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 |
|---|---|---|---|---|---|---|
Q51702 | NIRC_PARDP | Cytochrome c55X | Paracoccus | MARLALLLVLLAGTAVAGPPDAARQDELRHLVRQDCGSCHGLRMTGGLGRPITAAALAGRDVEDLSDVILDGMPGTAMPGWRPLLTEDDARWIADYLLKTETE | Monoheme c-type cytochrome. | Q51702 |
Q32LQ6 | MFSD1_DANRE | Major facilitator superfamily domain-containing protein 1 | Danio | MADREEHQGLLDGDRDEDEGDKAPSVHLNPICDPNHLLHRILVLIFMCFLGFGSYFCYDNPAALQSQVIQDMNLNTASFMQLYAWYSWPNVVLCFLGGFLLDRVFGIRLGTVIFSLFVLVGQIIFAAGALANHFWLMNVGRFVFGIGGESLAVAQNTYAVNWFKGKELNLVFGLQLSMARLGSTVNMNVIGWVYGRIQMSMGSAGPTTLGITLMIAASTCLFSLICALVLGFLDKRAERILNKEQGKTGEVIKLTDVKDFSVSLWLIFIICVAYYVAIFPFIGLGQVFFIEKFGFTPVQARAINSVVYIISAPASPLLGF... | Lysosomal transporter which is essential for liver homeostasis. Required to maintain stability and lysosomal localization of GLMP. | Q32LQ6 |
Q9I8I2 | BOK_CHICK | Bcl-2-related ovarian killer protein | Gallus | MEVLRRSSVFAAEVMEVFDRSPTDKELVSQAKALCRDYINSRLIRAGVSWSKPEHNTPVPGGKLAEVSAILLRLGDELEYIRPNVYRNIARQLNISLHSETVVTDAFLAVAAQIFTAGITWGKVVSLYAVAAGLAVDCVRHAQPAMVHTIVDCLGEFVRKTLVTWLKRRGGWADITKCVVSTDPSLRSHWLVAAVCSFGHFLKAIFFVLLPER | May play a role in apoptosis. | Q9I8I2 |
P11610 | CD1D2_MOUSE | Antigen-presenting glycoprotein CD1d2 | Mus | MRYLPCLLLWAFLQVWGQSEVQQKNYTFRCLQTSSFANISWSRTDSLILLGDLQTHRWSNDSATISFTKPWSQGKLSNQQWEKLQHMFQVYRVSFTRDIQELVKMMSPKEDYPIEIQLSTGCEMYPGNASESFFHVAFQGKYAVRFRGTSWQRVLGAPSWLDLPIKVLNADQGTSATVQTLLNDTWPQFARGLLEAGKSDLEKQEKPVAWLSSVPSSAHGHLQLVCHVSGFYPKPVWVMWMRGDQEQQGTHRGDFLPNADETWYLQATLDVEAGEEAGLACRVKHSSLGGQDIILYWDARQAPVGLIVFIVLIMLVVVGA... | Antigen-presenting protein that binds self and non-self glycolipids and presents them to T-cell receptors on natural killer T-cells. | P11610 |
Q507Y2 | MATK_RANTR | Intron maturase | Ranunculus | MEELQRYLKMDRSRERDFLYPLLFQEYIYALAHDFGLTKLIPYESMQILSYDKKYSSLIVKRLIIRMYQQKHLIILDNDSNQKKFLEHNKNLYSQMLSEGFAVIVEIPFALRLVSSYQGKKMEKSINLGSIHSTFPFLEDKFVHLNHVLNIIIPYPIHLELLVQNLRCWIQDASFLHLLRFFLYEYHNWNSLTTQKTNQNLFFFKENRRFFWFLFNFHVYESESIFLFLRKKSYHLRSTSSIAFLDRTHFYGKIEHFQVVFRNDFHTILWLFKDPFMHYFRYQGKSIMSSKGTPLLMKKWKNYLVNLWEYHFHFWSQPDR... | Usually encoded in the trnK tRNA gene intron. Probably assists in splicing its own and other chloroplast group II introns. | Q507Y2 |
Q3JCP7 | PAND_NITOC | Aspartate 1-decarboxylase alpha chain | Nitrosococcus | MYLTLLKSKLHRACVTHIELEYEGSCAIDSVLLSTAGIQEYEQIHIYNLTNGERFVTYAIRAEDNSGIISVNGAAAHKACPGDRLIICTYAVFERSEMDSFKPLLIYLDDRNFITHTGNAIPVQVA | Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine. | Q3JCP7 |
Q3A605 | ATPB1_SYNC1 | F-ATPase subunit beta 1 | Syntrophotalea | MSNGKITQVIGPVIDVEFEAGELPEIYYALKVSNPSLGDEPWNLVAEVAQHLGENTVRAIAMDSTDGLVRGQEVLNTGRQISVPVGRGTLGRILNVIGEPVDEQGPVETDTTWEIHRPTPEFVDQSTKVEAFETGIKVVDLLAPYARGGKIGLFGGAGVGKTVLIMELIHNIAKKHGGFSVFAGVGERTREGNDLWNEMKESNVLDKTALVYGQMNEPPGARARVALSALTVAEYFRDQENQDVLLFVDNIFRFTQAGSEVSALLGRIPSAVGYQPTLSTEMGELQERITTTKNGSITSVQAIYVPADDLTDPAPATTFA... | Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. | Q3A605 |
Q34289 | CYB_DASAL | Ubiquinol-cytochrome-c reductase complex cytochrome b subunit | Dasyurus | MINMRKTHPLLKIINHSFIDLPAPSNISAWWNFGSLLGVCLIIQILTGLFLAMHYTSDTLTAFSSVAHICRDVNHGWLLRNLHANGASMFFMCLFLHVGRGIYYGSYLYKETWNIGVILLLTVMATAFVGYVLPWGQMSFWGATVITNLLSAIPYIGTTLAEWIWGGFAVDKATLTRFFAFHFILPFIIMALAIVHLLFLHETGSNNPSGINPDSDKIPFHPYYTIKDALGFMLLLLMLLLLALFSPDLLGDPDNFSPANPLNTPPHIKPEWYFLFAYAILRSIPNKLGGVLALLASILILLIIPLLHTANQRSMMFRPI... | 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... | Q34289 |
Q8CJM9 | NPD2_STRCO | Regulatory protein SIR2 homolog 2 | Streptomyces albidoflavus group | MTGKPLVAILSGAGVSTDSGIPDYRGPNGLWRRDPEAEKLVTYEYYMGDPEIRRRSWLMRRDSAALHAEPNAAHRAVADLERRGVPVRVLTQNVDGLHQLAGVSARKVLELHGTARDCVCTGCGARGPMADVLARIEAGEDDPPCLDCGGVLKTATVMFGERLDPVVLGEAAAISKACQVFVAVGTSLQVEPAAGLARVAVEHGARLVVVNAEPTPYDELADEVIREPIGSALPALLRGLG | NAD-dependent protein deacetylase which modulates the activities of several enzymes which are inactive in their acetylated form. | Q8CJM9 |
Q3B281 | HIS3_CHLL3 | Phosphoribosyl-AMP cyclohydrolase | Pelodictyon | MANNEGIDNSFLDTVKFDAKGLVPAIVQDHETGKVLMMAWMNRESLEMTLERKKACYWSRSRNKLWLKGESSGNMQDVYDILIDCDGDTLILKVSQIGGACHVGYHSCFYRRVLENGNMEICDTLMFDPEEVYGKKS | Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP. | Q3B281 |
Q7VBS7 | ISPG_PROMA | 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate synthase | Prochlorococcus | MTIENTQNINIDTLSRRYSTQIQRRKTRSVMVGNIGIGSDYPVAVQSMINEDTLDIEASTSAIRRLHEIGCEIVRLTVPSLSHAKAVGEIKRRLEQNYLPVPLVADVHHNGMKIALEVAKHVDKVRINPGLFVFSNPDPSRTEFSNSEISAIKEKIINNFEPIVNTLKAQNKALRIGVNHGSLAERMLFQYGDTPLGMVESAMEFVRICDSLDFHNIVISMKASRPPVMLAAYRLMADAMDKEGFNYPLHLGVTEAGDGDYGRIKSTVGIGTLLTEGLGDTIRVSLTEAPEKEIPVAYSILQTVGLRKTMVEYISCPSCG... | Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate. | Q7VBS7 |
Q0TMP3 | EFG_CLOP1 | Elongation factor G | Clostridium | MARQYPLEKFRNFGIMAHIDAGKTTTTERILFYTGRNHKIGETHDGASTMDWMAQEQERGITITSAATTCFWKGYELNIIDTPGHVDFTVEVERSLRVLDGAVTVLDAKSGVEPQTETVWRQADKYGVPRMIYVNKMDATGADYYNCINTVRERLQANAVAIQIPIGQEDQFQGMVDLLTNQAIIFKDDLGKDIEVSDVPADLADKAEEYRAAMIEAIAETDEELMMKYLEGEELTLEELKVALRKATINNEIIPVICGSSYKNKGVQQMIDGVVDYLPSPLDIPAVKGTNLDGEEEVREASDDAPMSALAFKIATDPFV... | Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respective... | Q0TMP3 |
Q50925 | HAO_NITEU | Hydroxylamine oxidoreductase | Nitrosomonas | MRIGEWMRGLLLCAGLMMCGVVHADISTVPDETYDALKLDRGKATPKETYEALVKRYKDPAHGAGKGTMGDYWEPIAISIYMDPNTFYKPPVSPKEVAERKDCVECHSDETPVWVRAWKRSTHANLDKIRNLKSDDPLYYKKGKLEEVENNLRSMGKLGEKETLKEVGCIDCHVDVNKKDKADHTKDIRMPTADTCGTCHLREFAERESERDTMVWPNGQWPAGRPSHALDYTANIETTVWAAMPQREVAEGCTMCHTNQNKCDNCHTRHEFSAAESRKPEACATCHSGVDHNNWEAYTMSKHGKLAEMNRDKWNWEVRL... | Catalyzes the oxidation of hydroxylamine to nitrite. The electrons released in the reaction are partitioned to ammonium monooxygenase and to the respiratory chain. The immediate acceptor of electrons from HAO is cytochrome c-554. | Q50925 |
A6U882 | RS11_SINMW | 30S ribosomal protein S11 | Sinorhizobium | MAKEATRVRRRERKNITSGVAHVNSSFNNTMITITDAQGNAIAWSSAGAKGFKGSRKSTPFAAQIAAEDCAKKAQEHGMKSLEVEVCGPGSGRESALRALQAAGFMITSIRDVTPIPHNGCRPRKKRRV | Located on the platform of the 30S subunit, it bridges several disparate RNA helices of the 16S rRNA. Forms part of the Shine-Dalgarno cleft in the 70S ribosome. | A6U882 |
Q60587 | ECHB_RAT | Beta-ketothiolase | Rattus | MTTILTSTFRNLSTTSKWALRFSVRPLSCSSQVQSAPAVQTKSKKTLAKPNLKNIVVVEGVRIPFLLSGTSYKDLMPHDLARAALSGLLYRTNIPKDVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPAHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPIRHSRNMRKMMLDLNKAKTLAQRLSLLTKFRLNFLSPELPAVAEFSTNETMGHSADRLAAAFAVSRMEQDKYALRSHSLAKKAQDEGHLSDIVPFKVPGKDTVSKDNGIRPSSLEQMAKLKPAFIKPYGTVTAANSSFLTDGASAML... | Mitochondrial trifunctional enzyme catalyzes the last three of the four reactions of the mitochondrial beta-oxidation pathway. The mitochondrial beta-oxidation pathway is the major energy-producing process in tissues and is performed through four consecutive reactions breaking down fatty acids into acetyl-CoA. Among th... | Q60587 |
Q9Z9K5 | RS17_HALH5 | 30S ribosomal protein S17 | Halalkalibacterium (ex Joshi et al. 2022) | MERNQRKVYTGRVVSDKMDKTITVLVETYKKDRLYGKRVKYSKKFKAHDENNSAKIGDIVRIQETRPLSKDKHFRLVEIVEEAVII | One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA. | Q9Z9K5 |
Q8YS61 | ISPE_NOSS1 | 4-(cytidine-5'-diphospho)-2-C-methyl-D-erythritol kinase | Nostoc | MRSYKLIAPAKINLYLEIIGDRPDGYHELVMILQSIDLADEIEIHSLSSETIHVHCNHPQVPTDKSNLVYRAAELMVTRFPEAFTKHGGVDITVHKHIPVAAGLAGGSTNAAAVLVGIDLLWNLGLTQTELEELGSTLGSDVPFCVAGGTVIATGRGEQLSPLPSLDHIYIVLGKYRSLEVSTAWAYKNYRQEYGSTYLRDTNDLASRAAAVHSGSIVKAIVEKDAVAIAQRLHNDLEKVVLPSYPQVLHLRELLASQPGVIGTMMSGSGPSVFALCETQAQAEQVQQQVRQTIPDEDLELFVTRTITHGIQVVGNG | Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol. | Q8YS61 |
B7MTZ5 | RF1_ECO81 | Peptide chain release factor 1 | Escherichia | MKPSIVAKLEALHERHEEVQALLGDAQTIADQERFRALSREYAQLSDVSRCFTDWQQVQEDIETAQMMLDDPEMREMAQDELREAKEKSEQLEQQLQVLLLPKDPDDERNAFLEVRAGTGGDEAALFAGDLFRMYSRYAEARRWRVEIMSASEGEHGGYKEIIAKISGDGVYGRLKFESGGHRVQRVPATESQGRIHTSACTVAVMPELPDAELPDINPADLRIDTFRSSGAGGQHVNTTDSAIRITHLPTGIVVECQDERSQHKNKAKALSVLGARIHAAEMAKRQQAEASTRRNLLGSGDRSDRNRTYNFPQGRVTDH... | Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA. | B7MTZ5 |
P0C6E3 | VM2B1_AGKBI | Disintegrin | Agkistrodon | QRYNPYKYIELFLVVDNRMVTKYNGDLDKIKTRIYELVNILNEIYRPLYIRVALVGIEFWCNKDLINVKSASSVTLASFANWRESVLPNRTSHDNAQLLTAIVFNRGVIGSAYPAGMCDPNRSVGTVQDHSEINLQVAITMAHEIGHNLGMGHDNNSCTCGGYSCIMLPALSDQPSKYFSNCSYIQYRDFIMNQDPQCILNEPSGTDIVSPPVCGNDILEVGEECDCGCPRNCQDPCCNAATCKKYSWVQCESGECCDQCRFKGAGTECRRAMGDDPGGRCTGQSADCPRN | This hemorrhagic toxin hydrolyzes the Aalpha-chain (FGA) and more slowly the Bbeta-chain (FGB) of fibrin and fibrinogen. Also hydrolyzes casein. It lacks platelet aggregation inhibitory activity. After intramuscular injection, it acts rapidly to disrupt the capillary endothelium without damaging the intercellular junct... | P0C6E3 |
Q3SL57 | PURA_THIDA | IMP--aspartate ligase | Thiobacillus | MAAKNVVVIGTQWGDEGKGKIVDWLTDRAQGVVRFQGGHNAGHTLVVGGKKTVLHLIPSGILRDNVTCYIGNGVVLAPDALLKEMDMLEAAGVDVASRLKISEACPLIMPHHVALDQAREIAKGAGKIGTTGRGIGPAYEDKVARRALRLQDLFHRERFAAKLGEVLDHHNFMLKNYYKVEVVSFNQTLDGMMAMAERLKPMVADVPRSLYEANKAGGNLLFEGAQGTLLDIDHGTYPFVTSSNCTAGGAATGSGVGPSAMHYVLGITKAYTTRVGSGPFPTELFDDVGQYLGEKGHEFGATTGRQRRCGWFDAAALKRS... | Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. | Q3SL57 |
A6KZR2 | COAD_PHOV8 | Pantetheine-phosphate adenylyltransferase | Phocaeicola | MRRAIFPGTFDPFTIGHYSVVKRALTFMDEVVIGIGINENKKTWFPTEKRVEMIEKLFADDPRVKVDAYDCLTIDFARAKEAQFIVRGIRTVHDFEYEETIADINRKLAGIETILLFTEPELTSISSTIVRELLQFGKDVTPFLPEGMKID | Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. | A6KZR2 |
Q87SA1 | LGT_VIBPA | Phosphatidylglycerol--prolipoprotein diacylglyceryl transferase | Vibrio | MSQGYLQFPNIDPVLVSIGPVSIRWYGLMYLVGFMFALWLANRRADKPGSGWTREQVSDLLFAGFLGVVIGGRVGYVIFYNFELFLDDPLYLFKVWTGGMSFHGGLLGVITAMFWYAHKNGRTFFGVADFVAPLVPFGLGMGRMGNFMNSELWGRVTDVPWAIVFPNGGPLPRHPSQLYEMLLEGVVLFFILNWFIKKPRPLGSVSGLFLAGYGTFRFLVEFVREPDAQLGLFGGYISMGQILSMPMIVLGILMMVWAYKRGLYQDKAQVKTK | Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins. | Q87SA1 |
A3PIZ9 | SURE_CERS1 | Nucleoside 5'-monophosphate phosphohydrolase | Cereibacter | MRILITNDDGINAPGLEVLEQIALQLAGPDGEVWTVAPAFEQSGVSHAISYTHPMMIAKLGPRRYAAEGSPADCVLAALYDVLQGARPDLVLSGVNRGNNSAENVLYSGTVGGALEAALQGLPAIALSQFLGPETEGLADPFECARTHGARIVRLLLERGLWDGEDYRLFYNVNFPPVPAANLRGHRVAAQGFRRDTSFGVEPHMSPSGRRFLWIRGGAQQSPTLPGTDAAVNLEGFVSITPLRADLTAHDRLAELEALIG | Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates. | A3PIZ9 |
Q7TTY9 | CH603_RHOBA | Chaperonin-60 3 | Rhodopirellula | MPKIIAFDQEAREAIRRGVSKLARTVKVTLGPKGRNVILQKSFGSPTVTKDGVTVAKEIELEDPYENMGASMVREVASKTSDVAGDGTTTATVMAEAIFNEGLKAVVAGVNPIQMKSGIETAVSDITEQLHSMAVKVKDQEAMANVATIASNNDREIGTLLADAMSKVGKDGVITVDEGKSLQTEQEWVEGMQFDRGYLSPYFVTDSTSMEVVLEDAYVLVFEKKISNIKDMVPLLEKVVQQGKPLLIIAEDVDGEALATLVINRLRGTFTVCAVKAPGYGDRRKAMMEDIAILTGGQAIFEALGVKLESVDLPQLGRAK... | Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. | Q7TTY9 |
Q9PDM3 | BIOH_XYLFA | Carboxylesterase BioH | Xylella | MYIEVTGYGPALVLIHGWAMHSGVFAPLVEQLRAHHTLYLVDLPGHGYNHTTLTPLALPHVVHAIAAATPPAVWLGWSLGGLFALHAAATLPQVRGLIMLAATPCFVRREDWPHAVEVSIFTQFAEDLKQNYTETINRFLALDTLGSTYAQSELRQLRQILNARHTPNTATLQAGLELLAHTDLRRAVIDLTPPSLWIAGQRDRLVPAASIHAATALAPSGQTELLTITGGGHAPFLSHANQMTAALQHFIATLP | The physiological role of BioH is to remove the methyl group introduced by BioC when the pimeloyl moiety is complete. It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway through the hydrolysis of the ester bonds of pimeloyl-ACP esters. | Q9PDM3 |
Q038M8 | TRUB_LACP3 | tRNA-uridine isomerase | Lacticaseibacillus | MNGILPLYKPTGMTSADAVYHARKILGIKKIGHSGTLDPNVDGVLPLAIGAGTKAVPQLMASGKVYTGEITLGFATTTEDLDGEVVDKTPLTQPFTADQLDAALTAWTGNITQIPPMFSAVKVNGRRLYEYARAGETVKRPERQATVSQFTRTDEPVFSATDGTQRFRFEVHVSKGTYIRTLAVDVGKTLGVAAVMSQLTRVKSGGFTLKQAVSIEQLKAHAAAGTLADVIQPIDIAFADLPQVDLTVEQFEAISHGRFLSLDQQTPRVRLHFAGVLKAIYRREDDQYRPDLMFLANEKNV | Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs. | Q038M8 |
P73912 | CCS1_SYNY3 | Cytochrome c biogenesis protein CcsB | unclassified Synechocystis | MTIANPSPSNFFQQLGRQCLKTLADLRLAIALLLLIAVFSISGTVIEQGESLSFYQQNYPEDPALFGFLSWQVILQLGLNQVYRTWWFLGLLILFGSSLTACTFNRQFPALKAARSWQFYHQPRQFKKLALSFSLPDGDINKIESLLRDRGYKIFQEGDSVYARKGLMGKVGPIIVHGAMLIILGGAIWGALTGFFAQHMIPSGETFQVSNIIEKGPLADSQIPKDWGIKVNRFWINYTENGAIDQFYSDLSVVNNQGEELDRQTISVNHPLRHRGVTFYQTNWGIAGVKVQLNNSPVLQLPMAPLQTANGGQLWGAYIP... | Probably not involved in heme transport or reduction as mutants deleted for the first 24 residues cannot be rescued by growth in the presence of heme or reductant. | P73912 |
Q6YXL0 | RK14_PHYPA | 50S ribosomal protein L14, chloroplastic | Physcomitrium | MIQPQTYLNVADNSGARKLMCIQILGASNRKYAHIGDIIIAVVKEAIPNMPLKKSEVVRAVVVRTCKELKRKNGTIIQFDDNAAVIINQEGNPKGTRVFGPVARELRESNFTKIVSLAPEVL | Binds to 23S rRNA. | Q6YXL0 |
Q08108 | PLB3_YEAST | Phospholipase B 3 | Saccharomyces | MIRPLCSKIIISYIFAISQFLLAANAWSPTDSYVPGTVSCPDDINLVREATSISQNESAWLEKRNKVTSVALKDFLTRATANFSDSSEVLSKLFNDGNSENLPKIAVAVSGGGYRSMLTGAGVLAAMDNRTEGAYEHGLGGLLQSTTYLSGASGGNWLVGTLALNNWTSVQDILNNMQNDDSIWDLSDSIVTPGGINIFKTAKRWDHISNAVESKQNADYNTSLADIWGRALAYNFFPSLNRGGIGLTWSSIRDFPVFQNAEMPFPISVADGRYPGTKVINLNATVFEFNPFEMGSWDPSLNSFANVKYLGTNVSNGVPL... | Sequentially removes both fatty acyl groups from diacylglycerophospholipids and therefore has both phospholipase A and lysophospholipase activities. Substrate preference is phosphatidylserine > phosphatidylinositol. Does not cleave phosphatidylcholine, phosphatidylethanolamine, phosphatidic acid and phosphatidylinosito... | Q08108 |
A7N121 | DEF_VIBC1 | Polypeptide deformylase | Vibrio | MSVLQVLTFPDDRLRTVAKPVEEVTPEIQKIVDDMIETMYDEEGIGLAATQVDIHKRIVVIDISETRDEPMVLINPEILEKRGEDGIEEGCLSVPGARALVPRAAEVTVKALDRDGKEYTFEADDLLAICVQHELDHLMGKLFVDYLSPLKRKRIQDKLAKIKRFNEKQQNA | Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | A7N121 |
Q87SA4 | RPPH_VIBPA | (Di)nucleoside polyphosphate hydrolase | Vibrio | MIDGDGYRLNVGIVICNNHGQVFWAKRYGQHSWQFPQGGIDEGETPEQAMFRELYEEVGLTKKDVKIIATSRHWLRYKLPKRLVRWDSKPVCIGQKQKWFLLRLECDESRINMQRGKSPEFDGWRWVSYWYPVRQVVSFKRDVYRRAMKEFASLAMPFRERKTKGKRKKQQRRG | Accelerates the degradation of transcripts by removing pyrophosphate from the 5'-end of triphosphorylated RNA, leading to a more labile monophosphorylated state that can stimulate subsequent ribonuclease cleavage. | Q87SA4 |
Q9SPG9 | MYB24_ARATH | Myb-related protein 24 | Arabidopsis | MEKRESSGGSGSGDAEVRKGPWTMEEDLILINYIANHGEGVWNSLAKSAGLKRTGKSCRLRWLNYLRPDVRRGNITPEEQLTIMELHAKWGNRWSKIAKHLPGRTDNEIKNFWRTKIQKYIIKSGETTTVGSQSSEFINHHATTSHVMNDTQETMDMYSPTTSYQHASNINQQLNYGNYVPESGSIMMPLSVDQSEQNYWSVDDLWPMNIYNGN | Transcription factor acting redundantly with MYB21 and MYB57 to control stamen filament elongation in the late developed flowers. Contributes with MYB21 to induction of MYB108 by jasmonate. Repressed at the transcript levels by DELLA proteins. | Q9SPG9 |
A0A482NAF7 | ICCC_TALVA | Ilicicolin H biosynthesis cluster protein C | Talaromyces | MITLQNLPWILLYTGFLAIFLSRLFSNGKQSRDEKANGCQPPARYPQWDPIMGLDLVYSQVSALKNNRYLEWLRDLHAKMPKTFSLNFFGQRWIYSIEPEILKAVYATNFRDFGVEPIRRHSKGSMPFADKGVNTTDGEDWEFSRLLIKPFFERNVYTDTDRIKVHADHFLSLIPADGETFDAQPLVQRWFLDLTTEFIFGESMGSLAHPERADIAWTMLDVLRGGRLRAQMHRFMWARDWTWWLKAVYKVHDYVNPYIRSTLKELAEREERIKQGLPVGPERTDLVWSMATHLRDEELLRSQLCLIIVPNNDTTSIFIS... | Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of ilicicolin H, a 4-hydroxy-2-pyridonealkaloid that has potent and broad antifungal activities by inhibiting the mitochondrial respiration chain . IccC catalyzes the ring expansion of the tetramate intermediate to the acyclic 2-pyri... | A0A482NAF7 |
Q5CZR5 | AEP1_DANRE | Jacalin-type lectin domain-containing protein 5 | Danio | MTYPTNLEIIGGQGGSSFSFTGENNGASLEKIWVWVGGWQIKAVRAWLSDGRDETFGVPSGSHQEYVFTPGECFTSLSLWGNGAGTRLGAIKFKTNKGGEFFAHMTSWGLKTEYPMDVGSGYCLGIVGRGGSDIDCMGFMFLNAVQSTVLTNVNYPTINQLIPKVATEEIKSVSFENKTSVKQEQKVETSKKVIKTSSWSMTKSFSSTFSVEVSAGIPEIAEVSTGFSISFGVESTHSLEQTDEKNETLTTTVEVPPKKKVDVHITIGRASFDLPYTGTVKITCKNGSVLQYETKGQYKGVAYTDIKVNTVEKDL | Pore-forming protein which might play a role in host defense. Exists as an antiparallel dimer in solution. Can also assemble into an octameric pore-like structure spanning the cell membrane. Oligomerization may be triggered by binding of the jacalin-type lectin domain to high-mannose cell-surface proteoglycans, and als... | Q5CZR5 |
Q96SN7 | ORAI2_HUMAN | Transmembrane protein 142B | Homo | MSAELNVPIDPSAPACPEPGHKGMDYRDWVRRSYLELVTSNHHSVQALSWRKLYLSRAKLKASSRTSALLSGFAMVAMVEVQLETQYQYPRPLLIAFSACTTVLVAVHLFALLISTCILPNVEAVSNIHNLNSISESPHERMHPYIELAWGFSTVLGILLFLAEVVLLCWIKFLPVDARRQPGPPPGPGSHTGWQAALVSTIIMVPVGLIFVVFTIHFYRSLVRHKTERHNREIEELHKLKVQLDGHERSLQVL | Ca(2+) release-activated Ca(2+)-like (CRAC-like) channel subunit which mediates Ca(2+) influx and increase in Ca(2+)-selective current by synergy with the Ca(2+) sensor, STIM1. | Q96SN7 |
Q9SAK2 | KSB_ARATH | Protein GA REQUIRING 2 | Arabidopsis | MSINLRSSGCSSPISATLERRLDSEVQTRANNVSFEQTKEKIRKMLEKVELSVSAYDTSWVAMVPSPSSQNAPLFPQCVKWLLDNQHEDGSWGLDNHDHQSLKKDVLSSTLASILALKKWGIGERQINKGLQFIELNSALVTDETIQKPTGFDIIFPGMIKYARDLNLTIPLGSEVVDDMIRKRDLDLKCDSEKFSKGREAYLAYVLEGTRNLKDWDLIVKYQRKNGSLFDSPATTAAAFTQFGNDGCLRYLCSLLQKFEAAVPSVYPFDQYARLSIIVTLESLGIDRDFKTEIKSILDETYRYWLRGDEEICLDLATCA... | Involved in the biosynthesis of ent-kaurene diterpenoids natural products and in the production of gibberellins phytohormones . Catalyzes the conversion of ent-copalyl diphosphate to the gibberellin precursor ent-kaur-16-ene . | Q9SAK2 |
C7C0H5 | NUOK_HELPB | NDH-1 subunit K | Helicobacter | MIGLNHYLIVSGLLFCIGLAGMLKRKNILLLFFSTEIMLNAINIGFVAISRYTHNLDGQMFALFIIAIAASEVAIGLGLVILWFKKYKSLDIDSLNAMKG | NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are t... | C7C0H5 |
Q6G0N1 | MIAB_BARQU | tRNA-i(6)A37 methylthiotransferase | Bartonella | MNKANPKNTPSVVPKKVFIKTYGCQMNVYDSQRMTDSLSSKGYVATQTPNDADLILLNTCHIREKAAEKLYSDLGRLRVMRQARTLDKPLMIGVTGCVAQAEGNEILRRAPMVDLVIGPQMYHRLPDLLEQTKQGKKIVETDYPVEDKFAHLPPHNKRAVRKRGVSAFLTVQEGCDKFCTFCVVPYTRGAEISRSVEQITEEARQLIEAGVKEITLLGQNVNGWHGQIANGKTWRLGDLLYHLAKLDGLKRLRYTTSHPRDMDDSLIAAHRDLDILMPYLHLPVQSGSDRILKAMNRQHKSIHYLHLIEKIRTARPDIAF... | Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine. | Q6G0N1 |
Q29AK9 | RUVB1_DROPS | Pontin | Sophophora | MKIEEVKSTVRTQRIAAHSHVKGLGLDEAGSALQSAAGLVGQKAAREAAGIVVDLIKSKKMAGRALLLAGPPGTGKTAIALAIAQELGNKVPFCPMVGSEVFSNEIKKTEVLMENFRRSIGLRIRETKEVYEGEVTELTPVETENPMGGYGKTISNVVIGLKTAKGTKQLKLDPSIFDALQKEKVEVGDVIYIEANSGAVKRQGRSDTFATEFDLETEEYVPLPKGDVHKKKEVIQDVTLHDLDVANARPQGGQDVLSMVGQLMKPKKTEITDKLRMEINKVVNKYIDQGIAELVPGVLFIDEIHMLDLETFTYLHKSLE... | Proposed core component of the chromatin remodeling Ino80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair. | Q29AK9 |
B1J266 | TPIS_PSEPW | Triose-phosphate isomerase | Pseudomonas | MRRPMVAGNWKMHGTRASVAELTQGLGNMLIPEGIEVAVFPPALFINEVIDGLKGKGITVGAQNSAVQPEQGALTGEVAPSQLAEVGCKFVLIGHSERRQVIGESEEVLNRKFAAAQKSGLTPVLCIGETLEEREAGKTLEVVGRQLSSVIDAFGIAAFANAVIAYEPVWAIGTGLTASPQQAQDVHAAIRKQLAAKDAEVAQNVQLLYGGSVKAANAAELFGMPDIDGGLIGGASLNADEFGAICRAAGN | Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P). | B1J266 |
B2VKA5 | UBIC_ERWT9 | Chorismate pyruvate-lyase | Erwinia | MTENALPLLSAIEWLPEPSPLLTASLLDWLLEADSMTRRFEAHCQKVTVNLLREAFISPEEIAAEAALLPPEKQYWLREIELCADGIPWLVARTLVPESTLVGPEQKLRQLGSVPLGRYLFASSSLTRDFIDVGQSAGLWARRSRLRLAGKPLLLTELFLPASPLYGSLAKENT | Removes the pyruvyl group from chorismate, with concomitant aromatization of the ring, to provide 4-hydroxybenzoate (4HB) for the ubiquinone pathway. | B2VKA5 |
Q8EX00 | FMT_MALP2 | Methionyl-tRNA formyltransferase | Malacoplasma | MGEKRNSCKNKKIVFMGTPEIATYALNALLEKSFDVVAVVCQPDKPIGRKKEIIFSSVKKLAIEKNIKFFQPNKIKEIENELKELNPFAFVTCAFGQFIPDSILSIPEFGCINIHASLLPKYRGGAPIHWAVINGEKETGVCLMRTIKQMDAGDVYCSRKVNIEESDTTSTLFKKMNNLVYDIVLNDLEKVFNLEYPPIKQDESKVSFAYNISKDDEKINFEKNAVEIVNLIRGLSETPGAYCFINDKKMKLFKAVSTNSKSNNAPGTINNISKEGILISTKDFDILVKEVQIEGKNRQEVKNILNGNSEIKIGVTLK | 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. | Q8EX00 |
Q8DKT0 | SYP_THEVB | Prolyl-tRNA synthetase | Thermosynechococcus | MRLSQMLFVTLRDEPAEAEIPSHKLLLRAGYIRRIASGIYSYLPLMWRVLQKVSAIVREEMNRSGALECLLPQLQPAELWQESGRWDTYTKAEGIMFSLTDRAQRQLGLGPTHEEVITALAKDLIRSYRQLPVHLYQIQTKFRDEIRPRFGLMRGREFIMKDGYSFHADVASLKETYQVMYDTYSRILQRCGLTFRAVEADSGAIGGSGSHEFMVLAAAGEDEVLYTADGQYAANVEKAVSLPPDAVPTTYKTVATLDTPNAATIDALVEQLQCHPTQIVKNVLYRAVFDNGRVGLVLVSIRGDQEVNSVKLHNTLTSLA... | 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... | Q8DKT0 |
Q92D47 | DLTA_LISIN | D-alanine-activating enzyme | Listeria | MTTSIIERIDAWAEKTPDFPCYEYAGTRLSYKELKRQSDAFGSFLLNTLNSDKEKPIIVYGHMSPLMLIAFLGTIKSGRAYVPVDVSMPVERIEQIKKAADPALFICTEELPSNLTITGCPVLTQDQLMDALEKHFEEVPDPAECVKNDDNYYIIYTSGSTGNPKGVQISQNNLVSFSNWILQDFSLRQGLRFLNQAPFSFDLSVMDLYPSLLSGGTLVPLDKTITANMKDLYREIPAQNFDVWVSTPSFADLCLLDDNFNQENNPNLTRFLFCGEVLAKKTASELLDRFPDAVIYNTYGPTEATVAVTQVKVTRELIDA... | Catalyzes the first step in the D-alanylation of lipoteichoic acid (LTA), the activation of D-alanine and its transfer onto the D-alanyl carrier protein (Dcp) DltC. In an ATP-dependent two-step reaction, forms a high energy D-alanyl-AMP intermediate, followed by transfer of the D-alanyl residue as a thiol ester to the ... | Q92D47 |
P07919 | QCR6_HUMAN | Ubiquinol-cytochrome c reductase complex 11 kDa protein | Homo | MGLEDEQKMLTESGDPEEEEEEEEELVDPLTTVREQCEQLEKCVKARERLELCDERVSSRSHTEEDCTEELFDFLHARDHCVAHKLFNNLK | Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidor... | P07919 |
A9QYG5 | RAVA_YERPG | Regulatory ATPase variant A | Yersinia | MAQSSQLAERISRLSHALESGLYERQEAIRLCLLAALSGESVFLLGPPGIAKSLIARRLKFAFRHARAFEYLMTRFSTPEEVFGPLSIQALKEEGRYQRMTGGYLPEAEIVFLDEIWKAGPAILNTLLTAINERRFRNGDREDSIPMRLLVTASNELPDADSSLEALYDRMLIRLWLDRVQEKQNFRSLLISRQNENHNPVAENLSITDEEFHQWQPLIDKITLPDHCFELIFQLRQRLSALEHTPYVSDRRWKKALRLLQASAFFSGRDEITPIDLILLKDCLWHDLNSFKLLQQQLEQLLTEQGYQQQNLLMKLQDIN... | Functions as an ATPase. May play a role in metal insertion (metal-chelatase) or as a chaperone. | A9QYG5 |
Q9SLB7 | LBD16_ARATH | ASYMMETRIC LEAVES 2-like protein 18 | Arabidopsis | MASSGNGTTAGTGSPCGACKFLRRKCASDCIFAPYFSSEQGAARFAAIHKVFGASNVSKLLLNVPIHDRCEAVVTIAYEAQARLHDPVYGCVSHIFALQQQVAFLQSQVMQMKAQIAGHQTSAAGDLRHSSESTNQFMTWQQTSVSPIGSAYSTPYNHHQPYYGHVNPNNPVSPQSSLEESFSNTSSDVTTTANVRETHHQTGGGVYGHDGIGFHEGYPNKKRSVSYCSSDLGELQALALRMMKN | Transcriptional activator . Involved in lateral root formation. Regulated by the transcriptional activators ARF7 and ARF19 . Functions in the initiation and emergence of lateral roots, in conjunction with LBD18, downstream of ARF7 and ARF19 . Acts downstream of the auxin influx carriers AUX1 and LAX1 in the regulation ... | Q9SLB7 |
P65687 | PCKG_MYCBO | Phosphoenolpyruvate carboxykinase [GTP] | Mycobacterium tuberculosis complex | MTSATIPGLDTAPTNHQGLLSWVEEVAELTQPDRVVFTDGSEEEFQRLCDQLVEAGTFIRLNPEKHKNSYLALSDPSDVARVESRTYICSAKEIDAGPTNNWMDPGEMRSIMKDLYRGCMRGRTMYVVPFCMGPLGAEDPKLGVEITDSEYVVVSMRTMTRMGKAALEKMGDDGFFVKALHSVGAPLEPGQKDVAWPCSETKYITHFPETREIWSYGSGYGGNALLGKKCYSLRIASAMAHDEGWLAEHMLILKLISPENKAYYFAAAFPSACGKTNLAMLQPTIPGWRAETLGDDIAWMRFGKDGRLYAVNPEFGFFGV... | Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle. | P65687 |
Q02YJ4 | PYRF_LACLS | OMP decarboxylase | Lactococcus cremoris subsp. cremoris | MQENRPVIALDFPEFSDVKDFLEKFDPSEKLYIKLGMELFYTAGPQVVYYVKSLGHSVFLDLKLHDIPNTVESSMRVLARLGVDMVNVHAAGGVEMMVAAKRGLEAGTPTGRQRPKLIAVTQLTSTSEEIMQNDQKIMTSLEESVINYAQKTAQAGLDGVVCSAHEVEKIKAATSKEFICLTPGIRPEGASKGDQKRVMTPKEARTIGSDYIVVGRPITQAKDPVSAYHAIKEEWNQ | Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP). | Q02YJ4 |
P48081 | ATPB_CYAPA | F-ATPase subunit beta | Cyanophora | MATTTSKTNTGYVTQVIGPVLDVSFPNGQLPKIYNAITVKGKNEAGQDITVTCEVQQLLGDNQVRAVSMSTTDGILRGMEVTDSGAAISVPVGTPTLGRIFNVLGEPVDELGAVVCDSTLPIHRPSPAFTQLETKSSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYQEMKESKVIDENNLPASKVALVYGQMNEPPGARMRVALTALTMAEYFRDVNNQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLGTEMGSLQERITSTTKGSITSIQAVYVP... | Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. | P48081 |
A7ZG01 | RL24_CAMC1 | 50S ribosomal protein L24 | Campylobacter | MANVKFKVKKGDTVKIIAGDDKGKTGKILAVLAKKGQVIVEGCKVAKKAIKPSEKTPNGGHVNKEMPIDISNVAKVEG | One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit. | A7ZG01 |
P34794 | RUB2_BRANA | CPN-60 alpha | Brassica | MATANALSSPSVLCSSRQGKLSGGSQQKGQRVSYRKANRRFSLRANVKEIAFDQSSRAALQAGIDKLADAVGLTLGPRGRNVVLDEFGSPKVVNDGVTIARAIELPDAMENAGAALIREVASKTNDSAGDGTTTASVLAREIIKHGLLSVTSGANPVSLKRGIDKTVQALIEELEKRSRPVKGGRDIKAVATISAGNDELIGAMIADAIDKVGPDGVSPIESSSSFETTVEVEEGMEIDRGYISPQFVTNPEKLLVEFENARVLITDQKITAIKDIIPILEKTTQLRAPLLIIAEDVTGEALATLVVNKLRGVLNVVAVK... | This protein binds RuBisCO small and large subunits and is implicated in the assembly of the enzyme oligomer. | P34794 |
Q88XY6 | RL3_LACPL | 50S ribosomal protein L3 | Lactiplantibacillus | MTTKGILGKKVGMTQVFTESGELVPVTVVEVQPNVVLQVKTVENDGYEAIQLGVDDKREVLTNKPAQGHAAKAKTTPKRFIREIRNVELGDYTVGDEVKADIFAAGDAVDVTGITKGHGYQGNIHKDGQSRGPMAHGSRYHRRPGSMGAIINRVFKGKKLPGRMGNHQRTMQNLQIVRADVENNVLLIKGNVPGANKSFVTVKTSVKSK | One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit. | Q88XY6 |
A7ILC5 | TIG_XANP2 | PPIase | Xanthobacter | MQVTETQADGLKRAFRVVVSAADLGAKADAKLAELKGQVKLNGFRPGKVPVAHLKRVYGKSVMSEVIEQTVNETNGKIVEEHGFKLALQPKVKLPEEDPQAQGLLEGGKDLAYDLEIEILPKIELGNFKDISVEKLVVEVSDAEVDETIQRIADANRPFVTREGGYAENGDRVTIDFTGYVDGEKFPGGEGQDIDVLLGSNGFIPGFEEQLLGVYAGDNRTLNVTFPEAYAAKELAGKAATFEVTVKSVAAPGPLTLDDEFAKTLGQESLEKLKEMVRARIASEHAGAARQKVKRALLDALDTTHQFAVPEGLVEQEFFG... | Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase. | A7ILC5 |
A4W9J7 | ASTD_ENT38 | Succinylglutamic semialdehyde dehydrogenase | Enterobacter | MSLWINGDWVTGEGERRVKTNPVGNEALWQGFDASPAQVEQACQAARKAFPAWAKLPFTARQAIVEKFATLLEANKAELTRVIARETGKPRWEATTEITAMINKITISVKAYHTRTGEQHTAMADGAATLRHRPHGVLAVFGPYNFPGHLPNGHIVPALLAGNTVIFKPSELTPWSGEAVVKLWEQAGLPPGVLNLVQGGRETGQALSALSDLDGLLFTGSAGTGYQLHRQLAGQPEKILALEMGGNNPLIVEDPEDIDAAVHLAIQSAFVTAGQRCTCARRLLVKNGAQGDAFLARLIEVTARLVPDAWDAEPQPFIGG... | Catalyzes the NAD-dependent reduction of succinylglutamate semialdehyde into succinylglutamate. | A4W9J7 |
P0CU74 | CLAB_PASFU | Cladofulvin biosynthesis cluster protein B | Fulvia | MTRQAVPKPAYEDLVDCQSAMFEWAESFDSKDWDRLSACLAPTLFLDYSDIMGKKWDALPVEEFIGMASSPHFLGNARIKTQHFIGASKWTQPDEGQIVGFHQMRVAHQKYGDDELKQVLYHGHAHGKATTYYRNVGGQWKFAGLVPDVRWTEFDCDKIFEH | Scytalone dehydratase-like protein; part of the gene cluster that mediates the biosynthesis of the bianthraquinone cladofulvin, a conidial pigment not required for virulence but that plays a role in fitness and resistance to environmental stresses including UV light and low-temperature stress . The pathway begins with ... | P0CU74 |
A2CC31 | RS19_PROM3 | 30S ribosomal protein S19 | Prochlorococcus | MGRSLKKGPFIADSLLRKLEKQNADDDKSVIKTWSRASTILPMMIGHTIAVHNGRSHVPVFITEQMVGHKLGEFAPTRTFKGHIKDKKGGR | Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA. | A2CC31 |
A0LDB5 | DAPA_MAGMM | 4-hydroxy-tetrahydrodipicolinate synthase | Magnetococcus | MFKGVYTALITPFKNRAVDYTALAKLVEQQINGGIHGLVPCGTTGESATLSHEEHKAVIRTVVELVQGRVKVLAGTGSNCTEESTELTCYAEEVGADGALLITPYYNKPTQAGLIAHYTTVANHTKLPVVLYNVPGRTAVDMHADTVIALSKVSNIVAIKEATGNMERASQIHKGAGSSMTLISGDDATFLPFLSVGGQGVISVTTNLAPRLVRDLWDLWHNGQINEAREVHEQLLEINGLLFCETSPIPVKAGAAMLGLCHNELRLPMTAMSEANQAKLHRAMVKLNLLEE | Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA). | A0LDB5 |
A4Y193 | ATP6_PSEMY | F-ATPase subunit 6 | Pseudomonas | MADTPAEYIQHHLQNLVYGSHPEKGWIIAQTPEEVKAMGFWAVHVDTLGWSLFMGLIFITLFRMAAKKAVTGVPSGLQNMAEMCIEFVQGIVKDTFHGKNPLVAPLALTIFVWVFLMNSLKWIPVDYIPGLAHAMGLPYFKIVPTADPNGTFGISLGVFLLIIFYSIKVKGVGGFTKELSFTPFNHWALIPFNLFLEIIGLLTKPLSLALRLFGNMYAGEVVFILIALLPFYVQWGLNVPWAIFHILVIPLQAFIFMVLTVVYLSAAHEDHH | Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. | A4Y193 |
Q31AS9 | ACSF_PROM9 | Magnesium-protoporphyrin IX monomethyl ester [oxidative] cyclase | Prochlorococcus | MSQSIIESKNKKDVNNGKIPAKETILSPRFYTTDFEAMENMDLSINEEELEAICEEFRKDYNRHHFVRNSEFDGAAEKLDPETRELFVDFLEGSCTSEFSGFLLYKELSRRIKDKNPLLAECFAHMARDEARHAGFLNKSMSDFGLQLDLGFLTANKDYTYFPPRSIFYATYLSEKIGYWRYIAIYRHLEKNPDSKIFPLFNYFENWCQDENRHGDFFDALMKAQPRTVKSLSQKINIGGTTFTHPLFDYFHRFRYFLNNLPITSKLWSRFFLLAVFATMYARDLGIKKDFYSSLGLDAREYDQYVINKTNETSARVFPV... | Catalyzes the formation of the isocyclic ring in chlorophyll biosynthesis. Mediates the cyclase reaction, which results in the formation of divinylprotochlorophyllide (Pchlide) characteristic of all chlorophylls from magnesium-protoporphyrin IX 13-monomethyl ester (MgPMME). | Q31AS9 |
Q28C34 | AN13C_XENTR | Ankyrin repeat domain-containing protein 13C | Silurana | MTGEKIRSLHRDQKPSKDEDLLEPDEEATAGGTFTRTGKLKNSKMFSNHKVIRSPSNPALLQNHHQQISPITPGESKTDAYFPVHECVFKGDIRRLSSLIRSHSIGQKDNHGNTPLHLAVMLGNKECAHLLLAHNAPVKVKNAQGWSPLAEAISYGDRQMITALLRKLKQQSRESVEEKRPRLLKALKELGDFYLELHWDFQSWVPLLSRILPSDACKIYKQGINIRLDTTLIDFTDMKCQRGDLSFIFNGDAAPSESFVVLDNEQKVYQRIHHEESEMETEEEVDILMSSDIYSATLSTKSISFTRAQTGWLFREDKTE... | Acts as a molecular chaperone for G protein-coupled receptors, regulating their biogenesis and exit from the ER. | Q28C34 |
P45461 | AMPR_YEREN | HTH-type transcriptional activator AmpR | Yersinia | MVRSYIPLNSLRAFEAAARQLSFTKAAIELNVTHAAISQQVKALEQRLNCRLFIRISRGLVLTTEGENLLPILNDSFDRIADTLDRFSTGIIREKVRVGVVGTFATGYLLSRLRDFQQHSPHVDILLSTHNNRVDVVAEGLDYAIRYGNGALAWHESHFMYAPPLAQLCAPSISKRFTPPTDLQRFMLLGSYRAMNWSAWFAAAGGSVPSPSQQIMMFDSSVSMLEAAQAEIGIALAPPAMFMHLLRSERIIQPFSTTVSLGGYWLTRLQSRTETPAMRDFALWLLSEMKSEGE | This protein is a positive regulator of gene expression of beta-lactamase (AmpC). | P45461 |
O51202 | CSRA_BORBU | Translational regulator CsrA | Borreliella | MLVLSRKANESIKINSDIEVLILEIKKDAVKIAIKAPENIKIFRSEIYEFIIEENKKSLLKDKHNISKIKSLFNHYFKNEN | A translational regulator that binds mRNA to regulate translation initiation and/or mRNA stability. Usually binds in the 5'-UTR at or near the Shine-Dalgarno sequence preventing ribosome-binding, thus repressing translation. Its main target seems to be the major flagellin gene, while its function is anatagonized by Fli... | O51202 |
B2TYP2 | SSRP_SHIB3 | Small protein B | Shigella | MTKKKAHKPGSATIALNKRARHEYFIEEEFEAGLALQGWEVKSLRAGKANISDSYVLLRDGEAFLFGANITPMAVASTHVVCDPTRTRKLLLNQRELDSLYGRVNREGYTVVALSLYWKNAWCKVKIGVAKGKKQHDKRSDIKEREWQVDKARIMKNAHR | Required for rescue of stalled ribosomes mediated by trans-translation. Binds to transfer-messenger RNA (tmRNA), required for stable association of tmRNA with ribosomes. tmRNA and SmpB together mimic tRNA shape, replacing the anticodon stem-loop with SmpB. tmRNA is encoded by the ssrA gene; the 2 termini fold to resemb... | B2TYP2 |
Q59LF9 | MAP2_CANAL | Peptidase M | Candida | MAGVTEGEDTKVIESKINELNIDKPKLEDNNEAKGNGNGNESGDDDDDDKEEDDDNEITEPSTSTASGDEKKKKNKNKKKKKKKIVSIDSSYPEGIFPEGQWMEYPLEDINSYRTTSEEKRYLDRQQNNKWQDFRKGAEIHRRVRHKAQSSIRPGMTMIEIANLIEDSVRNYSGNDHTLKAGIGFPTGLSLNHVAAHYTPNTGDKLILKKDDIMKVDIGVHVNGRICDSAFTMTFNEDGKYDTIMQAVKEATYTGIKESGIDVRLNDIGAAIQEVMESYEMEENGKTYPIKCIKNLNGHNIDDFVIHSGKSVPIIANGDM... | Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). | Q59LF9 |
P57620 | EX1_BUCAI | DNA deoxyribophosphodiesterase | Buchnera | MIQFQKKTPNFLFYDYETFGIHTALDKPAQFACIRTDINLNIIDDPQYFYCFPSDDYLPDPGSVLITHITPQYTEKNGTNEYNFSQKIYDILMQSNTCVVGYNNINFDDEITRNIFYRNFFDPYEWSWKNGNSRWDILNLLRACYALRPTGINWPKNELGLTSFKLSDLTKTNNIVHLNAHNAVSDVYATIEIAKLVKKKQPRLFDFFFKIRKKNELYKLIDLRNFQPIIYISAYFGAIYHNMSCILPIAWHENNSNILIAIDLFKDIKTLINMCKKICFDSIFIKNLLDSGVVLLHLNRCPILAPIQVIRKEDYNRLNF... | Degrades single-stranded DNA (ssDNA) in a highly processive manner. Also functions as a DNA deoxyribophosphodiesterase that releases deoxyribose-phosphate moieties following the cleavage of DNA at an apurinic/apyrimidinic (AP) site by either an AP endonuclease or AP lyase. | P57620 |
Q3ZXI2 | ILVC_DEHMC | Ketol-acid reductoisomerase type I | Dehalococcoides | MAVIYYDKDCDLSLIEKKLIGIVGYGAQGHAHAQNLRDSGLKVIVACVEGGRGWKKATADGFEVMCVAEMAKKADIIMMLAPDTSQAKIYKDSIEQGLKPGKMLMFAHGFNIHYGQIVPPSFVDVTMIAPKCPGYMLRQVFTEGAGAPSLIAVEQDASGKAKELALAYAKGIGSNRAGILETTFAEETETDLFGEQAVLCGGTTSLVKAGFETLVEAGYQPEVAYFECLHELKLIVDLMYQGGIAYMRDSISDTAKYGDFTRGPRVINEDTYETMGEILGEIQDGSFAKEWILENQAGRPVYNSLRRMESEHLIEEVGAE... | Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobu... | Q3ZXI2 |
P55835 | RL2_AGGAC | 50S ribosomal protein L2 | Aggregatibacter | MAIVKCKPTSAGRRHVVKVVNPELHKGKPFAALLDTKSKTGGRNNYGRITTRHIGGGHKQHYRLIDFKRNKLDIPGVVERLEYDPNRSANIALVLYKDGERRYILAPKGLAAGDQIQAGAHAPIKVGNALPMRNIPVGSTVHNVELKPGKGGQIARSAGSYVQIIAREGNYVTLRLRSGEMRKVLAECSATIGEVGNSEHMLRVLGKAGANRWRGVRPTVRGTAMNPVDHPHGGGEGRNFGKHPVTPWGVQTKGKKTRHNKRTDKYIVRRRGK | One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome. | P55835 |
A8AK32 | EX7S_CITK8 | Exodeoxyribonuclease VII small subunit | Citrobacter | MPKKNEAPASFETALSELEQIVTRLESGDLPLEEALNEFERGVQLARQGQAKLQQAEQRVQILLSDNEDASPEPFTPDNE | Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides. | A8AK32 |
Q9SXD5 | GSXL3_ARATH | Flavin-monooxygenase glucosinolate S-oxygenase-like 3 | Arabidopsis | MAPALSPTRSHHVAVIGAGPAGLVAARELRREGHSVVVFEKQKQVGGTWIYTDEVESDPLSVDPTRSVVHSSVYRSLRINGTRECTGYRDFPFVVRSGVSRDPRRFPSHGEVLAYLKDFAKEFGIEEMVRFETEVVKVSPAAEEGIGKWRIESTEKEKKVRRDEIYDAVVVCNGHYVEPRLAQIPGISSWPGKEMHSHNYRIPEPFRDKVVVLIGNSSSAEDISRDIARVAKEVHVACRSNPADTFIKQTGYNNLWTHSMIESVHEDGSVVYQNGKTISVDIIMHCTGYKYHFPFLDTNGIVTVDDNRVGPLYKDVFPPA... | Catalyzes the conversion of methylthioalkyl glucosinolates of any chain length into methylsulfinylalkyl glucosinolates. | Q9SXD5 |
A1B363 | PLSX_PARDP | Phosphate-acyl-ACP acyltransferase | Paracoccus | MASADSNTLPRAPGDGDGVVISVDAMGGDRGPATVVAGMAESAGKNPGIRFIVHGPQAELERLIARRGDLAGRCDIRDAAGVVTMDDKPSQVLRKGEGTSMWSTLESVRQGEATAAVSCGNTGALMALSMLRLRKLPGVNRPAIACLWPSRNPQGFNVMLDVGADIRADAQDLLTYALMGASYARNGFGLERPRVGLLNVGTEEHKGRPELKQAHELIPTTAQAANFDYVGFVEGGDLPSARVDVIVTDGFTGNVALKTGEGTAKLVGELLKEAFGKSVMSKFAALLAMGSLKRLQKRIDPRRINGGVFLGLNGTVVKSH... | Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA. | A1B363 |
P0DUI7 | APOE_DICSS | Apolipoprotein E | Dicerorhinus | MKVLWPALVVTLLAGCRADVEPGPEVQLGKEWATWQASQPWEQALGRFWNYLRWVQTLSEQVQEELLSSQVTEELTALMDDTMKEVKACKSELEEQLGPVAEETKARVSKELQAAQARLGADMEEVRNRLAQYRGELQAMVGQSTEELRGRLNAHLRKLRKRLLRDAEDLQQRLAVYQAGIREGAERSVNTLREHLGPLAEQAATMHTLVSKPLQERAEAWAQRLRGRLEKAGFPVGDRLDEVREQVQEVRAKVEEQANQVRLQAEAFQGRLKSWFEPLVQDMQQKWAELVEKVQLALRAVPTSVPSEKQ | APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids. APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance. Apoliproteins are amp... | P0DUI7 |
Q2G8W8 | RL5_NOVAD | 50S ribosomal protein L5 | Novosphingobium | MADKYTPRLKGKYDAEIAAAMQAKFGYKNALEIPRIEKITLNMGVGEASQDKKKVTTAAAEMELIAGQKPVITKAKKSIAQFKLREGMPIGCKVTLRRERMYEFLDRLITIAMPRIRDFRGLNPKSFDGRGNYAMGLKEQIIFPEISYDQIEKVRGMDIIVTTTAKTDDEARELLRLFGFPFPQDAAEQQQAA | This is 1 of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. In the 70S ribosome it contacts protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; this bridge is implicated in subunit movement... | Q2G8W8 |
G9N4A8 | VIRE_HYPVG | Virensol biosynthesis cluster protein E | null | MPKPWVVFGLGTLVLFLWRLNKIGRRPKNYPPGPPTLPLIGNLHLMPKKNAHLQFQRWAEEYGPVYSLMLGTKVAIVLSSDVAVKDLLDKRSSIYSGRPELYMGQEIMSGGNRPLFMGINSVWRRVRKLAHGLLNVKVSRTYVPYQDLESRDMLMGLLESPKDFLNHIRRYTTSLTTQMAFGYRTPSSDDKGLLEMFENFDELSRLTGSQSAAILDLYPIARILPDFLLPARRLGREYYEREKKLFMKHFLNARQQLNSGTSKPCCAIDLLRAQKEYGFSDEFGCYLSGSLLQAGSETTAIILTGFFQAMLVFPEVSKEA... | Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of virensols and trichoxide, fungal natural products that contain or are derived from a salicylaldehyde core . The pathway begins with the synthesis of the reduced chain in virensol C by the highly reducing polyketide synthase virA v... | G9N4A8 |
O68273 | DUSC_CUPNH | tRNA-dihydrouridine synthase C | Cupriavidus | MSRLFLAPMEGLADYVLRDVLTDTGGYDGCVSEFVRVTGSLLPARVYERETPEILAGGYTRSGTPMVIQLLGSDPEWLARNAAYAATLSPHGIDLNFGCPAKVVNRHGGGAMLLTNPELLNRIVASVRAAVPAHIAVTAKMRLGVSDASLAIDCATALAEGGAASLVVHARTRDHGYRPPAHWDWIARIAAAVDVPVIANGDVWTVADWERCRAVSGCADVMIGRGAVSDPFLALRIRGLMDGSPSDQEWPLVLRQIATYLKKLHARIASCHEHGRVKLWLSYLKRTWPQAAELHAAIRRMQDSLEIERVLEGLPGAATA... | Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines. Specifically modifies U16 in tRNAs. | O68273 |
Q4UY06 | CYSD_XANC8 | Sulfate adenylate transferase | Xanthomonas | MTLPPLSHLDRLEAESIHILREVAAEFRAPVMLYSVGKDSSVLLHLLLKAFAPSPPPIPLLHVDTRWKFREMIAFRDRRAAETAVDLRVHINPEGVAQDIGPISHGAAVHTDVMKTQGLKQALEQGGFDAAIGGARRDEEKSRAKERVFSFRNARHRWDPKNQRPELWNLYNARTKPGESVRVFPLSNWTELDIWLYIYRERIPVVPLYFAAPRPVVQRDGAWIMVDDDRLPLHPGETPQLRSVRFRTLGCYPLTGAIESTADTLEAVIAEMLVSTSSERQGRMIDHAPGASMEQKKLEGYF | With CysN forms the ATP sulfurylase (ATPS) that catalyzes the adenylation of sulfate producing adenosine 5'-phosphosulfate (APS) and diphosphate, the first enzymatic step in sulfur assimilation pathway. APS synthesis involves the formation of a high-energy phosphoric-sulfuric acid anhydride bond driven by GTP hydrolysi... | Q4UY06 |
P32445 | RIM1_YEAST | Mitochondrial ssDNA-binding protein | Saccharomyces | MFLRTQARFFHATTKKMDFSKMSIVGRIGSEFTEHTSANNNRYLKYSIASQPRRDGQTNWYNITVFNEPQINFLTEYVRKGALVYVEADAANYVFERDDGSKGTTLSLVQKDINLLKNGKKLEDAEGQENAASSE | This protein binds preferentially and cooperatively to single-stranded DNA (ssDNS). Involved in mitochondrial DNA replication. Stimulates PIF1 helicase activity. | P32445 |
Q55DR6 | FCSA_DICDI | Long-chain-fatty-acid--CoA synthetase 1 | Dictyostelium | MSSLSTKTDLLGDPDFIRLQSVEVDGSEVIPGETRPRRNTKFPKLTNSPDGKTFTLYDVYRINKDSDSNFLGIRELLADGKRGDYKWISYKQACIRANNIGSALVQLGLNKGDRIGIFSINRPEWVLSDMAAMNHSLVPVALYATLGANAIEYVVNHSEISVLLCEGKNVEKILSMPGTTIKTIVSYDPLPQATLDKFKDNENVKLYLLSDFEKLGEQNPAQHEVPSPEDLCTLLYTSGSTGNPKGVMLTHTNMVSEVAGANFSPAGVIPEDVHMSYLPLAHSFERAVVSLMCYVGGQIGFFSGLIPELFNDIQVLRPTF... | Long chain fatty acid acyl-CoA synthetases catalyze the formation of a thiester bond between a free fatty acid and coenzyme A during fatty acid metabolic process. May mediate fatty acid retrieval from the lumen of endosomes into the cytoplasm. | Q55DR6 |
B2SVN5 | TRPA_XANOP | Tryptophan synthase alpha chain | Xanthomonas | MRRIDFRFAELRANGRKALIPFITAGDPSLEATVPVMHALVRAGADVIELGVPFSDPMADGPTIQRSSERALGRGAGLAYVLEAVHEFRREDAATPVVLMGYLNPIEIHGTRRFAEAAVAAGVDGLLLVDLPPEEADETRAIFTEVGLALIALASPTTSEQRLDMLCSTAQGYLYYVSFAGVTGASNLLDTYAASDRLRQLRQRAGAPVVAGFGIKDAASAAAMAVDADGVVVGSALVAALAEADDVRSARERAEAFLAPLRQALDQA | The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. | B2SVN5 |
B6J5K2 | MURC_COXB1 | UDP-N-acetylmuramoyl-L-alanine synthetase | Coxiella | MQLDKKIINHVHCLGIGGIGVSALAEILLKKGCRVTGSDVSPNKNTERLQRLGAEIIFNHDGTAITQADCAVYSSAIGATNPELMAAKQAKIPLLKRGEMLANLMKEYQSIAVAGAHGKTTTSGMLSHAFVEANLDPTFMVGGVLNNSQTPARVGNGHYFIAEADESDASFLFMHPDIAVVTNIDADHLSTYDGDFNRLKQTYIQFLEQTAQDGVVVLCLDDPILREIAPLLSRRVITYGFSSDAQYRVVDYCQQGIQSLFQIHSPQRKAPLTVKLSMPGQHNALNATAVTAIADVVRMNEPALLKSLADFPGVDRRFTI... | Cell wall formation. | B6J5K2 |
O22833 | LRK54_ARATH | L-type lectin-domain containing receptor kinase V.4 | Arabidopsis | MSRTIGSRVIFLILALFCCTENSRGKLVMQGSAGFFKGYRTLTSTKKHAYGQAFEDEIVPFKNSANDTVTSFSVTFFFAIAPEDKHKGAHGMAFVISPTRGITGASADQYLGIFNKANNGDSSNHVIAVELDINKDEEFGDINDNHVGININGMRSIKFAPAGYYDQEGQFKDLSLISGSLLRVTILYSQMEKQLNVTLSSPEEAYYPNKPLLSLNQDLSPYILENMYVGFSASTGSVRAMHYMLSWFVHGGVDVPNLDLGIPTFPPYPKEKSLVYRIVLVTSLALVLFVALVASALSIFFYRRHKKVKEVLEEWEIQCG... | Involved in resistance response to the pathogenic oomycetes Phytophthora infestans and Phytophthora capsici and to the pathogenic bacteria Pseudomonas syringae. | O22833 |
P01611 | KVD12_HUMAN | Ig kappa chain V-I region Wes | Homo | MDMMVPAQLLGLLLLWFPGSRCDIQMTQSPSSVSASVGDRVTITCRASQGISSWLAWYQQKPGKAPKLLIYAASSLQSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQANSFP | V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition . Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as recep... | P01611 |
Q3Z6V4 | GATC_DEHM1 | Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit C | Dehalococcoides | MKLNREDVLHIARLAKLGLEEDEINRLSKELSALLEHFEVLQQVDTTGVEPTAQSTPVKSVLKEDIIKPSYDREEILSNAPRREGDYVRIRAVME | Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated ... | Q3Z6V4 |
A9MPK1 | DGTP_SALAR | Deoxyguanosinetriphosphate triphosphohydrolase | Salmonella | MASIDFRNKINWHRRYRSPQGVKTEHEILRIFESDRGRIINSPAIRRLQQKTQVFPLERNAAVRTRLTHSMEVQQVGRYIAKEILSRLKAQNLLEEYGLDALTGPFESIVEMACLMHDIGNPPFGHFGEAAINDWFRQRLYPEDAESQPLTHDRCVVSSLRLQEGEESLNDIRRKVRQDICYFEGNAQGIRLVHTLMRMNLTWAQVGGILKYTRPAWWRGPVPDSHRYLMKKPGYYLSEEKYIARLRKELQLAPYSRFPLTWIMEAADDISYCVADLEDAVEKRIFSVEQLYHHLYHAWGHHEKDSLFELVVGNAWEKSR... | dGTPase preferentially hydrolyzes dGTP over the other canonical NTPs. | A9MPK1 |
Q6KHL2 | ECFA2_MYCMO | Energy-coupling factor transporter ATP-binding protein EcfA2 | Mesomycoplasma | MQIEVKNISKVFEPKSPIEFTALKGVSLSFEQGEFISIIGPTGSGKTTFIEHLNALNLPSIGSIVIKGKFKDQKDKKNPVLIESEVILQKTKRKIKQIKEIRRQIGIVFQFAEYQLFESTIEKDIAFGPISLGISKEEAYKRAKKYISIVGLPENYLQRSPFELSGGQKRRVALAGILAMDPDFLIFDEPTAGLDPQGSKEILEIFGKLNSEGKTVIIVTHNLDHALEWTNRTIFFNDGFVIKDGKTYDVLEDVDFLRENEMEPPKLLVLKKLLQDKGINLSKVRSIEDFAREINQYLETKNKTKENN | ATP-binding (A) component of a common 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. | Q6KHL2 |
Q2LT94 | MIAB_SYNAS | tRNA-i(6)A37 methylthiotransferase | Syntrophus | MMKSSNKSSGSLIRLDKKHIYIQTLGCQMNVHDSEQIAALMEEKGYICTEDANEADLIILNTCSIREKAAQKAKSQLGRYRNLKRKKRNLLIGVGGCLAQQLGDELLTKVPDIDFIFGTHNIHQLPDFISRIEKSRKKIVETTLHPSTPSIGVLALPCNGQVSSFVTIMQGCNNFCSYCIVPYVRGREESRPPEDIIHEIRMLADHGVKEVTLLGQNVNSYARKTSGEMGFAELLREIEKIKGIERMRFTTSHPKDLSEFLITAFSDLSKLCHHIHLPFQSGSDRILALMNRGYTKSDYLAKVERLRTVCPDISITADVI... | Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine. | Q2LT94 |
Q83R85 | OPGD_SHIFL | Glucans biosynthesis protein D | Shigella | MDRRRFIKGSMAMAAVCGTSGIASLFSQAAFAADSDIADGQTQRFDFSILQSMAHDLAQTAWRGAPRPLPDTLATMTPQAYNSIQYDAEKSLWHNVENRQLDAQFFHMGMGFRRRVRMFSVDPATHLAREIHFRPELFKYNDAGVDTKQLEGQSDLGFAGFRVFKAPELARRDVVSFLGASYFRAVDDTYQYGLSARGLAIDTYTDSKEEFPDFTAFWFDTVKPGATTFTVYALLDSASITGAYKFTIHCEKSQVIMDVENHLYARKDIKQLGISPMTSMFSCGTNERRMCDTIHPQIHDSDRLSMWRGNGEWICRPLNN... | Probably involved in the control of the structural glucose backbone of osmoregulated periplasmic glucans (OPGs). | Q83R85 |
P65991 | RECR_MYCBO | Recombination protein RecR | Mycobacterium tuberculosis complex | MFEGPVQDLIDELGKLPGIGPKSAQRIAFHLLSVEPSDIDRLTGVLAKVRDGVRFCAVCGNVSDNERCRICSDIRRDASVVCIVEEPKDIQAVERTREFRGRYHVLGGALDPLSGIGPDQLRIRELLSRIGERVDDVDVTEVIIATDPNTEGEATATYLVRMLRDIPGLTVTRIASGLPMGGDLEFADELTLGRALAGRRVLA | May play a role in DNA repair. It seems to be involved in an RecBC-independent recombinational process of DNA repair. It may act with RecF and RecO. | P65991 |
Q13IY4 | RCOM2_PARXL | Regulator of CO metabolism 2 | Paraburkholderia | MKSSESAAATASERRAETFQHKLEQFNPGIVWLDPQGHVSAFNDVALHILGPAGEQSLGVAQDHLFGIDVVQLHPEKSRDKLRFLLQSRDAGGCPVRSPPPVAMMINIPDRILMIKVSKMTGAAGTCGSCMIFYDVTDLTTEPSSQPAGASVPAPRRLFKIPVYRKSRVILIDLKDIVRFQGDGHYTTIVTKDERYLSNLSLADLELRLDSSVYLRVHRSHIVSLPYAVELVKLDESVNLVMDDAEQTQVPVSRSRTAQLKELLGVV | One-component, b-type heme-containing aerobic sensor and transcriptional regulator that responds to CO by activating the expression of the oxidation operon cox. | Q13IY4 |
P0DP69 | PHNE1_ECOLI | Putative cryptic phosphonate transport system permease protein PhnE1 | Escherichia | MPDAVQAPYPAYRPEPNMQTITIAPPKRSWFSLLSWAVVLAVLVVSWQGAEMAPLTLIKDGGNMATFAADFFPPDFSQWQDYLTEMAVTLQIAVWGTALAVVLSIPFGLMSAENLVPWWVYQPVRRLMDACRAINEMVFAMLFVVAVGLGPFAGVLACWRCLSTPPACSPSCFPKRWKRLSPARWKAFAPPVPTSSKRSSTACCHR | N-terminal fragment of the PhnE protein, part of a phosphonate usage operon that is cryptic in K12 strains. Growth of K12 strains on phosphonate can be observed when it is used as the sole phosphorus source after a 60 hour lag period, suggesting the operon is activated . An intact PhnE in strain B is (AC A0A140NFA3). P... | P0DP69 |
B8F8H4 | TUSA_GLAP5 | Sulfur carrier protein TusA | Glaesserella | MTELTINHTLDTLGLRCPEPVMLTRKTIRNMADGEVLLIIADDPATTRDIPSFCQFMDHQLLKSQTDTKPYQYWVKKGLDHL | Sulfur carrier protein which probably makes part of a sulfur-relay system. | B8F8H4 |
C6WX51 | NUOK_METML | NDH-1 subunit K | Methylotenera | MVGLSHYLILGSLLFAISVIGIFLNRKNVIILLMAIELMLLAVNLNFIAFSHYLNDVAGQVFVFFILTVAAAESAIGLAILVVLFRNLRTINVDDLDSLKG | NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are t... | C6WX51 |
Q49SP3 | TPSPS_POGCB | Delta-guaiene synthase | Pogostemon | MELYAQSVGVGAASRPLANFHPCVWGDKFIVYNPQSCQAGEREEAEELKVELKRELKEASDNYMRQLKMVDAIQRLGIDYLFVEDVDEALKNLFEMFDAFCKNNHDMHATALSFRLLRQHGYRVSCEVFEKFKDGKDGFKVPNEDGAVAVLEFFEATHLRVHGEDVLDNAFDFTRNYLESVYATLNDPTAKQVHNALNEFSFRRGLPRVEARKYISIYEQYASHHKGLLKLAKLDFNLVQALHRRELSEDSRWWKTLQVPTKLSFVRDRLVESYFWASGSYFEPNYSVARMILAKGLAVLSLMDDVYDAYGTFEELQMFT... | Involved in the biosynthesis of patchoulol. Produces also at least 13 additional sesquiterpene products, including alpha- and beta-patchoulene, alpha-bulnesene, seychellene, pogostol and alpha-guiaene. | Q49SP3 |
Q65D09 | IOLJ_BACLD | 6-phospho-5-dehydro-2-deoxy-D-gluconate aldolase | Bacillus | MAFVSMKELLQEAKEHHYAIGQFNINGLQWTKAILEAAEEERSPVIAAASDRLIDYLGGFKTVSAMVAALIEEMSISVPVVLHLDHGKSPERCKQAIDAGFSSVMIDGSHSPIDENIAMTKEVVSYAGVRNVSVEAEVGTVGGMEDGLIGGVQYADIGECERIVKETGIDALAAALGSVHGKYQGEPNLGFKEMEEISRVTDIPLVLHGASGIPADQIARTIRLGHAKININTECMVAWTEKTRSIFKDNPDLYEPRAYMTPGISAVKETVKHKMREFGSSGKAVCTQKIEI | Produces dihydroxyacetone phosphate (DHAP or glycerone phosphate) and malonic semialdehyde (MSA or 3-oxopropanoate) from 6-phospho-5-dehydro-2-deoxy-D-gluconate (DKGP). | Q65D09 |
D3DJG4 | SOXA1_HYDTT | Thiosulfate-oxidizing multienzyme system protein SoxA1 | Hydrogenobacter | MGKWVTIIFVLFLYAIAQQENPAEEVKKQKELLLKEMGILPGDVYAEQGRDMFNKPMGNAGKSCSSCHGQDGRYLRGAYAHMPRYYKDMDAVADLDTRIKYCMEKYMGVGNVKHDLNFKSIATYVATLSNGMKMDVKLTHPKEREMYEKGRELWYARVGKMDFSCAICHDSEAGKRVFLQTVVAVKEDKVATHWPAYRFSNDQLWTMEDRIRGCFGDMRVAPPEHFHWAVVALNLYLSYKAKGGVVRVPGFIY | C-type diheme cytochrome, which is part of the SoxAX cytochrome complex involved in sulfur oxidation. The SoxAX complex catalyzes the formation of a heterodisulfide bond between the conserved cysteine residue on a sulfur carrier SoxYZ complex subunit SoxY and thiosulfate or other inorganic sulfur substrates. This leads... | D3DJG4 |
Q87YF8 | MURB_PSESM | UDP-N-acetylmuramate dehydrogenase | Pseudomonas | MTLHVQSAVSLRPFNTFGVDVQARLFAQARNDDEVREALAYSAEHDVPLLVIGGGSNLLLSGDVQALVLRMASRGIRIVREDCLEAIVEAEAGEPWHPFVQSCLELGLAGLENLSLIPGTVGAAPMQNIGAYGVEIKDVFHGLTALDRETGELREFALQDCAFGYRDSVFKHQPGRWLILRVRFKLSREANLHLEYGPVRQRLDQLGIDKPTPFDVSRAICAIRSEKLPDPAVLGNAGSFFKNPLVAAELYATIKSQHPGVVGYPQADGQVKLAAGWLIEQAGWKGYRDGDAGVHKLQSLVLVNYGHASGLQLLNLARRI... | Cell wall formation. | Q87YF8 |
B5Z7J7 | SPEE_HELPG | Spermidine synthase | Helicobacter | MWITQEITPYLRKEYTIEAKLLDVRSEHNILEIFKSKDFGEIAMLNRQLLFKNFLHIESELLAHMGGCTKKELKEVLIVDGFDLELAHQLFKYDTHIDFVQADEKILDSFISFFPHFHEVKNNKNFTHAKQLLDLDIKKYDLILCLQEPDIHKIDGLKRMLKEDGVFISVAKHPLLEHVSMQNALKNLGDFFAVAMPFVAPLRILSNKGYIYASFKTHPLKDLMAPKIEALTSVRYYNEDIHRAAFALPKNLQEVFKDNIKS | Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to putrescine (1,4-diaminobutane) to yield spermidine. | B5Z7J7 |
Q3BSJ1 | PROA_XANC5 | Glutamyl-gamma-semialdehyde dehydrogenase | Xanthomonas | MTIKTLALQCRDAAQVVSQLSAPAKHALLDAMAAALEADAAAILAANARDLEAARAKGTGSAMLDRLALDDKRLAGIAAALREVAQLPDPVGRITREDVRPNGIRVQKVRVPLGVIAMIYEARPNVTADAAALCIKAGNGVILRGGSEAIHSNTAIARALQRALREANVPDAALTLVEDLRRETMLELLQLNDIVDLAIPRGGEGLIRFVAEHARVPVIKHYKGVCHLFVDASAEMELALRLLIDGKATRPSACNSLETLLVHAGIAERFLPLAAQALRERKVELRGDAATQAVLPDIAAASDDDYAAEFLDLILAIRVV... | Catalyzes the NADPH-dependent reduction of L-glutamate 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate. | Q3BSJ1 |
D2Y270 | H1618_CYRHA | Peptide F4-19.87 | Haplopelma | MNTVRVTFLLVFVLAVSLGQADKDENRMEMQEKTEQGKSYLDFAENLLLQKLEELEAKLPEEDSEESRNSRQKRCIGEGVPCDENDPRCCSGLVCLKPTLHGIWYKSYYCYKK | Probable ion channel inhibitor. | D2Y270 |
Q2HJG8 | TAF7_BOVIN | Transcription initiation factor TFIID subunit 7 | Bos | MSKSKDDAPHELESQFILRLPPEYASTVRRAVQSGHVNLKDRLSIELHPDGRHGIVRVDRVPLAAKLVDLPRVMESLKTIDKKTFYKTADVCQMLVSTVDGDLYPPVEEPVATADPKASKKKDKDKEKKFVWNHGITLPLKNVRKRRFRKTAKKKYIESPDVEKEVKRLLSTDAEAVSTRWEIIAEDETKETENQGLDISSPGMSGHRQGHDSLEHDELREIFNDLSSSSEDEDETQHQDEEDINIIDTEEDLERQLQDKLNESDEQHQENEGTNQLVMGIQKQIDNMKGKLQETQDRAKRQEDLIMKVENLALKNRFQA... | The TFIID basal transcription factor complex plays a major role in the initiation of RNA polymerase II (Pol II)-dependent transcription. TFIID recognizes and binds promoters with or without a TATA box via its subunit TBP, a TATA-box-binding protein, and promotes assembly of the pre-initiation complex (PIC). The TFIID c... | Q2HJG8 |
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