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
|
|---|---|---|---|---|---|---|
Q9PJL1
|
LPXA_CHLMU
|
Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase
|
Chlamydia
|
MTNIHPTAIVEDGAQIGNNVTIEPYAIVKKNVKLCDDVVVKSYAYIDGFTTIGRGTTIWPSAMIGNKPQDLKFKGEKTFVEIGEHCEIREFAMITSSTFEGTTVSIGNNCLIMPWAHIAHNCSVGNNVVFSTHVQLAGHVQVGDCVTIGSMVGVHQFVRIGSYAMVGAMSGIRRDIPPFTIGTGNPYALGGVNKVGLQRRRVPFETRLALIKTFKRVFRSGESFQDSLGSVLEDFGDVPEVRHFVEFCRQPSKRGIERGIDCEASLDEPIDKKEGAFVES
|
Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
|
Q9PJL1
|
Q2SWZ7
|
EFTS_BURTA
|
Elongation factor Ts
|
pseudomallei group
|
MAAITASMVAELRAKTDAPMMECKKALTEADGDMAKAEELLRVKLGNKASKAASRVTAEGVVASFVGANAGALVELNCETDFVAKNDDFNAFAKTVAELVATQNPADVAALSALPLDGKTVDEVRLALVGKIGENISIRRFVRFETSNKLATYLHGSRIGVIVEYTGEQEQVGKDVAMHVAAMKPVSLSSDDVPAELIEKERRVAEQKAAESGKPAEIVAKMVDGSVQKFLKEVSLLNQPFVKNDKQTIEQMLKASNAAVQKFALFVVGEGIEKRQDDFAAEVAAQVAAAKQQ
|
Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome.
|
Q2SWZ7
|
Q2FVF0
|
CNTD_STAA8
|
Metal-staphylopine import system ATP-binding protein CntD
|
Staphylococcus
|
MTLLTVKHLTITDTWTDQPLVSDVNFTLTKGETLGVIGESGSGKSITCKSIIGLNPERLGVTGEIIFDGTSMLSLSESQLKKYRGKDIAMVMQQGSRAFDPSTTVGKQMFETMKVHTSMSTQEIEKTLIEYMDYLSLKDPKRILKSYPYMLSGGMLQRLMIALALALKPKLIIADEPTTALDTITQYDVLEAFIDIKKHFDCAMIFISHDLTVINKIADRVVVMKNGQLIEQGTRESVLHHPEHVYTKYLLSTKKKINDHFKHVMRGDVHD
|
Part of the ABC transporter complex CntABCDF (Opp1) involved in the uptake of metal in complex with the metallophore staphylopine (StP). Involved in the import of divalent metals ions such as nickel, cobalt and zinc. Probably responsible for energy coupling to the transport system . Plays a major role in nickel/cobalt import in zinc-depleted conditions. Contributes to virulence. Required for full urease activity in vitro .
|
Q2FVF0
|
B6I6W8
|
KDUI_ECOSE
|
DKI isomerase
|
Escherichia
|
MDVRQSIHSAHAKTLDTQGLRNEFLVEEVFVADEYTMVYSHIDRIIVGGIMPITKTVSVGGEVGKQLGVSYFLERRELGVINIGGAGTITVDGQCYEIGHRDALYVGKGAKEVVFASIDTATPAKFYYNCAPAHTTYPTKKVTPDEVSPVTLGDNLTSNRRTINKYFVPDVLETCQLSMGLTELAPGNLWNTMPCHTHERRMEVYFYFNMDDDACVFHMMGQPQETRHIVMHNEQAVISPSWSIHSGVGTKAYTFIWGMVGENQVFDDMDHVAVKDLR
|
Catalyzes the isomerization of 5-dehydro-4-deoxy-D-glucuronate to 3-deoxy-D-glycero-2,5-hexodiulosonate.
|
B6I6W8
|
O61374
|
SXL_CERCA
|
CCSXL
|
Ceratitis
|
MYGNMNNGGHAPYGYNGYRPSGGRMWGMSHSLPSGMSRYAFSPEDTDFTSSYPGPSMNRRGGYNDFSGGGGGGGGTMGSMNNMVNAASTNSLNCGGGGGRDGHGGGSNGTNLIVNYLPQDMTDRELYALFRTIGPINTCRIMRDYKTGYSFGYAFVDFAAETDSQRAIKSLNGITVRNKRLKVSYARPGGESIKDTNLYVTNLPRTITDDQLDTIFGKYGMIVQKNILRDKLTGKPRGVAFVRFNKREEAQEAISALNNVIPEGASQPLTVRLAEEHGKAKAQHYMSQLGLIGGGGGGGGGGGGGGGGMGGPPPPPMNMGYNNMVHRGRQNKSRFQKMHPYHNAQKFI
|
Unknown; apparently not involved in somatic sex determination.
|
O61374
|
B0TQA7
|
GLMM_SHEHH
|
Phosphoglucosamine mutase
|
Shewanella
|
MKQRQFFGTDGIRGKVGAGKMTPELALKLGWAAGRVLSRSGTQKVIIGKDTRISGYLFESALEAGLSAAGLDVMLIGPMPTPAVAYLTRTFRAEAGIVISASHNPYYDNGIKFFANDGSKLDDEVELEIEAELDKPLTCVESHELGKVVRIDDAAGRYIEYCKGHFPAEQTLSGLKIVVDCAHGATYHIAPSVFKELGAEVIAIGDKPNGLNINDKVGATSMGQICETVLAENADLGIALDGDGDRIMMVNRHGRVIDGDEILYILACDAQKRGVLRGGVVGTLMSNLGLDLALQALDIPFVRSKVGDRYVMELLKEHDWRIGGENSGHILNLDHGTTGDGIVAGILVLAAMQRQNATLEELTADIKMLPQVLVNVRFEGDNDPLVSEIVLAAKAEVEQKLGARGRVLLRKSGTEPLLRVMVEGDEQEAVTEYAHYIADAVRNLV
|
Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate.
|
B0TQA7
|
Q6G2Q2
|
MRAY_BARHE
|
UDP-MurNAc-pentapeptide phosphotransferase
|
Bartonella
|
MMLFFSSLSDWLPGVSVFRYITFRTIAAMLTSGLIVFLFGPSIIISLKLRQGKGQPIRADGPQTHFKKAGTPTMGGLMILSGIVVSAFLWCNLSNIYFWVSLFVMLSFGMIGFYDDYLKVTKQTEKGFSGKARLSLEFLVAAIAAFVFLQVGSPGLALPFVKDYFINLSWFFIPFSAFVIVATGNAVNLTDGLDGLAIVPVMVAALSFALIAYLSGNINFADYLQIHYVSGTGELAVLLGAVVGAGLGFLWFNAPPAAIFMGDTGSLALGGLLGSVAVATKHEIVLALIGGLFALEGFSVVIQVGYFKLTKKRAFLMAPIHHHFEKKGWTESQVVIRFWIISIVLALIGLSTLKLR
|
Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I.
|
Q6G2Q2
|
Q4K5I3
|
MIAB_PSEF5
|
tRNA-i(6)A37 methylthiotransferase
|
Pseudomonas
|
MAKKLYIETHGCQMNEYDSSRMVDLLGEHQALEVTARAEDADVILLNTCSIRERAQDRVYSQLGRWRELKLANPDMVIAVGGCVASQEGAAIRDRAPYVDVVFGPQTLHRLPEMIDVARITKLPQVDVSFPEIEKFDHLPEPRIDGPSAYVSVMEGCSKYCTFCVVPYTRGEEVSRPFDDVIAEIIHLAENGVREVTLLGQNVNGYRGQTHDGRMADLAELIRVVAAIDGIERIRYTTSHPLEFSDSLIQAHAEVPELVKHLHLPVQSGSDRILAAMKRNHTALEYKSKLRKLRAAVPGICISSDFIVGFPGETEKDFQQTMKLIEDVGFDFSYSFVYSQRPGTPAADLADETPEAVKKERLNALQHRLNQQGFEISRQMVGSTQRILVTDYSKKDPGELQGRTENNRIVNFRCDNPTLIGQFADVYIDSAQPHSLRGSLLQ
|
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.
|
Q4K5I3
|
Q9AKE4
|
DAPA_RICTY
|
4-hydroxy-tetrahydrodipicolinate synthase
|
typhus group
|
MYNIFKGLITALITPFKNNKLDLYAFESILNQQIKHEVDAVLIAGSTGEANSLSFEEYKLLLKTSVEIVNNRMPIISGCSSNNTAYAIELAIASKKIGVDGFMASPPSYVKPTQHGIYKHFEALHEACNLPIMLYSAPTRSGVDFSDETILRLSKLPRILALKDCGVDLERPMRIRAIVKEDFNILTGNDEVVLAFHAQGVIGWISVTSNIAPKICKELLDKWYNNDIQGALEMHQKLLPLYKALFLESNPIPVKYAAHYLGLCENEIRLPLTEASDSAKKQIKKIITSLSIKI
|
Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
|
Q9AKE4
|
A1BEI1
|
KATG_CHLPD
|
Peroxidase/catalase
|
Chlorobium
|
MSEQSKCPVTGRTAGNPVAGGSMLNRDWWPNQLHLDMLHQHSSLVNPMGDEFRYKEEFRKLDLGAVKKDLYALMTDSQEWWPADYGHYGGLFIRMAWHSAGTYRTSDGRGGGGRGNQRFAPLNSWPDNANLDKARRLLWPIKQKYGKMLSWADLMILAGNCALESMGFKTFGFGGGRVDIWEPEEDIYWGKEVEWLGNNRYSGERDLENPLAAVQMGLIYVNPEGPDGNPDPVAAGRDIRETFARMAMNDEETVALVAGGHTFGKCHGVGDPNLIGPEPEAAGIEEQGLGWKSGYGSGKGDETMTSGLEGAWTPDPIHWDMGYLGMLFKYEWELTKSPAGAWQWKPKDVAEEDLAPAAHDPSKRVPTMMTTADLAMRMDPVYGPISRRYYEHPDQFADAFARAWFKLTHRDMGPKSRYLGAEVPAEDLIWQDPVPAVDHELIGEGEIAELKKRLLASGLPIPELVSTTWASASTFRGSDKRGGANGSRIRLAPQKDWEVNQPEQLQRVLEKLEEIRHAFNGEQSGGKRVSLADLIVLGGCAAVEEAARRAGNDVTIPFAPGRTDASQAETDVESFAVLEPLADGFRNYARQKYSVTPEEMLVDRSQLLTLTATEMTVLLGGLRVLGANFRQSPHGVFTKRHETLTNDFFVNLLDMGTEWKPVSKEHDTFEGRDRKTGEPRWSATRVDLIFGSNARLRAIAEVYGSDDAQEKFVQDFVAAWNKVMNLDRFEIS
|
Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity.
|
A1BEI1
|
Q92540
|
SMG7_HUMAN
|
SMG-7 homolog
|
Homo
|
MSLQSAQYLRQAEVLKADMTDSKLGPAEVWTSRQALQDLYQKMLVTDLEYALDKKVEQDLWNHAFKNQITTLQGQAKNRANPNRSEVQANLSLFLEAASGFYTQLLQELCTVFNVDLPCRVKSSQLGIISNKQTHTSAIVKPQSSSCSYICQHCLVHLGDIARYRNQTSQAESYYRHAAQLVPSNGQPYNQLAILASSKGDHLTTIFYYCRSIAVKFPFPAASTNLQKALSKALESRDEVKTKWGVSDFIKAFIKFHGHVYLSKSLEKLSPLREKLEEQFKRLLFQKAFNSQQLVHVTVINLFQLHHLRDFSNETEQHTYSQDEQLCWTQLLALFMSFLGILCKCPLQNESQEESYNAYPLPAVKVSMDWLRLRPRVFQEAVVDERQYIWPWLISLLNSFHPHEEDLSSISATPLPEEFELQGFLALRPSFRNLDFSKGHQGITGDKEGQQRRIRQQRLISIGKWIADNQPRLIQCENEVGKLLFITEIPELILEDPSEAKENLILQETSVIESLAADGSPGLKSVLSTSRNLSNNCDTGEKPVVTFKENIKTREVNRDQGRSFPPKEVRRDYSKGITVTKNDGKKDNNKRKTETKKCTLEKLQETGKQNVAVQVKSQTELRKTPVSEARKTPVTQTPTQASNSQFIPIHHPGAFPPLPSRPGFPPPTYVIPPPVAFSMGSGYTFPAGVSVPGTFLQPTAHSPAGNQVQAGKQSHIPYSQQRPSGPGPMNQGPQQSQPPSQQPLTSLPAQPTAQSTSQLQVQALTQQQQSPTKAVPALGKSPPHHSGFQQYQQADASKQLWNPPQVQGPLGKIMPVKQPYYLQTQDPIKLFEPSLQPPVMQQQPLEKKMKPFPMEPYNHNPSEVKVPEFYWDSSYSMADNRSVMAQQANIDRRGKRSPGVFRPEQDPVPRMPFEKSLLEKPSELMSHSSSFLSLTGFSLNQERYPNNSMFNEVYGKNLTSSSKAELSPSMAPQETSLYSLFEGTPWSPSLPASSDHSTPASQSPHSSNPSSLPSSPPTHNHNSVPFSNFGPIGTPDNRDRRTADRWKTDKPAMGGFGIDYLSATSSSESSWHQASTPSGTWTGHGPSMEDSSAVLMESLKSIWSSSMMHPGPSALEQLLMQQKQKQQRGQGTMNPPH
|
Plays a role in nonsense-mediated mRNA decay. Recruits UPF1 to cytoplasmic mRNA decay bodies. Together with SMG5 is thought to provide a link to the mRNA degradation machinery involving exonucleolytic pathways, and to serve as an adapter for UPF1 to protein phosphatase 2A (PP2A), thereby triggering UPF1 dephosphorylation.
|
Q92540
|
O18823
|
AOAH_RABIT
|
Acyloxyacyl hydrolase large subunit
|
Oryctolagus
|
MKSPWRILVVSPLLLLPLHSSTSRAHDNQPGTIRSDHYTCVGCVLVVSVIEQLAQVHNSTVQASMERLCSYLPEEWVLKTACYMMVHVFGADIIKLFDKDVNADVVCHTLEFCKQEPGQPLCHLYPLPKESWKFTLEKARHIVKQSPIMKYTRSGAGICSLPFLAKICQKIKLAIKNSVPIKDVDSDKYSIFPTLRGYHWRGRDCNDSDKTVYPGRRPDNWDAHRDSNCNGIWGVDPKDGIPYEKKFCEGSQPRGIILLGDSAGAHFHIPPEWLTVSQMSVNSFLNLPTAVTNELDWPQLSGTTGFLDSASKIKENSIYLRLRKRNRCNHRDYQNISKNGASSRNVKSLIESLSRNQLLDHPAIVIYAMIGNDVCNGRKTDPVSAMTTPEQLYANVLKMLEALNSHLPTGSHVILYGLAHGAFLWDTLHSRYHPLGQLNKDVTYTQLYSFLGCLQVSPCPGWMSANETLRALTSERAQQLSETLRKIAASKKFTNFNLFYLDFAFQEVVEEWQKMGGQPWELIEAVDGFHPNEVALLLFADQLWEKVQRQWPDVLGKENPFNPQIEEVFGDQGGH
|
Removes the secondary (acyloxyacyl-linked) fatty acyl chains from the lipid A region of bacterial lipopolysaccharides (LPS). By breaking down LPS, terminates the host response to bacterial infection and prevents prolonged and damaging inflammatory responses. In peritoneal macrophages, seems to be important for recovery from a state of immune tolerance following infection by Gram-negative bacteria.
|
O18823
|
P77768
|
RPNB_ECOLI
|
Recombination-promoting nuclease RpnB
|
Escherichia
|
MTISTTSTPHDAVFKSFLRHPDTARDFIDIHLPAPLRKLCDLTTLKLEPNSFIDEDLRQYYSDLLWSVKTQEGVGYIYVVIEHQSKPEELMAFRMMRYSIAAMQNHLDAGYKELPLVLPMLFYHGCRSPYPYSLCWLDEFAEPAIARKIYSSAFPLVDITVVPDDEIMQHRKMALLELIQKHIRQRDLLGLVDQIVSLLVTGNTNDRQLKALFNYVLQTGDAQRFRAFIGEIAERAPQEKEKLMTIADRLREEGAMQGKHEEALRIAQEMLDRGLDRELVMMVTRLSPDDLIAQSH
|
A low activity DNA endonuclease yielding 3'-hydroxyl ends (Probable). Upon expression enhances RecA-independent DNA recombination 19-fold, concomitantly reducing viability by 98% and inducing DNA damage as measured by induction of the SOS repair response.
|
P77768
|
B3QQY0
|
RNH2_CHLP8
|
Ribonuclease HII
|
Chlorobaculum
|
MLSTEFETPLWENLSRVCGIDEAGRGPLAGPVVAAAVAFPRHFKPTGILEKLDDSKKLTAELREELAPAIRESAEAWAVAVVDAEIIDRINILQATMLAMNQAVESLAATPELLLVDGNRFRPVLPIPYQTIVKGDSKVFSIAAASVLAKTRRDELMVAYAAEYPAYGFDLHFGYPTARHVEAIARHGRCAIHRKSFKLRKLGEK
|
Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
|
B3QQY0
|
A3CXI2
|
RADB_METMJ
| null |
Methanoculleus
|
MKTDRVSTGSTAFDDLLGGGLERRAITQIYGEPASGKSTLCLMAAVATLRAGNSVVYIDTEGFSVERFTQIAGENAGTLADRLYLFEPLDFAQQGTMIADAEGLLKNGHAPVGLLVMDSATALYRTELDLGREAIRKLSHHMIKLLGLAKKYDIPVLITNQIYMDVERDRVAGLGGTALEHLSKAIIRLEKKDSARRAMLRKHRSRPEGLSFDFTITEDGIRTV
|
Involved in DNA repair and in homologous recombination. May regulate the cleavage reactions of the branch-structured DNA. Has a very weak ATPase activity that is not stimulated by DNA. Binds DNA but does not promote DNA strands exchange.
|
A3CXI2
|
P48282
|
CAH1_SHEEP
|
Carbonic anhydrase I
|
Ovis
|
MASPDWGYDGENGPEHWCKLHPIANGNNQSPIDIKTSETKRDPSLKPLSISYNPATAKEIVNVGHSFHVNFEDSDNRSVLKGGPLPESYRLRQFHFHWGSTDDCGSEHLVDGATFSAELHLVHWNSAKYPSFADAASQADGLVVVGVLMKVGQANPNLQKVLDALKTVKTKNKKAPFTNFDPSVLLPSCPDYWAYFGSLTHPPLHESVTWIIFKETISVSAEQLAQFRSLLANAEGDKEVCIKQNYRPPQPLKGRTVKASF
|
Catalyzes the reversible hydration of carbon dioxide.
|
P48282
|
Q96R69
|
OR4F4_HUMAN
|
Olfactory receptor OR19-3
|
Homo
|
MVTEFIFLGLSDSQELQTFLFMLFFVFYGGIVFGNLLIVITVVSDSHLHSPMYFLLANLSLIDLSLSSVTAPKMITDFFSQRKVISFKGCLVQIFLLHFFGGSEMVILIAMGFDRYIAICKPLHYTTIMCGNACVGIMAVAWGIGFLHSVSQLAFAVHLPFCGPNEVDSFYCDLPRVIKLACTDTYRLDIMVIANSGVLTVCSFVLLIISYTIILMTIQHCPLDKSSKALSTLTAHITVVLLFFGPCVFIYAWPFPIKSLDKFLAVFYSVITPLLNPIIYTLRNKDMKTAIRRLRKWDAHSSVKF
|
Odorant receptor.
|
Q96R69
|
Q9T467
|
CHLB_NEPOL
|
Light-independent protochlorophyllide reductase subunit B
|
Nephroselmis
|
MKLAYWMYAGPAHLGVLRVASSFKNVHAIMHAPLGDDYFNVMSSMLERDRDFTPVTASIVDRHVLATGSQRKVVATIHRKDQEDEPDLILVTPTCTSSILQEDLGNYVARAAPYTKSEVLLADVQHYRIHELQAQDRILEQVVRHIMDPERQKGTLDTTPTPTPSANLIGFFDLGFHHRDDSRELRRLLHGLGIEINSVLPKGGSIPDLHQLAKAWFNIIPYREAGLMTAKYLEESFHIPYIDRTPIGLIETRKFIGEIEAILQTRGVDRHEYYEKFIIHHETIVSQAAWFARSIDCQNLLGKRVIVFGDCTHAATITKLLVRELGIHVVCAGTYCKYDEAWFREQVNGYVDEILITEDHTQVADTISRLEPAAIFGTQMERHVGKRLDIPCGVISAPAHIQNFPLSFRPFLGYEGTNVVADLIYNTFRLGMEDHLLELFGGHDTKQIGESQMAESISNSKGCQWTPEAEKELAHIPRFVRSKVKRATERFAQEHGYPVINLECIYLAKQSTSVDIETIQHLLFNDETEVQ
|
Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (ChlN-ChlB) is the catalytic component of the complex.
|
Q9T467
|
Q6AZV1
|
HS90B_XENLA
|
Heat shock cognate protein HSP 90-beta
|
Xenopus
|
MPEVAHNGEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNASDALDKIRYESLTDPSKLDSGKDLKIDIIPNRLERTLTMIDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVVVITKHNDDEQYAWESSAGGSFTVKVDTGEPIGRGTKVILHLKEDQTEYLEEKRVKETVKKHSQFIGYPITLYLEKEREKEISDDEAEEEKEEKKEEEGENDKPKIEDVGSDEEEEGKDKKKKTKKIKEKYIDQEELNKTKPIWTRNPDDITQEEYGEFYKSLTNDWEDHLAVKHFSVEGQLEFRALLFIPRRAPFDLFENKKKKNNIKLYVRRVFIMDSCDELIPEYLNFVRGVVDSEDLPLNISREMLQQSKILKVIRKNIVKKCLELFCELAEDKENYKKFYEGFSKNLKLGIHEDSTNRKKLSELLRYHTSQTGDEMASLTEYVSRMKENQKSIYYITGESKDQVANSAFVERVRKRGFEVVYMTEPIDEYCVQQLKEFDGKTLVSVTKEGLELPEDEEEKKTMEENKTKFESLCKLMKEILDKKVEKVTVSNRLVSSPCCIVTSTYGWTANMERIMKAQALRDNSTMGYMMAKKHLEINPEHPIVETLRQKADTDKNDKAVKDLVVLLFETALLSSGFSLDDPQTHSNRIYRMIKLGLGIDDDDAPIEEASPSVPDDIPPLEGEEDASRMEEVD
|
Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself. Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone. After the completion of the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle.
|
Q6AZV1
|
B1MYC1
|
CCA_LEUCK
|
tRNA-NT
|
Leuconostoc
|
MKISTLPQEFMQAQPILEHIESAGFEAYFVGGAVRDMLLNKPIHDVDIATSAFPEEIKALFTKTVDTGIQHGTVMVLDHGDGYEITTFRTESTYTDFRRPDKVTFVRSLAEDLKRRDFTINAIAMTKDGDIIDLFDGLTDMAQKRIRAVGDAEVRFNEDALRIMRALRFSAQLGFDIAPHTKAALKQIGRNLEKIAVERIRVEFEKLLMGQYASNSLSVAIEADLIRYLPGHIKKEDWLTITADLKRNQPQARTVIWPYFLSRLSLRLNELQLFMRSWKTSREDMRAVLSIVPIVKHVQTVSVFELYAIYDYQALLFEVLTLIGTPLATQQRVKQIFDALPITHNRDMCISGGDLLANNIVTPGPQMGRILTQLEHAVIQRIISNRPDSLLEYAKELVDNEKN
|
Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate.
|
B1MYC1
|
A3NXT4
|
RSGA_BURP0
|
Small ribosomal subunit biogenesis GTPase RsgA
|
pseudomallei group
|
MKRAPTKQPAKPAARGGERAQGRVIAAHGRHYIVAPADGGPMLQCFPRGKKSEVAVGDRVAYERTSADQGVIVEIGERRNLLYRSDQFKSKLFAANLDQLLIVLATEPYFSEDLLGRALIAAEANELKPIVVLNKIDVEAALPVARERLAPYRALGYDVLELSVKGAPDDARAQLAPRLAGHSTILLGQSGMGKSTLVNLLVPDAEAATREISAALNSGRHTTTFTRLYPLQDGGALIDSPGFQEFGLYHLTEGRLERAFPEFRPLLAHCRFYNCHHLHEPGCAILEALADGRIAPTRHALYAQLVHEASQIVR
|
One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Helps release RbfA from mature subunits. May play a role in the assembly of ribosomal proteins into the subunit. Circularly permuted GTPase that catalyzes slow GTP hydrolysis, GTPase activity is stimulated by the 30S ribosomal subunit.
|
A3NXT4
|
Q604U6
|
SMC_METCA
|
Chromosome partition protein Smc
|
Methylococcus
|
MRLEKLKIAGFKSFVDPTTLPLPGNLVGVVGPNGCGKSNVIDAVRWVMGESSARHLRGETMADVIFNGSSTRKPASQASVELVFDNSSGRAGGEYARYQQIAIRRQVARDGQSSYFLNGTRCRRKDITDLFLGTGLGARSYAIIEQGTISRLIEAKPEEMREIIEEAAGISKYKERRHETEQRMRHTRENLERLADLREELGRQLGHLQRQARKAEKFIALRDEERRLKLELLGLRWRALERQLDRLKAELTDSEERFRRLTGEEHACETQLEGLNRLRGVAQEKLDVQQGRFYELGAEISRLDQFIRHTQKSRAELVQERERVEAELRKVESDRDDDRLRLEAVRAEAAELKGKLASLEQEVAEAVSVRQAAEAKLKTCREGWEALAGDRHRLEGQAALQRSRLQQLREHGQQLGGRRQRLLQQQSELEKALAALDVQAHRLEVAGIEAEREETVGAVEALAREAERQRDRLRFARERLNPARAGLHAVQGKVASLETLQRHAMGRDRSAAAAVLEAWQLSAADRLGEKIEVAPGWENAVETVLGAHLEAVCVDSLAPYLANLQAQEPAEFLALCEYRQGPVAEGTGGPRLLDYIRAPLALEGLLAGIYCASDPAEAAERARSLQPHESVVTPGGFRIGKGWVLAQKPDAGHAGALARERELRECRRRVEELEAQCRILEREASEAEVELERLESEGREARKKADELSAGLSLARSELAAAEARSEQWRHRLDQLSHELNELADQELELAEKRAEAEEALQTAERDSLRLQDVAAQRKGEWLALEEAFAAAEAAEKSLHEEVRALRSRAAMLESNAALTAAHLQRLEQQHGQTADRLAAIVQRLAESQTPLEDERSRLDALTEERGVLEAEMARQRRRLSELEADVRRVAGERQRAEHELAALRESIGQMKLAWQTAEVRRQGIEEQFAELGAAPAAVVAGLPEDAEESAWQASVIRLGEEIERLGPVNLTAMQEYQEQEARQRYLEEQDRDLTESLATLEQAIEKIDRECRARFKETFEKINAGFQRMFPKLFGGGKAALELTENNLLSAGVSVMAQPPGKRNSSIHLLSGGEKALTAAALVFAIFELNPAPFCLLDEVDAPLDDANVGRFSQLVKEMSEKVQFLFITHNKATMEIAQYLAGVTMREPGVSRIVTVDIDAAVELASV
|
Required for chromosome condensation and partitioning.
|
Q604U6
|
Q0VN64
|
YBEY_ALCBS
|
Endoribonuclease YbeY
|
Alcanivorax
|
MNGIPTPTVDIQWASDAPDAPDETHLCEWVRHAAIAAGGVVGDITLRIVDEEEIRTLNRDYRDKDAPTNVLSFPFEMPEGLPEGAMDPLVGDIIICAAVVRREANEQHKPLVAHWAHMVTHGVLHLLGYDHIDDDDAIVMETLEIRALGELGFPDPYSPAQQESQAQPENTELNP
|
Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
|
Q0VN64
|
A8A1X1
|
RCNA_ECOHS
|
Nickel/cobalt efflux system RcnA
|
Escherichia
|
MTEFTTLLQQGNAWFFIPSVILLGALHGLEPGHSKTMMAAFIIAIKGTIKQAVMLGLAATISHTAVVWLIAFGGMVISKRFTAQSAEPWLQLISAVIIISTAFWMFWRTWRGERNWLENMHGHDYEHHHHDHEHHHDHGHHHHHEHGEYQDAHARAHANDIKRRFDGREVTNWQILLFGLTGGLIPCPAAITVLLICIQLKALTLGATLVVSFSIGLALTLVTVGVGAAISVQQVAKRWSGFNTLAKRAPYFSSLLIGLVGVYMGVHGFMGIMR
|
Efflux system for nickel and cobalt.
|
A8A1X1
|
Q7MPA3
|
MURA_VIBVY
|
UDP-N-acetylglucosamine enolpyruvyl transferase
|
Vibrio
|
MEKFRVIGSTQPLMGEVTISGAKNAALPILFASILAEEPVEVANVPHLRDIDTTMELLKRLGAKVERNGSVHVDPSSIDEYCAPYDLVKTMRASIWALGPLVARFGQGQVSLPGGCAIGARPVDLHITGLEQLGATITLEDGYVKAHVDGRLQGAHIVMDKVSVGATITIMCAATLAEGTTVLDNAAREPEIVDTAKFLNTLGAKISGAGTDTITIEGVERLGGGKHAVVADRIETGTFLVAAAVSGGKVVCHNTQAHLLEAVLAKLEEAGALVETGEDWISVDMTGRELKAVNIRTAPHPGFPTDMQAQFTLLNMMAKGGGVITETIFENRFMHVPELKRMGAKAEIEGNTVICGDVERLSAAQVMATDLRASASLVIAGCIAKGETIVDRIYHIDRGYDKIENKLNALGAKIERFRESN
|
Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine.
|
Q7MPA3
|
Q47WD4
|
SELO_COLP3
|
Protein adenylyltransferase SelO
|
Colwellia
|
MSLILSNNYQALGESFSQQTLPAPVGQPSLLLWNEPLAKALTIPFTKDNDAELLSQYFSGNQLIEGSKPVAQAYSGHQFGHFNPQLGDGRAHLLGDIADTQGQRWDIQLKGSGVSDFSRQGDGRCALGPALREYIMSEAMFALGVPTTRCLAVVTTGENVYRERPYDGAVVTRIAASHIRVGTFQYFAARGDTDSLKKLTNYAINRHFPELIANSSENSSDNSDALKADNVISSQQVLEFFSAVLSKQIPLVLSWLRVGFIHGVMNTDNTTISGETIDYGPCAMMNAYHPETVFSSIDRNSRYAFGKQISIMQWNMTRLAETLLPLVDSDEDDAVEKIEPLLTQFHQDLQQGYLTMMAAKIGIDEPAEGDGKLINDLITLMKEQKLDYTQTFTALTDSLNDNTTEEPLTDVLNEWLPHWNSRIESFKSSAHTLMVSNNPIVIPRNHHVEAFLDSCQETGDLTALNKFLAVLRQPYTEIAETKNYQDAPVDGDKDYHTFCGT
|
Catalyzes the transfer of adenosine 5'-monophosphate (AMP) to Ser, Thr or Tyr residues of target proteins (AMPylation).
|
Q47WD4
|
O60504
|
VINEX_HUMAN
|
Sorbin and SH3 domain-containing protein 3
|
Homo
|
MQGPPRSLRAGLSLDDFIPGHLQSHIGSSSRGTRVPVIRNGGSNTLNFQFHDPAPRTVCNGGYTPRRDASQHPDPAWYQTWPGPGSKPSASTKIPASQHTQNWSATWTKDSKRRDKRWVKYEGIGPVDESGMPIAPRSSVDRPRDWYRRMFQQIHRKMPDLQLDWTFEEPPRDPRHLGAQQRPAHRPGPATSSSGRSWDHSEELPRSTFNYRPGAFSTVLQPSNQVLRRREKVDNVWTEESWNQFLQELETGQRPKKPLVDDPGEKPSQPIEVLLERELAELSAELDKDLRAIETRLPSPKSSPAPRRAPEQRPPAGPASAWSSSYPHAPYLGSARSLSPHKMADGGSPFLGRRDFVYPSSTRDPSASNGGGSPARREEKKRKAARLKFDFQAQSPKELTLQKGDIVYIHKEVDKNWLEGEHHGRLGIFPANYVEVLPADEIPKPIKPPTYQVLEYGEAVAQYTFKGDLEVELSFRKGEHICLIRKVNENWYEGRITGTGRQGIFPASYVQVSREPRLRLCDDGPQLPTSPRLTAAARSARHPSSPSALRSPADPIDLGGQTSPRRTGFSFPTQEPRPQTQNLGTPGPALSHSRGPSHPLDLGTSSPNTSQIHWTPYRAMYQYRPQNEDELELREGDRVDVMQQCDDGWFVGVSRRTQKFGTFPGNYVAPV
|
Vinexin alpha isoform promotes up-regulation of actin stress fiber formation. Vinexin beta isoform plays a role in cell spreading and enhances the activation of JNK/SAPK in response to EGF stimulation by using its third SH3 domain.
|
O60504
|
Q921Q3
|
ALG1_MOUSE
|
GDP-mannose-dolichol diphosphochitobiose mannosyltransferase
|
Mus
|
MAASCVALLVLALLLLVLLLGLWKRGRQTGRARHMVVVVLGDVGRSPRMQYHALSLAQSGFSVTLLGFYNSKPRDELLQNDRIRIVKLTDLRGLGAGPRILQYGVKVVFQAVYLLWKMMRMDPAAYIFLQNPPGLPAIAVCWFVGCICGSKLVIDWHNYGYSIMGLVHGPRHPIVLLAKWYEKFFGRLSHLNLCVTNAMREDLAENWCVRAVTLYDKPASFFKETPLDLQHELFMKLSHTYSPFQSCSDPSHPDTERSAFTERDCQSGVVRRLHGRPALLVSSTSWTEDEDFSILLRALEKFEQQALTGDSLPSLVCVITGKGPLREHYRHLISQKHLQHVRFCTPWLEAEDYPLLLGSADLGVCLHMSSSGLDLPMKVVDMFGCHLPVCAVNFKCLHELVRHGENGLVFKDAEELAAQLQMLFSKFPDPAGKLSQFRKKLQESGQQRWDESWQHTVLPLLAHSQMTPRPHPPCGHPSCRGF
|
Catalyzes the addition of the first of nine mannose moieties to form a dolichol-lipid linked oligosaccharide intermediate required for proper N-linked glycosylation.
|
Q921Q3
|
P18989
|
HBB_PROLO
|
Hemoglobin beta chain
|
Procyon
|
VHLTADEKTAVTTLWGKVNVEEVGGEALGRLLVVYPWTQRFFESFGDLSSADAIMGNPKVKAHGKKVLNSFSEGLKNLDNLKGTFAKLSELHCDKLHVDPENFRLLGNVLVCVLAHHFGKEFTPPVQAAYQKVVAGVANALAHKYH
|
Involved in oxygen transport from the lung to the various peripheral tissues.
|
P18989
|
Q0BAV4
|
GATA_BURCM
|
Glutamyl-tRNA(Gln) amidotransferase subunit A
|
Burkholderia cepacia complex
|
MHAKSLTELRAALAAKECSAVELAQLYLKRIDAARDLNAFVHVDADLTLAQAKAADAELARGAGGALTGLPIAHKDVFVTRGWRSTAGSKMLANYESPFDATVVARLQAAGMVTLGKTNMDEFAMGSSNENSAFGAVKNPWDTNAVPGGSSGGSSAAVAARLAPAATGTDTGGSIRQPASFAGVTGIKPTYGRVSRYGMIAFASSLDQGGPMAQSASDCALLLNAMSGFDERDSTSLEREDEDFTRHLGQPWAAGNDAGKPLAGLRIGLPNEYFGDGLADDVRASIDAALKQYEALGATLVPVSLPKTELSIPVYYVIAPAEASSNLSRFDGVRFGHRAAQYGDLLDMYKKSRAEGFGPEVKRRILVGAYVLSHGYYDAYYLQAQKIRRIIAQDFQEAFKSCDVIMGPASPTVAWDLGSKGDDPVQMYLADIYTLSVSLAGLPGMSVPCGFGASANAKRPVGLQIIGNYFNEARMLQVADAFQRATDWHKQVPAGV
|
Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
|
Q0BAV4
|
P36618
|
CDC16_SCHPO
|
Cell division control protein 16
|
Schizosaccharomyces
|
MPSIDCKRLQKLAPKSPENQSKCISRLRYMVMLDQVESDEGGNSSTRPYVWAVLLNAPPRNADEYIRYVRQGPSPMAQKIQNDVSRTLVVESQFHSRVSQSSLSRLLNAYVWKRGALYVQGMNVLASPFLYACKSENQAFQFFDRLLQNECPLYVLPNIDGVHRGAKLLDKCLEVLDHRLYTYLLSKGLTAKIYALPSILTLSACTAPLSEALTIWDFLFAYGIHLNILCVIAQMFIFREQLIDHPSPMTLLRTFPPLNAKNIMKITILLISKLPPELYNLLARHAWDSEAGVLIDRLT
|
Has a dual role in the cell cycle. In mitosis, it is involved in maintenance of cdc2 kinase activity. It is subsequently required for regulation of septum formation. Could be involved in maintenance of cdc2 kinase activity by preventing, directly or indirectly, the degradation of cyclin or the dephosphorylation of 'Thr-167' of cdc2.
|
P36618
|
O00559
|
RCAS1_HUMAN
|
Estrogen receptor-binding fragment-associated gene 9 protein
|
Homo
|
MAITQFRLFKFCTCLATVFSFLKRLICRSGRGRKLSGDQITLPTTVDYSSVPKQTDVEEWTSWDEDAPTSVKIEGGNGNVATQQNSLEQLEPDYFKDMTPTIRKTQKIVIKKREPLNFGIPDGSTGFSSRLAATQDLPFIHQSSELGDLDTWQENTNAWEEEEDAAWQAEEVLRQQKLADREKRAAEQQRKKMEKEAQRLMKKEQNKIGVKLS
|
May participate in suppression of cell proliferation and induces apoptotic cell death through activation of interleukin-1-beta converting enzyme (ICE)-like proteases.
|
O00559
|
Q9UTP5
|
MU162_SCHPO
|
Meiotically up-regulated gene 162 protein
|
Schizosaccharomyces
|
MDDEVYKQRLTALNNLRIVIFFDILIILLGYIGTWNLKTLQLVNPSLWSFSPSLWIYIRGTVLCADCIFTAGSANEYSAVQNSVFQVSSLMFYGLMMEFFGYSFDRVGCMELAFISFSAACYFNIRSIKSLSLKNKNWTIISIIEIPIKLHFILNVLLFLKFSEYMLPLLGRVHLSYHLFALWVINLYIWIKLIDSKDFVLGFLAGLSVLLLNTGSLITAKPLISYFNLLTSCLIIFPSIWIYAIEKKNFKNLSYEDDDYRNYW
|
Has a role in meiosis.
|
Q9UTP5
|
Q9MFN9
|
CYB_COLHO
|
Ubiquinol-cytochrome-c reductase complex cytochrome b subunit
|
Cochliomyia
|
MNKPLRIKHPILSITNSALVDLPAPSNISAWWNFGSLLFLCLMIQILTGLFLAMHYTADISLAFNSVNHICRDVNYGWLLRTMHANGASFFFICIYLHVGRGIYYGSYLFTPTWLVGVIILFLVMGTAFMGYVLPWGQMSFWGATVITNLLSAIPYLGIDLVQWVWGGFAVDNATLTRFFTFHFILPFIVLAATLIHILFLHETGSNNPIGVNSNIDKIPFHPYFTFKDIVGFIMMTMILILLVLINPYLLGDPDNFIPANPLVTPVHIQPEWYFLFAYAILRSIPNKLGGVIALVLSIAILAILPFYHLSKFRGIQFYPINQILFWIMVVTVILLTWIGARPVEEPYVLVGQILTVIYFSYFMFNPLIIKWWDNLLN
|
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 then used for ATP synthesis.
|
Q9MFN9
|
B6QGW6
|
RRG9_TALMQ
|
Required for respiratory growth protein 9, mitochondrial
|
Talaromyces sect. Talaromyces
|
MAVCAASRRLTLSNVLQGVYRTELVRQHAENSAINFYAQRLTRPALTAANSNPWLSKRSFSTSQAFKDGGNIVIYDVIATKAPDGDVLTELTSTKAEDSPKTPKSPKSSSEKPKSSKTKTKAAKKSGTKYLASELVNPEKKVKRPHWQTQKEALEKKFTEGWHPRKKLPPDSLDTIRHLHATKPDVWTTPVLADQFKISPEAIRRILKSKWQPTEEERERREERWAERYKKIYSHMEELGLRRRKGEWTAKVSDARRLGLEGKSIRQNFRRKPQARPEGTEINISRPDREASPKESTSLE
|
Required for respiratory activity and maintenance and expression of the mitochondrial genome.
|
B6QGW6
|
O67216
|
DAPA_AQUAE
|
4-hydroxy-tetrahydrodipicolinate synthase
|
Aquifex
|
MFQGSIVALITPFKEGEVDYEALGNLIEFHVDNGTDAILVCGTTGESPTLTFEEHEKVIEFAVKRAAGRIKVIAGTGGNATHEAVHLTAHAKEVGADGALVVVPYYNKPTQRGLYEHFKTVAQEVDIPIIIYNIPSRTCVEISVDTMFKLASECENIVASKESTPNMDRISEIVKRLGESFSVLSGDDSLTLPMMALGAKGVISVANNVMPREVKELIRAALEGDFRRAREIHYYLHDLFKVLFIETNPIPVKTACWMLGMCEKEFRLPLTEMSPENENKLREVLKKYNLPLKN
|
Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
|
O67216
|
Q2J1I1
|
NIFH_RHOP2
|
Nitrogenase reductase
|
Rhodopseudomonas
|
MAALRQIAFYGKGGIGKSTTSQNTLAALVELGQKILIVGCDPKADSTRLILNTKMQDTVLSLAAEAGSVEDLELEDVMKIGYKGIKCTEAGGPEPGVGCAGRGVITAINFLEENGAYEDVDYVSYDVLGDVVCGGFAMPIRENKAQEIYIVMSGEMMALYAANNIAKGILKYASSGGVRLGGLICNERQTDRELDLAEALAARLNSKLIHFVPRANIVQHAELRRQTVIEYAPDSQQAQEYRQLANKIHANSGNGTIPTPITMEELEGMLLDFGIMKTDEQALAELAEKEAAKAAAATA
|
The key enzymatic reactions in nitrogen fixation are catalyzed by the nitrogenase complex, which has 2 components: the iron protein and the molybdenum-iron protein.
|
Q2J1I1
|
B3LS51
|
GMT2_YEAS1
|
Probable GDP-mannose transporter 2
|
Saccharomyces
|
MIYTSSKSLQYLAVPIYTIFKNLTIILIAYGEVLFFGGKVTSMELTSFIMMVLSSVVATWGDQQAIAIKASSLEDLDQELVESTIFVLNPGYLWMFTNCISSALFVLIMRKRIRLTNFKDYDTMFYNNVLALPLLLVFSFIMEDWSTKNLSVNLSADSLAAMVISGLMSVGISYCSGWCVRVTSSTTYSMVGALNKLPIALAGLVFFDAPKNFLSFFSIFLGFLSGLLYAVAKQKKIQQQKVLAATLEK
|
Involved in the import of GDP-mannose from the cytoplasm into the Golgi lumen.
|
B3LS51
|
Q6CPC3
|
FIP1_KLULA
|
Pre-mRNA polyadenylation factor FIP1
|
Kluyveromyces
|
MSSEDEDDKFLYSDEEDSNVVAKQEGPALKRQKVEETPKILAHDVPEGNTNEVESEASNQDSSSDEDDSSDSDSDVEIIIGTGNDTSKIDSGKSQISAITDTTPLGTADHAIAAVAGISDVVPVQEGSIPPEQQQQQQQTIDLNPDAQFDGKPIVQIDPEILKEKPWRQPGANISDYFNYGFNEQTWMEYLHRQEHLTKEYNPQKILMNLLALQQQGKLNDPGSGQPVQNTIQPPPPPMGLPPMFGGFPGFPFPGMMNNMQNQNVSSMNNMNNMNNMNNMNNINNNNNNNLNDKK
|
Pre-mRNA polyadenylation factor that directly interacts with poly(A) polymerase.
|
Q6CPC3
|
Q12EL7
|
MURD_POLSJ
|
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase
|
unclassified Polaromonas
|
MRHLQDQTVLILGLGASGLAMARWWVRHGASVTVADTREAPALLATLRQELPAVKFVSGAFTPDLVQGSAVRAVYRSPGLAPAVIAPVVDAARAMGLPVGGELDLFSRALADLREVSATEVVKDHLVPPESPLSDASDISDASDATDAVDSLEGEAALAADASGDIEEMSASDVVEGAPVSEDAGEDAALPALLAPAPAEQAAGYRPVVLAITGTNGKTTVTSLVGQLVQRAGKTVAVAGNIGPTLLDTLSAHLDADTLPQVWVLELSSFQLADAQDFEPTAAVVLNVTQDHLDWHGDMDAYVAAKARIFGRSTFMLLNRDDPRVMEMLPTPVKVRLRPPQVRPHSTFGAGEPQRPGDYGIETVNGMAWLVRAAQADETIKRRKGEEVELHIQRLMPLDALRIRGRHNATNALAALGLAVAAGCSLAPMLHGLREYRGEPHRVESIAVVNDVEYFDDSKGTNVGATAAALAGLGAERKLVVILGGEGKGQDFSPLAEPVSHHARAVVLIGKDAPLIRSALQASQVALLDAASMQEAVSLAAAQAHTGDAVLMSPACASFDMFDNYEHRAQVFCDAVQALAQEQGVVL
|
Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
|
Q12EL7
|
P0CB87
|
NDUS5_PONAB
|
NADH-ubiquinone oxidoreductase 15 kDa subunit
|
Pongo
|
MPFLDIQKRFGLNIDRWLTTQSAEQPYKMASRCHAFEKEWIECAHGIGYTRAEKECKIEYDDFIECLLRQKTMRRTGTIRKQRDKLIKEGKYTPPPHHIGKGEPRP
|
Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
|
P0CB87
|
Q8FTQ2
|
IF3_COREF
|
Translation initiation factor IF-3
|
Corynebacterium
|
MNGFLVCQRGNFLKWYGTSSFSRTANRGVHISAEARINERIRVPEVRLVGPNGEQVGIVRIEDARKLAFDADLDLVEVAPTAKPPVCKIMDYGKFKYEAAQKARESRKNQQQTVVKEQKLRPKIDDHDYETKKSNVIRFLEKGSKVKVTIMFRGREQARPELGYRLLERLANDVAEYGVVETRAKQDGRNMTMVIGPLRKGKK
|
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.
|
Q8FTQ2
|
P08468
|
PT111_YEAST
|
Protein PET111, mitochondrial
|
Saccharomyces
|
MLQRRFISSSGIKRLLHRESNKVMHTVFFKVRYYSTELIKKKHKEDIEDWVKAQLKDSSTISGVYESRNKLDWMDSITKSPSSLDILKNQYNIVKDKDFGILWKQKFESADPDILMTIISLSTNQKVLFSIQQLLILINSLHFLKRDYDIGQIYTTYEQFTPLLASHTDKGTYGQFIEIMLVVQHNLHHFDVCETLFAEYIKYCKVKPQMISLGLNSFIRSNNTQLAVEFYTQAITNPDTFPITEKQLFEFLRCMERYLDMSSMKHIFYLWLKVKCGDEQSSSTNLPSFKTLAIIHRMLLRFSNTDELNDFLTNPVVLSTGYTSSVQFELIEFCHSLYCIKGDRTKSIDDSILMERVDKFITRLNNNISTRKELYMSVVQAYVSTNNFENLKVILEKIQRDNDISIDGSFHLCISRYFVNTNQFEGLFKYYRSVVKTTDGKTRLRPAFIQQLWSCAVNVYPMLAKEITNDLLVTLKRSQYSKCLTWVYTFLQENAHIHTRKINGGEDSSLSGFNAVDFERFEEFKKKVSHNDVYGAELVISNSLKEGIAPQFSFLYSVLALCLRNSLTGLARVVDVILRTRFRYIPLKVDILWLKWEIISNYRSFEKLSAEHLKELEFKLKEFERVHQKELSVQNYLQLTQICFHTRDFKYACYLISQARKNLDTSNNKQWMMYYMTSLKLASRMHESERFSRILKDWNCNHRASLITPGCIRQIKGFMKYFEKRPAYISTAASIDNKEIKDRIDELVLRYVDYKYQGLENMRKLTLFLKEWFDEEISLLKLEQNERKMKLFEENKKEEE
|
Required for translation of the mitochondrial gene for cytochrome c oxidase subunit II (COX2).
|
P08468
|
Q5EA87
|
B4GT3_BOVIN
|
UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 3
|
Bos
|
MLRRLLERPCTLALLVGSQLAVMMYLSLGGFRSLSALFGREQEPAFDYSHPHDVYSNLSHMPGAPVAPGGLPAPQGLPYCPKRSPLLVGPISVSFSPVPSLAEIVERNPRVEPGGRYRPARCEPRSRTAIIVPHRAREHHLRLLLYHLHPFLQRQQLAYGIYVIHQAGNGTFNRAKLLNVGVREALRDEEWDCLFLHDVDLLPENDHNLYVCDPRGPRHVAVAMNKFGYSLPYPQYFGGVSALTPDQYLKMNGFPNEYWGWGGEDDDIATRVRLAGMKISRPPTSVGHYKMVKHRGDKGNEENPHRFDLLVRTQNSWTQDGMNSLTYQLLSRELGPLYTNITADIGTDPRGPRTSSGPHYPPGSSQAFRQEMLQRRPPARPGPLPTANHTAPHGSH
|
Responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids.
|
Q5EA87
|
B7UJV5
|
NANK_ECO27
|
N-acetyl-D-mannosamine kinase
|
Escherichia
|
MTTLAIDIGGTKLAAALIGADGQIRDRRELPTPASQTPQALRDALSALVSPLQAHAQRVAIASTGIIRDGSLLALNPHNLGGLLHFPLVKTLEQLTNLPTIAINDAQAAAWAEYQALDGDITDIVFITVSTGVGGGVVSGGKLRTGPGGLAGHIGHTLADPHGPVCGCGRTGCVEAIASGRGIAAAAQGELAGANAKTIFTRAGQGDEQAQQLIHRSARTLARLIADIKATTDCQCVVVGGSVGLAEGYLALVETYLAQEPEAFHVDLLAAHYRHDAGLLGAALLAQGEKL
|
Catalyzes the phosphorylation of N-acetylmannosamine (ManNAc) to ManNAc-6-P.
|
B7UJV5
|
Q8EA37
|
RIMO_SHEON
|
Ribosome maturation factor RimO
|
Shewanella
|
MTVETFHPKQTTTLETPAKTLEAASADSVNTGNVATGNRIGFVSLGCPKNLVDSERILTQLRIDGYEVTNSYDNADLVIVNTCGFIDAAVEESLDAVREALEENGKVIVTGCLGAKENQIREVHPDVLEITGPHSYEAVLKHVHKYVPKPEHNPFTSLIPQTGVKLTPKHYAYLKISEGCDNRCTFCIIPALRGDLDSRGAGSVLDEAKRLVEAGVQEILVVSQDTSAYGKDKGGRTDFWNGMPVKQDITSLARQLGKMGAWVRLHYIYPYPWVDDLIPLMAEGLILPYLDIPMQHASPRILKMMKRPGRVDRQLEAIQRWREICPDLVIRSTFIVGFPGETEEDFEMLLDFLREARLDRVGCFKYSEVEGAVANTIAELISEEVKEDRYHRFMEVQAEISAERLARFVGRTMDILIDDVDEEGAIGRSFADAPEIDGMVFINGETELEPGMLVRAVITHSDEHDLWAELVDADAEDEVEA
|
Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein S12.
|
Q8EA37
|
Q1MAC8
|
MTGA_RHIL3
|
Peptidoglycan glycosyltransferase MtgA
|
Rhizobium
|
MDIAPEREDSVDMPARRRWFEDRRVLKRIVLAVLIVLILPYALIVFYLLPFIHPVSTLMLRDLVLLRGYDRQWVSLDNIAPVVVQSVMMSEDGQYCFHGGVDWAEMRMLVEDTLKGQATRGGSTIPMQTAKNLFLWNGRSFVRKALELPLAVTTDFVLSKRRLMEIYLNIAEWGPGIYGIEAAARHHFKVPASKLTRRQASLLAVSLPNPIDRNAGKPGRGLRRLAGVIERRAQGSGDYIKCIYD
|
Peptidoglycan polymerase that catalyzes glycan chain elongation from lipid-linked precursors.
|
Q1MAC8
|
B8E2G4
|
TRMD_DICTD
|
tRNA [GM37] methyltransferase
|
Dictyoglomus
|
MLRIDIVTIFPEMFKGPFDVSILKKAQDKGLVEIKVYNLRDFTEDKHRTVDDYPYGGGSGMVMKPEPIFKAVRSLKKEDSEVILLSPSGDLFNQKIAEELSKKNHLILICGRYEGVDERVKSIITREISIGDYVLTGGEIPAMVIVDAVVRLVPGVLGDPDSLREESFQWGILEYPQYTHPRDFEGMKVPDILLSGNHERIRRWRRKEALKKTFLKRPDLLEKTSLTQEDLELLEEIKKELREEV
|
Specifically methylates guanosine-37 in various tRNAs.
|
B8E2G4
|
Q8TIJ0
|
VATB_METAC
|
V-ATPase subunit B
|
Methanosarcina
|
MVKEYKTITQIAGPLIFVEKTEPVGYNEIVNIKMTDGTVRRGQVLDSSSDIVVVQVFEGTGGLDKDCGVIFTGETLKLPASIDLLGRILSGSGDPRDGGPRIVPDQLLDINGAAMNPYARLPPKDFIQTGISTIDGTNTLVRGQKLPIFSASGLPHNEIALQIARQASVPGSESAFAVVFAAMGITNEEAQYFMSDFEKTGALERAVVFLNLADDPAVERIVTPRMALTAAEYLAYEHGMHVLVILTDITNYAEALRQMGAARNEVPGRRGYPGYMYTDLATLYERAGIVKGAKGSVTQIPILSMPGDDITHPIPDLSGYITEGQIVVARELHRKGIYPPINVLPSLSRLMNSGIGPGKTREDHKAVSDQMYAGYAEGRDLRGLVAIVGKEALSERDTKFLEFADLFEDKFVRQGRNENRTIEDTLEIGWQILTHLPENQLGRIDNKYIQKYHPAHRKAK
|
Produces ATP from ADP in the presence of a proton gradient across the membrane. The archaeal beta chain is a regulatory subunit.
|
Q8TIJ0
|
Q32223
|
RBL_EPHTW
|
Ribulose bisphosphate carboxylase large chain
|
Ephedra
|
DGFKAGVKDYRLTYYTPEYQTKDTDILAAFRVTPQPGVPPEEAGWAVAAESSTGTWTTVWTDGLTSLDRYKGRCCDIEPVPGEDNQYFAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPTAYIQTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSRAFMRWRDRFVFCAEAIYKAQAETGEIKGHYLNATSGTCEEMIKRAVFARELGVPIVMHDYLTGGFTANTTLAHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRMSGGDHIHAGTVVGKLEGEREITLGFVDLLRDDFIEKDRSRGIYFTQDWVSMPGVLPVASGGIHVWHMPALTEIFGDDAVLQFGGGTLGHPWGNAPGAVANRVALEACVQARNEGRDLAREGNEVIREACKWSPELAAACEVWKEIKFEFATVDTL
|
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.
|
Q32223
|
B9JQX0
|
TRUA_AGRVS
|
tRNA-uridine isomerase I
|
Agrobacterium
|
MPRYKLTVEYDGTPYVGWQRQDNGPSVQGALEAAVLGLTGETVAIRGAGRTDSGVHASGQVAHVDLLRQWIPYKLRNALNAHLAQAGQAISILAAEAVPDAFDARFSALKRHYLYRIMSRPSRLALEANRAWWVSKPLDHEAMHAAAQMLVGNHDFTTFRSVHCQAISPVRTLDRLDVSRNGDLIEIRASAQSFLHNQIRSFAGTLKMAGEGKMTPEDVRAALEARDRKACGPVAPPQGLYFLQVDYPTDGNWRPYSKT
|
Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
|
B9JQX0
|
B0T2E3
|
KAD_CAUSK
|
Adenylate monophosphate kinase
|
unclassified Caulobacter
|
MNLILFGPPAAGKGTQAKRLVEQRGMVQLSTGDMLRAAIASGSELGQKVKGVLDRGELVTDEIVIALIEDRLPEAEAAGGAIFDGFPRTVPQAQALDAMLARRGQKIDSVLRLKVDEPALIERISKRFAEQGRPDDNPEVFVTRLAAYNAQTAPLLPYYREQGKLTELDGMASVETVAGSIDAALSVVA
|
Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
|
B0T2E3
|
Q8R7U3
|
RL1_CALS4
|
50S ribosomal protein L1
|
Caldanaerobacter
|
MKRGKRYLENLKLYDKTQQYSSDEAMDIVLKTANAKFDETIDLAVRLGVDPRHADQQVRGTVILPHGTGKTVKVLVFAKGEKAKEAEAAGADYVGAEELVEKIQKENWFDYDVVIATPDMMGVVGRLGKLLGPKGLMPNPKSGTVTFEVEKAVKEAKAGKIEYRIDKAGIIHVPIGKKSFGKEKLLENFRTVMDAIIKSKPAAAKGQYIKSVVLSSTMGPGVKVNPARIFE
|
Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA.
|
Q8R7U3
|
A9I8B8
|
MINE_BORPD
|
Cell division topological specificity factor
|
Bordetella
|
MSFLSFLLGQKKTSAVVAKERLQIILAHERSGRGASPDYLPQLQQELVAVISKYVNINPDDIKVHLERQDTLEVLEVKIEMPQKEA
|
Prevents the cell division inhibition by proteins MinC and MinD at internal division sites while permitting inhibition at polar sites. This ensures cell division at the proper site by restricting the formation of a division septum at the midpoint of the long axis of the cell.
|
A9I8B8
|
Q4ZWS5
|
RRF_PSEU2
|
Ribosome-releasing factor
|
Pseudomonas syringae
|
MINEIKKDAQTRMQKSLESLTHAFTRIRTGKAHPSILGGVMVPYYGADTPLSQVANVTVKDSRTLQVVAFERNMLAAVDKAIQSSGLGFNPTNLGELLLISMPALTEETRKGFTKQARDAAEDARVAVRNIRRDALSQLKDLVKEKEISEDEERRAADDVQKLTDKFVAEIEVAVKQKEADLMAV
|
Responsible for the release of ribosomes from messenger RNA at the termination of protein biosynthesis. May increase the efficiency of translation by recycling ribosomes from one round of translation to another.
|
Q4ZWS5
|
A4IJC8
|
RL25_GEOTN
|
General stress protein CTC
|
Geobacillus
|
MAIVLGAKERKDKKHSTLRRIRSQGGIPAVLYGKKVDNKMISISAADLEKALREGGRHSLVTLKVDGEDYSVLLREVQRDPLRGELLHADFQAVDMSAEVDVDVEVRLVGEAPGVKDGGVLQQNLHELSIRVLPANIPPAIEVDISGLQVGDVITVGDVQTGGTFEINHEPSEVIATILPPQQEEEIHSGEQQEPGQPEAEEGRETTPEG
|
This is one of the proteins that binds to the 5S RNA in the ribosome where it forms part of the central protuberance.
|
A4IJC8
|
Q65EG1
|
HIS5_BACLD
|
ImGP synthase subunit HisH
|
Bacillus
|
MIGVIDYGMGNLYSVSKALERIDAPYFVSEHPDELKRADSYILPGVGAFRDAMEILTENGLKTFIQAAANEGKPLLGICLGMQLLFEESEEHGASEGLGLLKGKVVKLKDCDQAGNRLKVPHMGWNLLKVHRDSPLLPKAKEGFAYFVHSYYVSGIEEEALLASAEYGVCVPAVVGLGNVYGAQFHPEKSSTVGMLILERFKQFTQEQKVKK
|
IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisH subunit catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the synthesis of IGP and AICAR. The resulting ammonia molecule is channeled to the active site of HisF.
|
Q65EG1
|
A0A1L8HU22
|
NEIL3_XENLA
|
Nei-like protein 3
|
Xenopus
|
MEALPPQVLKPLDCMSIYSRHREPENRHNELSTGRCGRGHVIFSSMKALQPQVLKPTGSHANLQQVLYAPAATIITAPASSHNDLSSLTGCSYAGVETLGKELFIYFGLKAMRVHFGMNGSMRINQPMKKGQENGRPIPIAVLEVQLTKDLICFYESTVDVRNASECQEKIRFFEELDVCSSKFSFPRAECEIKKQRTRMLCDILLDQMILPGVGNIIKNEALFDSGLHPGVQAGLLTDEQVSHLVKMTRDFTLLFYKCRKSGSALYKHYKVYKRPNCGQCGTKITVCRLGEHNRMTYFCPKCQKDKPQHVDVSKLPTRNSLIGWVQRTASNANEHVATSKEEHWACAVCTLINKPSDKQCDACLTLRPEVSSLAVSDEAAELNTDLVKYPCNNFAKVLPELKLNRRTAFGNTTLVLTDFGAKEGLADKNSQQNILNRSTFDVPLNNKYYHTKTPSNKRSNENEHWTNTLNAVNGHSAASNNVFNHPQKKLKTGHTTSNTIHLSSTISSPQSKMTGDAAAKTGNPQCSAHNVPCALQVVRKEGENKGRSFYTCSLPRERRCQYFEWADLHFPFCNHGKRCIVRTVLKIGPNNGKNFYVCPMGKDKQCNFFEWAKTE
|
DNA glycosylase which prefers single-stranded DNA (ssDNA), or partially ssDNA structures such as bubble and fork structures, to double-stranded DNA (dsDNA) . Mediates interstrand cross-link repair in response to replication stress: recruited to replication stress sites via interaction with ubiquitinated CMG helicase and acts by mediating DNA glycosylase activity . Cleaves one of the two N-glycosyl bonds comprising the interstrand cross-link, which avoids the formation of a double-strand break but generates an abasic site that is bypassed by translesion synthesis polymerases .
|
A0A1L8HU22
|
Q924N4
|
S12A6_MOUSE
|
K-Cl cotransporter 3
|
Mus
|
MHPPEATTKMSSVRFMVTPTKIDDIPGLSDTSPDLSSRSSSRVRFSSRESVPETSRSEPMSELSGATTSLATVALDPSSDRTSNPQDVTEDPSQNSITGEHSQLLDDGHKKARNAYLNNSNYEEGDEYFDKNLALFEEEMDTRPKVSSLLNRMANYTNLTQGAKEHEEAENITEGKKKPTKSPQMGTFMGVYLPCLQNIFGVILFLRLTWVVGTAGILQAFAIVLICCCCTMLTAISMSAIATNGVVPAGGSYFMISRALGPEFGGAVGLCFYLGTTFAAAMYILGAIEIFLVYIVPRAAIFRSDDALKESAAMLNNMRVYGTAFLVLMVLVVFIGVRYVNKFASLFLACVIVSILAIYAGAIKSSFAPPHFPVCMLGNRTLSSRHLDICSKTKEVDNMTVPSKLWGFFCNSSQFFNATCDEYFVHNNVISIQGIPGLASGIITENLWSNYLPKGEIIEKPSAKSSDVLGNLNHEYVLADITTSFTLLVGIFFPSVTGIMAGSNRSGDLKDAQKSIPIGTILAILTTSFVYLSNVVLFGACIEGVVLRDKFGDAVKGNLVVGTLSWPSPWVIVIGSFFSTCGAGLQSLTGAPRLLQAIAKDNIIPFLRVFGHSKANGEPTWALLLTAAIAELGILIASLDLVAPILSMFFLMCYLFVNLACALQTLLRTPNWRPRFRYYHWALSFMGMSICLALMFISSWYYAIVAMVIAGMIYKYIEYQGAEKEWGDGIRGLSLSAARFALLRLEEGPPHTKNWRPQLLVLLKLDEDLHVKHPRLLTFASQLKAGKGLTIVGSVIVGNFLENYGDALAAEQTIKHLMEAEKVKGFCQLVVAAKLKEGISHLIQSCGLGGMKHNTVVMGWPNGWRQSEDARAWKTFIGTVRVTTAAHLALLVAKNVSFFPSNVEQFSEGNIDVWWIVHDGGMLMLLPFLLKQHKVWRKCSIRIFTVAQLEDNSIQMKKDLATFLYHLRIEAEVEVVEMHDSDISAYTYERTLMMEQRSQMLRHMRLSKTERDREAQLVKDRNSMLRLTSIGSDEDEETETYQEKVHMTWTKDKYMASRGQKVKSMEGFQDLLNMRPDQSNVRRMHTAVKLNEVIVNKSHEAKLVLLNMPGPPRNPEGDENYMEFLEVLTEGLERVLLVRGGGSEVITIYS
|
Mediates electroneutral potassium-chloride cotransport. May be activated by cell swelling. May contribute to cell volume homeostasis in single cells.
|
Q924N4
|
A3MA48
|
HUTI_ACIBT
|
Imidazolone-5-propionate hydrolase
|
Acinetobacter calcoaceticus/baumannii complex
|
MKKLWQNCHIATMQNGQYSYIEDAAIVTEGHLIHWIGKQQQLPADTYSETVDLNGAWVTPGFIDCHTHSVFGGNRSVEFEKRLQGVSYAEIAASGGGIASTVRATREASEEQLLNSALKRIRCMQQDGVTTIEIKSGYGLNYENERKMLRVIRQIGEKLPMTVKSTCLAAHALPPEYKDQSDAYIEHICTEMLPKLHAEGLVDAVDAFCEHLAFSPAQVERVFKTAQSLNLPVKLHAEQLSSLGGSSLAARYHALSADHLEYMTEDDVKAMAASGTVAVLLPGAFYLLRETQYPPIESLIKHGVRIALSSDLNPGTSPALSLRLMLNMGSTLFRLTPEQALAGVTIHAAQALGLEQTHGSLEQGKVADFVAWDIEHPSEIVYWLGGDLPKRVVQHGQEVIF
|
Catalyzes the hydrolytic cleavage of the carbon-nitrogen bond in imidazolone-5-propanoate to yield N-formimidoyl-L-glutamate. It is the third step in the universal histidine degradation pathway.
|
A3MA48
|
P84988
|
CB21_POPEU
|
LHCII type I CAB-1
|
Populus
|
TGALLLDGNTLNYFGKIFLPDGLLDRYQAFELIHARKPEDFEKYQAFELIHAR
|
The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated.
|
P84988
|
Q14257
|
RCN2_HUMAN
|
E6-binding protein
|
Homo
|
MRLGPRTAALGLLLLCAAAAGAGKAEELHYPLGERRSDYDREALLGVQEDVDEYVKLGHEEQQKRLQAIIKKIDLDSDGFLTESELSSWIQMSFKHYAMQEAKQQFVEYDKNSDDTVTWDEYNIQMYDRVIDFDENTALDDAEEESFRKLHLKDKKRFEKANQDSGPGLSLEEFIAFEHPEEVDYMTEFVIQEALEEHDKNGDGFVSLEEFLGDYRWDPTANEDPEWILVEKDRFVNDYDKDNDGRLDPQELLPWVVPNNQGIAQEEALHLIDEMDLNGDKKLSEEEILENPDLFLTSEATDYGRQLHDDYFYHDEL
|
Not known. Binds calcium.
|
Q14257
|
Q2NRB3
|
MLTC_SODGM
|
Murein lyase C
|
Sodalis
|
MKKILPLVIIAPLLISCSSSKNKAENEAYIKDTNGFDILMGQFAHNIENLWGLNEVLIAGPKDYVKYTDQYETRSHINFDAGTITVETIAGDNPSAHLRQAIISTLLMGNDPGTIDLYSDADYIPISKEPFLYGQVLDNNGEPIRWEWHAAHFADYLLQTRLQTRTTGLRQIWSITIQLVPNHLDKRAHKYLGMVRKASQQYGVDQSLILAIMQTESSFNPYAVSHADALGLMQVVQHSAGRDVFKMKGKWGQPSRSYLFDPENNIDTGTAYLAMLQNSYLGGIVNPTSRRYAVITAYNGGAGSVLRVFSRDQNRAFQIINGMPPDQVYQTLSTQHPSAESRRYLYKVNNLQKNYRR
|
Murein-degrading enzyme. May play a role in recycling of muropeptides during cell elongation and/or cell division.
|
Q2NRB3
|
C4XSF4
|
ILVC_SOLM1
|
Ketol-acid reductoisomerase type I
|
Solidesulfovibrio
|
MKIYYDQDADLSLLADKTVAIIGYGSQGHAHAQNLRDSGVKVVIGQRPGGPNWELAKENGFTPMSAAEAAAAADLIMILVPDQHQKAVYEKDVLPHLKPGKMLLFAHGFNIHFQQIVPPADVDVAMVAPKGPGHLVRRVYTEGAGVPCLIAIHQNATGKAMETALAYAKGVGGTRGGVLTTTFKEETETDLFGEQAVLCGGAAELVKAGFETLCEAGYQPEIAYFECLHELKLIVDLMYEGGLSRMRYSISDTAEYGDYVSGPRVVTDETRAEMRQILKEIQDGTFARDFIMENMSGRAHFLSMRRINAEHPIEKVGAKLRGMMSWLKK
|
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-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate.
|
C4XSF4
|
P49910
|
ZN165_HUMAN
|
Zinc finger and SCAN domain-containing protein 7
|
Homo
|
MATEPKKAAAQNSPEDEGLLIVKIEEEEFIHGQDTCLQRSELLKQELCRQLFRQFCYQDSPGPREALSRLRELCCQWLKPEIHTKEQILELLVLEQFLTILPGDLQAWVHEHYPESGEEAVTILEDLERGTDEAVLQVQAHEHGQEIFQKKVSPPGPALNVKLQPVETKAHFDSSEPQLLWDCDNESENSRSMPKLEIFEKIESQRIISGRISGYISEASGESQDICKSAGRVKRQWEKESGESQRLSSAQDEGFGKILTHKNTVRGEIISHDGCERRLNLNSNEFTHQKSCKHGTCDQSFKWNSDFINHQIIYAGEKNHQYGKSFKSPKLAKHAAVFSGDKTHQCNECGKAFRHSSKLARHQRIHTGERCYECNECGKSFAESSDLTRHRRIHTGERPFGCKECGRAFNLNSHLIRHQRIHTREKPYECSECGKTFRVSSHLIRHFRIHTGEKPYECSECGRAFSQSSNLSQHQRIHMRENLLM
|
May be involved in transcriptional regulation.
|
P49910
|
C5BEU1
|
HSCA_EDWI9
|
Hsc66
|
Edwardsiella
|
MALLQISEPGLSAAPHQRRLAAGIDLGTTNSLVATVRSGQAETLADEQGHHLLPSVVRYQAGGHIVGAEAREQAADDPLNTVSSIKRMMGRSLADVQARYPHLPYQMHASESGMPQLATAAGSVNPIQVSADILAALSARAQAALGGELDGVVITVPAYFDDAQRQGTKDAARLAGLHVLRLLNEPTAAAIAYGLDSAQEGVIAVYDLGGGTFDISILRLSRGVFEVLATGGDSALGGDDFDHLLADWLREQAGLRDRSDAGLARRFLDAAVAAKIALSTQQETTVCVGDWQGEVSRDQLDALIAPLVKRTLLACHRTLKDAGVTRDEVLEVVMVGGSTRVPLVRTQVGDFFGRQPLTTIDPDRVVAIGAAIQADILVGNKPDADMLLLDVIPLSLGLETMGGLVEKVIPRNTTIPVARAQEFTTFKDGQTAMMIHVLQGERELVQDNRSLARFTLRGIPPLSAGGAHIRVTFQVDADGLLSVTAMEKSTGVQAAIQVKPSYGLSEDEIVGMLKDSMANAEGDLSARMLAEQKVEAARVLESLHGALQQDSALLGEQELAAIRQAQTALQAAADGDETSAIEAAIKVLDAQTQEFAARRMDSSIRRALAGHSVDEV
|
Chaperone involved in the maturation of iron-sulfur cluster-containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB. Involved in the maturation of IscU.
|
C5BEU1
|
Q883F2
|
UREF1_PSESM
|
Urease accessory protein UreF 1
|
Pseudomonas
|
MNTLSSLLLALQQADSFFPGGAVAWSWGLETLVADGRLGAGERVTARRRQRAVRLDRSAAVRGFVEGQLRHRWHSFDRVFLLAAWNAADDVSALTNLDAQIEALTLAKELRQGSRRVGQALLGVHVALGTPGAAAYQQQVRAGNTPGHLPVLQGLLWNRLGMHREHCQLAAAHGLCTGLVSAAVRLGVMGHIDAQRVLTDIQPLITELLALEPPEPEDACGFTPMAEIAVMRHETQDLRLFAN
|
Required for maturation of urease via the functional incorporation of the urease nickel metallocenter.
|
Q883F2
|
Q8DD25
|
NUSG_VIBVU
|
Transcription termination/antitermination protein NusG
|
Vibrio
|
MSEAPKKRWYVVQAFSGFEGRVAQSLREHIKMHGMEEYFGEVLVPTEEVVEMRAGQRRKSERKFFPGYVLVQMIMNDESWHLVRSVPRVMGFIGGTSDRPAPISDKEADAILNRLEKASEAPRPRTMYEVGEVVRVNEGPFADFNGTVEEVDYEKSRLKVSVSIFGRATPVELEFGQVEKLD
|
Participates in transcription elongation, termination and antitermination.
|
Q8DD25
|
Q38WP3
|
DEF_LATSS
|
Polypeptide deformylase
|
Latilactobacillus
|
MILMKDIIREGNPTLREIAQPVSFPLSDEDRQLAADMMTFLENSQDPEIAAKYQLRAGVGLAAPQVDVSKQMSAVLVPGPEGEAPILKDVIINPKIISHSVQDAALAEGEGCLSVDREVPGYVPRHDRITLRYQDVEGVSHKIRLKNYPAIVCQHEIDHLNGILFFDHINKENPFAAPDDMIILE
|
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.
|
Q38WP3
|
A8M532
|
EFG_SALAI
|
Elongation factor G
|
Salinispora
|
MAAADALANVRNIGIMAHIDAGKTTTTERILFYTGITYKIGEVHEGAAVMDWMAQEQERGITITSAATKCEWKGHTIQIIDTPGHVDFTVEVERSLRVLDGAVAVYDGVAGVEPQTENVWRQADKYNVPRMCFVNKLDRTGADFFRCVQMMVDRLNATPLVLQVPIGLEADHIGVVDLIDMRALTWRGETQKGEDYAVEEIPAELADTAAEWREKLMETLADVDDAVMEKYLEGGEFSVEEIKAAIRRATIAGKANPVLCGSAFKNKGVQPMLDAVVDFLPSPLDIPAIEGTGTDGETPLQRKPSTSEPFSGLAFKIQTDKHLGKLTYMRVYSGVLESGSQVVNSTKDRKERIGKIYQMHANKREERSSAKAGDIIAVQGLKQTTTGDTLCDPANPVILESMTFPEPVIEVAIEPKTKADQEKLSTAIQRLAEEDPTFRVKLDDETGQTVISGMGELHLDILVDRMRREFNVEANIGKPQVAYRETIRRKVEKVEYTHKKQTGGSGQYARVIVSLEPLPLDNDSPTYEFANAVTGGRVPREFIPSVDAGAQDAMQYGILAGFPLVGVKLTLVDGQYHEVDSSEMAFKIAGSMVLKDAARKADPALLEPMMAVEVTTPEENMGDVIGDINSRRGIIQAMEERGGARVVRALVPLSEMFGYVGDLRSKTQGRASYSMQFDSYAEVPASVAKEIIAKATGE
|
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, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.
|
A8M532
|
A4QL01
|
MATK_DRANE
|
Intron maturase
|
Draba
|
MEKFQGYLEFDGARQQSFLYPLFFREYIYVLAYDHGLNRLNRNRSIFVENSDYEKKYSSLIVKRLIWRMYEQNRLIIPTTDLHKNPVLGHTNHLYYQMISVLFAVIVEIPFSLSLGFSFEGKQIKKSYNLQSIHSLFPFLEDKLSHFNYVLDVLIPYPIHLEILVQTLRYRVKDASSLHFFRFCLYEYGNWKNFDIKKKCILNPRFFLFLYNSHICEYESIFFFLRKRSSHLRSIAYEVFFERILFYGKIHHFFKVFVNNFPATLGLLKDPFLHYVRYHGKNILATKDTPLLMNKWKFYFLNFWQCYFSVWFPSQKVNINQLSKDNLEFLGYLSSLRLNPLVVRSQMLENSFLIDNIRIKFDSKIPISSIIGSLAKDKFCNVLGHPISKATWTDSSDSDILNRFVRICRKISHYYSGSSKKKNLYRIKYILRLCCVKTLARKHKSTVRAFLKRLGSVLLEEFLTGEDQVLSLIFPRSYYASKRLYRVRIWYLDILYLHDLVNHE
|
Usually encoded in the trnK tRNA gene intron. Probably assists in splicing its own and other chloroplast group II introns.
|
A4QL01
|
Q0W6V4
|
COFH_METAR
|
FO synthase subunit 2
|
Methanocella
|
MLKDIYERSLSGEITIEDARKLLEANPFELFDTADQLRKEIVGDNVTYIVNRNINFTDFCVGTCKFCSFKNNKGFRLTLDEILQRVGAAKETGSTEVCIQGGLTEDMYLEDYAGMIRAIKSKYDIHTHAFSPMEVYHMSRMSGVTVEESLKTLKVAGLNSMPGTAAEILDDEIRSVICPGKLSTSEWVDVVSTAHRVGIPTTATIMYGHIETWEHRLKHLFIVRDVQRQTHGITEFVPLTFMHENNSLSGKSMGASGMDDLRMYALARIIFGRDIPNVQASWVKLGTKLAQVALNCGANDVGGTLMEENISKSAGSKSGEYLSPDDLQAMIKAAGRIPRQRNTLYKLLG
|
Catalyzes the radical-mediated synthesis of 5-amino-5-(4-hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil from 5-amino-6-(D-ribitylamino)uracil and L-tyrosine.
|
Q0W6V4
|
Q8BSN5
|
PHF23_MOUSE
|
PDH-containing protein JUNE-1
|
Mus
|
MLEAMAEPSPEDPPPTLKPETQPPEKRRRTIEDFNKFCSFVLAYAGYIPPSKEESDWPASGSSSPLRGESAADSDGWDSAPSDLRTIQTFVKKAKSSKRRAVQSGPTQPGPPRSTFSRLQAPDSATLLEKMKLKDSLFDLDGPKVASPLSPTSLTHTSRPPAALAPVPLSQGDLSQPRKKDRKNRKLGPGGGAGFGVLRRPRPAPGDGEKRSRIKKSKKRKLKKADRGDRLPPPGPPRAPPSDTDSEEEEEEEEEEDDEEEMTVGGGVPAPVLPTPPEAPRPPVTVHSEGAPPTDSEGKDVGSTETSQDGDASSSEGEMRVMDEDIMVESGDDSWDLITCYCRKPFAGRPMIECSLCGTWIHLSCAKIKKTNVPDFFYCQKCKELRPEARRLGGLPKSGEP
|
Acts as a negative regulator of autophagy, through promoting ubiquitination and degradation of LRSAM1, an E3 ubiquitin ligase that promotes autophagy in response to starvation or infecting bacteria.
|
Q8BSN5
|
P97379
|
G3BP2_MOUSE
|
GAP SH3 domain-binding protein 2
|
Mus
|
MVMEKPSPLLVGREFVRQYYTLLNKAPEYLHRFYGRNSSYVHGGVDASGKPQEAVYGQNDIHHKVLSLNFSECHTKIRHVDAHATLSDGVVVQVMGLLSNSGQPERKFMQTFVLAPEGSVPNKFYVHNDMFRYEDEVFGDSEPELDEESEDEVEEEQEDRQPSPEPVQENANSAYYDAHPVTNGIEEPLEESSHEPEPEPESETKTEELKPQVEEKHLEELEEKSATPPPAEPASLPQEPPKAFSWASVTSKNLPPSGTVSSSGIPPHVKAPVSQPRVDAKPEVQSQPPRVREQRPRERPGFPPRGPRPGRGDMEQNDSDNRRIIRYPDSHQLFVGNLPHDIDENELKEFFMSFGNVVELRINTKGVGGKLPNFGFVVFDDSEPVQRILIAKPIMFRGEVRLNVEEKKTRAARERETRGGGDDRRDIRRNDRGPGGPRGIVGGGMMRDRDGRGPPPRGGMTQKLGSGRGTGQMEGRFTGQRR
|
Scaffold protein that plays an essential role in cytoplasmic stress granule formation which acts as a platform for antiviral signaling.
|
P97379
|
Q0B0B4
|
SECA_SYNWW
|
Protein translocase subunit SecA
|
Syntrophomonas
|
MIKSLLKSLLDDDEREVKKLRRTVEVINSLEAEFQELAEEEFPQKTGEFKERLKNGEELDDILPEAFALVREASQRVLGMRHFDVQLIGGMVLHQGRIAEMKTGEGKTLVATLPAYLNALEGKGVHIVTVNDYLAARDADWMGPVLEYCGLSVGLIVHGLSYEERKAAYACDVTYGTNNEMGFDYLRDNMVVSADNMVQRELHYAIIDEVDSILVDEARTPLIISGEGDKPTTLYYQIAKFIPRLRNEEDYKVDEKAHVVTLTEEGVKKVEKYFTIENLSENMELAHHVNQGLKAHSLMKRDRDYVIKDEQVIIVDEFTGRLMFGRRYSDGLHQAIEAKEGVKIEKESQTLATITFQNYFRMYHKLGGMTGTAKTEEEEFRKIYGMDVVSIPTHNPMIREDQADMVYRTEEGKFRAVVEDIISRHQAKQPVLVGTISVEKSEYLSAMLAKRGVKHQVLNAKYHEKEAQIIAQAGQEETVTIATNMAGRGTDIVLGEGIQELGGLYVLGTERHESRRIDNQLRGRSGRQGDPGESRFYVSLEDDLMRLFGSANVEGLMDRLGMDDDMPIEHKMISRAIESAQKKVEARNFSIRKNVLEYDDVINQQREVMYGERRKVLFGEDLKETVASMVDDVIEQAVERFAGEFKYSDEWDLPGFLSYIEQSIIPQPDFNQEDMRGMRKNEVVAFLAEKTQTLYEQREKEMGSEIMRELEKAILLRIIDEKWMDHIDAMDQLRNGISLRAYGQKDPLIEYKFEAFEAFQMMIESMKEDVVRYIFRVKVVQQPEERKTFENQGEEAEKKPVRVGKKIGRNDLCPCGSGKKYKKCCGRGVS
|
Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane.
|
Q0B0B4
|
Q6GGV2
|
CCA_STAAR
|
tRNA-NT
|
Staphylococcus
|
MDKSLFEQARPILEQIQDNGFEAYYVGGSVRDYVMGRNIHDIDITTSATPDEIESIFSHTIPVGKEHGTINVVFNDENYEVTTFRAEEDYVDHRRPSGVTFVRDLYEDLQRRDFTMNAIAMDTANKLYDYFDGQQDINNRIIRTVGIAEERFQEDALRMIRCLRFQSQLSFDIATETFEAMRTQMADIKFLSIERIVIELTKLMRGINVEKSFNHLKSLKAFNYMPYFEHLDMNQINVTEPIDLELLIAIVSVKFDINYSLKPLKLSNRQVKDINQYIQIMNALPSIITKEQLKMFVYDYDTNLIKNVMVAADVLKANDIQGHEPLIVNLQTIDETLHRLPMHNRKDMMVNGGVLMAHLNAKSGPWLKDLLRQIEIAIVTGKVSNEETEILKWVDNHVKI
|
Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate.
|
Q6GGV2
|
P57805
|
RNC_PASMU
|
Ribonuclease III
|
Pasteurella
|
MTQNLERLQRQIGYQFNQPALLKQALTHRSAAVKHNERLEFLGDAILNFIIAEALYHQFPKCNEGELSRMRATLVREPTLASLARQFELGDYLSLGPGELKSGGFRRESILADCVEAIIGAISLDSDLATTTKIVQHWYQAQLKQIQPGDNQKDPKTRLQEYLQGKRLPLPTYNVVEIKGEAHCQTFTVECYVKNIDRTFMGSGASRRKAEQAAAEKILQLLEMK
|
CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). In this organism endogenous ribonuclease 3 and Cas9 are required for correct coprocessing of pre-crRNA and the trans-encoded small RNA (tracrRNA). Cas9, crRNA and tracrRNA are required for cleavage of invading DNA (Probable). Complements pre-crRNA and tracrRNA coprocessing defects in an rnc deletion in S.pyogenes strain 370 .
|
P57805
|
P39838
|
RCSD_ECOLI
|
Phosphotransfer intermediate RcsD
|
Escherichia
|
MRQKETTATTRFSLLPGSITRFFLLLIIVLLVTMGVMVQSAVNAWLKDKSYQIVDITHAIQKRVDNWRYVTWQIYDNIAATTSPSSGEGLQETRLKQDVYYLEKPRRKTEALIFGSHDNSTLEMTQRMSTYLDTLWGAENVPWSMYYLNGQDNSLVLISTLPLKDLTSGFKESTVSDIVDSRRAEMLQQANALDERESFSNMRRLAWQNGHYFTLRTTFNQPGHLATVVAFDLPINDLIPPGMPLDSFRLEPDATATGNNDNEKEGTDSVSIHFNSTKIEISSALNSTDMRLVWQVPYGTLLLDTLQNILLPLLLNIGLLALALFGYTTFRHFSSRSTENVPSTAVNNELRILRAINEEIVSLLPLGLLVHDQESNRTVISNKIADHLLPHLNLQNITTMAEQHQGIIQATINNELYEIRMFRSQVAPRTQIFIIRDQDREVLVNKKLKQAQRLYEKNQQGRMIFMKNIGDALKEPAQSLAESAAKLNAPESKQLANQADVLVRLVDEIQLANMLADDSWKSETVLFSVQDLIDEVVPSVLPAIKRKGLQLLINNHLKAHDMRRGDRDALRRILLLLMQYAVTSTQLGKITLEVDQDESSEDRLTFRILDTGEGVSIHEMDNLHFPFINQTQNDRYGKADPLAFWLSDQLARKLGGHLNIKTRDGLGTRYSVHIKMLAADPEVEEEEERLLDDVCVMVDVTSAEIRNIVTRQLENWGATCITPDERLISQDYDIFLTDNPSNLTASGLLLSDDESGVREIGPGQLCVNFNMSNAMQEAVLQLIEVQLAQEEVTESPLGGDENAQLHASGYYALFVDTVPDDVKRLYTEAATSDFAALAQTAHRLKGVFAMLNLVPGKQLCETLEHLIREKDVPGIEKYISDIDSYVKSLL
|
Component of the Rcs signaling system, which controls transcription of numerous genes. RcsD is a phosphotransfer intermediate between the sensor kinase RcsC and the response regulator RcsB. It acquires a phosphoryl group from RcsC and transfers it to RcsB. The system controls expression of genes involved in colanic acid capsule synthesis, biofilm formation and cell division.
|
P39838
|
P80098
|
CCL7_HUMAN
|
Small-inducible cytokine A7
|
Homo
|
MKASAALLCLLLTAAAFSPQGLAQPVGINTSTTCCYRFINKKIPKQRLESYRRTTSSHCPREAVIFKTKLDKEICADPTQKWVQDFMKHLDKKTQTPKL
|
Chemotactic factor that attracts monocytes and eosinophils, but not neutrophils. Augments monocyte anti-tumor activity. Also induces the release of gelatinase B. This protein can bind heparin. Binds to CCR1, CCR2 and CCR3.
|
P80098
|
Q8CXQ7
|
CH60_MALP2
|
Chaperonin-60
|
Malacoplasma
|
MAKEIKFSDSARNKLFNGVQQLFDAVKVTMGPRGRNVLIQKSYGAPVITKDGVSVAKEVDLTNPIENMGAQLVKDVASKTADEAGDGTTTATVLAYGVFKEGLRNVISGANPIEIKRGMDKTVNAIVNELNKSSKKIARKDEIIQVATISANSDKKIGELIANAMEKVGSDGVITVEEAKGINDELTVVEGMQFDRGYISPYFVTDTNKMIAKLENPYILITDKKVSSIKDILPILEEIMKTGRPLLIIADDVDGEALTTLVVNKMRGVFNVVAVKAPEFGDKRKQVLEDIAILTGGSFVTDDLGISFDKVTLQDLGQAESVVIDKDNSTIVKGKGLESQIKERISKIKTAIEMTDSDYDKDSLRNRLAKLNKGVAVIKVGAVSEVELKEKKDRVDDALSATKAAIEEGIVIGGGAALVHVSKRINVNTLNLIGDEKIGYQIVMSAIMSPISQIVSNAGFDKGVVINEILKATNPHLGFNAATGKYVDMFQTGIIDPVKVTRIALQNAVSVSSMLLTTEAVIYDVKDDKEDSVPAMPNMGMGGMM
|
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.
|
Q8CXQ7
|
B1JAJ9
|
RS14_PSEPW
|
30S ribosomal protein S14
|
Pseudomonas
|
MAKKSMKNRELKRQLTVAKFAKKRAELKATIVNLNASPEERFAAVVALQKQPRDASAARLRNRCRLTGRPHGVYRKFGLGRNMLRQAAMRGDVPGLVKASW
|
Binds 16S rRNA, required for the assembly of 30S particles and may also be responsible for determining the conformation of the 16S rRNA at the A site.
|
B1JAJ9
|
B3H5A9
|
PCEP6_ARATH
|
C-terminally encoded peptide 6.2
|
Arabidopsis
|
MKLSVYIILSILFISTVFYEIQFTEARQLRKTDDQDHDDHHFTVGYTDDFGPTSPGNSPGIGHKMKENEENAGGYKDDFEPTTPGHSPGVGHAVKNNEPNA
|
Extracellular signaling peptide that represses primary root growth rate. Modulates leaf morphology . Regulates systemic nitrogen (N)-demand signaling. Mediates up-regulation of genes involved in N uptake and assimilation pathways .
|
B3H5A9
|
Q8YLZ0
|
RNZ_NOSS1
|
tRNase Z
|
Nostoc
|
MQITFLGTSSGVPTRARNVSSVALRLPQRAELWLFDCGEGTQHQILRSDLKVSQLSRIFITHLHGDHIFGLMGLLASCGLAGNVQRVDIYGPSGLNDYIQSASRYSHTHFSYPIKVHTVRPGVIYENDEFTVTCGLLHHRITAFGYRVAEKDRAGRFDIEKAKELQIPPGRIYGQLKRGETVTLEDGRVINGAELCGPTEIGRKMAYCTDTIYCDGAVELAQDADVLIHEATFAHQDSEMAFQRLHSTTTMAAQTALAAGVRRLLMTHFSPRYAPGNTIELKDLLQEARAIFPRTDMAYDFMTYEVPRRREPVFSSVSSSSV
|
Zinc phosphodiesterase, which displays some tRNA 3'-processing endonuclease activity. Probably involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA.
|
Q8YLZ0
|
Q6ZIK5
|
GRF4_ORYSJ
|
Transcription activator GRF4
|
Oryza sativa
|
MAMPYASLSPAVADHRSSPAAATASLLPFCRSTPLSAGGGGVAMGEDAPMTARWPPAAAARLPPFTAAQYEELEQQALIYKYLVAGVPVPPDLVLPIRRGLDSLAARFYNHPALGYGPYFGKKLDPEPGRCRRTDGKKWRCSKEAAPDSKYCERHMHRGRNRSRKPVETQLVAQSQPPSSVVGSAAAPLAAASNGSSFQNHSLYPAIAGSNGGGGGRNMPSSFGSALGSQLHMDNAAPYAAVGGGTGKDLRYTAYGTRSLADEQSQLITEAINTSIENPWRLLPSQNSPFPLSSYSQLGALSDLGQNTPSSLSKVQRQPLSFFGNDYAAVDSVKQENQTLRPFFDEWPKGRDSWSDLADENANLSSFSGTQLSISIPMASSDFSAASSRSTNGD
|
Transcription activator that plays a role in the regulation of meristematic function in leaves, stems and inflorescences . Transcription activator that plays a regulatory role in grain development . Positively regulates grain size by promoting cell division and expansion, leading to increased grain length and width . Positively regulates the expression of genes promoting cell proliferation . Activates the expression of expansin genes to promote cell expansion and grain size . May promote grain size by activating brassinosteroid responses . Component of a network formed by the microRNA396 (miRNA396), the GRFs and their interacting factors (GIFs) acting in the regulation of meristem function, at least partially through the control of cell proliferation (Probable). Component of the miRNA396c-GRF4-GIF1 regulatory module that plays an important role in grain size determination (Probable) .
|
Q6ZIK5
|
Q4L5P8
|
LSPA_STAHJ
|
Signal peptidase II
|
Staphylococcus
|
MKKKYYITISLIVAIAILIIDQVTKRIIATTMNIGDSYEVIPNFLNITSHRNNGAAWGILSGKMGFFYIITIVILIVLVLFYIKEAKYNLFMQVAISLLFAGALGNFIDRLVNGEVVDFVDTNIFGYDFPIFNVADSSLTIGVLFIIIALLKDANSKE
|
This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
|
Q4L5P8
|
Q93V99
|
PDF2_ARATH
|
Homeodomain transcription factor PDF2
|
Arabidopsis
|
MYHPNMFESHHMFDMTPKSTSDNDLGITGSREDDFETKSGTEVTTENPSGEELQDPSQRPNKKKRYHRHTQRQIQELESFFKECPHPDDKQRKELSRDLNLEPLQVKFWFQNKRTQMKAQSERHENQILKSDNDKLRAENNRYKEALSNATCPNCGGPAAIGEMSFDEQHLRIENARLREEIDRISAIAAKYVGKPLGSSFAPLAIHAPSRSLDLEVGNFGNQTGFVGEMYGTGDILRSVSIPSETDKPIIVELAVAAMEELVRMAQTGDPLWLSTDNSVEILNEEEYFRTFPRGIGPKPLGLRSEASRQSAVVIMNHINLVEILMDVNQWSCVFSGIVSRALTLEVLSTGVAGNYNGALQVMTAEFQVPSPLVPTRENYFVRYCKQHSDGSWAVVDVSLDSLRPSTPILRTRRRPSGCLIQELPNGYSKVTWIEHMEVDDRSVHNMYKPLVQSGLAFGAKRWVATLERQCERLASSMASNIPGDLSVITSPEGRKSMLKLAERMVMSFCSGVGASTAHAWTTMSTTGSDDVRVMTRKSMDDPGRPPGIVLSAATSFWIPVAPKRVFDFLRDENSRKEWDILSNGGMVQEMAHIANGHEPGNCVSLLRVNSGNSSQSNMLILQESCTDASGSYVIYAPVDIVAMNVVLSGGDPDYVALLPSGFAILPDGSVGGGDGNQHQEMVSTTSSGSCGGSLLTVAFQILVDSVPTAKLSLGSVATVNSLIKCTVERIKAAVSCDVGGGA
|
Probable transcription factor that binds to the L1 box DNA sequence 5'-TAAATG[CT]A-3'. Plays a role in maintaining the identity of L1 cells, possibly by interacting with their L1 box or other target-gene promoters; binds to the LIP1 gene promoter and stimulates its expression upon imbibition . Acts as a positive regulator of gibberellins (GAs)-regulated epidermal gene expression (e.g. LIP1, LIP2, LTP1, FDH and PDF1) . Functionally redundant to ATML1 . Involved, together with HDG proteins (e.g. HDG1, HDG2, HDG5 and HDG12), in the regulation of flower organs development by promoting the expression of APETALA 3 (AP3) in the epidermis and internal cell layers of developing flowers . Seems to promote cell differentiation .
|
Q93V99
|
P40423
|
SQH_DROME
|
Protein spaghetti-squash
|
Sophophora
|
MSSRKTAGRRATTKKRAQRATSNVFAMFDQAQIAEFKEAFNMIDQNRDGFVEKEDLHDMLASLGKNPTDDYLDGMMNEAPGPINFTMFLTLFGERLQGTDPEDVIKNAFGCFDEENMGVLPEDRLRELLTTMGDRFTDEDVDEMYREAPIKNGLFDYLEFTRILKHGAKDKDEQ
|
Required for cytokinesis, could regulate contractile ring function.
|
P40423
|
P18289
|
JRA_DROME
|
dJun
|
Sophophora
|
MKTPVSAAANLSIQNAGSSGATAIQIIPKTEPVGEEGPMSLDFQSPNLNTSTPNPNKRPGSLDLNSKSAKNKRIFAPLVINSPDLSSKTVNTPDLEKILLSNNLMQTPQPGKVFPTKAGPVTVEQLDFGRGFEEALHNLHTNSQAFPSANSAANSAANNTTAAAMTAVNNGISGGTFTYTNMTEGFSVIKDEPVNQASSPTVNPIDMEAQEKIKLERKRQRNRVAASKCRKRKLERISKLEDRVKVLKGENVDLASIVKNLKDHVAQLKQQVMEHIAAGCTVPPNSTDQ
|
Transcription factor that recognizes and binds to the enhancer heptamer motif 5'-TGA[CG]TCA-3' . Plays a role in dorsal closure .
|
P18289
|
Q5ZJI0
|
TPST2_CHICK
|
Tyrosylprotein sulfotransferase 2
|
Gallus
|
MRVTMRRVLLAVGSVVALMVTLHLGQQVLECQHVLSKRRHRLMRPENEELVMVDSNHVEYRYSKEMPLIFIGGVPRSGTTLMRAMLDAHPEVRCGEETRIIPRVLAMRQAWSKSGREKMRLDEAGVTDQVLDAAMQAFILEVIAKHGEPARYLCNKDPFTLKSSVYLSRLFPNSKFLLMVRDGRASVHSMITRKVTIAGFDLNCYRDCLTKWNKAIEVMYSQCLEIGRSRCLPVYYEQLVLHPEQSMHAIMKFLGISWSDTVLHHEELIGKPGGVSLSKIERSTDQVIKPVNMEALSKWIGHIPGDVLQDMAHIAPMLARLGYDPYANPPNYGHPDPLVVNNTHRVLKGDYKTPANLKGHLQVTQNTSSSH
|
Catalyzes the O-sulfation of tyrosine residues within acidic motifs of polypeptides, using 3'-phosphoadenylyl sulfate (PAPS) as cosubstrate.
|
Q5ZJI0
|
O64969
|
CADH_EUCGL
|
Probable cinnamyl alcohol dehydrogenase
|
Eucalyptus
|
MGSLEKERTTTGWAARDPSGVLSPYTYSLRNTGPEDLYIKVLSCGICHSDIHQIKNDLGMSHYPMVPGHEVVGEVLEVGSEVTKYRVGDRVGTGIVVGCCRSCSPCNSDQEQYCNKKIWNYNDVYTDGKPTQGGFAGEIVVGERFVVKIPDGLESEQAAPLMCAGVTVYSPLVRFGLKQSGLRGGILGLGGVGHMGVKIAKAMGHHVTVISSSDKKRTEALEHLGADAYLVSSDENGMKEATDSLDYIFDTIPVVHPLEPYLALLKLDGKLILTGVINAPLQFISPMVMLGRKSITGSFIGSMKETEEMLEFCKEKGLTSQIEVIKMDYVNTALERLEKNDVRYRFVVDVVGSKLD
|
Involved in lignin biosynthesis. Catalyzes the final step specific for the production of lignin monomers. Catalyzes the NADPH-dependent reduction of coniferaldehyde, 5-hydroxyconiferaldehyde, sinapaldehyde, 4-coumaraldehyde and caffeyl aldehyde to their respective alcohols.
|
O64969
|
Q2A564
|
UBIA_FRATH
|
4-HB polyprenyltransferase
|
Francisella
|
MNKQQLKAYFMLMRLHRPIPILLILWPTLTALVLASHGLPDISYLVIFTIGVVVMRTVGCIINDIADVDFDKHVARTNTRPLTSGQLSIKNAIWLCISLTLVAFICVLFLNLYTILLSFVALFLAILYPFCKRFFAIPQLILGLAFNFGIFMAFSAIQNQIPVEAWIFYIATICWTIAYDTIYALADREFDLEIGIKSSAVLFGNKVFRYILLFNFLSLLLLIILGIYCDFNSFFYLGVVICSLFFVRNYFLYKKLGITNCINAFSANHWIGLIIFIIAVIQYI
|
Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of ubiquinone-8 (UQ-8) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate 3-octaprenyl-4-hydroxybenzoate.
|
Q2A564
|
Q9ESC2
|
TNMD_RAT
|
Myodulin
|
Rattus
|
MAKNPPENCEGCHILNAEALKSKKIRKSLKICGLVFGILALTLIVLFWGSKHFWPEVSKKTYGMEHTFYSNGEKKKISMEIDPITRTEIFRSGNGTDETLEVHDFKNGYTGIYFVGLQKCFIKTQIKVIPEFSEPEEEIDENEEITTTFFEQSVIWVPAEKPIENRDFLKNSKILEICDNVTMYWINPTLIAVSELQDFEEDGEDLHFPTSEKKGIDQNEQWVVPQVKVEKTRRTRQASEEDLPVNDYTENGIEFDPMLDERGYCCIYCRRGNRYCRRVCEPLLGYYPYPYCYQGGRVICRVIMPCNWWVARMLGRV
|
May be an angiogenesis inhibitor.
|
Q9ESC2
|
Q1WUJ3
|
FOLD_LIGS1
|
Methenyltetrahydrofolate cyclohydrolase
|
Ligilactobacillus
|
MVATILDGRMLSKKIRTNVSEKVSLLKQEGITPKLVVILVGEDPASQVYVRNKRKTAHALGIEAVDIRLPENVEEDELIRLIDELNSDGTVHGILVQLPLPKHINENKVTHRIIPEKDVDGFHPLNIGKLFMNIPGPLPCTPRGIMEFFKEYDIPVSGKRVVIVGRSNIVGRPMAALLVNSDATVTIAHSKTKNLAEVTKQADILIVAIGKGEFIDENYVKKGAVVIDVGMNRNNDGKLVGDVNMESVSKVASYITPVPGGVGPMTIAMLMKQTVELAERSVAGE
|
Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
|
Q1WUJ3
|
Q39127
|
TINY_ARATH
|
Ethylene-responsive transcription factor TINY
|
Arabidopsis
|
MIASESTKSWEASAVRQENEEEKKKPVKDSGKHPVYRGVRKRNWGKWVSEIREPRKKSRIWLGTFPSPEMAARAHDVAALSIKGASAILNFPDLAGSFPRPSSLSPRDIQVAALKAAHMETSQSFSSSSSLTFSSSQSSSSLESLVSSSATGSEELGEIVELPSLGSSYDGLTQLGNEFIFSDSADLWPYPPQWSEGDYQMIPASLSQDWDLQGLYNY
|
Putative transcriptional activator.
|
Q39127
|
P26308
|
GBB1_DROME
|
Guanine nucleotide-binding protein subunit beta-1
|
Sophophora
|
MNELDSLRQEAESLKNAIRDARKAACDTSLLQAATSLEPIGRIQMRTRRTLRGHLAKIYAMHWGNDSRNLVSASQDGKLIVWDSHTTNKVHAIPLRSSWVMTCAYAPSGSYVACGGLDNMCSIYNLKTREGNVRVSRELPGHGGYLSCCRFLDDNQIVTSSGDMSCGLWDIETGLQVTSFLGHTGDVMALSLAPQCKTFVSGACDASAKLWDIREGVCKQTFPGHESDINAVTFFPNGQAFATGSDDATCRLFDIRADQELAMYSHDNIICGITSVAFSKSGRLLLAGYDDFNCNVWDTMKAERSGILAGHDNRVSCLGVTENGMAVATGSWDSFLRVWN
|
Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.
|
P26308
|
P68350
|
DOF15_ARATH
|
Dof zinc finger protein DOF1.5
|
Arabidopsis
|
MATQDSQGIKLFGKTITFNANITQTIKKEEQQQQQQPELQATTAVRSPSSDLTAEKRPDKIIPCPRCKSMETKFCYFNNYNVNQPRHFCKGCQRYWTAGGALRNVPVGAGRRKSKPPGRVGGFAELLGAATGAVDQVELDALLVEEWRAATASHGGFRHDFPVKRLRCYTDGQSC
|
Transcription factor that binds specifically to a 5'-AA[AG]G-3' consensus core sequence. Acts as a negative regulator in the phytochrome-mediated light responses. Controls phyB-mediated end-of-day response and the phyA-mediated anthocyanin accumulation. Not involved in direct flowering time regulation.
|
P68350
|
Q635P1
|
MTNB_BACCZ
|
Methylthioribulose-1-phosphate dehydratase
|
Bacillus cereus group
|
MKQLFRQWYDLSEIKKELTTRNWFPATSGNISIKVSHEPLTFLITASGKDKTKTTPDDFLLVDHLGVPVLETELRPSAETILHTHIYNNTNAGCVLHIHTTDNNVITNLYSDAVTLQNQEIIKALDIWEEGATIHIPIIENHAHIPTLGENFRKHIQGDSGAVLIRNHGITVWGRDSFDAKKRLEAYEFLFQFHIKLLSIQGGVSNGANSYS
|
Catalyzes the dehydration of methylthioribulose-1-phosphate (MTRu-1-P) into 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P).
|
Q635P1
|
A3EWL3
|
REV1_ARATH
|
Rev1-like terminal deoxycytidyl transferase
|
Arabidopsis
|
MKRSLGSNSSNNSGSGSNKKSKKNNNPSNQKTLGAAWGAASSRSSFRSSPFSDFGSYMEVKNRKLQNQFETEASAASRGVSGSEKLIFQGVSIFVDGFTIPSHQELKGYMMKYGGRFENYFSRRSVTHIICSNLPDSKVKNLRTFSRGLPVVKPTWIVDSISANRLLGWVPYQLDQLNDTQPKLSAFFAPRSHLTPQMASPVTSFQPDTGYSEAEEGSSIRADDSEEARDHIDDEIDGVYIENTTPELTEQTGTGDLKSSEMNAEGLGNYDIEEKEVSSELQSTTNLHSTSDNKSVHANGKNGGKSIATAAGSSTRRHSTLEDPNFVENYFKNSRLHFIGTWRNRYRKRFHGSSNGLKWADSGQNTAEMAKKSTIIHIDLDCFFVSVVIKNRLELHDKPVAVCHSDNPKGTAEISSANYPARAYGVKAGMFVRHAKDLCPQLVIVPYNFEAYEEVADQFYDILHRHCRKVQALSCDEAFLDVSDLSDVETEVLASTIRNEILETTGCSASAGIGGTMLMARLATRVAKPAGQLYISAEKVEEFLDQLPVGTLPGVGSVLKEKLVKQNIQTCGQLRLISKDSLQKDFGVKTGEMLWSYSRGLDLRSVTAVQESKSIGAEVNWGVRFRDQQDVFILVQHFLQCLCKEVSLRLQGCEMIGRTFTLKIKKRKKDAEEPTKYMGCGDCDNLSRSITVPAATDDIEVLQRISKKLFGSFCLDVKEVRGVGLQVSKLDSADPSNKGSRTLKSWLSSAPAVVQIEQDDNVFAAKVRENSDCNRPVTGGVSRLRESNSEESSIQSGDTNSSLPPMCYLDMEVLENLPPELLSELDGTYGGKLFELIEKKRGKRRINCNSPHVSLDGTAASIKELKSLSVKIHGLSTSGEKEYKEPYVPHPSIARTSNQHTIEMTDLLPSSLSQVDVSVLQELPEELRADVLGAFPSHRRQQSSSDVPKETCKKQDEEPIDLKGTENEIGLSFSSLWFGNPPLWTEKFKVSGNCTMEKLSAIYFKVAQSRPMLSLVLQHAISEMSSFPDAASASDLDKAIYDVCELLKQYINLKVGGDIEEIYLCFRLLKRLAARSQLFLQVYEILSPFIQASISEHYGGSLSIP
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Deoxycytidyl transferase involved in DNA repair and translesion synthesis (TLS). Transfers a dCMP residue from dCTP to the 3'-end of a DNA primer in a template-dependent reaction. Mediates also the insertion of dTMP or dGMP when the opposite base is G, and, with a low efficiency, dGMP insertions opposite G, T, and C, dAMP insertions opposite G, A, and T, and dTMP insertion opposite A. May assist in the first step in the bypass of abasic lesions by the insertion of a nucleotide opposite the lesion. Required for normal induction of mutations by physical and chemical agents (e.g. UV and gamma ray), mostly via G to T transversions, and of spontaneous mutations in somatic cells. Confers resistance to ultraviolet-B (UV-B) and various DNA cross-linkers (e.g. mitomycin C MMC and cisplatin). Promotes stem growth.
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A3EWL3
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B7UNY1
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TORD_ECO27
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Chaperone protein TorD
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Escherichia
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MTTLTAQQIACVYAWLAQLFSRELDDEQLTQIASAQMAEWFSLLKSEPPLTAAVNGLENSIATLTVRDDARLELAADFCGLFLMTDKQAALPYASANKQDEQEIKRLLVEAGMETSGNFNEPADHLAIYLDLLSHLHFSLGEGTVPARRIDGLRQKTLTALREWLPEFAARCRQYDSFGFYAALSQLLLVLVECDYQKR
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Involved in the biogenesis of TorA. Acts on TorA before the insertion of the molybdenum cofactor and, as a result, probably favors a conformation of the apoenzyme that is competent for acquiring the cofactor.
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B7UNY1
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B2V704
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LPXB_SULSY
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Lipid-A-disaccharide synthase
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unclassified Sulfurihydrogenibium
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MKKIFLSVGEISGDNYASELAKHLKEYQITGITGPKMRAIGVKPVANLEDISVVGLTEALSKYKKIKEVFKQSVQALKSGVDLLIVVDFPGFNIKLLKEAKKLGIKTVYFISPQVWAWGSGRVKEIVENTDLLISILPFEEEIYKPYVSDKFKFAYVGHPLLDIIKIYENEDSFKQKLNIPKNKRIIGLLAGSRESEVNVILPILIEAARLLTKTFDDLHFVIPATVNMVDRVLEKVNFSLPITVITSNLSDKNLPKFENPSYEVMKNAVFSIITSGTATLEAAIIGNPFIIVYKVSPITYFIGKKLVKINYLGLPNIIAGNEIVPELLQDRCNPLDIANKTLEFLTDKNLYKTQKRNLEIVRKSLGKKGAIERASNLIRTLLEKGQA
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Condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
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B2V704
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