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
|
|---|---|---|---|---|---|---|
Q84SL0
|
CDPKK_ORYSJ
|
Calcium-dependent protein kinase 20
|
Oryza sativa
|
MGNCCVTPEGSGRGRKKQQQEQKQKQKEPKQQQQQQKKGKKPNPFSIEYNRSSAPSGHRLVVLREPTGRDIAARYELGGELGRGEFGVTYLCTERETGDAYACKSISKKKLRTAVDIEDVRREVDIMRHLPKHPNIVTLRDTYEDDNAVHLVMELCEGGELFDRIVARGHYTERAAALVTRTIVEVVQMCHKHGVMHRDLKPENFLFANKKETAALKAIDFGLSVFFTPGERFTEIVGSPYYMAPEVLKRNYGPEVDVWSAGVILYILLCGVPPFWAETEQGVAQAIIRSVIDFKRDPWPRVSDNAKDLVKGMLNPDPRRRLNAQQVLDHPWLQNIKKAPNVNLGETVKARLQQFSVMNKFKKHALRVIAEHLSVEEVAGIKDMFEKMDLNKDNMINFDELKLGLHKLGHQMADADVQILMDAADVDGNGSLDYGEFVALSVHLRKIGNDEHLHKAFAYFDRNQSGYIEIDELRESLADDLGANHEEVINAIIRDVDTDKDGKISYDEFAAMMKAGTDWRKASRQYSRERFTSLSLKLQKDGSLQLTTTQ
|
May play a role in signal transduction pathways that involve calcium as a second messenger.
|
Q84SL0
|
Q9TKR9
|
MATK_AUSBL
|
Intron maturase
|
Austrosteenisia
|
MDEYQVYLELDRSRNHDFLYPLIFREYIYGLAYGHDLNRSVFVENISYDNKSSLLIVKRLITRMYQQTYLIIFPNDSNKNPFWGYNNNFYSQIISEGFVIVVEIPFFLQFSSSLEETKIVKYYKNLRSIHSIFPLFEDKFTYLNHESDIRIPYPIHLEILVQILRYWIKDVPFLHLLRLFFYYYCNWNSLITPQKSISTFSKNNPRFFLFLFNFYVWEYESIFLFLRNKSTHLRLKSFRVLIERISFYAKVEHLVEVFAKDFSYTLSFFKDPFIHYVRYQGKSILVSKNMPLLMNKWKSYFIHLWQCHFDVWSQPRTIHIKQLSKHSFYFLGYFLNVQLNLSVVRSQMLQNSFLTEIVMKKLDTIVPIILLIRSLAKAKFCNVLGHPISKPVWADLSDFDIIDRFLWICRNFSQYYNGSSKKKSLYRIKYILRLSCIKTLSRKHKSTVRAFLKRLDSEKLLEEFFTEEEDIFSLIFSKTSSTLQRLYRGRIWYLDLLFSNDLINYS
|
Usually encoded in the trnK tRNA gene intron. Probably assists in splicing its own and other chloroplast group II introns.
|
Q9TKR9
|
P55659
|
Y4TE_SINFN
|
Probable amino-acid ABC transporter periplasmic-binding protein y4tE
|
Sinorhizobium
|
MTHLKISKTAPAVARFLPAGRIASVAAALSLFLSAQLAGAVTLEEVKARGYITIAIANEMPGSYTDPNGEVKGSEADVARRVLEKLGIKPENIQWVVTTFGSLIPGLQANRFDMTAAGMAIRPERCEKVIYSEPNSSYGEGMLVIKGNPRNFHSYEDVAQQGKIAIMAGADQLRMMQALGVPNENIITIAANADAISAVATGRADAYAAAASTAADLAKKSDKVELATPFQDPVIDGKIQRSWGAFSFNKESADLRDKFNEALLEFRKTDEFKQLLLGYGYLPESIAAIPDKTTKELCSN
|
Probably part of the binding-protein-dependent transport system y4tEFGH for an amino acid.
|
P55659
|
Q5YYW9
|
SYI_NOCFA
|
Isoleucyl-tRNA synthetase
|
Nocardia
|
MADDSNSAYPRVDYGAGTGAAFPDLERRVLEAWAADDTFRASIENRSGAAEFVFYDGPPFANGLPHYGHLLTGYVKDVIPRFQTMRGKRVDRRFGWDCHGLPAEIEAEKQLGITDKSQIDAMGLAEFNAACKSSVLRYTGEWRDYVTRQARWVDFDNDYKTLDLDFMESVMWAFKSLYDKGLIYQGFRVLPYSWYEQTPLSNQETRLDDAYKMRQDPAVTVDMVLSVPGEHPLRELDGANALIWTTTPWTLPSNLAIAVHPDVRYVHLRAADGTRYVLAAERVSHYSREFGEDATVLAEFEGAALVGLSYRPPFDFFLGHPNAHRVLAADYVTTDSGTGVVHMAPAFGEEDMEVCSANDIELVQPLDPGGRFTSMVPPYEGLMVFDANPVIIKDLKAAGKLLRHETIEHSYPHSWRSGQPLIYMAVPSWFVAVTKFRDRMVELNKQITWVPEHIRDGQFGKWLEGARDWNISRNRYWGSPIPVWVSDDPAYPRVDVYGSLEELERDFGVRPTDLHRPAIDQLTRPNPDDPTGRSMMRRVPEVLDCWFESGSMPYAQVHYPFENKEWFDSHFPGDFIVEYNGQTRGWFYTLHVLATALFDSPAFKTVAAHGIVLGDDGLKMSKSKGNYPDVNEVFDRDGSDAMRWFLMSSPILRGGNLIVTERGIREGVSHALRPLWNAWTFLQLYASKPGEWRTDSTHVLDRYILAKLAQTRDGMTEALEVYDIAGACEELRTFADALTNWYVRRSRSRFWSEDRDAVDTLHTVLEVATRLAAPLLPLISEVIWRGLTGGRSVHLADWPAAADLPADPELVSTMDEVRTVCSTVLSLRKAKNLRVRLPLAEVTIAAPDAERLAPYADIVADEVNVKKVDLTTDVAVHGRFELAVNARAAGPRLGKDVQRVIKAVKAGDWTESADGVVSAAGITLLPEEYTQRLVAAEPESTAALPGNAGLVVLDSVVTEELEAEGWARDLVRELQETRKSLGLDVSDRIHVVLEVPEARRSWAQTHRDLIAGEILATSLEFGTAGEPAAELAGGVRASVRKA
|
Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile).
|
Q5YYW9
|
B6JAP3
|
DAPF_AFIC5
|
PLP-independent amino acid racemase
|
Afipia
|
MTVLANHSFAKMNGIGNEIVIVDLRNTDSQLSAAEARAIAAPGGVPYDQLMVLQKPRMPGTTAFVRIYNNDGSEAGACGNGMRCVAKRVFGESGAQAATFETRAGLLNCWQGPSPDLYTVDMGTPKFGWQDIPLAEEFRDTRYIELQIGPIDAPVLHSPSVVSMGNPHAIFWVDDIEAYDLERLGPLLENHPIFPERANITLAHVVDRNHIRMRTWERGAGLTLACGSAACATAVAAARLKRTDRTVEMSLPGGDLTIEWRESDDHVLMTGAAVLEYEGLFDPDLFAALA
|
Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine and an essential component of the bacterial peptidoglycan.
|
B6JAP3
|
A4UM14
|
VTU4_DROSI
|
Vitelline membrane protein Vm32E
|
Sophophora
|
MKIVALTLVAFVALAGASCPYAAPAPAYPAPAAPSGYPAPPCPTNYLFSCQPNLAPAPCAQEAQAPAYGSAGAYTEQVPHYVGSPNREQVQQFHQRIGMAALMEELRGLGQGIQGQQY
|
Major early eggshell protein.
|
A4UM14
|
P21334
|
CRTI_NEUCR
|
Phytoene desaturase (3,4-didehydrolycopene-forming)
|
Neurospora
|
MAETQRPRSAIIVGAGAGGIAVAARLAKAGVDVTVLEKNDFTGGRCSLIHTKAGYRFDQGPSLLLLPGLFRETFEDLGTTLEQEDVELLQCFPNYNIWFSDGKRFSPTTDNATMKVEIEKWEGPDGFRRYLSWLAEGHQHYETSLRHVLHRNFKSILELADPRLVVTLLMALHPFESIWHRAGRYFKTDRMQRVFTFATMYMGMSPFDAPATYSLLQYSELAEGIWYPRGGFHKVLDALVKIGERMGVKYRLNTGVSQVLTDGGKNGKKPKATGVQLENGEVLNADLVVVNADLVYTYNNLLPKEIGGIKKYANKLNNRKASCSSISFYWSLSGMAKELETHNIFLAEEYKESFDAIFERQALPDDPSFYIHVPSRVDPSAAPPDRDAVIALVPVGHLLQNGQPELDWPTLVSKARAGVLATIQARTGLSLSPLITEEIVNTPYTWETKFNLSKGAILGLAHDFFNVLAFRPRTKAQGMDNAYFVGASTHPGTGVPIVLAGAKITAEQILEETFPKNTKVPWTTNEERNSERMRKEMDEKITEEGIIMRSNSSKPGRRGSDAFEGAMEVVNLLSQRAFPLLVALMGVLYFLLFVR
|
Phytoene desaturase involved in the carotenoid biosynthesis pathway. Converts phytoene into 3,4-didehydrolycopene via the intermediary of phytofluene, zeta-carotene, neurosporene and lycopene, by introducing up to five double bonds into phytoene.
|
P21334
|
O06913
|
FRDA_HELPY
|
Quinol-fumarate reductase flavoprotein subunit
|
Helicobacter
|
MKITYCDALIIGGGLAGLRASIACKQKGLNTIVLSLVPVRRSHSAAAQGGMQASLANAKKSEGDNEDLHFLDTVKGSDWGCDQQVARMFVTTAPKAIRELASWGVPWTRIKKGDRPAVVNGEHVTITERDDRHGYILSRDFGGTKKWRTCFTADATGHTMLYAVANEALHHKVDIQDRKDMLAFIHHDNKCYGAVVRDLITGEISAYVSKGTLLATGGYGRVYKHTTNAVICDGAGAASALETGVAKLGNMEAVQFHPTALVPSGILMTEGCRGDGGVLRDKFGRRFMPAYEPEKKELASRDVVSRRILEHIQKGYGAKSPYGDHVWLDIAILGRNHVEKNLRDVRDIAMTFAGIDPADSKEQTKDNMQGVPANEPEYGQAMAKQKGWIPIKPMQHYSMGGVRTNPKGETHLKGLFCAGEAACWDLHGFNRLGGNSVSEAVVAGMIIGDYFASHCLEAQIEINTQKVEAFIKESQDYMHFLLHNEGKEDVYEIRERMKEVMDEKVGVFREGKRLEEALKELQELYARSKNICVKNKVLHNNPELEDAYRTKKMLKLALCITQGALLRTESRGAHTRIDYPKRDDEKWLNRTLASWPSAEQDMPTIEYEELDVMKMEISPDFRGYGKKGNFIPHPKKEERDAEILKTILELEKLGKDRIEVQHALMPFELQEKYKARNMRLEDEEVRARGEHLYSFNVHELLDQHNANLKGEHHE
|
The fumarate reductase enzyme complex is required for fumarate respiration.
|
O06913
|
B5XU35
|
CCA_KLEP3
|
Phosphatase
|
Klebsiella
|
MKSYLVGGAVRDALLGLPVKDRDWVVVGATPQQMLDAGYQQVGRDFPVFLHPQSREEYALARTERKSGAGYTGFTCYAAPDVTLEADLLRRDLTVNALAQDADGTIIDPYGGQNDLRLRLLRHVSPAFSEDPLRVLRVARFAARYAHLGFRIAEETQALMHAMVEAGELAHLTPERVWKETESALTTRNPQVFFQTLRDCQALKVLFPEIDALYGVPAPAKWHPEIDTGLHTLMTVTMAAMLSPDVDVRFATLCHDLGKGLTPKALWPRHHGHGPAGVKLVEQLCARLRVPNDIRDLAKLVAEYHDLIHTLPILQPKTLVKLFDSIDAWRKPQRVQQIALTSEADVRGRTGFEASDYPQGRLLLEAWEVAQSVSTKEVVAAGFKGAQIREELTRRRIAAVAQWKEQRCPQPQG
|
Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. Also shows phosphatase, 2'-nucleotidase and 2',3'-cyclic phosphodiesterase activities. These phosphohydrolase activities are probably involved in the repair of the tRNA 3'-CCA terminus degraded by intracellular RNases.
|
B5XU35
|
C1KWJ1
|
RECU_LISMC
|
Recombination protein U homolog
|
Listeria
|
MAIGYPNGKKYAASHEVLPQQKRKAPVTYGKRGMSLEDDLNDTIAYYLTHEIAVIHKKPTPVQIVSVDYPKRSSAKIKEAYFKTPSTTDYNGVYKGKYVDFEAKETQNTTSFPLSNFHDHQMTHMANVLKQDGIVFVIIAFQKLGETHFIPFEKFYPFWERMQSGGRKSVTIAEIQDVSDQIPYGLNPRLDFLQSIDKLYF
|
Endonuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves mobile four-strand junctions by introducing symmetrical nicks in paired strands. Promotes annealing of linear ssDNA with homologous dsDNA. Required for DNA repair, homologous recombination and chromosome segregation.
|
C1KWJ1
|
B2I6R7
|
ACCA_XYLF2
|
Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha
|
Xylella
|
MNPNYLDFEQPIADLEAKIQDLRTASAGPSVNVDIEVRALENKLRLRTAQIFRNLSAWQISQLARHPRRPYTLDYISIVCDEFQELAGDRTLADDKAIVGGLARIGHRPVMLIGHQKGRDNKERLMRNFGMPKPEGYRKALRLMKLAERFGLPLLTFIDTMGAWPGIDAEERNQSEAIATNLIEMAELKIPVICTVIGEGGSGGALAIGIGDRTLMLEYSTYSVITPEGCASILWKDAAKASDAAEQLNLTARRLKEFGLIDKVIREPIGGAHRNPQQMANRLKAVLLNELEALDKVPLVTLLNQRHKRLRTYGAYENH
|
Component of the acetyl coenzyme A carboxylase (ACC) complex. First, biotin carboxylase catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the carboxyltransferase to acetyl-CoA to form malonyl-CoA.
|
B2I6R7
|
A1SLL4
|
SYP_NOCSJ
|
Prolyl-tRNA synthetase
|
Nocardioides
|
MIMRMSSLFVRTLREDPADAEVPSHRLLVRAGYIRRAAPGIYTWLPLGLRVLRKIENVIREEMDAIGAQEMLFPALLPREPYEATNRWTEYGDGIFRLQDRKGADYLLGPTHEEMFTLVVKDLYSSYKDLPLSIYQIQTKYRDEARPRAGLLRGREFVMKDSYSFDVDDAGLDVSYQKHRDAYVRIFDRLGFEYVIVEAMSGAMGGSKSEEFLAKASVGEDTYVRCTLCDYAANVEAVHSPPIPPVPYDDAPAAHAEQTPDTPTIETLVAHLNERFPREDRPWAASDTLKNVVFSVHHPDGATEALAVGLPGDREVDAKRLEAHLGEGVVFEPFGEADFAARPTLAKGYIGPGALGEKKPAGVRYLLDPRVVEGTRWVTGADAAGSHVIDLVAGRDFSGDGLIEVAEVRDGDPCPRGDGGTLETARGIEMGHIFQLGRKYADALDLKVLDEQGKLVTVTMGSYGIGPSRAVAAIAEGTHDELGLAWPREVAPADVHIVATGKDEHVFAAAERIAHELDKQGVEVLYDDRPKVSPGVKFKDAELIGVPTIVVVGKGLAAGTIEVKDRRTGQRQDVPADHLVDRVIAIVRA
|
Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Ala-tRNA(Pro). The misacylated Cys-tRNA(Pro) is not edited by ProRS.
|
A1SLL4
|
P27580
|
CYAA_GLUNI
|
Adenylyl cyclase
|
Glutamicibacter
|
MSTEHTNTPRADSPQSAAEAVRGARQHAPAATPAESDPILELAEAMEGPLRIPAHTPEAVRDTVASLEKRLIGGQREFRRREVASEAGVSLHSARKLWRAIGFPELSDDEVFFTEADKKALGTMVGMVREGALTEETAISLMRSVGQMTDRMVVWQIEALVEDMIANQNLSDRQARRQLFSLLPEIIPAIEDLLLYSWRRQLNSAVHRMALRVETGVAAYNQDRGEDDGGTPLPLARAVGFADLVSYTSLSRRMNERTLAQLVQRFEAKCAEIISVGGGRLVKTIGDEVLYVAETPQAGAQIALSLSRELAKDELFPQTRGAVVWGRLLSRLGDIYGPTVNMAARLTSLAEPGTVLTDAITANTLRNDARFVLTAQEITAVRGFGDIQPYELSAGEGAGLVID
|
Plays essential roles in regulation of cellular metabolism by catalyzing the synthesis of a second messenger, cAMP.
|
P27580
|
A6GYX5
|
DAPF_FLAPJ
|
PLP-independent amino acid racemase
|
Flavobacterium
|
MKLYKYQGTGNDFIMIDNRLQIFPKQNTALIQKLCDRRFGIGADGLILLENDQSTDFKMVYYNSDGNQSTMCGNGGRCLVAFAKKLNIIKNKTTFIAIDGLHHATINENDIISLQMKNVEEVNIHDNYVFLNTGSPHHVQFADNLSNFDVKNEGAKIRYSDLYGQAGSNINFVHQTSPTQFSIRTYERGVEDETLSCGTGATATAIAMKATGKTNSNNITINVQGGKLEVSFNQENSIFTNIFLKGPAEFVFETTI
|
Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine and an essential component of the bacterial peptidoglycan.
|
A6GYX5
|
Q6ZQQ2
|
S31D1_HUMAN
|
Protein FAM75D1
|
Homo
|
MENILCFLNSYTETGLSPDSHWLDIDPNFICLSGLGLFILYLFYVVLTLYSSPTEKNNDIQKHQGRAKRRRKGGTFKGFPDWKSFQREEEEERKLLSLLKSFGPPVSCSPRGQHHDTNHFRRLLCPDPVCRVCKRATADIQQLLSWESLKDAAPSVSPLASSASATESSFTLASTPSATPPEDLILSPRPKASPPPPLILSPDLITTLADLFSPSPLRDPLPPQPVSPLDSKFPIDHSPPQQLPFPLLPPHHIERVESSLQPEASLSLNTIFSFGSTLCQDISQAMNPIDSCARHHGPPIPSALPPEDCTVTQSKSSLTILKTFPEMLSLGGSGGSSTSAPTIKGIDHSHLASSEFTWWQPHAKDSFSSNFVPSDFMEELLTLHSSEAFLGGHSVANLIEPVNISFLSHDILALLERQVKKRGDFLMWKENGKKPGSFPKQLRPNYQLNSSRNMLTSIAVKHDLAESFPFWASKGKLEWQHIHQQPPHSKCFEDHLEQKYVQLFWGLPSLHSESLHPTVLVQRGHSSMFVFFNGITNTSISHESPVLPPPQPLSLPSTQPLPLPQTLPQGQSPHLTQVKSLAQPQSPFRALLPSPLFLIRICGVCFHRPQNEARSLLPSEINHLEWNVLQKVQESLWGLPSVVQKSQEDFCPPAPNPELVRKSFKVHVPISIIPGDFPLSSEVRKKLEQHIRRRLIQRRWGLPRRIHESLSLLRPQSKISELSVSERIHGPLNISLVEGQRCNVLKKSASSFPRSFHERSSNMLSMENVGNYQGYSQETVPKDHLLHGPETSSDKDLRSNSERDLETHMMHLSGNDSGVRLGQKQLENALTVRLSKKFEEINEGRMPGTVHSSWHSVKQTMSLPEKSHSQIKHRNLVTLVSEDHCVDTSQEISFLSSNKQKMLEAHIKTFRMRMLWGLPLKVLESIEIFKSKADLSTSFSHFDLPSSATFISQGDSKDGVSKSRSRSTFQGEKLGTTSSVPILDRPHPVSSPVVQEGQGTLRRQFSDTDHDLIETDSKDGASTSLRRGTTDFQSEKLDSTSSFPILGHSYLVTSPVNQEKQGTLRREFSDTDNDLTESVRTTEDGRQTFLPPPHSIVDEVSQKQTVLASRCSAELPIMQAGAGCESWDKRKSSFHNVDRLQGSRKTFPVTNALQSQTRNNLTTSKSGSCSLTNVKASTSNETEIFPPRISVPQDPKSSYLKNQMLSQLKLVQRKHSQPQSHFTDMSFALDNLSSKDLLTNSQGISSGDMGTSQVVHVHLEDSGIRVAQKQEPRVPTCVLQKCQVTNFPPAVNRVSPVRPKGGELDGGDAGLGTSQRRRKSLPVHNKTSGEVLGSKSSPTLKTQPPPENLFRKWMKTSLQWFNKPSISYEEQESSWEKGSSLSSCVQNIGRVIRAAFTGTTEAQKIRKDTREFLEEKLGHRHGIDITCPQEPLSFPVGLGKAQHNPEVHVRAEPVQGCPCNYRAPSCKVTRTKSCSQQAIFVGQNYPTRIRQIIDKDRQPQKVEAFKGKILCQSHPQSMPHRKPVPHPNPTCRRQVSLVCPAVPTSAKSPVFSDVPFLTGQKMLPKHLQGGKFPPTK
|
May play a role in spermatogenesis.
|
Q6ZQQ2
|
Q9RSJ5
|
RL17_DEIRA
|
50S ribosomal protein L17
|
Deinococcus
|
MRHGKAGRKLNRNSSARVALARAQATALLREGRIQTTLTKAKELRPFVEQLITTAKGGDLHSRRLVAQDIHDKDVVRKVMDEVAPKYAERPGGYTRILRVGTRRGDGVTMALIELV
|
Binds to the 23S rRNA.
|
Q9RSJ5
|
B2VE18
|
BAMA_ERWT9
|
Outer membrane protein assembly factor BamA
|
Erwinia
|
MAMKKLLIASLLLSSATVYGADGFVVKDIHFDGLQRVAVGAALLSMPVRVGDTVSDEDLSNTIRALFATGNFEDVQVLRDGNTLIVQVKERPTIASITFSGNKAVKEDMLKQNLEASGVRVGEALDRTTVSTIEKGLEDFYYSVGKYSASVKAVVTPLPRNRVDLKLVFTEGVSAKIQQINVVGNKAFSSDELISRFQLRDDVPWWNVVGDRKYQKQKLAGDLETLRSFYLDRGYARFNIDSTQVSLTPDKKGIYITVNITEGEQYKLSGVAVSGNLAGHSAEIEGLSKVKPGELYNGAKVTRTEDDIKKLLGRYGYAYPRVQTQTEIDDANKTVKLHINVDAGNRYYVRKVRFEGNDTSKDAVLRREMRQMEGAWLGSDLVEQGKDRLNRIGYFETVDTDTVRVPGSADQVDVVYKVKERNTGTLNFGVGYGTESGVSFQAGITQENWLGTGNTVGISGTKNDYQTYAEFSLTDPYFTVDGVSLGGRLFYNNFKADDADLSDYTNKSYGLDGTLGFPVNENNTLRVGLGYVHNSLSNMQPQVAMWRYLRSVGMNPSLSSNEDFSTDDFTFNYGWTYNTLDRGFFPTAGNRTNLNGKVTIPGSDNAFYKATLDTQQYVPLDQDHSWVLLGRGRVGYADGLSGKELPFYENFYAGGSSTVRGFRSNTIGPKAAYYNNGSSNCSGSDVAKICSSDDAVGGNAMAVASAELITPTPFLSEKYANSVRTSLFVDAGTVWDTHWDDTAATLGAGVPDYSKPGNIRMSAGLALQWMSPLGPLVFSYAQPFKKYDGDKAEQFQFNIGKTW
|
Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamD, the core component of the assembly machinery.
|
B2VE18
|
O31339
|
CYSA_BACC1
|
Sulfate-transporting ATPase
|
Bacillus cereus group
|
MSIQIQGVSKQYGTFQALTDIHLDIPKGELVALLGPSGSGKTTLLRIIAGLEEADEGSISFEGEDLTDIHVKNRQVGFVFQHYALFKHMNVFENVAFGLKVRKKSLRPSAEAIEEKVTELLKLVKMDGFAKRYPAQLSGGQRQRIALARALAVEPKILLLDEPFGALDAKVRKELRRWLRKLHDEFQITSVFVTHDQEEALDVADRIVVMNEGRIEQMGTPEEVYENPASPFVYDFLGNVNLFHGRVHKGKLNVGSVELEAPEHKHISNVDGVAYVRPHHLSISRTKQSVDAIPAKVSYSHAVGPVVYVELKRDGTDEYLEAEISKEQFRQLSIQAGDVVYVQPKEVKVFIPEDFVI
|
Part of the ABC transporter complex CysAWTP involved in sulfate/thiosulfate import. Responsible for energy coupling to the transport system.
|
O31339
|
Q8AXX8
|
SOX10_XENLA
|
SRY (sex determining region Y)-box 10
|
Xenopus
|
MSDDQSLSEVEMSPVGSEDPSLTPDPLPPHAHSSPDDDDDDDEEEEEETKVKKEQDSEDERFPVCIREAVSQVLNGYDWTLVPMPVRVNGGSKSKPHVKRPMNAFMVWAQAARRKLADQYPHLHNAELSKTLGKLWRLLNENDKRPFIEEAERLRMQHKKDHPDYKYQPRRRKNGKPSPGEGDGSSEAEGGAASIQAHYKNSHLDHRHGSPMSDGNSEHSTGQSHGPPTPPTTPKTELQAGKSDGKRDGSHALREGGKPQIDFGNVDIGEISHDVMSNMETFDVNEFDQYLPPNGHAGHPSHIGGYTSSYGLTGALAAGPSAWALAKQHSQTVADSKAQVKTESSSTSHYTEQPSTSQLTYTSLGLPHYGSAFPSISRPQFDYADHQPSSSYYSHSAQASSLYSAFSYMGPPQRPLYTAISDPPSVAQSHSPTHWEQPVYTTLSRP
|
Acts early in neural crest formation, functioning redundantly with the other group E Sox factors sox8 and sox9 to induce neural crest progenitors. Acts downstream of wnt-signaling at the neural plate border. Involved in the specification of neural crest progenitors fated to form the pigment cell lineage.
|
Q8AXX8
|
Q5XF36
|
KMS1_ARATH
|
Protein KILLING ME SLOWLY 1
|
Arabidopsis
|
MGSAGVASSSSDVAISALREKHEKEVENLTLTTQPLNTLKLFVEATIQYIKRSISYLLAHGGWFILITTLLVVSGGLLVTVDGPHGKHVEEVLEYVRYGLWWIALGVASSIGLGSGLHTFVLYLGPHIALFTLKATLCGRVDLKSAPYDTIQLKRVPSWLDKSCSEFGPPLMISAAGSRVPLTSILPQVQLEAILWGIGTALGELPPYFISRAASISGSTVDGMEELDGSSTEDSGFMATHLNRVKRWLLTHSQHLNFFTVLVLASVPNPLFDLAGIMCGQFGIPFWEFFLATLIGKAIIKTHIQTIFIICVCNNQLLDWMENELIWILSHVPGLASMLPGLTAKLHAMKEKYIDAPSPVPSHIKVKKWDFSFASIWNGIVWLMLLNFFVKIVTATAQRHLKKKQEKEMATLTHSD
|
Involved in the early secretory pathway. Required for the correct export of secretory products from the endoplasmic reticulum (ER) and involved in the maintenance of ER integrity.
|
Q5XF36
|
P02028
|
HBB_CHLAE
|
Hemoglobin beta chain
|
Chlorocebus
|
VHLTPEEKTAVTTLWGKVNVDEVGGEALGRLLVVYPWTQRFFESFGDLSSPDAVMGNPKVKAHGKKVLGAFSDGLAHLDNLKGTFAQLSELHCDKLHVDPENFKLLGNVLVCVLAHHFGKEFTPQVQAAYQKVVAGVANALAHKYH
|
Involved in oxygen transport from the lung to the various peripheral tissues.
|
P02028
|
P52489
|
KPYK2_YEAST
|
Pyruvate kinase 2
|
Saccharomyces
|
MPESRLQRLANLKIGTPQQLRRTSIIGTIGPKTNSCEAITALRKAGLNIIRLNFSHGSYEFHQSVIENAVKSEQQFPGRPLAIALDTKGPEIRTGRTLNDQDLYIPVDHQMIFTTDASFANTSNDKIMYIDYANLTKVIVPGRFIYVDDGILSFKVLQIIDESNLRVQAVNSGYIASHKGVNLPNTDVDLPPLSAKDMKDLQFGVRNGIHIVFASFIRTSEDVLSIRKALGSEGQDIKIISKIENQQGLDNFDEILEVTDGVMIARGDLGIEILAPEVLAIQKKLIAKCNLAGKPVICATQMLDSMTHNPRPTRAEVSDVGNAVLDGADCVMLSGETAKGDYPVNAVNIMAATALIAESTIAHLALYDDLRDATPKPTSTTETVAAAATAAILEQDGKAIVVLSTTGNTARLLSKYRPSCPIILVTRHARTARIAHLYRGVFPFLYEPKRLDDWGEDVHRRLKFGVEMARSFGMVDNGDTVVSIQGFKGGVGHSNTLRISTVGQEF
|
May be used by cells under conditions in which the level of glycolytic flux is very low.
|
P52489
|
Q9ZH75
|
DNAA_STRAQ
|
Chromosomal replication initiator protein DnaA
|
Streptomyces
|
MADVPADLAAVWPRVLEQLLGEGQQGIEPKDKQWIERCQPLALVADTALLAVPNEWGKRVLEGRLAPLISETLTRECGRPIRIAITVDDSAGEPPSPPAPPMHQSHQSQQGHRYPAQQRDDAPRGDAYDGYGHRPSDDGMPTRRPAYPDYQQQRPEPGAWPRTQEDLSWQQPRHGGYQDREQPSGEPYRESESYRERENEQYREQAPEQWRQPYGTGRPQQPQHDYRSGPPEHQGYEQQRPDRQDQGQGPRQGGHGPGRTGGSVPGPMGAQPAPAPGPGEPHARLNPKYLFDTFVIGASNRFAHAAAVAVAEAPAKAYNPLFIYGESGLGKTHLLHAIGHYARSLYPGTRVRYVSSEEFTNEFINSIRDGKGDTFRKRYRDVDILLVDDIQFLASKESTQEEFFHTFNTLHNANKQIVLSSDRPPKQLVTLEDRLRNRFEWGLTTDVQPPELETRIAILRKKAVQEQLNAPPEVLEFIASRISRNIRELEGALIRVTAFASLNRQPVDLGLTEIVLKDLIPGGEESAPEITAPAIMAATADYFGLTVDDLCGSSRTRVLVTARQIAMYLCRELTDLSLPKIGAQFGGRDHTTVMHADRKIRALMAERRSIYNQVTELTNRIKNG
|
Plays an important role in the initiation and regulation of chromosomal replication. Binds to the origin of replication; it binds specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'-TTGTCCACA-3'. DnaA binds to ATP and to acidic phospholipids.
|
Q9ZH75
|
Q5F1R7
|
RS12_GLAPU
|
30S ribosomal protein S12
|
Glaesserella
|
MATINQLVRKPRVKKVVKSNVPALEACPQKRGVCTRVYTTTPKKPNSALRKVCRIRLTNGYEVTSYIGGEGHNLQEHSVVLIRGGRVKDLPGVRYHTVRGALDCAGVKDRKQGRSKYGVKRPKS
|
Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S subunit contacting proteins on the other side and probably holding the rRNA structure together. The combined cluster of proteins S8, S12 and S17 appears to hold together the shoulder and platform of the 30S subunit.
|
Q5F1R7
|
Q466D4
|
NDK_METBF
|
Nucleoside-2-P kinase
|
Methanosarcina
|
MEQTYVMVKPDGVQRGLVGEIISRIEKRGLKIVALRMNVISEATAKEHYSEHAAKPFFPGLVGFITSGPSVSMVVEGKDAIRVMRAINGATNPVDAAPGTVRGDFALDVGRNVVHASDSPEAAAREIAIHFKDSEIGNYSRIDEVCLYE
|
Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate.
|
Q466D4
|
Q6DCV1
|
AB1IP_XENLA
|
APBB1-interacting protein 1
|
Xenopus
|
MDEIDEMFSNLLGEMDLLTQSLEIETLPPPTRSASTTEINFSVGFKDLNESLNALEDNDLDALMAELVADITDAEQNVATYNNKSTAPFPPADASNSYHFHPPPMPSIITEDLSLLPPPPEFDPHYPPPPPDPLTEPKTQEELESKAKANKINLALSKMKEAKVKKRIVKVHMIDSSTKTLMVEEHQTVRDVLDNLFEKTHCDCSIEWCLFEVTPELQIERFFEDHENIVEILANWTRDSVNTIHFLEKNEKYAVFKKPQNFYMATKGSADLKDMNEKNKVSLLEQSFCGASVTVPELEAALYLKEDGKKSWKKRYFLLRASGIYYVPKGKTKTSRDLACFVQFDNVNVYYGTQYRMKYKAPTDHCFVLKHPQIQKESQYIKYLCCEDPWLLHQWVTGIRIAKYGKILYDNYKTAVQRGGLASHWSTLGSSSVSTAAGSSQGNGQICQNVTTISSSFSDAWKHGEANKQEKKSSEVNKPETKSATPTVTKRPPPTPRRASSISRVTDHPAFPPKPKAINTDIMSGPPQFPPPEPLQPADDFLPPPPPDFFDAPPDFLPPSPPSFMSNAENPPPPPVTQLQMSNAPAPPPPPPPPAPAANVPPLPVKKHPPKPPKRQSIVGPMPGTNAHGGAGGQPDFMSDLMKALQKKREPPT
|
Appears to function in the signal transduction from Ras activation to actin cytoskeletal remodeling.
|
Q6DCV1
|
C6DKX3
|
MGSA_PECCP
|
Methylglyoxal synthase
|
Pectobacterium
|
MEFTTRTIAAQKHIALVAHDHCKQSLLDWVGTNKEQLKEHTLYATGTTGNLIQLNTGLPVKSMLSGPMGGDQQVGALISEGKIDLMIFFWDPLNAVPHDPDVKALLRLATVWNIPVATNRATADFLVNSALFKEPVQIAIPDYQRYLQDRLK
|
Catalyzes the formation of methylglyoxal from dihydroxyacetone phosphate.
|
C6DKX3
|
P02500
|
CRYAA_TRIIN
|
Alpha-crystallin A chain
|
Trichechus
|
MDVTIQHPWFKRALGPFYHNRLFDQFFGEGLFEYDLLPFQSLFRTVLDSGISEVRSDRDQFLILLDHFSPEDLTVKVLDDFVEIHGKHNERQDDHGYISREFHRRYRLPSNVDKSALSCSLSADGMLTFCGPKVQSGMDASHSERAIPVSREEKASSAPNS
|
Contributes to the transparency and refractive index of the lens. In its oxidized form (absence of intramolecular disulfide bond), acts as a chaperone, preventing aggregation of various proteins under a wide range of stress conditions. Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA.
|
P02500
|
C4L423
|
PRMA_EXISA
|
Ribosomal protein L11 methyltransferase
|
unclassified Exiguobacterium
|
MKWSEICVHTTQLAVEAVSNLLHEVGAQGVVIEDVEDFDRMMAEDHFGEIWDVSDRETYPTSGVHVKAYVPASGDFQDLLSNLKKEIERLRTMLDIGSGDVTVAEIDEEDWAHSWKQYYKPVKISQQLTIVPLWEEYTPQPEENVILLDPGMAFGTGTHPTTMLCIQAIENYIREGDHVIDVGTGSGVLSIAAAKLGAASVKALDLDSVAVESARQNVETNGVGELVQVDTGDLLKGVEGEYDLVVANILADVILLFIEDAYARTKSGGRFITSGIIGEKRAEVTNALVAAGFEIEETRVMEDWVAIIAKKG
|
Methylates ribosomal protein L11.
|
C4L423
|
Q5IBL2
|
YCF3_PLALA
|
Photosystem I assembly protein Ycf3
|
Plantago
|
MSRSRTNGNFIDKTFSIVANILLQIIPTTSGEKEAFTYYRDGMSAQSEGNYAEALQNYYEAMRLEMDPYDRSYILYNIGLIHTSNGEHTKALEYYFRALERNPFLPQAFNNMAVICHYRGEQAVREGDSEIAEAWFDQAAEYWKQAIALTPGNYIEAHNWLKITRRFE
|
Essential for the assembly of the photosystem I (PSI) complex. May act as a chaperone-like factor to guide the assembly of the PSI subunits.
|
Q5IBL2
|
C1DCW5
|
SYY_LARHH
|
Tyrosyl-tRNA synthetase
|
Laribacter
|
MSERNVIQELEARGLIAQQTDSGALQKLLESESVTLYCGFDPTADSLHLGHLVPLLMLRRFQEAGHRPIALVGGATGMIGDPSFKAAERKLNTPDVIAGWVDKIRRQLSPFLSFEGDNAAVMANNYDWFGQMNVLEFLRDIGKHFSVNAMIKKESVQQRISREDQGISFTEFSYSLLQGNDFAELNCRFGCKLQIGGSDQWGNITAGIDLTRRLNQQQVFGLTVPLITNSDGTKFGKSEGNAVWLDPQKCSPYKFYQFWLGVADADVYRFLRYFTFLSIEQIDAIEAADKTSGTRPQAQRILAEEATRLVHGDEALKAAQRITESLFSNDLSALTAEDLAQLALDGLPVLDMAGQGDGLIDALAASGLAKSKSEARTFIQSGAVSINGIKAEGLDYCLTGNDRLFGRYTLLKRGKKLYALLVWPA
|
Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).
|
C1DCW5
|
A4WQ76
|
EX7L_CERS5
|
Exodeoxyribonuclease VII large subunit
|
Cereibacter
|
MSDLFEDPAPARNTPEYTVSELSGAVKRVIEGEFGLVRVRGEIGRVSRPASGHLYFDLKDDRAVIAAICWKGQAGRLSVRPEEGMEVVATGRMTTFPGQSKYQIIVEDMAPAGAGALMAMLEKRRAALAAEGLFDAARKRPLPFLPRVIGVVTSPSGAVIRDILHRLRDRFPSHVLIWPVAVQGEKCAPEVAAAIRGFNALPDGGPIPRPDLLIVARGGGSLEDLWGFNEEIVVRAAAESRIPLISAVGHETDTTLIDHAADRRAPTPTAAAEMAVPVRLDLLAGLDGQGARLSRCAAETIRRRDQRLRDLSRALPRLDSLVAGPSQRFDLWSARLSGALGQSVAARRARLEPLGAHLRPRLLADLVARQKDRLADRGRGLETCLGRRSERARDRFEALSGRLAPAFARLVAESERTNRRDAAALGALAARLEAAPEARLLRLADRLEALDRLRQTLGYRETLRRGYAVVRADGEVVTTKTAAERAASLEIEFQDGRLTLGARKPRKGKAEPPAQGSLL
|
Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
|
A4WQ76
|
Q8TME2
|
NADA2_METAC
|
Quinolinate synthase 2
|
Methanosarcina
|
MENGVVMEDRLIAEEIKKLKEERNAIILAHFYTRGEVREFADFVGDSLSLCREAVNSKADVIVFAGVHFMAESASILSPEKSVLLPVPEAGCPMADMVTVETLRKEKEKHPDAAVVCYVNSSAAVKAESDICCTSSNAVNVVNSVENREIIFVPDKNLGAFVSLHTDKKIHLRPGFCHVHENIGKEDIEELKNLHPEAEFLAHPECRPEVMSFADHILSTSGIVKEAGRSESTEFIIGTEKEIVQSLKRKYPDRKFYPVSKKAVCYNMKKVTLESILNSLQNMEYEVQVPEHVRAKAKKALDRMLSVSGT
|
Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate.
|
Q8TME2
|
A5F6Y4
|
IHFB_VIBC3
|
Integration host factor subunit beta
|
Vibrio
|
MTKSELIERLCAEQTHLSAKEIEDAVKNILEHMASTLEAGERIEIRGFGSFSLHYREPRVGRNPKTGDKVELEGKYVPHFKPGKELRERVNL
|
This protein is one of the two subunits of integration host factor, a specific DNA-binding protein that functions in genetic recombination as well as in transcriptional and translational control.
|
A5F6Y4
|
Q7V0B9
|
RNZ_PROMP
|
tRNase Z
|
Prochlorococcus
|
MNITFLGTSSGVPTLTRNVSSLALKLSQTAEVWLFDCGEGTQHQLMKSNIKSSQIKKIFITHMHGDHIYGLPGLLATLGLSGNSNGIEIYGPSELKSFVTSALESSFCKLSFPLRFRAVEDFASLNKILFENDKLKVHCACLKHRLPAYGYRVSEKDKPGVFDIKKAEDSNIPPGPIYSELQAGKTVQLKDGRSFNGQDFCGPPRKGESFVYCTDTVFSKSAVNLSKNADLLVHESTFSKEDEKMAYEKLHSTTIMAAKTALLSNVKKLIITHLSPRYTQRSSIKPSDLLKEAQKIFPNTYLAKDFLTAEIK
|
Zinc phosphodiesterase, which displays some tRNA 3'-processing endonuclease activity. Probably involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA.
|
Q7V0B9
|
V6F2C2
|
MAMX_MAGGM
|
Magnetochrome MamX
|
Magnetospirillum
|
MNTKAVAHPDIAVWIMALGIAFSMALVLTALFNANPWEDHTYDLAPPIVAGMAAPHRDGREKMVCSSCHIVTPASAATGPGAGTLPIVEGTPAPHVDGREKMACASCHTIVKKGSVAKSGKASPAPVAFSQGMPLPEAMSVALAVTPAPAPLGNEAHERMVPFRYQGKIVSVAGAGTRSVWGDIYIQINDGINPPMWIDLAPLWFLQAEGCLVRPGMFVKGTAFRDPTQASAGLDYAMSVMANGEVCALRDDHLNGLWANVGGVDAEER
|
Required for correct biomineralization of the magnetosome, maybe via redox control . May function with MamY, MamZ amd Mms6 in biomineralization (Probable).
|
V6F2C2
|
Q9N126
|
RDH8_BOVIN
|
Photoreceptor outer segment all-trans retinol dehydrogenase
|
Bos
|
MADAPRTVLISGCSSGIGLELAVQLAHDPRQRYQVVATMRDLGKKGTLETAAGEALGQTLTVAQLDVCSDESVAQCLNCIQGGEVDVLVNNAGVGLVGPLEGLSLAAMQNVFDTNFFGAVRLVKAVLPSMKRRRQGHIVVVSSVMGLQGVVFNEVYAASKFAMEGFFESLAVQLLQFNIFISLVEPGPVVTEFEGKLLEQVSTAEFPGTDPDTLSYFRDLYLPASRELFHNVGQSPQDVAKVIVKVIGSARPPLRRRTNTRYTPLIALKAMDPSGSLYVRTSHCLLFRWPRLLNLGLRCLACSCFRTPVWPR
|
Retinol dehydrogenase with a clear preference for NADP. Converts all-trans-retinal to all-trans-retinol. May play a role in the regeneration of visual pigment at high light intensity.
|
Q9N126
|
B9WM88
|
UTP25_CANDC
|
U three protein 25
|
Candida
|
MAKQFKRKSNGVSENNRKRGRQELRKVTRTAARKQQDESHEDGLDVNNNFEEDNAEEEIDEEEVGEQDYDDRGKAYSALLTLLKSEHKEKSKNVTSGSLQVDRTNPSDSEDEEIAGANVEEDENEGEDENVDENGIDSESDNEDEDTVNRLSTDPFESHFNLPTEDYLAKEEKLVLKDNEKWCTVDKRTYSDLAVTSLVQLPPGEPINPPLLKSSKLNEYTIKKRVLDSYQQAYGAELTDLESTLINPILNYRDVNFQYKSFKNKSYRKLYTLHALNHIFKTRDRILKNTAKLHAAKEDSEELELRDQGFTRSKVLIMLPTRDSCYEVVEQLIKLSGTEQQENKKKFNDQFYVKAAPPANKPDDFRDAFKGNNSDFFCIGLKFTRKSLKLYSSFYSSDIILASPIGLSMILENPDKKKRQYDFLSSIEVLIVDRCNQIEMQNWDHVNTVMKYVNKVPKEFHDADFSRIRMWSINDQAKLLRQTLVFCEYLTPSINNLISSKSHNLSGKVKFKPIINSENSMMNSIGLKIKQIFQRFDSQSPLQDPDARYKYFINAILPSLLKTSSYEDGIMIFIPSYFDYLRVKNYLKTSTKFTFGSIDEYSSQSKLTKTRQEFASGKIKLLLYTERLHYFRRYEISGVKTLIMYGLPSNPLFYKELIRFIGKSVFKEECDLDLALVKILFSKWDAVNLEKMVGNERAPVLCNSMNELYEFR
|
DEAD-box RNA helicase-like protein required for pre-18S rRNA processing, specifically at sites A0, A1, and A2.
|
B9WM88
|
C0H692
|
SCR3_ACRMI
|
Small cysteine-rich protein 3
|
Acropora
|
MGVKLNICLLLLLVAIISSQGFNLRKKEDSKDEKPFGNYRRGSPCSNYEGSCTPNHIPCPPGSHECRQLPGCYPGVERCCCQY
|
This recombinant protein induces severe neurotoxicity on zebrafish larvae (Danio rerio) at a concentration of 230 mg/ml, but does not show toxicity when injected in blowfly larvae (Sarcophaga falculata). All fish incubated with this protein died within 16 hours of exposure . Has also been claimed to be implied in calcification, but this function seems improbable .
|
C0H692
|
Q733H9
|
HUTU_BACC1
|
Imidazolonepropionate hydrolase
|
Bacillus cereus group
|
MEKVKQTIRAPRGTELQTKGWVQEAALRMLMNNLDPEVAEKPEELVVYGGIGRAARNWESYNAIVDSLKTLESDETLLVQSGKPVAIFKSHEDAPRVLLANSNLVPKWANWNHFRELEKKGLMMYGQMTAGSWIYIGTQGILQGTYETFGEAARQHFGGSLKGTLTLTAGLGGMGGAQPLAVTMNGGVVIAIDVDKRSIDRRIEKRYCDMYTESLEEALTVANEYKEKKEPISIGLLGNAAEILPELVKRNITPDLVTDQTSAHDPLNGYIPVGYTLEEAAKLREEDPERYVQLSKESMTKHVEAMLAMQAKGAITFDYGNNIRQVAFDEGLKNAFDFPGFVPAFIRPLFCEGKGPFRWVALSGDPEDIYKTDEVILREFADNEHLCNWIRMARQQVEFQGLPSRICWLGYGERAKFGRIINEMVANGELSAPIVIGRDHLDCGSVASPNRETEAMKDGSDAVADWPILNALINSVNGASWVSVHHGGGVGMGYSLHAGMVIVADGTEAAAKRIERVLTSDPGMGVVRHVDAGYDLAVETAKEKGVNIPMMK
|
Catalyzes the conversion of urocanate to 4-imidazolone-5-propionate.
|
Q733H9
|
Q0AX18
|
QUEA_SYNWW
|
Queuosine biosynthesis protein QueA
|
Syntrophomonas
|
MQHDKNEDIYRLSTYYYDLPPELIAQYPAEYRDSSRLLVLDRKSGDLNDRAFKDISLYLKKGDALVLNETRVIPARFFAYKESGARVEILLLKKLGDDWEALVKPARRLKAGSRVFLSPDKPLVIEIVEELDFAGGRRVRFQDSVDEDTLLQEQGHIPLPPYINRPDEELDRERYQTVYACKSGSVAAPTAGLHFTPDLLKEITLQGINIVRIVLHVGMGTFRPVKNEDIRQHNMHLEYYEVAEDAAALLNLTRESGGQIVAVGTTVVRTLESVYNKDCGFLAGKGETNKYIFPGYQFRAIDKLLTNFHLPGSSLLMLVAGFAGTESTLAAYRHAVENRYRFFSYGDAMLVI
|
Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA).
|
Q0AX18
|
Q7KSD8
|
TAD2A_DROME
|
dADA2a
|
Sophophora
|
MSFMNPVDMVDEDAADLQFPKVALLHIFTTLNCLFAVEPLGPQVKRFIHAHQNEHTRNSMVLYNPHTLHRYLEEMEEKTRDQNSSVPSATKDANRCATCRCSLTEPYIKCSECLDTLLCLQCFSRGKEAFSHRNNHAYIIVRDNIQVFADEPHWTARDERILLKTLRTHGYGNWEAVSQALDQRHEPAEVRRHYHDCYFGGIFERLLNLKHARDSYVPERMPYVFKMRSLDPPRHDDIASMQFRLSAGYRCARGDFDTPYDTSAESLLSIMVDHRGRDDDNEASESEFEREVTEELQLGLVRAYNNRLRERQRRYKIMRQHGLIMPNRTVSWISKYVHAFGSDASCMRFLGFMQICPDPIKFDMLLESLRYYRELHSQLHKLYDLREHGVRTLSGAKLYARLSKERQQAQRDYSRLKQTDAFDWQQLVQHYESNRSGDPGPLAINSKLYVMNTRRKASPIEIGGGKHFTHCLTPTEYNFSLIPDLPGYSKLDDGERKLCSVARLVPQSYLDYKNQLVTEQAKLGYLRLADARRLIKIDVNKTRQIYDFLLEHGHISRPPSYG
|
GCN5-independent Rpb4 complexes are highly enriched in decondensed chromosome puffs so may play a role in RNA polymerase II-dependent transcription.
|
Q7KSD8
|
Q48514
|
TRA3_LEPBO
|
Transposase for insertion sequence element IS1533
|
Leptospira
|
MKRKVYVGMDVHKETIQIAYLTSNSKEILKEQQIKHNEVQIKKFIKKLKLEWNEIHCCYEAGVTGYPLYRYLKSLGVNCILLAPGKIPRQNTDKIKTDKRDAIKLARLMRSWRIGIDSCFPVEEDEAVRDYLRSRDSLRLDLGRNRQRLMKFLLRKDIKLLPTTKYWTVSHYKWLNNLHFNNEILQETFNDYYSRVRVQEENLKAMDKKIQEIAESEPYREKVGILRCFRGVDYLTAMFLLCEVNDFKPIQNGRFVHEFSWTCSWRIFQRFQKKTNRDYVKLEVPRLRRILTEAAWQHRFPGTGSKIITARRSGQPALVVALAEKASLRLHKKFRNLQPKRKKLLK
|
Required for the transposition of the insertion element.
|
Q48514
|
Q83F34
|
FTSL_COXBU
|
Cell division protein FtsL
|
Coxiella
|
MNTATRVIVAQNVRTRNRTFQITKQGVVIVALVIALLCSAFGVVYFKDLNRRLFIQYQTLQREKAEELIQWGKLLLEQTTWSTQSRVQRIAEQQLGMQLPSAKEVILVNADAMIE
|
Essential cell division protein. May link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic.
|
Q83F34
|
Q7M734
|
OTOP1_RAT
|
Otopetrin-1
|
Rattus
|
MPGDRGALSSPAASSGSPSAAPSGIAACPPPPSPLARASPQASGPRRGASVPQKLAETLSSQYGLNVFVAGLLFLLAWAVHATGVGKSDLLCVLTALMLLQLLWMLWYVGRSYMQRRLIRPKDTHAGARWLRGSITLFAFITIVLGCLKVAYFIGFSECLSATEGVFPVTHAVHTLLQVYFLWGHAKDIIMSFKTLERFGVIHSVFTNLLLWANSVLNESKHQLNEHKERLITLGFGNITIVLDDHTPQCNCTPPALCSALSHGIYYLYPFNIEYQILASTMLYVLWKNIGRRVDSSRHQKMQCRFDGVLVGSVLGLTVLAATIAVVVVYMIHIGRSKSKSESALIMFYLYAITVLLLMGAAGLVGSWIYRVDEKSLDESKNPARKLDADLLVATASGSWLLSWGSILAIACAETRPPYTWYNLPYSVLVIVEKYVQNIFIIESVHLEPEGVPEDVRTLRVVTVCSGEAAALAASSLGSQGTAQDGSPAVNGNLHLQQRCEKEDQEADWEGATGTTRCLDFLQGGMKRRLLRNITAFLFLCNISLWIPPAFGCRPEYDNGLEEIVFGFEPWIIVVNLAMPFSIFYRMHAAAALFEVYCKI
|
Proton-selective channel that specifically transports protons into cells. Proton channel activity is only weakly-sensitive to voltage. Proton-selective channel activity is probably required in cell types that use changes in intracellular pH for cell signaling or to regulate biochemical or developmental processes. In the vestibular system of the inner ear, required for the formation and function of otoconia, which are calcium carbonate crystals that sense gravity and acceleration. Probably acts by maintaining the pH appropriate for formation of otoconia. Regulates purinergic control of intracellular calcium in vestibular supporting cells. May be involved in sour taste perception in sour taste cells by mediating entry of protons within the cytosol. Also involved in energy metabolism, by reducing adipose tissue inflammation and protecting from obesity-induced metabolic dysfunction.
|
Q7M734
|
Q07817
|
B2CL1_HUMAN
|
Apoptosis regulator Bcl-X
|
Homo
|
MSQSNRELVVDFLSYKLSQKGYSWSQFSDVEENRTEAPEGTESEMETPSAINGNPSWHLADSPAVNGATGHSSSLDAREVIPMAAVKQALREAGDEFELRYRRAFSDLTSQLHITPGTAYQSFEQVVNELFRDGVNWGRIVAFFSFGGALCVESVDKEMQVLVSRIAAWMATYLNDHLEPWIQENGGWDTFVELYGNNAAAESRKGQERFNRWFLTGMTVAGVVLLGSLFSRK
|
Isoform Bcl-X(S) promotes apoptosis.
|
Q07817
|
Q8CPQ4
|
MENB_STAES
|
1,4-dihydroxy-2-naphthoyl-CoA synthase
|
Staphylococcus
|
MTRQWEILREYDEIKYEFFEGIAKVTINRPEVRNAFTPKTVAEMIDAFSRARDDQNVSVIVLTGEGDKAFCSGGDQKKRGHGGYVGEDDIPRLNVLDLQRLIRVIPKPVIAMVRGYAIGGGNVLNVVCDLTIAADNAIFGQTGPKVGSFDAGYGSGYLARIVGHKKAREIWYLCRQYNAQEALDMGLVNTVVPLEQVEDETVKWCKDIMQHSPTALRFLKAAMNADTDGLAGLQQMAGDATLLYYTTDEAKEGRDAFKEKRNPDFDQFPKFP
|
Converts o-succinylbenzoyl-CoA (OSB-CoA) to 1,4-dihydroxy-2-naphthoyl-CoA (DHNA-CoA).
|
Q8CPQ4
|
B3EKA1
|
NUOA_CHLPB
|
NUO1
|
Chlorobium
|
MDQTLSDFGTVFVFLLLGIIFVVGGYLTARLLRPSRPNPEKLAIYECGEEAVGSAWVKFNIRFYVVALIFIIFDVEVVFLFPWATVFKQLGEFALIEALVFAGILVIGLVYAWVKGDLDWVRPTPNIPKMPVLEEDESQVVS
|
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
|
B3EKA1
|
Q2PS07
|
2SS_FAGES
|
Buckwheat 16 kDa major allergen
|
Fagopyrum
|
MKLFIILATATLLIAATQATYPRDEGFDLGETQMSSKCMRQVKMNEPHLKKCNRYIAMDILDDKYAEALSRVEGEGCKSEESCMRGCCVAMKEMDDECVCEWMKMMVENQKGRIGERLIKEGVRDLKELPSKCGLSELECGSRGNRYFV
|
Seed storage protein.
|
Q2PS07
|
B1VHG8
|
LIPA_CORU7
|
Sulfur insertion protein LipA
|
Corynebacterium
|
MTVSANGRRMLRIEAKNSQTPIEAKPRWIRTTAKMGPEYRDMKNRVTGMSLHTVCQEAGCPNIHECWEDREASFLIGGDTCSRRCDFCQIKSGKPTPLDRDEPRRVAESVREMGLKYATVTGVTRDDLDDEGAWLYAEVVRKIHELNPNTGVENLTPDFSNKPELLQIVFESQPEVFAHNLETVPRIFKRIRPAFKYERSLEVIRAAHDYGLITKSNLILGMGETEEEVVEAMRDLREAGTDILTITQYLRPTSMHHPIERWVRPEEFVAHSEAAYDMGFPAVMSGPLVRSSYRSGRLYAQAMRARGREIPENLSHLNEKLDGSTQQEATNLLDKYGASEETPVAYR
|
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
|
B1VHG8
|
Q9CIJ4
|
NADK_LACLA
|
ATP-dependent NAD kinase
|
Lactococcus
|
MNFGKKVWLIGNSSEKSKKTLNKLSKILKAEHFVFDDINPEIVISVGGDGTLLRAMHMYEYQLDRVRFLGVHTGHLGFYTDFTDEDLFEVVEALYDENPAQAIHYPLIRVQVSFTDGYQIVRHVLNEATIRRASKTMVGDVRISDYLFERFRGDGLSISTPTGSTAYNKSIGGAVVHPRVKAMQVAEIASLNNVVYRTLGSPMIVAEKDTITVCPAPEDDYSLTFDQLTFEYKNIKSIEFSLDGTTISFANCAHTPFWERVSKSFIGEVE
|
Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
|
Q9CIJ4
|
B4EAX1
|
RLMN_BURCJ
|
tRNA m2A37 methyltransferase
|
Burkholderia cepacia complex
|
MTSETSVNLLDFDAEGLVAYCGSLGEKPFRAKQLQRWIHQYNAGDFDGMTDLAKSLREKLKGRASIVMPEIASDHVSTDGTRKWLIDVGNGNAVETVFIPEETRGTLCVSSQAGCAVNCRFCSTGKQGFSRNLSTAEIIGQLRMAEFALRASLGRAPGPNGKAERVVTNVVMMGMGEPLLNYSAVVPAMRLMLDDNAYGLSRRRVTLSTSGVVPMMDRLGAELPVALAVSLHAPNDALRDELVPLNKKYPLRELMAACQRYLKVAPRDFITFEYCMLDGVNDTEAHARELLAVTRDVPCKFNLIPFNPFPESGLIRSKPEQIKRFAQVLIDAGVVTTVRKTRGDDIDAACGQLAGAVKDRTRLAERTGAAGKIIEVRAV
|
Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity.
|
B4EAX1
|
Q96C28
|
ZN707_HUMAN
|
Zinc finger protein 707
|
Homo
|
MDMAQEPVTFRDVAIYFSREEWACLEPSQRALYRDVMLDNFSSVAALGFCSPRPDLVSRLEQWEEPWVEDRERPEFQAVQRGPRPGARKSADPKRPCDHPAWAHKKTHVRRERAREGSSFRKGFRLDTDDGQLPRAAPERTDAKPTAFPCQVLTQRCGRRPGRRERRKQRAVELSFICGTCGKALSCHSRLLAHQTVHTGTKAFECPECGQTFRWASNLQRHQKNHTREKPFCCEACGQAFSLKDRLAQHRKVHTEHRPYSCGDCGKAFKQKSNLLRHQLVHTGERPFYCADCGKAFRTKENLSHHQRVHSGEKPYTCAECGKSFRWPKGFSIHRRLHLTKRFYECGHCGKGFRHLGFFTRHQRTHRHGEV
|
May be involved in transcriptional regulation.
|
Q96C28
|
A5CC62
|
PNP_ORITB
|
Polynucleotide phosphorylase
|
Orientia
|
MFNEILKKVDWHGNVLSLSTGKIARNADGAVLASMGNTSVLCTVVFDKNTKKDMDFFPLGVYYREMAYAAGKIPGGFIKKEGKFSEYEVLVSRLIDRSIRPLFDSNFRNDTQIICTVMSYDPRYSPDILAIIGSSAALAISGIPIVKPIGAARVGIVNDEFILNPVIHDNTGVNELDLVVAATFDSVTMIEAQACEIDEEKMLAAIEFGYKSLKPVINAIEEIKSSIRKDIFEVTARPHLRYNDEILKHFSSDIKSALLLQTKNERNQQLQLIQQKVIDYFSSKANSEANDGDDILNIEKALDDAKSKIFRDLVLQNKTRIGNRAVDEIRPIICEAGLFNTVHGSALFTRGDTQSLATITLGSSTDEQIVEQLNKCERQNFLLDYIFLPYSVGEISPLRAASRREIGHGWLAKKAIQLVIPSKDVFPYTIRIVSEITQSDGSSSMATVCSASLSLMEAGVPIKTHVAGIAMGLVLGEGNKFEILSDISGCEDHLGDMDFKVASTKNGITALQLDIKVQGINLSMIESTFRQAKIGINHILNVMNNTISCPKSELSTYAPMVQTLEIQKEKIRDVIGLGGKVIKELCKTFDVEIDISENGEVKVWGNVGENVKKAVQSIENIVFVPQIGDIFDGEVVKVIESGAFIKYVTGRDGFVHISEINDTHIKDINAHVKLGDKVKVKIIGIDHKNRVKLTLRTDKEHCKNKNEQYNDITTTTGGVKKKIKIAPKEAAVISNRKYFD
|
Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
|
A5CC62
|
B3ELP8
|
PAND_CHLPB
|
Aspartate 1-decarboxylase alpha chain
|
Chlorobium
|
MRVHLLKSKIHNAVVTSGDLQYEGSITIDSELLDLANMIPNEKVLCVNNNNGERFETYIIEGKAGSREIQLNGAAARCALPGDEIIIMTFAEIEAREAKSFKPMILIVDKHNNPKRRHLVGEEDNPL
|
Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
|
B3ELP8
|
Q2S937
|
RPOA_HAHCH
|
Transcriptase subunit alpha
|
Hahella
|
MQRSLNEFLTPRTIEVNQINATHAKVTLEPLERGFGHTLGSALRRILLSSMPGCAVVEVEIDGVLHEYSTVEGVQEDVIEILLNLKNLAIKMHNRDEATLSLNKKGAGPVLASDIQLDHDVEIANPDMVICNLNSNGDVKMKLKVARGRGYEPADQRNSADDETRAIGRLQLDSSFSPVLRVAYNVESARVEQRTDLDKLVIDLETNGTIDPEEAIRRAATILQQQLAVFVDFDQQNEPEKVEEQEEIDPILLRPVDDLELTVRSANCLKAENIYYIGDLIQRTEVELLKTPNLGKKSLTEIKDVLASRGLSLGMRLENWPPASIRGDDRVLGG
|
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
|
Q2S937
|
P41802
|
ELIA1_PHYCR
|
Acidic elicitin A1
|
Phytophthora
|
MNFRALFAATVAALVGSTSATTCTTTQQTAAYVALVSILSDSSFNQCATDSGYSMLTATSLPTTDQYKLMCASTACNSMIAKIISLNAPDCELTVPTSGLVLNVYSYANGFSATCASL
|
Induces local and distal defense responses (incompatible hypersensitive reaction) in plants from the solanaceae and cruciferae families. Elicits leaf necrosis and causes the accumulation of pathogenesis-related proteins. Might interact with the lipidic molecules of the plasma membrane.
|
P41802
|
O70608
|
SYCP2_RAT
|
Synaptonemal complex lateral element protein
|
Rattus
|
MPVRPDPQQLEKCIDDALRKNDFKPLVTLLQIDICEDVKIKCSKQFLRKLDDLICRELHKKDIQTISNILISIGRCSKNIFILGQTGLQTMIKQGLVQKMVSWFENSKEIILSQRQSKDEAVMNMIEDLFDLLMVVYDVNDEGKNQVLESFIPHICALVIDSRVNFCIQQEALKKMNLMLDRIPQDANKILCNQEILTLMSNMGERILDVGDYELQVGIVEALCRMTTEKRRQELAYEWFSMDFIANAFKKIKDCEFETDCRIFLNLVNGMLGDRRRVFTFPCLSAFLGKYELQIPSDEKLEEFWIDFNLGSHTLSFYIAGDDDDHQWEAVTVPEEKVDMYNIEVRESKKLLTLTLKNIVKISKKEGKELLLYFDAALEITNVTKKLFGGNKYKEFTRKQDISVAKTSIHVLFDASGSQILVPESQPSPVKENLIHLKEKSNLQKKLTNPLEPDNSSSQRDRKNSQDEITTPSRKKMSEASMIVPDTDRYTVRSPILLINTSTPRRSRAPLQAIHSAEKAVSKTSESGVDYAVSLKSRQSDGRNRGNNRANHNKTATVQNKGHEHHESPDQTFNEIEETLSDAYAVEKVDKPVLPGVLDISKNKAHSRWACWTPVTTIKLCNNQRSCALPGDTFTQDTGVNKKCTKQKSVSDDDSEETQRVKYSKDVIKCNKSEEAEVCERNIQEQNHPKYSQKKNTANAKKNDWHIESETTYKSVLLNKTTEESLIYKKTCVLSKDVNTTICDKSPSRKSMRSHTKSRKELMSEVTSCELDEIPVRENSKGKRFTGTAESLINLINKRYNSSDDMISTRKLKEPRDGSGFSKKPELQFNKVQRKSYRKLKTVVNVTSECPLNDVYNFSLNGADEPVIKLGIQEFQATTREASMDNSIKLVDVRNRDERDLSLKTKDERILSHERKTLFSDTETECGWDDSKTDISWLRKPKSKRLMDYSRNKNTKKCKSIKSRSSTEKGQPRSTVVLSKNIAKNDYEVIVDGRTRLPRRATKTKKNYKDLSTSGSESESEKEISYLFKDKLPTKEETVHSSAQTKKLPKKQQKVFNTEALKGQPSEEQKNSSTLRNGREDSLYLSSASVSGSSSSVEVMRCTEKITERDFTQDYDYITKSLSPYPKAASPEFLNRSNRVVGHGKSPRISETSAVCVRKSCSPASGLPFSPRHTTKNNSVMNIKNTNSVINNQRTQHCNSYSDVSSNSSEKLYMEPESPDSCENHVQSKREENHAASPFSLSSEKIEKIWFDMPNDNTHVSGPSQRGSKRRMYLEEDELSNPSEAEVQEAEEREHLVSKKLCQREHFDQHTSETSLSTPEFSVPKDWQQELQGAGMFYDNINSDYKRKTDTQHKIMDDFTTKTLKLTQQHLLAMACQARGHRDENIDKFQVTLLDELEKVEKDSQTLRDLEKEFVDIEEKIVHKMRAFHQSERERFRALKTSLDKSLLVYNSVYEENVLTSEMCLMKANMKMLQDKLLKEMHEEELLNIRRGLESLFKDHEGNNA
|
Major component of the axial/lateral elements of synaptonemal complexes (SCS) during meiotic prophase . Plays a role in the assembly of synaptonemal complexes. Required for normal meiotic chromosome synapsis during oocyte and spermatocyte development and for normal male and female fertility. Required for insertion of SYCP3 into synaptonemal complexes. May be involved in the organization of chromatin by temporarily binding to DNA scaffold attachment regions. Requires SYCP3, but not SYCP1, in order to be incorporated into the axial/lateral elements.
|
O70608
|
Q9HAT2
|
SIAE_HUMAN
|
Sialic acid-specific 9-O-acetylesterase
|
Homo
|
MVAPGLVLGLVLPLILWADRSAGIGFRFASYINNDMVLQKEPAGAVIWGFGTPGATVTVTLRQGQETIMKKVTSVKAHSDTWMVVLDPMKPGGPFEVMAQQTLEKINFTLRVHDVLFGDVWLCSGQSNMQMTVLQIFNATRELSNTAAYQSVRILSVSPIQAEQELEDLVAVDLQWSKPTSENLGHGYFKYMSAVCWLFGRHLYDTLQYPIGLIASSWGGTPIEAWSSGRSLKACGVPKQGSIPYDSVTGPSKHSVLWNAMIHPLCNMTLKGVVWYQGESNINYNTDLYNCTFPALIEDWRETFHRGSQGQTERFFPFGLVQLSSDLSKKSSDDGFPQIRWHQTADFGYVPNPKMPNTFMAVAMDLCDRDSPFGSIHPRDKQTVAYRLHLGARALAYGEKNLTFEGPLPEKIELLAHKGLLNLTYYQQIQVQKKDNKIFEISCCSDHRCKWLPASMNTVSTQSLTLAIDSCHGTVVALRYAWTTWPCEYKQCPLYHPSSALPAPPFIAFITDQGPGHQSNVAK
|
Catalyzes the removal of O-acetyl ester groups from position 9 of the parent sialic acid, N-acetylneuraminic acid.
|
Q9HAT2
|
Q8NQJ3
|
ODHI_CORGL
|
Oxoglutarate dehydrogenase inhibitor
|
Corynebacterium
|
MSDNNGTPEPQVETTSVFRADLLKEMESSTGTAPASTGAENLPAGSALLVVKRGPNAGARFLLDQPTTTAGRHPESDIFLDDVTVSRRHAEFRINEGEFEVVDVGSLNGTYVNREPRNAQVMQTGDEIQIGKFRLVFLAGPAE
|
An essential component of the PknG signaling pathway. When unphosphorylated, it inhibits the activity of 2-oxoglutarate dehydrogenase. When phosphorylated it does not inhibit 2-oxoglutarate dehydrogenase.
|
Q8NQJ3
|
A6UR78
|
HEM1_METVS
|
Glutamyl-tRNA reductase
|
Methanococcus
|
MLVIKADYKKYPLPVLESMRINEDEFYGKYDACIIVQTCNRIEAYFDEEINDIEKIIPDFKGFDVIKGKKATLHFLNVACGMDSMILGENQILGQIKSSYHKSKELKKTSKYLENLFLKAIHVGQRVRAETKINEGGVSIGSAAVELAEMKLGLKNRNVLLIGAGEIGTLVAKALIEKHIKAVIVANRTYERAETLAKELKGMAVHFDKLKEAINFSDVIICATSSPHYILEKSDLLDVGNKIIIDIANPRDVDDSVRELENISLYTIDDLRNISDKNLQKRLKEVPIVENIIEEEYGILLKQIEKTNVEEVIKDFNTYIEDVRKKELEKAVRLCKNKSPDEIMENFSKAFVKRITHDFVSYSLSVSKEDLLNSIWWKK
|
Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
|
A6UR78
|
P59186
|
RS3_STRMU
|
30S ribosomal protein S3
|
Streptococcus
|
MGQKVHPIGMRVGIIRDWDAKWYAEKEYADYLHEDLAIRKFIQKELADAAVSTIEIERAVNKVNVSLHTAKPGMVIGKGGANVDALRAQLNKLTGKQVHINIVEIKSPDLDAHLVGENIARQLEQRVAFRRAQKQAIQRTMRAGAKGIKTQVSGRLNGADIARSEGYSEGTVPLHTLRADIDYAWEEADTTYGKLGVKVWIYRGEILPARKNTKGGK
|
Binds the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation.
|
P59186
|
Q7NVB8
|
KPTA_CHRVO
|
Probable RNA 2'-phosphotransferase
|
Chromobacterium
|
MIARNPIKQDPAMRNTQDDHSRFLSLVLRHQPETIGLQLDDQGWADIGELLARLAAKGRNLGRKQLEKIVLDNDKQRFAISEDGLRIRANQGHSIKIDLGLAACEPPDRLYHGTASRFLDAILAEGLRPGQRQHVHLSADGQTARKVGARHGKPVVLEIDARAMRQAGLAFYRSDNGVWLIDGVPPVFIRQTEAR
|
Removes the 2'-phosphate from RNA via an intermediate in which the phosphate is ADP-ribosylated by NAD followed by a presumed transesterification to release the RNA and generate ADP-ribose 1''-2''-cyclic phosphate (APPR>P). May function as an ADP-ribosylase.
|
Q7NVB8
|
P22355
|
PSPB_RAT
|
Pulmonary surfactant-associated proteolipid SPL(Phe)
|
Rattus
|
MAKLHLQWLLLLPTLCSLGAATESASSPDCAQGPKFWCQSLEQAIQCRALGHCLQEVWGHAGANDLCQECEDIVHLLTKMTKEDAFQDTIRKFLEQECDILPLKLLVPRCRQVLDVYLPLVIDYFQGQIKPKAICSHVGLCPLGQTKPEQKPEMLDAIPNPLLNKLVLPALPGAFLARPGPHTQDLSEQQLPIPLPFCWLCRTLIKRVQAVIPKGVLAVAVSQVCHVVPLVVGGICQCLAERYTVLLLDALLGRVVPQLVCGLVLRCSTADAIGPALPALEPLIEKWPLQDTECHFCKSVINQAWNTSEQAMPQAMHQACLRFWLDRQKCEQFVEQHMPQLLALVPRSQDAHTSCQALGVCEAPASPLQCFQTPHL
|
Pulmonary surfactant-associated proteins promote alveolar stability by lowering the surface tension at the air-liquid interface in the peripheral air spaces. SP-B increases the collapse pressure of palmitic acid to nearly 70 millinewtons per meter.
|
P22355
|
P66338
|
RS10_STRAW
|
30S ribosomal protein S10
|
Streptomyces
|
MAGQKIRIRLKAYDHEVIDSSAKKIVETVTRTGASVAGPVPLPTEKNVYCVIKSPHKYKDSREHFEMRTHKRLIDILDPTPKTVDSLMRLDLPAGVDIEIKL
|
Involved in the binding of tRNA to the ribosomes.
|
P66338
|
B8ELF8
|
RL22_METSB
|
50S ribosomal protein L22
|
Methylocella
|
MSKEKTPRALKDNEAKAVARMLRISPQKLNLLAQLIRGKKVERALAELEFSRKRAAFDVRKTLESAIANAENNHSLEVDDLVVAEAFVGKALVMKRFSPRARGRSGKIQKPFSHLTIVLREVAVAAQA
|
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.
|
B8ELF8
|
A8F5E8
|
PYRH_PSELT
|
Uridine monophosphate kinase
|
Pseudothermotoga
|
MYQRVLVKLSGEVMCGEGSRGFDQSNINYLVQQIAQIVDYGVNVGIVIGAGNIFRGEELSEIPHSLADQIGMLGTVINALYLKGSLQKVGIKCVVVSQVTSLPSIRPIHYDDINLYFDAGYVVIFAGGTSNPFFTTDTAAALRAVEMGANLLIKATKVDGIYDSDPKKNKSARKLDKISYYDAISRGLKVMDMEAFSICGRYKLPIVILNFFEDGSLLRAVRGEDVGSIIMPD
|
Catalyzes the reversible phosphorylation of UMP to UDP.
|
A8F5E8
|
Q65RK9
|
MEND_MANSM
|
Menaquinone biosynthesis protein MenD
|
Basfia
|
MSVSTFNRCWSKVILETLTRHGVKHFCIAPGSRSTPLTLEANRLQEQRRALCHTHFDERGLGFFALGLAKSSQTPVAIIVTSGTAAANLYPAIIEARQTGDNLIVLTADRPDELIECGANQAILQQNMFAGYPVASVNLPRPSQDYIVSWLISTLDQACHQQAQQAGVIHINVPFAEPLYDADEDEIDVHPWLAPVQRWLNHNKPWADHQALQEEVVMHEHWDNWRTKRGVIVAGRLTQEQSMGITAWANTMGWVVLTDIQSGVEPSLPYADIWLANKTVREKLLQADLVIQLGYAFVSKRINQFLADFKGEYWIVDESAHRVDPYHHIHTRFTAKVHHWLRAHPPLRQKPWLLEPLALSKFCASFIEQQVGGNLNEASLAHHIERILPNNGILFLGNSLFVRLVDALGKLPEGYPVITNRGASGIDGLLATAAGVGMGSNQPVVAMIGDVSALYDLNSLALFKNVNQPTIIFLINNNGGAIFDMLPVESSVKSEFYRMPHHTEFSQAASMFDLKYARPYTWADLSSVLKQAYSRKEATVIEIKVGPMDGSNTYKRLIEQISYAVIGA
|
Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC).
|
Q65RK9
|
P52837
|
F4ST_FLACH
|
Flavonol 4'-sulfotransferase
|
Flaveria
|
METTKTQFESMAEMIKKLPQHTCSSLKGRITLYKYQDFWGLQNNIEGAILAQQSFKARPDDVFLCSYPKSGTTWLKALAYAIVTREKFDEFTSPLLTNIPHNCIPYIEKDLKKIVENQNNSCFTPMATHMPYHVLPKSILALNCKMVYIYRNIKDVIVSFYHFGREITKLPLEDAPFEEAFDEFYHGISQFGPYWDHLLGYWKASLERPEVILFLKYEDVKKDPTSNVKRLAEFIGYPFTFEEEKEGVIESIIKLCSFENLSNLEVNKSGNSKGFLPIENRLYFRKAKDGDWKNYFTDEMTEKIDKLIDEKLSATGLVLK
|
Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of quercetin 3-sulfate > kaempferol 3-sulfate > isorhamnetin 3-sulfate > patuletin 3-sulfate, but not tamarixetin 3-sulfate. O-sulfation of position 4' of flavonol. May play a role in auxin transport.
|
P52837
|
Q9JRG1
|
DPO4_NEIMA
|
DNA polymerase IV
|
Neisseria
|
MSSRKIIHIDMDAFYASVELREQPHLKGRPVVVAWEGARSVICAASYEARQFGLHSAMSVATAKRLCPQAVYVPPHFDLYRQVSAQIHAVFRRYTDLIEPLSLDEAYLDVTRNFKNIPYASEVAKEIRAAIFAETGLTASAGIAPNKFLAKIASDWRKPNGQFVLPPHKVMAFLETLPLGKIPGVGKVTLKKMQSLGMQTAGDLRRFERGELLNHFGRYGYRLYDLARGTDERPVKAERECLQISTEITLPEDLPLEQAAGHLPHLAEDLWRQITRKNVEAQSVTLKLKTYDFRIITRTLTYSSVLPDCTALLQAAQMLMARVPPQTEDAFRLIGIGVGHLVPKNQQQDLWA
|
Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII.
|
Q9JRG1
|
C0HLM0
|
SCX2_TITMA
|
Toxin Tma2
|
Tityus
|
KKDDYPVDTAERNCKFECNIVDDKGYCDNLCKGRKAEKGYCYSLKASCYCYGLPDDSPTKTSKRCNPNV
|
Inhibits voltage-gated sodium channels (Nav). This toxin shows insect lethality against crickets.
|
C0HLM0
|
P69928
|
NA13_ANTMC
|
Peptide toxin Am-3
|
Antheopsis
|
MNRLIILVVAAVFLGMASAEEDVLKRGFPCRCDSDGPSVHGNPLSGTIWVTSCATGWHKCNSENELFHECCKQG
|
Inhibits voltage-gated sodium channels (Nav).
|
P69928
|
P69882
|
KAD_STRP1
|
Adenylate monophosphate kinase
|
Streptococcus
|
MNLLIMGLPGAGKGTQAAKIVEEFGIAHISTGDMFRAAMANQTEMGRLAKSYIDKGELVPDEVTNGIVKERLAEDDIAEKGFLLDGYPRTIEQAHALDATLEELGLRLDGVINIKVDPSCLVERLSGRIINRKTGETFHKVFNPPVDYKEEDYYQREDDKPETVKRRLDVNMAQGEPILEHYRKLGLVTDIEGNQEITDVFADVEKALLELK
|
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.
|
P69882
|
Q67JT8
|
RS12_SYMTH
|
30S ribosomal protein S12
|
Symbiobacterium
|
MPTINQLVRQGRKKLTEKSASPALKGNPFKRGVCTVVKTTTPKKPNSALRKIARVRLSNNIEVTAYIPGIGHNLQEHSVVLVRGGRVKDLPGVRYHIVRGALDAAGVANRMQGRSKYGAKRPKAGKK
|
Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S subunit contacting proteins on the other side and probably holding the rRNA structure together. The combined cluster of proteins S8, S12 and S17 appears to hold together the shoulder and platform of the 30S subunit.
|
Q67JT8
|
Q55DP8
|
ACY1_DICDI
|
N-acyl-L-amino-acid amidohydrolase
|
Dictyostelium
|
MNSIQENEHVTVFREFLKIRTDHPTPDYESSTKFLVEKAKEYNIPYEVYRETGTPIVLMKIEGLEPNLKTVLLNSHVDVVPAVHDSWKVDPFSAWKDESGNIFGRGTQDMKCVCMQFLEVARRIVQSGQKLKRTLHLSFVPDEEIGGSGKGMEKFVYTEKFRQLNIGLCLDEGLASPTNDFTVFYGERAPWWVHITAVGNAGHGSRFIEGTAIEKLMRTINKMLAFRQEQFESLHHGQHECGKKLGDVTSLNLTVLKAGIPIDHSNNFSYNVIPTQAEAGFDIRIPPTVNLDQFLDQIKEWTAEEGLSFKFASYIPKNEMTKLDSDNKWWENFKESCKKMDINLVTEIFPAATDSRFIRNLGIPAFGFSPINNTPILLHDHNEFLNEKVYLRGIDIFMGIIPNLVNME
|
Involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate).
|
Q55DP8
|
B3EWH5
|
CYCA_PETHY
|
Cyclotide phyb-A
|
Petunia
|
MVGVNSLRSALYLIVLILFVQLTYFSDARVMDVDLSRAFLPLTGIGCGESCVWIPCVSAAIGCSCSNKICYRNGIIPKK
|
Probably participates in a plant defense mechanism.
|
B3EWH5
|
P45509
|
CFA_CITFR
|
Cyclopropane-fatty-acyl-phospholipid synthase
|
Citrobacter freundii complex
|
ISHIAEASESRFVMEDWHNFGSDYDKTLMAWHERFNQAWPELSSRYSATFRRMFNYYLCACAGAFRARDIELWQVLFSRGVEGGIRVYR
|
Transfers a methylene group from S-adenosyl-L-methionine to the cis double bond of an unsaturated fatty acid chain resulting in the replacement of the double bond with a methylene bridge.
|
P45509
|
Q39CH4
|
COAX_BURL3
|
Pantothenic acid kinase
|
Burkholderia cepacia complex
|
MNEPHLLIDAGNSRIKWALADAQRTLVETGAFGHTRDGGADPDWSTLPRPRGAWISNVAGADVAARLDTLLDARWPGLPRTTIRSRHTQCGVTNGYTTPDQLGSDRWAGLIGAHAAFPGEHLLIATFGTATTLEALRADGRFTGGLIAPGWALMMRALGTHTAQLPTLTTDIASGLLAGAQAEPFQVDTPRSLSAGCLYAQAGLIERAWRDLADAWQAPVRLVLAGGAADDVARALTLPHTRHDALILSGLALIAAEAAAATAAQA
|
Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
|
Q39CH4
|
B1LL33
|
MNME_ECOSM
|
tRNA modification GTPase MnmE
|
Escherichia
|
MSDNDTIVAQATPPGRGGVGILRISGLKAREVAETVLGKLPKPRYADYLPFKDADGSVLDQGIALWFPGPNSFTGEDVLELQGHGGPVILDLLLKRILTIPGLRIARPGEFSERAFLNDKLDLAQAEAIADLIDASSEQAARSALNSLQGAFSARVNHLVEALTHLRIYVEAAIDFPDEEIDFLSDGKIEAQLNDVIADLDAVRAEARQGSLLREGMKVVIAGRPNAGKSSLLNALAGREAAIVTDIAGTTRDVLREHIHIDGMPLHIIDTAGLREASDEVERIGIERAWQEIEQADRVLFMVDGTTTDAVDPAEIWPEFIARLPAKLPITVVRNKADITGETLGMSEVNGHALIRLSARTGEGVDVLRNHLKQSMGFDTNMEGGFLARRRHLQALEQAAEHLQQGKAQLLGAWAGELLAEELRLAQQNLSEITGEFTSDDLLGRIFSSFCIGK
|
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.
|
B1LL33
|
Q46IC1
|
GCSP_PROMT
|
Glycine dehydrogenase (aminomethyl-transferring)
|
Prochlorococcus
|
MSKAELKDFTFKSRHIGPTNEDEALMLQHLGYENAEEFISSVIPNEIFDSENNGVSIPDGCDQNKALTEINIISKKNVEHRSLIGLGYHSTVIPPVIQRNVLENPNWYTAYTPYQAEISQGRLEALFNFQTLISELTGLPISNASLLDEATAAAEAISLSLTVRKNKNANKFLVDQEILPQTLDVLKTRCEPLGISLEMFDNNNFEIDKNVFGILIQLPGKNGRIWDPTKIINDAHKCNAIVTIAIDPLAQVLIKPMGEFGADIVVGSAQRFGVPIAFGGPHAAFFATKEIYKRQIPGRIVGQSVDVEGNQALRLALQTREQHIRRDKATSNICTAQVLLAVLSSFYAVHHGPKGLKQIAENVVKYRSNFESILMNLEYPIEKYSAFDSVDVYCSEASEVIQLASEEGYNLRVLPIGSDFENAKGFGVTFDELTCDEEIYKLHQILAQVKGKKTHDLSNFIFENASLIDIPLREKSWLEQSVFNQYQSETDLMRYIHCLVSKDFSLVQGMIPLGSCTMKLNAAAELLPIEWREFSSIHPFAPHTQLTGFHEIINDLENWLSALTGFQGVSLQPNAGSQGEFAGLLVIRSWHQSLGEGHRNICLIPTSAHGTNPASAVMSGFKVVSVKCDEYGNVDLEDLKNKSKIHSKNLAALMVTYPSTHGVFEPNIREMCQVIHQEGGQVYLDGANLNAQVGICRPGSYGIDVCHLNLHKTFSIPHGGGGPGVGPIAVADHLVPYLPGHSIIKCGGQKAISAVSAAPFGSAGILPISWMYIRMMGSDGLRKASSIAILSANYLAKRLDPYYPVLFKDPNGLVAHECILDLRPLKSQLGIEVEDVAKRLMDYGFHAPTISWPVAGTLMVEPTESESLPELDRFCDAMIGIREEIEQIKLGKIDPINNPLKQSPHTLKTVTSDDWDRPYSRKEAAYPLPDQEKYKFWPSVSRINNAYGDRNLICSCPSVQDLEDINSV
|
The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein.
|
Q46IC1
|
B7IHT2
|
KTHY_THEAB
|
dTMP kinase
|
Thermosipho
|
MFIAFEGIDGSGKSTQLNLLSQYLKSKGKKVLNIREPGGTILGEKIREILLDNNLNINKRSELLLFLASRAQLVEEVIKPHLKRGFFVLADRFSDSSIAYQGGARNIGVETVSTLNDFATDNIYPDIVFYIDIPTKIAMERLKDKNLDRLEKEGQIFLEKVRNTYLKLSKLRDNFFIIDGTKSIDNVFAEIKSIVEKHLQS
|
Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
|
B7IHT2
|
B1XYL1
|
MNMG_LEPCP
|
Glucose-inhibited division protein A
|
Leptothrix
|
MLYPQEFDVIVVGGGHAGTEAALAAARMGCDTLLLTHNIETLGQMSCNPSIGGIGKGHLVKEVDALGGAMAAATDESGIQFRILNSSKGPAVRATRAQADRILYKAAIRQRLENQPHLWLFQQAVDDLMVEGDRVVGAVTQVGIRFRARTVVLTAGTFLDGKIHVGLNNYPAGRAGDPPAVSLSARLKELKLPQGRLKTGTPPRIDGRSIDFSKLIEQPGDGVAAADGTPASSPMPVFSFLGSAAQHPRQMPCWITNTNQRTHDILRTGFDRSPMFTGVIEGVGPRYCPSIEDKINRFADKNSHQIFLEPEGLTTNEYYPNGISTSLPFDIQLAAVRTMLGMENAYILRPGYAIEYDYFDPRELKTSFESKAIGGLFFAGQINGTTGYEEAAAQGLYAGANAALQAQGNPPLSFGRDQAYLGVLVDDLITKGVTEPYRMFTSRAEFRLQLREDNADMRLTEIGRSVGLVDDVRWDAFNRKRDAVSRETERLKSTWVHPAILPAADSERLFGKALEHEYNLADLMRRPGISYDTVAEALTIARPGNYVSRETLNSQLGADLAAAVIEQLEIAIKYAGYIDKQNEDVQRAAHYEHLRLPDELDYAQVTALSFEVRQKLTKHRPETLGQASRISGVTPAALSLLLIHLKRGRFKGFTGNDKVAAGPISADAVNTDINDNPAHAATDAA
|
NAD-binding protein involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
|
B1XYL1
|
P25152
|
BSAP_BACSU
|
Leucyl aminopeptidase
|
Bacillus
|
MKKLLTVMTMAVLTAGTLLLPAQSVTPAAHAVQISNSERELPFKAKHAYSTISQLSEAIGPRIAGTAAEKKSALLIASSMRKLKLDVKVQRFNIPDRLEGTLSSAGRDILLQAASGSAPTEEQGLTAPLYNAGLGYQKDFTADAKGKIALISRGDLTYYEKAKNAEAAGAKAVIIYNNKESLVPMTPNLSGNKVGIPVVGIKKEDGEALTQQKEATLKLKAFTNQTSQNIIGIKKPKNIKHPDIVYVTAHYDSVPFSPGANDNGSGTSVMLEMARVLKSVPSDKEIRFIAFGAEELGLLGSSHYVDHLSEKELKRSEVNFNLDMVGTSWEKASELYVNTLDGQSNYVWESSRTAAEKIGFDSLSLTQGGSSDHVPFHEAGIDSANFIWGDPETEEVEPWYHTPEDSIEHISKERLQQAGDLVTAAVYEAVKKEKKPKTIKKQMKAKASDIFEDIK
|
Catalyzes the hydrolysis of a range of N-terminal amino acids.
|
P25152
|
A1R8T1
|
RL6_PAEAT
|
50S ribosomal protein L6
|
Paenarthrobacter
|
MSRIGRLPITVPAGVEVKLDGSVISVKGAKGELSHTVASPIEVTQEENTLTVTRPNDERNSRSLHGLTRTLIANMIQGVTEGYEKKLEIVGTGYRVQAKGSDLEFALGYSHPVNVSAPEGITFVVEGPTKLSVAGINKQQVGEVAANIRKLRKPDPYKGKGVRYAGEVIRRKVGKAGK
|
This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center.
|
A1R8T1
|
P22358
|
DNAK2_SYNY3
|
Heat shock protein 70-2
|
unclassified Synechocystis
|
MGKVVGIDLGTTNSCVAVMEGGKPTVIANAEGFRTTPSVVGYAKNGDRLVGQIAKRQAVMNPGNTFYSVKRFIGRKFDEITNEATEVAYSVVKDGNGNVKLDCPAQGKQFAPEEISAQVLRKLVDDASKYLGETVTQAVITVPAYFNDSQRQATKDAGKIAGIEVLRIINEPTAASLAYGLDKKDNETILVFDLGGGTFDVSILEVGEGVFEVLATSGDTHLGGDDFDKKIVDFLAGEFQKAEGIDLRKDKQALQRLTEAAEKAKIELSGVSQTEINLPFITATQDGPKHLDTTLSRAKFEEICSDLIDRCGIPVENAIRDAKIDKSALDEIVLVGGSTRIPAVQEVVKKILGKDPNQGVNPDEVVAVGAAIQGGVLSGEVKDILLLDVSPLSLGVETLGGVMTKIIPRNTTIPTKKSETFSTAVDGQSNVEIHVLQGEREMANDNKSLGTFRLDGIPPAPRGVPQIEVTFDIDANGILNVTAKDRGTGKEQSISITGASTLPDTEVDRMVKEAESNAAADKERREKIDRKNQADSLVYQAEKQITELGDKVPAADKIKAEGLIKDLKEAVAQEDDAKIQTVMPELQQVLYSIGSNMYQQAGAEAGVGAPGAGPEAGTSSGGGDDVIDAEFSEPEK
|
Acts as a chaperone.
|
P22358
|
Q8CGP7
|
H2A1K_MOUSE
|
Histone H2A type 1-K
|
Mus
|
MSGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTETHHKAKGK
|
Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
|
Q8CGP7
|
A1KSD4
|
QUEC_NEIMF
|
Queuosine biosynthesis protein QueC
|
Neisseria
|
MSNQKALVIFSGGQDSTTCLIQAIQIYGRENVQAITFQYGQRHAVELERARWIAQDLGVKQTVLDLSLMRQITHNALMDDTAAIETAENGVPNTFVDGRNALFLLYAAIYAKGQGIRHIIAGVCETDFSGYPDCRDVFVKSMNVTLNLAMDYDFQIHTPLMYLTKAQTWALADEMGVLDYIREQTHTCYNGIVGGCRECPSCILRERGLAEYLESKKAV
|
Catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)).
|
A1KSD4
|
Q5M108
|
ATPF_STRT1
|
F-type ATPase subunit b
|
Streptococcus
|
MSLLINSTTLGNIIITLGSVFLLYYLIRKFAWDQITGIFVAREKKIATDIDSAENARQEAEILVQKRQEELAAARTEATQIIDEAKKTGKTKESKIIAEAYDEAKRLKEKANQDIAQSWVEALAGVKGEVADLTVLLAEKVMKQNLDAKAQSDLIDSYLDQLGDA
|
Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
|
Q5M108
|
A5IT22
|
SCPB_STAA9
|
Segregation and condensation protein B
|
Staphylococcus
|
MDNHGILESLLFTAGDEGLDEKQLLEILDMSKDQLVELIENYSSHGLMIQRFGTTYVLTTKKEAATYIEQLIEQKSQMKLSQAAMEVLSIIAYNQPLSRSDIELIRSINSDGAVKTLIAKGLVEAKVVNEQRSQQLITTDLFLNVFGISNIEDLPTTEEDDEEMDAFFSNLVNQKGENND
|
Participates in chromosomal partition during cell division. May act via the formation of a condensin-like complex containing Smc and ScpA that pull DNA away from mid-cell into both cell halves.
|
A5IT22
|
Q6C4D4
|
DBP2_YARLI
|
ATP-dependent RNA helicase DBP2
|
Yarrowia
|
MSYGDDYNNNDRGYGGGRGFGGGRGGRGGSRGGRGGFGGDRGFGGDRGGYGGGGYQDNDFGNLPKQDWDLEKLPQFEKNFYKEDPAVTERTDEEVTAFRKENQMTLHGDGIPKPVTNFDEAGFPPYVLKEVKQQGFEKPTAIQCQGWPMALTGRDVIGIASTGSGKTLSYCLPAIVHINAQPMLSHGDGPIVLVLAPTRELAVQIQQECSKFGKSSKIRNTCVYGGVPRGQQIRDLARGVEIVIATPGRLLDMLESGKTNLRRVTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVQRLAHDYLKDQIQVNIGSLELSASHNITQVVEVCTEYEKRDRLVKHLETVMENKESKCLIFTGTKRVADDITKFLRQDGWPALAIHGDKQQQERDWVLNEFRQGKSPIMVATDVASRGIDVKGINFVINYDYPSNSEDYVHRIGRTGRAGTKGTAYTYFTEDNRKQARDLLVILREAKQHIDPKLEEMGGGRGGRGGWGGRGGRGGRGGRGGYRRGGYGGGGYGGGRGSDITGSNSAPLSNSRW
|
ATP-dependent RNA helicase involved nonsense-mediated mRNA decay and ribosome biogenesis through rRNA processing.
|
Q6C4D4
|
C5P5Q3
|
SUB9_COCP7
|
Subtilisin-like protease CPC735_033790
|
Coccidioides
|
MGFLSSAILLLITAFPAAQAGEMINAAAGATDVIPDSYIVVMNEGISESDFESHRTWATSMNSKSRKRAGAFSGVSRTWSATGMKGYSGSFARETIEQIANNSAVAYVEPDRMVNITAFVTQRNAPSYGLGRISNKRPGNRDYIFDESAGRGITIYGVDTGIDIRHPEFEGRATWGTNEINDVNQDENGHGTHTAGTFAGRNFGVAKRANIVAVKVLNAEGSGSTSGIISGINWCVDHARRNNILGRAVMNLSLGGTGARAFNQVATNAANAGIFLAVAAGNDGEDAANTSPASARGVCTVSASTERDTRADFSNFGSVVDIYAPGDQIPSVFPNNARRVLSGTSMAAPHVAGVGAYLMALEGISSGQVCNRIKRLSQPRIRNPGRDTTNRLLYNNSGV
|
Secreted subtilisin-like serine protease with keratinolytic activity that contributes to pathogenicity.
|
C5P5Q3
|
B0JGG3
|
RNZ_MICAN
|
tRNase Z
|
Microcystis
|
MEITFLGTSSGVPTRSRNVSSIALRLPQRAEIWLFDCGEGTQHQLLRSDLKSSQIRRIFITHMHGDHIFGLMGLLASIGLAGSAQDIDIYGPPGLGDYLRACAKYSYTNLANRVRVHAISPGILYEDEEFTVSCQLLKHRIPAHGYRIAEKDRPGRFDVEKANALGIPPGPIYGKLKKGETVTLPDGSKIRGQSLCGETEIGRKIAYCTDTIFCEGSIELAQNADVLIHEATFAHQDAGLAFESVHSTSTMAAQVALAAQVKLLLMTHFSPRYLPGNSLDISNLLEEARAIFPNTKLAYDFLTYEVPRNRQEMALGVK
|
Zinc phosphodiesterase, which displays some tRNA 3'-processing endonuclease activity. Probably involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA.
|
B0JGG3
|
B8J3A9
|
RS18_DESDA
|
30S ribosomal protein S18
|
Desulfovibrio
|
MAFKKKFAPRRKFCRFCADKDLPLNYKRPDILRDFITERGKIIARRITGTCAHHQRLLTREIKRARQMALLIYTATHDSGVQKKSSI
|
Binds as a heterodimer with protein S6 to the central domain of the 16S rRNA, where it helps stabilize the platform of the 30S subunit.
|
B8J3A9
|
P02067
|
HBB_PIG
|
Hemoglobin beta chain
|
Sus
|
MVHLSAEEKEAVLGLWGKVNVDEVGGEALGRLLVVYPWTQRFFESFGDLSNADAVMGNPKVKAHGKKVLQSFSDGLKHLDNLKGTFAKLSELHCDQLHVDPENFRLLGNVIVVVLARRLGHDFNPNVQAAFQKVVAGVANALAHKYH
|
Involved in oxygen transport from the lung to the various peripheral tissues.
|
P02067
|
Q9HGV0
|
RLA1_ASPFU
|
AfP1
|
Aspergillus subgen. Fumigati
|
MSTAELACSYAALILADDGVEITADKIQTLLGAAKVADVEPIWTSLFAKALEGKDIKDLLTNVGSGGAAAPAAVGGAAAGAAAPAEAAAAEEKKEEEKEESDEDMGFGLFD
|
Plays an important role in the elongation step of protein synthesis.
|
Q9HGV0
|
A7NKL7
|
TRPA_ROSCS
|
Tryptophan synthase alpha chain
|
Roseiflexus
|
MSRIADTFARLRAAGRTALMPYLMTGYPERDSVLDLAPALEDAGADLFELGVPFSDPLADGATIQRASERALANGVRLEHCIATIAVLRERGVRAPIVPMGYYNPFLQYGLARLARDMAAAGADGLIIPDLPPEEAQECHAACREYGLDLIFFVAPTTPDERIARITALASGFIYCVSLTGVTGARRELWSGLPAFLERVRRHTTLPLVVGFGISSADHVREVGRHAAGAIVASALINVIEQSHPGEYVARAAEFVRLLRG
|
The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
|
A7NKL7
|
A4G075
|
ARGC_METM5
|
N-acetyl-glutamate semialdehyde dehydrogenase
|
Methanococcus
|
MKTVSIIGGTGYTGSELLRLLSNHDKVEVLNVTSRKEAGKKLTDFHPQVRNLRNYNDLEFQNIAPEDIDTDIVFCATPHGASMAIVPTLHEKGINIIDLSGDYRFEDIEMYESWYGLKHTGKIESAVYGLPELHREKIKKSKTIANPGCYPTGAILSMAPLVANDLVDERIIFDSKSGVSGAGVVASQTTHFPNVNENLGAYKITKHRHSPEIGKELEYLGNKRLKVSFTPHLLPVTRGILTTAHSYLKEDVSRVDVIEIYEEFYKDEFFVRIFEESMPSLTGVRGTNFCDIGGFEIDQHGRIVVVSAIDNLVKGASGQAIQNMNIIMGFDEKEGLSVGGMRP
|
Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.
|
A4G075
|
Q04G22
|
ATPA_OENOB
|
F-ATPase subunit alpha
|
Oenococcus
|
MAIKSDQISSLIKQQLEKYDSTLKIDEVGTVTYVGDGVARASGLANVMSGELVEFENGVYGMAQNLEESEVGIIVLGDFDGISQGDTVKRTGKVMEVPVGDEMIGRVVNALGQPIDGNGAIKTKHTRPVEFKAPGVMQRKSVFEPLQTGIKVIDALVPIGRGQRELIIGDRKTGKTSLAIDTILNQKDQDMIVVYVAIGQKDSTVRTQVETLREMGALDYTIVVSAAPSEPAPMLYLAPYVGAALGEYFMYNGKHVLIVYDDLSKQATAYRELSLILRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSMTALPIIETQAGDVSAYIPTNVISITDGQIFLDADQFYSGNRPAIDAGTSVSRVGGDAQIKAMKKVSGTLRLDLASYHELEAFAQFGSDLDAPTQAKLARGRRTVEVLNQPLHQPMPVEHQVIVLYALTHGYLDDIDVSDIQRFQKELIDFVSGDKSYKKIFAAIKKTGNLPDEKDINSAIDDFKKHFSKSVEPTDYVAPSTKQEANK
|
Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
|
Q04G22
|
A5D2K2
|
MUTS_PELTS
|
DNA mismatch repair protein MutS
|
Pelotomaculum
|
MIRQYLEIKKQYPDAILFFRLGDFYEMFFDDARLASRELEITLTGRDGGSERVPMCGIPYHAADGYIARLISKGYRVAICEQVEDPAEAKGIVRREVTRVITPGTVTEGHFLEDKKNNYLASIAPFEEGYGLAVTDITTGVFMVSSFSGVRAWSELIDEMARLNPAEVIIPLAYSDKMGGDLKQQGILAVSGYRDTAFSPAEAVPAFEEQFGSAGSLCNRTIDYHAAVAAAGALLIFLRETQKRVLKHINKAAFYRPGKYMILDANTRRNLELTRAISDGSRRNTLLSVIDHTVTAMGGRLLRNWIEQPLLDVAEIKARLEATEDLAGNAMLRLELKSLLKNVYDLERLTGKISFGTANARDLIGLKKSLANLPLIKQLLLAQAGAALLKDVARSIDPLEEVRELLEAAIDDNPPLSLKDGGIIKKGYNHEVDRLRQARREGKSMLAGLEERERARTGIKSLKVGFNKVFGYYIEVTRANLELVPEDYQRRQTLANAERFITPELKEYEDMILRAEERLASLERRLFDEVLERLSGEIHRIQKSASAIATADALYSLAEAAVKGRYSRPEIAEDGKLHVKDGRHPVLEQVMGPGRFVPNDTFMDNEESRFILLTGPNMAGKSTYMRQVALIVLLAQIGSFVPALFARIPVFDRIFTRVGASDDIAGGQSTFMVEMNECRIIVNEATEKSLIIMDEVGRGTSTYDGISIARALAEYIHTKIRAKTLFSTHYHELTDLDSMPGIVNFNVAVREEGEDIIFLRKVVPGKSDRSYGIQVARLAGLPGEIINRSMEILKTLELAAERPPQPSPAKEWPAYRYKENECHVIQELRRLNVLEMTPLEAINKLYMLHKKLTESATLKTTSL
|
This protein is involved in the repair of mismatches in DNA. It is possible that it carries out the mismatch recognition step. This protein has a weak ATPase activity.
|
A5D2K2
|
P47939
|
RES18_MOUSE
|
Regulated endocrine-specific protein 18
|
Mus
|
MQSSLKPAGSGHLQLLVCFLLLYSRPGSCSDINAHDGQGQVGSEQLWTFQGLIASVFQYLQLIFHQIVPEGMFWADDIAYELMTKKVEHLSRLHPQYPCRKDMKAVSPTANAGVRSKQEEKLQLLSPQKSPTVKVNRDRCFTTKVIPKATKQEATHPTKGFFGPFPTVGLNLVAD
|
May play an important regulatory role in corticotrophs.
|
P47939
|
Subsets and Splits
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