWPVSEVVFQVAVVKSLKLQLLPHTGDAIIAPGKQNAAHEIMNITNIPADASDLRIRWRVQWIIGTDHRVEQGESHLPL | May play a role in the regulation of membrane traffic through the trans-Golgi network. | Q10410 |
Q7M721 | TR120_MOUSE | Taste receptor type 2 member 120 | Mus | MNLVEWIVTIIMMTEFLLGNCANVFITIVNFIDCVKRRKISSADRIITAIAIFRIGLLWAMLTNWHSHVFTPDTDNLQMRVFGGITWAITNHFTTWLGTILSMFYLFKIANFSNSLFLHLKRKLDNVLLVIFLGSSLFLVAYLGMVNIKKIAWMSIHEGNVTTKSKLKHVTSITNMLLFSLINIVPFGISLNCVLLLIYSLSKHLKNMKFYGKGCQDQSTMVHIKALQTVVSFLLLYATYSSCVIISGWSLQNAPVFLFCVTIGSFYPAGHSCILIWGNQKLKQVFLLLLRQMRC | Putative taste receptor which may play a role in the perception of bitterness. | Q7M721 |
Q7XLD4 | ZIP3_ORYSJ | ZRT/IRT-like protein 3 | Oryza sativa | MGAKKHTLQVLPWLLLFAQHTAASACDCANTTDGADRQGAMKLKLIAIASILAAGAAGVLVPVIGRSMAALRPDGDIFFAVKAFAAGVILATGMVHILPAAFDALTSPCLKRGGGDRNPFPFAGLVSMSAAVSTMVVDSLAAGYYHRSQFRKARPVDNINVHKHAGDERAEHAQHINAHTHGGHTHSHGDIVVCGSPEEGSVAESIRHKVVSQVLELGILVHSVIIGVSLGASVRPSTIRPLVGALSFHQFFEGVGLGGCIVQANFKVRATVIMAIFFSLTAPVGIVLGIAISSSYNVHSSTAFVVEGVFNSASAGILIYMSLVDLLATDFNNPKLQINTKLQLMAYLALFLGAGLMSMLAIWA | Zinc transporter that may mediate zinc uptake from the rhizosphere. Seems specific to zinc ions and may not transport other divalent cations. | Q7XLD4 |
Q8TL02 | TRM56_METAC | tRNA ribose 2'-O-methyltransferase aTrm56 | Methanosarcina | MKRIVLLRLGHRPERDKRITTHVGLTARMLGAEGMLLASDDQGIVHSLEDVVRRWGGDFYIKNNVNFKQEIRAWKEEGGKVCHLSMYGVNLPDVTGELKKCKKLMIVVGAEKVPPEIYQLANWNVAVGSQPHSEVAAVAITMDRIAEGEPLEKEFPGAELTIVPAERGKHVIENIRE | Specifically catalyzes the AdoMet-dependent 2'-O-ribose methylation of cytidine at position 56 in tRNAs. | Q8TL02 |
Q5EA03 | TM186_BOVIN | Transmembrane protein 186 | Bos | MAAVLRAVARSPGPAAWGRPLHRLCCCGGQDPRRWVGSGPPHSKEKPLGPETEKFQMVYRFDAIKAFGYLSRLKVAQTALTVAALPPGLYCYSQGLMPFSSLCLAGGVAGFALAMLCWMSHFFRRLVGILYVNEEGTVLRVAHLTFWGRRQDTYCPVADVIPMTESPDRPQELFMRIQQYSGKQTFYLTLRYGRVLDQERFTQVFGVLDALK | As part of the MCIA complex, required for efficient assembly of the mitochondrial complex I. | Q5EA03 |
Q47HW8 | Y807_DECAR | Nucleoid-associated protein Daro_0807 | Dechloromonas | MMKGGLAGLMKQAQAMQENMKKAQEQLAQVEVEGVAGAGMVKVLMTCAHEVRRVNIDPSVMDDREMLEDLIAAALNDAVRRGEALSKDKMSGFTSGLNLPPGFKLPF | Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection. | Q47HW8 |
Q48KH5 | TAL_PSE14 | Transaldolase | Pseudomonas | MTSKLDQLKKFTTVVADTGDFGAIKSLEPEDATTNPSLLLKAASDVNNAQMLADAFSGAKGDIGLACDRFAVAIGQEILKVVPGRVSTEVDARLSFDTNALIERSERLIGLYDAAGIKRDRVLIKLAATWEGIRAAEKLEKDGIQTNLTLLFSFAQAIACAEAGVFLISPFVGRIYDWYKKSSGTDYVGAEDPGVQSVTRIYNYYKANDFKTVVMGASFRNLNQIEQLAGCDRLTISTDLLKKLAEDTGTLERKLAPGNAGEARQSLTESQFRWASNEDAMATEKLAEGIRQFARDQEKLEALLSAKA | Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway. | Q48KH5 |
O87009 | TFTD_BURCE | Two component enzyme D | Burkholderia cepacia complex | MRTGKQYLESLNDGRVVWVGNEKIDNVATHPLTRDYAERVAQFYDLHHRPDLQDVLTFVDADGVRRSRQWQDPKDAAGLRVKRKYHETILREIAAGSYGRLPDAHNYTFTTYADDPEVWEKQSIGAEGRNLTQNIHNFLKLLREKDLNCPLNFVDPQTDRSSDAAQARSPNLRIVEKTDDGIIVNGVKAVGTGIAFGDYMHIGCLYRPGIPGEQVIFAAIPTNTPGVTVFCRESTVKNDPAEHPLASQGDELDSTTVFDNVFIPWEQVFHIGNPEHAKLYPQRIFDWVHYHILIRQVLRAELIVGLAILITEHIGTSKLPTVSARVAKLVAFHLAMQAHLIASEETGFHTKGGRYKPNPLIYDFGRAHFLQNQMSVMYELLDLAGRSSLMIPSEGQWDDSQSGQWFVKLNNGPKGNPRERVQIGRVIRDLYLTDWGGRQFMFENFNGTPLFAVFAATMTRDDMSAAGTYGKFASQVCGIEFGGAEPTAYAATADYAKALDKGLAPEPAAAESATS | Oxygenase component of a two-component system that degrades 2,4,5-trichlorophenol. Uses FADH(2) supplied by TftC to oxidize 2,4,5-trichlorophenol (2,4,5-TCP) to 2,5-dichloro-p-benzoquinone, which is chemically reduced to 2,5-dichloro-p-hydroquinone (2,5-DiCHQ). Then, TftD oxidizes the latter to 5-chloro-2-hydroxy-p-benzoquinone. | O87009 |
P34787 | TBG_PLAFO | Gamma-tubulin | Plasmodium (Laverania) | MPREIITLQCGQCGNQIGVEFWKQLCNEHNIDQEGILKNNNFLNEDRKDIFFYQADDEHFIPGALLFDLEPRVINSIQTSEYRNLYNPENMFISKEGGGAGNNWGCGYSQGHKVEEEIIDMIDREVDNSDNLEGFILSHSIAGGTGSGMGSYLLELLNDNYSKKMIQTFSVFPLLTNESSDVVVQPYNSILTLKRLILSTDSVVVIDNTSLNRIFVERLKLNNPTFQQTNTIISNVMSASTTTLRYPGSMNNDMISLISSLIINPKCHFLITSYTPITIDKHISNVQKTTVLDVMKRLLHTKNIMVSAPVRRGMYISILNIIRGETDPTQVHKGLQRIRDRKLVNFIKWNPASIQVTLAKQSPHVVSQHKVCGLMMANHTSISTLFERCVTQFDRLYKRRAFLENYKKESMFSSADGQGNFEEMESSKEITQNLIDEYKSAERDDYFTNTYI | Tubulin is the major constituent of microtubules. The gamma chain is found at microtubule organizing centers (MTOC) such as the spindle poles or the centrosome, suggesting that it is involved in the minus-end nucleation of microtubule assembly. | P34787 |
P54405 | TBG_RETFI | Gamma-tubulin | Reticulomyxa | MPREIITLQVGQCGNQIGTEFWGRLIAEHGIGPDGIVKEFATEGTDRKDVFFYQADDQHYIPRALLIDLEPRVINSLQESEFKNLWNPENVYIDSQGGGAGNNWAVGYTHATEKYEHIMDMIDREDNSDSLEGFVLTHSIAGGTGSGFGSHMLEQLTDRYPKKIIQTYSVFPNDSERSSVVVHPYNSVLALKRLILNADAVVVIDNTSLHRIADERLQLDFASFKETNSIISTVMAASTTTLRYPGYMNNDLVGLIASLVPTPRAHFLMTSFTPLVIKGAQRRIQKTSVLDVMRRLLQPKNIMVSCGTKKGVYVSILDIIRGDVDPTDIHKSLQRIREKKIVNFIPWGPASIQVALSKQSPYANVPYRVSGCMMANHSNLGNLFARIIRTYDILRKRNAFLNVYKETPVFSENLDEFEDAKETITNLIEEYKAIQTSDYINWGMKQQQSQISQKESSSLANENGNGANNKPGKSAMAL | Tubulin is the major constituent of microtubules. The gamma chain is found at microtubule organizing centers (MTOC) such as the spindle poles or the centrosome, suggesting that it is involved in the minus-end nucleation of microtubule assembly. | P54405 |
Q8PN26 | UVRA_XANAC | Excinuclease ABC subunit A | Xanthomonas | MAMDFIRIRGARTHNLKNIDLDLPRDKLIVITGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLSVMEKPDLDHIEGLSPAISIEQKSTSHNPRSTVGTITEIYDYLRLLYARVGQPRCPDHGFPLEAQTVSQMVDHMLAQDQEQRYMLLAPVIRDRKGEHAQVFEQLRAQGFVRVRVDGELYEIDAVPPLALRQKHTIEAVIDRFRPREDIKQRLAESFETALKLGEGMVAVQSLDDPAAAPHLFSSKYSCPVCDYSLPELEPRLFSFNAPVGACPSCDGLGVAEFFDPDRVVVHPELSLSAGAVRGWDRRNAYYFQLIASLAKHYKFDVDAVWNTLPAKVRQAVLFGSGDEVISFTYFTDAGGRTTRKHRFEGILPNLERRYRETESPAVREELTKYVSQQPCPACNGTRLNRAARNVFVADRPLPELVVLPVNEALSFFRGLSLPGWRGEIAAKIVKEIGERLGFLVDVGLDYLTLERKADTLSGGEAQRIRLASQIGAGLVGVMYVLDEPSIGLHQRDNERLLGTLTRLRDLGNTVIVVEHDEDAIRLADHVLDIGPGAGVHGGEICAQGTLDDILKSPRSLTGQYLSGKRRIEIPKQRHKPNPKMMLHLRGATGNNLKNVDLDIPAGLLTCITGVSGSGKSTLINDTLFTLAANEINGASHTVAPHREVENLDLFDKVVDIDQSPIGRTPRSNPATYTGMFTPLRELFAQVPEARARGYSPGRFSFNVRGGRCEACQGDGMIKVEMHFLPDVYVPCDVCHGKRYNRETLEIRYKGFNISDVLQMTVEDALRLFEPVPSIARKLETLVDVGLSYIKLGQSATTLSGGEAQRVKLSKELSRRDTGRTLYILDEPTTGLHFHDIEALLGVLHKLRDEGNTVVVIEHNLDVIKTADWIVDLGPEGGHRGGTILVSGTPEEVAAHKASYTGQFLAKMLPSVKARETRPAAMANKPDARPPRKVKPEKVAKAAKSATKKTAKKAS | The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrA is an ATPase and a DNA-binding protein. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. When the presence of a lesion has been verified by UvrB, the UvrA molecules dissociate. | Q8PN26 |
O87880 | VATD_THET8 | V-ATPase subunit D | Thermus | MSQVSPTRMNLLQRRGQLRLAQKGVDLLKKKRDALVAEFFGLVREAMEARKALDQAAKEAYAALLLAQAFDGPEVVAGAALGVPPLEGVEAEVENVWGSKVPRLKATFPDGALLSPVGTPAYTLEASRAFRRYAEALIRVANTETRLKKIGEEIKKTTRRVNALEQVVIPGIRAQIRFIQQVLEQREREDTFRLKRIKGKIEAREAEEEGGRPNPQVEIGAGL | Produces ATP from ADP in the presence of a proton gradient across the membrane. | O87880 |
Q9CJL4 | UPPS_PASMU | Undecaprenyl pyrophosphate synthase | Pasteurella | MVELDPNNIPQHVAIIMDGNGRWAQQKGKMRIFGHKNGVKAVREAVSYARKVGIKVLTLYAFSSENWNRPKKEVNALMALFMQALDLEVKKLHKNNIKLNILGDVTGFSASLQNKIHQAEKLTENNTALTLNIAANYGGCWDIVQATKSLAQQVKEGKLAVDEINAQVLQQALVTKEQPQVDLLIRTSGEQRISNFLLWQIAYAELYFSDVLWPDFNEKEFNEAIIAYQQRHRRFGGAEE | Catalyzes the sequential condensation of isopentenyl diphosphate (IPP) with (2E,6E)-farnesyl diphosphate (E,E-FPP) to yield (2Z,6Z,10Z,14Z,18Z,22Z,26Z,30Z,34E,38E)-undecaprenyl diphosphate (di-trans,octa-cis-UPP). UPP is the precursor of glycosyl carrier lipid in the biosynthesis of bacterial cell wall polysaccharide components such as peptidoglycan and lipopolysaccharide. | Q9CJL4 |
C7AJA4 | TUT7_TRYBB | Mitochondrial editosome-like complex associated TUTase | Trypanosoma | MNVAKREFIRGMMAHYRASLPPPEHSVVIHELQKRVLDIGMLAVNKAHVELFGSHVSGFCTPHSDADISLTYRNFSPWLQGMERVDEQNNKRMTRFGKEASAMGMEDVRYIRARIPVVQFTDGVTGIHCDVSIGNIGGVENSKILCAIRQVFPDFYGAYIHLVKAWGKAREVIAPERSTFNSFTVTTMALMVLQELGLLPVFSKPTGEFGELTVADAEMLLQEFKLPPIYDSLHDDDEKLGEAVFFCLQRFAEYYAKYDFSAGTVSLIHPRRHRTVYERVVRRHLELLGSRKRLEWEKHIAEHKEDGPLDENDFSASMQNETTQRPSNSPYVVEDFVNYVNCGRRVQASRVRHIQQEFNRLREMLIDKESELKFDEVFRESDTVPRFQGFEGVGTRDHRVKTFRPQ | Terminal uridylyltransferase which, as part of the mitochondrial RNA editing core-like complex (RECC-like), is involved in the post-transcriptional editing of mitochondrial RNA, a process involving the addition and deletion of uridine (U) nucleotides in the pre-mRNA . Specifically, catalyzes the addition of U to single-stranded RNA with a preference for a 3'-terminal U and adds the number of Us specified by a guide RNA (gRNA) to precleaved double-stranded RNA editing substrates . Essential for insect and bloodstream developmental forms viability . | C7AJA4 |
Q57H64 | THIG_SALCH | Thiazole synthase | Salmonella | MLRIADKTFDSHLFTGTGKFASSQLMVEAIRASGSQLVTLAMKRVDLRQHNDAILAPLIEAGVTLLPNTSGAKTAEEAIFAAQLAREALGTHWLKLEIHPDARWLLPDPIETLKAAEALVKQGFVVLPYCGADPVLCKRLEEVGCAAVMPLGAPIGSNQGLETKAMLEIIIQQATVPVVVDAGIGVPSHAAQALEMGADAVLVNTAIAVADDPVMMATAFRLAVEAGLLARQAVPGNRSTYASATSPLTGFLEALA | 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. | Q57H64 |
A5VNL5 | UREF_BRUO2 | Urease accessory protein UreF | Brucella | MTIITPITNDPTTALLRLMAWLSPVFPAGSFSYSHGLERAVHDGLVVDAAGLQDWLQWLVRRGSGWNDAVLCAESWRCAMKGEDLHEIAELAEALAGSRERHMETMLQGGAFLAAARSWPCEIFDRLPPDCAYPVAVGAVAGGHGVPLAQALAAFLQAFCINLLQASIRLSVTGQSGVTAIMAALEPVLGETAARAALSSMEDLGSATFIADIMAMKHETQHSRLFRS | Required for maturation of urease via the functional incorporation of the urease nickel metallocenter. | A5VNL5 |
Q61241 | TSSK1_MOUSE | Serine/threonine-protein kinase 22A | Mus | MDDAAVLKRRGYIMGINLGEGSYAKVKSAYSERLKFNVAVKIIDRKKAPSDFLEKFLPREIEILAMLNHRSIVKTYEIFETSDGKVYIVMELGVQGDLLEFIKTRGALQEDDARKKFHQLSSAIKYCHDLDVVHRDLKCENLLLDKDFNIKLSDFGFSKRCLRDDSGRLILSKTFCGSAAYAAPEVLQGIPYQPKVYDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRVNFPRSKHLTGECKDLIYRMLQPDVNRRLHIDEILNHCWVQPKARGLSSGAINKEGESSRATEPSWIPEPGADKKSATKLEPREEARSEARSESKPQEDTLQVVRQSENVGLSSELNRDTEEGHPQQPSETHT | Testis-specific serine/threonine-protein kinase required during spermatid development . Phosphorylates 'Ser-281' 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 . | Q61241 |
Q7LJF8 | TRI5_FUSCO | Sesquiterpene cyclase | Fusarium | MENFPTEYFLNTSVRLLEYIRYRDSNYTREERIENLHYAYNKAAHHFAQPRQQKMLKVDPKRLQASLQTIVGMVVYSWAKVSKECMADLSIHYTYTLVLDDSSDDPHPAMVNYFDDLQAGREQAHPWWALVNEHFPNVLRHFGPFCSLNLIRSTMDFFEGCWIEQYNFGGFPGSDDYPQFLRRMNGLGHCVGASLWPKDLFDERKNFLEITTAVAQMENWMVWVNDLMSFYKEFDDERDQISLVKNFVTCHEITLDEALEKLTQETLHSSKQMVAVFADKDPQVMDTIECFMHGYVTWHLCDARYRLHEIYEKVKDQDTEDAKKFCKFFEQAANVGAVAASEWAYPPVAQLASVRAKSDVKEAQKPFLSSIELVE | TS is a member of the terpene cyclase group of enzymes. It catalyzes the isomerization and cyclization of farnesyl pyro-phosphate to form trichodiene, the first cyclic intermediate in the biosynthetic pathway for trichothecenes. It serves to branch trichothecene biosynthesis from the isoprenoid pathway. | Q7LJF8 |
Q2NT68 | YCIB_SODGM | Inner membrane-spanning protein YciB | Sodalis | MKQFLDFLPLVVFFIVYNLYDIYYASGALIVASALVLVYTWLRYRKVEKVALITFVLVAIFGSLTLYYHNAEFIKWKVTVIYSLFAAALLISQFVFGKPLIQRMLDKEIHLPARVWNNLNIAWALFFLACGAANIYIAFWLPQSVWVNFKVFGLTGLTLVFTLLSGIYIYRYNNTH | Plays a role in cell envelope biogenesis, maintenance of cell envelope integrity and membrane homeostasis. | Q2NT68 |
Q9ZRR5 | TBA3_HORVU | Tubulin alpha-3 chain | Hordeum | MRECISIHIGQAGIQVGNACWELYCLEHGIQPDGQMPGDKTVGGGDDAFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLISGKEDAANNFARGHYTIGKEIVDLCLDRIRKLADNCTGLQGFLVFNAVGGGTGSGLGSLLLERLSVDYGKKSKLGFTVYPSPQVSTSVVEPYNSVLSTHSLLEHTDVAVLLDNEAIYDICRRSLDIERPTYTNLNRLVSQVISSLTASLRFDGALNVDVNEFQTNLVPYPRIHFMLSSYAPVISAEKAYHEQLSVAEITNSAFEPSSMMAKCDPRHGKYMACCLMYRGDVVPKDVNAAVATIKTKRTIQFVDWCPTGFKCGINYQPPSVVPGGDLAKVQRAVCMISNSTSVVEVFSRIDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDLAALEKDYEEVGAEFDEGEDGDEGDEY | 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. | Q9ZRR5 |
Q8FFY0 | THIM_ECOL6 | 4-methyl-5-beta-hydroxyethylthiazole kinase | Escherichia | MQVDLLSSAQSAHALHLFHQHSPLVHCMTNDVVQTFTANTLLALGASPAMVIETEEASQFAAIASALLINVGTLTQPRAQAMSAAVEQATRSQTPWTLDPVAVGALDYRRRFCVELLSHKPTAIRGNASEIMALAGVANGGRGVDTTDAAANAIPAAQTLARETGAIVVVTGEVDYVTDGHRIIGIHGGDPLMTKVVGTGCALSAVVAACCALPGDTLENIASACHWMKQAGERAVARSEGPGSFVPHFLDALWQLAQEVQA | Catalyzes the phosphorylation of the hydroxyl group of 4-methyl-5-beta-hydroxyethylthiazole (THZ). | Q8FFY0 |
Q58DA8 | ZDHC9_BOVIN | Zinc finger DHHC domain-containing protein 9 | Bos | MSVMVVRKKVTRKWEKLPGRNTFCCDGRVMMARQKGIFYLTLFLILGTCTLFFAFECRYLAVQLSPAIPVFAAMLFLFSMATLLRTSFSDPGVIPRALPDEAAFIEMEIEATNGAVPQGQRPPPRIKNFQINNQIVKLKYCYTCKIFRPPRASHCSICDNCVERFDHHCPWVGNCVGKRNYRYFYLFILSLSLLTIYVFAFNIVYVALKSLKIGFLETLKETPGTVLEVLICFFTLWSVVGLTGFHTFLVALNQTTNEDIKGSWTGKNRVQNPYSHGNIVKNCCEVLCGPLPPSVLDRRGILPLEESGSRPPSTQEASTSLLPQGPAPIDHLSNEMPEDTSTPEEMPPPEPPEPPQEVTEAEK | Palmitoyltransferase that could catalyze the addition of palmitate onto various protein substrates. The ZDHHC9-GOLGA7 complex is a palmitoyltransferase specific for HRAS and NRAS. May have a palmitoyltransferase activity toward the beta-2 adrenergic receptor/ADRB2 and therefore regulate G protein-coupled receptor signaling. | Q58DA8 |
P58262 | THIG_CLOAB | Thiazole synthase | Clostridium | MDELEIGGVKLDSRLFVGTGKLASNEVIPKIMEKSNSKVITVALRRVDITSKQDNILNFIDKDLILLPNTSGARNAEEAIRLARIAKAAGCGNWIKIEVISDNKYLLPDNYETIKATEALVKEGFIVLPYVNPDLMDARRLVNVGAAAVMPLGAPIGSNRGLRTKEMLKILIEEINEVPVVVDAGIGKPSDAAMAMEMGADAVLVNTAIATADNPVLMAEAFSLAVKAGRMAYVAKIGEEKEYASASSPLTGFLR | 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. | P58262 |
B5ED52 | TAL_CITBB | Probable transaldolase | Citrifermentans | MKFFIDTADVKEIREANELGLVDGVTTNPSLIAKSGRRFEEVIKEITGIVDGPISAEVISLEHDGMIAEATELAKIHPNIVIKLPMTPEGLKATKTLYKRGIKTNVTLIFTPMQALLAAKAGATYVSPFVGRLDDISQNGMGIIQEIRTIFDNYGMDAEIIVASIRNPIHVLDSALIGADVCTIPYSVMLQLAKHPLTDAGIKKFLEDWEKVPK | Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway. | B5ED52 |
Q8NZW1 | Y1709_STRP8 | DegV domain-containing protein spyM18_1709 | Streptococcus | MTWKIVTDSGCDLRSLTRQSKELRFERVPLTLQIGTEIFRDDDGLDIDNMMTTMYQSSKATTSSCPSPEAFLQAYRGSDNVIVMTITGTLSGSHNSARLAKNELLEENPNVNIHLIDSLSAGGEMDLLVLELERLINLGLSFEEVVKQITAYQQKTRLIFVLAKVDNLVKNGRLSKLVGKVIGLLNIRMVGKASNKGTLELLQKARGQKKAVSALIEEIQKEGYVGGKVYIAHAQNPKICEQISEKIKSLYPDAVIQTGRTSGLCSFYAEDGGLLMGYEI | May bind long-chain fatty acids, such as palmitate, and may play a role in lipid transport or fatty acid metabolism. | Q8NZW1 |
F4K4L7 | TAF4B_ARATH | TBP-associated factor 4b | Arabidopsis | MDPSIFKLLEEDEDESMHSGADVDAFQAALNRDIEGSMTTSIPHVTNPGNNHSSRQQFSTWKNGIGDSNINVQTQHSLESTQMKEQEGSTLENQHQHDLKRANEPHLQHNQPQDLHRAGQLWENPSQVPQSTGLPISEKNPTGNESDRSHNQESESQYMKLQKMSSQQARGVEPPVNPMNVNPINRNPKQVPFAALLPTLMNQLDKDRALQLRTLYARLKKNEIPKEGFTRHMKDIVGDQMLRMAVSKLQQVNYNQGKIGIQAPSTEINNQKSQSDPRAVHLNQLPSSASGTLGSSVPVQGLTKHPQHQMQHPPSSFPMYTTSGSFHSFPGPNTNASGSTLRPHLHDSHMRHVAHNQPMGSTGLGGPPQSTTNMMTMPKFERPSSVNDPSRVQGGATSHFQNSSSLPLNSAPGQGSSVSHVKQESVDQSFEKNNAASMTSNEDLEKESSRMVLSTPNNMAPASSVSPSMTTQLDASTTMNSRGPLGTSQGGANARMPPKKPSVGQKKPLETLGSSPPPPSKKQKVAGNSMDQSIEQLNDVTAVSGVNLREEEEQLFSGAKEDGRVSEASRRVVHEEEERLILQKNPLQRKLAEIMAKAGLKQISNDVERCLSLCVEERMRGLLSHIIRLSKQRVDAEKSRHRTFITSDIRLQINEMNQKVKEEWEKKQAEAEKLKKPSESEEGDGGVDSEKDKEDNRSKGVKGNKEDDDKMRTTAANVAARAAVGGDDAFLKWQLMAEARQKSVSEAGKDGNQKTTSGGGKNSKDRQDGGRRFSGTESSCGVGIVYRVSSSRFWFAMMSFGFLFAGGRRVGKNQGSSLQPKVVRTISVKDVVAVLEREPQMSKSTLMYRLIQ | TAFs are components of the transcription factor IID (TFIID) complex that is essential for mediating regulation of RNA polymerase transcription. | F4K4L7 |
P76524 | YPDF_ECOLI | Aminopeptidase YpdF | Escherichia | MTLLASLRDWLKAQQLDAVLLSSRQNKQPHLGISTGSGYVVISRESAHILVDSRYYVEVEARAQGYQLHLLDATNTLTTIVNQIIADEQLQTLGFEGQQVSWETAHRWQSELNAKLVSATPDVLRQIKTPEEVEKIRLACGIADRGAEHIRRFIQAGMSEREIAAELEWFMRQQGAEKASFDTIVASGWRGALPHGKASDKIVAAGEFVTLDFGALYQGYCSDMTRTLLVNGEGVSAESHLLFNVYQIVLQAQLAAISAIRPGVRCQQVDDAARRVITEAGYGDYFGHNTGHAIGIEVHEDPRFSPRDTTTLQPGMLLTVEPGIYLPGQGGVRIEDVVLVTPQGAEVLYAMPKTVLLTGEA | Hydrolyzes the N-terminal methionine when the next amino acid is alanine, proline or serine. The substrate preference for methionyl aminopeptidase activity is Pro > Ala > Ser. Also able to hydrolyze the Xaa-Pro peptide bond when the first amino acid is alanine, asparagine or methionine. | P76524 |
A9GC83 | UPPP_SORC5 | Undecaprenyl pyrophosphate phosphatase | Sorangium | MFWFDAVLLGVLEGLTEFLPVSSTGHLILLGAWLGHQSEAAKTLDIVIQLGAVLAVVVYFRERLSTTVRGMVRRDPDSLRLALALAFAFLPAAVVGLLFHKAIKAHLFGPGPVAAALIVGGFLMIGVESLRRRRPDQGAPRVEDVTFQRALAIGFAQCFSLWPGASRSMTTIVGGQLSGLSTAAAAEFSFLLAIPTLGAATVFDLVKNGRALLDAPGGIVALVVGLAVSFAVALLVIAVFLRYLKRYGLAPFGWYRIALGALVLWLWIASRSAPAEAGAASASPAPRGDVAAAVDGLARTGDHPSRP | Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin. | A9GC83 |
A8FMV1 | UVRC_CAMJ8 | Excinuclease ABC subunit C | Campylobacter | MTKENLENELKTLPNSAGVYQYFNQEGKLLYVGKAKNLKNRVKSYFAFTPNLHANPRNSLRIQKMIEETVHLEFITTNSEADALILENSFIKQLHPKYNILLRDDKTYPYIYVDFEEEFPRFEITRKLVKKSKIKYFGPFFKGARELLDALYLYYPLKQKASCKSPCIFYQISRCLAPCDKRISREKYLEILDEAMHALLNPSILIKNLEKQMLVLAQNENYEEAAKVRDQIVTIKDLEVKVEIDIAKLEDFEVFALAFENSMLSTLRFVVQNGKIISVNSKITPIKNDIQWDKNEIYKQLILENFSMDIPLLANVIYVYEEFEDRMLLEEILSQRFDKKISIKIPKIGEKRRICDLAFQNALLNIEKEQKNHDFTIQKELKSYFELENLPNDIEIFDNSHLQGVANVGAMVTYSANSWDKSKYRKFHLKHKNDYDQMREVLMRRALDFDKIPPPDLWLIDGGKALLDLAKEIIVSSGANVDILAISKEKIDAKAHRAKGGARDKIHSLKGEFSLSINDKKLQFLQKLRDEAHRFAISFHQNTKKKQDLNSSKLVNLGLSSGVIQKLLAYYGNFESIYKADFKDLAMLVGKKVAQKIKEN | 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. | A8FMV1 |
A1WIU9 | YCIB_VEREI | Inner membrane-spanning protein YciB | Verminephrobacter | MKILLDFLPIVLFFGSYKLYGIYVATAVLMAATALQMALIYAIDRRLQTMHKVTLALILSFGALTLALQDDRFIKWKPTVLYGAMSVALALTLWALKKNFLKLLLGSQLALPDMVWLRLNWAWIAYCAFMSAINAYVVLHWSTDAWVDFKLWGYVFPLVFLIGQGLYIAPHLKNQGRT | Plays a role in cell envelope biogenesis, maintenance of cell envelope integrity and membrane homeostasis. | A1WIU9 |
Q32PZ9 | YJU2B_RAT | Coiled-coil domain-containing protein 130 | Rattus | MGERKGQNKYYPPDFNPEKHGSLNRYHNSHPLRERARKLSQGILIIRFEMPYNIWCDGCKNHIGMGVRYNAEKKKVGNYYTTPIYRFRMKCHLCVNYIEMQTDPANCDYVIVSGASRKEERWDMEDNEQVLTTEHEKKEKLETDAMFRLEHGEADRSTLKKALPTLSHIQEAQNAWKDDFALNSMLRRHFREKKKAMQEEEEKDQALQAKANLAIPLVPESEDDRRLAALLRLHTLDSYEDKQRMKRTEIIHRSWFPSAQGPSTSSSKASTVLKKLCRGRRPPTGSAGAPGDLGIVRRKSREAPESPQCTADNSLSEEPRGPPGTTPDSKTLQGTAEAPRTSKTLESKRNCSDQALPLGSSQEDLLHPNTPNASLVADYSDSESE | May be involved in mRNA splicing. | Q32PZ9 |
P05620 | VSP1_PROFL | Snake venom serine protease 1 | Protobothrops | MVLIRVLANLLILQLSYAQKSSELVIGGDECNINEHPFLVALYDAWSGRFLCGGTLINPEWVLTAAHCDSKNFKMKLGAHSKKVLNEDEQIRNPKEKFICPNKKNDEVLDKDIMLIKLDSPVSYSEHIAPLSLPSSPPSVGSVCRIMGWGSITPVEETFPDVPHCANINLLDDVECKPGYPELLPEYRTLCAGVLQGGIDTCGFDSGTPLICNGQFQGIVSYGGHPCGQSRKPGIYTKVFDYNAWIQSIIAGNTAATCLP | Thrombin-like snake venom serine protease that clots fibrinogen (FGA) by releasing fibrinopeptide A. According to PubMed:8585090, only cleaves rabbit fibrinogen, whereas no specificity is described in PubMed:3910643 (tests done on bovine fibrinogen). Also acts as a C3 convertase that independently cleaves human C3 and kick-starts the complement cascade. Also increases urokinase-type plasminogen activator (PLAU) and plasminogen activator inhibitor (SERPINE1) in cultured bovine pulmonary artery endothelial cells. Dose-dependently inhibits collagen-induced platelet aggregation. | P05620 |
B1IND8 | TIG_CLOBK | PPIase | Clostridium | MNVKVENIEKNVVKLEITVDSEKFNEAVKKSFKKNAKRFNVPGFRKGKAPLNIIKKYYGEGVLFEDAINFCCEDTYPKAIEENNIKPVDYPQIDVVQIGEGKDFIYTAEVTTVPEVKLGEYKGVEVKKVSYEVEDEAVENELKSMQEKNARVSLKEEGEIEKGNIAIIDFKGYVDGKAFEGGEAKDYEIEIGSGTFIGDFEDQLVGLKKDESKEVNVSFPEEYGREDLNGKPATFEVTIKDIKVKELPALDDEFAKEVSEFDTLEELKSDIKDRMKKELSEKAKAEYEEAVVEAVGANAEIEIPKVMIEKEIENMVRDLEMRLKYQGLDLKSYYEFTNSSEEKVKEYMRETAEKRVKTDLIMQEIAKVEDIKATEEELKEKAMEVAKQYGQKDVEKTAELIANAQKAYLEIDIVNGKVLDLLVENSKEIA | 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. | B1IND8 |
P47061 | VPS53_YEAST | Vacuolar protein sorting-associated protein 53 | Saccharomyces | MLEGTVDYDPLEDITNILFSKESLNNIDELISITRSYKKQLQEDILKEENELKEHPKNSAEIEASLRKVFQDFKETQDVSASTELTISNLTEGISYLDIAKKNLTHSLTLFQNLKILTDSYIQCNELLSQGSFKKMVSPYKIMCSLAENTFISYKSLDEINYLLSSISRLKGDTLSKIKQNYNALFSGGNISEHDTALTMELREGACELLDCDTSTRAQMIDWCLDKLLFEMKEIFRVDDEAGSLENLSRRYIYFKKILNNFNSKFADYFLKDWEMAVRLTTTFYHITHKDLQTLLKREFKDKNPSIDLFMTALQSTLDFEKYIDVRFSKKIKEPKLSSCFEPYLTLWVSHQNQMMEKKFLSYMSEPKYPSNETESLVLPSSADLFRTYRSVLTQTLELIDNNANDSILTSLANFFSRWLQTYSQKILLPLLLPDNIEVQDKLEAAKYTVLLINTADYCATTIDQLEDKLSEFSGNREKLANSFTKTKNIYDDLLAKGTSFLLNRVIPLDLNFVWREFINNDWSNAAIEDYSRYMVTLKSVLKMPALTDASIKQQQEQPSTLAFILSQFNRDVYKWNFLDKVIDIITTNFVSNTIRLLQPVPPFSLAGSKRKFETRTVVNIGEQLLLDLELLKEIFHTLPESVSNDSDLRENTSYKRVKRHADNNIDQLLKFIKLLMAPLDSADDYYETYSKLTNNNPDSAVWSFVLALKGIPWDLALWKKLWSAYNLETDDTDEGSRPDSNRDLFIFKWDKVLLGQFENNLARMQDPNWSKFVRQDLKISPPVMKRIVSTPQIQQQKEEQKKQSLSVKDFVSHSRFFNRGT | Involved in retrograde transport from early and late endosomes to late Golgi by linking the vesicle through the t-SNARE TGL1 to the Golgi, leading to the membrane fusion between late Golgi and endosomal vesicles. | P47061 |
Q8T380 | TPM_LEPSA | Tropomyosin Lep s 1 | Lepisma | MEAIKKKMQAMKLEKDNAMDKADALEAQARDANRKADKILEEVQDLKKKPSQVETDFTTTKENLATANKNLEDKEKTLTNTESEVASLNRKVQMIEENLERSEERLGTALTKLGEASHAADEASRMCKVLENRSQQDEERMDQLTNQLKEARMLAEDADGKSDEVSRKMAQVEDDLEVAEDRVKSGDSKIMELEEELKVVGNSLKSLEVSEEKANQRVEEYKRQIKTLTVKLKEAEARAEYAEKYVKKLQKEVDRLEDELGINKDRYRALADEMDQTFAELSGY | Tropomyosin, in association with the troponin complex, plays a central role in the calcium dependent regulation of muscle contraction. | Q8T380 |
Q0Z7W6 | TMX1_BOVIN | Thioredoxin domain-containing protein 1 | Bos | MAPSGSLRIPVAVLLLLLWGAPWAHGKRSDVRIITDENWRELLEGEWMIEFYAPWCPACQNLQPEWESFAEWGEDLEVNVAKVDVTEQPGLSGRFIITALPTIYHCKDGEFRRYQGPRTKKDFINFISDKEWKSIEPVSSWFGPGSILMSSMSALFQLSMWIRTCHNYFIEDLGLPIWGSYTVFALATLLSGLLLGLFMIFVADCLCPSKRRRPQPYPSRKLLPESSQPLKKVEEEQEADVEDVSEEESESKEGANKDFAQNAVRQRSVGPSLATDKS | May participate in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyze dithiol-disulfide exchange reactions. | Q0Z7W6 |
C0H9B6 | ZPLD1_SALSA | Zona pellucida-like domain-containing protein 1, secreted form | Salmo | MEQICLIILLISKALSVGAQFNGYNCDANFHSRFPAERDISVYCGVQTITLKINFCPVLFSGYTDTDLALNGRHGDAHCRGFINNNTFPTVVLFSISLATLETCGNALVVSTAQGPNAYGNLSLVQIGNISGYIDTPDPPTIISYLPGLLYKFSCSYPLEYLVNNTQLASSAAAISVKDSNGTFVSTLSLLLYNDSSYVQQLSIPMAGLTLKTRVFAAVKATNLDRRWNVLMDYCYTTASGNPNDELRYDLFFSCDKDPQTTVFENGKSQMGRFAFEVFRFVKHKNQKMSTVFLHCVTKLCRADDCPMLMPICGSRKKRDVSERTESNSASGNAIITAGPIITRSDDTPMNNSQLAQLNSPVFRMNTVTSALISGIIILGVMSLCFFILSLTLLKGKRAPPTILSGARNPAFN | Glycoprotein which is a component of the gelatinous extracellular matrix in the cupulae of the vestibular organ. | C0H9B6 |
A8AX17 | UVRB_STRGC | Excinuclease ABC subunit B | Streptococcus | MINRITDNKFELISKYEPSGDQPQAIEQLVDNIEGGEKAQILMGATGTGKTYTMSQVIAQVNKPTLVIAHNKTLAGQLYGEFKEFFPNNAVEYFVSYYDYYQPEAYVPSSDTYIEKDSSVNDEIDKLRHSATSALLERNDVIVVASVSCIYGLGSPKEYSDSVVSLRPGLEISRDKLLNDLVDIQFERNDIDFQRGKFRVRGDVVEIFPASRDEHAFRVEFFGDEIDRIREVEALTGRVLGEVDHLAIFPATHFVTNEDHMEVAIAKIQAELEEQLAKFEKEGKLLEAQRLKQRTEYDIEMLREMGYTNGVENYSRHMDGRSEGEPPYTLLDFFPDDFLIMIDESHMTMGQIRGMYNGDRSRKEMLVNYGFRLPSALDNRPLRREEFESHVHQIVYVSATPGDYENEQTDTVIEQIIRPTGLLDPEVEVRPTMGQIDDLLGEINARVEKNERTFITTLTKKMAEDLTDYFKEMGVKVKYMHSDIKTLERTEIIRDLRLGVFDVLVGINLLREGIDVPEVSLVAILDADKEGFLRNERGLIQTIGRAARNSEGHVIMYADTMTQSMQRAIDETARRRAIQMAYNEEHGIVPQTIKKEIRDLISVTKTALPDKEETVEIESLNKQERKDMIKKLEGQMQEAAGLLDFELAAQIRDMILEIKAMD | 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. | A8AX17 |
P40009 | YND1_YEAST | Yeast nucleoside diphosphatase 1 | Saccharomyces | MLIENTNDRFGIVIDAGSSGSRIHVFKWQDTESLLHATNQDSQSILQSVPHIHQEKDWTFKLNPGLSSFEKKPQDAYKSHIKPLLDFAKNIIPESHWSSCPVFIQATAGMRLLPQDIQSSILDGLCQGLKHPAEFLVEDCSAQIQVIDGETEGLYGWLGLNYLYGHFNDYNPEVSDHFTFGFMDMGGASTQIAFAPHDSGEIARHRDDIATIFLRSVNGDLQKWDVFVSTWLGFGANQARRRYLAQLINTLPENTNDYENDDFSTRNLNDPCMPRGSSTDFEFKDTIFHIAGSGNYEQCTKSIYPLLLKNMPCDDEPCLFNGVHAPRIDFANDKFIGTSEYWYTANDVFKLGGEYNFDKFSKSLREFCNSNWTQILANSDKGVYNSIPENFLKDACFKGNWVLNILHEGFDMPRIDVDAENVNDRPLFQSVEKVEERELSWTLGRILLYASGSILAGNDDFMVGIAPSERRTKLTGKKFIPGKLLESDQLRKQSSSLSNKGFLMWFAIICCIFYLIFHRSHIIRRRFSGLYNITKDFKTGIRRRLKFLRRSDPFSRLEEGELGTDVDGFKDVYRMKSSSMFDLGKSSATMQREHEPQRTASQSANLAPSNLRPAFSMADFSKFKDSRLYD | Catalyzes the hydrolysis of phosphoanhydride bonds of nucleoside tri- and di-phosphates. Has equal high activity toward ADP/ATP, GDP/GTP, and UDP/UTP and approximately 50% less toward CDP/CTP and thiamine pyrophosphate. Has no activity toward GMP. Required for Golgi glycosylation and cell wall integrity. Together with CDC55, required for adenovirus E4orf4 (early region 4 open reading frame 4) induced toxicity, the apyrase activity is not required for this function. Plays a role in sphingolipid synthesis. | P40009 |
Q05939 | TOXS_VIBPA | Transmembrane regulatory protein ToxS | Vibrio | MKIKVASAVLAVSILFSGWLYWGSDLKVEQVLTSNEWQSTMVTVITDNLPDDTVGPLRRVNVESNVKYLPNGDYIRVANIKLFAQGSTAESTINISEKGRWEVSDNYLLVSPSEFKDISSSQSKDFSEAQLRLITQIFKLDAEQSRRIDVVNEKTLLLTSLNHGSTVLFRN | Interacts with ToxR and stimulates its activity. | Q05939 |
Q58952 | TYW2_METJA | tRNA wyosine derivatives biosynthesis protein Taw2 | Methanocaldococcus | MGIKYQKIGDVVIVKKELSEDEIREIVKRTKCKAILLYTTQITGEFRTPHVKILYGKETETIHKEYGCLFKLDVAKIMWSQGNIEERKRMAFISNENEVVVDMFAGIGYFTIPLAKYSKPKLVYAIEKNPTAYHYLCENIKLNKLNNVIPILADNRDVELKDVADRVIMGYVHKTHKFLDKTFEFLKDRGVIHYHETVAEKIMYERPIERLKFYAEKNGYKLIDYEVRKIKKYAPGVWHVVVDAKFERI | S-adenosyl-L-methionine-dependent transferase that acts as a component of the wyosine derivatives biosynthesis pathway. Catalyzes the transfer of the alpha-amino-alpha-carboxypropyl (acp) group from S-adenosyl-L-methionine to 4-demethylwyosine (imG-14), forming 7-aminocarboxypropyl-demethylwyosine (wybutosine-86) at position 37 of tRNA(Phe). | Q58952 |
P39889 | TCMH_STRGA | Tetracenomycin polyketide synthesis hydroxylase TcmH | Streptomyces | MATISPSPDLFTLVNVFGVAPEKQRELRDHLVQVTEDLIRHMPGFVSATFHLSRDGEQVVNYAQWRSEADFRAMHADPRLQPHFDYCRSVSRPKPIFCEVTHSFGATSPEGA | Oxygenase required for conversion of tetracenomycin F1 to tetracenomycin D3. | P39889 |
B3GXW4 | YCIB_ACTP7 | Inner membrane-spanning protein YciB | Actinobacillus | MKQLLEFIPLILFFTVYKLYGVQQAAITLVIATVIQLIVLKVLYKKIEKSQWIMGIFVVFFGILTAYFNDLNFLKWKVTIINGLFAAVLLVSQFVFKKPIIQMLLGKELKLPTNVWNRLNLGWAGFFIICMLLNIVISYYFSDDVWATFKTFGFTGLSLIAAIATGVYLYPHLKNVENTNEQA | Plays a role in cell envelope biogenesis, maintenance of cell envelope integrity and membrane homeostasis. | B3GXW4 |
Q88WR8 | YIDC1_LACPL | Membrane protein YidC 1 | Lactiplantibacillus | MKSKKGLTLTITLGTLALFLSGCVQTTKAGKPYGFVYEYLAKPGQNVMEWLSQLFGNNYGWAIIGLTVIVRLVLLPMMINQQRKSTYQQEKMSAVRPQMEKIQARQKAATTQEEKAAISNELMQLYRDNGISMTGGIGCLPLLIQLPIFSALYYAIRYSPELSKATFMGISLGKSSLILAILAFLSYLAQGYLSMIGLPEEQKKTMRLMLIMSPVMILFVSMSAPAGLGLYFFVGGLFACLQTLIINFFRPRIRREVEAELKKHPIKTPTPTQPKPINATESKPSHPRPQNNAGRGRNAGKQQRHHK | 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. | Q88WR8 |
A1WFS6 | TATA_VEREI | Sec-independent protein translocase protein TatA | Verminephrobacter | MGTFSIWHWLIVLLVVVVVFGTKKLRNIGTDLGSAVKGFKDGMKDAATDTAPAGQVANQSTADQTIDVQTKPKG | 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. | A1WFS6 |
P0A8I3 | YAAA_ECOLI | UPF0246 protein YaaA | Escherichia | MLILISPAKTLDYQSPLTTTRYTLPELLDNSQQLIHEARKLTPPQISTLMRISDKLAGINAARFHDWQPDFTPANARQAILAFKGDVYTGLQAETFSEDDFDFAQQHLRMLSGLYGVLRPLDLMQPYRLEMGIRLENARGKDLYQFWGDIITNKLNEALAAQGDNVVINLASDEYFKSVKPKKLNAEIIKPVFLDEKNGKFKIISFYAKKARGLMSRFIIENRLTKPEQLTGFNSEGYFFDEDSSSNGELVFKRYEQR | Involved in the cellular response to hydrogen peroxide (H(2)O(2)) stress. During H(2)O(2) stress, prevents oxidative damage to both DNA and proteins by diminishing the amount of unincorporated iron within the cell. | P0A8I3 |
Q6GB72 | UVRB_STAAS | Excinuclease ABC subunit B | Staphylococcus | MTMVEHYPFKIHSDFEPQGDQPQAIEEIVEGIKAGKRHQTLLGATGTGKTFTMSNVIKEVGKPTLIIAHNKTLAGQLYSEFKEFFPENRVEYFVSYYDYYQPEAYVPSTDTFIEKDASINDEIDQLRHSATSALFERDDVIIIASVSCIYGLGNPEEYKDLVVSVRVGMEMDRSELLRKLVDVQYTRNDIDFQRGTFRVRGDVVEIFPASKEELCIRVEFFGDEIDRIREVNYLTGEVLKEREHFAIFPASHFVTREEKLKVAIERIEKELEERLKELRDENKLLEAQRLEQRTNYDLEMMREMGFCSGIENYSVHLTLRPLGSTPYTLLDYFGDDWLVMIDESHVTLPQVRGMYNGDRARKQVLVDHGFRLPSALDNRPLKFEEFEEKTKQLVYVSATPGPYEIEHTDKMVEQIIRPTGLLDPKIEVRPTENQIDDLLSEIQTRVERNERVLVTTLTKKMSEDLTTYMKEAGIKVNYLHSEIKTLERIEIIRDLRMGTYDVIVGINLLREGIDIPEVSLVVILDADKEGFLRSNRSLIQTIGRAARNDKGEVIMYADKMTDSMKYAIDETQRRREIQMKHNEKHGITPKTINKKIHDLISATVENDENNDKAQTVIPKKMTKKERQKTIDNIEKEMKQAAKDLDFEKATELRDMLFELKAEG | 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. | Q6GB72 |
Q5VWG9 | TAF3_HUMAN | Transcription initiation factor TFIID 140 kDa subunit | Homo | MCESYSRSLLRVSVAQICQALGWDSVQLSACHLLTDVLQRYLQQLGRGCHRYSELYGRTDPILDDVGEAFQLMGVSLHELEDYIHNIEPVTFPHQIPSFPVSKNNVLQFPQPGSKDAEERKEYIPDYLPPIVSSQEEEEEEQVPTDGGTSAEAMQVPLEEDDELEEEEIINDENFLGKRPLDSPEAEELPAMKRPRLLSTKGDTLDVVLLEAREPLSSINTQKIPPMLSPVHVQDSTDLAPPSPEPPMLAPVAKSQMPTAKPLETKSFTPKTKTKTSSPGQKTKSPKTAQSPAMVGSPIRSPKTVSKEKKSPGRSKSPKSPKSPKVTTHIPQTPVRPETPNRTPSATLSEKISKETIQVKQIQTPPDAGKLNSENQPKKAVVADKTIEASIDAVIARACAEREPDPFEFSSGSESEGDIFTSPKRISGPECTTPKASTSANNFTKSGSTPLPLSGGTSSSDNSWTMDASIDEVVRKAKLGTPSNMPPNFPYISSPSVSPPTPEPLHKVYEEKTKLPSSVEVKKKLKKELKTKMKKKEKQRDREREKDKNKDKSKEKDKVKEKEKDKETGRETKYPWKEFLKEEEADPYKFKIKEFEDVDPKVKLKDGLVRKEKEKHKDKKKDREKGKKDKDKREKEKVKDKGREDKMKAPAPPLVLPPKELALPLFSPATASRVPAMLPSLLPVLPEKLFEEKEKVKEKEKKKDKKEKKKKKEKEKEKKEKEREKEKREREKREKEKEKHKHEKIKVEPVALAPSPVIPRLTLRVGAGQDKIVISKVVPAPEAKPAPSQNRPKTPPPAPAPAPGPMLVSPAPVPLPLLAQAAAGPALLPSPGPAASGASAKAPVRSVVTETVSTYVIRDEWGNQIWICPGCNKPDDGSPMIGCDDCDDWYHWPCVGIMTAPPEEMQWFCPKCANKKKDKKHKKRKHRAH | The TFIID basal transcription factor complex plays a major role in the initiation of RNA polymerase II (Pol II)-dependent transcription . TFIID recognizes and binds promoters with or without a TATA box via its subunit TBP, a TATA-box-binding protein, and promotes assembly of the pre-initiation complex (PIC) . The TFIID complex consists of TBP and TBP-associated factors (TAFs), including TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13 . The TFIID complex structure can be divided into 3 modules TFIID-A, TFIID-B, and TFIID-C . TAF3 forms the TFIID-A module together with TAF5 and TBP . Required in complex with TBPL2 for the differentiation of myoblasts into myocytes . The TAF3-TBPL2 complex replaces TFIID at specific promoters at an early stage in the differentiation process . | Q5VWG9 |
C0HKW2 | TACHY_AGRIP | KAQMGFFGMR-amide | Agrotis | MGAPRTCLIFITIQLVSLAYAQEVSKRVPQGFLGMRGKKYFDEEGIEQFYKRKPQFFVGVKGKKSLQDILEAPEEYYKRAPMGFMGMRGKKDLGDSQSTELFPKRDGSLIGKIDYSSKEENADPDFPILNELLLQYLSQLDAPRNTYMQSSESMEPEQSNDLDKRAANFNQFYGVRGKKSINNKRPYDLTFRGKFIGVRGKKDLKNSNAHEIKFLVDQNGPLPKRKAQMGFFGMRGKKWTDEPSLEMDMPN | Tachykinins are active peptides which excite neurons, evoke behavioral responses, are potent vasodilators and secretagogues, and contract (directly or indirectly) many smooth muscles. | C0HKW2 |
A4SHM8 | UPPP_AERS4 | Undecaprenyl pyrophosphate phosphatase | Aeromonas | MTESYALFVAFVLGIVEGLTEFLPVSSTGHMIIVGHLLGFEGPKAATFEVVIQMGSILAVVAVFWRRLFGLIGIHFGQKPPQDHATLSLVHIILGMLPAVIIGLGIHSWIKANLFGPETVMYALVAGGILLIIAEKFRPTVRSETLDDISYKQAFGIGLFQCLALWPGFSRSGATISGGMLMGISRQAAAEFSFILAVPMMVAASGLDLYKSRDLLSMADFPMFAVGFITAFVVAMIAIKTFLALIRRLDFIPFAIYRFIVAFAVYLVFVA | Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin. | A4SHM8 |
Q6G1G9 | TRUA_BARQU | tRNA-uridine isomerase I | Bartonella | MPRFKLTLEYDGSNYAGWQRQAELHTIQSALEQAIFHFSGQQLTTTTAGRTDAGVHATGQVAHVDFIKNWQTYTVRDALNAYLQKQGEEIAVLNVQNVPDNFDARFSAIKRHYLFKILNRLSPPALNIKRVWWIPKPLNVDAMHQAAQKLVGQHDFTTFRSAHCQAKSPIRTLERLDVYREGEEIFLYAQARSFLHHQIRSFAGSLMEVGIGRWTAQDLEAALHAKDRKRCGMVAPPSGLYLTQVDY | Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs. | Q6G1G9 |
A1US90 | TPIS_BARBK | Triose-phosphate isomerase | Bartonella | MTSSIRPLLAGNWKMNGTSESLRELRAIASGIDSDRDRCFEALVCVPATLLSRASDILSDENIFLGGQDCHFNDSGPHTGDISACMLKEAGASHVILGHSERRTDYRESDAIVCAKVKAAWRAGLVALICIGETLEERENNTVLDVLAQQLKGSVPAGAMDHNTVIAYEPRWAIGTGKTPTSEDIAQVHGFIRKEVSHRFGDEGHKIRLLYGGSVKPSNASELLETSHVNGALIGGASLKATDFLTICNIYRKL | Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P). | A1US90 |
Q89A63 | TUSC_BUCBP | tRNA 2-thiouridine synthesizing protein C | Buchnera | MKKIAFVFSYVPHGVSLGREGLDLLLSVSIMNSKISVFFIGDGIFQLLKNQKPDEILSKNYVLSFKILPFFGIYDFFLCNESLKERGLFKKTDFLLDVSILSAIEIRNKLKNSDLIINF | Part of a sulfur-relay system required for 2-thiolation of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at tRNA wobble positions. | Q89A63 |
Q0HSD9 | UPPP_SHESR | Undecaprenyl pyrophosphate phosphatase | Shewanella | MDTFQVIILALIQGLTEFLPISSSAHLILPAQLLGWEDQGLSFDVAVNTGSLFAVVIYFRNELWAMFKAWIASMVKGQHSDDSKLAWWIILATLPAVFFGFIAKDFIETHLRSAGVIAVTTIVFGLLLWWADKMSRRDLTVYQTGWRKALLIGFAQALALIPGTSRSGATMTAALMLGLSRDAAARFSFLMSVPVSLGAAILVGKDLAESPLPIDYQALTLGTVISFVAAYLCIHYFLKIISRMGMTPFVIYRLILGAVLCGFIFL | Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin. | Q0HSD9 |
Q8NBZ7 | UXS1_HUMAN | UDP-glucuronate decarboxylase 1 | Homo | MVSKALLRLVSAVNRRRMKLLLGIALLAYVASVWGNFVNMRSIQENGELKIESKIEEMVEPLREKIRDLEKSFTQKYPPVKFLSEKDRKRILITGGAGFVGSHLTDKLMMDGHEVTVVDNFFTGRKRNVEHWIGHENFELINHDVVEPLYIEVDQIYHLASPASPPNYMYNPIKTLKTNTIGTLNMLGLAKRVGARLLLASTSEVYGDPEVHPQSEDYWGHVNPIGPRACYDEGKRVAETMCYAYMKQEGVEVRVARIFNTFGPRMHMNDGRVVSNFILQALQGEPLTVYGSGSQTRAFQYVSDLVNGLVALMNSNVSSPVNLGNPEEHTILEFAQLIKNLVGSGSEIQFLSEAQDDPQKRKPDIKKAKLMLGWEPVVPLEEGLNKAIHYFRKELEYQANNQYIPKPKPARIKKGRTRHS | Catalyzes the NAD-dependent decarboxylation of UDP-glucuronic acid to UDP-xylose . Necessary for the biosynthesis of the core tetrasaccharide in glycosaminoglycan biosynthesis . | Q8NBZ7 |
B8D7X0 | TYSY_BUCAT | Thymidylate synthase | Buchnera | MKQYIKLIKKIIRVGNQKKDRTGTGTLSIFGYNMKFDLKKGFPLLTTKKCHIASIIYELLWFLKGDTNIAYLNENKISIWNNWANESGDVGPIYGKQWRNWSTPEGHEIDQIKNVLIQLKKNPDSRRMLVSSWNVGDIDKMRLPPCHVLFQFYVFNNTLSCQLYQRSCDVFLGLPFNIASYSILIHMIAQQCDLKVGDFLWTGGDVHLYNNHIELAKKQILRIPRTLPKLTILKKPQSLFQYCFEDFKIIGYHPYPAIKGEISI | 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. | B8D7X0 |