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
|
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Q9PRP7 | SL114_ECHCA | CA-1 25 kDa subunit chain 1 | Echis | DCLPDWFHYEGHCYRVFDEPKKWADAEKFC | Calcium-dependent prothrombin activator. This protein may activate prothrombin via recognition by the regulatory subunit of the calcium ion bound conformation of its gamma-carboxyglutamic acid (GLA) domain, and the subsequent conversion of prothrombin to active thrombin is catalyzed by the catalytic subunit. | Q9PRP7 |
Q49467 | GYRA_MYCGO | Mgo GyrA intein | Mycobacterium | FRPDRSHAKSARSVAETMGNYHPHGDASIYDTLVRMAQPWSLRYPLVDGQGNFGSPGNDPPAAMRYCLTGDALVRLPFGQSMRIGDVAPGARTNSDNAGELKVLDRHGDPVFADRLFHSGDHQTFRVQTAEGYEVTGTSNHPVLCLVNLAGVPTLLWMLIEEIRPDDYVVLQRAPPVESGPANWRDAMEALLLGAFISEGFMSESRAGFNNVDRDYFNAVVAAYDAVVGGKRYVAQRTIASGSVLNELDIHDVSALKGTRLGVLCGQRSADKSVPEWLWQSPAAVKRVFLQALFEGDGSCSALPRNTIQVSYSTRSRQLAIDVQQMLLEFGVISRRYRHAVGEYKVVITNRAQAELFATQIGFGGAKQSKLTRILGSLPPCAGMDTNHVPGLAAFIRSHCDSEWVDKEWLRKHNIDRLSRWRRDGAEILSRIANPDVRAIATDLTDGRFYYAQVTSVTEAGVQPVYSLRVDSEDHAFLTNGFVSHNTEARLTPLAMEMLREIDEETVDFIPNYDGRVQEPTVLPSRFPNLLANGSGGIAVGMATNIPPHN | A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner. | Q49467 |
A6T3N1 | TTCA_JANMA | tRNA 2-thiocytidine biosynthesis protein TtcA | Janthinobacterium | MSQALMNTAAATAETDAAMSFKQNEKIVYENNKLHKRLCRQVGQAIGDFNMIEDGDKVMVCLSGGKDSYALLDILMTLRERAPIKFDIVAVNLDQKQPNFPDHILPAYLKQLDIPFHIENQDTYSIVKRLIPEGKTTCSLCSRLRRGILYRVADELGANKIALGHHRDDIMETFFLNMFFGAKIKGMPPKLQSDDGKHIVIRPLAYVKEADTERYAEVKNFPIIPCDLCGSQENLQRKQIKGMLREWEKKFPGRVDNIFSSLSTVVPSHLMDKELFGFADLKATGEAMANGDIAFDEEPCSTGSTSIPGIIPLRADD | 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. | A6T3N1 |
Q8Y206 | MIAB_RALSO | tRNA-i(6)A37 methylthiotransferase | Ralstonia | MKKVFIKTFGCQMNEYDSDKMADVLNAAEGLVPTDTPEDADVILFNTCSVREKAQEKVFSDLGRVKALKARNPDLVVGVGGCVASQEGASIVARAPYVDVVFGPQTLHRLPELIDARRRTGRPQVDVSFPEIEKFDHLPPARVEGPSAFVSIMEGCSKYCSYCVVPYTRGEEVSRPFEDVLAEVAGLAEQGVREVTLLGQNVNAYIGKMGGTSERADFALLLEYVAEIPGIERIRYTTSHPKEFTARLIEAYATNRKLVDHLHLPVQHGSDRILMAMKRGYTVLEYKSIIRKLRAIRPDISIATDFIVGFPGETDADFAKTMDLVHEIGYDNSFSFIYSPRPGTPAANLHDDTPHAVKLERLKHLQATIDANMARISEGMVGSVQRILVEGPSRKDPSELHGRTENNRVVNFALPDLPQARRDQLVGQMLDVRIVHAYPHSLRGDVVEQRPDGVTQH | 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. | Q8Y206 |
Q1H4Q1 | EFTU1_METFK | Elongation factor Tu 1 | Methylobacillus | MAKGKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLTKKFGGEAKDYSQIDNAPEEKARGITINTSHVEYETETRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIIVFLNKADMVDDAELLELVEMEVRELLSKYDFPGDDTPIIKGSAKLALEGDQSDIGEPAIFRLAEALDTYIPTPERAVDGTFLMPVEDVFSISGRGTVVTGRVERGIVKVGDEIEIVGLKPTIKTTCTGVEMFRKLLDQGQAGDNVGVLLRGTKREEVERGQVLAKVGSIKPHTKFTAEIYVLGKDEGGRHTPFFNGYRPQFYFRTTDVTGAVELPAGTEMVMPGDNVSISVSLIAPIAMEEGLRFAIREGGRTVGAGVVAKIIE | This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. | Q1H4Q1 |
B2IG63 | PTH_BEII9 | Peptidyl-tRNA hydrolase | Beijerinckia | MLLFVGLGNPGKAYSANRHNIGFMAIDAIAREYGAPAFRARFQGLTSEITLSGEKIVLLKPETYMNESGRSVSDAVHFYKIDASRVIVFHDELDLAPGKVRVKKGGGNAGHNGLKSITQHITNDYRRVRIGIGHPGIKDMVRHYVLGDFSKTESAWVETLCLSIAVNAPLLAKGEDENFQNKIFHAMETAGLAKDGLF | The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis. | B2IG63 |
Q99M64 | P4K2A_RAT | Phosphatidylinositol 4-kinase type II-alpha | Rattus | MDETSPLVSPERAQPPEYTFPSVSGAHFPQVPGGAVRVAAAGSGPSPPCSPGHDRERQPLLDRARGAAAQGQTHTVAAQAQALAAQAAVAVHAVQTHRERNDFPEDPEFEVVVRQAEIAIECSIYPERIYQGSSGSYFVKDSQGRIIAVFKPKNEEPYGNLNPKWTKWLQKLCCPCCFGRDCLVLNQGYLSEAGASLVDQKLELNIVPRTKVVYLASETFNYSAIDRVKSRGKRLALEKVPKVGQRFNRIGLPPKVGSFQLFVEGYKDADYWLRRFEAEPLPENTNRQLLLQFERLVVLDYIIRNTDRGNDNWLIKYDYPMDNPNCRDTDWVMVREPVIKVAAIDNGLAFPLKHPDSWRAYPFYWAWLPQAKVPFSQEIKDLILPKISDPNFVKDLEEDLYELFKKDPGFDRGQFHKQIAVMRGQILNLTQALKDNKSPLHLVQMPPVIVETARSHQRSSSESYTQSFQSRKPFFSWW | Membrane-bound phosphatidylinositol-4 kinase (PI4-kinase) that catalyzes the phosphorylation of phosphatidylinositol (PI) to phosphatidylinositol 4-phosphate (PI4P), a lipid that plays important roles in endocytosis, Golgi function, protein sorting and membrane trafficking and is required for prolonged survival of neurons. Besides, phosphorylation of phosphatidylinositol (PI) to phosphatidylinositol 4-phosphate (PI4P) is the first committed step in the generation of phosphatidylinositol 4,5-bisphosphate (PIP2), a precursor of the second messenger inositol 1,4,5-trisphosphate (InsP3). | Q99M64 |
Q2S2A5 | HEM1_SALRD | Glutamyl-tRNA reductase | Salinibacter | MRFYAVGLNHECTSLEQTETFALSAEEQEALYANLSLSADAEVVVLSTCNRTEAYLYGTEADLRQVKALIGQGGGTRWPEETAFQERDEAAVRHLLQVTSGLRSVVLGERQIFAQVKAAYERAVDAGGIHSVMHRLFHTAFRAAKRVSSETGLGRGAASVSTAAVEMARQDLSEAGGEGLRNTEIVLVGAGKMGRLALEALADESLASLTVVNRSPDRAREVASPFGGDTEPWADRHRAVATADLALVATGASDPVLHAPALPAPDEATLVVDVAMPRNVDPAVDERPGYRLYDLDDLEAWTAEVRERRADAVPEAESICEELLEDFVTWVFHQQALQPAIQAIRSTFDTIREQEVDRHAHRTGMDREEVDRLTESIMQKLLAVPIVRLKNVDPESIDFVQGIELLHALFAPSDESDAGRSLAEAPDADTPDLGEAPSRCPYMTHDPGGDGTETEEVQKALRLSAAHQAASHSEEVRGG | Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA). | Q2S2A5 |
Q4L5D8 | COAD_STAHJ | Pantetheine-phosphate adenylyltransferase | Staphylococcus | MAKTKAVIPGSFDPITYGHIDIIERSAGRFDELHICVLKNSNKTGTFNIDERMALIEESVKHLSNVEVHNYNGLLVDFCDKIGAQTIIRGLRAVSDFEYELRLTSMNKKLNSNVETMYMMTSTNYSFISSSVVKEVAQYKADISDFVPPNVEKALKEKFKK | Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. | Q4L5D8 |
Q03K76 | HISZ_STRTD | ATP phosphoribosyltransferase regulatory subunit | Streptococcus | MKKTTLALGMHDKLFKRARTMYQIEHCICDLLMTKGFLRIETPTLEHFEVFSDVVDNGNYNFFDKNGDLISLRPDITSQIGRVIASTQVHTPIKFSYSGKVFNYNEEMRGLSNEHTQAGVEIIGFPVHQALEEAVISAKEALDVAGVRNYKFEFSHAQLLQLIFEELNLPAVKEAELATYIRDKSITGLKEFTKENPSQYDKVLEQLPSLFGETTAVLTEARQLTDNESFLTALDSLEVLTSRLADNLPETTLDLAQLPAVPYYTGIMFKVFGDKVPDAFVSGGRYDKLFERFGATELTAVGWAIDIDSVYQAVHDDVEFGGDMDD | Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine. | Q03K76 |
Q4JAC0 | CDPAS_SULAC | CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol synthase | Sulfolobus | MIGLLLGLIYYIPALVANGSAPFIKSGTPIDFKRKLNDGRRVLGDGKTFEGLLLSLTFGTTVGAIISRFLGIEWIIIGFVESLGAMLGDMLGAFIKRRIGLERGARAPILDQLDFILGATVVLISFNVNLNIYQVVFVCVLVIALHMFTNYVAYRLKIKSVPW | Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) and CTP. This reaction is the third ether-bond-formation step in the biosynthesis of archaeal membrane lipids. | Q4JAC0 |
Q9A5A7 | MURB_CAUVC | UDP-N-acetylmuramate dehydrogenase | Caulobacter | MTWKTQLPTARGKLLIDEALAPFTWFRVGGPADVVFLPADEQDLSDFLKGLDPSVPVMAIGVGSNLLVRDGGVDGVVIRLGKGFNGVEALGDNRIKAGSAVPDAILARKAAEAGIAGLEFYVGVPGTIGGAVIMNAGCYGAETVNVVKSVRVMNRAGVVRELSVEDLHYTYRHSALQDGEPVIVLDAIFEGTPDEPEAIKARMAEITARRETTQPIREKTGGSTFKNPPGHSSWKLVDEAGWRGKPYGGAMFSPLHSNFLINTGEATAADLEGLGEAVRADVLAKTGVQLDWEIKRIGRAG | Cell wall formation. | Q9A5A7 |
Q4L6J7 | XERD_STAHJ | Tyrosine recombinase XerD | Staphylococcus | METIIEEYLKFIQIEKGLSENTIGAYRRDLKKYQLYMQEQKIAHIDFIDRQTIQECLGSLIDQGASAKSIARFISTIRSFHQFALREKYAAKDPTVLIETPKYEKKLPDVLDVEEVIQLLETPDLTKNNGYRDRTILELLYATGMRVTELIQIEIDDVNLIMGFVKVFGKGNKERIIPLGDTVIEYLDTYINNVRSQLLKKTVTNVLFLNLHGRPLTRQGIWKLIKQYGLRANINKTLTPHTLRHSFATHLLENGADLRAVQEMLGHSDISTTQLYTHVSKTQIRQMYNQFHPRA | Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. The XerC-XerD complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids. | Q4L6J7 |
Q8TCV5 | WFDC5_HUMAN | p53-responsive gene 5 protein | Homo | MRTQSLLLLGALLAVGSQLPAVFGRKKGEKSGGCPPDDGPCLLSVPDQCVEDSQCPLTRKCCYRACFRQCVPRVSVKLGSCPEDQLRCLSPMNHLCHKDSDCSGKKRCCHSACGRDCRDPARGTAPGCPGQANSDLGSVALHLSWGPTERVHDGRPGALPAGQHYLYQRWFQPSDNHWPADTSLQPIHPWFLLLGVKVHSLSSEEGLCITPVLCTTAIRASHPS | Putative acid-stable proteinase inhibitor. | Q8TCV5 |
B4SGD1 | RISB_PELPB | 6,7-dimethyl-8-ribityllumazine synthase | Pelodictyon | MQVKQIEGVLNAKDIRFALVVGRFNDFIGQKLVEGAIDCICRHGGSEECIAMYRCPGAFELPMVAKKVALSGKYDAIITLGVIIRGSTPHFDVLAAEATKGIAQVALDTMVPIAFGVLTTENIEQAIERAGTKAGNKGFDAAMTAIEMVNLYRQI | Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin. | B4SGD1 |
P97527 | CNTN5_RAT | Neural recognition molecule NB-2 | Rattus | MASSWRLILFLSFTSCLSEYSEALSGLSTSYAALLRIKKSSTSSAFGSKSRPRYSSPSLGTLSVSPPSWRGAAQQYHSPVNLYHSPDAFRQDESVDYGPVFVQEPDDIIFPTDSDEKKVALNCEVRGNPSPTYRWLRNGTEIDLESDYRYSMIDGTFIINNPSESRDSGLYQCLATNTFGSILSREATLQFAYLGNFSGRTRSAVSVREGQGVVLMCSPPPHSPEIIYSWVFNEFPSFVAEDSRRFISQETGNLYISKVQTSDVGSYICLVKNAVTNARVLSPPTPLTLRNDGVMGEYEPKIEVHFPTTVTAAKGTTVKMECFALGNPVPTITWMKVNGYIPSKSRLRKSQAVLEIPNLQLDDAGIYECTAENSRGKNSFRGQLQIYTYPHWVQKLNDTQLDSGSPLQWECKATGKPRPTYRWLKNGAPLLPQSRVDTANGVLAIHSVNQSDAGMYQCLAENKYGAIYASAELKILASPPSFELNQVKKSIIVTKDREVLIECKPQGSPKPAISWRKGDKAVRGNKRIAILPDGSLRILNASKADEGKYICQGVNIFGSAEIIASVSVKEPTRIELTPKRTELTVGESIVLNCKAMHDSSLDVTFYWTLKGQPIDFEKEGGHFESIRAQASSADLMIRNILLMHAGRYGCRVQTTADSVSDEAELLVRGPPGPPGVVIVEEITESTATLSWSPATDNHSPISSYNLQARSPFSLGWQTVKTVPEVITGDMESAMAVDLNPWVEYEFRVVATNPIGTGDPSIPSRMIRTNEAVPKTAPSNVSGGSGRRHELVIAWEPVSEEFQNGEGFGYIVAFRPNGTRGWKEKMVTSSDASKFIYRDESVPPLTPFEVKVGVYNNKGDGPFSQIVVICSAEGEPTAAPTDVTATSVSVSEIFVVWKHVKESLGRPQGFEIGYWKDTEPEDSAETVRTRGNESFVMLTGLEGDTLYHLTVRAYNGAGYGPPSREVSATTKRHPPSEPPGNLRWEQQGSQVSLGWEPVRPLANESEVMGYKVFYRQEGHSKGQVIETQKPQAVVPLPEAGVYIIEVRAYSEGGDGTASSQIRVPSYAGGKITSAQSTLHSLSKWSSVTLLLALMLPSSSW | Contactins mediate cell surface interactions during nervous system development. Has some neurite outgrowth-promoting activity in the cerebral cortical neurons but not in hippocampal neurons. Probably involved in neuronal activity in the auditory system. | P97527 |
B9DHG0 | PYG7_ARATH | Protein PALE YELLOW GREEN 7 | Arabidopsis | MFESNMVLQTLSSSSPPIHRLYLHHSQILPSSGSPSKISLQIHGRTLAIRSFHDYVFAEISARGLPALNKASLKKLPIKGSTFLLGQSLLMVSAHPQLAAAAEIIKPEPIYEVGELFELSIQLSYLLLLLGLLGVGTFYVIRQVLVRRELDLSAKELQEQVRSGDASATELFELGAVMLRRKFYPAANKFLQQAIQKWDGDDQDLAQVYNALGVSYVREDKLDKGIAQFEMAVKLQPGYVTAWNNLGDAYEKKKELPLALNAFEEVLLFDPNNKVARPRRDALKDRVKLYKGVVAVKSKKR | Nuclear genome-encoded factor required for the accumulation of photosystem I (PSI). Functions as PSI biogenesis factor . Cooperates with PSA3 to promote the stable assembly of PSI in the thylakoid membrane. May target primarily the PsaC subunit . | B9DHG0 |
B0TZI5 | GLGB_FRAP2 | Glycogen branching enzyme | Francisella | MKNVNSKQNNHSTIGEQDIHFFHEGKHIYAYEFMGAHKASEDGIDGIRFTTWAPNAKSICVIGDFNHWQVEDKNHMKRITDAGLWSVFIADVKDGDKYKFVVTNKDTNHYVYKSDPYAFFSELRPNTASVISTQTTYKWHDEKWLKKRATADYYNSPMNTYELHLASWKTKDDRFMTYEEIAEVLPKYVKDMGYTHVEFMPLHEHPLDASWGYQPTGFYSINSRHGDLVGLKHLVDKLHTHDIGVILDWVPGHFCKDQHGLINFDGSACYEYQEPTKAINKGWGTHNFDLGRNEVKCFLISNAMYWINEFHIDGLRVDAVSNILYLNYDREDGQWVPNIHGGHENLEGIAFLRELNGVLKHTCKGVITIAEESSSWPNISTPVEQGGLGFDFKWNMGWMNDTLRYISLDPVYRKYHHNLITFSMVYHYSEKFILSISHDEVVHGKKSLINKMWGDLWNKYAGLRLYMSFMIGHPGKKLIFMGSEFGQFIEWREYEQLQWQVVDEYHTHRETLNFFKKLNEFYKAETALWECDYDHKGFQWIDANNSEQSILSFVRSNKDGKEKLIFVCNFTPVTYYDYHIGVPDAGSYIEAFNSDDLEFGGSGQLIADEIFSTPESSHGFDQRITIKVPPMATLVLKLKK | Catalyzes the formation of the alpha-1,6-glucosidic linkages in glycogen by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position. | B0TZI5 |
Q6P9X9 | PARM1_RAT | Prostatic androgen-repressed message 1 protein | Rattus | MVCKALITLCIFAAGLRVQGSPTPTLLPVSLTTKSTAPMATWTTSAQHTAMATTPVASATHNASVLRTTAASLTSQLPTHPREEAVTSPPLKREVNSTDSSPTGFSSNSSGIHLAPTPEEHSLGSPETSVPATGSQSPTLLFSQGPTSASTSPATSPSEPLSASVTSNHSSTVNNIQPTGAPMAPASPTEEHSSSHTPTSHVTEPVPKEKSPQDTEPGKVICESETTTPFLIMQEVENALSSGSIAAITVTVIAVVLLVFGAAAYLKIRHSSYGRLLDDHDYGSWGNYNNPLYDDS | May regulate TLP1 expression and telomerase activity, thus enabling certain prostatic cells to resist apoptosis. | Q6P9X9 |
B0B960 | MURB_CHLT2 | UDP-N-acetylmuramate dehydrogenase | Chlamydia | MTDSFPFSVQESVPLSRFSTFRIGGPARYFKELTSLSEALTVFSYLHTHPLPYIIIGKGSNCLFDDQGFDGLVLYNNIQGQEFLSDTQIKVLSGSSFALLGKRLSSQGFSGLEFAVGIPGTVGGAVFMNAGTTLANTASSLINVEIIDHSGILLSIPREKLLFSYRTSPFQKKPAFIASATFQLTKDPQAAKRAKALIEERILKQPYEYPSAGCIFRNPEGLSAGALIDRAGLKGLKIGGGQISEKHGNFIINTGNACTADILELIEIIQKTLKKQGISLHKEVRIIPFRL | Cell wall formation. | B0B960 |
Q8T295 | PRP8_DICDI | Splicing factor Prp8 | Dictyostelium | MDDTNSNINQSNESQHLEEKAKKWIQLNNKKYSEKRKFGAVEIRKEDMPPEHLRKIIKDHGDMSNRRFRDDKRVYLGALKYMPHAILKLLENIPMPWEQVKYVKVLYHLSGAITFVNEIPFVIEPIYIAQWATMWVTMRREKRDRTHFRRMKFPLFDDEEPPLDYSDNILDNEVEDPIQMELDENDDSEVIDWLYDSKPLVNTKFVNGSSYRKWRLNLPIMSTLFRLASPLLSDLTDSNYFYLFDDNSFFTSKALNMAIPGGPKFEPLFRDVDDDDEDWNEFNDINKVIIRNKIRTEYKIAFPYLYNSRPRKVKTPTYHTPNNCYIKNDSPDLPGFYFGAALNPIPSYKTSGNKNEQSEYGTEDDEFQLPEEIETILSKTEIEHDNLANGIQLYWAPRPFSLRSGTTRRAEDIPLVKSWYKEHCPSEHPVKVRVSYQKLLKCHVLNKLHHRKPKAQTKRNLFKSLKATKFFQSTEIDWVEAGLQVCRQGYNMLNLLIHRKNLNYLHLDYNFYLKPIKTLTTKERKKSRFGNAFHLCREILRLTKLVVDVHVKFRLGDADAFQLADAIQYLFSHLGLLTGMYKYKYRLMRQIRMCKDLKHLIYYRFNTGAVGKGPGCGFWAPMWRVWLFFLRGIVPLLERWLGNLLARQFEGRQTKGMAKTVTKQRVESHFDYELRAAVMHDILDMMPEGIKANKSRIILQHLSEAWRCWKSNIPWKVPGLPIPIENMILRYVKSKADWWTNIAHYNRERIKRGATIDKTASKKNLGRLTRLWLKAEQERQHNYLKDGPYVSAEEAVAIYTTTVHWLEKRRFSAIPFPQTSYKHDIKILTLALERLKEAYSVKSRLNQSQREELSLVEQAYDNPHDALARIKRHLLTQRTFKEVGIEFMDMYTHLVPIYDVDPFEKITDAYLDQYLWYEADKRQLFPNWVKPSDNEPPPVLIHKWCQGINNLDQVWETSQGECVVLLETQFSKVYEKMDLTLMNRLLRLIVDQNIADYMSGKNNVVINYKDMNHTNSYGLIRGLQFASFIFQYYGLVLDLLVLGLERASALAGPPNLPNSFLTFPSVQTETAHPIRLYSRYVDRIHVLYKFTADEARKLIQKYMSEHPDPNNENVVGYNNKKCWPRDCRMRLMKHDVNLGRAVFWQIKNRLPRSLTTIDWEDSFVSVYSKDNPNLLMNMAGFDIRILPKCRTPLDQLAPKDAVWSLQNVNTKERTAQAFLRVDTESQERFENRIRMILMASGSTTFTKIVNKWNTALIGLMTYYREAVVTTREMLDILVRCENKIQTRVKIGLNSKMPNRFPPVVFYTPKELGGLGMLSMGHVLIPQSDLKYSKQTDTGITHFTSGMSHDEDQLIPNLYRYIQPWEQEIKDSQRVWAEYAIKYEEAKSQNKNLTLEDLEDSWDRGIPRINTLFQKSRHTLAYDKGWRVRTDWKQYQVLKNNPFWWTNQRHDGKLWNLNNYRTDIIQALGGVEGILEHTLFKGTYFPTWEGLFWEKASGFEESMKYKKLTHAQRSGLNQIPNRRFTLWWSPTINRKNVYVGFQVQLDLTGIFMHGKIPTLKISLIQIFRAHLWQKIHESLVMDLCQVFDQELDNLEISVVNKEAIHPRKSYKMNSSCADILLRATHKWQVSRPSLLNDNRDTYDNTTTQYWLDVQLKWGDFDSHDIERYSRAKFLDYTTDSMSLYPSPTGCLIGLDLAYNIYSSFGNWFLGVKPLVQKAMAKILKSNPALYVLRERIRKGLQLYSSEPTEPYLSSQNFGELFSNKIMWFVDDSNVYRVTIHKTFEGNLTTKPINGAIFIFNPRTGQLFLKIIHTDVWLGQKRLGQLAKWKTAEEVAALIRSLPVEEQPKQIIATRKGMMDPLEVHLLDFPNIVIQGSELQLPFQACLKVEKFGDLILKATEPKMVLFNIYDDWLSTIHSYTAFLRLILILRALHVNLERTKIILKPNKNVITQPHHIWPTLTEQEWLTVEGSLKDLILADFGKRNNVNVASLTQSEIRDIILGMEISAPSQQREDQIAEIEKQKTEASHLTAVTVRSTNIHGEEIITTATSPHEQKVFSSKTDWRVRAISATNLHLRTNQIYVNSDNAKETGGFTYVFPKNILKKFITIADLRTQIMGYCYGISPPDNPSVKEIRCIVMPPQWGTPVHVTVPNQLPEHEYLKDLEPLGWIHTQPTELPQLSPQDVITHSKIMSDNKSWDGEKTVIISVSVAWPCTLTAYHLTPSGFEWGKNNKDSLNYQGYQPQFYEKVQMLLSDRFLGFYMVPDRGSWNYNFMGVKHSTNMTYGLKLDYPKNFYDESHRPAHFQNWTQMAPSANDDEENQPENENLFE | Functions as a scaffold that mediates the ordered assembly of spliceosomal proteins and snRNAs. Required for the assembly of the U4/U6-U5 tri-snRNP complex. Functions as scaffold that positions spliceosomal U2, U5 and U6 snRNAs at splice sites on pre-mRNA substrates, so that splicing can occur. Interacts with both the 5' and the 3' splice site. | Q8T295 |
P36630 | CG22_SCHPO | G2/mitotic-specific cyclin cig2 | Schizosaccharomyces | MALYSISKPVGSKINKHSYQDENTLVGKQALSKGTEKTKLSTNFEINLPRRTVLSDVSNVGKNNADEKDTKKAKRSFDESNLSTNEEADKPVESKFVKKLKVYSKNADPSVETLQKDRVSNVDDHLSSNPLMAEEYAPEIFEYIRKLDLKCLPNPKYMDQQKELTWKMREILNEWLVEIHSNFCLMPETLYLAVNIIDRFLSRRSCSLSKFQLTGITALLIASKYEEVMCPSIQNFVYMTDGAFTVEDVCVAERYMLNVLNFDLSYPSPLNFLRKISQAEGYDAQTRTLGKYLTEIYLFDHDLLRYPMSKIAAAAMYLSRRLLRRGPWTPKLVESSGGYEEHELKEIAYIMLHYHNKPLEHKAFFQKYSSKRFLKASIFVHQLVRQRYSVNRTDDDDLQSEPSSSLTNDGH | Essential for the control of the cell cycle at the G2/M and G1/S (mitosis) transition. Interacts with the cdc2 protein kinase to form MPF. Interaction with res2 promotes the phosphorylation of res1 and inhibits MBF-dependent gene transcription. Forms an autoregulating feedback-inhibition loop with MBF which is important for normal regulation of the cell cycle. G2/M cyclins accumulate steadily during G2 and are abruptly destroyed at mitosis. Negatively regulates conjugation via interacting with cell cycle 'start' genes. Degraded by skp1, pop1 and pop2 in the G2 and M phases of the cell cycle. | P36630 |
Q3B6L9 | IF3_CHLL3 | Translation initiation factor IF-3 | Pelodictyon | MKKQKATSQKPKITYRVNEQIRVPEVRIIFPDGTQQVMKTIDARRMAEDRNTDLIEVQPNAEPPVCKFDNLGKLLYKMAQRDKDLKKKQKTTTLKELRFHPNTDKHDFDFKTAHLEEFLRKGNRVRATIVFLGRSIIYKDKGLELADRLTERLSVVGNREGEPKFEGKKLFVYFEPDKKKIDAYERIRSKTGTPLAPLEESADAED | IF-3 binds to the 30S ribosomal subunit and shifts the equilibrum between 70S ribosomes and their 50S and 30S subunits in favor of the free subunits, thus enhancing the availability of 30S subunits on which protein synthesis initiation begins. | Q3B6L9 |
A8FZE2 | MIAA2_SHESH | Isopentenyl-diphosphate:tRNA isopentenyltransferase 2 | Shewanella | MKNFNLILVIGATASGKTRLGVELARQLEGEIISADSRQVYKGLDIGSGKDLAEYGEVPHHLIDIVEPGHEYNAFQFQQDFFEAFTYIESRNKQPILVGGTGLYVDAVVSGYEFVQLDKDLALRAELDLQPLEQVQKLLLELDAAQYEKTDLTVRPRLYRAIEIAKNKQTNPKPAKALPEIRPLYFGIQWDRKVLRKRIKTRLKERFEQGMVEEVQGLLDNGVSHEQLEYYGLEYRFVSQYIAGQIGYEEMFDRLNTAICQYAKRQETWFRRIEKHGGKIHWLQGSGDIYQQACEVLADLG | Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A). | A8FZE2 |
Q6KI50 | RL22_MYCMO | 50S ribosomal protein L22 | Mesomycoplasma | MESRATVKVQRISARKARLVADLIRYKSANDALSILYNTNKKASALFIKLLNSAVANAINNHGMNNEKLVVEKVLVNEGPTLKRFQPRSQGRAYSIFKRTSHLEIVLKEK | The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome. | Q6KI50 |
A6LMK5 | PANB_THEM4 | Ketopantoate hydroxymethyltransferase | Thermosipho | MTIQKFLAMKGKEKIVMVTAYDTPTAKIAEEAGVDIILIGDSIGNNVLGYDSTIPVTMEEIIIHLKAVRRGAPNSFIVADMPFLSYGHSIEEAVKNAGILIKNGANAVKIEGGKFHCNLIEKCINIGIPVMGHLGFTPQSINIFGGYKVQGKKEDSKKTILESAIALEQCGVFSIVLEMVTEELAKEITEKISIPTIGIGAGRYCDGQVLVFHDIVGLNPNFKPKFSKQYANTYSIMLNALKEFKKDVKEKNFPKERHTFKGGK | Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate. | A6LMK5 |
A3MRW0 | RS3_BURM7 | 30S ribosomal protein S3 | pseudomallei group | MGQKIHPTGFRLAVSRNWASRWYANNNNFAAMLQEDIGVREYLKKKLKNASVGRVVIERPAKNARITIFSSRPGVVIGKKGEDIELLKTELQRRMGVPVHVNIEEIRKPETDAQLIADSITQQLERRIMFRRAMKRAMQNAMRLGAQGIKIMSAGRLNGIEIARTEWYREGRVPLHTLRADIDYATSEAKTTYGIIGVKVWVYKGDTLGRNDAPVVEEVTEDKRPRRNARPGDRRPRRDGEGGAPGARRGGPRRGAGKPEDGKTGE | Binds the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation. | A3MRW0 |
Q06FK6 | PSAJ_PELHO | PSI-J | Pelargonium | MRDLKTYLSAAPVLSTIWFGALAGLLIEINRFFPDALTFPFFSF | May help in the organization of the PsaE and PsaF subunits. | Q06FK6 |
P27683 | RK24_SPIOL | Chloroplastic large ribosomal subunit protein uL24c | Spinacia | MAAMAALQSSFTSLSLSSNSFLGQRLFPSPTTLQVKTEGHSPCLIVMRIKRWERKDCKPNSLPKLHKMHVKVGDTVKVISGGEKGKIGEISKIHKHNSTVIIKDLNLKTKHVKSKEEGEQGQIIKIEAAIHSSNVMLYSKEQEVASRVGHKILEDGRKVRYLIKTGEIVDTPDRWKEIQNKKESETAVAVAA | Component of the chloroplast ribosome (chloro-ribosome), a dedicated translation machinery responsible for the synthesis of chloroplast genome-encoded proteins, including proteins of the transcription and translation machinery and components of the photosynthetic apparatus. | P27683 |
P0AE58 | CAIF_ECOLI | Transcriptional activatory protein CaiF | Escherichia | MCEGYVEKPLYLLIAEWMMAENRWVIAREISIHFDIEHSKAVNTLTYILSEVTEISCEVKMIPNKLEGRGCQCQRLVKVVDIDEQIYARLRNNSREKLVGVRKTPRIPAVPLTELNREQKWQMMLSKSMRR | Potential transcriptional activator of carnitine metabolism. | P0AE58 |
Q9H8T0 | AKTIP_HUMAN | Fused toes protein homolog | Homo | MNPFWSMSTSSVRKRSEGEEKTLTGDVKTSPPRTAPKKQLPSIPKNALPITKPTSPAPAAQSTNGTHASYGPFYLEYSLLAEFTLVVKQKLPGVYVQPSYRSALMWFGVIFIRHGLYQDGVFKFTVYIPDNYPDGDCPRLVFDIPVFHPLVDPTSGELDVKRAFAKWRRNHNHIWQVLMYARRVFYKIDTASPLNPEAAVLYEKDIQLFKSKVVDSVKVCTARLFDQPKIEDPYAISFSPWNPSVHDEAREKMLTQKKPEEQHNKSVHVAGLSWVKPGSVQPFSKEEKTVAT | Component of the FTS/Hook/FHIP complex (FHF complex) . The FHF complex may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting complex (the HOPS complex). Regulates apoptosis by enhancing phosphorylation and activation of AKT1. Increases release of TNFSF6 via the AKT1/GSK3B/NFATC1 signaling cascade. FHF complex promotes the distribution of AP-4 complex to the perinuclear area of the cell . | Q9H8T0 |
A5USH9 | RL14_ROSS1 | 50S ribosomal protein L14 | Roseiflexus | MVQQETRLRVADNTGAKEILCIRVLGGSRVRYGRVGDVIVASVKEATPGGAVKKGEVVRAVIVRTAKEYGRPDGSHIRFDDNAAVIIGKDNNPRGTRIFGPVARELRERAFMKIISLAPEVL | Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome. | A5USH9 |
Q31I42 | DDL_HYDCU | D-alanylalanine synthetase | Hydrogenovibrio | MTQSSNQTKDRVQRLGKVAVLMGGVAAERDVSLRSGAEVLKALKSEGVDAVGCDVTSVAQLVEIAQKYDRAFIALHGRWGEDGGVQAVLDSLALPYTGSGMTASALAMDKLRTKWLWKGVGLPTPAFIVVSPSRPLDVETFDLTFPVIVKPSHEGSSIGMRKVDTLDALQEAVDFAQQYDSEILIEQWITGREFTCAVLDGEALPMIQLKTDHDFYDFDAKYQSNTTEYLCPCGLEIAEEKRIQALVLQAFDAVGARHWGRVDLMLDDQNQPWLIEINTVPGMTDHSLVPMAAKAVDLSFSKLVLKLISLTLP | Cell wall formation. | Q31I42 |
A6Q908 | AROB_SULNB | 3-dehydroquinate synthase | unclassified Sulfurovum | MIVPIELAHTKNITYDITIDALPQLTFDTKVAVVTNPTVAGYHLQTLLAHIKAPQLEVITVPDGEEYKTLETVETILNELFEHKFDRKSLLIAFGGGVIGDMTGFTASLYQRGIDFIQIPTTLLSQVDASVGGKTGVNNRYGKNLIGAFYQPKAVYIDPAFLKTLPSREFSAGVAEIIKMAVMFDKDYFEFLVTADLSDEEVLKETIRRSVELKAWVVNQDEKEAGIRAVLNYGHTFGHVVENETGYTTYLHGEAVAIGMVMANALAVELGLLGETEADRIKALLEKASLPTHYTIKDVDDFYEHFFLDKKSANNSIKFILPEGIGGHKIVSDIDESVVKNVLKKFEEEV | Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ). | A6Q908 |
Q7GBC8 | URM1_ORYSI | Ubiquitin-related modifier 1 homolog | Oryza sativa | MHLTLEFGGGLELLLEKSTKVHKVDLQPNDGDGKVVMKGLLAWVKSNLIKERPEMFLKGDSVRPGVLVLINDCDWELCGGLDAELEEKDVVVFISTLHGG | Acts as a sulfur carrier required for 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Serves as sulfur donor in tRNA 2-thiolation reaction by being thiocarboxylated (-COSH) at its C-terminus by MOCS3. The sulfur is then transferred to tRNA to form 2-thiolation of mcm(5)S(2)U. Also acts as a ubiquitin-like protein (UBL) that is covalently conjugated via an isopeptide bond to lysine residues of target proteins. The thiocarboxylated form serves as substrate for conjugation and oxidative stress specifically induces the formation of UBL-protein conjugates. | Q7GBC8 |
Q1QP86 | GLMM_NITHX | Phosphoglucosamine mutase | Nitrobacter | MSRKYFGTDGIRGRANGLITPELAMKVGQAAGLVFQRGEYRHRVVIGKDTRLSGYMIEYALVAGFTSVGMDVLLLGPMPTPAVAMLTKSMRADLGVMISASHNLFEDNGIKMFGPRGFKLSDAVEKQIEQLLDENLDKKLAQSTGLGRARRIDGVHDRYIEFAKRTLPRELSLDGLRVVVDCANGAAYRVVPEALWELGADVVPISVEPDGFNINKECGSTAPEALCRKVREMRADIGIALDGDADRVIIVDERGHVVDGDQLLAVIAESWKEDGRLTKPGIVATVMSNLGLERFLEGQELSLVRTPVGDRYVLEQMLKQGYNLGGEQSGHIILSDYATTGDGFVSALQVLAVVQKLGRPVSEVCHKFEPLPQILKNYRYRSGKPLDRAEVKSAITAGEKRLNGHGRLLVRSSGTEPVIRVMGEGDDRILVEDVVDTIVSALGGPAAA | Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate. | Q1QP86 |
B7MRB3 | RPOB_ECO81 | Transcriptase subunit beta | Escherichia | MVYSYTEKKRIRKDFGKRPQVLDVPYLLSIQLDSFQKFIEQDPEGQYGLEAAFRSVFPIQSYSGNSELQYVSYRLGEPVFDVQECQIRGVTYSAPLRVKLRLVIYEREAPEGTVKDIKEQEVYMGEIPLMTDNGTFVINGTERVIVSQLHRSPGVFFDSDKGKTHSSGKVLYNARIIPYRGSWLDFEFDPKDNLFVRIDRRRKLPATIILRALNYTTEQILDLFFEKVIFEIRDNKLQMELVPERLRGETASFDIEANGKVYVEKGRRITARHIRQLEKDDVKLIEVSVEYIAGKVVAKDYIDESTGELICAANMELSLDLLAKLSQSGHKRIETLFTNDLDHGPYISETLRVDPTNDRLSALVEIYRMMRPGEPPTREAAESLFENLFFSEDRYDLSAVGRMKFNRSLLREEIEGSGILSKDDIIDVMKKLIDIRNGKGEVDDIDHLGNRRIRSVGEMAENQFRVGLVRVERAVKERLSLGDLDTLMPQDMINAKPISAAVKEFFGSSQLSQFMDQNNPLSEITHKRRISALGPGGLTRERAGFEVRDVHPTHYGRVCPIETPEGPNIGLINSLSVYAQTNEYGFLETPYRKVTDGVVTDEIHYLSAIEEGNYVIAQANSNLDEEGHFVEDLVTCRSKGESSLFSRDQVDYMDVSTQQVVSVGASLIPFLEHDDANRALMGANMQRQAVPTLRADKPLVGTGMERAVAVDSGVTAVAKRGGVVQYVDASRIVIKVNEDEMYPGEAGIDIYNLTKYTRSNQNTCINQMPCVSLGEPVERGDVLADGPSTDLGELALGQNMRVAFMPWNGYNFEDSILVSERVVQEDRFTTIHIQELACVSRDTKLGPEEITADIPNVGEAALSKLDESGIVYIGAEVTGGDILVGKVTPKGETQLTPEEKLLRAIFGEKASDVKDSSLRVPNGVSGTVIDVQVFTRDGVEKDKRALEIEEMQLKQAKKDLSEELQILEAGLFSRIRAVLVAGGVEAEKLDKLPRDRWLELGLTDEEKQNQLEQLAEQYDELKHEFEKKLEAKRRKITQGDDLAPGVLKIVKVYLAVKRRIQPGDKMAGRHGNKGVISKINPIEDMPYDENGTPVDIVLNPLGVPSRMNIGQILETHLGMAAKGIGDKINAMLKQQQEVAKLREFIQRAYDLGADVRQKVDLSTFSDEEVMRLAENLRKGMPIATPVFDGAKEAEIKELLKLGDLPTSGQIRLYDGRTGEQFERPVTVGYMYMLKLNHLVDDKMHARSTGSYSLVTQQPLGGKAQFGGQRFGEMEVWALEAYGAAYTLQEMLTVKSDDVNGRTKMYKNIVDGNHQMEPGMPESFNVLLKEIRSLGINIELEDE | DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | B7MRB3 |
A5EG97 | CCME_BRASB | Heme chaperone CcmE | unclassified Bradyrhizobium | MTRKQRRLTIIGGALFVLAVAAGLVLNALRDSIVFFSTPTMVAEKHIGPGKRFRLGGLVQPGSLKRGDDLAVTFEVADGGAKLPVAYKGILPDLFREGQGVVAEGALDAAGVFKADTVLAKHDETYMPKEVADTLKKQGHWKDDYGKPQAAKPGPVSMREGEKTAAGATQ | Heme chaperone required for the biogenesis of c-type cytochromes. Transiently binds heme delivered by CcmC and transfers the heme to apo-cytochromes in a process facilitated by CcmF and CcmH. | A5EG97 |
Q72SX8 | ATPE_LEPIC | F-ATPase epsilon subunit | Leptospira | MSANKLKVSVISPEKILYKGEVDSLIVPGSEGFFGILPNHAPLVATLGIGILEIRKGEKLKVLSVEGGFVEIKDNSISILTDHGALKEDIDLEVEKKNLAEAEKLPPSDSKNLFLQKTKTRILVASR | Produces ATP from ADP in the presence of a proton gradient across the membrane. | Q72SX8 |
Q8ST83 | PHO_DROME | Transcription factor YY1 homolog | Sophophora | MAYERFGIILQSEQYDEDIGNTKVNQKMNEGNHYDLHRKNAFDRIIHSESKKGDNVINYNIHENDKIKAADNIFSSKLKMNPNMSYEMNINCFKNIGYGENQETSKVLTNSLSNNDINTEESGVVDKNSPFLTLGTTILNSNGKSRRWEQKLVHIKTMEGEFSVTMWASGISDDEYSGSDQIVGASDLLKGKEEFGIDGFTSQQNKEYQKMESKFTNAQTLEMPHPISSVQIMDHLIKERGNLSQENNISERILSKTTLSFEEPILLPDSSSIELVNETAAMTINNHRTLSNHTGNTGDLHALPSSVPFRIGLHEGQVNDCLSTISQSTHQDNTDSTGCGEMNLSEVTVSYTNDKKIACPHKGCNKHFRDSSAMRKHLHTHGPRVHVCAECGKAFVESSKLKRHQLVHTGEKPFQCTFEGCGKRFSLDFNLRTHVRIHTGDRPFVCPFDACNKKFAQSTNLKSHILTHAKAKRNTSISGKSGCSNAESNSQSEDTSANYVKVELQDSVTENHVPFVVYAD | Proposed core component of the chromatin remodeling Ino80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair. | Q8ST83 |
Q7U9F0 | AROC_PARMW | 5-enolpyruvylshikimate-3-phosphate phospholyase | Parasynechococcus marenigrum | MGSSFGDLFRISTFGESHGGGVGVIVEGCPPRLDLDVDAIQAELDRRRPGQSHITTPRKEADQVEVLSGLLDGQTTLGTPIAMLVRNKDQRPGDYKDMAVAFRPSHADATYQVKYGVQARSGGGRASARETIGRVAAGAIAKQLLAKAAGTEVLAWVKRIHTIEANVDPQAVTLDAIESNIVRCPDASTAAQMVERIEAIGRDGDSCGGVIECVVRNPAPGLGMPVFDKLEADLAKAVMSLPATKGFEIGSGFSGTLLKGSEHNDAFVPTDDGRLQTATNNSGGIQGGISNGEPIVIRVAFKPTATIRKEQQTIDSDGKATTLAGKGRHDPCVLPRAVPMVEAMVALVLADHLLRQQGQCSLW | 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 second double bond into the aromatic ring system. | Q7U9F0 |
A4XA62 | SYE_SALTO | Glutamyl-tRNA synthetase | Salinispora | MRFAPSPTGMFHVGGARSALQNWIFAKQQGGVFVLRVEDTDAARNKPEWTEGILAALEWIGIARGSYEGPYFQSSYATEHRAAASRLHEGGRAYYCDCTREVVQARTGSPHTGYDGFCRDRNLGPGAGRALRFRTPDEGATVVVDLIRGEPTFDNRLIEDFVIARSDGSPVFLLANVVDDMTMGITHVIRAEEHLPNTPKQQLLWDALGVKPPVWAHVPVVVNEKRQKLSKRRDKVALEAYRDEGYLADAMCNYLMLLGWAPSGDREIVPWPVIEEEFRLEEVNPSSAFFDEKKLRAFNGEYIRALPIAEFIAGCQPWLTGTATIAPPPWQPDEFDAEAFAAVAPLAQTRIAVLSEIVPNVDFLFLDSPLIDEGAWAKAMKEGAGDLLDAVIAAFTALPSWDADSTKSTLEAVGAEHGLKLGKAQAPVRVAVTGRRVGLPLFESLEVLGRERTLTRLRAARLRLP | 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). | A4XA62 |
P52195 | CMA1_PAPHA | Mast cell chymase | Papio | MLLLPLPLLLLFLCSRAEAGEIIGGTECKPHSRPYMAYLEIVTSNGPSKSCGGFLIRRNFVLTAAHCAGRSITVTLGAHNITEKEDTWQELEVIKQFRHPKYNTSTLHHDIMLLKLKEKASLTLAVGTLPFPSQFNFVPPGRMCRVAGWGRTGVLKPGSDTLQEVKLRLMDPQACSHFRYFDHNLQLCVGNPRKTKSAFKGDSGGPLLCAGVAQGIVSYGRLDAKPPAVFTRISHYRPWINKILQAN | Major secreted protease of mast cells with suspected roles in vasoactive peptide generation, extracellular matrix degradation, and regulation of gland secretion. | P52195 |
J4UHQ6 | OPS1_BEAB2 | Oosporein synthase | Beauveria | MPSFFPVFSGLGSGSVFSEENVGRAEENALSPECAVLLQSCHRTFREQVSDAIARNILPEDSIDLDDFAEPASLIRPLSKYSRNVVMQHAALYLHQILAYMTSQKELGNLIGSAGFCTGLLPAAVAAASQTSVITLISQSHHFFQVALWIGIRSEQYRVDHLTNDTQDADGESMLPCSYVLEGVSEAAAQDLLHKTNMGNEVFVSAILSPTRVTISGIPTKLSTFISKHLPANCRTTVAVVHSLYHHESLLEVRNLVMADLERQDTLLQARVELSAPILSTKTGKPLALSSVTTLEQVACAILDLIFIEKVDWLNLQQSIVSHTSQDALDRPINIVNYGPGLGMAPSAFAQAQEKDVCIMDAAKISKGSFQNSGASRLAWDDIAIVGMAVELPGASDADTLWQNLVDGYQACSEIPPSRFNVNDYNNGKGSRTLNTKYGNFLENPFLFDAEHFGISRREAKSMDPQQRILLQTAYRALEDAGYVPDTTTSSARDTFGCWIGNATLDYVDNLRSDIDVYYSTGTLRAFLSARISYVFGWSGPSITLDTACSSSIVALHQAARSILAGDCRSALVGAANTITSPDMYLGLDRAHFLSPSGQCKAFDASADGYCRAEGCGVFVIKRLSDALAEGDRIHGVIKAIEINQSGNTHSITHPHVPTQEALFDKMFRESRINPHEISVVEMHGTGTQAGDPNEVESVRRALCKARSPLNPVYLTSLKANIGHAEAVSGIAGLAKLILMTRNGYIPPQVSLKTLNPRIRPLGVDGAAIDANGTEWPRAGPKKARMSMLNNFGAGGSNAAVIIGEHLSQDESEAQQPACGATIFVCGVSAKNDRALVKLQETVADYLTSAGQSRKPPSLADVCATLTSRRQMYNHRVAVVASSLEELAENLRSASSHNVSKSICEAPEAVFIFSGQGSQYLGMGRELIEQYEDFAHTVNVCDGWLVKNNYPSCLAVITGEQRESEDDKVDAHTWQSFQSAIYVIEVALAKLLESWGIRPQAVAGHSLGEYAALVTAGVIRLMDGLKLVAHRAKLMMEQCDLGQTSMLAVNCSAAVITSIIEASTDFEGLAISCNNSETDCVVGGPVPQLVLLKKHLTDRAQVRSKLLDVPMAFHTAAMDPILEEFTAFAAREVRVFPPTLPVVSNVLGRTVAVGEQAFSPEYFAKQCRGTVAFDDGIKHFLALGDCESTPYRWIEIGPHPSVQPMLRGRLGKAATSHIQLTTLKKNVPPASTLSQLLSHFYQTSSGVNWRSVFSRNAHRRFKLIQLPGMPFFPSEFHVPYREMAGEPASTSQSSGDAASNVVPNSFAVHAIQKLSHGASNSCAIYETPAVLLKEFIEGHLVCGYALCPASVYHEMVLAALNDCQSAAGSSVVWGLSKVSYCAPMVYDGNSNQVLRVVITPRLTLPDRYDFAVMSYVAGTDPNERSTVHCRGVVKQSNMASAELKYSRLQASMKGSMDGLKHVGQLGAPAASCVQVFSKRAMYEKIFTRVVEYSDPYQKVETIRIREDTGEALATCVSPAPYLARDSSIPASHAIFMDVLLHVAGFVSNLNLPNDVMGICKEVGGATTLRAPVVRDGACAPFDVYCSTFDTQDSDGRSFTISNAYAVDSSGVMAVFKGMVFQHVKIPLIEQALKRATRSSPNAAVSASHPAQPKRRNDVTSFVNAQSVERMALPRAAAPVRAAPEVSVPELVAKVCGLDAGQLGVDSRLDAHGVDSLMGIEIAAALSSALGVDVLPDTLGSCDTVGDIERLCEALSPTPVGNDVDNDSPTPGSERGSDSAISTPASVSTVDASSIDMVQIVAELCGARAEAVSPDSELRALGVDSLMFLELADRLQDLDRGIALSSNDLADCQTIGDIERLIVKRPGTPAYQSGISTKIYPEAVHASSEAVRLSAQQPATQISLLASEEAVLPQIERLLHLSQQPEEIQVGSLDRKFSGKSPLFLIHDGSGICTHYRGLRPLGRRVLALHDPKFLIQSSKQRSWASLTTMANEYASSISSTMGMTGGEDCILGGWSFGGVVAFEAARILMSRGHRVKGVVLIDSPPPIGHIPLSESIISAVTAQPAEKDAAAGSTTASKCVSPVASAIRKLVQQSFRICAGLIGDFGTSAELQQRGLSNKPVGPVPRVILLRSAVGWTPPRGYTGAAVEEMENPWLQDRRDRSLATAGWEILTGGPIQCLDIPGNHFQVFDAPNIAAVSAALVDACSEFELK | Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the bibenzoquinone oosporein, a metabolite required for fungal virulence that acts by evading host immunity to facilitate fungal multiplication in insects . The non-reducing polyketide synthase OpS1 produces orsellinic acid by condensing acetyl-CoA with 3 malonyl-CoA units . Orsellinic acid is then hydroxylated to benzenetriol by the hydroxylase OpS4 . The intermediate is oxidized either nonenzymatically to 5,5'-dideoxy-oosporein or enzymatically to benzenetetrol by the oxidoreductase OpS7 . The latter is further dimerized to oosporein by the catalase OpS5 . OpS6 probably functions en route for protecting cells against oxidative stress by scavenging any leaked free radical form of benzenetetrol by activating the thiol group of glutathione . | J4UHQ6 |
B3LTK6 | AIM21_YEAS1 | Altered inheritance of mitochondria protein 21 | Saccharomyces | MPSEVTPKVPERPSRRKTSELFPLSGSESGDIKANSEPPTPAGTPNVPTRRPILKAKTMTSFESGMDQESLPKVPLQRPVRRSTTEELNNVMNNTSKELEEIESLISKHNIHNVSRKKSPTSVEEGKVAAIHQNGQRSASDNKTSTNPSPLEKNEHEGAEGNESAISPSNLVNKSNNEVTEHSDSEDLTEKQKVHAALDNEAGDRSHFEEKLIPGDMKVQVDVSKDVEEGSLNALPPSGITESDDKAEKFTKHPESSLEELQKHQEQQEEKIFQNPTDEESTTSLNEKQEGKDNMEVNSQPQGPSDTETVIAATSSNVPSQIASEEENDVPVIPRSRPKKDFEAHVQKEELPNTQEKRVSEECDSTLISTEEESKIPKIPSERPKRRAPPPVPKKPSSRIAAFQEMLQKQQQQDLHNNGNSSATTASADIAKKHTDSSITSDTTKADFTSKLNGLFALPGMVNPGQLPPSLEKKLSSPDTESKLGPQDQSQAKTGPLGGTRRGRGPRGRKLPSKVASVEKIEEDDNTNKIEIFNNWNVSSSFSKEKVLIDTTPGEQAERALDEKEKLPANAESDPLSQLPQTNTVGNRKAISEESLSPSEAITNRDQNDTTEIQEQQMEEQMEVDMERELSGGYEDVDSALHSEEASFHSL | Involved in mitochondrial migration along actin filaments. | B3LTK6 |
Q8ZKY3 | MNME_SALTY | tRNA modification GTPase MnmE | Salmonella | MSHNDTIVAQATPPGRGGVGILRISGLKARDVAQEVLGKLPKPRYADYLPFKDVDGSALDQGIALWFPGPNSFTGEDVLELQGHGGPVILDLLLKRILTLPGVRIARPGEFSERAFLNDKLDLAQAEAIADLIDASSEQAARSALNSLQGAFSARVNHLVEALTHLRIYVEAAIDFPDEEIDFLSDGKIEAQLNGVIADLDAVRTEARQGSLLREGMKVVIAGRPNAGKSSLLNALAGREAAIVTDIAGTTRDVLREHIHIDGMPLHIIDTAGLRDASDEVERIGIERAWQEIEQADRVLFMVDGTTTDAVDPADIWPDFIARLPKNLPITVVRNKADITGETLGISEVNGHSLVRLSARTGEGIDVLRNHLKQSMGFDTNMEGGFLARRRHLQALAEAAEHLEQGKAQLLGAWAGELLAEELRLAQQSLSEITGEFTSDDLLGRIFSSFCIGK | Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34. | Q8ZKY3 |
B9KBJ8 | RL1_THENN | 50S ribosomal protein L1 | Thermotoga | MPKHSKRYLEAKKLVDRTKYYDLDEAVELVKKTATAKFDETIELHIQTGIDYRKPDQHIRGTIVLPHGTGKEVKVLVFARGEKAKEAQEAGADYVGAEDLVEKIEKEGFLDFDVAIATPDMMRVIGRLGKILGPRGLMPSPKSGTVTNEVAEAVKEFKKGRIEVRTDKTGNIHIPVGKKSFDNEKIKENVISAIKQIMQMKPAGVKGQFIKKAVLASTMGPGIKLNLQSILNE | Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA. | B9KBJ8 |
C4LGF9 | RL9_CORK4 | 50S ribosomal protein L9 | Corynebacterium | MKLILTAAIDNLGVPGDIVEVKAGYGRNYLLPRGYAVPATRGAEKQVQDLKRAQEARAIRDADRAREVKEQLANLEGVSVAVRTANNGKLFGSVKPNDVAQAVVAAGGPELDKHSIDMTKGFVKSTGKYSVDVKLHEDIHGTINFEVVSQ | Binds to the 23S rRNA. | C4LGF9 |
Q16280 | CNGA2_HUMAN | Cyclic nucleotide-gated channel alpha-2 | Homo | MTEKTNGVKSSPANNHNHHAPPAIKANGKDDHRTSSRPHSAADDDTSSELQRLADVDAPQQGRSGFRRIVRLVGIIREWANKNFREEEPRPDSFLERFRGPELQTVTTQEGDGKGDKDGEDKGTKKKFELFVLDPAGDWYYCWLFVIAMPVLYNWCLLVARACFSDLQKGYYLVWLVLDYVSDVVYIADLFIRLRTGFLEQGLLVKDTKKLRDNYIHTLQFKLDVASIIPTDLIYFAVDIHSPEVRFNRLLHFARMFEFFDRTETRTNYPNIFRISNLVLYILVIIHWNACIYYAISKSIGFGVDTWVYPNITDPEYGYLAREYIYCLYWSTLTLTTIGETPPPVKDEEYLFVIFDFLIGVLIFATIVGNVGSMISNMNATRAEFQAKIDAVKHYMQFRKVSKGMEAKVIRWFDYLWTNKKTVDEREILKNLPAKLRAEIAINVHLSTLKKVRIFHDCEAGLLVELVLKLRPQVFSPGDYICRKGDIGKEMYIIKEGKLAVVADDGVTQYALLSAGSCFGEISILNIKGSKMGNRRTANIRSLGYSDLFCLSKDDLMEAVTEYPDAKKVLEERGREILMKEGLLDENEVATSMEVDVQEKLGQLETNMETLYTRFGRLLAEYTGAQQKLKQRITVLETKMKQNNEDDYLSDGMNSPELAAADEP | Odorant signal transduction is probably mediated by a G-protein coupled cascade using cAMP as second messenger. The olfactory channel can be shown to be activated by cyclic nucleotides which leads to a depolarization of olfactory sensory neurons. | Q16280 |
P87233 | PHF1_SCHPO | PHD finger domain-containing protein phf1 | Schizosaccharomyces | MSQKNFFDEGKSYGVNDYAGFHFENGADSSLPQVSAQGVVRETDSSNFDASPVASGSGISDVGPFGADFHQLQQHVQTPYGGMTMPASSSSGATSVPPEQDPSLSVSFNRLPKSASTKTKNGRIRSSRREDDNRIPFYDLDVAEGAEDDLQEDFHVEGMKTKSGRKIQRPVAYNPNATALKRKSRKVDMVTLCSVCQRGHSPLSNRIVFCDGCNSPYHQLCHHPPIDDATVQDVDAEWFCMKCQYRRAKQPLETGMTAQDLGLSESDKKMYLSSLPTPHLADLILFCEKSYPSLPIYNPRTRELLGEIRHQLLVSSERQQISLQERLHAKQDEAPSDEPAPVPYTASYVANSGTLYDYPTLIRLAIRNTLSPSKDEIFNWLAQNVPLLPTFHDSASEAIRWMVNKGQLVRSGSIYQIATVEEYPHLQPSLLPTFQRNRKVPKLVPVSFPTDDPQNLCATVL | Component of the SWM histone demethylase complex that specifically demethylates H3K9me2, a specific tag for epigenetic transcriptional activation, thereby acting as a corepressor. Has a role in regulating heterochromatin propagation and euchromatic transcription. | P87233 |
Q8A011 | RF1_BACTN | Peptide chain release factor 1 | Bacteroides | MADNSTILEKLDGLVARFEEISTLITDPAVIADQKRYVKLTKEYKDLDDLMKARKEYIQLLGNIEEAKNILSNESDADMREMAKEEMDNSQERLPALEEEIKLMLVPADPQDSKNAILEIRGGAGGDEAAIFAGDLFRMYAKFCETKGWKMEVSNANEGTAGGYKEIVCSVTGDNVYGILKYESGVHRVQRVPATETQGRVHTSAASVAVLPEAEEFDVVINEGEIKWDTFRSGGAGGQNVNKVESGVRLRYIWKNPNTGVAEEILIECTETRDQPKNKERALARLRTFIYDKEHQKYIDDIASKRKTMVSTGDRSAKIRTYNYPQGRITDHRINYTIYNLAAFMDGDIQDCIDHLIVAENAERLKESEL | Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA. | Q8A011 |
P61134 | CO6_PANTR | Complement component C6 | Pan | MARRSVLYFILLNALINKGQACFCDHYAWTQWTSCSKTCNSGTQSRHRQIVVDKYYQENFCEQICSKQETRECNWQRCPINCLLGDFGPWSDCDPCVEKQSKVRSVLRPSQFGGQPCTEPLVAFQPCIPSKLCKIEEADCKNKFRCDSGRCIARKLECNGENDCGDNSDERDCGRTKAVCTRKYNPIPSVQLMGNGFHFLAGEPRGEVLDNSFTGGICKTVKSSRTSNPYRVPANLENVGFEVQTAEDDLKTDFYKDLTSLGHNENQQGSFSSQGGSSFSVPIFYSSKRSENINHNSAFKQAIQASHKKDSSFIRIHKVMKVLNFTTKAKDLHLSDVFLKALNHLPLEYNSALYSRIFDDFGTHYFTSGSLGGVYDLLYQFSSEELKNSGLTEEEAKHCVRIETKKRVLFVKKTKVEHRCTTNKLSEKHEGSFIQGAEKSISLIRGGRSEYAAALAWEKGSSGLEEKTFSEWLESVKENPAVIDFELAPIVDLVRNIPCAVTKRNNLRKALQEYAAKFDPCQCAPCPNNGRPTLSGTECLCVCQSGTYGENCEKQSPDYKSNAVDGHWGCWSSWSTCDATYKRSRTRECNNPVPQRGGKRCEGEKRQEEDCTFSIMENNGQPCINDDEEMKEVDLPEIEADSGCPQPVPPENGFIRNEKQLYSVGEDVEISCLTGFETVGYQYFRCLPDGTWRQGDVECQRRECIKPVVQEVLTITPFQRLYRIGESIELTCPKGFVVAGPSRYTCQGNSWTPPISNSLTCEKDTLTKLRGHCQLGQKQSGSECICMSPEEDCSHHSEDLCVFDTDSNDYFTSPACKFLAEKCLNNQQLHFLHIGSCQDGHQLEWGLERTRLSSNSTKKESCGYDTCYDWEKCSASTSKCVCLLPPQCFKGGNQLYCVKMGSSTSEKTLNICEVGTIRCANRKMEILHPGKCLA | Constituent of the membrane attack complex (MAC) that plays a key role in the innate and adaptive immune response by forming pores in the plasma membrane of target cells. | P61134 |
A4VMR6 | KTHY_PSEU5 | dTMP kinase | Pseudomonas | MKGLFVTLEGPEGAGKSTNREYLAERLRARGLDVVLTREPGGTPLAERIRELLLTPADEPMAVDTELLLVFAARAQHLAQVIRPALARGAVVLCDRFTDATYAYQGGGRGLSLERIAQLETFVQGDLRPDLTLIFDLPVDVGLARAAARGRLDRFEQEGMRFFEAVRSAYLQRAEAAPSRYRVIDAGQALNAVQCDVEALIPELLVRLDD | Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis. | A4VMR6 |
Q9STT2 | VPS29_ARATH | Vesicle protein sorting 29 | Arabidopsis | MVLVLALGDLHVPHRAADLPPKFKSMLVPGKIQHIICTGNLCIKEIHDYLKTICPDLHIVRGEFDEDARYPENKTLTIGQFKLGLCHGHQVIPWGDLDSLAMLQRQLGVDILVTGHTHQFTAYKHEGGVVINPGSATGAYSSINQDVNPSFVLMDIDGFRAVVYVYELIDGEVKVDKIEFKKPPTTSSGP | Plays a role in vesicular protein sorting. Component of the membrane-associated retromer complex which is essential in endosome-to-Golgi retrograde transport. Required for the auxin-carrier protein PIN2 sorting to the lytic vacuolar pathway and the PIN1 recycling to the plasma membrane, thus influencing auxin transport orientation . Also involved in the efficient sorting of seed storage proteins globulin 12S and albumin 2S. The VPS29-VPS26-VPS35 subcomplex may be involved in recycling of specific cargos from endosome to the plasma membrane. | Q9STT2 |
Q9HGM2 | GET1_SCHPO | Guided entry of tail-anchored proteins 1 | Schizosaccharomyces | MMDLIISTILLSLFIHFFDKFAKKRTIDGAYRIYVSVSNNKDLKKNKEILEQLLTVKKELNATSSQDQFAKWARLNRKYEQLSQEWEKQSANVKIFQDTFKRVLSLFLWILTRGFRFYIQFKESKTPVFFLPAFLLPSWALWVLSLPRSIYGSVSLTVWNFAVQKTISGIF | Required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Acts as a membrane receptor for soluble get3, which recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. | Q9HGM2 |
Q940B8 | KN13A_ARATH | AtKINESIN-13A | Arabidopsis | MGGQMQQNNAAAATALYDGALPTNDAGDAVMARWLQSAGLQHLASPVASTGNDQRHLPNLLMQGYGAQTAEEKQRLFQLMRNLNFNGESTSESYTPTAHTSAAMPSSEGFFSPEFRGDFGAGLLDLHAMDDTELLSEHVITEPFEPSPFMPSVNKEFEEDYNLAANRQQRQQTEAEPLGLLPKSDKENNSVAKIKVVVRKRPLNKKETAKKEEDVVTVSDNSLTVHEPRVKVDLTAYVEKHEFCFDAVLDEDVSNDEVYRATIEPIIPIIFQRTKATCFAYGQTGSGKTFTMKPLPIRAVEDLMRLLRQPVYSNQRFKLWLSYFEIYGGKLFDLLSERKKLCMREDGRQQVCIVGLQEYEVSDVQIVKDFIEKGNAERSTGSTGANEESSRSHAILQLVVKKHVEVKDTRRRNNDSNELPGKVVGKISFIDLAGSERGADTTDNDRQTRIEGAEINKSLLALKECIRALDNDQLHIPFRGSKLTEVLRDSFVGNSRTVMISCISPNAGSCEHTLNTLRYADRVKSLSKSGNSKKDQTANSMPPVNKDPLLGPNDVEDVFEPPQEVNVPETRRRVVEKDSNSSTSGIDFRQPTNYREESGIPSFSMDKGRSEPNSSFAGSTSQRNNISSYPQETSDREEKVKKVSPPRGKGLREEKPDRPQNWSKRDVSSSDIPTLTNFRQNASETASRQYETASRQYETDPSLDENLDALLEEEEALIAAHRKEIEDTMEIVREEMKLLAEVDQPGSMIENYVTQLSFVLSRKAAGLVSLQARLARFQHRLKEQEILSRKRVPR | Internal motor kinesin involved in trichome morphogenesis . Participates in regulating the formation of Golgi-associated vesicles . Plays a central role in microtubule disassembly via the active ARAC10-ICR5 cascade, which establishes the secondary cell wall pattern in metaxylem vessel cells . Acts redundantly with KIN13B to modulate cell wall synthesis and cell expansion via the THE1 pathway . | Q940B8 |
A5ESR5 | Y7345_BRASB | Nucleoid-associated protein BBta_7345 | unclassified Bradyrhizobium | MADFLGMMKQAAQLQSKMQAMQEELGSLEVEGISGGGLVAVRMTAKMEVKGIKIDPSLLKPDEAEILEDLLVTAHGDARRKAEAAMQEKMQAITGKLGLPPGFGFG | Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection. | A5ESR5 |
B5VRP4 | MDM12_YEAS6 | Mitochondrial inheritance component MDM12 | Saccharomyces | MSFDINWSTLESDNRLNDLIRKHLNSYLQNTQLPSYVSNLRVLDFDLGKVGPAITLKEITDPLDEFYDSIREEADQETEENNDNKEDSEHICPDRTIANHEGPKDDFEAPVVMPSPNDIQFLLEVEYKGDLLVTIGADLVLNYPVEKFMTLPVKLSISDIGLHSLCIVACLSKQLFLSFLCDVSDPALDDNQTVLDPKGPILAATKPLERISIVRSMKIETEIGEQYQGQGSVLRSVGELEQFLFTIFKDFLRKELAWPSWINLDFNDGDE | Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondria. MDM12 is required for the interaction of the ER-resident membrane protein MMM1 and the outer mitochondrial membrane-resident beta-barrel protein MDM10. The MDM12-MMM1 subcomplex functions in the major beta-barrel assembly pathway that is responsible for biogenesis of all mitochondrial outer membrane beta-barrel proteins, and acts in a late step after the SAM complex. The MDM10-MDM12-MMM1 subcomplex further acts in the TOM40-specific pathway after the action of the MDM12-MMM1 complex. Essential for establishing and maintaining the structure of mitochondria and maintenance of mtDNA nucleoids. | B5VRP4 |
A1STF0 | GCH4_PSYIN | GTP cyclohydrolase FolE2 | Psychromonas | MPDIANSAQAQTEGKLDRVGMSNIELPLMVQTDDCPPQQVSANAEVFVNLGDAQAKGIHMSRLYLQLDELSTESELNISTLTALLQGFITSHHELSQRAFVKFSFDYHLRRKSLISEKRGWKAYPVIIIGRLSEGNFEVELQVNVPYSSTCPCSAALARQLIQQAFSQKYDQQTEVNKEEIFAWLGSTKGIVATPHSQRSIVEVKVKLNSLNQSFPIIELIDLIEKTLKTPVQAAVKREDEQEFALLNGQNLMFCEDAARHLQHSLHQETKFDDFWLRVNHYESLHAHDAVAMTTKGIEGGYLA | Converts GTP to 7,8-dihydroneopterin triphosphate. | A1STF0 |
P24674 | RBL_PICPU | Ribulose bisphosphate carboxylase large chain | Picea | MSPKTETKASVGFKAGVKDYRLTYYTPEYQTKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYDIEPVAGEETQFIAFVAYPLDLFEEGSVTNLFTSIVGNVFGFKALRALRLEDLRIPPAYSKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFVFCAEAIYKAQAETGEIKGHYLNATAGTCEEMMKRAVFARELGVPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRMSGGDHIHGGTVVGKLEGERDITLGFVDLLRDDFIEKDRSRGIYFTQDWVSMPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQARNEGRDLAREGNEVIREASKWSPELAAACEVWKEIKFEFEAVDTI | RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site. | P24674 |
Q8IS20 | GEFC_DICDI | RasGEF domain-containing protein C | Dictyostelium | MSVFTFGHGSNGALGLGKITDDTCPTPQKVNYFTEIDKRVKKVACGSYHTVFVTDDEHLYICGIKKDPKHGTTLFYTSPPPTTTTTTTTTSSTSATTTTTNGMVNEKNNNNKNNNGEKIVNSKPESVIIKDGASNTTNDSTSSSSTSTSSLSSSLPPTNIETPRDKKKPPIKLDKGIPHHRSTRELIQRPESPLLNKLLTSKAEMEFKHYESNEKSKDEMKDNENENEEDEDDDDDDSTIRQNEDKESSLIDDNESETSLRINKKDAENITNNIRLIKELDEQQQQPQQPQQNLKGIMNQPPLPTNDDLDEDPNIHFTPIRISTHFLENSPLNTIKQVALGNYHIVLLTEGGNVWTWGSNSNGQLGYLVDTQQQQQQQLQQQQSMSSLQPSASSSSPSSSSLQTTCTPKMVEIKCVKYIATGVKNTAALTEWGELYMWGINEHGELGLGDTIDRRTPTRVIRLKNEVVSTIACSSTHSACYTESGKMYVWGQSDETGKIQAIPSPLPIHSYLDREIKSPNGGGVGGFFGGGGKIKQLACGQRCIAVLTQMGEVFMWEIPGIPIPLRNALENHSVRNIVMGNFHLVCLTDSGEVVTIGRNKTGQLGRTDAENEPGIVKQLSFDPDGLNSDEFVVSIAAGEFHSVALVENTPKTKLALQLVRMQRNYLRQLNILNNIYYKSMMSMASPYDPVVLSMMNNGSASTLPPSLKGLSGGLPDNANNTIKNGKDKDNHHNGDSNGHHSNGHYHGNGNNGNNSITTSNSISSPSLLGSGGTLKSRSASIATIRGLFGINHMLHHSQSQSFQEENSTVTEDEIKEIFSDIEALSKLTEKFLSYLDQRMDNWDPVSKVLGDIFLDEALMAAYRIYIPYSDSYNTSCMTLFNIRRRNERLSNIIKDCEKKSKSFGVKLDQEFVKEIDLKSLLLSPLQNIPRIYILLRELGSDDSGNINPRDIDLINFAATKFQVLLERMNQNFQFVNAVEILHCSSNEYGNPQIMGGSLPQLVDKLTHHNISDPNFRDVFLLTFRAFTTPCNLFDLLVETFQRQKHLKNGRVVNVITSWVVHHFYDFEKDKLSDFTQDPNHNPQLLSEKLEQFIYSEDHQSVSQIKLQYFSHRKRLESSINLIDNQKLTQNEITTPPPLQIQNNNQNNNLENNNNNNNNNNTTTTTTTPNDNINDINNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNLTNSTIKLVVQPPIPINFNLLDSQPIEVAQTLTIMDHHYFAMIDKREFLGQRWAKNKSPNIQISTDHFNRTSQVVVTEILKSKNSKQRSATLGYFISVAYCCFELNNLSGTASIIYGLNSASIQRLKKSWSKLPKESMIAFEYLDKIVTPMKNYISLRHLMTTIQPPCVPFLGTYLKDLTFIEEGNPSIIGGLINFYKQRKIAEVIFQIQQHQQVVYSAIRSNPTIKAFLMSSHTFDDKQAQKISSEAE | Promotes the exchange of Ras-bound GDP by GTP. | Q8IS20 |
A8EVZ6 | RL10_ALIB4 | 50S ribosomal protein L10 | Aliarcobacter | MTREEKSQVIDFLTAEFKSSLAVVVCDYKGLTHKELETLRKEAKANNTKVQVAKNTLVTVAVKNAELGDIELSGTNIFLWSDDQISACKVADKFASANKEKFAIKSGIIEGQISDASKVNAFAKLPSREELLGMLASVWMGPVRNFTIGLDALRRKKEEEAA | Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors. | A8EVZ6 |
B9E8Q0 | EFTU_MACCJ | Elongation factor Tu | Macrococcus | MAKEKFDRSKTHANIGTIGHVDHGKTTLTAAIATVLSKKLGGEARSYDQIDNAPEEKERGITINTSHIEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGGILVVSAADGPMPQTREHILLSRNVGVPALVVFLNKVDMVDDEELLELVEMEVRDLLSEYDFPGDDVPVIAGSALKALEGVEEYEDKIMELMDAVDEYIPTPERDSDKPFMMPVEDVFSITGRGTVATGRVERGQVKVGEEVEIIGLTEEPSKTTVTGVEMFRKLLDYAEAGDNIGALLRGVSREDVQRGQVLAKPGSITPHTKFKAEVYVLSKEEGGRHTPFFTNYRPQFYFRTTDVTGVVNLPEGTEMVMPGDNIEMNVELISPIAIEDGTRFSIREGGRTVGSGVVSVIEK | This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. | B9E8Q0 |
A9AGH3 | KYNB_BURM1 | N-formylkynurenine formamidase | Burkholderia cepacia complex | MDILWDISPPISAATPVWPGDTPVSVERVWRIEAGSPVNVARLTLSPHTGAHCDAPLHYDADGAAIGAVPLDTYVGPCRVIHCIGASPVVRPADVAAALDGVPPRVLLRTYANAPTAHWDSAFCAVAPDTVDLLAAHGVKLIGIDTPSLDPQESKTMDAHHRVHAHRMAILEGIVLDEVPPGDYELIALPLKFATLDASPVRAVLRALPARAA | Catalyzes the hydrolysis of N-formyl-L-kynurenine to L-kynurenine, the second step in the kynurenine pathway of tryptophan degradation. | A9AGH3 |
A2Y9X7 | PSA4A_ORYSI | 20S proteasome subunit alpha-3 | Oryza sativa | MSRRYDSRTTIFSPEGRLYQVEYAMEAIGNAGSALGVLAADGVVLVGEKKVTSKLLQTSRSAEKMYKIDSHLACAVAGIMSDANILLNTARLHAQRYALSYQEPIPVEQLVQSLCDTKQGYTQFGGLRPFGVSFLFAGWDKHHGFQLYMSDPSGNYSGWKAAAVGANSQAAQSMLKQDYRDGMTREEAVALALKVLSKTMDSTSLTAEKLELAEVFLQPGTGEVQYQVCSPEAMGKLLAKAGLSQPAPEA | The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. | A2Y9X7 |
Q7X7H9 | SK3_ORYSJ | Shikimate kinase 3, chloroplastic | Oryza sativa | MDAGVGLRAKPGAWAGLGNPRRSSTARVPVRFAVEKFAQPLVLGSDRRSCGAKLKVSCSRKPAGIDKTYYSADEALVLKQKAEDVVPYLNDRCIYLVGMMGSGKTTVGKILAEVLGYSFFDSDKLVEKAVGISSVAEIFQLHSEAFFRDNESEVLRDLSSMHRLVVATGGGAVIRPINWSYMKKGSTIWLDVPLDALARRIAAVGTASRPLLHQESGDPYAKAYAKLTALFEQRMDSYANADARVSLEHIAVKQGHSNVTTLTPSAIAIEALLKMESFLTEKAMIRN | Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate. | Q7X7H9 |
O54908 | DKK1_MOUSE | Dickkopf-related protein 1 | Mus | MMVVCAAAAVRFLAVFTMMALCSLPLLGASATLNSVLINSNAIKNLPPPLGGAGGQPGSAVSVAPGVLYEGGNKYQTLDNYQPYPCAEDEECGSDEYCSSPSRGAAGVGGVQICLACRKRRKRCMRHAMCCPGNYCKNGICMPSDHSHFPRGEIEESIIENLGNDHNAAAGDGYPRRTTLTSKIYHTKGQEGSVCLRSSDCAAGLCCARHFWSKICKPVLKEGQVCTKHKRKGSHGLEIFQRCYCGEGLACRIQKDHHQASNSSRLHTCQRH | Antagonizes canonical Wnt signaling by inhibiting LRP5/6 interaction with Wnt and by forming a ternary complex with the transmembrane protein KREMEN that promotes internalization of LRP5/6 . Inhibits the pro-apoptotic function of KREMEN1 in a Wnt-independent manner, and has anti-apoptotic activity . Plays a role in limb development; attenuates Wnt signaling in the developing limb to allow normal limb patterning . | O54908 |
Q6FKA1 | BOS1_CANGA | Protein transport protein BOS1 | Nakaseomyces/Candida clade | MNALYIHAQKQKTQLQQDIAKFEQDNLTAPISLQGSISATLVAFEKTIEQYKQHFDKRRAGGSNDEEQLDPKYELRLVSLKKDHKDFDAKFKELKQKYNENNARSKLFESPLDAQTGGESVMNQRRTATNDHTSQPGNTSSNYGLPMYDGLQKEQSIFQRGNAQLDMILEMGQQSLDDIMEQNQILLKVQDQMSRSLRTLGVSEETIQTINKRVFKDKLIFILIIFLFLVGVYYVLKWFR | SNARE required for protein transport between the ER and the Golgi complex. | Q6FKA1 |
B4SG68 | PROA_PELPB | Glutamyl-gamma-semialdehyde dehydrogenase | Pelodictyon | MKETITKQLIAVQQASREIITLTDETINSLLCALADSIPSHQEAILQANQKDIERMDPADPMVDRLLLNASRLDAIAADIRNVASLPSPLDALLEERVLPNGLNLKKVTVPIGVIGIIYEARPNVTFDVFALCLKSGNATVLKGGSDAMYSNIAIVELIHSVLKQHGINPDTLYLLPAEREAAAVMLNAVGYIDMIIPRGSQKLIDFVRNNAKVPVIETGAGIVHTYFDKSGDLDLGKHIIFNAKTRRPSVCNALDTLVIHQERLADLPALVEPLQEKQVMLFADEAAFQALQGSYPDDLLHQAEPEHFGTEFLSLKMSVKTVSSLEEALEHITRYSSRHSEAIIATDPETTATFLKRVDAAVVYANTSTAFTDGAQFGLGAEIGISTQKLHARGPMALKELTTYKWIIEGNGQTRPA | 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. | B4SG68 |
C5CXR6 | FLHC_VARPS | Flagellar transcriptional regulator FlhC | Variovorax | MTRKSVLGEVREVQLAIQLIQLGARLQFLESEVGLSRERLIRLYKEIKGVSPPKGLLPFSTDWYMTWLANIHSSMFYNMYQFMKIHSDEEKVWILIKSYKLYLQQIAAQDSEPILDFTRAYTMVRFFDSDMLQLSTCCRCSGQFVAHAHDHKSGYVCVLCRPPSRAGKARGAKRGAEGEAGALGIEGMGFGVEAAPGGAGFH | Functions in complex with FlhD as a master transcriptional regulator that regulates transcription of several flagellar and non-flagellar operons by binding to their promoter region. Activates expression of class 2 flagellar genes, including fliA, which is a flagellum-specific sigma factor that turns on the class 3 genes. Also regulates genes whose products function in a variety of physiological pathways. | C5CXR6 |
Q556R7 | CF50_DICDI | GH family 25 lysozyme 1 | Dictyostelium | MNKMNNIFLIISSIILSIVIFVSGECAIDFSSEISVGISDSQWSCLASNNQRVIIQVWSGGGQYNSNISSVVSAAEQAGFDNIDLYAFLCSECDGNYPASSAIQSLVSSLKSDGINFNMLWIDVEQCDGCWGAESDNADYVQEAVETAQGLGVLVGVYSSEGEWPQTVGNLSTLSQYPLWYAHYDDNPSFSDTAFYEFGGWTSPAMKQYIGNTNQCGVSVDLDFYGSGSGCSTSSGSASGSASGSASGSASGSNSGSSNSGSSNSGSSNSGSNSGSSNSGSGNSGSSNSGSASGSGTGSGSSI | Cell-counting factor that limits the maximum size of the multicellular structure during aggregation. Has a very low lysozyme activity. | Q556R7 |
Q5SID2 | TRMFO_THET8 | Folate-dependent tRNA(M-5-U54)-methyltransferase | Thermus | MERVNVVGAGLAGSEAAWTLLRLGVPVRLFEMRPKRMTPAHGTDRFAEIVCSNSLGGEGETNAKGLLQAEMRRAGSLVMEAADLARVPAGGALAVDREEFSGYITERLTGHPLLEVVREEVREIPPGITVLATGPLTSEALAEALKRRFGDHFLAYYDAASPIVLYESIDLTKCFRAGRYGQSADYLNCPMTEEEYRRFHQALLEAQRHTPHDWEKLEFFEACVPVEELARRGYQTLLFGPMKPVGLVDPRTGKEPFAVVQLRQEDKAGRMWSLVGFQTGLKWPEQKRLIQMIPGLENAEIVRYGVMHRNTYLNAPRLLGETLEFREAEGLYAAGVLAGVEGYLESAATGFLAGLNAARKALGLPPVAPPEESMLGGLVRYLATANPEGFQPMYANWGLVPPVEGRMGKKEKRQAMYRRGLEAFSAWLSGLNPPLPRPEAALV | Catalyzes the folate-dependent formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs. | Q5SID2 |
A4SG83 | HIS3_CHLPM | Phosphoribosyl-AMP cyclohydrolase | Chlorobium | MGENEGIDKSFLDTVKFDDRGLIPAIVQDHETGKVLMMAWMNRESLEMTLERKKACYWSRSRNKLWLKGESSGNMQEVFDILIDCDGDTLILKVSQIGGACHVGYHSCFYRKVNEDGSMQICDTLMFNPEEVYGKKH | Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP. | A4SG83 |
A5EY84 | ORN_DICNV | Oligoribonuclease | Dichelobacter | MDKKNNLVWIDLEMTGLDPQHDEIIEIATIVTDAQLNILAEGPVIAVYQPEPILAQMDAWNQKHHGASGLIERVRQSSFNTLEAEAQTLSFLEQYSEKGRSPICGNSICQDRRFLSRLMPRLEAFFHYRNLDVSTIKELVARWYPEHYFHKNTTHQALQDIRDSIDELRHYRQRIFVNPS | 3'-to-5' exoribonuclease specific for small oligoribonucleotides. | A5EY84 |
Q11183 | TXND9_CAEEL | Thioredoxin domain-containing protein 9 | Caenorhabditis | MAANIQQQFGEQLLRAAQVVEEQIDQEMNKLENLEEDDLEVIRRQRMEQMKKAQKDRIEMLSHGHGKYEEVADEKEFFEATKKSDKVVCLFYLPGNFRCKIVDKHFEILARKHVGTRFIHVNAEKVHFLTTRLNIRVIPSIAIVVKQQTVDYIRGFDELGGKDEFTTETMENRLARSEVLTVEKKHTAPAKKKIIRSGVEEYDNEEDW | Required for normal microtubule organization and function . Regulates tubulin acetylation in ALM and PLM neurons . | Q11183 |
P95526 | RECA_PASMU | Recombinase A | Pasteurella | MATKEEKNKALAAALGQIEKQFGKGSIMKLGDTQALDVEAVSTGSLSLDVALGIGGLPMGRIVEIFGPESSGKTTLTLSVIAQAQKEGKTCAFIDAEHALDPIYAAKLGVNVNELLVSQPDNGEQALEICDALVRSGAVDVIIVDSVAALTPKAEIEGEMGDSHMGLQARLMSQALRKLTGQIKNSNCLVVFINQIRMKIGVMFGNPETTTGGNALKFYASVRLDIRRTGAIKEGEEVIGNETRVKVVKNKVAAPFRQVDFQILYGQGISKTGELIELGVKHKLVDKAGAWYAYNGEKIGQGKANAMKWLEEHPEEALALETKLRNELLANPEKVLAADIAEKNESSTGLEADY | Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage. | P95526 |
Q8DPG6 | CRCB2_STRR6 | Putative fluoride ion transporter CrcB 2 | Streptococcus | MKKEQFYPLGIFLAAMLGGLVRYLVSTWLPASPDFPWGTLFVNYLGIFCLIFLVKGYLVYKGTSKGLILALGTGFCGGLTTFSSLMLDTVKLLDTGRYFSLVLYLLLSIGGGLLLAYFLGRKKW | Important for reducing fluoride concentration in the cell, thus reducing its toxicity. | Q8DPG6 |
Q7ZWM3 | CEL3B_XENLA | Trinucleotide repeat-containing gene 4 protein B | Xenopus | MKEPDAIKLFIGQIPRNLDEKDLKPIFEQFGKIYELTVIKDKFTGMHKGCAFLTYCARESALKAQSALHEQKTLPGMNRPIQVKPADSESRGEDRKLFVGMLGKQQTDEDVRRMFETFGNIDECTVLRGPDGTSKGCAFVKFQTHTEAQAAINALHGSRTLPGASSSLVVKFADTEKERGLRRMQQVANQLGMFSPIALQFGAYSAYTQAVSDQLMQQQAALVAAQSAYLNPMATMAAVQMQQMATINPNGIIATPITQINSITSSSGTSTPPTLTATPVSAIPATLGVNGYSAVPTQSTVQPSSEAIYTNGLHPYPAQSPVAQLDPLQQAYAGMQHYTAAYPAAYGLVSPAFTQPPAILTQQPPQQQQQREGPEGCNIFIYHLPQEFTDSEILQMFLPFGNVISAKVFVDRATNQSKCFGFVSFDNPGSAQAAIQSMNGFQIGMKRLKVQLKRPKDANRPY | RNA-binding protein that may be involved in the regulation of pre-mRNA alternative splicing. | Q7ZWM3 |
Q8GXF8 | SHGR9_ARATH | RING-type E3 ubiquitin transferase SGR9 | Arabidopsis | MEDENTTIIMASLSALSPSHLTNLTHSILSISHHHRRRLGAVLSSPTLFSLTLRHLLSLSLPDKTHLIANHLLSLLHPLLIHRKHHSSYAVTMKLRDLDAVVLLLFLCETHQLHPDVLEASADNWREILGNTYSNNMLSNNSGLWTCDAGILMPYIETLVRCKRFVDIMGGYNHLRRRDQKEGYQVPAARAAVVALRAVEVFNVAASNAGEVECVICKEEMSEGRDVCEMPCQHFFHWKCILPWLSKKNTCPFCRFQLPTDDVFSEIQRLWEILVKSSELHVA | E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Modulates amyloplast dynamics and sedimentation in statocytes during inflorescence, hypocotyl and root gravitropism, probably by regulating amyloplast interaction with actin filaments (AFs) in endodermal cells. | Q8GXF8 |
B2VE93 | DER_ERWT9 | GTP-binding protein EngA | Erwinia | MVPVVALVGRPNVGKSTLFNRLTRTRDALVADFPGLTRDRKYGRAEIEGREFICIDTGGIDGNEEGVETRMAEQSLLAIEEADVVLFMVDARAGLMPADTAIAKHLRSRQKPTFLVANKTDGLDADSAVVDFWSLGLGEIHPIAASHGRGVTSLLELVLLPWMDEVVPQRELTEEEENAAYWAELAAKEAKVNGEATADEEDDFNPLDLPIKLAIVGRPNVGKSTLTNRILGEDRVVVFDMPGTTRDSIYIPMERDGREYILIDTAGVRKRGKVTETVEKFSVIKTLQAIEDANVVMLVIDAHEGISDQDLSLLGFILNSGRSLVIVVNKWDGLSQEVRDEVKEALDYRLGFIDFARIHFISALHGSGVGNLFESVTEAYDCSTRRVNTSMLTRIMHMAADDHQPPLVRSRRVKLKYAHAGGYNPPIVVIHGNQVKDLPDSYKRYLMNYFRRSLDIMGTPIRIQFKEGDNPYEGKRNLLTPNQQRKRQRLMSHLKKNKR | GTPase that plays an essential role in the late steps of ribosome biogenesis. | B2VE93 |
Q9CCL1 | CTPC_MYCLE | Manganese-exporting P-type ATPase | Mycobacterium | MTLAMAEQIATADNPAFVVVSDAAGRMRIQIEWVRSNPRRAVTVEEAIAKCNGVRVVHAYPRTGSVVVWYSPRCCDRQSILAAISGAAHVAAELIPTRAPHSSDIRNIEVLRMAIGAAALTLLGVRRYVFARPLLLPTTSRLVASGVTIFTGYPFLRGALRFGKTGTDALVSVATIASLILRENVVALAVLWLLNIGEYLQDLTLRRTRRAISALLSGTQDTAWIRLTDGPQAGTEIQVPIGTVQIGDEVVVHEHVAIPVDGEVIDGEAVVNQSAITGENLPVSVMAGSHVHAGSVVVRGRLMVRASAVGKHTTIGRIVTRVEEAQHDRAPIQTVGENFSRCFVPTSFVVSAITLAITKDVRRTMTVLLIACPCAVGLATPTAISAAIGNGARRGILIKGGSHLEQAGRVDAILFDKTGTLTVGRPVVTNIVAMHKDWSPEQVLAYAASSEIHSRHPLAEAVIRSTEERHISIPPHEECEVLVGLGMRTWADGRTLLLGSPSLLCAEKVKVSKTASEWVDKLRHQTETPLLFAVDGTLVGLISLRDEVRPEAAEVLTKLRASGVRRIVMLTGDHPDIAKAVATELGIDEWRAEVMPEDKLKVVRDLQNEGYVVGMVGDGVNDAPALAAADIGIAMGLAGTDVAVETADVALANDDLNRLLDVRDLGGRAVEVIRENYGMSIAVNAAGLFIGAGGALSPVLAAVLHNASSVAVVANSSRLIRYRLD | High affinity, slow turnover Mn(2+) transporting ATPase. | Q9CCL1 |
A9B8B2 | CLPX_HERA2 | ATP-dependent Clp protease ATP-binding subunit ClpX | Herpetosiphon | MAQSAFMPPTYYCSFCGRNQDEVDRLVTGPGALFICNECIELLSAIIANEERKEAPHAPILPPTLPIPHAIRDHLDEYVIGQDRAKKVMAVAVYNHYKRLRAQAQGDTDVEIQKSNILLVGPTGSGKTLLAQTLARMLDVPFAIADATALTEAGYVGEDVETILLRLIQAADGDVDRAQMGILYIDEIDKIARKADNPSITRDVSGEGVQQALLKILEGGVVNVPPMPGRKHPQQEFIPFDTTNVLFICGGAFEGLEHHIAERMGSGGTLGFGKTIVKEERLERSKKLLSLVNPDDLLHFGFIPEFIGRMPVVAALTPLDKDAMMRILTEPRNAIIKQYQKMLALDHVQLEVSGDAMEAIVERALAGKTGARGLRTAVEEILLDVMFDLPSETDVVRCVITAETVRDGAMPTLIRRTSSRSRAGKQPTTKAS | ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | A9B8B2 |
Q89H51 | AMIF_BRADU | Formamide amidohydrolase | Bradyrhizobium | MNGLGGLNKSPEGVVIGLVQLQLPNVVTRADLARQTERIVWMVGKARRNLSTMDLVVFPEYSLHGLSMDTNPEIMCRLDGPEVTAFKKACVDNRIWGCFSIMEFNPHGNPYNSGLIIDDHGEIKLYYRKLHPWIPVEPWEPGDIGIPVIEGPKGARIALIICHDGMFPEMARECAYKGAEIMIRTAGYTAPIREAWRFTNQANSFQNLMVTANVCMCGSDGSFDSMGEGMIVNFDGAVLAHGTTGRADEIITAEVRPDLVREARINWGVENNIYQLWHRGYVAVKGGAMDCPYTFMQDMVAGTFRLPWEDQVKVTDGSSCGFPAPTRMYGKTAKAAE | Is an aliphatic amidase with a restricted substrate specificity, as it only hydrolyzes formamide. | Q89H51 |
O67315 | MURA_AQUAE | UDP-N-acetylglucosamine enolpyruvyl transferase | Aquifex | MKNTTLYTYRDYFVIRGGKPLTGKVKISGAKNAALPIMFATILTEEPCTITNVPDLLDVRNTLLLLRELGAELEFLNNTVFINPSINSFITNQEIIRRMRASVLSLGPLLGRFGRAVVGLPGGCSIGARPIDQHLKFFKEAGADVEVREGYVYVNLKEKRRVHFKFDLVTVTGTENALLYLASVPEESILENIALEPEVMDLIEVLKKMGAHVKVEGRSAYVKGSENLKGFTHSVIPDRIEAGTFMVGAVLTDGEILLENARINHLRAVVEKLKLIGGEVVEENGNLRVFRKESLRACDIETQVYPGFPTDMQAQFMALLSVAKGKSRIKENIFEHRFHHAQELNRLGANITVRGNTAYVEGVERLYGSEVYSTDLRASASLVLAGLVAQGETVVRDVYHLDRGYEKLEEKLKKLGADIERVSEL | Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. | O67315 |
O57314 | DHB12_ANAPL | Estradiol 17-beta-dehydrogenase 12 | Anas | MLPAAGLLWWVGALGALYAAVRGALGLLGALRVWGIGAGRAALGPGLGAWAVVTGATDGIGKAYAKELAKRGMKVALISRSKEKLDQVAGEITEQYGVETKVIVADFGEREDIYDRIRAGLEGLEIGVLVNNVGISYSYPEYFIDVPDLDKTIDKMININIMSVCKMTRLVLPGMLERSKGVILNISSAAGMYPTPLLTLYSASKAFVDYFSRGLHAEYKSKGIIVQSVMPYYVATKMSKISKPSFDKPTPETYVRAAIGTVGLQSQTNGCLPHAFMGWVFSILPTSTVMNLLMKTNKQIRARFLKKKMKEK | Catalyzes the second of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme has a 3-ketoacyl-CoA reductase activity, reducing 3-ketoacyl-CoA to 3-hydroxyacyl-CoA, within each cycle of fatty acid elongation. Thereby, it may participate in the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. May also catalyze the transformation of estrone (E1) into estradiol (E2) and play a role in estrogen formation. | O57314 |
Q6PGA0 | RCOR3_MOUSE | REST corepressor 3 | Mus | MPGMMEKGPELLGKSRSANGGAKSPAGGGGSSANGGLHFSEPESGCSSDDEHGDVGMRVGAEYQARIPEFDPGATKYTDKDNGGMLVWSPYHSIPDAKLDEYIAIAKEKHGYNVEQALGMLFWHKHNIEKSLADLPNFTPFPDEWTVEDKVLFEQAFSFHGKSFHRIQQMLPDKTIASLVKYYYSWKKTRSRTSLMDRQARKLANRHNQGDSDDDVEEAHPMDGNDSDYDPKKEAKREGNADQPVQTSKIGLGRREYQSLQHRHHSQRSKCRPPKGMYLTQEDVVAVSCSPNAANTILRQLDMELISLKRQVQNAKQVNSALKQKMEGGIEEFKPPEAQTPQAPRTLGPSPPAPSSTPTPTVPIATLNQPPPLLRPTLPAAPALHRQPPPLQQQARFIQPRPTLNQPPPPLIRPANSMPPRLNPRPVLTTVGGQQPPSLIGIQTDSQPSLH | May act as a component of a corepressor complex that represses transcription. | Q6PGA0 |
Q3YZN3 | MEPA_SHISS | D-alanyl-D-alanine-endopeptidase | Shigella | MNKTAIALLALLASSASLAATPWQKITQPVPGSAQSIGSFSNGCIVGADTLPIQSEHYQVMRTDQRRYFGHPDLVMFIQRLSSQVSNLGMGTVLIGDMGMPAGGRFNGGHASHQTGLDVDIFLQLPKTRWTSAQLLRPQALDLVSRDGKHVVSTLWKPEIFSLIKLAAQDKDVTRIFVNPAIKQQLCLDAGTDRDWLRKVRPWFQHRAHMHVRLRCPADSLECEDQPLPPSGDGCGAELQSWFAPLKPGTTKPEKKTPPPLPPSCQALLDEHVI | Murein endopeptidase that cleaves the D-alanyl-meso-2,6-diamino-pimelyl amide bond that connects peptidoglycan strands. Likely plays a role in the removal of murein from the sacculus. | Q3YZN3 |
Q393X2 | LEUC_BURL3 | Isopropylmalate isomerase | Burkholderia cepacia complex | MAQTLYDKLWNTHVVHTEEDGTTLLYIDRQLLHEVTSPQAFEGLKIAQRPVWRISANLAVSDHNVPTTDRSHGIADPVSKLQVDTLDANCDAFGITQFKMNDVRQGIVHIIGPEQGATLPGMTIVCGDSHTSTHGAFGALAHGIGTSEVEHVLATQTLLQKKSKNMLVKVEGTLPRGCTAKDIVLAIIGKIGTAGGTGYAIEFGGSTIRALTMEGRMTVCNMAIEAGARAGMVAVDDTTIDYLKGRPFVPTGAEWNQAVEYWRQFKSDDGAQFDRVVELNAAEIVPQVTWGTSPEMVTSIDGRVPDPEREKDPVKRDAMERALAYMALEPNTPIESIKVDKIFIGSCTNARIEDIRAAAYVVKKLNRRVASNVRLAMVVPGSGLVKAQAEREGLDKVFTDAGFEWREPGCSMCLAMNADRLDPGERCASTSNRNFEGRQGAGGRTHLVSPAMAAAAAIEGHFVDIRQLG | Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate. | Q393X2 |
Q6NMI3 | COG6_ARATH | Component of oligomeric Golgi complex 6 | Arabidopsis | MASTVGLAPGLSRKLKKVLDCRTDSPDLVASLNALSSFYDENSAHARRNLRSTIEKRALQINSEFLNAADSTQIALDRVEEEVNALADCCDKIAAALSSSAATTSDIISTTERLKQELEVTTQRQEIVNCFLRDYQLSNEEIKALREDELNENFFQALSHVQEIHSNCKLLLRTHHQRAGLELMDMMAVYQEGAYERLCRWVQAECRKLGDTDNPEVSELLRTAVRCLKERPVLFKYCAEEVGNLRHNALFRRFISALTRGGPGGMPRPIEVHAHDPLRYVGDMLGWLHQALASERELVHALFDIDSADHQSNAKNTSENIALKAGESDFTFVLDRIFEGVCRPFKVRVEQVLQSQPSLIISYKLTNTLEFYSYTISDLLGRDTALCNTIGMVKDAAQKTFFDILKTRGEKLLRYPPPVAVDLSPPPAVREGVSLTLEIIENYNSMMVSASGEKPAFDPVLSALLDPIIKMCEQAAEAHKSKKSGQLPRRSRTSSDSSQLTSVDALLSSSPSPPQNNETPSKIFLINCLCAIQQPLLRHDVASQYVTNIGLMIENHINLLVQNEVDTLLHKCGLSDKMQIFRSSTSELPLSERQDTSPAMLSECLKAFFGLVLGSEGSLPEFEQIQVPKLRSEACVRVAKTLAEAYEVIYQAVTDQQNGYPDPKSLARHPPDQIRTILGI | Required for normal Golgi function. | Q6NMI3 |
B9L7B6 | THIG_NAUPA | Thiazole synthase | Nautilia | MSDILKIGKYEFTSRLIVGSGKYPDFQTTRDATLASGAEMITVAVRRVNIMDPNEENLMDYFKDTDVKILPNSAGCTTAEEAITLFRLVREATGIDIIKLEVIGDTAKTLYPDVMETLKACEVLAKEDFTIMAYTNDDPIMAKRLENAGAHAVMPLAAPIGSGLGVQNRYNVVFVKDAVNVPVIVDAGIGTASDAAVAMELGADGVLTNTAIAQAKNPIAMAEAMKHAVIAGRMAYKAGRIPKKPYATASSPLEGLIEF | Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is provided by the thiocarboxylate moiety of the carrier protein ThiS. In vitro, sulfur can be provided by H(2)S. | B9L7B6 |
A2BTN6 | TIG_PROMS | PPIase | Prochlorococcus | MAKDALIVKTTPLPQSRISFELEIPSETCKTCVNETINSISRSAKIPGFRLGKIPKQVLIQRIGITQLHASALEKIIDKSWQEALKIKSIEPLSEPELVDGFESLLAKFSPEKSLKVTLQTDVAPELKLKKSKGLSVEISKTKFDPKSIDEALEKSRNQFANIIPVTNRAAKLGDIAVVSFKGKYKDSGKEIDGGTSESMDLELEKNKMIPGFVEGIVKMKIGDTKTLNLKFPDDYSHEDSRGKEAIFEVNLKDLKEKELPELNDDFAKQSGNKESLKELKKDIEKQLKDNFEKTQKDIKIEALLDALTNELVAEIPKSMIDIEVRNNIEQTAQRFAQQGLDVKSTFTPELVKSLADSTRPQAEKNVQRNLALKALAETENIKVEQDEIDSKMKDYEDAISQSSKQIDIKKLTEVLTNDLLKEKLIIWLEENSEVKEKTTKTSKATKTSKTTKATKTASKTTKTTKTQNKKEKK | 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. | A2BTN6 |
B7HLH4 | TRMD_BACC7 | tRNA [GM37] methyltransferase | Bacillus cereus group | MKIDILTLFPDMFTGVFGSSILKKAQEKEAVELRVVNFRDYTTSKHNSVDDYPYGGGAGMVLTPQPIFDAVEDLTKETERKPRVVLMCPQGERFTQKKAEELAEEEHLIFVCGHYEGYDERIREHLVTDEISIGDYVLTGGELASMVITDSVVRLLPGVLGNHASQVEDSFSTGLLEHPHYTRPADFRGMKVPDVLMSGNHKNIDEWRHKESLRRTYTRRPDLLEERELSKQEKKWLEQIKEGK | Specifically methylates guanosine-37 in various tRNAs. | B7HLH4 |
Q82U05 | FABZ_NITEU | Beta-hydroxyacyl-ACP dehydratase | Nitrosomonas | MKQGDRQTVMDIHEILKYLPHRYPLILVDRVVSLESGKRIHAYKNVSINEPYFSGHFPHHPVMPGVLIIEALAQAAALLTIRSENMEKDNGQVYYFVGIDAVRFKKPVIAGDQLVLKVEITRQLKGIWKYAACAEVDGQVVTEAQLMCTARAI | Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs. | Q82U05 |
A6TDB1 | COBQ_KLEP7 | Cobyric acid synthase | Klebsiella | MTLAVMLQGTASDVGKSVLVAGLCRIFHQDGLRTAPFKSQNMALNSGITPDGKEMGRAQIFQAEAAGIAPDVRMNPILLKPTSDRQAQVVLMGQVATSMDAVSYHQYKPRLREQILAVYQSLAGEYEALVLEGAGSPAEINLRDRDIVNMGMAEMAQCPVILVADIDRGGVFAAIYGTLALLQPQERARVKGVIINKFRGDVALLRSGIEQIEALTGVPVLGVMPWLDVDLEDEDGVALQAGKYHRTDRRDIDIAVVHLPHIANFTDFNALAAQPDVRVRYVRDPQALADADLVILPGSKNTLGDLCWLRESGMAHAVEQARQRKVPLLGICGGYQMLGETIIDEVESGLGAQPGLGVLKTVTHFAQHKTTTQVQATLGSALPDWLADAAGLRVSGYEIHMGETRREAGCPPLLQLHKAGQAVDDGAISDDGLAFGTYLHGLFDSDAFTRALLNGLRQRKGLAPLDSALEYARYKTRQFDRLAEAMREHIAIDKIYAIMRQHQEPLC | Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation. | A6TDB1 |
Q92HH1 | PRIA_RICCN | ATP-dependent helicase PriA | spotted fever group | MRIAKILLPVAKLFPLDYLIPEDLELNIGDLVVVPFRNKELTGIVWELVSNSEAKKIKTIRVKVPLNLNITSEVLELIKWMSSYYMSELGSIAKLVLPMDIAEKPIKVKEQKVNNNFVLPDLSEEQKQAVTILNESNKPTLVKGVTGSGKTEIYFHLIADYLAKGKQVLVMLPEIALSTQIINRFIERFGFEPIIWNSSVTKAHKKMILRGILSDKVKVVIGARSSLFLPFKNLGLIVIDEEHDDSYKQDDGILYNARDTAIVRGTFDKAQIVLCSATPSIETIHNIEIGKYQLVTLVNRYKNVDLPNIEIIDMTKEKLSKNSYLSKLLIEAIKGNLDNKKQVLLFLNRRGYAPLMLCKACGYRLTCKFCSSWMVVHKATKKLECHHCGYQSKIFSSCPECLEDETLTICGPGIERIEEEAKALFPESKIAVISKDHAKSPEKIAQLLHQMENLEIDILIGTQIITKGYHFPNLTLVGVIDADLGSNNADLRASERTFQLLHQVGGRAGRGDSKGVVYLQSYYPDNTIFSYVKAGDEDSFFANELEIRKSADMPPFSKTASVILSGSSEAKILEIARDMVRIAPKANVKILGPASSLMSKLAGKYRYRILIIANKKFNLQKYLKFWLSLIKIPSFCHLKIDIDPKSFY | Involved in the restart of stalled replication forks. Recognizes and binds the arrested nascent DNA chain at stalled replication forks. It can open the DNA duplex, via its helicase activity, and promote assembly of the primosome and loading of the major replicative helicase DnaB onto DNA. | Q92HH1 |
Q496J9 | SV2C_HUMAN | Synaptic vesicle glycoprotein 2C | Homo | MEDSYKDRTSLMKGAKDIAREVKKQTVKKVNQAVDRAQDEYTQRSYSRFQDEEDDDDYYPAGETYNGEANDDEGSSEATEGHDEDDEIYEGEYQGIPSMNQAKDSIVSVGQPKGDEYKDRRELESERRADEEELAQQYELIIQECGHGRFQWALFFVLGMALMADGVEVFVVGFVLPSAETDLCIPNSGSGWLGSIVYLGMMVGAFFWGGLADKVGRKQSLLICMSVNGFFAFLSSFVQGYGFFLFCRLLSGFGIGGAIPTVFSYFAEVLAREKRGEHLSWLCMFWMIGGIYASAMAWAIIPHYGWSFSMGSAYQFHSWRVFVIVCALPCVSSVVALTFMPESPRFLLEVGKHDEAWMILKLIHDTNMRARGQPEKVFTVNKIKTPKQIDELIEIESDTGTWYRRCFVRIRTELYGIWLTFMRCFNYPVRDNTIKLTIVWFTLSFGYYGLSVWFPDVIKPLQSDEYALLTRNVERDKYANFTINFTMENQIHTGMEYDNGRFIGVKFKSVTFKDSVFKSCTFEDVTSVNTYFKNCTFIDTVFDNTDFEPYKFIDSEFKNCSFFHNKTGCQITFDDDYSAYWIYFVNFLGTLAVLPGNIVSALLMDRIGRLTMLGGSMVLSGISCFFLWFGTSESMMIGMLCLYNGLTISAWNSLDVVTVELYPTDRRATGFGFLNALCKAAAVLGNLIFGSLVSITKSIPILLASTVLVCGGLVGLCLPDTRTQVLM | (Microbial infection) Possible receptor for C.botulinum neurotoxin type D (BoNT/D, botD); note that type D does not usually infect humans. | Q496J9 |
Q3APJ2 | RL15_CHLCH | 50S ribosomal protein L15 | Chlorobium | MNLSSLRPAKGSVRNKKRVGRGQGSGNGTTAGKGNKGQQARSGYKRPIIEGGQVPVYRRLPKFGFTSRSRKTITTINLLQIEQWLEQGVVSNELTVQDFKTLLHASNTDYFKVLGAGEVTQPITITAHFFSKSAEEKIAAAGGKTIIAFRTLAEAVNIKGLPIEEALLKEKVKLVKVKKAKPTA | Binds to the 23S rRNA. | Q3APJ2 |
Q92CH2 | MURI_LISIN | Glutamate racemase | Listeria | MKQAIGFIDSGVGGLTVVREVLKQLPHEQVYYLGDTARCPYGPRDKEEVAQFTWEMTNFLVDRGIKMLVIACNTATAAALYDIREKLDIPVIGVIQPGSRAALKATRNNKIGVLGTLGTVESMAYPTALKGLNRRVEVDSLACPKFVSVVESGEYKSAIAKKVVAESLLPLKSTKIDTVILGCTHYPLLKPIIENFMGDGVAVINSGEETASEVSALLDYHNLLDATDDEIEHRFFTTGSTQIFKDIAKDWLNMPDMTVEHIKLGK | Provides the (R)-glutamate required for cell wall biosynthesis. | Q92CH2 |
B0TAH2 | DUT_HELMI | dUTP pyrophosphatase | Heliomicrobium | MKVQIKRLHPEAMIPERQTKLASGFDLHVLDAVLPENASDPYYDHFEAIRIFPGERILVRTGIAIQMGEGMEAQVRPRSGLALRHGITLLNSPGTVDADYTGDVGVILINLGDKHVDIRKKDRVAQLVFQPVFHQVELEERESLNETERGDGGFGHTGVNSQP | This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA. | B0TAH2 |
Q9JZG6 | CRCB_NEIMB | Putative fluoride ion transporter CrcB | Neisseria | MLSNIIPLSIGAALGATARWLLNLAVPASIPPATGNLFANWIGAFLIGIFAETVNHPQWKLLLITGFLGSLTTLSGFSLETVTLLQLNRPASALANIFLHTAGSLLLTWLGLKIGAAVK | Important for reducing fluoride concentration in the cell, thus reducing its toxicity. | Q9JZG6 |