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
|
|---|---|---|---|---|---|---|
Q5FL49
|
TPIS_LACAC
|
Triose-phosphate isomerase
|
Lactobacillus
|
MSRTPIIAGNWKLHMNPEQTTEFVDAVKGKLPDPSKVESLICAPAVDLDALRKAAEGSNLHIGAENCYFEDEGAYTGETSPKVLKEMGIDYVIIGHSERRGYFHETDEDINKKAKAIFANGMKPIICCGESLETREANKQEDWVVAQIKAALDGLTAEQVSSLVIAYEPIWAIGTGKTASSDQAEEMCKTIRETVKDLYNEETAENVRIQYGGSVKPANVKELMSKPDIDGGLVGGASLDPESFLALVNYQD
|
Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
|
Q5FL49
|
P33226
|
TORC_ECOLI
|
Cytochrome c-type protein TorC
|
Escherichia
|
MRKLWNALRRPSARWSVLALVAIGIVIGIALIVLPHVGIKVTSTTEFCVSCHSMQPVYEEYKQSVHFQNASGVRAECHDCHIPPDIPGMVKRKLEASNDIYQTFIAHSIDTPEKFEAKRAELAEREWARMKENNSATCRSCHNYDAMDHAKQHPEAARQMKVAAKDNQSCIDCHKGIAHQLPDMSSGFRKQFDELRASANDSGDTLYSIDIKPIYAAKGDKEASGSLLPASEVKVLKRDGDWLQIEITGWTESAGRQRVLTQFPGKRIFVASIRGDVQQQVKTLEKTTVADTNTEWSKLQATAWMKKGDMVNDIKPIWAYADSLYNGTCNQCHGAPEIAHFDANGWIGTLNGMIGFTSLDKREERTLLKYLQMNASDTAGKAHGDKKEEK
|
Part of the anaerobic respiratory chain of trimethylamine-N-oxide reductase TorA. Acts by transferring electrons from the membranous menaquinones to TorA. This transfer probably involves an electron transfer pathway from menaquinones to the N-terminal domain of TorC, then from the N-terminus to the C-terminus, and finally to TorA. TorC apocytochrome negatively autoregulates the torCAD operon probably by inhibiting the TorS kinase activity.
|
P33226
|
A2T334
|
YCF3_ANGEV
|
Photosystem I assembly protein Ycf3
|
Angiopteris
|
MPRSQRNDNFIDKTFTIVADILLRVIPTTQREKEAFTYYRDGMSAQSEGEYAEALQNYYKAMRLEIDPYDRSYILYNIGLIHTSNGEHAKALEYYSQALERNPSLPQAFNNMAVICHYRGEQAIQQGDPETSEAWFDQAAEYWKQAIALAPSNYIEAQNWLKITGRLKEWV
|
Essential for the assembly of the photosystem I (PSI) complex. May act as a chaperone-like factor to guide the assembly of the PSI subunits.
|
A2T334
|
B0TP00
|
Y1591_SHEHH
|
Nucleoid-associated protein Shal_1591
|
Shewanella
|
MFGKGGMGNLMKQAQQMQDKMAKVQEEIARMEVTGEAGAGLVKVTMTGSHSVRKVDIDASLLEDDKEMLEDLIAAACNDAARRVEENQKEKMAEVTGGMQLPPGMKMPF
|
Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection.
|
B0TP00
|
Q4QJX4
|
UVRB_HAEI8
|
Excinuclease ABC subunit B
|
Haemophilus
|
MSEKINTKPFILHSDFRPSGDQPQAIEKLAENLTDGLAHQTLLGVTGSGKTFTIANVIAQLNRPAMLLAPNKTLAAQLYAEMKAFFPENAVEYFVSYYDYYQPEAYVPSSDTFIEKDASINDQIEQMRLSATKSFLERRDTIVVASVSAIYGLGDPDSYLQMMLHLQQGAIIDQRQILAKLAELQYTRNDQAFQRGTFRVRGEIIDIFPAESDDRAVRIELFDDEIERLSLFDPLTGSSFGAVPRFTIYPKTHYVTPRERILDAIENIKKELVSRREYFIKEHKLLEEQRISQRTQFDIEMMNELGYCSGIENYSRYLSGRNEGEPPPTLFDYMPSDAILIIDESHVTVPQIGGMYRGDRSRKETLVEYGFRLPSALDNRPLRFEEFERLAPQTIYVSATPGPYELEKSGTEIIDQVVRPTGLLDPLIEIRPVSIQVDDLLSEARQRADKNERVLVTTLTKKMAEDLTDYLDEHGIRVRYLHSDIDTVERVEIIRDLRLGEFDVLVGINLLREGLDIPEVSLVAILDADKEGFLRSERSLIQTIGRAARNLNGKAILYADSITKSMEKAITETNRRREKQIKYNEEHGIVPQALNKKVGELLDIGQGANQKAKANKQRGKMAAEPTALYNAPKNAKEYQQQIKKLEQQMYKFAQDLEFEKAAAIRDQLHQLREQFVFDN
|
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.
|
Q4QJX4
|
Q3JEI2
|
TYSY_NITOC
|
Thymidylate synthase
|
Nitrosococcus
|
MKPYLELIQKILDTGVERDDRTGTGTWSIFGHQMRFDLRQGFPLITTKKLHIRAIFIELLWFLRGETNVKYLHDHGVTIWDEWADEQGELGPIYGYQWRSWPLPDGGYLDQMAKTLTQIRNHPHSRRHVVVAYNPACVDEMALPPCHALFQFYVAQGRLSCQLYQRSADVFLGVPFNIASYALLTHLIAQQCDLDVGEFVWTGGDVHLYRNHLEPARLQLTREPLSLPHLRIKRRPPSLFEYQYDDLEIVDYQSYPAIKAAISV
|
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.
|
Q3JEI2
|
Q43848
|
TKTC_SOLTU
|
Transketolase, chloroplastic
|
Solanum
|
MASSSSLTLSQVIFSPSLPRHGSSSSSSPSLSFSTFSGLKSTPFTSSHRRILPSTTVTKQQFSVRASAAVETLEKTDAAIVEKSVNTIRFLAIDAVEKANSGHPGLPMGCAPMGHILYDEVMKYNPKNPYWFNRDRFVLSAGHGCMLQYALLHLAGYDSVQEDDLKSFRQWGSRIPGHPENFETPGVEVTTGPLGQGIANAVGLAVAEKHLAARFNKPDAEIVDHYTYVILGDGCQMEGISNEVCSLAGHWGLGKLIAFYDDNHISIDGDTEIAFTEDVSARFESLGWHVIWVKNGNTGYDEIRAAIKEAKAVKDKPTMIKVTTTIGFGSPNKANSYSVHGSGLGAKEVEATRNNLGWPYEPFHVPEDVKSHWSRHTPEGAALETEWNAKFAEYEKKYAEEAADLKSIITGELPAGWEKALPTYTPESPADATRNLSQQNLNALAKVLPGFLGGSADLASSNMTLLKMFGDFQKNTPEERNLRFGVREHGMGAICNGIALHSLGLIPYCATFFVFTDYMRGAMRISALSEAGVIYVMTHDSIGLGEDGPTHQPIEHLASFRAMPNILMFRPADGNETAGAYKVAVLKRKTPSILALSRQKLPQLAGTSIEGAAKGGYIVSDNSSGNKPDVILIGTGSELEIAVKAAEELKKEGKTVRVVSFVCWELYDEQSAEYKESVLPSSVTARVSIEAGSTFGWQKFVGDKGKAIGIDGFGASAPADKIYKEFGITAEAVVAAAKQVS
|
Catalyzes the reversible transfer of a two-carbon ketol group from fructose-6-phosphate or sedoheptulose-7-phosphate to glyceraldehyde-3-phosphate to yield xylulose-5-phosphate and erythrose-4-phosphate or ribose-5-phosphate, respectively.
|
Q43848
|
B5QYE5
|
THIG_SALEP
|
Thiazole synthase
|
Salmonella
|
MLRIADKTFDSHLFTGTGKFASSQLMVEAIRASGSQLVTLAMKRVDLRQHNDAILAPLIEAGVTLLPNTSGAKTAEEAIFAAQLAREALGTNWLKLEIHPDARWLLPDPIETLKAAEALVKQGFVVLPYCGADPVLCKRLEEVGCAAVMPLGAPIGSNQGLETKTMLEIIIQQATVPVVVDAGIGVPSHAAQALEMGADAVLVNTAIAVADDPVMMATAFRLAVEAGLLARQAVPGNRSTYASATSPLTGFLEALA
|
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.
|
B5QYE5
|
P54078
|
TATC_MYCLE
|
Sec-independent protein translocase protein TatC
|
Mycobacterium
|
MRACDLLKRIKQHYRRSRTNPDATMSLIDHLTELRTRLLISLAAIVVTTIFGFIWYSHSIFGLESLGEWLRRPYCSLPQSARADISPDGQCRLLATAPFDQFMLRIKVGMAAGIVLASPVWFYQLWAFITPGLYTKERRFTVAFVVPAAVLFAGGTVLAYLVLSKALGFLLIVGSGVQVTALSGDRYFGFLLNLLVVFGVSFEFPLLIVMLNIAGLLTYQRLKSWRRGLIFAMFVFAAVFTPGSDPFSMTALGAALTVLLELAIQLVRLHDKRRVKHEALIADDEASVIEPPSSIPERSYTATRSHDDVT
|
Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. Together with TatB, TatC is part of a receptor directly interacting with Tat signal peptides.
|
P54078
|
Q9V0K1
|
UPP_PYRAB
|
UPRTase
|
Pyrococcus
|
MIEDKRWKGVYSFEDSPFIMEILTQLRDKNTDSIEFRKGLVKLGRYMGYELTKTMEVEKVKVETPLEETEGIIVKDRRNVVIITVLRAAIPLMEGLIKVFEHARVGIVSAVRGKAPEFKIEMDYVKIPQIKPEDTVIVADPMIATGSTLTRVLGEVKKYGEPKRTIVLGVLAAPEGISKIKSEFPDVEIFVAKIDRELDHKGYILPGLGDAGDRAFGEPLKLSTLPQVHHIE
|
Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate.
|
Q9V0K1
|
Q5XAG6
|
TRMB_STRP6
|
tRNA(m7G46)-methyltransferase
|
Streptococcus
|
MRVRKRKGAEEHLANNPHYVILNPEDAKGRWHDVFGNDRPIHIEVGSGKGGFITGMALKNPDINYIGIDIQLSVLSYALDKVLASEVSNVKLLRVDGSSLTNYFEDGEVDMMYLNFSDPWPKTKHEKRRLTYKDFLDTYKRILPEHGEIHFKTDNRGLFEYSLASFSQYGMTLRQIWLDLHASNYEGNVMTEYEEKFSNKGQVIYRVEANF
|
Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
|
Q5XAG6
|
Q8FZV9
|
UREG2_BRUSU
|
Urease accessory protein UreG 2
|
Brucella
|
MKKIPRIGVGGPVGSGKMAIIEAVVPILIKLGYRILVITNDIVTTEDAKHVQRTLKGVLIEDRIVGVETGGCPHTAVREDPSMNLAAVEEMEAKFPDTDLVLLESGGDNLTLTFSPALIDFFIYVIDVAAGDKIPCKNGPGISQSDILVINKTDLAPYVGASLQVMDDDSRMMRGKKPFVFTNCKTNEGIDDLVHLIRENVLFDTEVSKESA
|
Disrupting the ure2 operon has no effect on urease activity, or pathogen survival in BALB/c mice when inoculated by gavage, but confers slightly enhanced resistance to low pH killing in vitro.
|
Q8FZV9
|
Q75WH3
|
TX24A_MACGS
|
Neurotoxin magi-10
|
Macrothele
|
MKVFSFTVVVVMILSLSAFVLAGDEGDVMKKIVAMEEAVEERACLAEYQKCEGSTVPCCPGLSCSAGRFRKTKLCTK
|
Inhibits Kv11.1/KCNH2/ERG1, Kv1.1/KCNA1 and Kv1.3/KCNA3 voltage-gated potassium channels and Nav1.7/SCN9A voltage-gated sodium channels . In vivo, intracranial injection into mice causes lack of coordination for 10 min, followed by fast recovery.
|
Q75WH3
|
P41388
|
TBB_VENIN
|
Beta-tubulin
|
Venturia
|
MREIVHLQTGQCGNQIGAAFWQTISGEHGLDGSGVYNGTSDLQLERMNVYFNEASGNKFVPRAVLVDLEPGTMDAVRAGPFGQLFRPDNFVFGQSGAGNNWAKGHYTEGAELVDQVLDVVRREAEGCDCLQGFQITHSLGGGTGAGMGTLLISKIREEFPDRMMATFSVVPSPKVSDTVVEPYNATLSVHQLVENSDETFCIDNEALYDICMRTLKLNNPSYGDLNHLVSAVMSGVTTCLRFPGQLNSDLRKLAVNMVPFPRLHFFMVGFAPLTSRGAHSFRAVTVPELTQQMFDPKNMMAASDFRNGRYLTSSAIFRGKVSMKEVEDQMRNVQNKNSSYFVEWIPNNVQTALCSIPPRGLKMSSTFVGNSTSIQELFKRVGDQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQEASVSEGEEEYDEEAPLEGEE
|
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.
|
P41388
|
A7I162
|
THIC_CAMHC
|
Thiamine biosynthesis protein ThiC
|
Campylobacter
|
MRSQWLKNRKNDKTPTQMYYAKNGIITEEMRYVAKIEQMDAEILRSEVARGKTIIPANINHTNLVPMGIGRSLKCKINSNIGSSSVSSGVEEEVEKLKISIKYGADTVMDLSTGGDLNEIRTQIIKNSTVPIGTVPIYQIIHDVGSIENLTISQMLKTIENQAIQGVSYFTIHAGFLLEFMPLVAKRKMGIVSRGGSLMATWMMKNHKENPFFTAFDEILEICAKYDVSLSLGDSLRPGCIYDASDAAQISELKILGDLARRAWTKNVQVMIEGPGHVPFNEIASNMQLERVLCDDAPFYVLGPLPTDIGAGYDHITSAIGGTMAAFSGASMLCYVTPKEHLGLPNAKDVREGIVAHKIAAHIADVALGKKGAIERDHAMSDARYNFDWNKQFELSLDPDRAKEYHDETLPQEVFKEAEFCSMCGPKFCAYKISREISKNSCEFYKECK
|
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.
|
A7I162
|
Q328K6
|
ULAR_SHIDS
|
HTH-type transcriptional regulator UlaR
|
Shigella
|
MTEAQRHQILLEMLAQLGFVTVEKVVERLGISPATARRDINKLDESGKLKKVRNGAEAITQQRPRWTPMNLHQAQNHDEKVRIAKAASQLVNPGESVVINCGSTAFLLGQEMCGKPVQIITNYLPLANYLIDQEHDSVIIMGGQYNKSQSITLSPQGSENSLYAGHWMFTSSKGLTAEGLYKTDMLTAMAEQKMLSVVGKLVVLVDSSKIGERAGMLFSRADQIDMLITGKNANPETLQQLEAQGVSILRV
|
Represses ulaG and the ulaABCDEF operon.
|
Q328K6
|
C6DJE0
|
YIHI_PECCP
|
Der GTPase-activating protein YihI
|
Pectobacterium
|
MNRPVKGAADKAGKPKVKRKTREELEREARERKKDKKHRGHVAGSRTQEKASTDQRSGQRKAADPRIGSKKPVPLGVLDSAVAKPKPKSKPSAPVENVVAAKPTMSPEEELEMLENDSRLDALLDRLDSGETLSAKDQSWVDETLDRIDILMEELGIELGDDDEEEPQEDMLQLLKRNNPKDAF
|
A GTPase-activating protein (GAP) that modifies Der/EngA GTPase function. May play a role in ribosome biogenesis.
|
C6DJE0
|
Q0BTT3
|
UPPP_GRABC
|
Undecaprenyl pyrophosphate phosphatase
|
Granulibacter
|
MRIESMNAIQAIAIAILQGATELFPVSSLGHAVVLPALLGWSLPQHSQTFLPFLVFLHLGTAAALLLYFWRDWWALFSGVIGFAPAHHVPQARRIFMLLVVATLPAIVVGGLLEHMLRALFESAPIAAFFLVVNGGLLLFGEKLRGAASPYPQTSDHEVTERRALSTLTVMDAFTIGCWQCAALIPGISRSGATIVGGLLRGIDHEASAHFSFLIALPIILGATVLEVPKLLHADIAPGVFQTAALAAVAAGITAWLSTAFLMRYFRDHDSWALKPFAFYCIIAGLGALAWLHFA
|
Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
|
Q0BTT3
|
P57970
|
UBIA_PASMU
|
4-HB polyprenyltransferase
|
Pasteurella
|
MPISKQKWIAYAQLMRFDKPIGTLLLLWPTLWALFLSVKGMPDLSILSIFVLGVIFMRAAGCVINDYADRHIDGAVKRTSKRPLATGAATPEEAKWLFVLLVFCSFILVLFLNTYAIVLSFIAVFLAFIYPFMKRYTHLPQLFLGMAFGWSIPMAYGASIEALPLECWLLFFANLAWTVAYDTQYAMVDRDDDLRIGVKSTAILFAQYDNKIISLLQIVTLFFLGLIGYLSQLHTSYFVVLFLATLLFVYQCKLIKDRERESCFKAFLNNNYFGAMVFVAFLFGIFFDKL
|
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-hydroxybenzoate.
|
P57970
|
A2BLE8
|
TOP6A_HYPBU
|
Type II DNA topoisomerase VI subunit A
|
Hyperthermus
|
MAEEYVDVVDIEARKKALAVFREKFKEILEQVMRGENPTIMLPKRTLSNTIYDEKRKLLLLGPEKLKRSFFDLHESKKFMQTLLMARIIYEALERNEYPTIRDLYYRGKHTIVYREPGGRRHEENTWDEQRESDAVIRDIEVFTGLLREEMLILSKEKGKVVGNMRIRSGGDIIDLSKMGHGAYAIEPTPDLIEFIDVDAEYVLVVEKDAVFQQLHRIGFWKKHRAILITSAGQPDRATRRFVRRLNEELGLPVYILTDADPYGWYIYSVFKIGSITLSYESERLATPNARFIGVSMTDIFGYKSKKPYLTEQERRNFIIKAKEADIKRAYELKNYKWFQTKKWQIEIDIFLEKKAKLEIEAMTSKGLRFLADKYLPEKIETGDWIE
|
Relaxes both positive and negative superturns and exhibits a strong decatenase activity.
|
A2BLE8
|
O15273
|
TELT_HUMAN
|
Titin cap protein
|
Homo
|
MATSELSCEVSEENCERREAFWAEWKDLTLSTRPEEGCSLHEEDTQRHETYHQQGQCQVLVQRSPWLMMRMGILGRGLQEYQLPYQRVLPLPIFTPAKMGATKEEREDTPIQLQELLALETALGGQCVDRQEVAEITKQLPPVVPVSKPGALRRSLSRSMSQEAQRG
|
Muscle assembly regulating factor. Mediates the antiparallel assembly of titin (TTN) molecules at the sarcomeric Z-disk.
|
O15273
|
Q0HZP9
|
UBIB_SHESR
|
Ubiquinone biosynthesis protein UbiB
|
Shewanella
|
MTLASIRRGYHVIKTLLQYGLDDVLPPKMTPWYFKLARNSLFWIRNKHKGKSGGERLKLAMQELGPVYIKLGQMLSTRRDLLSDEWANELAMLQDKVPPFDGALARQAIEAELKAPIESFFDDFNETPLASASISQVHTATLKSNGKAVVLKVLRPNVEAKIQADLLLMSQTAKVIDYLLGEGNRLRPSEVIEDYRVTILGELNLKLEALNAIKLRNNFLDSDALYIPYVYEEFCYPRLMVMERIYGIPVSDIAALKAQGTNFKLLAERGVELFFTQVFRDNFFHADMHPGNIFISRDHPENPYYIGLDCGIMGTLSEVDKRYLAENFLAFFNRDYHRIAQLYIESGWVSEKTDLQAFEQAIKVVCEPMFNKPLDEISFGHVLLELFRTARHFDIVVQPQLVLLEKTLLYIEGLGRQLYPQLDLWQTAKPFLEQWMAEQVGPKAMFKKVSTKLPYWSDKLPEFPELIYDNLKLGRKLLSSQQQMLDKYLKYQQQAHKSNYLLITSAILLICGTLLFNQDATLWSPYVCLISGAALWIIGWRSRPKNRKF
|
Is probably a protein kinase regulator of UbiI activity which is involved in aerobic coenzyme Q (ubiquinone) biosynthesis.
|
Q0HZP9
|
Q15035
|
TRAM2_HUMAN
|
Translocating chain-associated membrane protein 2
|
Homo
|
MAFRRRTKSYPLFSQEFVIHNHADIGFCLVLCVLIGLMFEVTAKTAFLFILPQYNISVPTADSETVHYHYGPKDLVTILFYIFITIILHAVVQEYILDKISKRLHLSKVKHSKFNESGQLVVFHFTSVIWCFYVVVTEGYLTNPRSLWEDYPHVHLPFQVKFFYLCQLAYWLHALPELYFQKVRKEEIPRQLQYICLYLVHIAGAYLLNLSRLGLILLLLQYSTEFLFHTARLFYFADENNEKLFSAWAAVFGVTRLFILTLAVLAIGFGLARMENQAFDPEKGNFNTLFCRLCVLLLVCAAQAWLMWRFIHSQLRHWREYWNEQSAKRRVPATPRLPARLIKRESGYHENGVVKAENGTSPRTKKLKSP
|
Necessary for collagen type I synthesis. May couple the activity of the ER Ca(2+) pump SERCA2B with the activity of the translocon. This coupling may increase the local Ca(2+) concentration at the site of collagen synthesis, and a high Ca(2+) concentration may be necessary for the function of molecular chaperones involved in collagen folding. Required for proper insertion of the first transmembrane helix N-terminus of TM4SF20 into the ER lumen, may act as a ceramide sensor for regulated alternative translocation (RAT) .
|
Q15035
|
P51854
|
TKTL1_HUMAN
|
Transketolase-related protein
|
Homo
|
MADAEARAEFPEEARPDRGTLQVLQDMASRLRIHSIRATCSTSSGHPTSCSSSSEIMSVLFFYIMRYKQSDPENPDNDRFVLAKRLSFVDVATGWLGQGLGVACGMAYTGKYFDRASYRVFCLMSDGESSEGSVWEAMAFASYYSLDNLVAIFDVNRLGHSGALPAEHCINIYQRRCEAFGWNTYVVDGRDVEALCQVFWQASQVKHKPTAVVAKTFKGRGTPSIEDAESWHAKPMPRERADAIIKLIESQIQTSRNLDPQPPIEDSPEVNITDVRMTSPPDYRVGDKIATRKACGLALAKLGYANNRVVVLDGDTRYSTFSEIFNKEYPERFIECFMAEQNMVSVALGCASRGRTIAFASTFAAFLTRAFDHIRIGGLAESNINIIGSHCGVSVGDDGASQMALEDIAMFRTIPKCTIFYPTDAVSTEHAVALAANAKGMCFIRTTRPETMVIYTPQERFEIGQAKVLRHCVSDKVTVIGAGITVYEALAAADELSKQDIFIRVIDLFTIKPLDVATIVSSAKATEGRIITVEDHYPQGGIGEAVCAAVSMDPDIQVHSLAVSGVPQSGKSEELLDMYGISARHIIVAVKCMLLN
|
Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate.
|
P51854
|
Q4L5T8
|
Y1678_STAHJ
|
UPF0122 protein SH1678
|
Staphylococcus
|
MGKNDLVKTLRMNYLFDFYQTLLTEKQRNYMELFYLRDYSLSEIAETFDVSRQAVYDNIRRTGDLVEDYEAKLNLYEKFEQRRKIYDDMKQTLNDSKKLEQYINQLEELE
|
Might take part in the signal recognition particle (SRP) pathway. This is inferred from the conservation of its genetic proximity to ftsY/ffh. May be a regulatory protein.
|
Q4L5T8
|
B9DUQ2
|
TRHO_STRU0
|
tRNA hydroxylation protein O
|
Streptococcus
|
MSEKIRVLLYYKYVPIEDAQAYAAKHLEFCKSIGLKGRIIIADEGINGTVSGDYETTQKYMDWVHSDERFSDLWFKMDEEEEQAFKKMFVRYKKEIVHLGLEDNQFDEDINPLEVTGQYLNPKEFKEALLDEDTIVLDTRNDYEYDLGHFRGAVRPDIRNFRELPQWVRDNKDKFMEKRVVVYCTGGVRCEKFSGWMVREGFKDVGQLHGGIATYGKDPEVQGELWDGAMYVFDERISVPINHVDPTVISKDHFDGRPCERYVNCANPFCNKQIFASEENEAKYVRGCSPECRAHERNRYVSENGLSRQEWAARLEAIGETLPQVETV
|
Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs.
|
B9DUQ2
|
Q96WV0
|
UREG_SCHPO
|
Uncharacterized urease accessory protein ureG-like
|
Schizosaccharomyces
|
MAIPFLHKGGSDDSTHHHTHDYDHHNHDHHGHDHHSHDSSSNSSSEAARLQFIQEHGHSHDAMETPGSYLKRELPQFNHRDFSRRAFTIGVGGPVGSGKTALLLQLCRLLGEKYSIGVVTNDIFTREDQEFLIRNKALPEERIRAIETGGCPHAAIREDVSGNLVALEELQSEFNTELLLVESGGDNLAANYSRDLADFIIYVIDVSGGDKIPRKGGPGITESDLLIINKTDLAKLVGADLSVMDRDAKKIRENGPIVFAQVKNQVGMDEITELILGAAKSAGALK
|
Probably facilitates nickel incorporation.
|
Q96WV0
|
Q4LCT2
|
TXA5_ANDAU
|
Toxin-like peptide AaF1CA5
|
Androctonus
|
MMKLMLFSIIVILFSLIGSIHGADVPGNYPLDSSDDTYLCAPLGENPFCIKICRKHGVKYGLMLRLPCWCEYFGKIKNVKI
|
Probable neurotoxin that inhibits ion channels.
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Q4LCT2
|
Q7W419
|
UREF_BORPA
|
Urease accessory protein UreF
|
Bordetella
|
MHLSSPALPIGGFSYSQGLEAAIELGLVHDEASTLAWIESQLVTVMARAEAPLWCLLFEAWRAGDDAAAHGWNQWFHASRETRELRQETEQMGRSLARLAQELGWGTAATRAAVAALRPATLPAVHACACAMWALPREAGLGAYVFSWLENQVAAAIKGVPLGQMAGQRMLERLRAGLPAVLADARARAGATPPRLDTFAPQYALVSARHETQFSRLFRS
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Required for maturation of urease via the functional incorporation of the urease nickel metallocenter.
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Q7W419
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Q03ER2
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TGT_PEDPA
|
tRNA-guanine transglycosylase
|
Pediococcus
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MEPAIKYRLIKTDKHTGARLGEIITPHGTFPTPIFMPVGTQATVKAMSPEELEDLGADIILSNTYHLWVRPGEDIVKEGGGLHQFMNWKKGILTDSGGFQVFSLAKLRDITEEGVHFKNELNGANMFLSPEKAIQIENDLGPDIMMSFDECPPYFESYDYVKHSVERTSRWAERGLKAHRNPETQGLFGIIQGAGFEDLRRQSAKDLVSMDFPGYSIGGLSVGESKEEMNRVLDFTTQLIPENKPRYLMGVGSPDALIDGVLRGVDMFDCVLPTRIARNGTCMTSHGRLVVKNAKYARDFTPIDDNCQCYTCRNYTRAYIRHLIKTDETFGLRLTSIHNVYFLVHLMKDVRQAIMDDNLLEFRQNFFEEYGYNKENSKNF
|
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
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Q03ER2
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P60590
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WGRTX_GRARO
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Omega-grammotoxin SIA
|
Grammostola
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MKAQIFVVVLGLAALSVLCYGSEADESALHEEIFQLLAASDEVPKPQERDCVRFWGKCSQTSDCCPHLACKSKWPRNICVWDGSVGK
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Inhibits P/Q- (Cav2.1/CACNA1A) and N-type (Cav2.2/CACNA1B) voltage-gated calcium channel by modifying voltage-dependent gating . It selectively and reversibly blocks the calcium channels coupled to glutamate release . Also inhibits potassium channels (Kv2.1/KCNB1) with lower affinity . Has also been shown to weakly inhibit Kv11.1/KCNH2/ERG1, Kv1.2/KCNA2, Kv1.3/KCNA3, Nav1.5/SCN5A, Nav1.7/SCN9A and TRPV1 .
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P60590
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Q0BU78
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YIDC_GRABC
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Membrane protein YidC
|
Granulibacter
|
MDQKRLFLAIAISLGILLGFQGLYRHFVPEPPAAARTATNAGQGKPNNTLGAVPTDATASQSPPPKEGARLAVDAPRVKGSISLVGARFDDLVLRDYHETVDKNSPLVRLLAPLSGDEPYYVEYGWVPEESGIATPGRDTEWKADAATLTPNKPVTLSWDNGAGLTFMLKVAVDADYMFSVTQSVRNTTGKPVVLHPYARVRRDYRPEVEGYTVLHEGLIGVVDGILHEITYKSADSDGAKNNGLAFEHASTGGWAGITDKYWLTALIPDQITSVDFSFRDTKPNGRDGYQVGIISHNPDQVAAGAESASTTHLFAGAKVVSLLDHYQAEYHIPSFWEAVDFGWFWFITRPFFYALDWLYHLVGNFGVAILIFTVLVKAAFYPLASKSYRSMSKMRLLAPKIQSLRERYKDDPTRMQQEVMQLYKAEGANPASGCLPMLLQFPIFFSLYKVIFVTIEMRHAPFFGWIHDLSAVDPTNLFNLFGLLPFDPTHISPFLHLGIWPLIMGGTMYLQQKMNPPMPDPVQARMFQFMPIIFTFMLARFPVGLVIYWSWNNLLSIGQQWLIQRRTKLPRPELAKV
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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. Aids folding of multispanning membrane proteins.
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Q0BU78
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P13528
|
UNC86_CAEEL
|
Uncoordinated protein 86
|
Caenorhabditis
|
MQNTAPVPTTTTASKMQPFNNSLFGSFDDPILNARAAQVALADIDVKNVPQLTNPLMRPHDMFSYSNYFSGIHDTSAATNIYQGLPSSSEPFDASVVVPTSSDDQMTPLQQVMAMQQSYGAPPPFQYNMTHPFSTTSIASSNNLARYPIAPPTSDMDTDPRQLETFAEHFKQRRIKLGVTQADVGKALAHLKMPGVGSLSQSTICRFESLTLSHNNMVALKPILHSWLEKAEEAMKQKDTIGDINGILPNTDKKRKRTSIAAPEKRELEQFFKQQPRPSGERIASIADRLDLKKNVVRVWFCNQRQKQKRDFRSQFRARSAAAVMGPRVMPVLNGNNSNNNLKQGQTTYNGLPGFFD
|
Transcription factor required for correct cell fate determination and differentiation in diverse neuronal cell lineages where it plays a role in specifying the fate of daughter cells during cell divisions . Involved in sensory neuron production and function . Binds both alone and with mec-3 to the mec-3 promoter to initiate and maintain mec-3 expression which is required for sensory neuron differentiation . In addition, binds both alone and with mec-3 to the promoters of mec-4 and mec-7 which act to regulate sensory neuron function . Involved in determining the identity of the serotonergic NSM neurons and the cholinergic IL2 sensory and URA motor neurons . Promotes expression of the cfi-1 transcription factor in the URA and IL2 neurons which in turn activates normal URA and IL2 gene expression . Required to determine the identity of BDU sensory neurons in concert with transcription factor unc-86, regulating expression of a number of genes, including transcription factors ceh-14 and ahr-1, neuropeptides flp-10, nlp-1 and nlp-15, and tyramine receptor-encoding ser-2 . Regulates expression of a number of genes in NSM neurons including bas-1, cat-1, dop-3, mgl-3, nlp-13, scd-2 and ptps-1 . In the IL2 neurons, required for expression of cho-1, gcy-19, klp-6, lag-2, unc-5 and unc-17 . Promotes expression of pkd-2 in the male-specific CEM head neurons . Required for dauer-specific branching of IL2Q neurons and nictation behavior . Controls both the timing and direction of axon outgrowth in HSN neurons . Plays a role in serotonin production by regulating expression of the tryptophan hydrolase tph-1 which catalyzes serotonin synthesis, in the AIM, NSM, HSN and RIH neurons . Involved in regulation of lin-11 expression in the AIZ interneurons, the major interneurons of the olfactory pathway, and is required for odortaxis behavior . Involved in neurite pruning between AIM neurons during larval development by regulating the expression of transcription factor mbr-1 . Required for correct localization of unc-40 .
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P13528
|
O94888
|
UBXN7_HUMAN
|
UBX domain-containing protein 7
|
Homo
|
MAAHGGSAASSALKGLIQQFTTITGASESVGKHMLEACNNNLEMAVTMFLDGGGIAEEPSTSSASVSTVRPHTEEEVRAPIPQKQEILVEPEPLFGAPKRRRPARSIFDGFRDFQTETIRQEQELRNGGAIDKKLTTLADLFRPPIDLMHKGSFETAKECGQMQNKWLMINIQNVQDFACQCLNRDVWSNEAVKNIIREHFIFWQVYHDSEEGQRYIQFYKLGDFPYVSILDPRTGQKLVEWHQLDVSSFLDQVTGFLGEHGQLDGLSSSPPKKCARSESLIDASEDSQLEAAIRASLQETHFDSTQTKQDSRSDEESESELFSGSEEFISVCGSDEEEEVENLAKSRKSPHKDLGHRKEENRRPLTEPPVRTDPGTATNHQGLPAVDSEILEMPPEKADGVVEGIDVNGPKAQLMLRYPDGKREQITLPEQAKLLALVKHVQSKGYPNERFELLTNFPRRKLSHLDYDITLQEAGLCPQETVFVQERN
|
Ubiquitin-binding adapter that links a subset of NEDD8-associated cullin ring ligases (CRLs) to the segregase VCP/p97, to regulate turnover of their ubiquitination substrates.
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O94888
|
Q9FNB3
|
Y5360_ARATH
|
Putative BTB/POZ domain-containing protein At5g13600
|
Arabidopsis
|
MASLKLGSKSEVFHLSGHTWLCKTGLKPDVMIQVVDESFHLHKFPLLSRSGYLETLFSKASETTCVAQLHDIPGGPETFLLVAKFCYGVRIEVTPENAVSLRCAAEYLQMSENYGDANLIYLTESFLNDHVFVNWEDSIKALEKSCEPKVLPLAEELHIVSRCIGSLAMKACAEDNTSFFNWPISLPEGTTTTTIYWNGIQTKATSENWWFNDVSSFLDLPMYKRFIKTVESRGVNAGIIAASVTHYAKRNLPLLGCSRKSGSPSEEGTNYGDDMYYSHEEQRSLLEEIVELLPGKKCVTSTKFLLRLLRTSMVLHASQVTQETLEKRIGMQLDEAALEDLLIPNMKYSGETLYDTDSVQRILDHFMLTFDSSIVEEKQMMGDSHPLKSITKVASLIDGYLAEVASDENLKLSKFQALGALIPEDVRPMDDGIYRAIDIYIKAHPWLTESEREQLCLLMNCQKLSLEACTHAAQNERLPLRVIVQVLFFEQMRLRTSIAGWLFGSEENNDTSGALEGNKNTNANMVMHGMRERVFELEKECMSMKQDLDKLVKTKEGRNFFSKIFGSRSKTKTSPCGKGGEDALVIPETKN
|
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.
|
Q9FNB3
|
B1MYE1
|
YBEY_LEUCK
|
Endoribonuclease YbeY
|
Leuconostoc
|
MDLAIIDQTHDGVSRYHHDLVESVLNFAGEALKLPVNTEMSVTFVNNDEIQRYNRDYRGVDKPTDVISFAIEEGEDDFNIISDDAWTEDIAKNIGDIIVSVDIIGAQAEYLGHSYERELGFLVVHGFLHLNGYDHMLGDAEEKEMFDLQREILDNYGLKR
|
Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
|
B1MYE1
|
Q2P0V3
|
TPIS_XANOM
|
Triose-phosphate isomerase
|
Xanthomonas
|
MRRKIVAGNWKLHGSRAFATELVAKLAAHMPLEGIDVVILPPLPYLGDLIEDFEAHHLSFGAQDVSSNEKGAYTGEVSASMLVDVGAGYGLVGHSERRQYHQESSELVARKFAAAIHAGLTPVLCVGESLEQREAGQTEAILRAQLEPVLALVGSAGFAGAVLAYEPIWAIGTGCTATPEQAQAVHAFLRGEVAKADARIADSLPILYGGSVKPDNAGELFAQPDVDGGLVGGASLVAEDFLAIARAAAAC
|
Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
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Q2P0V3
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Q5TC79
|
ZBT37_HUMAN
|
Zinc finger and BTB domain-containing protein 37
|
Homo
|
MEKGGNIQLEIPDFSNSVLSHLNQLRMQGRLCDIVVNVQGQAFRAHKVVLAASSPYFRDHMSLNEMSTVSISVIKNPTVFEQLLSFCYTGRICLQLADIISYLTAASFLQMQHIIDKCTQILEGIHFKINVAEVEAELSQTRTKHQERPPESHRVTPNLNRSLSPRHNTPKGNRRGQVSAVLDIRELSPPEESTSPQIIEPSSDVESREPILRINRAGQWYVETGVADRGGRSDDEVRVLGAVHIKTENLEEWLGPENQPSGEDGSSAEEVTAMVIDTTGHGSVGQENYTLGSSGAKVARPTSSEVDRFSPSGSVVPLTERHRARSESPGRMDEPKQPSSQVEESAMMGVSGYVEYLREQEVSERWFRYNPRLTCIYCAKSFNQKGSLDRHMRLHMGITPFVCRMCGKKYTRKDQLEYHIRKHTGNKPFHCHVCGKSFPFQAILNQHFRKNHPGCIPLEGPHSISPETTVTSRGQAEEESPSQEETVAPGEAVQGSVSTTGPD
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May be involved in transcriptional regulation.
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Q5TC79
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A1SJ31
|
TYSY_NOCSJ
|
Thymidylate synthase
|
Nocardioides
|
MRAYLDLLQRVVDEGVPKGDRTGTGTLSVFGHQMRFDLRAGFPLVTTKKVHTRSVFGELLWFLRGDTNVKWLQDRGITIWDEWADEQGDLGPVYGYQWRSWPTPDGRHVDQIAQVVEQIRDSPDSRRHVVSAWNVADIPDMALAPCHTMFQFYVAPPGPGEESGPGRLSCQLYQRSADVFLGVPFNIASYALLTHMVAQVTGLEVGDFVHTLGDAHLYSNHLDQARLQLTREPRPLPRLVLDSSVTELDAFDLEHIAVEGYDPHPGIKAPIAV
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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.
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A1SJ31
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Q746Q2
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YIDC_GEOSL
|
Membrane protein YidC
|
Geobacter
|
MEKRALIAVVLSILFFYGYTALFSPPPKETPKPVATATQSQPAQQVTAAPVPVAVPAQPQPAVAARDVSVDTPAYSVTFSTQGGSIKRLDLKRYHETAGPGGKNVTLVSEDNPSNYTIGLRAPGFGLDQNAVFVPSADALTVGPGEKKQLSFTWVSPAGVTVTKTYNFSGDGYGLEIQYQVTNSGSARVSSPVQTVQTYPLVPKVKESRFETFGPATFAQDKLFEDKVKDLESGAKTHAAPLWSGFADKYFLSAVLAHEGSMAAATIRKTASGYLENTISSPELSLNPGEGRALTYRLFFGPKDIDVLKAQGNSLERAINLGWFAMLAKPLLHSLKFFHNYTGNYGIAIIIITVIIKVIFYPLTHSSYKSMKEMQKLQPKMQQLREKYKNDREAMNRAMMELYQTHKVNPVGGCLPMLVQIPVFFALYKALMFSIELRHAPFMLWITDLAAKDPYYVTPIIMGVTMVIQQKMTPSQMDPVQQKMMMALPVVFTFMFLNFPSGLVLYWLVNNVLTIIQQYYINRSISTAEAK
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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. Aids folding of multispanning membrane proteins.
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Q746Q2
|
B7VMM4
|
YCIB_VIBA3
|
Inner membrane-spanning protein YciB
|
Vibrio
|
MKQILDFIPLIIFFALYKMYDIYTATGALIVASAVQIILTYFIYKKVEKMQVITFLMVAVFGGMTIFLHDDNFIKWKVTIVYALFAIGLTVSHIMGKSAIKGMLGKEITLPDSIWGKINWAWTLFFTLCAILNVYVAFNLPLDVWVNFKVFGLLIATFAFTLLTGVYIYKHLPKDQHLPKDKHQQRDQETQNDTQQELSGKNTEEK
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Plays a role in cell envelope biogenesis, maintenance of cell envelope integrity and membrane homeostasis.
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B7VMM4
|
P75691
|
YAHK_ECOLI
|
Zinc-dependent alcohol dehydrogenase YahK
|
Escherichia
|
MKIKAVGAYSAKQPLEPMDITRREPGPNDVKIEIAYCGVCHSDLHQVRSEWAGTVYPCVPGHEIVGRVVAVGDQVEKYAPGDLVGVGCIVDSCKHCEECEDGLENYCDHMTGTYNSPTPDEPGHTLGGYSQQIVVHERYVLRIRHPQEQLAAVAPLLCAGITTYSPLRHWQAGPGKKVGVVGIGGLGHMGIKLAHAMGAHVVAFTTSEAKREAAKALGADEVVNSRNADEMAAHLKSFDFILNTVAAPHNLDDFTTLLKRDGTMTLVGAPATPHKSPEVFNLIMKRRAIAGSMIGGIPETQEMLDFCAEHGIVADIEMIRADQINEAYERMLRGDVKYRFVIDNRTLTD
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Catalyzes the reduction of a wide range of aldehydes into their corresponding alcohols. Has a strong preference for NADPH over NADH as the electron donor. Cannot use a ketone as substrate. Is a major source of NADPH-dependent aldehyde reductase activity in E.coli. The in vivo functions of YahK has yet to be determined.
|
P75691
|
Q26503
|
TPM_SCHHA
|
Tropomyosin
|
Schistosoma
|
MDGIKKKMIAMKLEKENAMERAVQYEELLKKKEEEREKRESEIAELNTKMKQAQIDCDEVQETLQEQMNKLEETDKRATNAEAEVAAMTRRIRLLEEDLEVSSSRLTETLTKLEEASKTAEESERGRKDLEIRSIADDERLNQLEDQQKEAKYIAEDADRKYDEAARKLAIAEVDFKRAEARLEAAESKIVELEEELRVIGNNMKALEISEQESAQREESYEETIRDLTERLKAAEQRATEAERQVSKLQNEVDHLEDDLLAEKERYKALSGELDQTFAELTGY
|
Tropomyosin, in association with the troponin complex, plays a central role in the calcium dependent regulation of muscle contraction.
|
Q26503
|
Q31TC4
|
ULAA_SHIBS
|
Ascorbate-specific permease IIC component UlaA
|
Shigella
|
MFFNQVMTNAPLLLGIVTCLGYILLRKSVSVIIKGTIKTIIGFMLLQAGSGILTSTFKPVVAKMSEVYGINGAISDTYASMMATIDRMGDAYSWVGYAVLLALALNICYVLLRRITGIRTIMLTGHIMFQQAGLIAVTLFIFGYSMWTTIICTAILVSLYWGITSNMMYKPTQEVTDGCGFSIGHQQQFASWIAYKVAPFLGKKEESVEDLKLPGWLNIFHDNIVSTAIVMTIFFGAILLSFGIDTVQAMAGKVNWTVYILQTGFSFAVAIFIITQGVRMFVAELSEAFNGISQRLIPGAVLAIDCAAIYSFAPNAVVWGFMWGTIGQLIAVGILVACGSSILIIPGFIPMFFSNATIGVFANHFGGWRAALKICLVMGMIEIFGCVWAVKLTGMSAWMGMADWSILAPPMMQGFFSIGIAFMAVIIVIALAYMFFAGRALRAEEDAEKQLAEQSA
|
The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II UlaABC PTS system is involved in ascorbate transport.
|
Q31TC4
|
Q3SYZ6
|
XYLB_BOVIN
|
Xylulose kinase
|
Bos
|
MAERAARHCCLGWDFSTQQVKVVAVDAELSVFYEDSVHFDRDLVEFGTQGGVHVHKDGLTVTSPVLMWVQALDIILEKMKASGFDFSQVLALSGAGQQHGSVYWKTGASQVLTSLSPDLPLREQLQACFSISNCPVWMDSSTAAQCRQLEAAVGGAQALSLLTGSRAYERFTGNQIAKIYQQNPEAYSHTERISLVSSFAASLFLGSYSPVDYSDGSGMNLLQIQDKVWSQACLGACAPRLEEKLGRPVPSCSIVGAISSYFVQRYGFPPECKVVAFTGDNPASLAGMRLEEGDIAVSLGTSDTLFLWLQEPTPALEGHIFCNPVDPQHYMALLCFKNGSLMREKIRDESASGSWSKFSKALQSTGMGNSGNLGFYFDVMEITPEIIGRHRFTAENHEVSAFPQDVEIRALIEGQFMAKKIHAEALGYRVMPKTKILATGGASHNRDILQVLADVFGAPVYVIDTANSACVGSAYRAFHGPSLLCLVSIY
|
Phosphorylates D-xylulose to produce D-xylulose 5-phosphate, a molecule that may play an important role in the regulation of glucose metabolism and lipogenesis.
|
Q3SYZ6
|
Q92BC5
|
TPX_LISIN
|
Thioredoxin-dependent peroxiredoxin
|
Listeria
|
MTQVTFKHNPVTLVGTERKVGDKAPNFTVVNRDLEEVTLHDYDGKVRLISVVPSIDTSVCSTQTRKFNEEASNLDNTVVLTISVDLPFAQKKWCAAEGLPNAITLSDHRDLSFGEAYGVIMKELRLLARSVFVVNAKGEIVYTEVVPEGSDHPNYEAAIEAAKKA
|
Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides.
|
Q92BC5
|
P42461
|
THIX_CORGL
|
Thiamine biosynthesis protein X
|
Corynebacterium
|
MSISRTVFGIAATAALSAALVACSPPHQQDSPVQRTNEILTTSQNPTSASSTSTSSATTTSSAPVEEDVEIVVSPAALVDGEQVTFEISGLDPEGGYYAAICDSVANPGNPVPSCTGEMADFTSQAWLSNSQPGATVEIAEDGTATVELEATATGTGLDCTTQACVAKVFGDHTEGFRDVAEVPVTFAAA
|
Is necessary for biosynthesis of the 4-methyl-5-(beta-hydroxyethyl)thiazol component from which thiamine is formed.
|
P42461
|
Q65WC1
|
TSAC_MANSM
|
tRNA threonylcarbamoyladenosine biosynthesis protein TsaC
|
Basfia
|
MELAQIVERLKKNEVVAYPTEAVFGLGCNPNSKSAVEKLLILKQRPVEKGLILVAHKLDLLLPFIDESRLKQSHWQLLTQQYDCPTTWVVPAKLSVPKFITGQFDSVAVRLCTHPAVAQLCEQTGFALTSTSANLSGLPPCKTAQQVRSQFGEFFPVLDMAVGNAVNPSEIRDIFSRQIFRRG
|
Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Catalyzes the conversion of L-threonine, HCO(3)(-)/CO(2) and ATP to give threonylcarbamoyl-AMP (TC-AMP) as the acyladenylate intermediate, with the release of diphosphate.
|
Q65WC1
|
A6TFL2
|
TDH_KLEP7
|
L-threonine 3-dehydrogenase
|
Klebsiella
|
MKALSKLKAEEGIWMTDVPEPEVGHNDLLIKIRKTAICGTDVHIYNWDEWSQKTIPVPMVVGHEYVGEVVGIGQEVRGFKIGDRVSGEGHITCGHCRNCRAGRTHLCRNTIGVGVNRPGCFAEYLVIPAFNAFKIPDNISDDLASIFDPFGNAVHTALSFDLVGEDVLVSGAGPIGVMAAAVAKHVGARNVVITDVNEYRLELARKMGVTRAVNVAKENLNDVMAELGMTEGFDVGLEMSGAPPAFRSMLDTMNHGGRIAMLGIPPSDMSIDWTKVIFKGLFIKGIYGREMFETWYKMAALIQSGLDLSPIITHRFGIDDFQKGFDAMRSGQSGKVVLSWD
|
Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2-amino-3-ketobutyrate.
|
A6TFL2
|
Q223B1
|
UBID_ALBFT
|
Polyprenyl p-hydroxybenzoate decarboxylase
|
Rhodoferax
|
MAYRDLRDFITQLEHLGELKRVQAEVSPYLEMTALCDRTLRAGGPALLFENPTGHNTPVLGNLFGTTRRVALGMGVNDVSELRQFGHVLASLKEPEAPKGFKELMGLGSLVKTLWAMAPKELRSAPCQEIIWEGADVDLARLPIQHCWPGDVAPLITWGLVITQGPHKARQNLGIYRQQVLARNKVIMRWLAQRGGALDFKEHAALNPGQPYPVCVALGADPATILGAVTPVPDSLSEYQFAGLLRGSRTELVKALGSELRVPAFAEIVLEGHIYPDATHASGFEHALEGPFGDHTGYYNEQDWFPVFTIDRITQRRDPIYHSTYTGKPPDEPAMLALALNELFVPLLQRQYPEITDFYLPPEGCSYRLAVVQIKKSYPGHARRVMFGIWSFLRQFMYTKFIVVVDDDVNIRDWKDVIWAITTRVDPTRDTLLADSTPIDYLDFASPVSGLGSKMGLDATNKWPGETSREWGRPLTMSADVTARVEQVWQTLGL
|
Catalyzes the decarboxylation of 3-octaprenyl-4-hydroxy benzoate to 2-octaprenylphenol, an intermediate step in ubiquinone biosynthesis.
|
Q223B1
|
Q2FKX5
|
TRPD_METHJ
|
Anthranilate phosphoribosyltransferase
|
Methanospirillum
|
MIQDTIRKVVSMQDLAPDEARDLMTSIADGKVTDAQIGSILTALSMKGVTAHEITAFAHVLRDRAVQLKTDTSGTFVDTCGTGGDGAHTFNISTAAALVAAAAGVRVVKHGNRGVSSRSGSADVLEALGIPITLTPEEAAASVSSHNIAFLFAPGYHPAIGRVASARREIGFFSVFNILGPLLNPAGASARLIGVGDTRHIPSITGALANLGVSHAMVVHGDGTDEITITGETEVYELSGGTICRYTLTPEEFGIRRVSRETIAGGSPAENAEIIMDIFSGRKGPCRDIVLLNAAAAIYLGEKATCIYDGYRIAREVVDSGQAYRLVMALRRTT
|
Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
|
Q2FKX5
|
A6ZVR0
|
URM1_YEAS7
|
Ubiquitin-related modifier 1
|
Saccharomyces
|
MVNVKVEFLGGLDAIFGKQRVHKIKMDKEDPVTVGDLIDHIVSTMINNPNDVSIFIEDDSIRPGIITLINDTDWELEGEKDYILEDGDIISFTSTLHGG
|
Acts as a sulfur carrier required for 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Serves as sulfur donor in tRNA 2-thiolation reaction by being thiocarboxylated (-COSH) at its C-terminus by the MOCS3 homolog UBA4. The sulfur is then transferred to tRNA to form 2-thiolation of mcm(5)S(2)U. Prior mcm(5) tRNA modification by the elongator complex is required for 2-thiolation. Also acts as a ubiquitin-like protein (UBL) that is covalently conjugated via an isopeptide bond to lysine residues of target proteins such as AHP1. The thiocarboxylated form serves as substrate for conjugation and oxidative stress specifically induces the formation of UBL-protein conjugates.
|
A6ZVR0
|
P43349
|
TCTP_SOLTU
|
p23
|
Solanum
|
MLVYQDLLTGDELLSDSFPYKEIQNGMLWEVQGKWVVQGAVDVNIGANPSAEGGGEDEGVDDQAVKVVDIVDTFRLQEQPAFDKKQFVTYIKRYIKNLTPKLEGEAQEAFKKNIESATKFLLSKLKDFQFFVGEGMHDDSALVFAYYKDGSADPTFLYLAPGLKEIKC
|
Involved in calcium binding and microtubule stabilization.
|
P43349
|
A6UWW4
|
TRM56_META3
|
tRNA ribose 2'-O-methyltransferase aTrm56
|
Methanococcus
|
MVVEVLRLGHRWGRDKRISTHVALTSRALGADKILFVSNDDHVKDSVNRIVEQWGGDFKFDVVDSWKQYIWSFKKNNGIVIHLTMYGENINEIMKKIIEKRQEGKDSKNILIIIGAEKVPKEAYELADYNVSVGNQPHSEVAAIAILLDRLFEGSSLYKEYPDAKIKVNPSDRYKSVEIR
|
Specifically catalyzes the AdoMet-dependent 2'-O-ribose methylation of cytidine at position 56 in tRNAs.
|
A6UWW4
|
Q491V9
|
UBID_BLOPB
|
Polyprenyl p-hydroxybenzoate decarboxylase
|
Candidatus Blochmannia
|
MKYKDLRDFIKILEHRGDLKRIKFPINPDLEITEIADRTIKSGGPALFFENPTGYTIPVLCNLFGTPNRIALGMGKESILSLRDVGKLLAFLREPELPTGVHDFFSKIPHFRHILHMPIKRVSTAPCQENVWCNQDVDITHMPIMRCWPQDVSPVITWGITITRGLKSKRQNLGIYRQQVLSKNKIIMRWLSHRGGALDFQEWHKNTSERRFPITVALGADPATLIGAVVPIPDTLSEYAFSGLLRGCRTEVIKCISCDLDVPANSEIVLEGYLERDETAIEGPFGDHTGYYNTTAKFPVCTITHITQRNNPIYLSTYTGRPPDEPAILGMAMNEMFIPIIQKQFPEITDFYLPPEGCSYRLAIVTIKKQYIGHAKRIIFGIWSFLKQFMYTKFIIVCDDDINARDWNDVVWAITTRMEPDRDTIIVKNTPIDYLDFSSPISGLGSKIGMDATNKWPGETEREWGIPIKMHDTVRHYIDSIWDKLDI
|
Catalyzes the decarboxylation of 3-octaprenyl-4-hydroxy benzoate to 2-octaprenylphenol, an intermediate step in ubiquinone biosynthesis.
|
Q491V9
|
O95801
|
TTC4_HUMAN
|
Tetratricopeptide repeat protein 4
|
Homo
|
MEQPGQDPTSDDVMDSFLEKFQSQPYRGGFHEDQWEKEFEKVPLFMSRAPSEIDPRENPDLACLQSIIFDEERSPEEQAKTYKDEGNDYFKEKDYKKAVISYTEGLKKKCADPDLNAVLYTNRAAAQYYLGNFRSALNDVTAARKLKPCHLKAIIRGALCHLELKHFAEAVNWCDEGLQIDAKEKKLLEMRAKADKLKRIEQRDVRKANLKEKKERNQNEALLQAIKARNIRLSEAACEDEDSASEGLGELFLDGLSTENPHGARLSLDGQGRLSWPVLFLYPEYAQSDFISAFHEDSRFIDHLMVMFGETPSWDLEQKYCPDNLEVYFEDEDRAELYRVPAKSTLLQVLQHQRYFVKALTPAFLVCVGSSPFCKNFLRGRKVYQIR
|
May act as a co-chaperone for HSP90AB1 . Promotes Sendai virus (SeV)-induced host cell innate immune responses .
|
O95801
|
P0CD94
|
UQCC3_RAT
|
Ubiquinol-cytochrome-c reductase complex assembly factor 3
|
Rattus
|
MEAARKALAVVAVLGAGGGVGSILFALVTPGELQKQLMLQEMPERDSRRRDEAVRTKELVMATLKDAAATKENVAWRRNWTVRGDGRSA
|
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 protein, it may also control the cardiolipin composition of mitochondria membranes and their morphology.
|
P0CD94
|
A2RI47
|
THIT_LACLM
|
Thiamine ECF transporter S component ThiT
|
Lactococcus cremoris subsp. cremoris
|
MSNSKFNVRLLTEIAFMAALAFIISLIPNTVYGWIIVEIACIPILLLSLRRGLTAGLVGGLIWGILSMITGHAYILSLSQAFLEYLVAPVSLGIAGLFRQKTAPLKLAPVLLGTFVAVLLKYFFHFIAGIIFWSQYAWKGWGAVAYSLAVNGISGILTAIAAFVILIIFVKKFPKLFIHSNY
|
Probably a thiamine-binding protein that interacts with the energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates. The substrates themselves are bound by transmembrane, not extracytoplasmic soluble proteins.
|
A2RI47
|
Q6YQR9
|
YQGF_ONYPE
|
Putative pre-16S rRNA nuclease
|
Candidatus Phytoplasma asteris
|
MLKCQNNASLGLDLGEKTLGIALSQTGIIAQNLKTIFFATHKYDRLIAPLQEIIFQYQIKTIVLGYPKHMNNDIGIKAKISSDFKKTLENKFEQVKVILWDERLSTVQAIQMLKTNNKKKGKILQMKDEIAATIILQNYLDYIKLHTNKEH
|
Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
|
Q6YQR9
|
P24421
|
VSDF_SALDU
|
Virulence protein VsdF
|
Salmonella
|
MLRATKVCIYPTPEQAEHLNAQFGAVRFVYSKSLHIKKHAYQRHGVSLTPRKDIKPLLAVAKKFRKFRKFRKYAWLKEYDSIALQQAVINLDVAFSNCFNPKLKARFPMFKRKHGKLLG
|
Expressed but non-essential protein, involved in the virulence of Salmonellas.
|
P24421
|
Q5FNP1
|
UVRC_GLUOX
|
Excinuclease ABC subunit C
|
Gluconobacter
|
MTDLPPHSSHHPADQGEPLVPAEKKQGVEAIREALKTIPYSPGVYRMLSEKGEVLYVGKALSLKKRVSSYIRINQLPERLRRMVSMTVSMEIVITRTEADALLLEANYIKRMKPRFNILLRDDKSYPWLMLTESHEFPQITKQRGKPVKGATYWGPFANAWAVNQTLNLVQRSFLLRSCSDAVLNSRTRPCLLYQIKRCSAPCVDRISKEDYAELVSEARQFLSGHSTELQQRLVAEMEQASQELNYERAASIRDRIRGFASIQGSSTINPTSINDADIMTIWQEAGQSCIQVFFIRGSRNNGNRAFYPAHAEEETAADVLSAFMIQFYDNKPPPPSILVNCELPEPKLVEEALSIRRGQKVEILRPQRGEKKDVVEHAALNAREALERKLAENTGQRRLLEGVAEVFGLPEIPQRIETYDNSHIMGQAPYGVMVVGGPEGFNKRAYRKYAIKGPVTPGDDFGMMREVMERRFGHRSENGERPEDWPDLLLIDGGLGQFNAVRAVLADLGVTGIPIVAIAKGPDRDAGREWFFTETKSPFQLPPRDPVLYYLQRLRDEAHRFAITTHRAGRSKGLRSSELDHVPGIGAARKKALLNHFGSAKSVRQASLEELENAPGISSSTATAIYGHFHPEWVQKTSADNRSH
|
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.
|
Q5FNP1
|
K7WDC8
|
TS21I_MAIZE
|
Terpene synthase 21
|
Zea
|
MGERANFLKGEVRKKFEAAAMSAIDAAMLVDAVVHLGIDHCFREEIATALRSVHEDEEGEFGSCDDLHTVAVRFLVLRQHGLWVSADVFDKFRDDKGSFSKSLLCSNPRGLLSLYNAAHMAVTPEEKVLDDAIAFARSHLVEAMIGELRSPMVEQVSRSFDIPLPRFSRRLESMHYIAEYGQEEEGHDAQILELARLEFELVRSLHLRELREICSAEYGATGEEAFAFIANMTENAWRKINQACMEMDPAMLPAFKVAVVDLSRSIEIIYLGGKRDAYTFGSNLKDLVTSLFLKPCA
|
Inactive selinene synthase.
|
K7WDC8
|
P06708
|
TNNC2_ASTLP
|
Troponin C, isotype gamma
|
Astacus
|
MDTLDEEQLSALKKAFDSFDTDSKGFITPETVGVILRMMGVKISEKNLQQVIAETDEDGSGELEFEEFVELAAKFLIEEDEEALKAELKEAFRIYDKGGDGYITTDVLREILRELDNRLTEDDLDGIIEEVDEDGSGTLDFDEFMEMMSG
|
Troponin is the central regulatory protein of striated muscle contraction. Tn consists of three components: Tn-I which is the inhibitor of actomyosin ATPase, Tn-T which contains the binding site for tropomyosin and Tn-C. The binding of calcium to Tn-C abolishes the inhibitory action of Tn on actin filaments.
|
P06708
|
Q9HCJ5
|
ZSWM6_HUMAN
|
Zinc finger SWIM domain-containing protein 6
|
Homo
|
MAERGQQPPPAKRLCCRPGGGGGGGGSSGGGGGAGGGYSSACRPGPRAGGAAAAAACGGGAALGLLPPGKTQSPESLLDIAARRVAEKWPFQRVEERFERIPEPVQRRIVYWSFPRSEREICMYSSFNTGGGAAGGPGDDSGGGGGAGGGGGGGSSSSPAATSAAATSAAAAAAAAAAAAAAAAGAGAPSVGAAGAADGGDETRLPFRRGIALLESGCVDNVLQVGFHLSGTVTEPAIQSEPETVCNVAISFDRCKITSVTCSCGNKDIFYCAHVVALSLYRIRKPDQVKLHLPISETLFQMNRDQLQKFVQYLITVHHTEVLPTAQKLADEILSQNSEINQVHGAPDPTAGASIDDENCWHLDEEQVQEQVKLFLSQGGYHGSGKQLNLLFAKVREMLKMRDSNGARMLTLITEQFMADPRLSLWRQQGTAMTDKYRQLWDELGALWMCIVLNPHCKLEQKASWLKQLKKWNSVDVCPWEDGNHGSELPNLTNALPQGANANQDSSNRPHRTVFTRAIEACDLHWQDSHLQHIISSDLYTNYCYHDDTENSLFDSRGWPLWHEHVPTACARVDALRSHGYPREALRLAIAIVNTLRRQQQKQLEMFRTQKKELPHKNITSITNLEGWVGHPLDPVGTLFSSLMEACRIDDENLSGFSDFTENMGQCKSLEYQHLPAHKFLEEGESYLTLAVEVALIGLGQQRIMPDGLYTQEKVCRNEEQLISKLQEIELDDTLVKIFRKQAVFLLEAGPYSGLGEIIHRESVPMHTFAKYLFTSLLPHDAELAYKIALRAMRLLVLESTAPSGDLTRPHHIASVVPNRYPRWFTLSHIESQQCELASTMLTAAKGDVRRLETVLESIQKNIHSSSHIFKLAQDAFKIATLMDSLPDITLLKVSLELGLQVMRMTLSTLNWRRREMVRWLVTCATEVGVYALDSIMQTWFTLFTPTEATSIVATTVMSNSTIVRLHLDCHQQEKLASSARTLALQCAMKDPQNCALSALTLCEKDHIAFETAYQIVLDAATTGMSYTQLFTIARYMEHRGYPMRAYKLATLAMTHLNLSYNQDTHPAINDVLWACALSHSLGKNELAAIIPLVVKSVKCATVLSDILRRCTLTTPGMVGLHGRRNSGKLMSLDKAPLRQLLDATIGAYINTTHSRLTHISPRHYSEFIEFLSKARETFLMAHDGHIQFTQFIDNLKQIYKGKKKLMMLVRERFG
|
involved in nervous system development, important for striatal morphology and motor regulation.
|
Q9HCJ5
|
Q03QE7
|
TRMB_LEVBA
|
tRNA(m7G46)-methyltransferase
|
Levilactobacillus
|
MRVRNKPWAKGYMADHLDRLVVEPEPLKGNWQSRFPSNQPLFVEIGTGKGQFIIEMARQHPDRNFIGIEIQTSVIAVALKGVVNSGLTNIQLVHTDGEAINTFFEAGEVSGLYLNFSDPWPKKRHTKRRLTSPVFLAHYADVLQPEGQLQFKTDNRGLFEYSLGSLNNFGMVFEGVWLDLHAATDGVEDIQTEYEQKFSKKGPIYQVIAHFPTNN
|
Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
|
Q03QE7
|
Q0KEH6
|
UBIE_CUPNH
|
Demethylmenaquinone methyltransferase
|
Cupriavidus
|
MSETHFGFEKVDEAEKADKVAGVFHSVASKYDVMNDLMSGGMHRLWKMFTIAQAGVRPGHKVLDIAGGTGDLAKAFAKQAGPTGEVWLTDINESMLRVGRDRLLNKGIVTPVCLCDAERIPFPDNHFDLVTVAFGLRNMTHKDAALAEMRRVVKPGGKVMVLEFSKVWKPLEKAYDVYSFKVLPWLGERVAGDAPSYRYLAESIRMHPDQASLVRLMEHAGLENVEYFNLTAGVVALHVGRKY
|
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).
|
Q0KEH6
|
Q9CFG8
|
XYLB_LACLA
|
Xylulose kinase
|
Lactococcus
|
MTYVLGIDLGTSSLKGILMDEVGNLITTKSAEYQIDTPKQGYSEQRPEYWIVALESVLTGLSVEISDFGQQLAGISFSGQMHSLVVLDDNNKPVYPAILWNDVRTSKQCQEITDRLGQRLLEITKNIALEGFTLPKILWLQENEPEVWSRVKKIMLPKDYLSLWLTGNIYTEFSDAAGTLLLDIEKKQWSEEITDAFNIDRRILPELIESTDRTGFVKAEIAERYKLTNEVKVFAGGADNAAAALGVGLINEEVGLISMGTSGVVSAYEPKIADYKGKLHFFNHTVPGACYSMGVTLAAGNSLNWYKETFGKGLSFNELLSEVYTVSPGSEGLLFTPYIVGERTPHFDSKIRGSFIGISAHHEQKHFSRAVLEGITFSLRDSKDIMEKTKNKKFKRLISVGGGAQNPDIMQMQADIFNSEMIRLTVEQGPGLGACMIAAFGCGLFDSLEAVTKAFVHYKEASFIPNPKNVARYEQIYQIWKQVYKNTSEISHQLVEFNDEG
|
Catalyzes the phosphorylation of D-xylulose to D-xylulose 5-phosphate.
|
Q9CFG8
|
Q65JH8
|
TRUB_BACLD
|
tRNA-uridine isomerase
|
Bacillus
|
MYNGVLLLHKPVGMTSHDCVMKIRKLLKTKKVGHTGTLDPEVSGVLPICVGRATKIVEYLTEKSKTYDAEVTLGCSTETEDQTGEVTEKKPVLAPPDEQTVQSVLRSLEGTIEQVPPMYSAVKVGGKKLYEYARAGIEVERPKRTITIHHIELTSEIRHEGDKARFRFVVTCSKGTYVRTLAVTIGEKLGYPAHMSNLVRTASGPFTLDECLTFEDVEGLIADGTLSEKLVPIERALDHLPKWIISDTLAKKVENGAVLETPGSFSHLTSEDRIAVFTEAGRCTAVYYPHPTKTGLLKPAKVLVQKSEQ
|
Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
|
Q65JH8
|
Q06417
|
TDA5_YEAST
|
Topoisomerase I damage affected protein 5
|
Saccharomyces
|
MNIDCLCRWVVLPLLRYPLLVALVLRWSLSDSISICLTIYTLLINAFLIANSYIKRSGQVAWKSLREFKNGIVLITGGSKGLGRAIVSQLLQDYSNLTILNVDICPSSVRNTRVKDLICDLSDDEEVAALLNLLKRKYKNEIRLIVNNAGVRANFTGFNGMERDNLDKIFKINTFAPLQFIQELAPSRHSTRQCYIVNIASILGILTPAKVAAYAASKAALIAFHQSYSFELQNEGVRNIRTLLVTPGQLNTEMFAGFKPPRQFFAPVIDITTLAAKIVRYCELGQRGQLNEPFYCSFAHLLMCVPYSLQRIVRSFSRIDCCLPDE
|
Involved in the resistance to DNA-damaging agents.
|
Q06417
|
Q4L4I5
|
UVRB_STAHJ
|
Excinuclease ABC subunit B
|
Staphylococcus
|
MVEHYPFKLNSEFDPQGDQPQAIEKIVKGVKEGKRHQTLLGATGTGKTFTMSNVIKEVGKPTLIIAHNKTLAGQLYSEFKEFFPENRVEYFVSYYDYYQPEAYVPSTDTFIEKDASINDEIDQLRHSATSALFERDDVIIIASVSCIYGLGNPEEYKDLVVSVRVGMEMDRSELLRKLVDVQYSRNDIDFQRGTFRVRGDVVEIFPASREEMCIRVEFFGDEIDRIREVNYLTGEVIREREHFAIFPASHFVTREEKMKIAIERIEKELEERLKELKDENKLLEAQRLEQRTNYDLEMMREMGFCSGIENYSVHLTLRPLGSTPYTLLDYFGDDWLVMIDESHVTLPQIRGMFNGDRARKQVLVDHGFRLPSAMDNRPLKFEEFEQKTNQLVYVSATPGPYEIEHTDEMIEQIIRPTGLLDPKIDVRPTKNQIDDLLSEIQERIDRDERVLVTTLTKKMSEDLTTYMKEAGIKVNYLHSEIKTLERIEIIRDLRMGTYDVVVGINLLREGIDIPEVSLVVILDADKEGFLRSNRSLIQTIGRAARNEKGEVIMYADKITDSMQYALDETQRRRDIQTAHNEKYGITPKTINKKIHDVISATVDNDETNEKQQTELPKKMTKKERQKTIENIEKEMKKAAKDLDFEKATELRDMLFELKSEG
|
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.
|
Q4L4I5
|
P06015
|
VSA1_TRYBB
|
Expression-linked copy
|
Trypanosoma
|
MVTKERNAALKIVMLVASALTLHPQQALAQTAGRPLADVVGKTLCTYSKTAKRQAANLAQTLQRASSAAKQSRQAQQLAALALAKLPDYKEAAATLLIYATHKIQDAQASIENWTGENTKLVGQAMYSSGRIDELMLLLEGHREDGANGQDKTCLGAAAGGNTVNEFVKTECDTESGHNIEADNSNIGQAATTLSQESTDPEASGGASCKITANLATDYDSHANELPLLGGLLTIHNAGGFKTGQSLQTAAPTNKLISALKNKGAGVAAKLATVTSAAPTSKQELKTLLASKGERAKLQAANDEYNNWKPGAKPEDFDAHIKKVFGAEDGKDSAYAIALEGISIEAPLGGGQTQNKQLYSMQPKDLMAALIGTIAELQTAAATKPACPGHKQTTTESDALCSKIKDANECNSKHFCSYNGTETDSAKKCKYNATKASASDAPVTQAQTTSRSETPAEKCTGKKKDDCKDGCKWEAETCKDSSILLTKNFALSVVSAALVALLF
|
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.
|
P06015
|
P05471
|
YKP5_KLULA
|
Uncharacterized killer plasmid pGKl-2 protein 5
|
Kluyveromyces
|
MIYDKIDTKLIKLGKTNKFSGEEEKSITSLYYEDESFEFSFKNKYVKITKIETNAYGKKFVTIKSKLYADIVEKVAKELDAVSPILSDGSFRATINDATSFSKDVGEYSFYACVSLYFPSIYKDTEKTTLQVYLKEVVVTKIIKNNLEVEFDKLSLAI
|
The presence of the two linear plasmids, termed pGKL1 and pGKL2, in strains of Kluyveromyces lactis confers the killer phenotype to the host cell, by promoting the secretion of a toxin able to inhibit the growth of sensitive strains.
|
P05471
|
Q5HQX0
|
UVRB_STAEQ
|
Excinuclease ABC subunit B
|
Staphylococcus
|
MVEHVPFKLKSEFEPQGDQPQAIQKIVDGVNEGKRHQTLLGATGTGKTFTMSNVIKEVGKPTLIIAHNKTLAGQLYSEFKEFFPENRVEYFVSYYDYYQPEAYVPSTDTFIEKDASINDEIDQLRHSATSSLFERDDVIIIASVSCIYGLGNPEEYKNLVVSVRVGMEMERSELLRKLVDVQYSRNDIDFQRGTFRVRGDVVEIFPASREEMCIRVEFFGDEIDRIREVNYLTGEVIREREHFTIFPASHFVTREEKMKVAIERIEKELEERLKELRDENKLLEAQRLEQRTNYDLEMMREMGFCSGIENYSVHLTLRPLGSTPYTLLDYFGDDWLVMIDESHVTLPQIRGMYNGDRARKQVLIDHGFRLPSALDNRPLKFEEFEEKTKQLVYVSATPGPYELEHTDEMVEQIIRPTGLLDPKIDVRPTENQIDDLLSEIQDRVDKDERVLVTTLTKKMSEDLTTYMKEAGIKVNYLHSEIKTLERIEIIRDLRMGTYDAIVGINLLREGIDIPEVSLVVILDADKEGFLRSDRSLIQTIGRAARNDKGEVIMYADKITDSMQYAIDETQRRREIQIAHNKEHGITPKTINKKIHDVISATVESDETNQQQQTELPKKMTKKERQKTIENIEKEMKKAAKDLDFEKATELRDMLFELKAEG
|
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.
|
Q5HQX0
|
Q9RJ68
|
TATA_STRCO
|
Sec-independent protein translocase protein TatA
|
Streptomyces albidoflavus group
|
MFGRLGAPEIILILVVIILLFGAKKLPDMARSLGKSARILKSEAKAMKSEAKADDAAPADPPNPEQSAAQRTIQAAPGDVTSSRPVTEPTDTTKR
|
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.
|
Q9RJ68
|
Q7PYU6
|
ZGPAT_ANOGA
|
Zinc finger CCCH-type with G patch domain-containing protein
|
Anopheles
|
MSVDELNQSILQYKEQLEQIAQALQLTRDETERSELNKLKSDLIELLELTVESLAATSDDDDAPDTAGRAPPATADNPIDDEFALFMREIKELQTEDSAAGEQAGEQTATEPERQPNDDDADNDDDADDKLDLDGLVGSKCSAPHLHTWGSTAYHNAMVCSLDADDLAHATAKVLFTNPTHREMLPCAYFLEGECRFTDEKCRYSHGEVVRLDQLRDYRAPQFERLRRAGSRALVKQSTRLWCKGTVTEVDFDAKRCKVRLEEGKREQLEVPFEDLLPLDEDEDGQEAAEDSESDTDGADEEEADDEALRKALLVEKSLFHPAPDRRLGEWEEHTRGIGSKIMQKMGYIVGTGLGREGEGIVVPVSAQVLPQGRSLDYCMELREQSNGDKDLFSVEKKLVQLKRQEAKRAAKDYERQRARESKSKDVFSFINEQVFSGAAGGESSRPNRNRPGALSRQELKEHSCKNLNIASLKLSEEIRRTEADVERLKIALTRHRAGTPAADNLLRQIDAKRAEISRMQASEGNISREQQLRSDKKKLTIF
|
Transcription repressor.
|
Q7PYU6
|
Q4V7E0
|
TRMO_RAT
|
tRNA methyltransferase O
|
Rattus
|
MRGLEKQGPSATAAPCGCAQPALETGNLLTEPIGYLESCFSAKIGTPRQPSICSQSRACLKIRKSIFNNPEHSLMGLEQFSHVWILFVFHKNGHLNYKAKVQPPRLNGAKTGVFSTRSPHRPNAIGLTLAKLEKVEGGAVYLSGIDMIHGTPVLDIKPYIADYDSPQNLEPQTKHHKLRAAGPSDATANSCDQQLLSGCEKAQPCHSTKEKPKCREHRTSDENSQKFRDTSEIQHTLPEDRERAVDLALESSREETMDEPEDQLGPQELKSFLEEGTDRPRKVEGALVLRGSSAETRWDASCHARTADRVPCSVVPSWVKEAPVATLQVRFTPHAEMDLRKLSSGGASQTSFKYFHSAEEAKCAIEAMLSADPRSVYRRKLCEDRLFFFTVDIAHVTCWFGDGFAEVLRIKLASEPVEVADPEESLVALGS
|
S-adenosyl-L-methionine-dependent methyltransferase responsible for the addition of the methyl group in the formation of N6-methyl-N6-threonylcarbamoyladenosine at position 37 (m(6)t(6)A37) of the tRNA anticodon loop of tRNA(Ser)(GCU). The methyl group of m(6)t(6)A37 may improve the efficiency of the tRNA decoding ability. May bind to tRNA.
|
Q4V7E0
|
A4SGX9
|
TAL_CHLPM
|
Probable transaldolase
|
Chlorobium
|
MKFFIDTADLDEIRSAAELGMLDGVTTNPSLIAKIVKDPSNFTRTDFFDHIAAICDLVDGPVSAEVTSLDTASMIKEGEALAAIHDNVVVKCPLTIDGLKAIRHLSEAGIATNATLVFSPSQAILAAKAGASFVSPFVGRLDDISTDGMALVEDIVDIYDNYGYMAEVIVASVRHPQHVVEAARIGADIATIPFSVISRLAVHPLTESGLKKFMEDASVIKP
|
Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
|
A4SGX9
|
F1R013
|
ZDHC9_DANRE
|
Zinc finger DHHC domain-containing protein 9
|
Danio
|
MSAVMITRKITRKWEKLPGKNTFCCDGRVMMARQKGVFYLTLFLIVGTCSLFFAFECPYLAVHLSPAIPVFAVLLFVFVMAMLLRTSFSDPGVLPRALPEEANFIEMEIEAANGNVLAGQRPPPRIKNVQINNQIVKLKYCYTCKIFRPPRASHCSICDNCVDRFDHHCPWVGNCVGKRNYRYFYLFTLSLSLLTIYIFAFDIVHVVLRSVDSGFVNTLKETPGTVLEVLVCFFTLWSVVGLTGFHTYLISLNQTTNEDIKGSWSGKNRVQNPYSHKNIIKNCCEVLCGPTYPSVLDRRGLMLEDSCSSAPSNGATTVPVNKSSNPATQTTKSSAPLIPNEHTPDEAKPSICSGTQKSSSSPKEEKPSSPISPNAVAPAVIKESTH
|
Palmitoyltransferase that could catalyze the addition of palmitate onto various protein substrates.
|
F1R013
|
P20005
|
VSP1_OVOOK
|
Snake venom serine protease
|
Ovophis
|
VIGGDECNINEHRFLAALYD
|
Thrombin-like snake venom serine protease that releases specifically fibrinopeptide B from fibrinogen (FGB) to form fibrin clots. Shows a preferential cleavage at Arg-|-Gly bonds in fibrinogen beta chains. Cleaves fibrinogen beta chains preferentially to alpha chains.
|
P20005
|
B7HH02
|
TRPA_BACC4
|
Tryptophan synthase alpha chain
|
Bacillus cereus group
|
MGVEKIKAAFENGKKAFIPYVMGGDGGFEKLKERIRFLDEAGASIVEIGIPFSDPVADGPTIQRAGKRALDSGVTVKGIFQALIEVRKEVQIPFVLMTYLNPVLAFGKERFIENCIEAGVDGIIVPDLPYEEQNIIASLLREVNIALIPLVTVTSPIERIEKITSESEGFVYAVTVAGVTGVRQNFKEEIHSYLEKVKSHVNLPVVAGFGISTKEHVEEMVTICDGVVVGSKVIELLENEKREEICELIYATKQKEEA
|
The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
|
B7HH02
|
Q57637
|
Y173_METJA
|
Putative transcriptional regulatory protein MJ0173
|
Methanocaldococcus
|
MVEDSFLTDTQIKVLKLRKKGLTQEEIAKMLGTSRANISMIEKRAKENIKKAYNTIKIYNRIMAPLSIEIEEGTDVLEIPDIVFKKADEEGIKVKYNTLELIELIKENASEFIEKRTVKKKFKIYILENGDLDVGGS
|
Putative transcriptional regulator.
|
Q57637
|
Q8E4B4
|
TARI_STRA3
|
Ribitol-5-phosphate cytidylyltransferase
|
Streptococcus
|
MNIGVIFAGGVGRRMNTKGKPKQFLEVHGKPIIVHTIDIFQNTEAIDAVVVVCVSDWLDYMNNLVERFNLTKVKAVVAGGETGQMSIFKGLEAAEQLATDDAVVLIHDGVRPLINEEVINANIKSVKETGSAVTSVRAKETVVLVNDSSKISEVVDRTRSFIAKAPQSFYLSDILSVERDAISKGITDAIDSSTLMGMYNRELTIVEGPYENIKITTPDDFYMFKALYDARENEQIYGM
|
Catalyzes the transfer of the cytidylyl group of CTP to D-ribitol 5-phosphate.
|
Q8E4B4
|
A2T736
|
ZKSC8_PANTR
|
Zinc finger protein 192
|
Pan
|
MAEESRKPSAPSPPDQTPEEDLVIVKVEEDHGWDQESSLHENNPLGQEVFRLRFRQLCYQETLGPREALIQLRALCHQWLRPDLNTKEQILELLVLEQFLTILPEELQTLVKEHQLENGEEVVTLLEDLERQIDILGRPVSARVHGHRVLWEEVVHSASAPEPPNTQLQSEATQHKSPVPQESQERAMSTSQSPTRSQKGSSGDQEMTATLLTAGFQTLEKIEDMAVSLIREEWLLDPSQKDLSRDNRPEDFRNVFSLGGETRSENRELASKQVISTGIHPHGETAAKCNGDVIRGLEHEEARDLLGRLERQRGNPTQERRHKCDECGKSFAQSSGLVRHWRIHTGEKPYQCNVCGKAFSYRSALLSHQDIHNKVKRYHCKECGKAFSQNTGLILHQRIHTGEKPYQCNQCGKAFSQSAGLILHQRIHSGERPYECNECGKAFSHSSHLIGHQRIHTGEKPYECDECGKTFRRSSHLIGHQRSHTGEKPYKCNECGRAFSQKSGLIEHQRIHTGERPYKCKECGKAFNGNTGLIQHLRIHTGEKPYQCNECGKAFIQRSSLIRHQRIHSGEKSESISV
|
May be involved in transcriptional regulation.
|
A2T736
|
P58034
|
YMGF_ECOLI
|
Inner membrane protein YmgF
|
Escherichia
|
MNNSNNLDYFTLYIIFSIAFMLITLLVILIAKPSTGLGEVLVTINLLNALVWLAINLVNRLRERLVNHRDQQ
|
Could be involved in cell division. May participate in the stabilization of the cell divisome under specific conditions.
|
P58034
|
B3PVV3
|
TRPA_RHIE6
|
Tryptophan synthase alpha chain
|
Rhizobium
|
MTARMDKRFAELKAEGRPALVTYFMGGDPDYDTSLGIMKALPEAGSDIIELGMPFSDPMADGPAIQLAGQRALKGGQTLKKTLQLAADFRKTDDATPIVMMGYYNPIYIYGVEKFLDDALTAGIDGLIVVDLPPEMDDELCIPAIRKGINFIRLATPTTDEKRLPAVLKNTSGFVYYVSMNGITGSALPDPSLVSGAVQRIKQHTELPVCVGFGVKTAEHAKVIGGSADGVVVGTAIVNQVATSLTKDGKATADTVQAVATLVRGLSSGTRSARLVAAE
|
The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
|
B3PVV3
|
B2VHS0
|
THII_ERWT9
|
tRNA 4-thiouridine synthase
|
Erwinia
|
MKFIIKLFPEITIKSQSVRLRFIKILTGNIRNVLKPYDETLAVVRHWDNIEVRAKDESKRAAIVAELTRIPGIHHILAVEDRPYTDVHHIFEQTLEMNRERIEGKTFCVRVKRRGKHEFSSQDVERYVGGGLNQHVASAQVQLNRPQVTVNLEIEDERLILVTARYEGIGGYPIGTQEDVLSLISGGFDSGVSSYMLMRRGCRVHYCFFNLGGAAHEIGVRQVAHYLWKRYGSTHRVRFVAINFEPVVGEILEKVDDGQMGVVLKRMMVRAASKIAERYGVQALVTGEALGQVSSQTLTNLRLIDNASDTLILRPLISHDKEHIIKLAREIGTEDFARTMPEYCGVISKSPTVKAVKAKIEHEEQNFDFAILERMVEEATNVDIREIAEKAQEEVAEVETVASFSHNDVILDIRSNDEQEARPLEVEGVVVKSLPFYKLATQFGDLDQSKSWLLYCERGVMSRLQALYLHEQGFKNVKVYRP
|
Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiamine biosynthesis pathway. The sulfur is donated as persulfide by IscS.
|
B2VHS0
|
E7CQW6
|
UGTA1_STABO
|
UDP-glucosyltransferase A1
|
Starmerella
|
MSPSSHKPLILACGLPLSGHIMPVLSLVHGLTDDGYEATVVTGRAFEQKVRDVGADFVPLEGNADFDDHTLDDLVPGRKDMAPSFDRTVQDVEHMMVATLPEQFAAIQRAFKKLSASGRPVVLVSEVLFFGAHPISLGAPGFKPAGWICLGVLPLLIRSDHTLGLDNDRSPEAHAKKLAMNHALEHQIFVKATAKHKEICRELGCTEDPKFIWEHSYIAADKFLQLCPPSLEFSRDHLPSNFKFAGSTPKHRTQFTPPSWWGDVLSAKRVIMVTQGTFAVSYKHLIVPTLEALKDEPDTLTVAILGRRGAKLPDDVVVPENARVIDYFNYDALLPHVDALVYNGGYGGLQHSLSHSVPVVIAGDSEDKPMVASRAEAAGVAIDLKTGLPTVEQIKEAVDSIIGNPKFHEASKKVQMELESHNSLKILEESIEEIASHDFGLLTKSDEETEDIPVKGPALAVSS
|
Catalyzes the first glycosylation step of sophorolipid biosynthesis, the coupling of glucose to a hydroxylated fatty acid to give rise to a glucolipid . Can glycosylate all hydroxyl fatty acids generated by cytochrome P450 monooxygenases CYP52M1, CYP52N1 and CYP52E3 into their corresponding glucolipids. Main products are 17-O- and 18-O-(beta-D-glucopyranosyl)-octadecenoic acids .
|
E7CQW6
|
G3Y417
|
YANB_ASPNA
|
Yanuthone D biosynthesis cluster protein B
|
Aspergillus subgen. Circumdati
|
MDRIDVHHHFIPPAYVEAFKTTGGDPSGWHLPQWTPESSLSLMDSHNTRTAILSLTAPGTSILAHSPGASATLAREINLYAAKLHNENPTRFGFFASLPHLTPDTIPAAIEEAIYALETLHADGITLYTRYTGTGYLGHDAFAPLWEELNRRKAVVFIHPTNTAADARNRSILVNPALPQPIIDYPHETCRTAVDLITSGTISRNPDVKIILSHGGGTLPILATRAAHLLYDAKLTSISPEDFLEQARSFYFDLALSGNDENMQLLVGRNGFAKGGHVFYGSDFPYAPVSTINKYVRMMEGFSVQGEEVEKAIARDSAVKLFPRFQMPADLRVGKTNNWGAFSACLLLPVGLSALYSVLQSRVHTYST
|
Decarboxylase; part of the gene cluster that mediates the biosynthesis of yanuthone D, a fungal isoprenoid epoxycyclohexenone that acts as an antibiotic against fungi and bacteria . The first step of the pathway is the synthesis of 6-methylsalicylic acid (6-MSA) by the polyketide synthase yanA . 6-MSA is then converted to m-cresol by the decarboxylase yanB . The cytochrome P450 monooxygenase yanC then catalyzes the oxidation of m-cresol to toluquinol . Epoxidation of toluquinol is then performed by the short chain dehydrogenase yanD, with the help of yanE, and a further prenylation by yanG leads to 7-deacetoxyyanuthone A . The next step is the hydroxylation of C-22 of 7-deacetoxyyanuthone A by the cytochrome P450 monooxygenase yanH to yield 22-deacetylyanuthone A . O-Mevalon transferase yanI then attaches mevalon to the hydroxyl group of 22-deacetylyanuthone A to produce yanuthone E . Finally, the FAD-dependent monooxygenase yanF oxidizes the hydroxyl group at C15 of yanuthone E to form yanuthone D . Furthermore, several branching points in the pathway lead to the production of yanuthones F and G from 7-deacetoxyyanuthone A; yanuthones H and I from 22-deacetylyanuthone A; and yanuthone J from yanuthone E .
|
G3Y417
|
C3NGV3
|
VATD_SULIN
|
V-ATPase subunit D
|
Sulfolobus
|
MSQKVLPTKINLIQFRRQLRLITVIKRLLENKREVLLLYLRTYASEYEKIYNEVNEEMKKVYESYLQAVASEGISNIEEIALSQKPSLEVSSSIKVIFGVKVPTIKLDKSTIPSKPFSDVETSPYLSESYEEMTEAFNKIIELVELESTIRSLVSELRKTQRLINSIDNYILPFYRGSIKFIKQILEDRQREEFSRLKIIRRILQRRRESGSG
|
Produces ATP from ADP in the presence of a proton gradient across the membrane.
|
C3NGV3
|
P0DMW8
|
VKT33_ACTEQ
|
Kunitz-type proteinase inhibitor AEPI-III
|
Actinia
|
NSFCNLPAVVGRCKGYFPRYFYNTEAGKCQRFIYG
|
Dual-function toxin that inhibits both the serine protease trypsin and voltage-gated potassium channels (Kv).
|
P0DMW8
|
Q9X2T1
|
THIO_PSEAE
|
Thioredoxin
|
Pseudomonas
|
MSEHIVNVTDASFEQDVLKADGPVLVDYWAEWCGPCKMIAPVLDEVARDYQGKLKVCKLNIDENQDTPPKYGVRGIPTLMLFKDGNVEATKVGALSKSQLAAFLDANI
|
Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions.
|
Q9X2T1
|
G3FIN9
|
UGTK5_MANES
|
Cyanohydrin UDP-glucosyltransferase UGT85K5
|
Manihot
|
MGSLASEIPPHAVLVPYPAQGHVNPLMQLGKLLHSRGFYITFVNTEHNHRRLIRSRGQEFIDGLPDFKFEAIPDGLPYTDRDATQHVPSLSDSTRKHCLAPFIDLIAKLKASPDVPPITCIISDGVMAFAIDAARHFGIPEIQFWTTSACGFMAYLHHIELVRRGIVPFKDESFLHDGTLDQPVDFIPGMPNMKLRDMPSFIRVTDVNDIMFDFMGSEAHKSLKADAIILNTYDELEQEVLDAIAARYSKNIYTVGPFILLEKGIPEIKSKAFRSSLWKEDLSCIEWLDKREPDSVVYVNYGCVTTITNEQLNEFAWGLANSKHPFLWIVRPDVVMGESAVLPEEFYEAIKDRGLLVSWVPQDRVLQHPAVGVFLSHCGWNSTIECISGGKPMICWPFFAEQQTNCKYACDVWKTGVELSTNLKREELVSIIKEMMETEIGRERRRRAVEWRKKAEEATSVGGVSYNNFDRFIKEAILQHKTK
|
UDP-glucosyltransferase catalyzing in planta synthesis of cyanogenic glucosides. Able to glucosylate acetone cyanohydrin and 2-hydroxy-2-methylbutyronitrile, forming linamarin and lotaustralin. Accepts also to some extent, a wide range of potential acceptor substrates, including simple alcohols, flavonoids, isoflavonoids and other hydroxynitriles such as p-hydroxymandelonitrile, mandelonitrile, (E)-4-hydroxy-2-methylbut-2-enenitrile and (E)- 2-(hydroxymethyl)but-2-enenitrile.
|
G3FIN9
|
Q5M5E1
|
TRHO_STRT2
|
tRNA hydroxylation protein O
|
Streptococcus
|
MAKPIRVLLYYKYVPIENAEQFAADHLAFCKSIGLKGRILVADEGINGTVSGEYETTQKYMDYVHSLPGMEDLWFKIDEEEEQAFKKMFVRYKKEIVHLGLEDNNFDSDINPLETTGAYLSPKEFKDALLDEDTVVLDTRNDYEYDLGHFRGAIRPDIRNFRELPQWVRDHKEEFMDKRVVVYCTGGVRCEKFSGWLVREGYKDVGQLHGGIVTYGKDPEVQGELWDGKLYVFDERIAVDVNHVDPIVVGKDWFDGTPCERYVNCGNPFCNRRILTSEENEDKYLRGCSHECRVHPRNRYVSENDLSQEEVVERLAAIGESLDVTPA
|
Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs.
|
Q5M5E1
|
P84152
|
TCTP_PLAKN
|
Translationally-controlled tumor protein homolog
|
Plasmodium (Plasmodium)
|
MKVYKDVFTNDEVCSDSYNQEDPFGIADFREIAFEVKSNKRIKGNDDYGIADNSEEAVDGMGADVEQVIDIVDSFQLTSTSLSKKEYSVYIKNYMQKILKYLEEKKPDRVDVFKTKAQPLIKHILTNFDDFEFYMGESLDMDAGLTYSYYKGEEVTPRFVYISDGLYEEKF
|
Involved in calcium binding and microtubule stabilization.
|
P84152
|
O75348
|
VATG1_HUMAN
|
Vacuolar proton pump subunit M16
|
Homo
|
MASQSQGIQQLLQAEKRAAEKVSEARKRKNRRLKQAKEEAQAEIEQYRLQREKEFKAKEAAALGSRGSCSTEVEKETQEKMTILQTYFRQNRDEVLDNLLAFVCDIRPEIHENYRING
|
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 . In aerobic conditions, involved in intracellular iron homeostasis, thus triggering the activity of Fe(2+) prolyl hydroxylase (PHD) enzymes, and leading to HIF1A hydroxylation and subsequent proteasomal degradation .
|
O75348
|
B8DNP8
|
TATA_DESVM
|
Sec-independent protein translocase protein TatA
|
Desulfovibrio
|
MFGIGIQELLVVLVLVLLVFGANKLPEIGGGLGRAIRNFKRATSEPDEIDITPGKKNGKTDKDDKQA
|
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.
|
B8DNP8
|
F4IY62
|
UGPA3_ARATH
|
UDP-glucose pyrophosphorylase 3
|
Arabidopsis
|
MANPQASPILHHPQNHLSLFHFRTTTSPRSFSSLHFRKPLLFLSSSSSFSSKLQQSEQQCNNHQVRHVSTVPVEYSTPTPPESDDFLSEIDRLKSLLSKLDVSKDLRRKDAVIDADSRVRRFFSENRGGLSKVFGYLGLNSNEMFLVKCVIAAGQEHALCMNYEEAFGEEEEEYTVRSSVKNALYALVEMIERFDVNSSGYKGRREMGTVLDSEEIAHFRKFLTFLEEIEQFYDCIGGIIGYQVMVLELLHQSSKRRNTNRSQLVEESLGCQYLEMHTPSVLDLTQEEDYASQAALWGIEGLPDLGEIYPLGGAADRLGLIDSETGECLPAAMLAHCGRTLLEGLIRDLQAREFLYFKLYGKQCVTPVAIMTSAAKNNHEHVSSLCERLKWFGRGQSNFRLFEQPLVPAVSAEDGQWIVSKPFVPVSKPGGHGVIWKLAYDKGVFNWFYDHGRKGATVRQVSNVVAATDVTLLALAGIGLRYNKKLGFASCKRNAGATEGINVLMEKKNFDGKWEYGISCIEYTEFDKFDISNRSPSSNGLQADFPANTNILYVDLHSAELIGSSSNAKSLPNMVLNTKKRIEYLDQYGDYHSVMGGRLECTMQNIADNFFNKFPSRCHGSLEDKLDTYIVYNERRKVTSSAKKKKPHASAALHQTPDGALLDILRNGYDLLTECDIKLPMIEANDKYVDSPPPYLILLHPALGPLWEVSRQKFKGGSISSCSELQLEIAEFSWNNVQVDGSLIVTAENAMGSTTPNDNGEPILQYGLRCGKCKLHNVNVVNRGIDWNSKSNVYWRNDVNRLETCKIILHGNAEFEASNVTIEGHHVFEVPDGHKLKITSGNAGLSINLEALKEEVMETGSWYWNYQLNGSHIHLQQVEVSQS
|
Involved in the biosynthesis of sulfolipids in the chloroplast. Catalyzes the first committed step in sulfolipid biosynthesis. Converts glucose 1-phosphate to UDP-glucose, the precursor of the polar head of sulfolipid. In addition to glucose 1-phosphate, can use galactose 1-phosphate, but with much lower activity. No uridyltransferase activity with other hexose monophosphates. Specific for UTP and cannot use ATP, CTP, and GTP.
|
F4IY62
|
Q5M7U7
|
VSTM5_RAT
|
V-set and transmembrane domain-containing protein 5
|
Rattus
|
MRPPRCVGRTQGIPLGLLAFWVATARCLQSQGVSLYIPRSAINATVQEDILLSVDYICHGVPTIEWEYTPNWGVQKIVEWKPGTPANVSQSHRDRVCTFDNGSIQLFSVGVRDSGYYVITVTEHPGSSQSGTILLHVSEIRYEDLHFVAVFFALLAAVAVVLISLMWVCNQCAYKFQRKRRYKLRESTTEEIEMKDVEC
|
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 synapse formation by altering dendritic spine morphology and actin distribution. Promotes formation of unstable neuronal spines such as thin and branched types. Regulates neuronal morphogenesis and migration during cortical development in the brain.
|
Q5M7U7
|
Q6G547
|
TRUA_BARHE
|
tRNA-uridine isomerase I
|
Bartonella
|
MPRFKLTLEYDGSNYAGWQRQAELRTIQSALEQALFHFSGQQLTITTAGRTDAGVHATGQVAHVDFEKNWRTHTVRDALNAHLQKQGDNIAILHVQNVPDSFDARFSAIKRHYLFKILNRRSPPALNTKRVWWIPKPLNAQAMHEAAQKLVGKHDFTTFRSAHCQAKSPIRTLERLDVQREGEEIFLYAQARSFLHHQIRSFAGSLMEVGIGRWTTQDLEAALHAKDRTRCGMVAPPSGLYLTKVEY
|
Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
|
Q6G547
|
A1CQN6
|
YPI1_ASPCL
|
Type 1 phosphatases regulator ypi1
|
Aspergillus subgen. Fumigati
|
MSRTQQAPMNAGSASGVQVASPLSQDNSTIRVSGTLRLRGDNGTRNNGEDLTTTRHIRWSEDVVDNEGMGKKSSKVCCIYHKDRPVGESSSESDDTDSSSDDCSDCDSDTRIPTHKGDQGGEASSRCSPSRLAERKCGTSCSKRHSKQRSRRHMSPNAYEKMPKFKGQPGKR
|
Regulator of type 1 phosphatases which maintains protein phosphatase activity under strict control.
|
A1CQN6
|
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