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 |
|---|---|---|---|---|---|---|
B0B846 | YIDD_CHLT2 | Putative membrane protein insertion efficiency factor | Chlamydia | MQTSRISSFFRGLVHLYRWAISPFLGAPCRFFPTCSEYALVALKKHPLRKSLFLIAKRLLKCGPWCIGGIDLVPRTSVEEYLSSPTPLAESPDDRTVPHTQETS | Could be involved in insertion of integral membrane proteins into the membrane. | B0B846 |
B7GKQ8 | THIE_ANOFW | Thiamine-phosphate pyrophosphorylase | Anoxybacillus | MMKQKLSLYFVMGSIDCTKDPLAVLDEAIKGGITMFQFREKGKGALTGIEKYRLAEKLLERCRMYNIPFIVNDDVDLALALQADGVHVGQEDEVAERVRDRIGDKYLGVSVHNLNEVKKALAACADYVGLGPIFPTVSKEDAKQACGLTMIEHIRAHEKRVPLVAIGGITEQTAKQVIEAGADGIAVISAICRAEHIYEQTKRLYEMVMRAKQKGDR | 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). | B7GKQ8 |
P12321 | TRPD_SERMA | Anthranilate phosphoribosyltransferase | Serratia | MQPILEKLYRAESMSQQESQQLFSAIVRGELEPSQLAA | Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA). | P12321 |
Q8KB57 | TIG_CHLTE | PPIase | Chlorobaculum | MQKNITNVSEIAQELEIILTAEEYQPEYDQQLEEARKSVRIKGFRQGHVPVGMLKRIIGPSIEAEVAEKMASKYFAAIAEEEKINPASRAQIESYNYEDGKLTIKISYEIHPEFELKDFSEYTFTQAEYTISDEDVDREIKLILRGHGTMVTSEDAAAEGDTVIGDVTKLDADGADIEGSKNENHHFNLEYLPADNPFRMALEGKKAGDVVDVTVKPKEEGGETNRFRIEIKEVKHLELPELDDELVKEISQQRFEKVEDFRNDIRLQLQAHFSDKSEYDLLEAISSKLIEEHPVPTPSAMVAHFQNILLENAKRQVGGQ... | 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. | Q8KB57 |
Q9WTT4 | VATG2_MOUSE | Vacuolar proton pump subunit G 2 | Mus | MASQTQGIQQLLQAEKRAAEKVADARKRKARRLKQAKEEAQMEVEQYRREREQEFQSKQQAAMGSQGNLSAEVEQATRRQVQGMQSSQQRNRERVLAQLLGMVCEVRPQVHPNYRVTV | Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types,... | Q9WTT4 |
Q0J932 | YSL10_ORYSJ | Protein YELLOW STRIPE LIKE 10 | Oryza sativa | MARSGRERRDQEEEAAVVSVERVFEGRVVPGWKEQVTLRALAVSALLGAMFSVIVMKLNLTTGIIPSLNVSAGLLGFFLLTSWTKLLDKAGVASVRPFTRQENTVVQTCVVACSGIAFSGGFGSYIFAMSDRISDQSGEARDEHNIKNPSLGWMIGFLFIVSFLGLFSVVPLRKIMIIDYKLIYPSGTATAHLINSFHTPQGAKLAKMQVKMLGKFFVMSFSWGFFQWFYTGGDGCGFMSFPTLGLEAYRNKFFFDFSATYVGVGMICPYLVNISVLLGGVMSWGIMWPLIEHKKGDWYPADLKPSSLRGIVGYRVFISI... | May be involved in the transport of nicotianamine-chelated metals. | Q0J932 |
Q5QWR0 | Y1848_IDILO | Nucleoid-associated protein IL1848 | Idiomarina | MFKGGMGNMMKQAQQMQERMQQAQEEVANMEVTGEAGAGLVKITMLGNHNVKRVSIDPSLMEDDQEMLEDLIAAATNDAVRRVEETSKERMSEITGGMGLPPGFKMPF | Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection. | Q5QWR0 |
A0A1L1QJU3 | TP1A_HADIN | Double-knot toxin | Hadronyche | NECIRKWLSCVDRKNDCCEGLECYKRRHSFEVCVPIPGFCLVKWKQCDGRERDCCAGLECWKRSGNKSSVCAPIT | This toxin potently and selectively inhibits ASIC1a (IC(50)=0.4 nM on rASIC1a and IC(50)=0.52 nM on hASIC1a), an isoform of the gene ASIC1 . It incompletely inhibits ASIC1a activation in a pH-independent and slowly reversible manner (Tau(off)=14.2 min for rASIC1a and 31.8 min for hASIC1a) . This toxin acts by binding t... | A0A1L1QJU3 |
Q8G4D1 | TSAD_BIFLO | tRNA threonylcarbamoyladenosine biosynthesis protein TsaD | Bifidobacterium | MSEPVVLGIESTCDETAAAIVRGRELLSNVVASSMEEHARYGGVIPEIASRAHAEAFVPCVSKALVDANMTLADVDAIAVSAGPGLAGCLAVGVSGAKALAWAANKPIYGINHVIGHIAVTQLQFGPFPKDTLALIVSGGHTSLLHVEDMPRKIDVVGTTLDDAAGECFDKVARLLGFPYPGGPHIDRHGQNGDPHAIKVPMGLTQGKAGAAHPYDFSFSGVKTAVARWVESEQAAGHEIPVDDVCASLADSVATVLARKAMRGCRQYDSNTLIVGGGFSANSQLRAKLLEFGENYGVDVRIPQIKLCTDNGAMVAMLGV... | 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... | Q8G4D1 |
Q6LLQ8 | YIHI_PHOPR | Der GTPase-activating protein YihI | Photobacterium | MTRKKRSRGVGSEGPAVFREKSTTQVDVEARKSQKDKKRKGLKSGNRNAEALDPKHYANGQKKDPRLGSKKPIPLVVEKKPTTKKERRLSAEQELDMLENDAQLMVLLDRIEAGEKLGAGLQKQVDQKLDRIEHLMGRLGLLEVEEPEVTEEAPVRKGAKTDEDLLDQFENMDLDSFGKE | A GTPase-activating protein (GAP) that modifies Der/EngA GTPase function. May play a role in ribosome biogenesis. | Q6LLQ8 |
O66953 | TRUA_AQUAE | tRNA-uridine isomerase I | Aquifex | MPNYLLRLAFVGTNFYGWQVQPNLRTVQGEIQKALSQILCEDVKVTGCCRTDSGVHALDYIANFKTQKDFPEEKLLKALNGILPKDVGVYAVKKVSEEFNARYSVKGKVYLYKIWNSEVRNPFLYPFSWQVKREINTEVLRNILKKFEGTHDFRALTKLEEERNTVINLEEVSLNVEYPLIEIRLKASHFLRYMVRRIVGTAVKISLGLYSEEVLEELLQGKGNSPYTAPPQGLHLEKVLL | Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs. | O66953 |
Q9KDN6 | YHAM_HALH5 | 3'-5' exoribonuclease YhaM | Halalkalibacterium (ex Joshi et al. 2022) | MSRGILYYQVGEALESYFLIKSATKAVASNGKPFLTLILSDHTGEIEAKLWGCSPEDEATFVSGAIVHISGQLSEYRGRQQLKIGSIRPTTAMDQVKVSDFVRSAPLSPDDMLEQITQYIFEMKNPKIQRMTRHLLKKHQTAFLEYPAATTNHHEFVSGLAYHVVCMLNVAKSLAALYPTLDTDLLYAGIILHDLGKVKELSGPIDTTYTIEGKLLGHISILVNEIGETANELGIEGEEVIILQHLVLAHHSKGEWGSPKPPLIREAEILHMIDNIDAKMNMMDRALERVQPGEFSERIKAMDNRSFYKPNFHEPPLDLS | Shows a 3'-5' exoribonuclease activity. | Q9KDN6 |
B2FNZ6 | TRUA_STRMK | tRNA-uridine isomerase I | Stenotrophomonas maltophilia group | MRYALGVEYDGSDFRGWQNLGEGGPSVQASLEQALSSVADTPLQVVCAGRTDAGVHGQCQVVHFDTDVVRDPRAWMLGTTTRLPRSIAVRWCVPVADDFHARFSARARRYRYRLLNREVRPALDRQTLSWERRALDETLMHAAGQALIGENDFSAFRSVQCQALHARRELQSLQVSRQGEVIEVAVQGNAFLHHMVRNIVGSLILVGSGEKPVEWIAELLAGRDRTVAGPTAPPQGLVFLGPLYPDNWHLPAEVTL | Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs. | B2FNZ6 |
Q96BR6 | ZN669_HUMAN | Zinc finger protein 669 | Homo | MVSGLRLASRSGEEGWLKPAVARLGPPRHRLRNLRTESPWRSRGSVLFCSGPGRAGRAAEPLHPVCTCGRHFRRPEPCREPLASPIQDSVAFEDVAVNFTQEEWALLDSSQKNLYREVMQETCRNLASVGSQWKDQNIEDHFEKPGKDIRNHIVQRLCESKEDGQYGEVVSQIPNLDLNENISTGLKPCECSICGKVFVRHSLLNRHILAHSGYKPYGEKQYKCEQCGKFFVSVPGVRRHMIMHSGNPAYKCTICGKAFYFLNSVERHQRTHTGEKPYKCKQCGKAFTVSGSCLIHERTHTGEKPYECKECGKTFRFSCS... | May be involved in transcriptional regulation. | Q96BR6 |
O32123 | YUTH_BACSU | Endospore coat-associated protein YutH | Bacillus | MVKGTIKEKYGIHIRQLSMYQHTYQCFQTPNSYFLIVPVSQFSETELAELYYMSQYLQEQSDPYVSVFIFTKEGELTFEHEGKTYALLKAAPPYSNRAFSIGAELAEFHRKGRGYPYEVKAAGRIGQWKDLWGKRIDQLEAFWQRKVQTPPHEPFDKKMIESFPYYLGLSENAIQYLVDTELDDKPQAADSGTICHQRMERHTWSPESLIRIPADWVFDHASRDLAEYMRHTFLHHRQDFNQQGFLFLQEYEQVTPLSSFSKRLLYSRLLFPLHYFEIVESYYMSSESEKHYFEEQLDFILNDCGRYEQFLNTAQEFMNM... | Involved in sporulation. | O32123 |
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