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 |
|---|---|---|---|---|---|---|
A1KB60 | THIE_AZOSB | Thiamine-phosphate pyrophosphorylase | Azoarcus | MGERIRGLYLVTPDAADSATLLASVERVLPARPALLQYRNKLADPLRQLDEARSLRQLCSSAGVPLIINDDVALARAVAADGVHLGRDDGSPAAARAVLGADALIGVSCYDEWVRAEDAAAAGADYVAFGAMFPSSTKPGAVRAPLTLLTRARAALDCPVAAIGGITLDNAPALIEAGADLLAVISDVFAAADPLQRALAYSALFA | 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). | A1KB60 |
Q880X7 | UVRC_PSESM | Excinuclease ABC subunit C | Pseudomonas | MTQTFDPSAFLATCSGRPGVYRMFDADATLLYVGKAKNLKKRLASYFRKTGHAPKTGALVARIAQIETTITNNETEALLLEQTLIKEWRPPYNILLRDDKSYPYVFLSDGTYPRLSIHRGAKKAKGRYFGPYPSAGAIRESLSLLQKTFQVRQCEDSFFKNRNRPCLQYQIKRCKGPCVGLVEPEVYAEDVRHSVMFLEGRSNALSDELNASMEKAAMALDFERAAELRDQVALLRRVQDQQSMDGGTGDVDVVAAFVNPGGACVHLISVRGGRVLGSKNFFPQVGIEEEVGEVMSAFLAQYFLGGVDRELPSEVIVNVV... | 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. | Q880X7 |
P28274 | URA7_YEAST | UTP--ammonia ligase 1 | Saccharomyces | MKYVVVSGGVISGIGKGVLASSTGMLMKTLGLKVTSIKIDPYMNIDAGTMSPLEHGECFVLDDGGETDLDLGNYERYLGVTLTKDHNITTGKIYSHVIAKERKGDYLGKTVQIVPHLTNAIQDWIERVAKIPVDDTGMEPDVCIIELGGTVGDIESAPFVEALRQFQFKVGKENFALIHVSLVPVIHGEQKTKPTQAAIKGLRSLGLVPDMIACRCSETLDKPTIDKIAMFCHVGPEQVVNVHDVNSTYHVPLLLLEQKMIDYLHARLKLDEISLTEEEKQRGLELLSKWKATTGNFDESMETVKIALVGKYTNLKDSYL... | Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. | P28274 |
A4JCS0 | UVRC_BURVG | Excinuclease ABC subunit C | Burkholderia cepacia complex | MTSPEAADTPFEPKKILAQLPHMPGVYRYYDATGAVLYVGKARDLKKRVSSYFTKTQLSPRIAMMVTRIARIETTVTRSEAEALLLENNLIKALAPRYNILFRDDKSYPYLKLTAHRFPRMAYYRGSVDKQNQYFGPFPSAWAVRESIQILQRVFQLRTCEDSVFNNRTRPCLLHQIGRCTAPCVGAITEDDYAIDVSNAARFLLGRQSEVMNELEQKMHAFAAELKFEQAAAVRNQMSSLATVLHQQAIEVGGDSDVDILAVVAQGGRVCVNLAMVRGGRHLGDKAYFPTHVESALTLAEGGLGDEADGVDDAAAAMPD... | 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. | A4JCS0 |
C5A338 | VATD_THEGJ | V-ATPase subunit D | Thermococcus | MAELLNVKPTRMELLNLKRRIQLAKKGHKLLKDKQDALIMEFFTIYDEALQLRRELNEKMGVAFETLTRAQIEAGTLPLREAALAVKPNKEVEIKRRNVMGVSVPLIEAEGFKRKASERGYAFVSTSPFVDIAAEKFEEVLDLAVRLAEVEETLKRLAREIETTKRRVNALEYIIIPRMEATVKFIKQRLDEMERENFFRLKRVKALIEARSGS | Produces ATP from ADP in the presence of a proton gradient across the membrane. | C5A338 |
A3CK49 | VATB_STRSV | V-ATPase subunit B | Streptococcus | MSVIKEYRTVSEVVGPLMIVDQVAGVHFNELVEIQLHDGSKRQGQVLEVQEDKAMVQLFEGSSGINLEKAKVRFTGRPLELPVSEDMVGRIFNGMGKPIDGGPAILPEKYLDIDGQAINPVARDYPDEFIQTGISAIDHLNTLVRGQKLPVFSGSGLPHKELAAQIARQATVLNSDENFAVVFVAMGITFEEAEFFMNDLRETGAIDRSVLFINLANDPAIERIATPRIALTAAEYLAYEKDMHVLVIMTDMTNYCEALREVSAARREVPGRRGYPGYLYTNLSTLYERAGRLVGKKGSVTQIPILSMPEDDITHPIPDL... | Produces ATP from ADP in the presence of a proton gradient across the membrane. The V-type beta chain is a regulatory subunit. | A3CK49 |
P43348 | TCTP_RABIT | Translationally-controlled tumor protein | Oryctolagus | MIIYRDLISHDEMFSDIYKIREIAGGLCLEVEGKMVSRTEGNIDDSLIGGNASAEGPEGEGTESTVITGVDIVMNHHLQETSFTKEAYKKYIKDYMKSIKGKLEEQRPERVKPFMTGAAEQIKHILANFKNYQFYIGENMNPDGMVALLDYREDGVTPFMIFFKDGLEMEKC | Involved in calcium binding and microtubule stabilization. | P43348 |
O59490 | XERA_PYRHO | Tyrosine recombinase XerA | Pyrococcus | MKEREEIVNSDILEEFATYLELEGKSKNTIRMYTYYLSKFFEEGYSPTARDALKFLAKLRKSGYSIRSLNLVIQALKSYFKFEGLDSEAEKLKNPKIPKSLPKSLTEDEVKKIVSVADNLRDKLILLLLYGAGLRVSELCNLKIEDVNFEKSFLIVRGGKGGKDRVIPISKTLLFEIERYLKTRKDNSPYLFVEKRRNRKDKLSPKTVWMLVKKYGKKVGLNVTPHQLRHSFATHMLERGVDIRIIQELLGHANLSTTQIYTKVTTKHLREAIEKAKLIETILGG | Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. | O59490 |
Q28VU8 | UPPP_JANSC | Undecaprenyl pyrophosphate phosphatase | unclassified Jannaschia | MSLFTLFLLALVQGITEFLPISSSGHLILLPNLLGIEDQGQAIDVAVHVGTLGAVILYFWRDVKAAIAGTPRLLTGRIDTPGAKLAFLLIIATIPVIIFGLFLEVTGIYDSLRSIAVIGWTMLIFGLVLYWADQRGGTEKQSDDWSLRDAVTMGLWQAVALIPGTSRSGITITAARFLGYDRESAARVAMLMSIPTIIATGVFAGAEVIATADAQTARDGAIAAALSFLAALAALTLMFRLLKSVSFTPYVIYRVILGVILLVIAYA | Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin. | Q28VU8 |
Q8IN42 | TOTZ_DROME | Protein Turandot Z | Sophophora | MYFAIRLSFVLAVLICLTGNGSARMLDADRNRLQQLQIRSQQSADANTQVDIAYEVIGIYDKYKGQGGSNVLREAQLNSQVNDFKRKTMVIDGVPAQGGVWGILGAIKKAADAVPDNVKKDAENLVKSSTKVLVRGIYDYLMGKMKH | A humoral factor that may play a role in stress tolerance. | Q8IN42 |
O00268 | TAF4_HUMAN | Transcription initiation factor TFIID 135 kDa subunit | Homo | MAAGSDLLDEVFFNSEVDEKVVSDLVGSLESQLAASAAHHHHLAPRTPEVRAAAAGALGNHVVSGSPAGAAGAGPAAPAEGAPGAAPEPPPAGRARPGGGGPQRPGPPSPRRPLVPAGPAPPAAKLRPPPEGSAGSCAPVPAAAAVAAGPEPAPAGPAKPAGPAALAARAGPGPGPGPGPGPGPGPGKPAGPGAAQTLNGSAALLNSHHAAAPAVSLVNNGPAALLPLPKPAAPGTVIQTPPFVGAAAPPAPAAPSPPAAPAPAAPAAAPPPPPPAPATLARPPGHPAGPPTAAPAVPPPAAAQNGGSAGAAPAPAPAAG... | 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... | O00268 |
B8NM70 | USTYB_ASPFN | Ustiloxin B biosynthesis protein Yb | Aspergillus subgen. Circumdati | MPSDGNHLTRSTGGNGFIAVNQTERYTLPPPIKQLALEGQDPRTDNPGTDGTGAVHICKDFDGILAWADSRRLVDAKHN | Oxidase; part of the gene cluster that mediates the biosynthesis of the secondary metabolite ustiloxin B, an antimitotic tetrapeptide . First, ustA is processed by the subtilisin-like endoprotease Kex2 that is outside the ustiloxin B gene cluster, at the C-terminal side of Arg-Lys, after transfer to Golgi apparatus thr... | B8NM70 |
Q3KP31 | ZN791_HUMAN | Zinc finger protein 791 | Homo | MDSVAFEDVSVSFSQEEWALLAPSQKKLYRDVMQETFKNLASIGEKWEDPNVEDQHKNQGRNLRSHTGERLCEGKEGSQCAENFSPNLSVTKKTAGVKPYECTICGKAFMRLSSLTRHMRSHTGYELFEKPYKCKECEKAFSYLKSFQRHERSHTGEKPYKCKQCGKTFIYHQPFQRHERTHIGEKPYECKQCGKALSCSSSLRVHERIHTGEKPYECKQCGKAFSCSSSIRVHERTHTGEKPYACKECGKAFISHTSVLTHMITHNGDRPYKCKECGKAFIFPSFLRVHERIHTGEKPYKCKQCGKAFRCSTSIQIHER... | May be involved in transcriptional regulation. | Q3KP31 |
B0Y4Q5 | TVP38_ASPFC | Golgi apparatus membrane protein tvp38 | Aspergillus subgen. Fumigati | MPADYTSTARALSLPMSPAESLSPAEEDTRPLWSHLASSRRNTASPSVRESTGLRDQVVNQATKMLRRTKKTWRRLTFWQRIGAIGAALLAILLGLSFMIFTGQVFFWLGPVAEKWEQSWLAFFVLWLCVFFVSFPPLVGWSTFGTISGFIYGIWKGWILYATATVLGSTCSFIVSRTILSKFVNRMMERDKRFAALALTLKYDGLKLLCMIRLCPLPYSVCNGAVSTFPTVHPLMYGLATALITPKLLVPAFIGSRIRILSEKNEEMSAASKAVNICSIILTIGIGVFTGWYIYRRTLARAKELEAKERADIRRSLQAD... | Golgi membrane protein involved in vesicular trafficking and spindle migration. | B0Y4Q5 |
Q96493 | UFOG_GENTR | UDP-glucose flavonoid 3-O-glucosyltransferase | Gentiana | MSPVSHVAVLAFPFGTHAAPLLTLVNRLAASAPDIIFSFFSTSSSITTIFSPTNLISIGSNIKPYAVWDGSPEGFVFSGNPREPIEYFLNAAPDNFDKAMKKAVEDTGVNISCLLTDAFLWFAADFSEKIGVPWIPVWTAASCSLCLHVYTDEIRSRFAEFDIAEKAEKTIDFIPGLSAISFSDLPEELIMEDSQSIFALTLHNMGLKLHKATAVAVNSFEEIDPIITNHLRSTNQLNILNIGPLQTLSSSIPPEDNECLKWLQTQKESSVVYLSFGTVINPPPNEMAALASTLESRKIPFLWSLRDEARKHLPENFIDR... | In the presence of other necessary color factors, this glycosylation reaction allows the accumulation of anthocyanin pigments . Anthocyanidins are the preferred substrates, while flavonols are only a minor substrate in vitro . | Q96493 |
Q2SUI1 | TRPD_BURTA | Anthranilate phosphoribosyltransferase | pseudomallei group | MTITPQEALQRTIEHREIFHDEMLHLMRLIMRGDMSPVMAAAIITGLRVKKETIGEITAAATVMREFARHVEVEDNANFVDIVGTGGDGSHTFNISTATMFVAAAAGAKVAKHGNRGVSSKSGSADVLEALGVNIDLQPEQVAASIAETGMGFMFAPNHHPAMRNIAPVRRELGVRTIFNILGPLTNPADAPNQLMGVFHPDLVGIQVRVMQRLGARHVLVVYGKDGMDEVSLGAATLVGELRDGEVREYEIHPEDFGMQMVSNRTLKVENAGESRVMLLEALGNKPGVAREIVTLNAGTALYSANVAGSIADGIQLARE... | Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA). | Q2SUI1 |
P38669 | TBA2_NEUCR | Tubulin alpha-B chain | Neurospora | MREIISLNVGQAGCQIANSCWELYCLEHGIQPDGYLTEERKAADPDHGFSTFFSETGNGKYVPRTIYADLEPNVIDEVRTGAYRGLFHPEHMISGKEDASNNYARGHYTVGKELIDQVLDKVRRVADNCSGLQGFLVFHSFGGGTGSGFGALLMERLSVDYGKKSKLEFCVYPAPQTATSVVEPYNSILTTHTTLEHADCSFMVDNEAIYDICRRNLGLERPNYENLNRLIAQVVSSITASLRFDGSLNVDLNEFQTNLVPYPRIHFPLVAYAPVISAAKAAHEANSVQEMTMSCFEPNNQMVKCDPRHGKYMATCLLYR... | 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-... | P38669 |
Q9U3V9 | XMAS_DROME | Protein xmas | Sophophora | MAEPRPGGYNYKTLLCRNIPELFLDKYVARSHFGRFGTLVNFVLRPRRMTCTVSYASEDEAARALLDGASFQGHLFDISYADNETAPAQKTEEWVDPDIQAELSALQSGWRNEYGSGKPIKKPQNGSSGSGGSSMLPAIPVGPATAPVSRDRTPAQLRDLENMMRRPAHTSEEKFSVLDARDKLLRLNRTQHKLSGATQGHCADMCPEKERVLREFQRQVAYYELQPGSDELICHERALKQYSRSSADQETPLPHELRNETALHMTMSYLMHEIMDISERQDPQSHMGDWFHFVWDRTRSIRKEITQQELCSLGAVKLVE... | Involved in mRNA export and mRNA coupled transcription activation . Component of the nuclear pore complex (NPC)-associated TREX-2/AMEX complex (anchoring and mRNA export complex) which functions in docking export-competent ribonucleoprotein particles (mRNPs) to the nuclear entrance of the nuclear pore complex (nuclear ... | Q9U3V9 |
B4STS7 | TRMB_STRM5 | tRNA(m7G46)-methyltransferase | Stenotrophomonas maltophilia group | MTNPFDSAGSKAPPKPFTVSEGRREVRSFVLRQGRFTPAQQRAFDERWPRFGIDYNGQPRDLDATFGRPAHKVLEIGFGNGAAMRFAAQHDPSRDYIGIEVHAPGVGRLLNALADDNADHVRLYHHDAVEVLQNEIADGALDEVRIYFPDPWHKKRHNKRRLLQPAFAELIVRKLRPGGRLHCATDWEDYAEQMWDVLDATAGLVNRAGPRGSVPRPDWRPQTHFETRGQKLGHGVWDLLYDRT | Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. | B4STS7 |
P61410 | THIE_BACC1 | Thiamine-phosphate pyrophosphorylase | Bacillus cereus group | MSRISKAEMSRLLSVYFIMGSNNCTKDPLQILKDALEGGITIFQFREKGEGALTGEERICFAKELQAICKEYGVPFIVNDDVELALELDADGVHVGQEDEGITSVREKMGDKIIGVSTHTIEEARWAIENGADYLGVGPIFPTSTKKDTKAVQGTKGLAHFREQGITIPIVGIGGISIENTASVIEAGADGVSVISAISLAESAYESTKQLVEEVSKKGTSHKY | 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). | P61410 |
Q07402 | UREF_BACSB | Urease accessory protein UreF | Bacillus | MNRLLSLFQLCDSNFPSGSFSHSFGLETYIQEKVITDKESFKNAISVYIRKQLFFTEGLACILAYEAMEKNEPSALVELDHILFASNVAQETRSGNQRMGERMAKLCVDLYPSPILIEYTNRIKEKKAYGHSAIVFAIVAYHLKVTKETAVGAYLFANVSALVQNAVRGIPIGQTDGQRILVEIQPLLEEGVRTISQLPKEDLGAVSPGMEIAQMRHERLNVRLFMS | Required for maturation of urease via the functional incorporation of the urease nickel metallocenter. | Q07402 |
Q5L5I5 | TAL_CHLAB | Transaldolase | Chlamydia | MSSQFEQLKLLSVLVCDTGDPELVKSSESQDATTNPSLILKVAQEPKYQELLTEAIAWGIRQNGDDVQTLTFVLDKIQVNFGLEILKHIPGRVSLEIDARLSFNTEAMVQRAIFLSELFAASGGDKKRLLVKIPGTWEGIQAVELLEKQGIACNVTLIFNLIQAIAAAKAKATLISPFVGRIYDWWIAAYGDDGYSIDADPGVASVSNIYTYYKKFDITTQIMAASFRSKEQVLALAGCDLLTVSPKLLDELKKDQSPVERKLDPAEAKKLDVQPVELTESIFRFLMNEDAMATEKLAEGIRIFSGDTQILEAAVTEFIK... | Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway. | Q5L5I5 |
P9WIZ6 | Y3131_MYCTO | Putative NAD(P)H nitroreductase MT3217 | Mycobacterium tuberculosis complex | MTAAVDGKGPAAMNTHFPDAETVRTVLTLAVRAPSIHNTQPWRWRVCPTSLELFSRPDMQLRSTDPDGRELILSCGVALHHCVVALASLGWQAKVNRFPDPKDRCHLATIGVQPLVPDQADVALAAAIPRRRTDRRAYSCWPVPGGDIALMAARAARGGVMLRQVSALDRMKAIVAQAVLDHVTDEEYLRELTIWSGRYGSVAGVPARNEPPSDPSAPIPGRLFAGPGLSQPSDVLPADDGAAILALGTETDDRLARLRAGEAASIVLLTATAMGLACCPITEPLEIAKTRDAVRAEVFGAGGYPQMLLRVGWAPINADP... | Stimulates pro-inflammatory cytokine expression via TLR2 signaling pathway. Activation of TLR2 results in the phosphorylation and activation of NF-kappa-B. Also induces TLR2 expression. May influence the innate immune responses to facilitate the survival of M.tuberculosis in the granulomatous microenvironment. | P9WIZ6 |
Q07748 | THI13_YEAST | Thiamine pyrimidine synthase | Saccharomyces | MSTDKITFLLNWQPTPYHIPIFLAQTKGYFKEQGLDIAILEPTNPSDVTELIGSGKVDMGLKAMIHTLAAKARGFPVTSVASLLDEPFTGVLYLKGSGITEDFQSLKGKKIGYVGEFGKIQIDELTKHYGMKPEDYTAVRCGMNVAKYIIEGKIDAGIGIECMQQVELEEYLAKQGRPASDAKMLRIDKLACLGCCCFCTVLYICNDEFLKKNPEKVRKFLKAIKKATDYVLADPVKAWKEYIDFKPQLNNDLSYKQYQRCYAYFSSSLYNVHRDWKKVTGYGKRLAILPPDYVSNYTNEYLSWPEPEEVSDPLEAQRLM... | 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... | Q07748 |
Q9ZRX0 | TCTP_PSEMZ | Translationally-controlled tumor protein homolog | Pseudotsuga | MIVYQDLLSGDELLSDSFPYKELYNGVLWEVEGKWVVQGAVDVDIGANPSAEGGDEEGVKIRLVKVVDIVDTFRLQEQPPFDKKQFLGFIKRYIKNLATKLSEERQAEFKKNVEGAAKMLVSKLSDLQFFVGESMHDDGSMVFAYYKDGATDPTFLYFADGLKEVKC | Involved in calcium binding and microtubule stabilization. | Q9ZRX0 |
Q03LR5 | TRHO_STRTD | tRNA hydroxylation protein O | Streptococcus | MAKPIRVLLYYKYVPIENAEQFAADHLAFCKSIGLKGRILVADEGINGTVSGDYETTQKYMDYVHSLPGMEDLWFKIDEEEEQAFKKMFVRYKKEIVHLGLEDNNFDSDINPLETTGAYLSPKEFKDALLDEDTVVLDTRNDYEYDLGHFRGAIRPDIRNFRELPQWVRDHKEEFMDKRVVVYCTGGVRCEKFSGWLVREGYKDVGQLHGGIVTYGKDPEVQGELWDGKLYVFDERIAVDVNHVDPIVVGKDWFDGTPCERYVNCGNPFCNRRILTSEENEDKYLRGCSHECRVHPRNRYVSENDLSQEEVVSRLAAIGE... | Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs. | Q03LR5 |
Q3SQ36 | TYSY_NITWN | Thymidylate synthase | Nitrobacter | MNQYHDLLERILGEGTEKHDRTGTGTLSVFGHQMRFDLASGFPMLTTKKLPFRSIVHELLWFLRGETNIKYLKDNGVSIWDEWADANGDLGPVYGSQWRSWPARDGRGIDQIANVIDLIQRNPDSRRLIVSAWNPADVDRMALPPCHCLFQFYVAGGKLSCQLYQRSADVFLGVPFNIASYALLTMMVAQVTGLKPGDFVHSLGDAHLYSNHLDQARLQLSRPTRPLPTMTINPEVKDIFAFRYEDFRLENYDPHPHIKAEVAV | 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 intracell... | Q3SQ36 |
C6E4K4 | TRUD_GEOSM | tRNA-uridine isomerase D | unclassified Geobacter | MSIYLTAEVPGTGGVIKATPEDFLVEEIPAYLPSGQGEHCFAVLEKRGIATLEALRRLAKALGVQERDLGYAGMKDAIGITRQTISIPRVAPEKVLALEIPGITVLSASMHGNKLRLGHLKGNRFVIRVRDVAQGAAGNAEAALEIMTRRGVPNRFGVQRYGAQGNTHEIGAAMLRREFKSAVDRLIGDPAAVTDERWRLAIEAYRRGEVAESLALFPGHFRVERELLTRLVQRPDGFERAFNSVQPRMKRLYLSAFQSSLFDLVLGKRLDSFDQVNVGDIAFKHENGACFLVQDLAAEAPRAESFEISPTGPMFGCTMM... | Responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs. | C6E4K4 |
B0TQA0 | TRUB_SHEHH | tRNA-uridine isomerase | Shewanella | MARRSRGRFIDGILLLDKDTGMSSNFALQRVKRFFNANKAGHTGALDPLATGMLPICLGEATKFSQHLLDADKRYLVTAKLGQRTDTSDSDGEIVQTREVNFTQEQLDTALEHFRGETMQVPSMYSALKHKGQPLYKYAREGIEVPREARPINVFELNFISLEGDELTLDIHCSKGTYIRTITDDLGEMLGCGAHVIMLRRTQVAGYPYDKMVSLKQLEELVTKADAESLSLSEVLDPLLLPMDTAVSGFKEINVSDELATYLMNGNPVQVANLPVDELVRITIGDARQFVGIGQMNDDGQLAPKRLIVLREQQD | Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs. | B0TQA0 |
P82959 | TXH21_CYRSC | Huwentoxin-II | Cyriopagopus | MKVTLIAILTCAAVLVLHTTAAEELEAESQLMEVGMPDTELAAVDEERLFECSFSCEIEKEGDKPCKKKKCKGGWKCKFNMCVKV | Lethal neurotoxin that blocks neuromuscular transmission. Acts cooperatively to potentiate the activity of huwentoxin-I. This toxin is active against insects. | P82959 |
Q4QML9 | TRUD_HAEI8 | tRNA-uridine isomerase D | Haemophilus | MLEQLPYLALKTPPKTTALLKAECADFIVKEHLGYEMSGDGEFVALYVRKTDCNTLFVGEKLAKFAGVSERNMGYAGLKDRRAVTEQWFCLQMPGMETPDFSQFELDGVEILTVTRHNRKIRTGSLEGNYFDILLRGAEESDELKVRLDFVANFGFPNYFTEQRFGREGHNLTQALRWAQGEIKVKDRKKRSFYLSAARSEIFNLVVAARIAKGATNQVLPNDIVQLAGSHSWFKADEKEDLTVLQVRLENQDILLTAPLIGEDILAASDIENEIVNQHSAFDSLMKQERMKAVRRPLLMKAKGFSWAFEPEGLRLKFYL... | Responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs. | Q4QML9 |
B3R8A8 | ZAPD_CUPTR | Z ring-associated protein D | Cupriavidus | MILYEYPFNERIRTLLRLEDLFDRLEYFLGQDHAQQHHVALTTLFEIIDVAGRADLKTDLIKELERQRQALAPLRANPQIDQDALDSVIGEIEQGIAMLNQTVGKAGQLLTDNEWLTSIRSRAIIPGGTCEFDLPAYYAWQHRPAEDRRADILKWARPLVSLRMGTTIVLRLLREAGQSGKVIATGGSYQQMLSGRSYQLMQVYLDDSLLAFIPEMSANKYMLWVRFTQQDGDLRPRSVDADIPFLLKLCNF | Cell division factor that enhances FtsZ-ring assembly. Directly interacts with FtsZ and promotes bundling of FtsZ protofilaments, with a reduction in FtsZ GTPase activity. | B3R8A8 |
Q9K6X9 | UVRB_HALH5 | Excinuclease ABC subunit B | Halalkalibacterium (ex Joshi et al. 2022) | MSQSFELVSQYKPQGDQPNAIRQLVAGINEGKKHQTLLGATGTGKTFTMSNVIQQVNKPTLVIAHNKTLAGQLYSEFKEFFPNNAVEYFVSYYDYYQPEAYVPQSDTYIEKDASINDEIDKLRHSATSALFERNDVIIVASVSCIYGLGSPEEYKELVCSLRTGMEIERNDLLRQLVDIQYDRNDVNFTRGTFRVRGDVVEIFPASRDEQCIRVEFFGDEIDRITEVDALTGEIKGERNHVAIFPASHFVTREEKLKRATKSIEAELEERLKELHDRGKLLEAQRLEQRTRYDLEMIHEMGFCSGIENYSRHLTLRKAGE... | 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 bindi... | Q9K6X9 |
Q41738 | THI41_MAIZE | Thiazole biosynthetic enzyme 1 | Zea | MATAAASSLLKSSFAGSRLPAATRTTPASLVVATGPRGAGAGPICASMSMSSSNPPYDLTSFRFSPIKESIVSREMTRRYMTDMITYADTDVVIVGAGSAGLSCAYELSKDPAVSIAIVEQSVSPGGGAWLGGQLFSAMVVRKPAHLFLDELGVAYDEAEDYVVIKHAALFTSTVMSLLLARPNVKLFNAVAVEDLIVRGGRVGGVVTNWALVSMNHDTQSCMDPNVMEAKVVVSSCGHDGPFGATGVKRLQDIGMISAVPGMKALDMNTAEDEIVRLTREVVPGMIVTGMEVAEIDGAPRMGPTFGAMMISGQKAAHLA... | Involved in biosynthesis of the thiamine precursor thiazole. Catalyzes the conversion of NAD and glycine to adenosine diphosphate 5-(2-hydroxyethyl)-4-methylthiazole-2-carboxylic acid (ADT), an adenylated thiazole intermediate. The reaction includes an iron-dependent sulfide transfer from a conserved cysteine residue o... | Q41738 |
O94266 | THI22_SCHPO | Hydroxymethylpyrimidine phosphate kinase 2 | Schizosaccharomyces | MPYNPLYESLSNQFDPSRIETVLDPMGYTIKRRALPVSLTIAGSDCSGGAGIQADLKTMTSLGVYGMSAITCLVAENAGGVDSVEEMSPAFVESQIDCCIRDIPCHVVKTGMLGSPEIVKAVARSAKKFNFSKLVVDPVMVATSGDSLVTKDIVSVLNEELLPLTYLVTPNIPEAIVLAKNQGLDISNINSVSDMERCAAVIHKLGPKHVLLKGGHMPVNNLGLKSSDDEDLRVVDILYDGNRFYHFSSSYLKKGEVHGTGCTLSSAIASFLAWEHSLTEAVQFGIDYVHGAITHSPPINNCSTNILNHMTRLRIVPFAP... | Catalyzes the phosphorylation of hydroxymethylpyrimidine phosphate (HMP-P) to HMP-PP, and of HMP to HMP-P. | O94266 |
A7ZNQ8 | YEGS_ECO24 | Probable lipid kinase YegS | Escherichia | MAEFPASLLILNGKSTDNLPLREAIMLLREEGMTIHVRVTWEKGDAARYVEEARKLGVATVIAGGGDGTINEVSTALIQCAGDDIPALGILPLGTANDFATSVGIPEALDKALKLAIAGNAIAIDMAQVNKQTCFINMATGGFGTRITTETPEKLKAALGGVSYIIHGLMRMDTLQPDRCEIRGENFHWQGDALVIGIGNGRQAGGGQQLCPNALINDGLLQLRIFTGDEILPALVSTLKSDEDNPNIIEGASSWFDIQAPHEITFNLDGEPLSGQNFHIEILPAALRCRLPPDCPLLR | Probably phosphorylates lipids; the in vivo substrate is unknown. | A7ZNQ8 |
P29501 | TBB2_PEA | Beta-2-tubulin | Pisum | EIVHIQGGQCGNQIGAKFWEVVCAEHGIDPTGRYGGDTDLQLERINVYYNEASCGRYVPRAVLMDLEPGTMDSVRSGPYGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAENCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEYPDRMMLTFSVFPSPKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLTTPSFGDLNHLISATMSGVTCCLRFPGQLNSDLRKLAVNLIPFPRLHFFMLGFAPLTSRGSQQYRALSVPEITQQMWDSKNMMCAADPRHGRYLTASAIFRGKMS... | 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-... | P29501 |
Q9I163 | Y2418_PSEAE | Pirin-like protein PA2418 | Pseudomonas | MKKVLGIYGNANRHWVGDGFPVRSLFSYNTLGQHISPFLLLDYAGPADFPPAQQRRGVGQHPHRGFETVTIVYQGEVEHHDSTGAGGRIGPGDVQWMTAASGILHEEYHSERFRSTGGTLEMVQLWVNLPSSDKMNPPRYQTLLDADIPRVGLPDRAGELRVIAGRYGRHQGPALTHSPLAVWDVQLKAGKHLALDLPKGHTCAVVVLRGTLAVGDEIVREAQVALLDRDDPRLELEANNDVQLLVLSGEPLDEPIIGYGPFVMSSREEIDQAIEDFENGRFIRAH | Putative quercetin 2,3-dioxygenase. | Q9I163 |
Q2TA17 | ZN668_BOVIN | Zinc finger protein 668 | Bos | MEVESPEERSPAPGYKRSGRRYKCLSCTKTFPNAPRAARHAATHGLADCTEEMAEAKLKPETDPKAEDASGDKVSGAAAKPRPYACPLCPKAYKTAPELRSHGRSHTGEKPFPCPECGRRFMQPVCLRVHLASHAGELPFRCAHCPKAYGALSKLKIHQRGHTGERPYTCADCGKSFADPSVFRKHRRTHAGLRPYSCERCGKAYAELKDLRNHERSHTGERPFLCSECGKSFSRSSSLTCHQRIHAAQKPYRCPACGKGFTQLSSYQSHERTHSGEKPFLCPRCGRMFSDPSSFRRHQRAHEGVKPYRCEKCGKDFRQP... | May be involved in transcriptional regulation. | Q2TA17 |
B8I0U9 | TRPD_RUMCH | Anthranilate phosphoribosyltransferase | Ruminiclostridium | MIQEAIYQVINKQDLDLDKTIQVMEEIMEGRATNAQIGSFLTAMRMKGETIDEITACATVMRQKCKRIHPEKDVLDIVGTGGDEANTFNISTVSSFVVSAGGVPVAKHGGRSVSSKCGSADLLEALGINIALSAEQSAEILQKIGMCFMFAPTYHASMKYAAPVRKELSVRTIFNILGPLANPAGANMQLLGVYDENLVEPLARVLLNLGVKRAMVVHGHDGLDEVTLCNTTTICEVSNGNINSFFLSPEQLGFSRCLLKELVGGDPKKNASIALDILNGSKGPKRDIVVLNSALCLYMSYNQITLRDCVKMAEQLIDSG... | Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA). | B8I0U9 |
Q91053 | VSP1_GLOUS | Snake venom serine protease | Gloydius | MVLISVLANLLILQLSYAQKSSELVIGGDECNINEHRFLVALYNSRSRTLFCGGTLINQEWVLTAAHCERKNFRIKLGIHSKKVPNEDEQTRVPKEKFFCLSSKNYTLWDKDIMLIRLDSPVSNSEHIAPLSLPSSPPSVGSVCRIMGWGRISPTKETYPDVPHCANINLLEYEMCRAPYPEFGLPATSRTLCAGILEGGKDTCRGDSGGPLICNGQFQGIASWGDDPCAQPHKPAAYTKVFDHLDWIQSIIAGNTDASCPP | Thrombin-like snake venom serine protease. Has a coagulant activity. Acts on alpha-chains of fibrinogen (FGA) generating fibrinopeptide A. | Q91053 |
Q4FUL2 | TRPA_PSYA2 | Tryptophan synthase alpha chain | Psychrobacter | MTRIESTFEILKAQNKKALIPYVMAGDPNPSNFVGLLHDLVKHGADMIEVGLPFSDPMADGPTVALAGERALAAGTSTRDALKMVAEFRQQDTQTPIILMGYLNPVEIIGYDNFVALCEQSGVDGILMVDLPPAEAGSFTQHLTEHSMNEIFLLSPTTLPERREQVLTHCGGYIYYVSLKGVTGSATLDTDDVATQVQAIKAETDLPVCVGFGIRDAASAKAIGAHADGIIVGSALVQNFADIDGNDATAVAHAQQKIMAKMTELREALDSLSVSSNG | The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. | Q4FUL2 |
P18732 | ZG64_XENLA | Gastrula zinc finger protein XlCGF64.1 | Xenopus | PSGKQYECPECGKTFKYKNSLTIHQRGHTEEKPFMCTQCGKCFRQKKALRRHQFIHTGEKPYVCTECEKRFLEKSQLILHQRGHTGEKPFTCTECGESFRHKQVLMRHQFIHTGEKPYECTQCGEGFLLKSKLIHHQRGHTGEKPFMCTECGKGFRQKQVLIEHQFIHTGEKPLMCTDCGKHFRQKHVLRLHKLSH | May be involved in transcriptional regulation. | P18732 |
Q0S3C4 | TSAD_RHOJR | tRNA threonylcarbamoyladenosine biosynthesis protein TsaD | Rhodococcus | MIVMGIESSCDETGVGIVRWNGDGTCELLADEVASSVEEHARYGGVVPEVASRAHLEAIVPTMRRALAVAGIAKPDALAVTIGPGLAGALLVGVAAAKAYAAAWDVPFYAVNHLGGHVSVDTLEHGPMPPCVALLVSGGHTHLLHVEDLAKPIVELGTTVDDAAGEAFDKVARLLGLGFPGGPALDAAAQDGDRNAIPFPRGMTGPRDARHDFSFSGLKTAVARYVESKERAGEVCSVPDIAASFQEAVADVLTMKAVRAARDVGVDTLVLGGGATANSRIRALAEERCADAGLTLRVPKPRLCTDNGVMIASLGAHLIA... | 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 ca... | Q0S3C4 |
P09123 | THRC_BACSL | Threonine synthase | Bacillus | MYKGLLKQYASYLPVNEKTPDVSLMEGNTPLIPLLNISKQLGVQLYGKYEGANPTGSFKDRGMVMAVAKAKEEGSEAIICASTGNTSASAAAYAARLGMKCIIVIPEGKIAHGKLAQAVAYGAEIISIEGNFDDALKAVRNIAAEEPITLVNSVNPYRIEGQKTAAFEICDQLQNAPDVLAIPVGNAGNITAYWKGFCEYEKEKGYKKPRIHGFEAEGAAAIVKGHVIEEPETIATAIRIGNPASWSYAVEAAEQSHGEIDMVSDEEILHAYRLLAKTEGVFAEPGSNASLAGVIKHVESGKIKKGETVVAVLTGNGLKD... | Catalyzes the gamma-elimination of phosphate from L-phosphohomoserine and the beta-addition of water to produce L-threonine. | P09123 |
P70904 | VLP23_BORHE | Variable large protein 23 | Borrelia | MRKRISAIIMTLFMVLVSCNSGGVAEDPKTVYLTSIANLGKGFLDVFVTFGDMVAGAFGIKADTKKSDIGKYFNDIEKTMTTVKKRLQDEVAKNGNYVKVKEVVDKFVADVLDKIAAGAKKQLRATGDAAIGMLLNEDAAPAEVASVNSLVKGIKEIVGVVLKDNEGDAAATKTADAEKKSVGKLLGKGAADGTETQAAAASASIGAITGADILQAIAKSGKAGAGEIKIEEAKNAAEIAAAKADSKDLAIDSAKKDAVIAAGIALRAMAKDGKFAAKNNEEKSANAVNGAAASAVGKTLSTLIIAIRNTVDSGLKTINE... | The Vlp and Vsp proteins are antigenically distinct proteins, only one vlp or vsp gene is transcriptionally active at any one time. Switching between these genes is a mechanism of host immune response evasion. | P70904 |
O48559 | UNI_PEA | Protein UNIFOLIATA | Pisum | MDPDAFTASLFKWDPRTVLSTAPSPRPQLLDYAVTPTTAPMTYHPARLPRELGGLEELFQAYGIRYYTAAKIAELGFTVSTLVDMKDDELDDMMNSLSQIFRWDLLVGERYGIKAAIRAERRRLDEEEIKRRGLLSGDTTNALDALSQEGLSEEPVVQREKEAMGSGGGSTWEVAVVEERRKRQQIRRRRMKMKGNDHGENEEGEEEEEDNISGGGVGGGERQREHPFIVTEPAEVARGKKNGLDYLFHLYEQCREFLIQVQAIAKERGEKCPTKVTNQVFRYAKKAGASYINKPKMRHYVHCYALHCLDEEVSNELRRG... | May regulate indeterminacy during leaf and flower development. | O48559 |
Q148G8 | UQCC3_BOVIN | Ubiquinol-cytochrome-c reductase complex assembly factor 3 | Bos | MTTLRKLLLVGALLGAGAGVGTALFALVTPGEERKQAMLKEMPEQYPQRRDEAARTKELLLATLQEAAATQENVAWRKNWMSGGGGGGGGGGRSA | Required for the assembly of the ubiquinol-cytochrome c reductase complex (mitochondrial respiratory chain complex III or cytochrome b-c1 complex), mediating cytochrome b recruitment and probably stabilization within the complex. Thereby, plays an important role in ATP production by mitochondria. Cardiolipin-binding pr... | Q148G8 |
Q9FL26 | WRKY8_ARATH | WRKY DNA-binding protein 8 | Arabidopsis | MSHEIKDLNNYHYTSSYNHYNINNQNMINLPYVSGPSAYNANMISSSQVGFDLPSKNLSPQGAFELGFELSPSSSDFFNPSLDQENGLYNAYNYNSSQKSHEVVGDGCATIKSEVRVSASPSSSEADHHPGEDSGKIRKKREVRDGGEDDQRSQKVVKTKKKEEKKKEPRVSFMTKTEVDHLEDGYRWRKYGQKAVKNSPYPRSYYRCTTQKCNVKKRVERSYQDPTVVITTYESQHNHPIPTNRRTAMFSGTTASDYNPSSSPIFSDLIINTPRSFSNDDLFRVPYASVNVNPSYHQQQHGFHQQESEFELLKEMFPSV... | Transcription factor. Interacts specifically with the W box (5'-TTGAC[CT]-3'), a frequently occurring stress-responsive cis-acting element. Functions as positive regulator of salt stress response. Binds the W box of LTI78/RD29A stress-response gene and directly regulates its transcription under salt stress. Functions a... | Q9FL26 |
Q8NHX9 | TPC2_HUMAN | Two pore calcium channel protein 2 | Homo | MAEPQAESEPLLGGARGGGGDWPAGLTTYRSIQVGPGAAARWDLCIDQAVVFIEDAIQYRSINHRVDASSMWLYRRYYSNVCQRTLSFTIFLILFLAFIETPSSLTSTADVRYRAAPWEPPCGLTESVEVLCLLVFAADLSVKGYLFGWAHFQKNLWLLGYLVVLVVSLVDWTVSLSLVCHEPLRIRRLLRPFFLLQNSSMMKKTLKCIRWSLPEMASVGLLLAIHLCLFTMFGMLLFAGGKQDDGQDRERLTYFQNLPESLTSLLVLLTTANNPDVMIPAYSKNRAYAIFFIVFTVIGSLFLMNLLTAIIYSQFRGYLM... | (Microbial infection) Required for cell entry of coronaviruses SARS-CoV and SARS-CoV-2, as well as human coronavirus EMC (HCoV-EMC), by endocytosis. | Q8NHX9 |
P25295 | TBG_SCHPO | Gamma-tubulin | Schizosaccharomyces | MGREIITLQAGQCGNQIGSQFWQQLCLEHGIGPDGTLESFATEGVDRKDVFFYQSDDTRYIPRAILIDLEPRVVNNILSDTYGSLYNPENILITKNGGGAGNNWANGYSHAERIFEDIMDMIDREADGSDSLEGFSLLHSIAGGTGSGLGSFLLERLNDRYPKKIIQTYSVFPNSQSVSDVVVQPYNSLLALKRLTLNADSVVVLDNAALAHIAADRLHTQNPTFHQQNQLVSTVMSASTTTLRYPGYMNNDLVSIIASLIPSPRCHFLLTSYTPFTNQQVEEAKAIRKTTVLDVMRRLLLPKNQMVSVNPSKKSCFISI... | 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. | P25295 |
Q8U1G7 | UPP_PYRFU | UPRTase | Pyrococcus | MIEDKRWGGVYSFEDSPYIMEILTELRDKDTDSIKFRKGLVKLGRYMGYEITKTMDVEKVKVETPLEETEGIIVKDRRNVVIITVLRAAIPFMEGLIKVFEHARVGIVSAARGKPPKFEIEMNYIKIPQITPEDTVIVADPMIATGSTLLRVLEEVKKYGTPKRTLVVGVLAAPEGITRIKEKFPEVEIFVAKIDRELNDKGYILPGLGDAGDRAFGEPVKITTLPQVHYIE | Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate. | Q8U1G7 |
Q5R7Z3 | TRAM1_PONAB | Translocating chain-associated membrane protein 1 | Pongo | MAIRKKSTKSPPVLSHEFVLQNHADIVSCVAMVFLLGLMFEITAKASIIFVTLQYNVTLPATEEQATESASLYYYGIKDLATVFFYMLVAIIIHAVIQEYMLDKINRRMHFSKTKHSKFNESGQLSAFYLFACVWGTFILISENYISDPTILWRAYPHNLMTFQMKFFYISQLAYWLHAFPELYFQKTKREDIPRQLVYIGLYLFHIAGAYLLNLNHLGLVLLVLHYFVEFLFHISRLFYFSNEKYQKGFSLWAVLFVLGRLLTLILSVLTVGFGLARAENQKLDFSTGNFNVLAVRIAVLASICITQAFMVWKFINFQL... | Involved in the translocation of nascent protein chains into or through the endoplasmic reticulum (ER) membrane by facilitating the proper chain positioning at the SEC61 channel. Regulates the exposure of nascent secretory protein chain to the cytosol during translocation into the ER. May affect the phospholipid bilaye... | Q5R7Z3 |
O32036 | TRMR_BACSU | ho5U methyltransferase | Bacillus | MTDRYEQINDYIEALLKPRPDNVKRLEAYAEEHHVPIMEKAGMEVLLQILSVKQPKKILEIGTAIGYSAIRMALELPSAEIYTIERNEKRHEEAVNNIKEFQLDDRIHVFYGDALELADAVHVTAPYDVIFIDAAKGQYQNFFHLYEPMLSPDGVIITDNVLFKGLVAEDYSKIEPKRRRRLVAKIDEYNHWLMNHPDYQTAIIPVGDGLAISKKKR | Catalyzes the methylation of 5-hydroxyuridine (ho5U) to form 5-methoxyuridine (mo5U) at position 34 in tRNAs. | O32036 |
Q86ZP5 | TBB_UNCNE | Beta-tubulin | Erysiphe | MREIVHLQTGQCGNQIGAAFWQTISGEHGLDGSGVYNGTSDLQLERTNVYFNEASGNKYVPRAVLVDLEPGTMDAVRAGPFGQLFRPDNFVFGQSGAGNNWAKGHYTEGAELVDQVLDVVRREAEGCDCLQGFQITHSLGGGTGAGMGTLLISKIREEFPDRMMATFSVVPSPKVSDTVVEPYNATLSVHQLVENSDETFCIDNEALYEICMRTLKLSNPSYGDLNHLVSAVMSGVTTCLRFPGQLNSDLRKLAVNMVPFPRLHFFMVGFAPLTSRGAHSFRAVTVPELTQQMYDPKNMMAASDFRNGRYLTCSAIFRGK... | 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-... | Q86ZP5 |
A5VNL6 | UREG1_BRUO2 | Urease accessory protein UreG 1 | Brucella | MTQKNGPLRVGIGGPVGSGKTTLTEKLCKAMRDKYSVAIITNDIYTQEDALILARRQALSEDRIIGVETGGCPHTAIREDASINLQAVVEMTRRFPDLDVVFIESGGDNLAATFSPDLADLTLYVISVCQGEEIPRKGGPGITRSDFLVINKSDLAPYVHVDLEVMEADAMRMRAKRPFGFTDLHRGKGVQEIIDFIVENGGLEPRSN | Facilitates the functional incorporation of the urease nickel metallocenter. This process requires GTP hydrolysis, probably effectuated by UreG. | A5VNL6 |
Q5E8U1 | UBID_ALIF1 | Polyprenyl p-hydroxybenzoate decarboxylase | Aliivibrio | MQYKDLRDFIGHLEDIGQLKRISHPIDPHYEMTEISDRTLRAGGPALLFENPIGYDIPVLTNLFGTPERVAIGMGRKDVLELREVGKLLAYLKEPEPPKGFKDALDKLPVFKQVLNMPTKNIRKAACQQIVWQGDDVDLDKVPVMSCWADDVAPLLTWGLTITKGPHKKRQNLGIYRQQKLSKNKVIMRWLAHRGGALDLRDWMETHPGEPFPVSVAFGADPATILGAVTPVPDTLSEYAFAGLLRGSRTEITKSISNDLEVPASAEIVLEGYIDPTEFADEGPYGDHTGYYNEVEKHHVFTVTHITMRKEPIYHSTYTG... | Catalyzes the decarboxylation of 3-octaprenyl-4-hydroxy benzoate to 2-octaprenylphenol. | Q5E8U1 |
Q6H3Z3 | YSL15_ORYSJ | Protein YELLOW STRIPE LIKE 15 | Oryza sativa | MEHADADRTRVAPEIGSLHDEDAEADPARAREMERLQPWREQVTARGVVAAALIGFVFSVIVMKIALTTGLVPTLNISAALLAFLALRGWTRALERLGFSPRPFTRQENTVVQTCAVACYTIAFGGGFGSTLLGLNKRTYELAGNSPGNVPGSYKEPGIGWMVGLLLAISFAGNLSLIPLRKALVVDYKLTYPSGTATAVLINGFHTAQGDKNAKLQLHGFLKYFGLSLFWSFFQWFYTGGNACGFVQFPTFGLKAWKQSFFFDFSLTYVGAGMICSHLVNLSTLLGAVISWGIMWPLISKHKGDWYPANIPESSMTSLY... | Involved in Fe(3+) uptake from the rhizosphere and phloem transport of iron. Plays an important role in iron homeostasis during the early stages of growth. Transports Fe(3+)-phytosiderophore, but not Fe(3+)- or Fe(2+)-nicotianamine. May not transport other chelated metals. | Q6H3Z3 |
Q06708 | VAC14_YEAST | Swollen vacuole phenotype 2 protein | Saccharomyces | MEKSIAKGLSDKLYEKRKAAALELEKLVKQCVLEGDYDRIDKIIDELCRDYAYALHQPMARNAGLMGLAATAIALGINDVGRYLRNILPPVLACFGDQNDQVRFYACESLYNIAKIAKGEILVYFNEIFDVLCKISADTENSVRGAAELLDRLIKDIVAERASNYISIVNNGSHGLLPAIKTDPISGDVYQEEYEQDNQLAFSLPKFIPLLTERIYAINPDTRVFLVDWLKVLLNTPGLELISYLPSFLGGLFTFLGDSHKDVRTVTHTLMDSLLHEVDRISKLQTEIKMKRLERLKMLEDKYNNSSTPTKKADGALIAE... | The PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Regulates the synthesis of PtdIns(3,5)P2 by positive activation of FAB1 and by controlling FIG4 localization. Required for FIG4-mediated turnover of PtdIns(3,5)P2 after hyperosmotic shock... | Q06708 |
Q9P0T7 | TMEM9_HUMAN | Transmembrane protein 9 | Homo | MKLLSLVAVVGCLLVPPAEANKSSEDIRCKCICPPYRNISGHIYNQNVSQKDCNCLHVVEPMPVPGHDVEAYCLLCECRYEERSTTTIKVIIVIYLSVVGALLLYMAFLMLVDPLIRKPDAYTEQLHNEEENEDARSMAAAAASLGGPRANTVLERVEGAQQRWKLQVQEQRKTVFDRHKMLS | Transmembrane protein that binds to and facilitates the assembly of lysosomal proton-transporting V-type ATPase (v-ATPase), resulting in enhanced lysosomal acidification and trafficking . By bringing the v-ATPase accessory protein ATP6AP2 and the v-ATPase subunit ATP6V0D1 together, allows v-ATPase complex formation and... | Q9P0T7 |
C3P1B4 | TAGU_BACAA | Polyisoprenyl-teichoic acid--peptidoglycan teichoic acid transferase TagU | Bacillus cereus group | MKKKILFWVLGILGVLIIGGGIYAYNVYSSVSNTLKEVHQPLKRDQNNSNVGEKVSKSEPVSILLLGADERGEDKGRSDSLMVITLNPKNNSMKTVSIPRDTYTEIVGKGKSDKINHAYAFGGVDMSVATVENFLNVPINYYIEVNMEGFKDIVDAVGGVDVKNDLEFTQDGHHFAKGNIHLTGDQALAFTRMRKQDPRGDFGRQMRQRQVMQGVIKKGASFSSLTGYGDVLSAIQKNVKTNLTQDQMFDMQKNYKDCLKNSEDIQIPGDGHKAADGIWYYYVPDAAKQDLTNKLRTHLEVTK | May catalyze the final step in cell wall teichoic acid biosynthesis, the transfer of the anionic cell wall polymers (APs) from their lipid-linked precursor to the cell wall peptidoglycan (PG). | C3P1B4 |
A8ACY2 | UBIE_CITK8 | Demethylmenaquinone methyltransferase | Citrobacter | MVEDSQETTHFGFQTVAKEQKADMVAHVFHSVASKYDVMNDLMSFGIHRLWKRFTIDCSGVRRGQTVLDLAGGTGDLTAKFSRLVGETGNVILADINDSMLKMGREKLRNIGVIGNVKYVQANAEALPFPDNTFDCITISFGLRNVTEKEKALRSMYRVLKPGGRLLVLEFSKPIIEPLSKAYDAYSFHILPRIGSVVANDADSYRYLAESIRMHPDQDTLKAMMQDAGFESVDYYNLTAGVVALHRGYKF | 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). | A8ACY2 |
O13059 | VSP1_TRIGA | Snake venom serine protease 1 | Trimeresurus | MVLIRVLANLLILQLSYAQKSSELVVGGDECNINEHRSLVAIFNSTGFFCSGTLINQEWVVTAAHCDSNNFKMKFGAHSQKVLNEDEQIRNPKEKFICPNKKNNEVLDKDIMLIKLDSSVSNSEHIAPLSLPSSPPSVGSVCRIMGWGSITPTKVTYPDVPYCANINLLDDAECKPGYPELLPEYRTLCAGIVQGGKDTCGGDSGGPLICNGQFHGIVSYGAHPCGQSLKPGIYTTVFDYNDWIKSIIAGNTAATCPP | Snake venom serine protease that may act in the hemostasis system of the prey. | O13059 |
P42724 | TFXB_RHILT | Trifolitoxin-processing protein TfxB | Rhizobium | MDFVQRFVIDRSFHLRYYSLDAYLYRAVDQVAWDADITHNRLFWDIWSAFMQPRSLVDAVETLSDYDPDEVAAAIEGMCESGIIEPVGLKDRQFDPLTVELSHVPQAWDYHLVSSRIDWINYLDGKDVKRQDLEQMDKHLSEEAVPSNFHKAANSRPKYDLPSLVPLTAFEFNNSASVAFGHEKAPLPNELSLDIITLLLNYAAAKTDTVNMYATGEHLRKAVPSGGARHPIEFYVVVGDEIAGIEAGVYHYNVRHHRLDAIEIASTSLKALQEASSVLPRSRSKPFGFAFIHTCRFERSMFRYREPRSYRVMQFDLGHI... | The actions of the proteins TfxB, TfxD and TfxF are implicated in the processing of the inactive trifolitoxin (TfxA) precursor into the active peptide. | P42724 |
Q2SPJ7 | TRHO_HAHCH | tRNA hydroxylation protein O | Hahella | MSQYVICALYKFVALDNFEALRAPLLEVMEKNEVKGTLLLAREGVNGTVSGTREGMDALLAWLKSDPRLADLSYKESYDENIPFYRTKVKLKKEIVTMGVEGIDPKRVVGTYVKPQDWNALITDPEVLLIDTRNDYEVQIGKFKNAINPNTETFREFPDYVKSNLDPAKHKKVAMYCTGGIRCEKSTAYLKELGFEDVYHLEGGILKYLEDVPQEESTWEGECFVFDNRVAVDHSLNKGSYDQCHACRMPISAEDMQSEHYKKGVSCPHCYDKVSEDQLRRFAAREQQIELAKSRGEEHIGSEAAKAIKKRQAEKKLKRK... | Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs. | Q2SPJ7 |
P06016 | VSAC_TRYBB | Variant surface glycoprotein ANTAT 1.1C | Trypanosoma | LHPQQALAQTAGRPLADVVGKTLCTYSKTAKRQAANLAQTLQRASSAAKQSRQAQQLAALALAKLPDYKEAAATLLIYATHKIQDAQASIENWTGENTKLVGQAMYSSGRIDELMLLLEGHREDGANGQDKTCLGAAAGGNTVNEFVKTECDTESGHNIEADNSNIGQAATTLSQESTDPEASGGASCKITANLATDYDSHANELPLLGGLLTIHNAGGFKTGQSLQTAAPTNKLISALKNKGAGVAAKLATVTSAAPTSKQELKTLLASKGERAKLQAANDEYNNWKPGAKPEDFDAHIKKVFGAEDGKDSAYALALEG... | VSG forms a coat on the surface of the parasite. The trypanosome evades the immune response of the host by expressing a series of antigenically distinct VSGs from an estimated 1000 VSG genes. | P06016 |
A1VES8 | XGPT_DESVV | Xanthine phosphoribosyltransferase | Desulfovibrio | MSTADRYRKVFPVTWEQLHRDAKALSWRLLEKGPYKGIIAIARGGLVPAAVIARELDIHLVETICISSYQWQEQTSSHKVLKTVEGRGEGWLIIDDLVDTGGTARLVREMLPEAHFATVYAKPAGRPLVDTFITEVSQDTWILFPWDSEVQYVVPLVNQPQQS | 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... | A1VES8 |
C1DH67 | TRPA_AZOVD | Tryptophan synthase alpha chain | Azotobacter | MSRLQTRFAELKQADRAALVTFVTAGDPDYETSLAILKGLPEAGADVIELGMPFTDPMADGPAIQLANIRALGAGQNLVKTLRMVRAFREGDRTTPLVLMGYFNPIHYYGVERFIAEAREAGVDGLIVVDLPPEHNEDLCDPAQAAGLDFIRLTTPTTDDKRLPRVLAGSSGFVYYVSVAGVTGAHAASLEHVEQAVARLRRHTDLPLCIGFGIRSPEHAGSVARLAEGVVVGSALVDRIAKAGSKEQAVGDVLGLCRELAEGVRRARR | The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. | C1DH67 |
P32966 | UVRC_PSEPH | Excinuclease ABC subunit C | Pseudomonas | MTDPFDPSAFLSTCSGRPGVYRMFDSDTRLLYVGKAKNLKSRLASYFRKTGLAPKTAALVGRIAQIETTITANETEALLLEQTLIKEWRPPYNILLRDDKSYPYVFLSDGEFPRFSIHRGAKKQKGKYFGPYPSAGAIRESLSLLQKTFMVRQCEDSYYKNRTRPCLQYQIKRCKAPCVGLVEAEVYAEDVRHSVMFLEGRSNALTDELSAGMEQAASTLDFEKAAELRDQISLLRRVQDQQSMEGGSGDVDVVAAFVNPGGACVHLISVRGGRVLGSKNFFPQVGIEEEVAEVMSAFLGQYFLSSPERDLPSELIVNVV... | 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. | P32966 |
O26981 | THIRX_METTH | Thioredoxin | Methanothermobacter | MMKIQIYGTGCANCQMLEKNAREAVKELGIDAEFEKIKEMDQILEAGLTALPGLAVDGELKIMGRVASKEEIKKILS | Does not function as a glutathione-disulfide oxidoreductase in the presence of glutathione and glutathione reductase. Has low thioredoxin activity in vitro. | O26981 |
B7N528 | YDIB_ECOLU | NAD-dependent shikimate 5-dehydrogenase | Escherichia | MDVTAKYELIGLMAYPIRHSLSPEMQNKALEKAGLSFTYMAFEVDNDSFPGAIEGLKALKMRGTGVSMPNKQLACEYVDELTPAAKLVGAINTIVNDDGYLRGYNTDGTGHIRAIKESGFDIKGKTMVLLGAGGASTAIGAQGAIEGLKEIKLFNRRDEFFDKALAFAQRVNENTDCVVTVTDLADQQAFAEALASADILTNGTKVGMKPLENESLVNDISLLHPGLLVTECVYNPHMTKLLQQAQQAGCKTIDGYGMLLWQGAEQFTLWTGKDFPLEYVKQVMGFGA | The actual biological function of YdiB remains unclear, nor is it known whether 3-dehydroshikimate or quinate represents the natural substrate. Catalyzes the reversible NAD-dependent reduction of both 3-dehydroshikimate (DHSA) and 3-dehydroquinate to yield shikimate (SA) and quinate, respectively. It can use both NAD o... | B7N528 |
Q56242 | UVRA_THET8 | Excinuclease ABC subunit A | Thermus | MDRIVIRGAREHNLKNISLELPRGKFIVITGVSGSGKSTLAFDTIYAEGQRRYVESLSSYARQFLGVMDKPEVESIEGLSPAISIDQKTTSHNPRSTVGTVTEIHDYLRLLFARVGQAFCPECGRPIEKQSASEITDRLLKRPPGTRAILMAPLVRGRKGEYRKLFQQLLKEGYARVRVDGVIYLLEEAQGLSLEKYEKHDIDLVIDRVVLKEEERPRIAEAVELALLRGEGLLRVLYPDTGEEELFSEKFACPEHGSVLEELEPRIFSFNSPYGACPACSGLGYRQEFDPELVVNPELSLAEGAILPWSRGRDTGRSYL... | 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. | Q56242 |
Q2S1Z6 | TRPD_SALRD | Anthranilate phosphoribosyltransferase | Salinibacter | MNTLLQTIADGDPLSRPEAEEAMATMMSGSARDEHIAALLMGLRTRGETLDELVGFTKTMREFAVSVETDDPQTIDLCGTGGDGASTFNISTTASFIAAGAGATVAKHGNRSVSSQSGSADVLEALGVQIDLEKEGVEHCLHEAGIAFLFAPFFHPAMRHVMPVRKALGVRTFFNILGPLCNPAGVTRQIVGAFDTSTAQTMVRILAELDADHVITLHADDGLDEVSISASTTLFEYDASDQNPVPRSHEVGPERHDLDRASISTLEGGTAQQNASILRNILSGEDQGPRRDVALLNAAYALHVSDQYADLDACLEAAAE... | Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA). | Q2S1Z6 |
G3X9G7 | ZN809_MOUSE | Zinc finger protein 809 | Mus | MGLVSFEDVAVDFTLEEWQDLDAAQRTLYRDVMLETYSSLVFLDPCIAKPKLIFNLERGFGPWSLAEASSRSLPGVHNVSTLSDTSKKIPKTRLRQLRKTNQKTPSEDTIEAELKARQEVSKGTTSRHRRAPVKSLCRKSQRTKNQTSYNDGNLYECKDCEKVFCNNSTLIKHYRRTHNVYKPYECDECSKMYYWKSDLTSHQKTHRQRKRIYECSECGKAFFRKSHLNAHERTHSGEKPYECTECRKAFYYKSDLTRHKKTHLGEKPFKCEECKKAFSRKSKLAIHQKKHTGEKPYECTECKKAFSHQSQLTAHRIAHS... | Transcription factor specifically required to repress retrotransposons in embryonic stem cells. Recognizes and binds retroviral DNA sequences from a large subset of mammalian retroviruses and retroelements and repress their expression by recruiting a repressive complex containing TRIM28/KAP1 . | G3X9G7 |
P18725 | ZG5_XENLA | XlCGF5.1 | Xenopus | MLQIKTEKEELDCGDDQNPKESSAVPLTDGASPEPQPQILQIKIKEEEPDYEYYLPTIKREMDPVPGAASPLAESEILQIKIKEEEPDSEDDGNSAATSAVTFRDWDNCWSDEENWDDSRPQLNQYNSDFPGSADTANTPAINTVLSRGNGLFVVNQEKRVATNSSCQSDTGHVDCSVGSEPSGFICCKCGDSFAHHSDLHTHLYACAGHNITSSFTNASEEGQHSHKNGGVLPREKPFKCTVCGKCFTLKNSLQLHHRIHTGEKPFTCTECGKSFAQSCSLQLHSRTHTGYNPYVCTECGKRFSSNSGLRRHMRTHTGV... | Binds to RNA homomers. | P18725 |
B1JVZ5 | UBIA_BURCC | 4-HB polyprenyltransferase | Burkholderia cepacia complex | MLARFPLYLRLVRMDKPIGSLLLLWPTLNALWIASDGRPRWPLLVIFTLGTLLMRSAGCAMNDYADRDFDRHVKRTADRPLTSGKIRAWEAVAIAVGLSFIAFLLILPLNTLTKELSVVALFVAGSYPFMKRFFAIPQAYLGIAFGFGIPMAFAAVQDTVPMLAWVMLVANIFWSVAYDTEYAMVDRDDDIKIGIRTSALTFGRFDVAAVMACYAATLGIYVWIGVTLGFGLAYWAGWAAAVGCALYHYTLIKDRERMPCFAAFRHNNWLGGVLFAGIAVHYLLAGN | Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of ubiquinone-8 (UQ-8) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate 3-octaprenyl-4-... | B1JVZ5 |
Q0BI45 | UBIA_BURCM | 4-HB polyprenyltransferase | Burkholderia cepacia complex | MLARFPLYLRLVRMDKPIGSLLLLWPTLNALWIASDGHPRWPLLAIFVLGTLLMRSAGCAMNDYADRDFDRHVKRTADRPLTSGKIRAWEAVAIAVVLAFISFLLIQPLNTLTKELSVVALFVAGSYPFMKRFFAIPQAYLGIAFGFGIPMAFAAVQDTVPMLAWVMLIANIFWSVAYDTEYAMVDRDDDIKIGIRTSALTFGRFDVAAVMLCYAATLGIYVWIGVTLGFGLAYWAGWAAAVGCALYHYTLIKDRERMPCFAAFRHNNWLGGVLFAGIAAHYLLAGTAGN | Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of ubiquinone-8 (UQ-8) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate 3-octaprenyl-4-... | Q0BI45 |
B3QLU3 | TAL_CHLP8 | Probable transaldolase | Chlorobaculum | MKFFIDTASLDEIKAANELGVLDGVTTNPSLIAKIVKDPANFTYADFKAHIKKICDIVDGPVSAEVTTLKAEEMIAQGEELAAIHENVVIKCPLTVEGLKAIKHFSSNGIKTNATLVFSPTQALLAAKAGADFVSPFVGRLDDISTNGMELVKQIVTIYDNYGYLTEVIVASVRNPLHVVESAMVGADIATIPYSVIKQLANHPLTDKGLEKFMEDAGVMKP | Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway. | B3QLU3 |
A8GF80 | TRPD_SERP5 | Anthranilate phosphoribosyltransferase | Serratia | MQTILEKLYRSESMNQQESQQLFSAIVRGELEPSQLAAALISMKIRGEHPEEIAGAAKALLADALPFPRPDYPFADIVGTGGDGTNSINISTASAFVAAACGAKVAKHGNRSVSSRSGSSDLLAAFGIRLDLPAEEARKALDELGVCFLFAPQYHTGFRHAMPVRQQLKTRTVFNVLGPLINPARPPLALIGVYSPELVLPIAETLRVLGYQRAAVVHGGGMDEVAIHATTHVAELNNGEIESYQLTPQSFGLQSYPLEALLGGSPEENRDILARLLQGKGDPAHAAAVAANVALLLKLFGHEDLRQNAQQALDMIHSGQ... | Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA). | A8GF80 |
Q6P2B1 | TNPO3_MOUSE | Transportin-3 | Mus | MEGAKPTLQLVYQAVQALYHDPDPSGKERASFWLGELQRSVHAWEISDQLLQIRQDVESCYFAAQTMKMKIQTSFYELPTDSHASLRDSLLTHIQNLKDLSPVIVTQLALAIADLALQMPSWKGCVQTLVEKYSNDVTSLPFLLEILTVLPEEVHSRSLRIGANRRTEIIEDLAFYSSTVVSLLMTCVEKAGTDEKMLMKVFRCLGSWFNLGVLDSNFMANNKLLALLFEVLQQDKTSSNLHEAASDCVCSALYAIENVETNLPLAMQLFQGVLTLETAYHMAVAREDLDKVLNYCRIFTELCETFLEKIVCTPGQGLGD... | Importin, which transports target proteins into the nucleus. Specifically mediates the nuclear import of splicing factor serine/arginine (SR) proteins, such as RBM4, SFRS1 and SFRS2, by recognizing phosphorylated SR domains. Also mediates the nuclear import of serine/arginine (SR) protein CPSF6, independently of CPSF6 ... | Q6P2B1 |
Q969M1 | TM40L_HUMAN | Protein TOMM40-like | Homo | MGNTLGLAPMGTLPRRSPRREEPLPNPGSFDELHRLCKDVFPAQMEGVKLVVNKVLSSHFQVAHTIHMSALGLPGYHLHAAYAGDWQLSPTEVFPTVVGDMDSSGSLNAQVLLLLAERLRAKAVFQTQQAKFLTWQFDGEYRGDDYTATLTLGNPDLIGESVIMVAHFLQSLTHRLVLGGELVYHRRPGEEGAILTLAGKYSAVHWVATLNVGSGGAHASYYHRANEQVQVGVEFEANTRLQDTTFSFGYHLTLPQANMVFRGLVDSNWCVGAVLEKKMPPLPVTLALGAFLNHWRNRFHCGFSITVG | Potential channel-forming protein implicated in import of protein precursors into mitochondria. | Q969M1 |
F6HH45 | TRM52_VITVI | tRNA methyltransferase 5 homolog 2 | Vitis | MLLDESKFDLQLKLWALRIPSQLCKVASRILNGYLLDKPRVKPITEDPTCETNRYIILSERIKNPDLSDIPEDKRDELKVLCKIEVVPYSLTLGYSYWSADHVLKQILPDGVEVPSSFETITFSLCHIAHLNITGELLPYKDVIAKVIYDKNYPRIKTVVNKVGTITNEFRVPKFEILVGKDDMVTEVKQYRATFKLDYSLVYWNSRLEHEHMRLVSQFRPGQIICDMFSGVGPFAIPAAQKGCLVYANDLNPDSIRYLKINAKINKVDDNIWAYNMDARKFISQLMEVPVHEILPEPDVPVLKATEECSIQANVQTESQ... | Specifically methylates the N1 position of guanosine-37 in various cytoplasmic and mitochondrial tRNAs. Methylation is not dependent on the nature of the nucleoside 5' of the target nucleoside. This is the first step in the biosynthesis of wybutosine (yW), a modified base adjacent to the anticodon of tRNAs and required... | F6HH45 |
C0HLF6 | TOP1C_OXYTA | Oxyopinin-1c | Oxyopes | FRGLAKLLKIGLKSFARVLKKILPKAAKAGKSLAKSLADENAIRQQNQ | Disrupts cell membranes, particularly those rich in phosphocholine, through formation of pores. Has antimicrobial activity, hemolytic activity and insecticidal activity. | C0HLF6 |
Q2HJE9 | TI17B_BOVIN | Mitochondrial import inner membrane translocase subunit Tim17-B | Bos | MEEYAREPCPWRIVDDCGGAFTMGVIGGGVFQAIKGFRNAPVGMRHRLRGSVNAVRIRAPQIGGSFAVWGGLFSTIDCGLVRLRGKEDPWNSITSGALTGAVLAARSVPLAMVGSAMMGGILLALIEGVGILLTRYTAQQFRNAPPFLEDPGQLPSKEGTPGPGYPSYQQYH | Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane. | Q2HJE9 |
B1YTH7 | UBIA_BURA4 | 4-HB polyprenyltransferase | Burkholderia cepacia complex | MLARFPLYLRLVRMDKPIGSLLLLWPTLNALWIASDGHPRWPLLAIFALGTLLMRSAGCAMNDYADRDFDRHVKRTADRPLTSGKIRAWEAVAIAVVLAFISFLLIQPLNTLTKELSVVALFVAGSYPFMKRFFAIPQAYLGIAFGFGIPMAFAAVQDTVPMLAWVMLIANIFWSVAYDTEYAMVDRDDDIKIGIRTSALTFGRFDVAAVMLCYAATLGIYVWIGVTLGFGLAYWAGWAAAVGCALYHYTLIKDRERMPCFAAFRHNNWLGGVLFAGIAAHYLLAGTAGN | Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of ubiquinone-8 (UQ-8) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate 3-octaprenyl-4-... | B1YTH7 |
B2I7X4 | TSAD_XYLF2 | tRNA threonylcarbamoyladenosine biosynthesis protein TsaD | Xylella | MKIIGIESSCDETGVAVYDTALSGSAALRAHSVYSQVALHAEYGGVVPELASRDHVRKLLPLLRQTLAEAKLSVEELDGVAYTAGPGLVGALLVGAGVARALAWALEVPAIGVHHMEGHLLSPLLEDDPPEVPFVALLVSGGHTQLVAVDAIGDYRLLGETLDDAAGEAFDKVAKLMGLPYPGGPQLAALAERGIPGRFCFTRPMVDRPGLDFSFSGLKTQVLLAWRNSDQSDAIRVDVARGFEDAVVDTLAIKCERALDTVACQTLVVAGGVGANKCLRARLQAMCRQRGGRACFPRPALCTDNGAMIAFAGALRLQAG... | 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 ca... | B2I7X4 |
A8MXK1 | VSTM5_HUMAN | V-set and transmembrane domain-containing protein 5 | Homo | MRPLPSGRRKTRGISLGLFALCLAAARCLQSQGVSLYIPQATINATVKEDILLSVEYSCHGVPTIEWTYSSNWGTQKIVEWKPGTQANISQSHKDRVCTFDNGSIQLFSVGVRDSGYYVITVTERLGSSQFGTIVLHVSEILYEDLHFVAVILAFLAAVAAVLISLMWVCNKCAYKFQRKRRHKLKESTTEEIELEDVEC | Cell adhesion-like membrane protein of the central nervous system (CNS) which modulates both the position and complexity of central neurons by altering their membrane morphology and dynamics. Involved in the formation of neuronal dendrites and protrusions including dendritic filopodia. In synaptogenesis, regulates syna... | A8MXK1 |
Q54ZX8 | Y7331_DICDI | SET and MYND domain-containing protein DDB_G0277331 | Dictyostelium | MIPNNINNRKKLKLPELFKEKYGFNKKGIELRYCDGEKGMGIFSNRKFNKGEKIMKIEPYVWSVAKHAIVCDECLKNKLDLEEGKTLKRCSNCKLVYYCSTDCQTKAWKIHKQECKILSTIPSTTDKKNINTKSTTMLLRLFIKRNLELINNNNNNNNNNNNNNNNNDNHITGQYEIIDGLLNHKDIRSDNNEYKSFSSGFCSLLGEDPQLKAPIVLEYLLKLEPNCITIPRCEASSIGLYPLMLFFNHSCKPNISIINNRKELLIITNKIIEKDEELFINYSPAICYRNERLDNLKQCFFFNCKCTLCLGEEKIKSKDL... | Probable methyltransferase. | Q54ZX8 |
Q12TL1 | TRPD_METBU | Anthranilate phosphoribosyltransferase | Methanococcoides | MKYYLQKLIDGHDLSMVESEAAMGQILESATDAQVGAFVMGMKMKGETSDEVAGFAKGMLNVANMIRPKVDGILVDTCGTGGDRHNTINISTAAAIVAAAAGVTVAKHGNHSFTSLSGSADVFKELGVKIDLEPDLVKSSIEDIGIGFMLAPKFHPAMKRMVGPRKELAVRTMFNILGPLTNPTGAKAQVIGVFDKDLCNLMAEVLKKLGKEHVMVFHGDGMDEISTLSETFVAELKDGIISNYTLTPEELGVARAKATDIVGGTPEENAHDLLYILNGEKGAKRDIVVVNAAAAIYVAGLAISIKDAIPLAEEAIDSRK... | Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA). | Q12TL1 |
Q04W54 | TRMB_LEPBJ | tRNA(m7G46)-methyltransferase | Leptospira | MSQDLEQKLWSIASGIPFVSDYFLQASPARKLKKENLFSKVFETYFLELGSGWGEVAIAMALQRRNTGFVLMEKKFDRIRHTIREIEKHSLDNVKILCVNFNWFLADVFEENLFSEILLNFPDPWPKKRHHKKRTINSKFIESLRVLLPEKGKFSFATDYGPYARKTIRLFRDSEIFKPETMEFRLERKEIPVSHFERKKRKEGKRIYYIDQILIRK | Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. | Q04W54 |
Q21VT9 | YCIB_ALBFT | Inner membrane-spanning protein YciB | Rhodoferax | MKILIDFFPILLFFGAYKAYDIYIGTGVLMAATLIQMGLIYTLDRKLTVMHKITLALILVFGTLTLVLHDERFIKWKPTVLYAAMAIGLALAVWVWKKNFLKLLLGSQMELPDPVWMRLNMVWVVYCVFMSLINAYVAAYYSTEAWVNFKLWGYAFPLVFIVAQGFYISRYLKTDEPKA | Plays a role in cell envelope biogenesis, maintenance of cell envelope integrity and membrane homeostasis. | Q21VT9 |
A5PJS6 | UBP10_BOVIN | Ubiquitin-specific-processing protease 10 | Bos | MALRSPQYIFGDFSPDEFNQFFVTPRASVELPPYGGTVLCGAQAADDLPDGHDYQRIEFGVNEVIEPSDTLPRTPNYSISSTLNPQAPEFILSCTTSKKLPDDIDKEVNYSSANCQYPGPALALDGGSPAEAEALENDGVSGGLGQRERKKKKKRPPGYYSYLKDGGEGGPSAEALVNGHAGPAVSNSVGAEDTDLMGDVPTAGTPRTWGSPQDATDFVSDAGPAGAFPGALDGGARTAGQLEGCPGADSEASCLPAEAGRDTLLRTAVAQPSVGTDTTENLGVTNGQILESLGEGTAANGVELHTVESSDSDPAKAESA... | Hydrolase that can remove conjugated ubiquitin from target proteins such as p53/TP53, BECN1, SNX3 and CFTR. Acts as an essential regulator of p53/TP53 stability: in unstressed cells, specifically deubiquitinates p53/TP53 in the cytoplasm, leading to counteract MDM2 action and stabilize p53/TP53. Following DNA damage, t... | A5PJS6 |
Q07VB6 | UBIG_RHOP5 | 3-demethylubiquinone 3-O-methyltransferase | Rhodopseudomonas | MAMQSETPGNPASTVDPAEIAKFSKLSAEWWDPTGRMAPLHKINPHRVAFIRDAACRKFDRNPKSLNSLAGLRMIDIGCGAGLLCEPFTRLGAQVIGIDPSATNIAAAKVHAEKSRLLIDYRNTTAEAMDPRERFDIVLAMEVIEHVTDVGAFLGRCAAMMKPTGLMVVATLNRNWKSFALAIVGAEYVMRWLPRGTHQWDKFVTPEELTRHLQNSRLAVTEQAGLVYNPLADKWNLSADMDVNYMMVAESAG | O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway. | Q07VB6 |
P58923 | U7A_CONTU | Conotoxin TVIIA | Gastridium | SCSGRDSRCPPVCCMGLMCSRGKCVSIYGE | By structural similarity with conotoxin GS, may inhibit the sodium channel (Nav). No effect was observed upon intracranial injections into mice and intraperitoneal injections into goldfish (25 ug). | P58923 |
A1W560 | UPPP_ACISJ | Undecaprenyl pyrophosphate phosphatase | unclassified Acidovorax | MDTLLLLKAAIMGVVEGLTEFLPISSTGHLILAGSLLGFDDAKAKVFDIAIQTGAIFAVILVYWQRIRATLVALPTERQARRFALNVLIGFLPAVLLGLLLGKAIKAHLFTPVVVASTFILGGFVILWAERRQQAAVRIHAVDDMTPLDALKVGLVQCLAMVPGTSRSGATIIGGMLLGLSRKAATDYSFFLAIPTLIGAGVYSLYKERALLSAADIPLFAVGLVFSFISAWLCVRWLLRYISLHSFVPFAWYRIAFGLVVLATAWSGLVTWAE | Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin. | A1W560 |
B3STU4 | VCL_CARIL | Cariv | Carya | MVTKAKIPLFLFLSALFLALVCSSLALETEDLSNELNPHHDPESHRWEFQQCQERCQHEERGQRQAQQCQRRCEEQLREREREREREEIVDPREPRKQYEQCRETCEKQDPRQQPQCERRCERQFQEQQERERRERRRGRDDDDKENPRDPREQYRQCEEHCRRQGQGQRQQQQCQSRCEERFEEEQRRQEERERRRGRDNDDEENPRDPREQYRQCQEHCRRQGQGQRQQQQCQSRCEERLEEEQRKQEERERRRGRDEDDQNPRDPEQRYEQCQQQCERQRRGQEQQLCRRRCEQQRQQEERERQRGRDRQDPQQQYH... | Seed storage protein. | B3STU4 |
P31816 | TPM_LOCMI | Tropomyosin | Locusta | MDAIKKKMQAMKLEKDNALDRALLCEQQARDANLRAEKAEEEARALQKKIQTIENDLDQTQESLGQVMAKLEEKEKALQNAESEVAALNRRIQLLEEDLERSEERLATATAKLAEASQAADESERARKILENRSLADEERMDALENQLKEARFLAEEADKKYDEVARKLAMVEADLERAEERAEAGESKIVELEEELRVVGNNLKSLEVSEEKANQREEEISNRLRTLTTRLKEAEARAEFAERSVQKLQKEVDRLEDELVIEKEKYKIIGDDLDSAFVELIL | Tropomyosin, in association with the troponin complex, plays a central role in the calcium dependent regulation of muscle contraction. | P31816 |
Q86TV6 | TTC7B_HUMAN | Tetratricopeptide repeat protein 7-like-1 | Homo | MATKKAGSRLETEIERCRSECQWERIPELVKQLSAKLIANDDMAELLLGESKLEQYLKEHPLRQGASPRGPKPQLTEVRKHLTAALDRGNLKSEFLQESNLIMAKLNYVEGDYKEALNIYARVGLDDLPLTAVPPYRLRVIAEAYATKGLCLEKLPISSSTSNLHVDREQDVITCYEKAGDIALLYLQEIERVILSNIQNRSPKPGPAPHDQELGFFLETGLQRAHVLYFKNGNLTRGVGRFRELLRAVETRTTQNLRMTIARQLAEILLRGMCEQSYWNPLEDPPCQSPLDDPLRKGANTKTYTLTRRARVYSGENIFC... | Component of a complex required to localize phosphatidylinositol 4-kinase (PI4K) to the plasma membrane. The complex acts as a regulator of phosphatidylinositol 4-phosphate (PtdIns(4)P) synthesis. In the complex, plays a central role in bridging PI4KA to EFR3B and FAM126A, via direct interactions . | Q86TV6 |
Q5X149 | TRHO_LEGPA | tRNA hydroxylation protein O | Legionella | MKDIIIASFYKFIPLNDFESLREPILTKMHEIGIKGTIILAHEGVNGGFAGNREQMNVFYDYLRSDSRFADLHFKETYDNKNPFDKAKVKLRKEIVTMGVQKVDPSYNTGTYLSPEEWHQFIQDPNVILLDTRNDYEYELGTFKNAINPDIENFREFPDYVQRNLIDKKDKKIAMFCTGGIRCEKTTAYMKEQGFQHVYQLHDGILNYLESIPESESLWEGKCFVFDDRVAVDQKLDRVYPQLPQDYKYEREQK | Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs. | Q5X149 |
Q1QZV1 | TAL_CHRSD | Transaldolase | Chromohalobacter | MTQLEALKQLSMVVADTGDLEAIKRYQPHDATTNPSLILKAFELPGYQALIDETLAQVKADIADPQARVDEAVDRLSVAMGSEITQLIPGRVSTEVAAKLSFDREASIAKAHRLIELYEQRGIGRERVLIKLASTWEGIRAAEQLEKEGIQCNLTLLFSEAQARACFDAGVYLISPFVGRVTDWYKQKTGQEYTPEEDPGVVFVRKVCDIASRYRYDTVVMGASFRTKGQILGLAGCNRLTISPALLEELESEEGDIERKISDVGDASERLAPIDEAAFRWGLNQDAMATEKLAEGIRRFADDQATLEEKLAARLG | Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway. | Q1QZV1 |
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