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 | MQKNITNVSEIAQELEIILTAEEYQPEYDQQLEEARKSVRIKGFRQGHVPVGMLKRIIGPSIEAEVAEKMASKYFAAIAEEEKINPASRAQIESYNYEDGKLTIKISYEIHPEFELKDFSEYTFTQAEYTISDEDVDREIKLILRGHGTMVTSEDAAAEGDTVIGDVTKLDADGADIEGSKNENHHFNLEYLPADNPFRMALEGKKAGDVVDVTVKPKEEGGETNRFRIEIKEVKHLELPELDDELVKEISQQRFEKVEDFRNDIRLQLQAHFSDKSEYDLLEAISSKLIEEHPVPTPSAMVAHFQNILLENAKRQVGGQFPKGFDEREFFNAMKPNAEKHARWLLISQKIAKENNLEVTDEDIKAFAEKEAEKEPSLTVDQLLNTYLSTEFKDYIIDTILKEKIYDVIKSKVTITKEATPVPAHN | 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, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment. | Q9WTT4 |
Q0J932 | YSL10_ORYSJ | Protein YELLOW STRIPE LIKE 10 | Oryza sativa | MARSGRERRDQEEEAAVVSVERVFEGRVVPGWKEQVTLRALAVSALLGAMFSVIVMKLNLTTGIIPSLNVSAGLLGFFLLTSWTKLLDKAGVASVRPFTRQENTVVQTCVVACSGIAFSGGFGSYIFAMSDRISDQSGEARDEHNIKNPSLGWMIGFLFIVSFLGLFSVVPLRKIMIIDYKLIYPSGTATAHLINSFHTPQGAKLAKMQVKMLGKFFVMSFSWGFFQWFYTGGDGCGFMSFPTLGLEAYRNKFFFDFSATYVGVGMICPYLVNISVLLGGVMSWGIMWPLIEHKKGDWYPADLKPSSLRGIVGYRVFISISLILGDGLYNFLKVMTRTTTALVMQVRAMMSEPTLPVSGGGGQTPEETFDDKRRTELFLKDQIPNWLALSAYVVIAVVSIATVPRIFHQLRWYHVAVSYVVAPVLAFCNAYGCGLTDWSLATTYGKLAIFTVGAWADASDGGIIAGLAACGVMIGIVSTASDLTQDFKTGYMTLASPRSMFVSQVIGTAMGCVIAPSVFWLFYKAFHDIGMPGSEYPSPNALVYRNMAILGVQGLGSLPKHCLDLCIGFFVAAIAVNLARDLAAPKVARFLPLPMAMAIPFYLGPYFGIDMCIGSLIRFVWDRLDGARAKAFAPPVASGLICGDGIWTLPQSVLALAGVKPPICMKFLSRTTNIKVDAFIAKLPSS | 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 to and stabilizing the closed state of the channel, thereby impeding the transition into a conducting state . This toxin may bind to the acidic pocket of ASIC1a, since mutation of a key residue of this pocket (Arg-350) abolishes the ability of the toxin to inhibit ASIC1a . In addition, it shows antiparasitic activities, since it moderately inhibits the larval development of the major pathogenic nematode of ruminants (H.contortus, IC(50)=22.9 uM) . In vivo, this toxin protects the brain from neuronal injury when administered up to 8 hours after stroke onset . | A0A1L1QJU3 |
Q8G4D1 | TSAD_BIFLO | tRNA threonylcarbamoyladenosine biosynthesis protein TsaD | Bifidobacterium | MSEPVVLGIESTCDETAAAIVRGRELLSNVVASSMEEHARYGGVIPEIASRAHAEAFVPCVSKALVDANMTLADVDAIAVSAGPGLAGCLAVGVSGAKALAWAANKPIYGINHVIGHIAVTQLQFGPFPKDTLALIVSGGHTSLLHVEDMPRKIDVVGTTLDDAAGECFDKVARLLGFPYPGGPHIDRHGQNGDPHAIKVPMGLTQGKAGAAHPYDFSFSGVKTAVARWVESEQAAGHEIPVDDVCASLADSVATVLARKAMRGCRQYDSNTLIVGGGFSANSQLRAKLLEFGENYGVDVRIPQIKLCTDNGAMVAMLGVNLVEAGVAPSAPDFPIDSAMPLTKVSM | Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction. | 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 | MVSGLRLASRSGEEGWLKPAVARLGPPRHRLRNLRTESPWRSRGSVLFCSGPGRAGRAAEPLHPVCTCGRHFRRPEPCREPLASPIQDSVAFEDVAVNFTQEEWALLDSSQKNLYREVMQETCRNLASVGSQWKDQNIEDHFEKPGKDIRNHIVQRLCESKEDGQYGEVVSQIPNLDLNENISTGLKPCECSICGKVFVRHSLLNRHILAHSGYKPYGEKQYKCEQCGKFFVSVPGVRRHMIMHSGNPAYKCTICGKAFYFLNSVERHQRTHTGEKPYKCKQCGKAFTVSGSCLIHERTHTGEKPYECKECGKTFRFSCSFKTHERTHTGERPYKCTKCDKAFSCSTSLRYHGSIHTGERPYECKQCGKAFSRLSSLCNHRSTHTGEKPYECKQCDQAFSRLSSLHLHERIHTGEKPYECKKCGKAYTRSSHLTRHERSHDIEAGCSDSAYNPSTLGGQGVWIA | May be involved in transcriptional regulation. | Q96BR6 |
O32123 | YUTH_BACSU | Endospore coat-associated protein YutH | Bacillus | MVKGTIKEKYGIHIRQLSMYQHTYQCFQTPNSYFLIVPVSQFSETELAELYYMSQYLQEQSDPYVSVFIFTKEGELTFEHEGKTYALLKAAPPYSNRAFSIGAELAEFHRKGRGYPYEVKAAGRIGQWKDLWGKRIDQLEAFWQRKVQTPPHEPFDKKMIESFPYYLGLSENAIQYLVDTELDDKPQAADSGTICHQRMERHTWSPESLIRIPADWVFDHASRDLAEYMRHTFLHHRQDFNQQGFLFLQEYEQVTPLSSFSKRLLYSRLLFPLHYFEIVESYYMSSESEKHYFEEQLDFILNDCGRYEQFLNTAQEFMNMRAQKLFVPRVSWLGKGSSR | Involved in sporulation. | O32123 |