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 |
|---|---|---|---|---|---|---|
A6TCD6 | RLMN_KLEP7 | tRNA m2A37 methyltransferase | Klebsiella | MSEQIVTPDTAALTVPNKDAKINLLDLNRQQMREFFKNMGEKPFRADQVMKWMYHYCCDDFDEMTDINKVLRSKLKEVAEIRAPEVVEEQRSTDGTIKWAIAVGDQRVETVYIPEEDRATLCVSSQVGCALECKFCSTAQQGFNRNLRVSEIIGQVWRAAKIVGAVKTTGVRPITNVVMMGMGEPLLNLNNVVPAMEIMLDDFGFGLSKRRVTLSTSGVVPALDKLGDMIDVALAISLHAPNDTIRDEIVPINKKYNIETFLNSVRGYISKSNANQGRVTIEYVMLDHVNDGTEHAHELAALLKDTPCKINLIPWNPFPG... | Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity. | A6TCD6 |
A8MQN2 | LNK1_ARATH | Night light-inducible and clock-regulated 1 | Arabidopsis | MSDLYIHELGDYLSDEFHGNDDGIVPDSAYEDGGQFPILVSNRKKRRNDDMGSGTNHLKSNTFIKREANMLGKNPWPEKDSGGSSVSRDTGTGKDVQDMTLEDTNTSDHGFNGGHVDVVENFSTGDPMLCDTSAATNDGVYNYSLNSIPDAENDLSFFDNGDKEKNDLFYGWGDIGNFEDVDNMLRSCDSTFGLDSLNNEGDLGWFSSAQPNEETAGAMTDDLKPDKMLENQRTAMLQVEDFLNNSEPNHAVEDEYGYTIEDDSAQGKSSQNVFDTSLQKKDILMLDVEANLEKKQTDHLHHLDGKSDGFSENSFTLQHS... | Transcriptional coactivator necessary for expression of the clock genes PRR5 and TOC1 . Antagonizes REV8 function in the regulation of anthocyanin accumulation . Involved in red light input to the clock . Activates clock-controlled genes with afternoon peak . Mediates light inhibition of hypocotyl elongation . | A8MQN2 |
Q466X0 | AMPPA_METBF | Nucleoside monophosphate phosphorylase | Methanosarcina | MQLKLEHFNIKIGQHKILLNIADAKELGVNPGDRVRIRGRESISAIADTTDDMVPPGTLGVFSEVYEHFVNWDKPVEVVPAFRSKSASVIKKMMDKKPVVQEEIKTLVNDIVEENLSEIELSAFITSSYIHGMTDDEVEWLTRAMIESGDTIEFDTHPIMDKHSIGGVPGNKISLLVVPIIAANGLLIPKTSSRAITGAGGTADLMEVLCPVEFSSQEVKEITEKVGGALVWGGATNIAPADDKLIRVEYPLSIDPYYQMLASIMAKKGAIGADNVVMDIPVGPSTKVPTVQEGQKLARDLINLGHRLGMNVECAITYGS... | Catalyzes the conversion of AMP and phosphate to adenine and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CMP and UMP in addition to AMP. Functions in an archaeal AMP degradation pathway, together with R15P isomerase and RubisCO. | Q466X0 |
Q92QZ9 | RL9_RHIME | 50S ribosomal protein L9 | Sinorhizobium | MEVILLERIAKLGQMGETVKVRDGFARNYLLPLGKALRANAANKARFESERSTLEARNLERKSEAQKVADSLDGKSFIIVRSAGETGQLYGSVAARDIVETLAAEGFNINRNQVDLNQPIKAIGLHKVTLHLHGEVDVAIEINVARSAEEAERQAKGESLTSADAIYGVDEDALKPEDFFNPEAELESEEE | Binds to the 23S rRNA. | Q92QZ9 |
B9DRT7 | ATPE_STRU0 | F-ATPase epsilon subunit | Streptococcus | MTQMTVQVVTPDGIKYDHQAKFISVETTDGEMGILPRHINLIAPLVIHEMKIRRTDDDNHVDWVAINGGIIEIKDNVVTIVADSAERSRDIDVSRAERAKLRAEREIEAAKSAHDIDEVQRAQVALRRALNRINVGNK | Produces ATP from ADP in the presence of a proton gradient across the membrane. | B9DRT7 |
Q8R173 | ZDHC3_MOUSE | Zinc finger DHHC domain-containing protein 3 | Mus | MMLIPTHHFRDIERKPEYLQPEKCAPPPFPGPAGAMWFIRDGCGIACAIVTWFLVLYAEFVVLFVMLVPSRDYAYSIINGIVFNLLAFLALASHCRAMLTDPGAVPKGNATKEFIESLQLKPGQVVYKCPKCCSIKPDRAHHCSVCKRCIRKMDHHCPWVNNCVGENNQKYFVLFTMYIALISLHALIMVGFHFLHCFEEDWTKCSSFSPPTTVILLILLCFEALLFLIFTSVMFGTQVHSICTDETGIEQLKKEERRWAKKTKWMNMKAVFGHPFSLGWASPFATPDQGKADPYQYVV | May also function as a calcium transporter. | Q8R173 |
Q1QDI9 | NTPPA_PSYCK | Nucleotide pyrophosphatase | Psychrobacter | MDIILASGSPRRRELLSRVQLEFTVISVDIDETPYQDESPEDYIVRMVAAKAEAATVQLNRQLKNNDAHIYQSLLSKPIILLTSDTIGVLPDGKTVLVKPNNREDAYRMWQQMSDSTHEVWTAVQATQLSLQPKRSDEFNNEQVWQIINQQQIIERTEVTFVALTLEMMSDYWDSGEPADKAGGYGIQGLGAAWVSRINGSYTNVVGLPLAQTLALIKEMNDTDTL | Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids. | Q1QDI9 |
Q7S9H0 | NUF2_NEUCR | Kinetochore protein 2 | Neurospora | MAFNPRMSILPPQPQQSRQRKKEEEAAYANMRLPDREIVGCINELGIPFTLADLQKPNPIQVQMIFEWFGELLMNKTRQTVDPAMRAAAEDVCGPELGEAMMPSDTRNLLGFYVSLRRLMLDCGVNDFSFNDLYKPTHDRLVRMLSYVINFVRFRESQTSVIDEHCNKAEQTKARIEQLYVENQNMEAQLEEMRHNRRAMEVLVQEKTVRNEELKKRLLELRRSQEKVAARLEEAKTKKGELAAELEEKTATKIALKQESAKLRPYVLQSPSALQASLAELSNTLNNDKAHIDALDRRSRALQTSTDSFSVVASDVASCI... | Acts as a component of the essential kinetochore-associated NDC80 complex, which is required for chromosome segregation and spindle checkpoint activity. | Q7S9H0 |
C6E4R4 | RPOB_GEOSM | Transcriptase subunit beta | unclassified Geobacter | MAYSIANNPLLRKNFAKIHKIIDIPNLIDIQKNSYKRFLQLDTPVDARKNSGLEAVFRSVFPIRDFSDTASLEYVSYSLGAPKYDVEECHQRGMTFAAPMKVKVRLVVWDVAKDPGTRSIRDIKEQEVYFGEIPLMTDNGTFIINGTERVIVSQLHRSPGVFYDHDKGKTHSSGKVLYSARVIPYRGSWLDFEFDHKDILYVRIDRRRKMPATVLLKALGYSNDALINYFYKSEDVKVGDNGSMTKIADAELLSNQKATADIVDPATGEVILKANRKFTKAAIRKMSEHGIKEIPISEEEVVGKVASHDIYDPATGEIIV... | DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | C6E4R4 |
A6GZM3 | LPXK_FLAPJ | Lipid A 4'-kinase | Flavobacterium | MNFLRKTLFPFAILYGFITSIRNFLFDCGILKSHAFPIPVIAVGNLSVGGTGKTPQIEYLIRLLSNKYQIATLSRGYKRKSEGFILANPTSNAEILGDEPFQFYKKFPNIQVAVAANRKNGIERLLSLPNKPEIILLDDAFQHRKVKAGFYILLTAYNDLFINDFMLPTGNLRESRSGAKRANMIIVTKCPKDISELAQNKIKEALINYNNKKAEVFFTFIDYDDKIYSANKALNVNEVKTASKLLLAGIAKPESFFAHLQSQNDECLVYPDHHHFLEKNITDIKEKAKNKIIITTEKDFVRLSEKLNSDNLFYLPIKSL... | Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA). | A6GZM3 |
B8ZRD4 | UPPP_MYCLB | Undecaprenyl pyrophosphate phosphatase | Mycobacterium | MTAVSAMSWWQVIVLAVVQGLTEFLPVSSSGHLAIVSRILFTGDAGASFTAVSQLGTEVAVLVYFGRDIVRILHAWCRGLTVTLHRTADYWLGWYVIIGTIPICILGLVCKDEIRSGIRPLWVVATALVAFSGVIAFAEYVGRQNRCIEQLNWRDALVVGVAQTLALIPGVSRSGSTISAGLFLGLDRELAARFGFLLAIPAVFASGLFSIPDAFHPITEGMSATGAQLLVATVIAFVVGLVAVSWLLRFLVQHNLYWFVGYRIVVGVGVLILLAVKTVAAT | Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin. | B8ZRD4 |
B0FHH8 | ML1P_MANSE | MD-2-related lipid-recognition protein | Manduca | MAALHWLLLAALLGCTLAEEQAIFYNCEEASEAVCSVKEVRINPCNPNKKCIFKKGVNASISFDFEPNFASSKLVTTLYGPFDVEFDEMTNVDACQYTKCPTEPGKSQVLDYTLYIGKKLPQGTYTFKWKLWNPEETSQLCCFKTTIKIRK | Binds to lipopolysaccharide from a variety of Gram-negative bacteria and to lipid A. | B0FHH8 |
Q2G1B9 | TARJ1_STAA8 | Ribitol-5-phosphate dehydrogenase 1 | Staphylococcus | MINQVYQLVAPRQFEVTYNNVDIYSDYVIVRPLYMSICAADQRYYTGSRDENVLSQKLPMSLIHEGVGEVVFDSKGVFNKGTKVVMVPNTPTEKDDVIAENYLKSSYFRSSGHDGFMQDFVLLNHDRAVPLPDDIDLSIISYTELVTVSLHAIRRFEKKSISNKNTFGIWGDGNLGYITAILLRKLYPESKIYVFGKTDYKLSHFSFVDDVFFINKIPEGLTFDHAFECVGGRGSQSAINQMIDYISPEGSIALLGVSEFPVEVNTRLVLEKGLTLIGSSRSGSKDFQDVVDLYIQYPDIVDKLALLKGQEFEIATINDL... | Catalyzes the NADPH dependent reduction of D-ribulose 5-phosphate to D-ribitol 5-phosphate. | Q2G1B9 |
U3KPV4 | A3LT2_HUMAN | Isoglobotriaosylceramide synthase | Homo | MALKEGLRAWKRIFWRQILLTLGLLGLFLYGLPKFRHLEALIPMGVCPSATMSQLRDNFTGALRPWARPEVLTCTPWGAPIIWDGSFDPDVAKQEARQQNLTIGLTIFAVGRYLEKYLERFLETAEQHFMAGQSVMYYVFTELPGAVPRVALGPGRRLPVERVARERRWQDVSMARMRTLHAALGGLPGREAHFMFCMDVDQHFSGTFGPEALAESVAQLHSWHYHWPSWLLPFERDAHSAAAMAWGQGDFYNHAAVFGGSVAALRGLTAHCAGGLDWDRARGLEARWHDESHLNKFFWLHKPAKVLSPEFCWSPDIGPR... | Synthesizes the galactose-alpha(1,3)-galactose group on the glycosphingolipid isoglobotrihexosylceramide or isogloboside 3 (iGb3) by catalyzing the transfer of galactose from UDP-Galactose to its acceptor molecule Gal-beta-1,4-Glc-ceramide. Can also catalyze the addition of galactose to iGb3 itself to form polygalactos... | U3KPV4 |
Q06H07 | RPOC2_DRIGR | Plastid-encoded RNA polymerase subunit beta'' | Drimys | MEVLMAERADLVFHNKVIDGTAMKRLISRLIDHFGMAYTSHILDQVKTMGFQQATATSISLGIDDLLTIPSKGWLVQDAEQQSLILEKHHHYGNVHAVEKLRQSIEIWYATSEYLRQEMHPNFRMTDPSNPVHIMSFSGARGNASQVHQLVGMRGLMSDPQGQMIDLPIQSNLREGLSLTEYLISCYGARKGVVDTAVRTSDAGYLTRRLVEVVQHIVVRRTDCGTIRGISVSPRNGIGMTEKMLIQTLIGRVLADDIYMGLRCIAARNQDIGVGLVNRFIAFRAQSIYIRTPFICRSTSWICRLCYGRSPTHGDLVELG... | DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | Q06H07 |
P38138 | GLU2A_YEAST | Reversal of TOR2 lethality protein 2 | Saccharomyces | MVLLKWLVCQLVFFTAFSHAFTDYLLKKCAQSGFCHRNRVYAENIAKSHHCYYKVDAESIAHDPLENVLHATIIKTIPRLEGDDIAVQFPFSLSFLQDHSVRFTINEKERMPTNSSGLLISSQRFNETWKYAFDKKFQEEANRTSIPQFHFLKQKQTVNSFWSKISSFLSLSNSTADTFHLRNGDVSVEIFAEPFQLKVYWQNALKLIVNEQNFLNIEHHRTKQENFAHVLPEETTFNMFKDNFLYSKHDSMPLGPESVALDFSFMGSTNVYGIPEHATSLRLMDTSGGKEPYRLFNVDVFEYNIGTSQPMYGSIPFMFS... | Catalytic subunit of glucosidase 2, which cleaves sequentially the 2 innermost alpha-1,3-linked glucose residues from the Glc(2)Man(9)GlcNAc(2) oligosaccharide precursor of immature glycoproteins. | P38138 |
B3WC74 | MUTS2_LACCB | Endonuclease MutS2 | Lacticaseibacillus | MNEKILKTLEYDKIQQALLGQVVTANGRQLVQAMQPLTDPVAVQQALDETADGASALRLKGGIPVPQLENIDPALKRVDIGAVLNGQELASISRVLQTVSAIDKFLTDLQDQIDFRQLYTLQESLTVLPQLSRRLKTAVDPDGTLTDEASPQLHGVREQIKSIEGKIRGKMTNYTRGAQSKYLSDPIVTIRDDRYVIPVKAEYRAKFGGVVHDQSATGQTLFIEPQVIVALNNRLREAQLAEVAEINRILAELSNELAPYTGQIKANAAVLGHFDFINAKARLAKAEKATEPLVSADNDVLLRDARHPLIDPHKVVGNDI... | Endonuclease that is involved in the suppression of homologous recombination and may therefore have a key role in the control of bacterial genetic diversity. | B3WC74 |
Q8DC53 | MUTS_VIBVU | DNA mismatch repair protein MutS | Vibrio | MKAEQQHTPMMQQYLRLKAENPDILLFYRMGDFYELFYDDAKKASQLLDISLTKRGASAGEPIPMAGVPFHAVEGYLAKLVQLGESVAICEQVGDPATSKGPVERKVVRIVTPGTVTDEALLSERLDNLIAAIYHHNGKFGYATLDVTSGRFQLVEPQSEEAMAAELQRTSPRELLFPEDFEPVHLMTGRNGNRRRPVWEFELETAKQQLNQQFGTKDLVGFGVENAVLGLCAAGCLIQYVKDTQRTTLPHIRALTYDRQDDSVILDAATRRNLELTQNLAGGSDNTLAAVLDRCATPMGSRMLKRWIHQPMRCITTREH... | This protein is involved in the repair of mismatches in DNA. It is possible that it carries out the mismatch recognition step. This protein has a weak ATPase activity. | Q8DC53 |
B5FB35 | MURG_ALIFM | Undecaprenyl-PP-MurNAc-pentapeptide-UDPGlcNAc GlcNAc transferase | Aliivibrio | MKNKNKRLLVMAGGTGGHVFPGLAVAKQLQSEGWEIRWLGTADRMEADLVPKHGIEIDFIKVKGLRGQGLKKLIAAPFQILGAISQAKKHIKAWQPDVVLGMGGYVSGPGGIAAWLSGIPVVLHEQNAVAGLTNQWLSKIAKRVFQAFPGAFPNAEVVGNPVREDVCQLPHPKERFAQRTGPIRLLVMGGSQGARILNTTLPEALPQLSHEIEIWHQAGKGSQETVEQAYRDNGIADAKVTEFIDNVAEAYAWADLLVCRSGALTVSEVSAAGVGSIFIPFMHKDRQQALNADHLVQCGAAQMIEQQDLTVQGLVDTLNG... | Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II). | B5FB35 |
Q9HU66 | THII_PSEAE | tRNA 4-thiouridine synthase | Pseudomonas | MKLIVKTFQEITIKSRPVRKRFIRQLAKNIRAVLRDLDPELKVEGEWDNLEVETAVVDAKARREMIERLTCTPGIGHFLEVHEYPLGDFDDILAKCKAHFGDQLAGKTFAVRCKRAGKHAFTSMEVERYVGSGLRRECGAAGIDLKQPEVEVRMEIRLDRLFVIHRQHPGLGGYPLGALEQVLVLMSGGFDSTVAAYQMMRRGMISHFVFFNLGGRAHELGVMEVAHYLWEKYGRSQRVLFVSVPFEEVVGEILTKVDDSYMGVTLKRMMLRAASRVAERLELDALVTGEAISQVSSQTLPNLSVIDRVTDTLVLRPLIV... | 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 biosynt... | Q9HU66 |
Q7M8W7 | TRPB2_WOLSU | Tryptophan synthase beta chain 2 | Wolinella | MTMFMPTPSQFDPDERGHFGKFGGRFVPETLMPALLELESAYNELRFDREFWSEVDYYLKEYVGRPSPLYYAERLSDELGAKIYLKREDLNHTGAHKINNTVIQGLLAKRLGKKKIIAETGAGQHGVATATIAALLGLECEVFMGSKDTARQELNVFRMKLLSSKVQSVESGSKTLKDAMNEAIRHWVTHARDTFYIIGTVAGPHPYPMMVRDFQSVISFEAKKQILEKEERLPDYVIACIGGGSNAAGMFARFLDEESVRCIGIEAGGLGIESHHHGASLAKGSPGILHGQMSYLLQDSEGQIEEAYSISAGLDYPGIG... | The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. | Q7M8W7 |
B2JA20 | TPIS_NOSP7 | Triose-phosphate isomerase | Nostoc | MRKIVIAGNWKMFKTQAETQEFLQGFLPHLEETPQGREVILCPPFTDLSVLSKTLHGSLIQLGAQNIHWEEFGAYTGEISGPMLTESGVRFVIVGHSERRQYFGETDATVNLRLRTAQRFGLTPILCVGETKQQRDAGETESLIALQLDKGLVDIDQNNLVIAYEPIWAIGTGETCEAVEANRIIGLIRSQLSNPNVSIQYGGSVKPNNIDEIMAQPEIDGVLVGGASLEPESFARIVNFHLV | Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P). | B2JA20 |
P29529 | OLEO_HELAN | Oleosin | Helianthus | TTTTYDRHFTTTQPHYRQDDRSRYDQQTHSQSTSRTLAIIALLPVGGILLGLAALTFIGTLIGLALATPLFVIFSPIIVPAVLTIGLAVTGFLASGTFGLTGLSSLSYLFNMVRQTAGSVPESLDYVKGTLQDAGEYAGQKTKDFGQKIQSTAHEMGDQGQVGVHAQVGGGKEGRKSGDRT | May have a structural role to stabilize the lipid body during desiccation of the seed by preventing coalescence of the oil. Probably interacts with both lipid and phospholipid moieties of lipid bodies. May also provide recognition signals for specific lipase anchorage in lipolysis during seedling growth. | P29529 |
B1M6N9 | TRUA_METRJ | tRNA-uridine isomerase I | Methylobacterium | MPRYKLVIEYDGSPFCGWQRQADDPTVQGAIEAAVTRFSGENARLTCAGRTDAGVHAIHQVAHLDLAKDWRTDTVRDALNAHLRPQPVAILSAETVPDSFDARHSAIRRHYRYRILNRRSPAALTRAHVWHVPWPLDADLMHDAAQRLVGRHDFSAFRAAECQANSPIRTLEQLDVARAPMALHDEIVVATAARSFLHHQVRAMVGTLMLAGCRRLAADDVAEILASGDKSRCGPLAPAAGLTFVGVDYDPGK | Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs. | B1M6N9 |
B3Q8S9 | KDPC_RHOPT | Potassium-translocating ATPase C chain | Rhodopseudomonas | MLKEVRPAVVSLLALTMITGLAYPLAVTGLATVLFPYQAQGSLVERGGKVVGSALIGQEFKGDEYFHGRPSATVAPDPADSSKTVSAPYNAANSGGSNLGPTSKALADRLSEDVAKLKAENPAAPIPVDLVTTSGSGLDPDISPEGALFQVPRVAKARGVTEEQIRKLVGASIEQPLGGVLGESRVNVLKLNLALDAAAPR | Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit acts as a catalytic chaperone that increases the ATP-binding affinity of the ATP-hydrolyzing subunit KdpB by the formation... | B3Q8S9 |
Q0AGZ8 | UBIC_NITEC | Probable chorismate pyruvate-lyase | Nitrosomonas | MKANPPLAWHPVPVSAPVNLRWWLMHQESLTRLLQAHCEHFRVEPVFQTLATACIDELEVMNLRRQNQVLVREVYLRCNETPVVFAHSIVKKEHLRGAWRGLSRLGNRSLGTMLFTNPLIQRTPLAFKKLKPHHPLFERACKQLQMRPINLWARRSLFILLRQPILVTEVFLPAIHQL | Removes the pyruvyl group from chorismate, with concomitant aromatization of the ring, to provide 4-hydroxybenzoate (4HB) for the ubiquinone pathway. | Q0AGZ8 |
Q493I7 | RS13_BLOPB | 30S ribosomal protein S13 | Candidatus Blochmannia | MVRIAGVNVPDRKHAVVALMSIYGIGKSRARSICLNTGIDEHVQLCKLSEIHIDKLRDAVDEYIVEGDLRREVTLNIKRLIDLGTYRGLRHRRNLPVRGQRTRTNARTCKGPRKSMNKQFK | Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA. In the 70S ribosome it contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit (bridge B1b), connecting the 2 subunits; these bridges are implicated in subunit movement. Contacts the tRNAs in the A and P-sites. | Q493I7 |
A4J247 | LIPA_DESRM | Sulfur insertion protein LipA | Desulforamulus | MNKRKPDWLKIKLQGAEKSHEVKDMLKRLSLHTVCEEANCPNLIECFGRKTATFMILGSVCTRNCTFCNVTKGLTQAVDAEEPSNVAQAVKELGLKHVVITSVTRDDLPDGGAGHFAKVIEKLRPTEVIVEVLIPDFQGDREALDTVIRAKPHILNHNIETVPRLYATVRPKASYARSLELLKNSKELDPGIFTKSGIMVGLGEQEEEVIAVLQDLRAVDCDLLTIGQYLAPSAKHHPVIEYIHPELFKKYKDVAYEMGFKYVASDPLVRSSYHAADVSHIIG | Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives. | A4J247 |
A2WXD3 | MRS2E_ORYSI | Magnesium transporter MRS2-E | Oryza sativa | MERRAQPVSAAVAPVTGRRKGAAASRKWMVVPAVGEERRVEFGKHQIMKMTGLPGRDLRVLDPVLSYPSTILGRDRAIVVRLQGVKAIITATEVLVPDHDDVLLASFLLDLRSRLSLPDAAPSTNPAAADRGNGTEQGDQGSVPGLAISGAGNAKIPPFEFKVLEVCLEHACKDLESQTRSLEKEAYPALDKLGSKVSTLNLDHVRNLKSRMVDLSGRVQKIRDELEHLLDDDMDMSEMYLTRKLSFQGLSGSLSRADSHKYASVDHDDDREEEDHDDETESGRESSVYVKPDIEELEMLLEAYFVQIDGTLNTLYHIRE... | Magnesium transporter that may mediate the influx of magnesium. | A2WXD3 |
P55046 | TYRT_STRGB | Tyrosinase cofactor | Streptomyces | MPDITRRRAYTTAAAVAATASAAAPTAAPAATAAARHDHTAPDSFDEVYKGRRIQGGPASGGGHHHEHGGGYAVFVDGVQLHVMQNADGTWISVVSHYAPVATPRAAARAAVDELQGAPLLPFPTN | This protein may function to deliver copper to tyrosinase. | P55046 |
Q56NG9 | BPTA_BORBD | Borrelial persistence in ticks protein A | Borreliella | MRKILFFGLLSICFLFVFFFYKQKENKIIYNKIVEKFEDNVVIDETYTHLFKDSNLKELVFIKSRLIIPELEHKKMMKATGYRADAYRALSTVYKFDFKVHDNKILGFKSVIFEGFEDAKVSKHENNLPSEKWQQLKDFNIGDPNINEKFFHLEFPFVVKNTLCVTISKGFFKKIKKLKRLKIMLISNEDREYKIDIENFLPKYNL | Virulence-associated protein essential for survival of the bacterium within the tick host and therefore within the natural life cycle of the spirochete. | Q56NG9 |
Q8IWE4 | DCNL3_HUMAN | Squamous cell carcinoma-related oncogene 3 | Homo | MGQCVTKCKNPSSTLGSKNGDREPSNKSHSRRGAGHREEQVPPCGKPGGDILVNGTKKAEAATEACQLPTSSGDAGRESKSNAEESSLQRLEELFRRYKDEREDAILEEGMERFCNDLCVDPTEFRVLLLAWKFQAATMCKFTRKEFFDGCKAISADSIDGICARFPSLLTEAKQEDKFKDLYRFTFQFGLDSEEGQRSLHREIAIALWKLVFTQNNPPVLDQWLNFLTENPSGIKGISRDTWNMFLNFTQVIGPDLSNYSEDEAWPSLFDTFVEWEMERRKREGEGRGALSSGPEGLCPEEQT | Contributes to the neddylation of all cullins by transferring NEDD8 from N-terminally acetylated NEDD8-conjugating E2s enzyme to different cullin C-terminal domain-RBX complexes and may play a role in the cell cycle progression by regulating the SCF ubiquitin E3 ligase complex, after UV damage . At the cell membrane, c... | Q8IWE4 |
G3XCR8 | RNC_PROMA | Ribonuclease III | Prochlorococcus | MTKKDIVSIVSKERAEEIYGLLTQSNLHSSDIEVIKKNEDYCLKILNEALTHTSFNLSINHERLEFQGDAVLRLAASEYIQSHFPKLSVGDRSALRAQLVSDRWLAKVGYKIGIKTTMLIANKALKDEAATDTICAEGTEALIGALYECLRNIDAIQNWLEPYWNIESEEVLADPHKQNEKSALQEWSQGQGLNKPIYTIKEISKQHGDLKRFYCTVHIQNDFRGEGWGSSRKKAQKEAAKEALKKLTN | Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the organism. | G3XCR8 |
B3MQP7 | T23O_DROAN | Tryptophanase | Sophophora | MSCPYAGSGNDHDDAAVPLSTEVGKIYGEYLMLDKLLDAQCMLSKEDKRPVHDEHLFIITHQAYELWFKQIIFEFDSIRDMLDAEVIDETKTLEIVKRLNRVVLILKLLVDQVPILETMTPLDFMDFRKYLAPASGFQSLQFRLIENKLGVLTEQRVRYNQKYSDVFGGDEDALTAIRSSEQEPSLLELVQRWLERTPGLEESGFNFWEKFQQSVDKFLEAQVHSAMEEPVERAKNYRLMDIEKRREVYRSIFDPAVHDALVRRGDRRFSHRALQGAIMITFYRDEPRFSQPHQLLTLLMDIDSLITKWRYNHVIMVQRM... | Heme-dependent dioxygenase that catalyzes the oxidative cleavage of the L-tryptophan (L-Trp) pyrrole ring and converts L-tryptophan to N-formyl-L-kynurenine. Catalyzes the oxidative cleavage of the indole moiety. | B3MQP7 |
A4XHR9 | ILVD_CALS8 | Dihydroxy-acid dehydratase | Caldicellulosiruptor | MRSDIVKKGFEKAPQRSLFKAMGYTDEEIRRPLIAVVNSWNEVVPGHIHLDKIAEAVKAGIRLAGATPMEFNVIGVCDGIAMGHIGMKYSLITRELIADSIEAMVMAHQFDGMVLIPNCDKIVPGMLMAAARVNIPSILISGGPMLAGRVDNKVCDLNSVFEAVGAYSAGKITDEELFALEENACPGCGSCSGMFTANTMNCLSEVLGMALPGNGTIPAVMAARIRLAKMAGMKIVELVERDIKPSDILTIEAFENALTVDMALGGSTNTILHLPAIANELGIKLNLDIINDISDKTPNLCKLSPAGHYHIEDLYFAGGV... | Functions in the biosynthesis of branched-chain amino acids. Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3-methylpentanoate (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3-methylpentanoate (2-oxo-3-methylvalerate) and of (2R)-2,3-dihydroxy-3-methylbutanoate (2,3-dihydroxyisovalerate) into 2-oxo-3-methylbutanoate (... | A4XHR9 |
A0KJ41 | RLMN_AERHH | tRNA m2A37 methyltransferase | Aeromonas | MSETKTNLLDLDRDAMRAFFVELGEKPFRADQVMKWIYHFGCDDFDQMNNVNKVLRERLKAIAEIRAPEVSREQRSSDGTIKWALQVGGQEVETVYIPEEDRATLCVSSQVGCALECKFCSTAQQGFNRNLKVSEIIGQVWRAAKIVGGKRPITNVVMMGMGEPLLNLANVVPAMRLMMDDFGYGISKRRVTISTSGVVPALDMLGDQIDVALAISLHAPNDKLRSEIMPINDKYNIEEFLAGVRRYLGKSNANGGRVTVEYVLLDHINDDMQHAHELAKVLKDTPSKINLIPFNPFPGNPYGKPSNSRIDRFSKVLMEY... | Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity. | A0KJ41 |
Q9HAY2 | MAGF1_HUMAN | MAGE-F1 antigen | Homo | MLQTPESRGLPVPQAEGEKDGGHDGETRAPTASQERPKEELGAGREEGAAEPALTRKGARALAAKALARRRAYRRLNRTVAELVQFLLVKDKKKSPITRSEMVKYVIGDLKILFPDIIARAAEHLRYVFGFELKQFDRKHHTYILINKLKPLEEEEEEDLGGDGPRLGLLMMILGLIYMRGNSAREAQVWEMLRRLGVQPSKYHFLFGYPKRLIMEDFVQQRYLSYRRVPHTNPPEYEFSWGPRSNLEISKMEVLGFVAKLHKKEPQHWPVQYREALADEADRARAKARAEASMRARASARAGIHLW | Enhances ubiquitin ligase activity of RING-type zinc finger-containing E3 ubiquitin ligases. Proposed to act through recruitment and/or stabilization of the E2 ubiquitin-conjugating enzyme at the E3:substrate complex. MAGEF1-NSMCE1 ubiquitin ligase complex promotes proteasomal degradation of MMS19, a key component of t... | Q9HAY2 |
Q1MAA2 | RGMG_RHIL3 | Putative ribose/galactose/methyl galactoside import ATP-binding protein | Rhizobium | MAVSPTTMAAVRASGAVPNAEYLLSAEGVRKEFPGVVALDDVQFRLKRASVHALMGENGAGKSTLMKILAGIYTPDKGDIRLKGIEIQLKSPLDALENGIAMIHQELNLMPFMTVAENIWIRREPKNRLGFIDHGVMHRMTEELFTRLNIAIDPDIEVRFLSVANRQMVEIAKAVSYNSDVLIMDEPTSALTEREVEHLFRIIRDLKAQGIGIVYITHKMNELFEIADEFSVFRDGRYIGTHASTDVTRDDIIRMMVGREITQMFPKEEVPIGEVMLSVKDLCLNGVFKNVSFEVRAGEILGVAGLVGSGRSNVAETLFG... | Part of an ABC transporter complex involved in carbohydrate import. Could be involved in ribose, galactose and/or methyl galactoside import. Responsible for energy coupling to the transport system. | Q1MAA2 |
A1AWB1 | PNP_RUTMC | Polynucleotide phosphorylase | Candidatus Ruthia | MGINTKSFVMGKHTITLETGRIARQAHGAVLVSMDDTQVLVTVVGSKKMHPGQDFFPLSVDYIEKTYAAGKIPGGFLKREARPSEKETLTSRLIDRPIRPLFPNGFMNEVQVLITVISANSEVDPDIISMLGVSAALSISGIPFNGPIGSARVGYSNGKYTLNPTYTELVDSDLDMVVAGTDKAILMVESEASELSEKIILDAIIYAHEQYQVAITNIAEFVTQVGVQKWDWEAPATNEVLLSNIKSQFGKQINEAYKIKEKLNRHVKVGEIKTAAIEALVNEDKNGNSIDEVSKYFNKVEKSTVRERILNNDPRIDGRD... | Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction. | A1AWB1 |
P40390 | PGM_NEIGO | Glucose phosphomutase | Neisseria | MASITRDIFKAYDIRGIVGKTLTDDAAYFIGRAIAAKAAEKGIARIALGRDGRLSGPELMEHIQRGLTDSGISVLNVGMVTTPMLYFAAVNECGGSGVMITGSHNPPDYNGFKMMLGGDTLAGEAIQELLAIVEKDGFVAADKQGSVTEKDISGAYHDHIVGHVKLKRPINIAIDAGNGVGGAFAGKLYKGLGNEVTELFCEVDGNFPNHHPDPSKPENLQDLIAALKNGDAEIGLAFDGDADRLGVVTKDGNIIYPDRQLMLFAQDVLNRNPGAKVIFDVKSTRLLAPWIKEHGGEAIMEKTGHSFIKSAMKKTGALVA... | This enzyme participates in both the breakdown and synthesis of glucose. | P40390 |
A5UQQ2 | RIMO_ROSS1 | Ribosome maturation factor RimO | Roseiflexus | MKFHIITLGCPKNQVDSEGMSSILAAQGHTPVAHADDADVVVVNTCSFIAAAREETLDVLREVAARKTPGQYLVAAGCMAESHSALVAAAPGVDALLSTREWMRIGDVVDTLQREPAVAASSAAREIIPLSSAPASSDDLRVPGAYADWRTAPIRRRITGPSAYLKISDGCNLRCAFCTIPSFKGDMRSKAVGAILGEAQELADAGVKEIVLVAQHLTDYGRDLGLKDGLALLLDELCAVLPKDRWVRLMYAYPHGISERLIATMARHPQICHYLDMPLQHAHPETLRRMHRPPDSDRTRRLIADLRAAMPDIALRSTFI... | Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein S12. | A5UQQ2 |
Q6AQ97 | FMT_DESPS | Methionyl-tRNA formyltransferase | Desulfotalea | MVSSQIESEEKSLRIIFMGTPDFASSNLRALLAGPDQVVAVVTQPDRPKGRGKKLTSPPVKVIAEEAGLPVLQPTKVRTDEFLEALAAYAPDLIVVTAYGRILPKPILDLAPLGCINVHGSLLPKYRGAAPIQWAVIQGDDEVGVTTMQMDEGMDTGDILLRKIIIPSPDETAGTLFDKLAELGTSALLETIEGLKKGTIRAEAQDHAQATEAPMLSKNDGLIDWSRTATELESLIRGMDPWPSAFCFLEGKRLRLFMPEVSYQKTDAQPGAVLRAGRDGLLIATGKNCLLVKEIQPEGKKRMTVEAFLCGAKIGAETVL... | Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus. | Q6AQ97 |
B0V6G5 | OTC_ACIBY | Ornithine carbamoyltransferase | Acinetobacter calcoaceticus/baumannii complex | MALRHFLTLRDLSTLELNRILERASELKKMQQSNKVYQPFVGKVLGMIFEKSSTRTRISFEAGINQFGGSAIFLSPRDTQLGRGEPIEDSARVISSMLDIVMIRTFGHDIVERFASYSKVPVINGLTDDHHPCQLLADLQTYIEHRGSIEGKTVAWIGDGNNMCNSYIEAAHMMGFKLKIASPKGYEPKPEFLAEFGHCVELFDNAEDAAVNADLIVTDVWASMGQEEEQKLREKAFANFQVNEKLMGLAHPDCLFMHCLPAHRGEEISETMLDHKNAVVWDEAENRLHAQKALMEFLLNENLKKA | Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline. | B0V6G5 |
Q13EN8 | UBIE_RHOPS | Demethylmenaquinone methyltransferase | Rhodopseudomonas | MNQPGETTHFGFRDVPLNDKQTMVNDVFHSVASRYDLMNDLMSGGMHRLWKDVMITTLNPPRDDAPFRLLDVAGGTGDISFRAAKASGAGFQATVCDINTDMLEVGRQRAVQRHLDGQVDFVEGNAEALQFPDRSYDAYTIAFGIRNVPRIDLALKEAYRVLKPGSRFLCLEFSSVDVPGLNKIYDLFSFKVIPEIGRVVTGDAESYQYLVESIRKFPKPYDFAEMMRDAGFARVNWQMMSGGIVALHSGWRL | 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). | Q13EN8 |
D2NWE2 | ECFT1_LISM1 | Energy-coupling factor transporter transmembrane protein EcfT 1 | Listeria | MIEKLILGRFVPGESLIHGLDARTKLLAGFYYIGILFLANNWWTYALMVLFTLMVVQMTGIKLKVFIKGVKPLIWLILFTVVMQILFASGGTIYFDWGPFTISSFGLLNGVFVFLRFVLIIIMSTVITLTTTPMNLTDAIAYILRPFAVLKVPVNDIALMISVALRFIPTLMGETDKIMKAQRARGVDFGEGNLFEQMKVVVPIFIPLFVSSFNRAEELADAMEARGYQGGEGRTRFRILHWHFGDLIAACVMILLTAGLVILRTS | Transmembrane (T) component of an 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. | D2NWE2 |
Q01579 | GSTT1_RAT | Glutathione S-transferase 5 | Rattus | MVLELYLDLLSQPCRAIYIFAKKNNIPFQMHTVELRKGEHLSDAFAQVNPMKKVPAMKDGGFTLCESVAILLYLAHKYKVPDHWYPQDLQARARVDEYLAWQHTTLRRSCLRTLWHKVMFPVFLGEQIRPEMLAATLADLDVNVQVLEDQFLQDKDFLVGPHISLADVVAITELMHPVGGGCPVFEGRPRLAAWYRRVEAAVGKDLFLEAHEVILKVRDCPPADPVIKQKLMPRVLTMIQ | Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Also binds steroids, bilirubin, carcinogens and numerous organic anions. Has dichloromethane dehalogenase activity. | Q01579 |
A5DJQ5 | ALG3_PICGU | Dolichyl-P-Man:Man(5)GlcNAc(2)-PP-dolichyl mannosyltransferase | Meyerozyma | MEETHEPKKHSEKEEIEDGLSSKTEAPHLPEFTFKNVCNDIINGVIALFMDPFCNAIVVPILVVFTSIACKIVIANVKYTEIDFKTYMQQIDMINDGELDYSLIAGDTGPIVYPAGFVQIYQWLSWLSSGGEDIPVVQSVFGYLHTLTVLLTCCTYSLVGDVQPWAYMLIVASKRLMSIYVLRLFNDCFTTACMVGVTLVLQAASYWFDTLGSTLVFLLTLVAADLYSMAISIKMNALLFMPAFLIVVYFLCMENILKLLAVILVMVLVQVMVGWKFLLVLFHDEDANYLRMTYLQRAFDFKRSFLYEWTVNWRFVPEEY... | Adds the first Dol-P-Man derived mannose in an alpha-1,3 linkage to Man(5)GlcNAc(2)-PP-Dol. | A5DJQ5 |
Q39C44 | CCA_BURL3 | Phosphatase | Burkholderia cepacia complex | MNIYAVGGAIRDELLGVPVQDRDYVVVGATPEQMAAQGFRPVGKDFPVFLHPRTQEEYALARTERKTAAGYHGFQFHYAPDVTLDEDLARRDLTVNAMAREVSPEGELVGPVIDPFDGQADLRARVFRHVSDAFVEDPVRILRIARFAARFADFTVADETLALMRRMVDAGEVDALVPERVWQEIARGLMEAKPSRMFAVLRECGALARILPEVDALWGVPQRADYHPEVDTGVHVMMVVDYAAKQGYSLPVRFAALTHDLGKATTPADVLPRHVGHEGRSVDLLKPLCERLRVPNECRDLALVVAREHGNLHRVMEMGA... | Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. Also shows phosphatase, 2'-nucleotidase a... | Q39C44 |
A4IRD5 | MINC_GEOTN | Probable septum site-determining protein MinC | Geobacillus | MAKQKQQYVTIKGTKDGLTLYLDDRCSYDDLMKEIEERLVKRSSVAANSPLVSVHLKVGNRYLTPAQEEELRALIRRSKNLVVDSIESNVISKAEAIEWVQKTEIVTVSRIVRSGQVLHVEGDLLLLGDVNPGGTVIAGGNIFILGALRGIAHAGYAGNKEAIIAASVMKPMQLRIGDVMNRAPDYKTDERNEMECAYINEHNQIVVDRLQLLMHLRPNLTRLERRM | Cell division inhibitor that blocks the formation of polar Z ring septums. Rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they mature into polar Z rings. Prevents FtsZ polymerization. | A4IRD5 |
Q27022 | SP23_TENMO | Spermatophorin SP23 | Tenebrio | MVASIAGEEEPAAEKSQQSPDHFQPYRPYYYPPYRGYPITYPYPYPHGYPKPYHNFQTIAKPNEGPTDQPEANSANSIEEGGVSKRLFIEPIFNLFRPRPRDPIVVNQAPPPPPVIYQAPPPPPPPPIFQQAPPTIYQQPSPTIIQQAPQPSVTKLVYSQPEPSHSVIYQTQPKTELVYLNQ | Structural protein of a layer within the wall of the spermatophore produced probably by cell type 4 of the bean-shaped gland (BAG). Fixation in the spermatophore seems to require covalent cross-linking of spermatophorins. | Q27022 |
Q493M1 | TRMD_BLOPB | tRNA [GM37] methyltransferase | Candidatus Blochmannia | MLLGVITLFPDMFQSIVRYGIVGRAIRRGILSIKLWNPRLFTYDRHHSVDARPYGGGPGMLMMIEPLRNAINQAKDELGNNIKVIYLSPQGRKLKQKYVYKLAYDHQKLILVCGRYQGIDERLIQTEIDEEWSIGDYILSGGELAAMVLIDTISRVLPGVLGNQDSKESDSFSKERLDCPHYTRPETFDGMKVPSVLLSGNHDEIHRWKQKQALGRTWIKRPDLLNYIQLTNEEKNLLSEFKNEYLLSLNKKTRK | Specifically methylates guanosine-37 in various tRNAs. | Q493M1 |
Q94JV5 | NILP2_ARATH | Protein nitrilase 1 homolog | Arabidopsis | MNAYSVSLDFTKPSLFTRITLSSQIPLTMATTVNKTVRVAAAQMTSVNDLMTNFATCSRLVQEAALAGAKLICFPENFSFVGDKEGESVKIAEPLDGPVMERYCSLARDSNIWLSLGGFQERFDDTHLCNTHVVIDDAGMIRDTYQKMHLFDVDVPGGSSYKESSFTVPGTKIVSVDSPVGRLGLTVCYDLRFPKIYQQLRFEQKAQVLLVPSAFTKVTGEAHWEILLRARAIETQCYVIAAAQAGKHNEKRESYGDTLIIDPWGTVVGRLPDRVSTGIVVADIDFSLIDSVRTKMPIDKQRVSIDL | Catalyzes the hydrolysis of the amide bond in N-(4-oxoglutarate)-L-cysteinylglycine (deaminated glutathione), a metabolite repair reaction to dispose of the harmful deaminated glutathione . Possesses amidase activity toward deaminated ophthalmate in vitro . | Q94JV5 |
A6URS1 | IF2P_METVS | Probable translation initiation factor IF-2 | Methanococcus | MALRCPIVSVLGHVDHGKTSLLDKIRSTRVTQREAGGITQHIGASEIPINTIKKVSKDLLGLFNANLSIPGLLVIDTPGHEAFTSLRKRGGALADIAILVVDINEGFKPQTIEAINILKQCKTPFVVAANKLDRIPGWSSSNGPFILNFNEKVQHPNAMTEFEIRLYENVIKHLNELGFDADLFSRVKDTTRTINVVPVSAITGEGVPDLLIIIAGLAQKFLEQKLALNVEGYAKGTVLEVKEEKGLGRTIDAIIYDGIARTGDYIVIGNPDGIVTSKVKALLKPKELDEMRDPKDKFKPSREISAATGVKISAPELEMV... | Function in general translation initiation by promoting the binding of the formylmethionine-tRNA to ribosomes. Seems to function along with eIF-2. | A6URS1 |
B2VKN8 | TTCA_ERWT9 | tRNA 2-thiocytidine biosynthesis protein TtcA | Erwinia | MQSNQENSKKGQYNLNKLQKRLRRNVGEAIADFNMIEEGDRIMVCLSGGKDSYTMLEILRNLQQSAPISFSLVAVNLDQKQPGFPAHILPEYLEQQGVEYKIVDEDTYSIVKEKIPEGKTTCSLCSRLRRGILYRTASELGCTKIALGHHRDDILQTLFLNMFYGGKMKGMPPKLMSDDGQHIVIRPLAYCREKDIERFAIARQYPIIPCNLCGSQPNLQRQVIGDMLRDWDKRYPGRIETMFTAMQNVVPSHLADADLFDFKQIRHGSEVIDGGDLAFDRETLPLQPSAWQPEEDEATPARLDVVQIR | Catalyzes the ATP-dependent 2-thiolation of cytidine in position 32 of tRNA, to form 2-thiocytidine (s(2)C32). The sulfur atoms are provided by the cysteine/cysteine desulfurase (IscS) system. | B2VKN8 |
Q1IDA6 | UBIG_PSEE4 | 3-demethylubiquinone 3-O-methyltransferase | Pseudomonas | MSNVDHAEIAKFEALAHRWWDRESEFKPLHDINPLRVNWIDERVSLAGKKVLDVGCGGGILSEAMAQRGATVTGIDMGEAPLAVAQLHQLESGVDVEYRQITAEALAEEMPEQFDVVTCLEMLEHVPDPSSVIRACYRMVKPGGQVFFSTINRNPKAYLLAIIGAEYILKMLPRGTHDFKKFIRPSELGAWSRVAGLEVKDIIGLTYNPLTKHYKLSNDVDVNYMIQTLREE | O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway. | Q1IDA6 |
Q4R4T0 | RPN1_MACFA | Ribophorin-1 | Macaca | MEAPVARLFLLLLLGSWTPAPGSASSEAPPLINEDVKRTVDLSSHLAKVTAEVVLAHLGGSSTSRATSFLLALEPELEARLAHLGVQVKGEDEEDNNLEVRETKIKGKSGRFFIVKLPVALDPGAKISVIVETVYTHVLQPYPTQITQSEKQFVVFEGNHYFYSPYPTKTQTMRVKLASRNVESYTKLGNPTRSEDLLDYGPFRDVPAYSQDTFKVHYENNSPFLTITSMTRVIEVSHWGNIAVEENVDLKHTGAVLKGPFSRYDYQRQPDSGISSIRSFKTILPAAAQDVYYRDEIGNVSTSHLLILDDSVEMEIRPRF... | Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-... | Q4R4T0 |
P55002 | MFAP2_MOUSE | Microfibril-associated glycoprotein 1 | Mus | MRAACLFLLFMPGLLAQGQYDLDPLPPFPDHVQYNHYGDQIDNADYYDYQEVSPRTPEEQFQSQQQVQQEVIPAPTPEPAAAGDLETEPTEPGPLDCREEQYPCTRLYSIHKPCKQCLNEVCFYSLRRVYVVNKEICVRTVCAHEELLRADLCRDKFSKCGVMAVSGLCQSVAASCARSCGGC | Component of the elastin-associated microfibrils. | P55002 |
P54406 | GBG_CAEEL | Guanine nucleotide-binding protein subunit gamma | Caenorhabditis | MENIKASTEQLCAEANIQRKKVSEVSKELLDFCEKNKTNDMLVSGPTDQHNPFQEKKSCSVL | Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction. | P54406 |
Q60022 | FUMC_THEAQ | Iron-independent fumarase | Thermus | MEYRVERDTMGEVKVPADRYWGAQTQRSLEHFRIGAWRFRMPLEIIRAYGMLKKAAARANLELGELPEEIARAIIQAAEEVIAGKLDDHFPLVVFQTGSGTQTNMNVNEVIANRASEILGKPLGSKYVHPNDHVNRGQSSNDTFPTAMYVATVLALHQHLYPAVEGLIATFEEKARAFDGIVKVGRTHLMDAVPITLGQEVGSWAAQLRNTLAMVKEAEKGLYNLAIGGTAVGTGLNAHPRFGELVARYLAEETGLPFRVAENRFAALAAHDELVHVMGALRTLAGALMKIGNDIRWLASGPYGGIGEIFIPANEPGSSI... | Involved in the TCA cycle. Catalyzes the stereospecific interconversion of fumarate to L-malate. | Q60022 |
A5D7M3 | DRC4_BOVIN | Growth arrest-specific protein 8 | Bos | MAPKKKGKKGKGKGTPIVDGLAPEDMSKEQVEEHIGRIREELDREREERNYFQLERDKIHTFWEITRRQLEEKKAELRNKDREMEEAEERHQVEIKVYKQKVKHLLYEHQSSLTEMKAEGTVVMKLAQKEHRAQEGTLRRDMRALKVELKEQELANEVMVKNLRLKHTEEITKMRNDFERQVREIEAKYDKKMKMLRDELDLRRKTEIHEVEERKNGQITTLMQRHEEAFTDIKNYYNDITLNNLALINSLKEQMEDMGKKEEHLEKEMTEVAMQNRRLADPLQKAREEMSDMQKKLGSYERDKQILVCTKARLKVTEKE... | Component of the nexin-dynein regulatory complex (N-DRC), a key regulator of ciliary/flagellar motility which maintains the alignment and integrity of the distal axoneme and regulates microtubule sliding in motile axonemes. Plays an important role in the assembly of the N-DRC linker. Plays dual roles at both the primar... | A5D7M3 |
B2HJL7 | RL19_MYCMM | 50S ribosomal protein L19 | Mycobacterium | MNRLDFVDQASLRDDIPAFSPGDTINVHVKVIEGAKERIQVFKGVVIRRQGGGIRETFTVRKESYGVGVERTFPVHSPNIDHIEVVTRGDVRRAKLYYLRELRGKKAKIKEKR | This protein is located at the 30S-50S ribosomal subunit interface and may play a role in the structure and function of the aminoacyl-tRNA binding site. | B2HJL7 |
B8G1Y5 | RL15_DESHD | 50S ribosomal protein L15 | Desulfitobacterium | MKLHELKPAQGSTKAPKRLGRGIGSGTGKTSGKGHKGQKARAGGGVRPGFEGGQQPLSRRMPKRGFTNIFKKEYVVLNVRDLEERFENGAVVGYESLFEVGLIKTIKDGVKILGTGELTKALTVQVDKVSQTAAEKIVAAGGKVEVE | Binds to the 23S rRNA. | B8G1Y5 |
C4KH54 | TRPD_SULIK | Anthranilate phosphoribosyltransferase | Sulfolobus | MNINDILKKLINKSDLEIDEAEELAKAIIRGEVPEILVSAILVALRMKGESKNEIVGFARAMRELAIKIDVPNAIDTAGTGGDGLGTVNVSTASAILLSLINPVAKHGNRAVSGKSGSADVLEALGYNIIVPPERAKELVHKTNFVFLFAQYYHPAMKNVANVRKTLGIRTIFNILGPLTNPANAKYQLMGVFSKDHLDLLSKSAYELDFNKVILVHGEPGIDEVSPIGKTFMKIVSKRGIEEVKFDVTDFGISSIPIDKLIVNSAEDSAIKIVRAFLGKDEHVAEFIKINTAVALFALDKVSDFKEGYEYAKYLIENSV... | Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA). | C4KH54 |
C5D9C3 | SYP_GEOSW | Prolyl-tRNA synthetase | unclassified Geobacillus | MRQSQSFIPTLREVPADAEVKSHQLLLRAGFIRQSASGVYTFLPLGQRVLQKVEAIIREEMNRAGAIELLMPALQPAELWQQSGRWYSYGPELMRLKDRHERDFALGPTHEEIITALVRDEVKTYKRLPLTLYQIQVKFRDEKRPRFGLLRGREFIMKDAYSFHTSQESLDETYNKMYEAYSNIFRRCGLNFRAVIADSGAIGGKDTHEFMVLSEIGEDTIAYSDASDYAANIEMAPVITTYEKSDEPLRKLEKVHTPGQKTIEEVASYLQVTPEKCIKSLLFKVDDRYVLVLVRGDHEANDVKVKNLFDASVVELATPE... | Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two addit... | C5D9C3 |
B7HS01 | REX_BACC7 | Redox-sensing transcriptional repressor Rex | Bacillus cereus group | MEQQKIPQATAKRLPLYYRFIQNLSLSGKQRVSSAELSEAVKVDSATIRRDFSYFGALGKKGYGYNVNYLLSFFRETLDQDDITRVALIGVGNLGTAFLHYNFTKNNNTKIEMAFDVSEEKVGTEIGGIPVYHLDELEERLSNDIQVAILTVPATVAQSVADRLAETNVHGILNFTPARLNVSENIRIHHIDLAVELQTLVYFLKNYPQ | Modulates transcription in response to changes in cellular NADH/NAD(+) redox state. | B7HS01 |
Q0BSM2 | LOLD_GRABC | Lipoprotein-releasing system ATP-binding protein LolD | Granulibacter | MSDYPSCALRLEQVARRYRSGDQELVVLDHADLELRPGEIVALVAPSGTGKSTLLHLAGLLEKPDEGRVWIGSHDAGGLSDTARTALRRDHLGFVYQFHHLLGEFSALENVVLPQMIAGRTRRQAEQHALTLLSAFGLQHRASHLPGMLSGGEQQRVAIARALANGPAVLLADEPTGNLDIHTAETVFSALLSAVRNQNVAALIATHNPDLAGRMDRQVTIREGQIVPA | Part of the ABC transporter complex LolCDE involved in the translocation of mature outer membrane-directed lipoproteins, from the inner membrane to the periplasmic chaperone, LolA. Responsible for the formation of the LolA-lipoprotein complex in an ATP-dependent manner. | Q0BSM2 |
Q9MLJ6 | CYB_DENPO | Ubiquinol-cytochrome-c reductase complex cytochrome b subunit | Dendroaspis | MSNQHILLTSNLLPVGSNISTWWNFGSMLLTCLILQITTGFFLAIHYTANINLAFSSVIHITRDVPHGWIMQNLHAIGASMFFICIYIHIARGLYYGLYLNKEVWLSGTALLILLMATAFFGYVLPWGQMSFWAATVITNLLTAIPYLGSALTTWLWGGFSINDPTLTRFFALHFILPFTIISMSSIHIILLHNEGSNNPLGTNPDIDKIPFHPYHSYKDMLMITIMITFMLLILSFSPDLMNDPENYSKANPLITPQHIKPEWYFLFAYGILRSIPNKLGGTLALFMSIAILMTAPFTHTSYTRSMSFRPLTQTMFWIL... | Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is... | Q9MLJ6 |
A8FMU8 | DCUP_CAMJ8 | Uroporphyrinogen decarboxylase | Campylobacter | MIFIDACFKKPTPYTPIWMMRQAGRYLPEYMEVRKQAGDFLSLCKDYKKASEVSLQPIDILDVDAAIIFSDILVVPLEMGMNLRFEKGEGPVFDNPISTLEDLEKLDDQNAHKKLNYVYDALKLTREKLSQNKALIGFCGSPWTIATYMIEGSGSKNYAKCKKMLYQNPELLHKILNKLTQVLKLYLEEQIKAGANAIQIFDSWASALEYDKFFEFSFNYMLEISNFIKSKYPNIPVILFPKGISGYLDRIDGNFDVFGVDWSTPLDLARDKLSHKYTLQGNMEPCRLYDKNAIKEGVEKILKTMQNKAHIFNLGHGILP... | Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III. | A8FMU8 |
B9WLD6 | ATP25_CANDC | ATPase synthesis protein 25, mitochondrial | Candida | MIVRGRCLSRSISKLVSLSSRPVGIISAKSFVTTTNLLQNSKNDSTEASIPWYMREENSSPVEVLNDVEVPELPDNSPQSLQEFVNLLTSEYGLTDLEIFDLSQLPEDHPKSLEEQNDENYVILATGKSEKHIYKAAYELRLYIKHTYEHLPIIEGMSSNSISKVTRRRLAKRVRRGPPATASTFGIGANTWVSCGTGIDGIVIHLLSRERRKSLNLEQLYSDEHENEESYSSPDIDQDRLFFGDRRGFHTSCRKLNSNVLSKIYDSYVLNGNFDTSQKFKAQFDLSFKGSSIEEYNKKFDLYRAINLVNANVVNVNEIE... | Probable mitochondrial mRNA stabilization factor. | B9WLD6 |
Q9SPU3 | BEATL_CLABR | Acetyl-CoA-benzylalcohol acetyltransferase | Clarkia | MNVTMHSKKLLKPSIPTPNHLQKLNLSLLDQIQIPFYVGLIFHYETLSDNSDITLSKLESSLSETLTLYYHVAGRYNGTDCVIECNDQGIGYVETAFDVELHQFLLGEESNNLDLLVGLSGFLSETETPPLAAIQLNMFKCGGLVIGAQFNHIIGDMFTMSTFMNSWAKACRVGIKEVAHPTFGLAPLMPSAKVLNIPPPPSFEGVKFVSKRFVFHENALTRLRKEATEEDGDGDDDQKKKRPSRVDLVTAFLSKSLIEMDCAPKELTKSRPSLMVHMMNLRKRTKLALENDVSGNFFIVVNAESKITVAPKITDLTESL... | Involved in the biosynthesis of benzyl acetate, a major constituent of the floral scent. Can use benzylalcohol, cinnamylalcohol, 3-cis-hexene-1-ol or heptanol as substrates. Has some activity with 2-phenylethanol and 2-naphtalene-ethanol. | Q9SPU3 |
A7EFH4 | MPH1_SCLS1 | FANCM-like protein 1 | Sclerotinia | MSDDEYGDIDAAVWDEAEALTQASQTLPSNFPHRRKRRRIGSEELDDGFLSGRRRGSHGFSRSDNDEADEKKSKYRIHLGAEEVPAAVIMGATQADEMPDSSPYRIRGPIYKRPRRSPPMELEQKSSPAQPSMVESAKTQKQNIVHSPQPTAQYDFSRELEDLPSDAFSPSPPQLRMSSIPITISSSPPLESTQSVRSQRLAAPQNGLRQTTLFGGRAPNQVPSSTQAKKVHKYLVDKVPEPPTHHTLDEEAIKTWIYPNNLGAERRYQYTIVHKGLFNNLLVALPTGLGKTFIAATIMLNFFRWTTDSQIVFMAPTKPL... | ATP-dependent DNA helicase involved in DNA damage repair by homologous recombination and in genome maintenance. Capable of unwinding D-loops. Plays a role in limiting crossover recombinants during mitotic DNA double-strand break (DSB) repair. Component of a FANCM-MHF complex which promotes gene conversion at blocked re... | A7EFH4 |
Q2UU72 | TRMB_ASPOR | tRNA(m7G46)-methyltransferase | Aspergillus subgen. Circumdati | MSTPPAKRQKRDQYRKRAAAAANEDTGKVKLPQKKFYRQRAHANPFSDHQLDYPLSPAHMDWSSHYPAFVNPDPEQKNLAGARKLLKDVEVVDIGCGFGGLLVGLAPLLPETLMLGMEIRTQVIEYVENRIQALRTQQNQLKNSSTTASESPAPAIPAEPATDGASPDAASTPETSNSPVPGGYQNISALRSNTMKFFPNFFGKQQLSKIFICFPDPHFKAKKHKARIISENLNAEYAYALKPGGLLYTITDVEEYHHWVLRHFREEGEHEASEGGVKDLFERVSEEELASDPCVEVMRESTEEGKKVTRNKGNKYVAVF... | Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. | Q2UU72 |
A5VJF8 | PRMA_LIMRD | Ribosomal protein L11 methyltransferase | Limosilactobacillus | MDWTAIKVITSSEAVEAVSYILTDMGAQGVQIEDAADFANLHEGKYGDHGEFIDPSSIPHRKNGAAVSGYFPQNVFVPELLPTIHQRVAKLREYGLNPGENDVSAATVDNQQWATVWQKYYHPLRVTDQLTIVPQWEEYQPADPKEKLIFLDPGMAFGTGTHPTTRLMLEALEKTIVGNEYVIDVGTGSGVLSIAAKHLGAGKVDAYDIDEVAVNSAKKNLALNPVAKDVKVGINSLLDGIHTKADLIVANILAEIIVPLIPQAYENLKPGGKFLVSGIIDDKAPLIRQKLQEQGFIIDDEQQMKDWHGMIAHKPTEVK | Methylates ribosomal protein L11. | A5VJF8 |
Q2YTA2 | COAE_STAAB | Dephosphocoenzyme A kinase | Staphylococcus | MPKVIGLTGGIASGKSTVSELLSVFGFKVVDADKAAREAVKKGSKGLAQVREVFGDEAIDENGEMNRRYMGDLVFNHPEKRLELNAIIHPIVRDIMEEEKQEYLKQGYNVIMDIPLLFENELENTVDEVWVIYTSESIQMDRLMQRNNLSLEDAKARVYSQISIDKKSRMADHVIDNLGDKLELKQNLERLLKEEGYIEKPNYGEED | Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A. | Q2YTA2 |
Q2P295 | MUTL_XANOM | DNA mismatch repair protein MutL | Xanthomonas | MAIRQLPEMLINQIAAGEVVERPASVVKELVENALDAGATRVDIELEEGGVRLIRIRDNGGGIAPDELPLAVSRHATSKIASLDDLETVATLGFRGEALPSIASVSRFTLTSRRHDAEHGSALEIDGGRLGEVVPRAHAPGTTVEVRELFFNVPARRKFLRAERTELGHIEEWLRSLALARPDVELRVSHNGKPSRRYKPGDLYSDARLGETLGEDFARQALRVDHSGAGLRLHGWVAQPHYSRASTDQQYLYVNGRSVRDRSVAHAVKMAYGDVLFHGRQPAYVLFLELDPARVDVNVHPAKHEVRFREARLIHDFVYR... | This protein is involved in the repair of mismatches in DNA. It is required for dam-dependent methyl-directed DNA mismatch repair. May act as a 'molecular matchmaker', a protein that promotes the formation of a stable complex between two or more DNA-binding proteins in an ATP-dependent manner without itself being part ... | Q2P295 |
Q9BH84 | O162_CONAE | Conotoxin ArMKLT1-0131 | Conus | MKLTCMMIVAVLFLTAWTSVTAVNTRGELENLFLRASHEMNSEASKLDKKVCVDGGTFCGFPKIGGPCCSGWCIFVCL | Omega-conotoxins act at presynaptic membranes, they bind and block voltage-gated calcium channels (Cav). | Q9BH84 |
B2IVW8 | UREE_NOSP7 | Urease accessory protein UreE | Nostoc | MLTFTQLKPPNGDATVTFTLALTAEERTRSRHRFETEDGKVVFLHLPRGTVLHDGDILLEETHNSLIRIIAKPELVVTAFAQTPLLLLRAAYHLGNRHVPVEITPTYLRFSSDSVLRAMLEQLGLEVKEEILPFQPELGAYGQHHHAH | Involved in urease metallocenter assembly. Binds nickel. Probably functions as a nickel donor during metallocenter assembly. | B2IVW8 |
Q9SH27 | LOR4_ARATH | Protein LURP-one-related 4 | Arabidopsis | MARVFPQAAISSPYMSTERETFTVWMKSLVYQTNGLTVYNSNGEITYRVENYDKCSNEVHIMDLHGNILFTIRKKKLWLFGSWYVYRECGSFTSTEEVKPCARIKRSSIRDGDWEVRDETNEVFWILRFDPKFAFQIIDIHGNIIAQVKPKQSSNGITLGEDVLTLEVKPRVDHSLVVTLVTVYGLIKGIDGEVKQLRDFEEEEVAVGDEIAIEI | Might be related to the phospholipid scramblase and tubby-like superfamily of membrane tethered transcription factors. | Q9SH27 |
Q971D0 | SYE_SULTO | Glutamyl-tRNA synthetase | Sulfurisphaera | MEEIEELIYKYALQNAYKHGGKAQDKAVVSKIFVERPDLRSRAKEISEIAKKIVEKVNSMSIQDQERELKEKYPDLLEEKKKEEPEKKTLPPIKVEGKFVTRFAPNPDGPIHLGNARAAIISYKYAEMYKGEFILRFDDTDPKVKKPIKEAYDWIRKDLKWLGIKWDKEVKASERLEFYYSMAKELISKGFAYVDTCSEEEFKKMRDASKPCPNRLKSAEDNLYLFEKMLNGEFKEGEAVVRIKTDLSLPDPSQRDWVLLRIIDVKKNPHPITGDKYWIWPTYNFASALDDHDLGITHIFRGKEHEVNAEKQKWIYNYMG... | Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu). | Q971D0 |
B9KE09 | AROC_CAMLR | 5-enolpyruvylshikimate-3-phosphate phospholyase | Campylobacter | MNSFGIRFKFTSFGESHGQAIGCVIDGMPAGVKFDFDFLQEMLDKRKPGQNKFSTPRKEEDKAQVLSGVFEGYTTGTPISVLVYNENTRSKDYEKDVFRPAHADFTYYHKYGIRDYRGGGRASARESIARVAAGALAQMLLKEFDIEIMSGVFGVGSIDSKLSNDEFDFNCAKNSEVYALDKNLEQSFKDEILKAKKAKDSIGARVFTRVKNPIKGLGEPLYDKLDSKLAHAIMGVNAVKAIEIGSGIQSSYMYGSQNNDELKDGVFLSNHSGGILGGISNGGFIDIKTYFKPTPSIFLPQQTQNIQGENIIRELKGRHD... | Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a s... | B9KE09 |
B1HM55 | ATPG_LYSSC | F-ATPase gamma subunit | Lysinibacillus | MVNLREIKGRINSTKSTKQITKAMQMVSSSKLRRAEQNAKAYVPYMEKIQDVVGAIASGTKDSGHPMLTARPVKKTAYLVIGSDRGLAGAYNSSILRQVQRTIDERHKSKDEYVILAIGRVVRDYFVKRDHNVISDVVGLPDQPTFADIKEIARNAVGMFIDGTYDQLYMYYNHFVSAIANEVTEKKLLPLTDLAPPSSNASYEFEPSGEAILEVLLPQYAESLVYGALLDGKASEHASRMTAMKNATDNASDLISDLSLQYNRARQAAITQEITEIVGGAAALE | Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex. | B1HM55 |
A8FK86 | PANC_CAMJ8 | Pantoate-activating enzyme | Campylobacter | MQVITSVKEAKQIVKDWKSHQLSIGYVPTMGFLHDGHLSLVKHAKTQDKVIVSIFVNPMQFGPNEDFSSYPRDLERDIKMCQDNGVDMVFIPDATQMYLKNFSTYVDMNTITDKLCGAKRPGHFRGVCTVLTKFFNILNPDIVYMGQKDAQQCVVVRHMVDDLNFDLKIQICPIIREEDGLAKSSRNVYLSKEERKASLAISQSIFLAEKLVREGEKNTSKIIQAMKDILEKEKLIKIDYIELVDFNTMENIENITDNVLGAVAAFVGKTRLIDNFLVQGLK | Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. | A8FK86 |
Q31U03 | THIC_SHIBS | Thiamine biosynthesis protein ThiC | Shigella | MSATKLTRREQRARAQHFIDTLEGTAFPNSKRIYLTGTHSGVRVPMREIQLSPTLIGGSKEQPQFEENEAIPVYDTSGPYGDPQIAINVQQGLAKLRQPWIDARGDTEELTVRSSDYTKARLADDGLDELRFSGVLTPKRAKAGRRVTQLHYARQGIITPEMEFIAIRENMGRERIRSEVLRHQHPGMSFGARLPENITAEFVRDEVAAGRAIIPANINHPESEPMIIGRNFLVKVNANIGNSAVTSSIEEEVEKLVWSTRWGADTVMDLSTGRYIHETREWILRNSPVPIGTVPIYQALEKVNGIAEDLTWEAFRDTLL... | 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. | Q31U03 |
Q9BJV9 | TOT2A_HADIN | Omega-atracotoxin-Hi2a | Hadronyche | MKFSKLSLTLALILTQALLVVCGKINEDFMENGLESHALHDEIRKPIDTEKADAERGVLDCVVNTLGCSSDKDCCGMTPSCTLGICAPSVGGIVGGLLGRAL | Potent inhibitor of insect, but not mammalian, voltage-gated calcium channels (Cav). | Q9BJV9 |
Q1GTW9 | ISPE_SPHAL | 4-(cytidine-5'-diphospho)-2-C-methyl-D-erythritol kinase | Sphingopyxis | MSATMRETGWAKINLALHVRARRADGYHDIETLFAFVDGGDTIEAALAATDTLVIDGEFAEGLSSGADNLVLRVLALLRARYGADRVPPLAVRLTKRLPLAAGIGGGSADAAAMARLVRTHFLPELGDATLARIVGPLGADIAACVASTTCMGSGTGEDLHAVAGLRIAGVPVLLVNPRQPVATGPVFAAWDGIDRGPLYIGTDYRAQLIGARNDLQRPALAACPAISDILLELGALRPWLARMSGSGATCFALFDAAADRDAAKAVLAARHPGWWLMAGALR | Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol. | Q1GTW9 |
Q8F148 | SYP_LEPIN | Prolyl-tRNA synthetase | Leptospira | MKASKYILPTEKENPADAVVASHRLMIRAGLVRKSSAGLYFYLPLGLKVLKKIEQIVREEMNSTGALEFDLPILTPSDFWEQSGRWSAMGKEMFRIQDRHDLSYALGPTHEESFSFLLKPLLKSYKDLPVNVYQIQTKFRDEIRPRFGVIRSREFIMKDAYSFHIDDSSLDDTYQAMRVAYRKIFDRCGLKTIPVQADSGSMGGSASEEFMVVSPIGEETLLLCNSCGYSSNSEKTPLILKKENSSAKFSEKKEISTPGKKTISEVSTLLGVSESETIKAVALKSEKKKILVFLRGDLELNLHKLHSLLKIADSEPMTDL... | Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two addit... | Q8F148 |
Q9I4W3 | DAPA_PSEAE | 4-hydroxy-tetrahydrodipicolinate synthase | Pseudomonas | MIAGSMVALVTPFDAQGRLDWDSLAKLVDFHLQEGTNAIVAVGTTGESATLDVEEHIQVIRRVVDQVKGRIPVIAGTGANSTREAVALTEAAKSGGADACLLVTPYYNKPTQEGMYQHFRHIAEAVAIPQILYNVPGRTSCDMLPETVERLSKVPNIIGIKEATGDLQRAKEVIERVGKDFLVYSGDDATAVELMLLGGKGNISVTANVAPRAMSDLCAAAMRGDAAAARAINDRLMPLHKALFIESNPIPVKWALHEMGLIPEGIRLPLTWLSPRCHEPLRQAMRQTGVLA | Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA). | Q9I4W3 |
Q87TB0 | RPOZ_VIBPA | Transcriptase subunit omega | Vibrio | MARVTVQDAVEKVGNRFDLVLIAARRARQMQTGGKDALVPEENDKPTVIALREIEEGLITKEVLDARERQEQQEQEAAELAAVSSIAHNR | Promotes RNA polymerase assembly. Latches the N- and C-terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits. | Q87TB0 |
B2JKI4 | ACEK_PARP8 | Isocitrate dehydrogenase kinase/phosphatase | Paraburkholderia | MNHFPKLLSSQIGFDVAETLLAGFDRHYCIFREAAIRAKNLFEAADWHGLQKLARERITSYDERVRECIAKLEDEYDAENIDDDVWQQIKLHYIGLLTTHRQPECAETFFNSVCCHILHRSYFNNDFIFVRPAISTEYIENDEPAAKPTYRAYYPGKDGLAVTLERIVTNFQLNPPFENLTRDVQCVIQALRDNFGTFNEAPNFQIHVLSSLFFRNKAAYIIGRIINGDMMLPFALPVHHVKPGLLALDALLCKRDQLLIIFSFAHSYFLVDMEVPSAYVEFLGSILHGKPKAEIYTSVGLQKQGKNLFYRDLLRHLKHS... | Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully activ... | B2JKI4 |
Q1R0G5 | RL14_CHRSD | 50S ribosomal protein L14 | Chromohalobacter | MIQTQTMLDVADNSGARRVQCIKVLGGSHRRYARVGDVIKVTVKEAIPRGKVKKGQVLKAVVVRTKSGVRRTDGSLIRFDGNAAVLLHNANEQPIGTRIFGPVTRELRNEKFMKIISLAPEVL | Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome. | Q1R0G5 |
O18719 | PGM_ENTDI | Glucose phosphomutase | Entamoeba | MQATVKRYPTTPISGQTMGTSGLRKRASEVENTPNYLENFVNAMFNAASNLQKPGKIIIGGDGRYLNLKALDIIIRVALSRGFTDIVVGKSGFMSTPAESATIIRRKAEAGFIMTASHNPAGKDHGDFGLKLNMSNGGPAPLEVTSKIEESARNIKEIVIAELNKPLTIDTIGDIEIECEGKKAIVHVIDPLEDYIAYLHECFDFEKLKQFVSKYHLKVQVDGFNAVTGIYNKKVFCELLGLPESSLKNAIPMPDFGGKHPDPNLTYAAELVHAVIPEDSPYDIGFAFDGDGDRNLIVGRGAFVSPSDSLAILSTKYNDI... | This enzyme participates in both the breakdown and synthesis of glucose. | O18719 |
P26996 | DNLJ_THET8 | Tth DNA ligase | Thermus | MTLEEARKRVNELRDLIRYHNYRYYVLADPEISDAEYDRLLRELKELEERFPELKSPDSPTLQVGARPLEATFRPVRHPTRMYSLDNAFNLDELKAFEERIERALGRKGPFAYTVEHKVDGLSVNLYYEEGVLVYGATRGDGEVGEEVTQNLLTIPTIPRRLKGVPERLEVRGEVYMPIEAFLRLNEELEERGERIFKNPRNAAAGSLRQKDPRITAKRGLRATFYALGLGLEEVEREGVATQFALLHWLKEKGFPVEHGYARAVGAEGVEAVYQDWLKKRRALPFEADGVVVKLDELALWRELGYTARAPRFAIAYKFP... | DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA. | P26996 |
Q2ILD4 | HSLV_ANADE | ATP-dependent protease subunit HslV | Anaeromyxobacter | MRPMHGTTVLCVRREGRVVIAGDGQVTLDKTVMKATARKVRRLGEGQVVAGFAGATADAFQLFELFEKKLKEHARSLPRAAVELAKQWRTDRMLRRLEALLVVADREHVLVLSGAGDVIEPDPVANGAAVAIGSGGPYALAAARALLAHSSLDARRVAEEAMKLAAEICIYTNGNLTIEEL | Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | Q2ILD4 |
Q9NQZ8 | ZNF71_HUMAN | Zinc finger protein 71 | Homo | MKELDPKNDISEDKLSVVGEATGGPTRNGARGPGSEGVWEPGSWPERPRGDAGAEWEPLGIPQGNKLLGGSVPACHELKAFANQGCVLVPPRLDDPTEKGACPPVRRGKNFSSTSDLSKPPMPCEEKKTYDCSECGKAFSRSSSLIKHQRIHTGEKPFECDTCGKHFIERSSLTIHQRVHTGEKPYACGDCGKAFSQRMNLTVHQRTHTGEKPYVCDVCGKAFRKTSSLTQHERIHTGEKPYACGDCGKAFSQNMHLIVHQRTHTGEKPYVCPECGRAFSQNMHLTEHQRTHTGEKPYACKECGKAFNKSSSLTLHQRNH... | May be involved in transcriptional regulation. | Q9NQZ8 |
Q732P8 | DXR_BACC1 | 2-C-methyl-D-erythritol 4-phosphate synthase | Bacillus cereus group | MKNISLLGASGSIGTQTLDVLRSHPDQFRLVAFSVGKNIDYAVKVIQEFSPQIVSVQREEDVLKLQAVSGNTKIVYGSEGLLEVALHPDAEIVVNAVVGSVGLLPTLRAIEAKKTIGIANKETLVTAGHLVMEAARKHNVSLLPVDSEHSAIFQCLNGENEKRISRLIITASGGSFRDKTRDELHHVTVEDALRHPNWSMGSKITIDSATMMNKGLEVIEAHWLFGIPYEQIDVVLHKESIIHSMVEFEDRSVMAQLGSPDMRVPIQYALTYPDRLPLSDTKQLNLWEMGTLHFEKMNQERFRCLRFAYEAGKTGGSMPA... | Catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP). | Q732P8 |
A4QBQ7 | RPOA_CORGB | Transcriptase subunit alpha | Corynebacterium | MLISQRPTITEEFVDNARSRFVIEPLEPGFGYTLGNSLRRTLLSSIPGAAVTSVKIDGVLHEFTTISGVKEDVSDIILNIKGLVLSSDSDEPVVMQLVKEGPGVVTAGDIQPPAGVEIHNPDLHIATLNETAKIEIELIVERGRGYVPATVTATGGEIGRIPVDQIYSPVLKVSYKVEATRVEQRTDFDKLVIDVETKNSITARDALASAGKTLVELFGLARELNIAAEGIEIGPSPQETEYIAAYSMPIEDLDFSVRSYNCLKREDIHTVGELAERAESDLLDIRNFGQKSINEVKIKLAGLGLTLKDAPEDFDPSTLE... | DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | A4QBQ7 |
Q8RHX3 | KDD_FUSNN | 3,5-diaminohexanoate dehydrogenase | Fusobacterium | MKKGCKYGTHRVIEPAGVLPQPAKKISNDMEIFSNEILIDVIALNIDSASFTQIEEEAGHDVEKVKAKIKEIVAERGKMQNPVTGSGGMLIGTVEKIGDDLVGKTDLKVGDKIATLVSLSLTPLRIDEIINIKPEIDRVEIKGKAILFESGIYAVLPKDMPENLALAALDVAGAPAQVAKLVKPCQSVAILGSAGKSGMLCAYEAVKRVGPTGKVIGVVRNDKEKALLQRVSDKVKIVIADATKPMDVLHAVLEANDAKEVDVAINCVNVPNTEMSTILPVKEFGIAYFFSMATGFSKAALGAEGVGKDITMIVGNGYTV... | Involved in the anaerobic fermentation of lysine. Catalyzes the oxidative deamination of L-erythro-3,5-diaminohexanoate (3,5-DAH) to 3-keto-5-aminohexanoate (KAH). It can use NAD or NADP. | Q8RHX3 |
P9WP47 | CSTA_MYCTU | Carbon starvation protein A homolog | Mycobacterium tuberculosis complex | MAAPTPSNRIEERSGHASCVRADADLPPVAILGRSPITLRHKIFFVAVAVIGALAWTVVAFFRNEPVNAVWIVVAAGCTYIIGFRFYARLIEMKVVRPRDDHATPAEILDDGTDYVPTDRRVVFGHHFAAIAGAGPLVGPVLATQMGYLPSSIWIVVGAVLAGCVQDYLVLWISVRRRGRSLGQMVRDELGATAGVAALVGIPVIITIVIAVLALVVVRALAKSPWGVFSIAMTIPIAIFMGCYLRFLRPGRVSEVSLIGIGLLLLAVVSGDWVAHTSWGAAWFSLSPVTLCWLLISYGFAASVLPVWLLLAPRDYLSTF... | Involved in peptide utilization. | P9WP47 |
Q9S1G9 | SERB_THASE | Selenate reductase iron-sulfur subunit | Thauera | MSQRQLAYVFDLNKCIGCHTCTMACKQLWTNRDGREYMYWNNVESRPGKGYPKNWEQKGGGFDKDGKLKTNGIIPIRADYGGTWNYNLLETLVEGKSNQVVPDEKPTWGPNWDEDEGKGEFPNNHYFYLPRICNHCSNPACLAACPTKAIYKREEDGLVVVDQSRCKGYRYCVKACPYGKMYFNLQKGTSEKCIGCYPRVEKGEAPACVKQCSGRIRFWGYRDDKDGPIYKLVDQWKVALPLHAEYGTEPNVFYVPPMNTTPPPFEEDGRLGDKPRIPIEDLEALFGPGVKQALATLGGEMAKRRKAQASELTDILIGYT... | Electron transfer subunit of the terminal reductase during anaerobic growth on selenate and nitrate. | Q9S1G9 |
Q9BHA0 | O26M_CONTE | Conotoxin TxMEKL-0512 | Cylinder | MEKLTILLLVAAVLLSIQALNQEKHQRAKINLLSKRKPPAERWWRWGGCMAWFGLCSKDSECCSNSCDVTRCELMPFPPDW | Gamma-conotoxins may act on voltage-gated non-specific cation pacemaker channels (HCN). | Q9BHA0 |
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