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Full Name
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sequence
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2.75k
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5.51k
AlphaFoldDB
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10
C1CXG0
RS3_DEIDV
30S ribosomal protein S3
Deinococcus
MGNKINPNGFRLGITRGWNSRWYAGKKQYAGLLKEDEKIRKLVDKKLSAAGIARVEIERAGQQVNVIISAAKPGIVIGKGGDSIKQLRADIEKLVSAGTVAVNVAEIPNPNISAPLVALRIAEQIERRFAFRRAMKQAAQRVMESGARGVKVVLSGRLGGAEQARRETVREGRVPLHTLRADIDYGTALARTTYGILGIKVMVFTGEVIGGRTETIARPQRRNDERRPEGGDRANRRRPTARRRAGGE
Binds the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation.
C1CXG0
Q9BBR0
RK20_LOTJA
50S ribosomal protein L20, chloroplastic
Lotus
MTRIKRGYIARKRRTKIRLFTSSFRGAHSRLTRTISQQKIKALVSAHRDRNRKKREFRGLWISRINAGIGDNDKKKNIYYSYSNFMYNLYKKQLLLNRKIVAQIAIFKGNCLFMIANEIIT
Binds directly to 23S ribosomal RNA and is necessary for the in vitro assembly process of the 50S ribosomal subunit. It is not involved in the protein synthesizing functions of that subunit.
Q9BBR0
A1VDN0
UVRB_DESVV
Excinuclease ABC subunit B
Desulfovibrio
MADTCFRLHTEFEPTGDQPEAIGQIVANLGQGVRDQVLLGVTGSGKTFTVANVIAACNRPALILAPNKTLAAQLYNEFRALFPDNAVEYFVSYYDYYQPEAYVPASDTYIEKDSSINDNIDKLRHAATHALLTRRDVVIVASVSCIYGLGSPEYYARLVIPVECGQRFSMDALMTRLVEVQYQRNDFDFHRGTFRVRGDVLEVIPAYHHERALRIEFFGDDIDAISEIDPLTGEVLGSVGKTVIYPASHYVSDRDNLVRAMSDIRDELGERLREYQSANRLVEAQRLEQRTMLDLEMMEELGYCNGIENYSRHLDGRAAGQPPSCLLDYFPDDFLLFVDESHITVPQVGAMYKGDRSRKSTLVDFGFRLPSALDNRPLEFAEFLTRINQTVYVSATPGKWELDRSQGVIAEQIIRPTGLVDPVVEVRPTRGQVDDLLAECRARAARDERVLITTLTKRMAEDLTEHLGNMGLSVRYLHSDIDTMERMAIIQALRRGECDVLVGINLLREGLDIPEVSLVSILDADKEGFLRSTGSLIQTFGRAARNAAGRVILYADTVTASMRAAMDETARRRERQQAWNEANGIEPRTIRKSLDTPFDAIYSAASEGGKGRGRGRGRQAAPAVENVAEYGTSPEDMAKHIQKLEREMREAAKELEFERAATLRDRIRLLRERLIEA
The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and the UvrB-DNA preincision complex is formed. This complex is subsequently bound by UvrC and the second UvrB is released. If no lesion is found, the DNA wraps around the other UvrB subunit that will check the other stand for damage.
A1VDN0
A4G8P4
PRMA_HERAR
Ribosomal protein L11 methyltransferase
Herminiimonas
MSWTEIVIEVARTHAEALSDALFDAGALSVSVEDADFGTDAEQPLFGEPGMEPTEAAWERSRVVALTPVEADQAAIVAEAAESIGLAAADLAFTLRNVDDQDWVRLTQSQFEPIHIGKNIWVVPSWHDVPDPAALVLELDPGLAFGTGSHPTTRLCMEWLEAHAPIGLSVLDYGCGSGILAMIAKKLDADTVVGIDIDPQAIQSAVFNTERNHCDVAYYLPDEFAASGHAHTFDVVVANILANPLKLMAPMLAGRVNPGGQLVLSGVLATQVDEVTAAYAPFIALTVWAEQEGWVALAGRSPVTVPDGQ
Methylates ribosomal protein L11.
A4G8P4
B5FIF0
RSXE_SALDC
Rsx electron transport complex subunit E
Salmonella
MSEIKDIVVQGLWKNNSALVQLLGLCPLLAVTSTATNALGLGLATTLVLTLTNLTVSALRRWTPAEIRIPIYVMIIASVVSAVQMLINAYAFGLYQSLGIFIPLIVTNCIVVGRAEAFAAKKGPWLSALDGFSIGMGATGAMFVLGSLREILGNGTLFDGADSLLGGWAKVLRVEIFHTDSPFLLARLPPGAFIGLGLMLAVKYLIDEKMKKRRAETAPSAVPAGETGKV
Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane. Required to maintain the reduced state of SoxR.
B5FIF0
B2TCJ9
BETB_PARPJ
Betaine aldehyde dehydrogenase
Paraburkholderia
MAVFATQRLYIGGGYVDATSGETFDTLDPATGETLASVQQASAADVDRAVRSAKQGQREWAALTAMQRSRILRRAVDLLRERNDELAALETRDTGKPIAETLAVDIVTGADVIEYYAGLATAIEGQQIPLRPTSFVYTRREPLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFKPSEITPLSALKLAEIFTEAGVPAGVFNVVQGDGRVGAMLAAHPDIEKISFTGGVETGKKVMSMAGASSLKEVTMELGGKSPLLVFDDANLERAADIATSANFFSSGQVCTNGTRVFVQRGVLDRFEALVLERVKRIRVGKPTDAATNFGPLVSAAQLHKVLGYIESGKQEGARLVAGGKRLTEGHFAGGQYVEPTVFADCRDDMRIVREEIFGPVMSILVFDDEDEAIARANHTAYGLAAGVVTENLARAHRVIHRLEAGICWINTWGESPAEMPVGGYKQSGVGRENGITTLEHYTRIKSVQVELGPYQPVF
Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the irreversible oxidation of betaine aldehyde to the corresponding acid.
B2TCJ9
Q2G6G9
RL25_NOVAD
General stress protein CTC
Novosphingobium
MSETLHLSAETRDRAGKGASRALRREGRTPAVIYGGNEEPVAIHLEEKALVKALGTGHFFNSVVELTVGGQTVRTLPKDVAFHPVTDRPEHADFLRVSKDSVVHVNVPVIFANEEKSPGLKKGGVLNIVRHELELVCAPDAIPDDIVIDVAGYEVGDSIHISAVKLPAGVKSAITDRDFTIATIVAPSSLKSEEGDTTKTDAEG
This is one of the proteins that binds to the 5S RNA in the ribosome where it forms part of the central protuberance.
Q2G6G9
Q4K843
SYA_PSEF5
Alanyl-tRNA synthetase
Pseudomonas
MKSAEIREAFLRFFEEQGHTRVASSSLIPGNDPTLLFTNAGMNQFKDCFLGQEKRAYTRAVSSQKCVRAGGKHNDLENVGYTARHHTFFEMLGNFSFGDYFKRDAITFAWTFLTSDKWLNLPKEKLWVTVYATDDEAYDIWTKEVGVPAERMVRIGDNKGAPYASDNFWTMGDTGPCGPCTEIFYDHGADIWGGPPGSPEEDGDRYIEIWNNVFMQFNRTADGVLHPLPAPSVDTGMGLERISAVLQHVHSNYEIDLFQSLLDAAAKAIGCTNDAQASLKVVADHIRSCGFLIADGVLPSNEGRGYVLRRIIRRACRHGNKLGAKGSFFYQIVAALVAEMGEAFPELKSQQAHIERVLKAEEEQFAKTLEQGLKILEQDLAELKGSVVPGDVVFKLYDTYGFPMDLTGDIARERNLTLDEEGFEREMEAQRVRARSASSFGMDYNSLVKVDVATEFTGYHATSGSAKVVALYKEGQSVDMLSEGEEGVVVLDQTPFYAESGGQIGDCGYLQAGNARFDVRDTTKTGGAFLHHGVLAKGSLTVGAPVETQVDAQVRHATSLNHSATHLLHAALRQVLGEHVQQKGSLVDSQRLRFDFSHFEAIKPEQIKALEDIVNAEIRKNTPVETEETDIDTAKKKGAMALFGEKYGDSVRVLSMGGDFSVELCGGIHANRTGDIGLLKITSEGGVASGVRRIEAVTGAAALAYLNAAEEQLKEAATLVKGSRDNLIDKLSAVLERNRLLEKQLEQLQAKAASAAGDDLSAQAADVKGVKVLAARLDGQDGKALLALVDQLKNKLGRAVILLGSVHEEKVVLVAGVTKDLTGQLKAGDLMKQAAAAVGGKGGGRPDMAQGGGVDAAALDAALALTVPFVEQGI
Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
Q4K843
O87627
NIFN_HERSE
Nitrogenase iron-molybdenum cofactor biosynthesis protein NifN
Herbaspirillum
MPSASLLKAAAVNALKMSQVGRGLCLPGMNRYMPVMHGAQGCTSFGLVLLVRDFREAIPLQTTAMNEVSSTLGGMENIAKAVLNIRLRAKRDLIAICSTGLTETKGDDVNAYLRLTAEAPRPGRYLTGLCPHALTTGASQDGWAKALEALAGRWESRGRADARQADNLLAGCHLTPADIEEMRDIVQSFGLEPIVLPDVSSWLDGHLPDNFSPTSMGGTTLAEMRALGASIVCIANRRTEAPPTAQAVQELCGVPYVVFDRLTGLQANDRFLAYLEYVSGQPIPARYRRQRSQLQDAMLGWPLLLRPGVKVAIGAEPEPVAVTLRHGWPRWAAELGGCRDHHDLAGARWRSPQPGWWIGANLEAPGTKGARARACAGSCWLTHSHGGQAAERLHIPFHRAGLPPCSTGLGAGHCLSVGYRGTRGLIFEIGQPVAGRGPCTYPG
This protein may play a role in the biosynthesis of the prosthetic group of nitrogenase (FeMo cofactor).
O87627
Q7MT55
FIMB_PORGI
Major fimbrium anchoring subunit FimB
Porphyromonas
MNDAKKYIVSVLILLVAGMFGGCIKEDYSDCPRPFRLTVRAWDADMQDITETGAVQRVVIFVFDETGRRIDRLMMDAAQVAARKPIPLEYDGPTTVSFVAWANPDDHMLEETANVQNVKDLFFRLSSTDGIAQSPGDLFSGVLTCPIEYGSIEQGTDQTVDIYRRTAQVHIIIRGYQEWLEANGPRQLPDYADILLGETPDTYTGLAELIGNAVQYRPDGQIQNGDFISPIFRVYPTLDTTPLHLKLYAYGQELLNISTGSDGVPFIPVIGKMLNIYIDLRGANLNVLVSVTPWDVVQQYAEY
Anchoring subunit of the major fimbriae. Regulates fimbrial length. These filamentous pili are attached to the cell surface; they mediate biofilm formation, adhesion onto host cells and onto other bacteria that are part of the oral microbiome. Fimbriae of P.gingivalis are major virulence factors.
Q7MT55
Q4K6I5
RSMH_PSEF5
rRNA (cytosine-N(4)-)-methyltransferase RsmH
Pseudomonas
MTIDSGFNHITVLLDEAVEALAVRPDGCYLDGTFGRGGHSRLILSKLGPQGRLLGFDKDPQAIATGQALAAEDGRFVVVQRSFAELGSEVAERGLAGKVSGVLLDLGVSSPQLDDPERGFSFLNDGPLDMRMDPTRGISAAQFIATAPVEEIARVFKEYGEERFSGRMARAVVERREIQPFERTADLAEVLKVANPAWEKGKNPATRAFQGLRIHVNNELGDLEAGLEAALESLEVGGRLVVISFHSLEDRIVKLFMRRLVKGESDNLPRNLPVRFEAFVPKIKIHGKAQFASEAELKANPRARSAVMRVAEKLR
Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
Q4K6I5
Q4ULQ8
SUCD_RICFE
Succinyl-CoA synthetase subunit alpha
spotted fever group
MAILINKKTKVICQGFTGSQGTFHSEQAIAYGTNMVGGVTPGKGGHTHLDLPVYNTVHEAKAKTGANASVIYVPPGFAADSILEAIDAEIEVVVCITEGIPVLDMVKVKRALVGSKTRLIGPNCPGVITPGECKIGIMPGHIHKRGTIGIVSRSGTLTYEAVAQTTAVGLGQSTCVGIGGDPVNGTNFVDCIDMFLKDDETKAIIMIGEIGGNAEEDAAEFIKQSKIKKPIVSFIAGITAPPGKRMGHAGAIIAGGKGSAEDKLEALQSAGVTITRSPADIGKTMFDLLNKG
Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and nucleotide specificity is provided by the beta subunit.
Q4ULQ8
Q8ETB7
RSGA1_OCEIH
Small ribosomal subunit biogenesis GTPase RsgA 1
Oceanobacillus
MNLNEFQQKYAYRKEINYDGQIDLLARVVMEQKERYILQTINGFKPAVVKGKMRHEAISREDYPAVGDWVVLQEKDFNDIVIIDQVLPRFSSIVRKVAGLRTDAQIVASNVTKVFIVISADEDLNERKLERYLTAVWESGASPHIVFSKVDLASDMDSIIEHADSIAFGIPLYKWNATNEEGKEDILANIHEDDSVVLIGSSGAGKSTLINALLTEKVLKTGSVREDDKRGRHTTTHRELFNLPTGGVIIDTPGMRELQLWTEDGDTLSHTFSDINHLIAECKFTDCKHDTEPDCAVKEALETGDLEEGRWNSYLKLQRELAYIERKQNAKLATEERKKWKKISMQQKKNR
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.
Q8ETB7
I6XHJ3
FADA6_MYCTU
Acetyl-CoA acetyltransferase FadA6
Mycobacterium tuberculosis complex
MPRVDDDAVGVPLTGNGRGAVMTEAYVIDAVRTAVGKRGGALAGIHPVDLGALAWRGLLDRTDIDPAAVDDVIAGCVDAIGGQAGNIARLSWLAAGYPEEVPGVTVDRQCGSSQQAISFGAQAIMSGTADVIVAGGVQNMSQIPISSAMTVGEQFGFTSPTNESKQWLHRYGDQEISQFRGSELIAEKWNLSREEMERYSLTSHERAFAAIRAGHFENEIITVETESGPFRVDEGPRESSLEKMAGLQPLVEGGRLTAAMASQISDGASAVLLASERAVKDHGLRPRARIHHISARAADPVFMLTGPIPATRYALDKTGLAIDDIDTVEINEAFAPVVMAWLKEIKADPAKVNPNGGAIALGHPLGATGAKLFTTMLGELERIGGRYGLQTMCEGGGTANVTIIERL
May be involved in the final steps of cholesterol and steroid degradation . Catalyzes the formation of 4-methyl-5-oxo-octanedioyl-CoA (MOODA-CoA) and acetyl-CoA from 6-methyl-3,7-dioxodecanedioyl-CoA (MeDODA-CoA) and coenzyme A (Probable).
I6XHJ3
A4QJB4
PSAB_AETCO
PsaB
Aethionema
MALRFPRFSQGLAQDPTTRRIWFGIATAHDFESHDDITEERLYQNIFASHFGQLAIIFLWTSGNLFHVAWQGNFETWVQDPLHVRPIAHAIWDPHFGQPAVEAFTRGGALGPVNIAYSGVYQWWYTIGLRTNEDLYTGALFLLFLSAISLIGGWLHLQPKWKPRVSWFKNAESRLNHHLSGLFGVSSLAWTGHLVHVAIPASRGEYVRWNNLLNVLPHPQGLGPLFTGQWNLYAQNPDSSSHLFGTSQGSGTAILTLLGGFHPQTQSLWLTDIAHHHLAIAILFLIAGHMYRTNFGIGHSIKDLLEAHIPPGGRLGRGHKGLYDTINNSIHFQLGLALASLGVITSLVAQHMYSLPAYAFIAQDFTTQAALYTHHQYIAGFIMTGAFAHGAIFFIRDYNPEQNEDNVLARMLDHKEAIISHLSWASLFLGFHTLGLYVHNDVMLAFGTPEKQILIEPIFAQWIQSAHGKTSYGFDVLLSSTNGPAFNAGRSIWLPGWLNAINENSNSLFLTIGPGDFLVHHAIALGLHTTTLILVKGALDARGSKLMPDKKDFGYSFPCDGPGRGGTCDISAWDAFYLAVFWMLNTIGWVTFYWHWKHITLWQGNVSQFNESSTYLMGWLRDYLWLNSSQLINGYNPFGMNSLSVWAWMFLFGHLVWATGFMFLISWRGYWQELIETLAWAHERTPLANLIRWKDKPVALSIVQARLVGLAHFSVGYIFTYAAFLIASTSGKFG
PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. Oxidized P700 is reduced on the lumenal side of the thylakoid membrane by plastocyanin.
A4QJB4
A2BZT9
RBFA_PROM1
Ribosome-binding factor A
Prochlorococcus
MANSRRVEKLAALLKREISELLVNGIRDERIHQAMITITSVEVSGDLQHARIFISLFGEEKKKDQVLVGLEEAKGFIRAELARRLQMRRSPELVFKIDKGMTKGPEVLDLLNALELERKSKDL
One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Associates with free 30S ribosomal subunits (but not with 30S subunits that are part of 70S ribosomes or polysomes). Required for efficient processing of 16S rRNA. May interact with the 5'-terminal helix region of 16S rRNA.
A2BZT9
P11454
ENTF_ECOLI
Seryl-AMP ligase
Escherichia
MSQHLPLVAAQPGIWMAEKLSELPSAWSVAHYVELTGEVDSPLLARAVVAGLAQADTLRMRFTEDNGEVWQWVDDALTFELPEIIDLRTNIDPHGTAQALMQADLQQDLRVDSGKPLVFHQLIQVADNRWYWYQRYHHLLVDGFSFPAITRQIANIYCTWLRGEPTPASPFTPFADVVEEYQQYRESEAWQRDAAFWAEQRRQLPPPASLSPAPLPGRSASADILRLKLEFTDGEFRQLATQLSGVQRTDLALALAALWLGRLCNRMDYAAGFIFMRRLGSAALTATGPVLNVLPLGIHIAAQETLPELATRLAAQLKKMRRHQRYDAEQIVRDSGRAAGDEPLFGPVLNIKVFDYQLDIPDVQAQTHTLATGPVNDLELALFPDVHGDLSIEILANKQRYDEPTLIQHAERLKMLIAQFAADPALLCGDVDIMLPGEYAQLAQLNATQVEIPETTLSALVAEQAAKTPDAPALADARYLFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTDDQLPRFSDVPNLTSLCYNAPLTPQGSAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTGEDVVAQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTHFVPSMLAAFVASLTPQTARQSCATLKQVFCSGEALPADLCREWQQLTGAPLHNLYGPTEAAVDVSWYPAFGEELAQVRGSSVPIGYPVWNTGLRILDAMMHPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLDNGAVEYLGRSDDQLKIRGQRIELGEIDRVMQALPDVEQAVTHACVINQAAATGGDARQLVGYLVSQSGLPLDTSALQAQLRETLPPHMVPVVLLQLPQLPLSANGKLDRKALPLPELKAQAPGRAPKAGSETIIAAAFSSLLGCDVQDADADFFALGGHSLLAMKLAAQLSRQVARQVTPGQVMVASTVAKLATIIDAEEDSTRRMGFETILPLREGNGPTLFCFHPASGFAWQFSVLSRYLDPQWSIIGIQSPRPNGPMQTAANLDEVCEAHLATLLEQQPHGPYYLLGYSLGGTLAQGIAARLRARGEQVAFLGLLDTWPPETQNWQEKEANGLDPEVLAEINREREAFLAAQQGSTSTELFTTIEGNYADAVRLLTTAHSVPFDGKATLFVAERTLQEGMSPERAWSPWIAELDIYRQDCAHVDIISPGTFEKIGPIIRATLNR
Involved in the biosynthesis of the siderophore enterobactin (enterochelin), which is a macrocyclic trimeric lactone of N-(2,3-dihydroxybenzoyl)-serine . EntF catalyzes the activation of L-serine via ATP-dependent PPi exchange reaction to form seryladenylate . Activated L-serine is loaded onto the peptidyl carrier domain via a thioester linkage to the phosphopanthetheine moiety, forming seryl-S-Ppant-EntF . EntF acts then as the sole catalyst for the formation of the three amide and three ester linkages found in enterobactin, using seryladenylate and 2,3-dihydroxybenzoate-S-Ppant-EntB (DHB-S-Ppant-EntB) as substrates, via the formation of a DHB-Ser-S-Ppant-EntF intermediate .
P11454
Q8YQ91
CBIM_NOSS1
Energy-coupling factor transporter probable substrate-capture protein CbiM
Nostoc
MLRRVLASKRASLILMGMLSFYIIVSASAPAYAMHIMEGYLPAGWAAFWWLVALPFMLLGVRSLTRITKANPELKLLLALAGAFTFVLSALKLPSVTGSCSHPTGTGLGSVLFGPLAMSVLGSLVLLFQALLLAHGGLTTLGANAFSMAIAGPFAAYWIYHLTIKLTGKQRIAIFLAATLADLLTYIITSVQLALAFPAPVGGFIASFAKFAGIFAITQIPLAISEGLLTVLVWNWLQSYSPQELQLLKLIQGESQSHESI
Part of the energy-coupling factor (ECF) transporter complex CbiMNOQ involved in cobalt import.
Q8YQ91
O59824
YME1_SCHPO
ATP-dependent zinc metalloprotease YME1 homolog
Schizosaccharomyces
MSRVLHPIFLFGKTSFLYSGCSKFGGRLFNNSIVHGWLRTRSYALASGLHPLRKQKLAHFEDLANANMSDPYMQAKLYKELADNFPEAIISRYETQGVARNSACDRYYQEALRKKSWSRSLSNNISLSQSSSSPATSSFSDPKAFSAGVPKFTSDTSSTVSSTPSLNHSLQNSMPPSTPTPPPVWAPTIVSSALGTSSKTPVYVVVDEPRFTKFFRIFKFIAGLSVASYFVLLGMSIFAETSGLNNIMTNTTEQEPMEERAINVRFSDVQGVDEAKEELEEIVDFLRDPTHFTRLGGKLPRGVLLTGPPGTGKTMLARAVAGEANVPFFFMSGSQFDEMYVGVGAKRVRELFAAARKQAPSIIFIDELDAIGQKRNARDAAHMRQTLNQLLVDLDGFSKNEDLAHPVVFIGATNFPESLDPALTRPGRFDRHIHVPLPDVRGRLAILLQHTRHVPLGKDVDLSIIARGTSGFAGADLANLINQAAVYASKNLSTAVSMRDLEWSKDRILMGAERKSAFITPENKLMTAYHEGGHALVALFTKNAMRPYKATIMPRGSSLGMTISLPDMDKDSWTREEYLAMLDVTMGGRAAEELLYGKDKITSGAHNDIDKATQVARRMVTEFGMSDRIGPVSLEAEMDNLSPATRALVESEIKSLLEASYERSLSLLKSHKKELDALATALVDYEFLTAEEMNRVVKGDRDLLRNKLS
Putative ATP-dependent protease.
O59824
Q8P1T8
Y713_STRP8
Nucleotide-binding protein spyM18_0713
Streptococcus
MSDKHINLVIVTGMSGAGKTVAIQSFEDLGYFTIDNMPPALVPKFLELIEQTNENRRVALVVDMRSRLFFKEINSTLDSIESNPSIDFWILFLDATDGELVSRYKETRRSHPLAADGRVLDGIRLERELLSPLKSMSQHVVDTTKLTPRQLRKTISDQFSEGSNQASFRIEVMSFGFKYGLPLDADLVFDVRFLPNPYYQVELREKTGLDEDVFNYVMSHPESEVFYKHLLNLIVPILPAYQKEGKSVLTVAIGCTGGQHRSVAFAHCLAESLATDWSVNESHRDQNRRKETVNRS
Displays ATPase and GTPase activities.
Q8P1T8
Q82ZB4
MSCL_ENTFA
Large-conductance mechanosensitive channel
Enterococcus
MIKEFKEFIMRGSVLDLAVGVVIGSAFTAIVTQVVEGLITPLISLIFVLTTGKKSADDALGALVYKVEGVEFNIGSVISALITFLITAFVLFLIVKAANKMKNRGKKEEAAEEEVVPTSEDYLKEIRDLLAAQTPPAETVKTDSTFTEK
Channel that opens in response to stretch forces in the membrane lipid bilayer. May participate in the regulation of osmotic pressure changes within the cell.
Q82ZB4
B0Z4R9
YCF2_OENAR
Protein Ycf2
Oenothera
MGNQRNRVNLNPFRFWVFELREILREIKNYRYRYLGPFNSVGSFIHIFVHQERFLKLLDPRIWSVLRSQGSTGVVLFLVAVLIYRINNRNMIERKNIYLTGLLPIPTNFAGPRNETLEESFLSSNINRLIVSLLHLPKVKRLSESCFLDPKESTRVLPITKWRNWIGKRRDSSQLKGSSDQSRDHFDSIGTEDSEYHTLINQREIQQRKERSSLLDPSFLQTERTEIESDRFSKGLSGSSSKSRLFTEGEKEMNNHLPPEEIEEFLGNPTRSILSFFSDEWSELHLGSNPTERSTVDQKLLKKEQEVSFAPFRRSETKEIVNLFKTMAYLQKTVSIHPISSDPGCDMVPKDELDSEERFQEMADLFTLSITEPDLVYHKGFAFSIDSSVLDQKQFLAEARDESKKKSLLVLPPVFYQENESFYRRIRKRGVQISCGNDLEDPKPKIVVFASNNIVEAVNQYRWIRNLIQIQYSTHGYIRNVLNRFFLMNRSDRNFEYGIQRDQIGNDTLNHRTFMKYTINQHLSNLKKSQKKGSDPLILISRTERSVNRDPNAYRYKWSKGSKNFQEHLEHFVSEQKSRFQVVFDRYRSIRNRYRSRINQYSSDRSEVSDKKDNRYRSRINQYSSDRSEVSDKKNLAKFRSFVFSKLLLFLSNSLPFFFVSFGNTPPIQRSEIRVSELKGPNDRLCNQFLESIGLQLVYLKKLKPFLLDDHETSQKSKLLFNKKPEGMIDSFHTRNNRGKSLDSYFSMISHDQDNWLNPVKPFHRSSLISSFYKANRLRFLNNPHDFGFFCNKRFPFYVDIKNLDFTYGQFLNILFIRNTKFSLCGDKKKHAFLERDTISSIESQVSNLFKDFPQSGDERYNFYKYFHLAMRSDPLVRRAIYSIADISGTPLTEGQRVNFERTYCQPLSDMNLSDSEGKNLYQYLNFNSNMGLIYSEKCFSSEKRKKKKPEKRKKKKPEKRKEKKPEKRKEKKPEKRKEKKPEKRKEKKPEKRKEKKQSLYLKQWVEKVQMDRALQGERVSLILSNWNLFKTYVMPFSLTSTGYNLLKLMFLDTLGSYVMPLLRSSPKFVSICYAISDPCGISWRILQKKLCLLQWNWISAISNKCFHKLLLSEESIHRNNESPSMTDLRWPNLGEFLYSILFLLFVAGHLVFSHLLFFSQAFSELQRDFARAQSLMIPSYIVELRELLDMYPAPRSFKKLFLAAREKLVNYLRWGGERKSFLIHLFELLNITPNPIDRIAFLKNTRHLSHTSKELYSLITELGDFSSLCSGQRYRYDQIIENVNGPCCLIDDKIESWISNCDAIEDKEREFLVPFCNFTRETRIDQILLSLTHSDHLSNNDSASQMSEEPGAFYLRHLVDIHKKGLMNYECNTSCLAERRIFLAHYQTITYSPCGDNRSHFPSHGKTFSLRLPLHPSRATLVIGSIGSGRSYLVKSLATNSYVPLITVVLNKFLKNWTPQGFDIHESGVYDEYGDDAEEANDYGASFFDFLDNDSDDYEDRDSDDYEPGASDDYEPGDMEDFVDSEMTEWLTKTNVPLVYQLLDDEIDEFYITLQFELAKAMSPCILWIPNIHDLDAKESDYLSLGLLVNHLSRDCGRRSTKNEILVIASTHIPQKVDPSLIGPDGLSTCIKTRRLLVPQQQQCLFTLSYTRGFHLENKMFHTHTNEFESTILGPSVPDLVALTNEALSISITQKKSIIDTTTIRYALHRKTWDLEADRNLSPAKEHGTLFYQVGRAFAHTVLLRNCPIDPISIYIKKNLCEAGDSSLYKWYFELGTSMKKLTILLYLLTCSAGSIAQDLLSPPGPDEQNLITSYGLVENDSDLVHGLSDIVHGLLELEGALVGSSPTEEEVEGTEEEVEGTEDEEVEGTEEEVEGTEDEEGEGTEEEVEGTEDEEGEGTEEEVEGTEEEVEGTEDEEGEGTEDEEVEGTEEEVEGTEDEEGEGTEEEVEGTEEEVEGTEEEVEGTEEEVEGTEDEEVEGTEEEVEGTEDEEGEGTEYEEVEGTEDEEVEGTEKDSSQFDNDRVTLLLRPKPRNPLDIQRLIYQHQKYESELEEDDDDDEDVFAPQKMLEDLFSELVWSPRIWHPWDFILDCEAEIPAEEIPEEEDPLPEEALETEVAVWGEEEEGEADDEEDERLEAQQEDELLEEEDEELKEEEDELHEEEEEEEEEEEEEDELHEEEEEEEEEEEDELQENDSEFFRSETQQPQARDGFSEEEGCFRISQFMWVPGDPLSFLYKDTPFVEVLSYPEEATEISKELLRLLNPKTKRDAPKRARQRWWTKKKQDKHYELVLDRQRWLITKSSLSKSNGFFRSNTPSESYQYLSNLFLSNRRLLDQMTKTFFRKKWLFPDEMKIGFMEQ
Probable ATPase of unknown function. Its presence in a non-photosynthetic plant (Epifagus virginiana) and experiments in tobacco indicate that it has an essential function which is probably not related to photosynthesis.
B0Z4R9
Q5WHR5
RUVB_ALKCK
Holliday junction ATP-dependent DNA helicase RuvB
Alkalihalobacillus
MEERIVSAEATELEEQSEQGLRPKRLADYIGQETVKHNLAVFMEAAKMREEALDHVLLYGPPGLGKTTLAAIIAAEMGGELRTTSGPAIERSGDLAAILTALEPGDVLFIDEIHRLNRTVEEVLYPAMEDFCLDIVIGKGPTARSVRLDLPPFTLVGATTRAGMLSSPLRDRFGVMARLEYYKPEELAQIVERSATVFQATLEPSAALELARRSRGTPRIANRLLRRVRDFAQVGGEAAISLERACSALEQLHVDPLGLDHIDDKLLKGMIEKFNGGPVGLETIAATIGEEAATIEEVYEPYLLQIGFIQRTPRGRIATPACYAHYGVEKQNG
The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing.
Q5WHR5
Q5WIL7
PHNC_ALKCK
Phosphonates import ATP-binding protein PhnC
Alkalihalobacillus
MIEIKNVSKTYPNGTKGLKNIDLTIERGEFVVVVGLSGAGKSTLLRSINRLNEITDGEILIDGLSITKAKGKELRQIRQRTAMIFQSFNLVKRSSVLRNVLSGRVGYHGTLRTVLNLFPKQDVELALQALNRVNILEKAYSRASDLSGGQQQRVAIARALAQEPSVILADEPTASLDPLTTKQVMDDLKRINKEDKITTIVNLHFIDLAREYATRIIGLRAGEVVFDGPVSEATDEKFAEIYGRPIQEDELLGEELDEPASEHASQ
Part of the ABC transporter complex PhnCDE involved in phosphonates import. Responsible for energy coupling to the transport system.
Q5WIL7
Q64VQ9
CYSN_BACFR
Sulfate adenylate transferase
Bacteroides
MADKLDIKAFLDKDEQKDLLRLLTAGSVDDGKSTLIGRLLFDSKKLYEDQLDALERDSKRLGNAGEHIDYALLLDGLKAEREQGITIDVAYRYFSTNNRKFIIADTPGHEQYTRNMITGGSTANLAIILVDARMGVITQTRRHTFLVSLLGIKHVVLAVNKMDLVDFSEERFNEIVAEYKKFVAPLGIPDVTCIPLSALDGDNVVDKSERTPWYEGLSLLDFLETVHIDSDNNFSDFRFPVQYVLRPNLDFRGFCGKVASGIIRKGDKVMALPSGKVSHVKSIVTFDGELDYAFPPQSVTLTLEDEIDVSRGEMLVHPDNLPIVDRNFEAMLVWMDEEPMDINKSFFIKQTTNVSRTRIDSIKYKVDVNTMEHSSVPFLSLNEIARVVFTTAKELFFDPYRKNKSCGSFILIDPITNNTSAVGMIIDRVEKKDMNIADDFPVLNLPELGIAPEHYEAIEKAVKSLSEQGFEVRIEK
With CysD forms the ATP sulfurylase (ATPS) that catalyzes the adenylation of sulfate producing adenosine 5'-phosphosulfate (APS) and diphosphate, the first enzymatic step in sulfur assimilation pathway. APS synthesis involves the formation of a high-energy phosphoric-sulfuric acid anhydride bond driven by GTP hydrolysis by CysN coupled to ATP hydrolysis by CysD.
Q64VQ9
Q940Z2
ARP5_ARATH
Actin-related protein 5
Arabidopsis
MAFVSRIRRQSDYNTYPSSIPIVIDNGASYFRIGWAGETEPRVVFRNIVQRPRHKATGETVTIVGDLDPSMMKYFDCTRSGPRSPFDSNVVYQFEIMEYILDYAFDRLGANGSGIDHPILITECACNPVQSRSKMAELLFETYGVPAVAFGVDAAFSYKYNQLHGICKKDGIVLCPGFTTTHSIPFVDGEPIYKGSSRTNIGGYHVTDYLKQLLSLKYPFHSSRFTWEKAEDLKLEHCYIAPDYASEIRLFQEGRKEAEEKTSYWQLPWIPPPTEVPPSEEEIARKAAIREKQGQRLREMAEAKRVSKINDMENQLISLRFLLKQVDQVEEDDIPTFLSDTGYASRQELESTITKVTQSLRKARGEPKNEPAEYEENPDSLNNEKYPLMNVPDDILTPEQLKDKKRQMFLKTTAEGRLRARQKRNEEELEKEKRNQLEEERRRENPESYLEELQAQYKEVLERVEQKKRLKTNGSSNGNNKSGGIGRGERLSAAQRERMRLLTTAAFDRGKGEDTFGSRDEDWQLYKLMSKDNDDDDEQPDSDEAELARLSSRLQEIDPTFVQKVEGELSQTSGEVPRVRPLTEEDYKIVIGIERFRCPEILFHPNLIGIDQVGLDEMAGTSIRRLPHDEKELEERLTSSILMTGGCSLLPGMNERLECGIRMIRPCGSPINVVRAMDPVLDAWRGASAFAANLNFLGNAFTKMDYDEKGEDWLRNYQIRYNYL
Probable subunit of a chromatin-remodeling complex. Involved in DNA repair. Required for multicellular development of all organs.
Q940Z2
Q11JI6
LOLD_CHESB
Lipoprotein-releasing system ATP-binding protein LolD
unclassified Chelativorans
MPTSVLELKSVDRHYVQGQNTLTILKAADFTLAPGEMVALVAPSGTGKSTLLHIAGLLEHPDGGDVIVNGQPCAGLADDRRTEIRRKEIGFVYQFHHLLPEFTAIENVMMPQLIAGLSPAEARERAGQLLAYMKLGSRTEHRPSELSGGEQQRVAIARAVANAPLVLLADEPTGNLDPVTAGYVFEALEAIVRHSGLAALIATHNEELAARMDRRVTLSDGRVVELPAK
Part of the ABC transporter complex LolCDE involved in the translocation of mature outer membrane-directed lipoproteins, from the inner membrane to the periplasmic chaperone, LolA. Responsible for the formation of the LolA-lipoprotein complex in an ATP-dependent manner.
Q11JI6
Q1H145
DXR_METFK
2-C-methyl-D-erythritol 4-phosphate synthase
Methylobacillus
MPMLQNVTILGATGTIGLNTLDVISRHPGRYRVFALTANSRVDELAELCLQHRPRYAVMLDSGAAEKLQQKLKGLETQVLSGLAALEEVAAHPEAHVVMAAIVGAAGLKPAMAAAYAGKRILLANKETLVMAGKLFMQAVEEGGATLLPIDSEHNAIFQVMPPARLSALADGGIRRILLTASGGPFRKSSFAELMAVTPAQALNHPNWVMGPKITIDSATLMNKGLEVIEAHWLFNAPADKIEVVVHPQSVIHSMVEYIDGSVLAQMGNPDMRTPIAYGLGYPERLKAGVNALDLFKVGRLDFEAPDTARFPCLRLAFDALRHGGTAPAILNAANEVAVDAFLNGNIGFQDIPRLIEAVLTAMDIEAVTSISQLIEVDALARAHALEWRQLEAC
Catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).
Q1H145
B1LK58
HLDD_ECOSM
ADP-L-glycero-beta-D-manno-heptose-6-epimerase
Escherichia
MIIVTGGAGFIGSNIVKALNDKGITDILVVDNLKDGTKFVNLVDLDIADYMDKEDFLIQIMAGEEFGDVEAIFHEGACSSTTEWDGKYMMDNNYQYSKELLHYCLEREIPLLYASSAATYGGRTSDFIESREYEKPLNVYGYSKFLFDEYVRQILPEANSQIVGFRYFNVYGPREGHKGSMASVAFHLNTQLNNGESPKLFEGSENFKRDFVYVGDVADVNLWFLENGVSGIFNLGTGRAESFQAVADATLAYHKKGQIEYIPFPDKLKGRYQAFTQADLTNLRAAGYDKPFKTVAEGVTEYMAWLNRDA
Catalyzes the interconversion between ADP-D-glycero-beta-D-manno-heptose and ADP-L-glycero-beta-D-manno-heptose via an epimerization at carbon 6 of the heptose.
B1LK58
P77544
YFCF_ECOLI
Glutathione S-transferase YfcF
Escherichia
MSKPAITLWSDAHFFSPYVLSAWVALQEKGLSFHIKTIDLDSGEHLQPTWQGYGQTRRVPLLQIDDFELSESSAIAEYLEDRFAPPTWERIYPLDLENRARARQIQAWLRSDLMPIREERPTDVVFAGAKKAPLTAEGKASAEKLFAMAEHLLVLGQPNLFGEWCIADTDLALMINRLVLHGDEVPERLVDYATFQWQRASVQRFIALSAKQSG
Exhibits glutathione (GSH) S-transferase activity toward 1-chloro-2,4-dinitrobenzene (CDNB); however this activity is as low as 1% of that of GstA. Also displays a GSH-dependent peroxidase activity toward cumene hydroperoxide. Is involved in defense against oxidative stress, probably via its peroxidase activity.
P77544
Q9FI79
TED7_ARATH
Protein TRACHEARY ELEMENT DIFFERENTIATION-RELATED 7
Arabidopsis
MAASVEYFPYYSPPSHQHPLPSPVPPPPSHISPPPPPFSPPHHPPPPHFSPPHQPPPSPYPHPHPPPPSPYPHPHQPPPPPHVLPPPPPTPAPGHHVIIVVVISLGSLFFLAFLAAALFCYLKKRRKSSTKAEIIEFDEHLKVQETIVQGPHGEQTRVVMLEEDIHLVEDIHKTEKLSRPSHLSSTGRHAIDISDPNHHFTEQKS
Essential protein . Involved in the secondary cell wall (SCW) formation of vessel elements (e.g. protoxylem and metaxylem), thus promoting tracheary element (TE) differentiation .
Q9FI79
Q9HQS1
KAD6_HALSA
ATP-AMP transphosphorylase
Halobacterium
MRVAVTGTPGTGKTTATGRLDTALDVAHLNDLVGTEGLYDGVDADRGSKIVDVDAVRDHFAGREDVLVESHLAHRLDDLDAVVVLRCAPETLATRLQDRGDSPEKAAENADSEALAIILSEAVRGHGADAVYEIDTTDRSPDAVAAAIQAVLDGDREPSAGTVDYTDYV
Broad-specificity nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates.
Q9HQS1
P11847
RCEM_RHOCA
Photosynthetic reaction center M subunit
Rhodobacter
MAEYQNFFNQVQVAGAPEMGLKEDVDTFERTPAGMFNILGWMGNAQIGPIYLGIAGTVSLAFGAAWFFTIGVWYWYQAGFDPFIFMRDLFFFSLEPPPAEYGLAIAPLKQGGVWQIASLFMAISVIAWWVRVYTRADQLGMGKHMAWAFLSAIWLWSVLGFWRPILMGSWSVAPPYGIFSHLDWTNQFSLDHGNLFYNPFHGLSIAALYGSALLFAMHGATILAVTRFGGERELEQIVDRGTASERAALFWRWTMGFNATMEGIHRWAIWMAVMVTLTGGIGILLSGTVVDNWYVWAQVHGYAPVTP
The reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis.
P11847
Q8DPQ6
NORM_STRR6
Multidrug-efflux transporter
Streptococcus
MYKTKCLREKLVLFLKIFFPILIYQFANYSASFVDTAMTGQYNTMDLAGVSMATSIWNPFFTFLTGIVSALVPIIGHHLGRGKKEEVASDFYQFIYLALGLSVVLLGMVLFLAPTILNHIGLEAAVAAVAVRYLWFLSIGIIPLLLFSVIRSLLDSLGLTKLSMYLMLLLLPLNSGFNYLLIYGAFGVPELGGAGAGLGTSLAYWVLLGISVLVLFKQEKLKALHLEKRILLNMDKIKEGVRLGLPIGGTVFAEVAVFSVVGLIMAKFSSLIIASHQSAMNFSSLMYAFPMSISSAMAIVVSYEVGAKRFDDAKTYIGLGRWTALIFAAFTLTFLYIFRGNVASLYGNDPKFIDLTARFLTYSLFFQLADTFAAPLQGILRGYKDTVIPFYLGLLGYWGVAIPVATLFDSLTDFGAYSYWIGLIISLIVSGALYRWRLTVIMKRFESLAKSKR
Multidrug efflux pump.
Q8DPQ6
Q8N684
CPSF7_HUMAN
Pre-mRNA cleavage factor Im 59 kDa subunit
Homo
MSEGVDLIDIYADEEFNQDPEFNNTDQIDLYDDVLTATSQPSDDRSSSTEPPPPVRQEPSPKPNNKTPAILYTYSGLRNRRAAVYVGSFSWWTTDQQLIQVIRSIGVYDVVELKFAENRANGQSKGYAEVVVASENSVHKLLELLPGKVLNGEKVDVRPATRQNLSQFEAQARKRECVRVPRGGIPPRAHSRDSSDSADGRATPSENLVPSSARVDKPPSVLPYFNRPPSALPLMGLPPPPIPPPPPLSSSFGVPPPPPGIHYQHLMPPPPRLPPHLAVPPPGAIPPALHLNPAFFPPPNATVGPPPDTYMKASAPYNHHGSRDSGPPPSTVSEAEFEDIMKRNRAISSSAISKAVSGASAGDYSDAIETLLTAIAVIKQSRVANDERCRVLISSLKDCLHGIEAKSYSVGASGSSSRKRHRSRERSPSRSRESSRRHRDLLHNEDRHDDYFQERNREHERHRDRERDRHH
Component of the cleavage factor Im (CFIm) complex that functions as an activator of the pre-mRNA 3'-end cleavage and polyadenylation processing required for the maturation of pre-mRNA into functional mRNAs . CFIm contributes to the recruitment of multiprotein complexes on specific sequences on the pre-mRNA 3'-end, so called cleavage and polyadenylation signals (pA signals) . Most pre-mRNAs contain multiple pA signals, resulting in alternative cleavage and polyadenylation (APA) producing mRNAs with variable 3'-end formation . The CFIm complex acts as a key regulator of cleavage and polyadenylation site choice during APA through its binding to 5'-UGUA-3' elements localized in the 3'-untranslated region (UTR) for a huge number of pre-mRNAs . CPSF7 activates directly the mRNA 3'-processing machinery . Binds to pA signals in RNA substrates .
Q8N684
Q88QQ2
SYY_PSEPK
Tyrosyl-tRNA synthetase
Pseudomonas
MKSVEEQLALIKRGAEEVLVESELVEKLKRGQPLRIKAGFDPTAPDLHLGHTVLINKLRQFQDLGHQVIFLIGDFTGMIGDPSGKSATRPPLTREQVLENAETYKQQVFKILDPAKTEVAFNSTWMDKLTPADFIRLASQYTVARMLERDDFDKRYTTNQPIAIHEFLYPLVQGYDSVALKADVELGGTDQKFNLLMGRELQRSYGQEAQNIVTMPLLEGLDGVKKMSKSLGNYVGIQEAPGVMYSKLVSIPDTLMWRYFELLSFRSMEEIEQFRADVANGANPRDIKIKLAEEIVARFHGEEAAANAHRAAGNRMKEGELPEDLPEIEVAAAEDLPIAAVLNRAGLVKNSAQARDLLNSGAVKVDGAVVDKDFMFVLGATHVCQAGKKSFGRVTLKAE
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).
Q88QQ2
P0CAX1
GYRB_CAUVC
DNA gyrase subunit B
Caulobacter
MTTEEAAAQYGADSIKVLKGLDAVRKRPGMYIGDTDDGSGLHHMVYEVVDNAIDEALAGHATKVQVILNADGSVTVTDDGRGIPVDMHEGEGVSAAEVIMTQLHAGGKFDQNSYKVSGGLHGVGVSVVNALSDWLELLIHRNGKVHQMRFERGDAVTSLKVTGDSPVRTEGPKAGETLTGTEVTFFPSKDTFAFIEFDRKTLEHRLRELAFLNSGVTIWFKDHRDVEPWEEKLFYEGGIEAFVRHLDKAKTPLLKAPIAVKGVKDKVEIDLALWWNDSYHEQMLCFTNNIPQRDGGTHLSAFRAALTRIITSYAESSGILKKEKVSLGGEDSREGLTCVLSVKVPDPKFSSQTKDKLVSSEVRPAVEGLVSEGLSTWFEEHPNEAKAIVTKIAEAAAAREAARKARELTRRKSALDITSLPGKLADCSERDPAKSEIFIVEGDSAGGSAKQARNRDNQAVLPLRGKILNVERARFDKMLSSDQIGTLITALGAGIGRDDFNPDKVRYHKIVLMTDADVDGAHIRTLLLTFFYRQMPELIERGYIYIAQPPLYKASKGKSSRYLKDDAEMDAFLVDEGVDGAELDLASGERMTGQDLLALVQTCRSAKANIDRLAARAPATAIEQAALSGLLGESPNAAAAATRLDLYAEEGDGPWSGERGDTGFVFSRVRRGVSERVVLDDVLLHAADARRLAERAVKLTEIFSGRAIFRRKDKSTTVRGPLDLVNAVLDAGRKGLTIQRYKGLGEMNPDQLWETTLDAEARTLLQVRVNHADDADDMFSRLMGDLVEPRREFIQENALDAEVDV
A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner.
P0CAX1
Q39JC7
DNAJ_BURL3
Chaperone protein DnaJ
Burkholderia cepacia complex
MAKRDYYEVLGVAKNAGDDEIKKAYRKLAMKYHPDRNPDNKDAEEHFKEVKEAYEMLSDGQKRAAYDQYGHAGVDPNMGGAGAQGFGGFADAFGDIFGDIFGQAAGGAARGGRGGPQVYRGADLRYSMEITLEQAAHGYDTQIRVPSWVSCEVCHGSGAKPGTKPETCPTCHGQGTVRMSQGFFSIQQTCPKCHGTGTYIPEPCVHCHGSGKVKETKTLEVKIPAGIDDGMRIRSAGNGEPGINGGPPGDLYVEIHIKPHSVFERDGDDLHCQMPIPFTTAALGGEIEVPTLAGRASFPVPEGTQSGKTFRLRGKGIKGLRSSIAGDLYVHVQVETPVKLTDNQRDLLKQFEKSLAEGGARHSPQSKSWFDRVKSFFE
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Q39JC7
B6J4B0
AROE_COXB1
Shikimate dehydrogenase (NADP(+))
Coxiella
MDKYAVIGNPVEHSLSPVIFQAFEKQTNHSFDYLKIKAPVNGFAAAVKKFHDEGGKGANITLPFKEEAYQLADKRCQEANEAHAASALQFREDGTIYAVNYDGLGLVQDLTRNHNITLTQKSILIVGAGGATRGILGPLLNAAPEKIVIVNRTPSKAHALAKIFHLRGEIQGGGFDELEPMRYDVIIHATSLGHQGKFPPLPDGLVGSQSCCYDLSYGKIASPFLQWAKDQGAKYNFDGLGMLVEHNAAVFYLWFGIYPDTNPVIEMLQAHL
Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).
B6J4B0
P02139
HBB_CYPCA
Hemoglobin subunit beta-1/2
Cyprinus
VEWTDAERSAIIALWGKLNPDELGPEALARCLIVYPWTQRFFASYGNLSSPAAIMGNPKVAAHGRTVEGGLMRAIKDMDNIKATYAPLSVMHSEKLHVDPDNFRLLADCITVCAAMKFGPSGFSPNVQEAWQKFLSVVVNALKRQYH
Involved in oxygen transport from gills to the various peripheral tissues.
P02139
A5IFX9
AROB_LEGPC
3-dehydroquinate synthase
Legionella
MAKFELYAEVDVSISGHQYPIIICRNGLIDPELINRFITSKQVLIVTNRTVAPLYLGHLQSGLPSKQCDVVILEDGEEHKNQRSLFTIYDSLIQNKHHRDTSIIALGGGVIGDMAGFAASTYQRGVRFIQLPTTLLAQVDASVGGKTAINHPAGKNMIGSFYQPQAVIIDLNTLKTLPEREFRAGIAEMIKYALLVGGPFFERIQAVLQQGLTVHSPELPLLIAECCQVKAKIVEQDERESGLRALLNLGHTFAHALETYTDYKKWLHGEAVAIGLYCAAVLSEKKGLLDKPIVDQVEKMLIHAGLPHKIPNSIDLIQLRELMSLDKKIKNNCLRFVMIKKPGACYIDDSVTEDCLHNTLINVVEGEQK
Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ).
A5IFX9
Q810Y8
PRAL7_MOUSE
Preferentially expressed antigen in melanoma-like protein 7
Mus
MVSAPPTLQDQAFRSLVRNEVLTVSDAECLIREFFPPLFKEASTQKKPKTIMILVEHWPYPCLHVGLLIDKPNFQIFQAILDGVDTWLKRKYRPRMGRLKKVDFRDAQHHASLDMQDEREGRDYLVGTLPKKQIVEDHSRTRKERLKLFHDLSFMSSLHEDKHQTLLLEWAKERTSFLHLCCEKLEIGAVEVSKVRNVLKFLQPELIKELKLNTVGNLSKLAKFVPFIRKMRNLQKLMLVRTFGTRTFTQEEKQNISKIISLFCKLSCLRHLTIDDVYFLTDQMKELLRCLEAPLVSLKITLCQLSQSDLESFAQRWNYSQLKHLCLRGVTLTNLDVTPLRDFLKRVAANLQTLDLEDCRMDDSHFRTLLPALIKCTQLTSINLYDNDISEDVLENFLHRTTNLSQLTTEMYPAPSEVYNESNYVIVEIFIQICSELMNKLMEVRQANSVCFGSSSCYDCDNRYLYEDDGDVTLCLCQE
Promotes maintenance and self-renewal of pluripotent embryonic stem cells (ESCs), downstream of LIF/STAT3 . Maintains the pluripotency state of ESCs by repressing DNA methylation through the regulation of UHRF1 stability. Mediates the proteasomal degradation of UHRF1. Is required for the establishment of the blastocyst .
Q810Y8
Q864K3
MSHR_ERYPA
Melanocortin receptor 1
Erythrocebus
MPVQGSQRRLLGSLNSTPTATPHLGLAANQTGARCLEVSIPDGLFLSLGLVSLVENVLVVTAIAKNRNLHSPMYCFICCLALSDLLVSGSNMLETAVILLLEAGALAARAAVVQQLDNVIDVITCSSMLSSLCFLGAIAVDRYISIFYALRYHSIVTLPRARRAVAAIWVASVLFSMLFIAYYDHAAVLLCLVVFFLAMLVLMAVLYVHMLARACQHAQGIARLHKRQRPAHQSFGLKGAATLTILLGIFFLCWGPFFLHLTLIVLCPQHPTCSCIFKNFNLFLTLIICNAIIDPLIYAFRSQELRRTLKEVLLCSW
Receptor for MSH (alpha, beta and gamma) and ACTH. The activity of this receptor is mediated by G proteins which activate adenylate cyclase. Mediates melanogenesis, the production of eumelanin (black/brown) and phaeomelanin (red/yellow), via regulation of cAMP signaling in melanocytes.
Q864K3
P00442
SODC_BOVIN
Superoxide dismutase [Cu-Zn]
Bos
MATKAVCVLKGDGPVQGTIHFEAKGDTVVVTGSITGLTEGDHGFHVHQFGDNTQGCTSAGPHFNPLSKKHGGPKDEERHVGDLGNVTADKNGVAIVDIVDPLISLSGEYSIIGRTMVVHEKPDDLGRGGNEESTKTGNAGSRLACGVIGIAK
Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
P00442
A3LWH1
MDM12_PICST
Mitochondrial inheritance component MDM12
Scheffersomyces
MSFEINWENLTSDSSINESLKEFLDRQFQNISLPSYIANLSVTNFSVGDIPPEITIRHIGDPFDEFYEDENDEGSSGPERVSSNSNMNTKETNYMSSDDEDDDEDNDLSTILSTIAEDSHLNSFSHSSTLYHSHEQSPPPGPAPTPPLLLRSRTSLDPISYIMANTSLNYLHNYNINNIGLGHAPSGTETPTTILNQNALTNAKNSRVISSLQKTTRGENDIQIIAEIEYSGNLHVDLIVNLLVNYPSPNFISLPIKLHITDIVIHSIATIAYLKKAVYFSFLCDINESTPDYFSTSSSSSVSTSTAAPATPTTYNSGGNFVDYIADPNNRERIDIVKKIKIESEIGELENNVLRNVGKVEKFLIEQLRNIIREELAWPSWICIDMSEDEDEEEQTPSPDSRDSNVNSI
Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondria. MDM12 is required for the interaction of the ER-resident membrane protein MMM1 and the outer mitochondrial membrane-resident beta-barrel protein MDM10. The MDM12-MMM1 subcomplex functions in the major beta-barrel assembly pathway that is responsible for biogenesis of all mitochondrial outer membrane beta-barrel proteins, and acts in a late step after the SAM complex. The MDM10-MDM12-MMM1 subcomplex further acts in the TOM40-specific pathway after the action of the MDM12-MMM1 complex. Essential for establishing and maintaining the structure of mitochondria and maintenance of mtDNA nucleoids.
A3LWH1
Q5WWQ2
TRUD_LEGPL
tRNA-uridine isomerase D
Legionella
MYSLNWPRAYGIPNSTATFKLCPEDFQVNELFEGQFSGEGEHIVLKIEKKGLTTEQVIKSLARLINKPIKLISYAGLKDKQALTTQWLSIHAPGEVIEGIETLEAPGWKILECTRHNKKLRPGFLSGNHFTITLRNVSDESDLIHRIEQIKFKGVPNYFGEQRFGRDGGNLIKAEEILVQGRKVKDRFLKGMYFSAARSWLYNLILSRRVKESSWNLPLLGDVIQLVGSNSIFVNDKSLDEQLLQRIGEKDVSPASPLPGRSKNLVKGTALQIINEVYAEWSAWLDGLEKNGLEEAWRANILYAEQIEYRINQGTVELSFVLPAGAYATVVLRELVQY
Responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs.
Q5WWQ2
Q47LJ3
RL3_THEFY
50S ribosomal protein L3
Thermobifida
MTTKQIKGVLGEKLGMTQVFDESGKVVPVTVLKAGPAVVTRVRTPETDGYSAIQLGYGHINPRKVNKPLGDYLRKHNLTPRRHYVEVRTSDASEYTVGQEITADVFQPGEKVDVTGKTKGKGYAGVMKRHGFGGLGASHGTQRKHRSPGSIGGCATPGRVFKGMRMAGRMGNVRRTVQNLTVHSVDAEKGLLLVKGAVPGPNGGLVLVRTAVKGGK
One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit.
Q47LJ3
C3N5E1
TRM1_SULIA
tRNA(m(2,2)G26)dimethyltransferase
Sulfolobus
MKLKEVTEGKVRIFVPDPKEYMIEGKFDPSWAPVFYNPKMTFNRDLSVIVVSLLKPKIILDALSATGIRGIRYYVESWKSEQLILNDKNSTAASLIQINVKNNGIENAKIFNKDANALLYEIKSEYIDIDPFGSPVPFILSSINATIRNGIAAFTATDLSPLEGSSRTSCRRKYDAINYKLSSSKELGLRILIGKIIREAATLEKTVHPLFSFYADYYYRLFVIVESGARKADENINKNLKYFGECPRCGFQTFVDENCKTKCPICGENFIIIGPLYIGPLHNMEFLKRMIDTYSDFNYLSSFNRIQKLLNVIEKEAKYKSVFYNISKLASKLKVSAIPPIDSILECLGDASKTHFAPTGIRTDKGYEEIIRCVKSLR
Dimethylates a single guanine residue at position 26 of a number of tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.
C3N5E1
C3PMT3
RPPH_RICAE
(Di)nucleoside polyphosphate hydrolase
spotted fever group
MSNSSKKHFDLPYRPGVGMMILNADNHIFVGKRIDTKISAWQMPQGGIVPGETPSIAAMREMLEEIGSDKGYIIAESKFWYSYDVPSFLIPKLWNGNFRGQQQRWFLIRFTGNNEDININTSNPEFDQWRWASLDELLSIIIPFKRKLYQAVVKEFESLIQ
Accelerates the degradation of transcripts by removing pyrophosphate from the 5'-end of triphosphorylated RNA, leading to a more labile monophosphorylated state that can stimulate subsequent ribonuclease cleavage.
C3PMT3
F5GUE5
DAF14_CAEEL
Abnormal dauer formation protein 14
Caenorhabditis
MSNEQEDFGSLFNNQGELGIMDDFAEFGFQTTTTPTNWAAAGNYMYPDQVHLPASINNPNMPINDWLEDAPMPDCYNVPSTSTDENNDPFPFSNISSQSSLKPKTPEKAVVEVRPTGNEMLDPEPKYPKEEKPWCTIFYYELTVRLGKAFEAKVPTITIDGATGASDECRMSLTSQPSSRNSKSSQIRNTVGAGIQLAYENGELWLTVLTDQIVFVQCPFLNQTLNKPLKYVFRLQNKGDQKRMKIFDKEQFEQEKTLALGPLTEKEVADERMRIFSNIRVSFCKGFGETYSRLKVVNLPCWIEIILHEPADEYDTVFRINNERPEIGSRS
Probably an atypical receptor-regulated SMAD (R-SMAD) that is an intracellular signal transducer and transcriptional modulator activated by TGF-beta-like daf-7 signaling . Plays a role in TGF-beta-like daf-7 signaling in regulating entry into a developmentally arrested larval state known as dauer, in response to harsh environmental conditions; partially redundant with R-SMAD daf-8 .
F5GUE5
Q0I3P7
RIMP_HAES1
Ribosome maturation factor RimP
Histophilus
MATLEDKLQELLQPSVEDLGCELWGIECQRSGRFFTVRLYIDKKDGGVTVDDCADVSRQVSAVLDVEDPIADKYNLEVSSPGLNRPLFTLKQFENYIGQDISVHLRVPMLDRRKWQGKLEKIENDMLTLIVDNQPQVLVFGNIQKANVVPKFN
Required for maturation of 30S ribosomal subunits.
Q0I3P7
C3PH09
PNP_CORA7
Polynucleotide phosphorylase
Corynebacterium
MSAKNAKKQPNNSVEFLIDDDYGITEAIATLDNGDFGTRTIRFETGQLARQAGGSVTTYLDEDTMLLSTTTASNQPREGFDFFPLTVDVEERMYAAGKIPGSFFRREGRPSTEAILACRLIDRPLRPTFVKGLRNEVQVVVTVLSMDPEEYYDVVAINGASASTQLSGLPVSGPVGGVRMALIADDKHPKGQWVAFPNNEQHERALFEMVVAGRIVKKGRKDDVAIMMVEAGAGVNVAERIKEGAPAPQESTVAEGLEAAKPFIKSLCEAQAGLAERAAKETQEFPLFPPYGDDVYAAVEKAASKKLEKLLTIPGKQDRDDATNEYMEQVEAKLIEDFDDLDEADASKQIRNAFNAVMKDIVRTKILTEGFRIDGRGVTDIRDLGVEVDLIPRAHGSSLFERGETQILGVTTLDMLKMEQQIDSLTPVESKRYMHHYNFPPYSTGETGRVGSPKRREIGHGALAERALLPVIPSREDFPYAIRQVSEALGSNGSTSMGSVCASTLSLYNAGVPLKAPVAGIAMGLVSGEVNGKEKFVALTDILGAEDAFGDMDFKVAGTSEFITALQLDTKLDGIPSHVLADALEQARDARAAILDTMSEVIESPDEMSGLAPRITSVTIPVNKIGELIGPKGKTINAITEETGADVSIEEDGTVYISAATGEAADAAIDRVNSIANPQLPKVGERFLGTVVKTVAFGAFVSLTPGRDGLVHISKLGGDERIEKVEDVVNVGDKIQVEIADIDNRGKISLVPVEED
Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
C3PH09
B8D8T4
TGT_BUCA5
tRNA-guanine transglycosylase
Buchnera
MNFEVLYQDNNARCGVFNFNQEIIETPVFMPVGTYGAVKSISTEEIKNTGSRIILSNAFHLYFRPGLEIIKLHGNLHNFMNWSGPILTDSGGFQVFSLSRFCKVNEEGVIFQNHIDGKKTFLTPKISMKIQSDLGSNIVMIFDQCIEYNQNWEKTKNAMERSLYWAKKSRIYFDSYKNKNSLFGIIHGGIYPSLRDISLQELIKIDFDGYALGGLAVGEPKIEMYKLLDHICPQIPKNKPRYLMGVGKPEDLIEGVRRGVDMFDCVIPTRNARNGHLFVTNGVIKIRNKKYKKDLSCLDKTCVCYTCRYYSRSYLHHLDACNEILGARLNTIHNLHYYQTLMSNIRNSIKNNTFEQFSLNFYKQKNKIDF
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
B8D8T4
P47966
IL4_MERUN
Lymphocyte stimulatory factor 1
Meriones
MGLSPQLAAVLLCLLVCTGNYARRQDREAGLREIIHNLDQVLKKETPCTEMFVPDVLIATKNTTEKGLLCRATRVLRKFYFPREVTPCLKNNSGVLSILRKLCRSISTLHPQESCSVSTPTLTTLNDFLGRLRGIMQMKNWQG
Participates in at least several B-cell activation processes as well as of other cell types. It is a costimulator of DNA-synthesis. It induces the expression of class II MHC molecules on resting B-cells. It enhances both secretion and cell surface expression of IgE and IgG1. It also regulates the expression of the low affinity Fc receptor for IgE (CD23) on both lymphocytes and monocytes. Positively regulates IL31RA expression in macrophages. Stimulates autophagy in dendritic cells by interfering with mTORC1 signaling and through the induction of RUFY4.
P47966
P02168
MYG_OTOCR
Myoglobin
Otolemur
MGLSDGEWQLVLKIWGKVEADLAGHGQDVLIRLFTAHPETLEKFDKFKNLKTADEMKASEDLKKHGVTVLTALGGILKKKGQHEAEIKPLAQSHATKHKIPVKYLEFISEAIIHVLQNKHSGDFGTDVQGAMSKALELFRNDIAAKYKELGFQG
Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.
P02168
B2UX54
SYS_CLOBA
Seryl-tRNA(Ser/Sec) synthetase
Clostridium
MLDLKRIRNNPEEIKKLLSNRGEDFDVAVIDEIVTLDEERRKILVEVESLKGKRNQVSAEIPKLKKAGEDVTQIMNDMRKLGEEIKNFDTRVNEINERIEYIMLRIPNIPNPEVPDGETDEDNVEIKKWGEPTKFTFEPKAHWDLGTDLNILDFERGGKVAGSRFTVYKGLGARLERSIINYFLDKHTTENGYTEILPPYMVNRDSMTGTGQLPKFEEDAFKVENNGYFLIPTAEVPVTNMYRNEVLSGDILPIKHAAYSACFRAEAGSAGRDTRGLVRQHQFNKVELVKFCKPEDSYAELDKLVEDAESVLQGLGLPYRIVRICKGDLGFTAALKYDIEVWMPSYNRYVEISSCSNFEDFQARRANIKYRETPKDKPKFIHTLNGSGVAIGRTVAAVLENYQKEDGTVEIPEAIKRFMNVDFIK
Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec).
B2UX54
Q3TDN2
FAF2_MOUSE
UBX domain-containing protein 8
Mus
MAAPEEQDLTQEQTEKLLQFQDLTGIESMEQCRLALEQHNWNMEAAVQDRLNEQEGVPSVFNPPPARPLQVNTADHRIYSYVVSRPQPRGLLGWGYYLIMLPFRFTYYTILDIFRFALRFIRPDPRSRVTDPVGDIVSFMHSFEEKYGRAHPVFYQGTYSQALNDAKRELRFLLVYLHGDDHQDSDEFCRNALCAPEVISLINSRMLFWACSTNKPEGYRVSQALRENTYPFLAMIMLKDRRMTVVGRLEGLIQPDDLINQLTFIMDANQTYLVSERLEREERNQTQVLRQQQDEAYLASLRADQEKERKKREEKERKRRKEEEVQQQKLAEERRRQNLQEEKERKLECLPPEPSPDDPESVKIIFKLPNDSRVERRFHFSQSLTVIHDFLFSLKESPEKFQIEANFPRRVLPCVPSEEWPNPPTLQEAGLSHTEVLFVQDLTDE
Plays an important role in endoplasmic reticulum-associated degradation (ERAD) that mediates ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins. By controlling the steady-state expression of the IGF1R receptor, indirectly regulates the insulin-like growth factor receptor signaling pathway. Involved in inhibition of lipid droplet degradation by binding to phospholipase PNPL2 and inhibiting its activity by promoting dissociation of PNPL2 from its endogenous activator, ABHD5 which inhibits the rate of triacylglycerol hydrolysis.
Q3TDN2
Q5XIW8
SNUT1_RAT
Squamous cell carcinoma antigen recognized by T-cells 1
Rattus
MGSSKKHRGEKEAAGTTAAAGTGGTTEQPPRHREHKKHKHRSSGGGSSGGERRKRSRERGAERGSGRRGAEAEARSGAHGRERSQAEPSERRVKREKRDEGYEAAASSKASSGDASSLSIEETNKLRAKLGLKPLEVNAVKKEAGTKEEPVAADVINPMALRQREELREKLAAAKEKRLLNQKLGKIKTLGEDDPWLDDTAAWIERSRQLQKEKDLAEKRAKLLEEMDQEFGVSTLVEEEFEQRRQDLYSARDLQGLTVEHAIDSFREGETVVLTLKDKGVLQEGEDVLVNVNMVDKERADKNVELRKKKPDYLPYAEDESVDDLAQQKPRSILAKYDEELEGERPHSFRLEQGGMADGLRERELEEIRTKLRLQAQSLNTVGPRLASEYLSPEEMVTFKKTKRRVKKIRKKEKEVIMRADDLLPLGEDQTQDGDFGSRLRGRGRRRVPEVEEEALEDEEKDPVAQPPPSDDTRVENMDISDEEDGGALPSGPPELEEDEAELELQKQLEKGRRLRQLQQLQQLRDSGEKVLEIVKKLESRQRGWEEEEDPERKGTIVFNATSEFCRTLGEIPTYGLAGNREEQEELMDFERDEERSANGGSESDGEENIGWSTVNLDEEKQHQDFSASSTTILDEEPIVNRGLAAALLLCQNKGLLETTVQKVARVKAPNKSLPSAVYCIEDKMAIDDKYSRREEYRGFTQDFKEKDGYKPDVKIEYVDETGRKLTPKEAFRQLSHRFHGKGSGKMKTERRMKKLDEEALLKKMSSSDTPLGTVALLQEKQKAQKTPYIVLSGSGKSMNANTITK
Plays a role in mRNA splicing as a component of the U4/U6-U5 tri-snRNP, one of the building blocks of the spliceosome. May also bind to DNA.
Q5XIW8
Q5NR23
OBG_ZYMMO
GTP-binding protein Obg
Zymomonas
MQFLDQAKIYLRSGAGGPGAVSFRHEKYIEYGGPDGGNGGKGGDIVFEAVPGLNTLIDFRYTQHFRAARGASGAGSNKTGAGAKDLVIHVPVGTQVLSEDKEEILHDFTKVGERIIFLKGGDGGRGNASYKSSTNRAPRQHGPGWPAQEAWVWLRLKLLADVGLVGLPNAGKSTFLKATTNAHPKIGNYPFTTLHPQLGVVRRHGQEFVLADIPGLIEGASEGIGIGDRFLGHIERCRILLHLIDASGEDPIAAWHEVQNELALYGAGLAEKPQLLALNKIDSVDEETCAELSQALEEASGQKVLLLSGATGQGLDPILDQLITMTGRAIEKAQESSAQTEKIWSPI
An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis control.
Q5NR23
C0MFG8
RNPA_STRS7
Protein C5
Streptococcus
MKKSYRVKREKDFQAIFKLGQSMANRKFVIYHLKGEHKHFRAGISVGKKLGNAVTRNAVKRKIRHVLMELGDHLKTEDFVVIARRGAEELDYQAVKQNLHHVLKLAKLLEEGFEIEKKS
RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
C0MFG8
Q54IX3
PKS26_DICDI
Probable polyketide synthase 26
Dictyostelium
METNNNKNIQEDIAIIGFRIPGCQDNTPSELWNNLMNKFSGVGKTTERWSDNYHLSGDINNGNSGLLPLKEWKKFDPAFFGINPTMVSTIDPQQRILLKCTWEALEDAGIDPIKLRGSNTSIFIGCSTGDYLDMVKSNNEIQTNLFGSVNHSLSNRISYCFDFHGASMTIDSACSSSLNTVLLGCQSINQGKSNLCIAGGVNFILDTTIPTAFSFLNILSKNGKCMTYDEGADGFVRGEGAGLVVLKSLKDAIKDGNNIYCIIKGGNTNVDGNGNADKANFFQPSKQSQSDNIKLALESIKKKSMLDIDIDYVETHGTGTPTGDPIEVEGISKVFKENHSPENPLLIGSLKSNIGHMEAASGVTSLIKCCLMFKNKSFAPNVNFQKINPKIKLDEWNIKVVTEAIPFKKNKITSMVVNSFGVTGSNCCLVLTESINNNNNSNVDKITKNEKEYLIPFSANSNQSLKNYIEEVSKIDESLQFEDFVYKQLSNKSTSLFQRFVVTSKDWKELKYKLSQPLPLKEISSSISVKKPNPITVFVFCGQGSQFNKMGLELYNNDKNFRNYIDRFDKKLLEYYGYSVISKLRSIDDNDLITIHDPIIAQPATAILQISLFELYKHWGINPSFIVGHSLGELPMAFCSGMIDFDTVCYLLYHRSLAQSKTNGCGKMLSCNISSEEFVKNYSPRYPFLEIACYNSPNSIVVAGKESILLELSKEFKNSGIFCAMLGSLSSFHTSSQLEVKDHIYSLKFESKEPVIPTFSTVTTHLFNSNKLYDNDYIFQNIMKPVLFNETISNLYKHVENNQLGSEMIFIELAPHQTLSFYLKQLIPKDSNYFSNSNSITILSPLHKKKNDYLEIQQTISTCYCKGYDVNFKSQILIESKTNISNKSLPLYQWDDKEFWKDLEKQKRILQGPPMDTLGFSNEKSPILKSFETKIDIKKKPFQYLKGHIVKGKIYFPGVGYIENLLKMYPSQDIDIDSMEFEAPLILIEGIVTCLQSNVYKIGKNEFKVQFHFQDQKTKQWIQSSFANYHLSHRDDFDPTTNKLNIQNLISNNCNLTKLSKNQFYNFIKAKAGLSYNGEFQGVEKCYLGDNCSLVEIPFDTSNQDVETNINMIPILDSCLHGVHILYVEQCQMVLEKIEGLKYYSSTLILSKQKEQQKLYVFTRIENKDLINNSISASIIVMISDGTVFFEIESVSLKSLIPLKDPISIENPTDELFSSYLQSIDSLISEPSSYKSIYKRNEFISSGMSDLSRSDYQQFISTLLYTNLIKRNQSIESDLRNQIEFEEIKAKYCKNSKFERLFTFVIETIKQYDGINGNLNSWNEGNIDIYKILIKSTRIISKLLFPLQGEDTTIDTPQSLFENNLLDDFYNINGNTVIQNQLVGEIITQSIKPLINEKMVFRILEFGGGVGSLSIVTLNKINQLLEQHPNFQIDIEYTWTDISPSFIPDAKKLLSNIKGVTIIYRSLDLEESLIEKQLLKPSYYDFVIMSNVLHVIKEIKFGIDEIYKVLSPNGQLLFIETPYRMLICDSIFGVFDQWWGFTDTGIRVDRCCMKQKTWFKLLSESNYQDIIMSDDIKDCCFVIQAKKPSISSLEYKLKIDSQENDKIIVFGENDTFMKYLENKSTKQIIKIKTCQQFSDLITSNSKEINNQSIIYFIKTLNQLLIENFKEITLEYIQINQLLLSSGLSCKHILLLNQSTSENYLGSSISGAARYFDEFPPLKLYSFDFDKYSLNNESINIIDDIIEPIIKSMNNSNIRKELLVRNNKIFFERYKQEKRIKENYKSTSFENDKSLFVHLNANLEYELKSKQVKLKQNEIEVNVKATGINYKDYLVYTAMTPSELINHKGESNPEFGHDFSGIITRIGDDDGDNDNEFKVGDQVYGIWFNTTASHIIVDKEFLCHKPSKLSHTIASSIPVVYITSLYSLYNIGNIQNDESILIHSASGGIGLSALNILKWKNHKSHIFVTVGSKEKEKYIHDTYGDFITGIYSSRNKDYLKLIKRKLTELGSNKKGVDIILNTLSSSEHMVSNFKCLNHRGRIIDLSITHLNHNEYTCNNNFKYNYGYHNVEVLFVKGDIISKLLKNITSAIENGSLSTGIPIIEFNDSDCFNAIEFINKRQHIGKIVVNHNKENLIQELIKKTNLPIIKSNYQINSDHLGKNILVTGQSGIILEILKWIVKYSTNVENIIILSRSSLKWELELLVNKNKNKLNFIYKSVDVGNSLEIEKVIDEILMENPQINNVDSIFHYAFTQISCKEHEIDQVHLNVSHQAKTMGAINLHNQSIKRNWKLINFIMASSAAGLIGSTDQCSYVCSSNVLDTFSKYRKHVLGLPSICINYGLIESTGFVSRNQSVAVMLDGQGIRPMQTNQILGSLDLFIQNPSKSTNIILTSFNFNEFATGNLQQSNVHKFDFQFNCCLSQKSKLMANNQASENPVKDLLINNICELLSIDESKLNIDIRLIDYGSDSLTIVQIKNLIDKNLLIPNLISIQMLQNNSISDNIKILTDSYNKKKQNEQNELKNIKVGSFTKK
Probable polyketide synthase.
Q54IX3
C4Z4W1
Y2017_LACE2
Nucleoid-associated protein EUBELI_02017
Lachnospira
MAKRGGFPGGMPGNMNNLMKQAQRMQRQMEEQQAELENKEFSATAGGGVVEVTVTGKREVSKVKIDPEAVDPDDVEMLEDLIVAATNEALRKCEEESQAQMAKITGGLGGLGGGLF
Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection.
C4Z4W1
A1JI37
STHA_YERE8
NAD(P)(+) transhydrogenase [B-specific]
Yersinia
MQQHFHFDAIVIGSGPGGEGAAMGLVKQGARVAVIERYNNVGGGCTHWGTIPSKALRHAVSRIIEFNQNPLYSDNARTISSSFSDILNHADRVINQQTRMRQGFYDRNHCQMFSGDASFIDANTINVRYADGTNDTLRADNIVIATGSRPYRPANVDFTHERIYDSDTILQLSHEPQHVIIYGAGVIGCEYASIFRGLSVKVDLINTRDRLLAFLDQEMSDALSYHFWNNGVVIRHNEEFEQIEGTVDGVIVHLKSGKKVKADCLLYANGRTGNTSGLGLEKIGLEADSRGLLKVNSMYQTALSHVYAVGDVIGYPSLASAAYDQGRIAAQAMIKGEANTHLIEDIPTGIYTIPEISSVGKTEQDLTAMKVPYEVGRAQFKHLARAQIVGMDTGSLKILFHRETKQILGIHCFGERAAEIIHIGQAIMEQKGEGNTIEYFVNTTFNYPTMAEAYRVAALNGLNRLF
Conversion of NADPH, generated by peripheral catabolic pathways, to NADH, which can enter the respiratory chain for energy generation.
A1JI37
A1TUV3
RBSD_ACIAC
D-ribose pyranase
Acidovorax
MKRTALLHADLSRAIAALGHGDMIVIGDAGLPIPPGPLRIDLAVTPGLPAVADVLAAVLSEMQVERALVATEAVERAGGALPGWAGALPVAPQTLSHEEFKRLTRDARAVVRTGECTPYANVILCAGVTF
Catalyzes the interconversion of beta-pyran and beta-furan forms of D-ribose.
A1TUV3
Q5FRT8
RL25_GLUOX
General stress protein CTC
Gluconobacter
MANLTTLAVSTRAKAGKGAARATRREGLVPAVIYGGKQEPSIIALDPRVIMKELHRGGWSSRVYNLAAEGAEPVAALIRDVQLHPVTDAPIHVDFQRVAAGTKVHVEVSIAFVGEEKSPGIKRGGVLNVVRHYVDVQADPANIPEHFTAELSGLDIHDNVRWTDLKGTEGVVLGSGQAADMVIASIAAPTIDAEMEAEAAAKAAAEAEAAAKPGAKKK
This is one of the proteins that binds to the 5S RNA in the ribosome where it forms part of the central protuberance.
Q5FRT8
Q60771
CLD11_MOUSE
Oligodendrocyte-specific protein
Mus
MVATCLQVVGFVTSFVGWIGIIVTTSTNDWVVTCSYTIPTCRKMDELGSKGLWADCVMATGLYHCKPLVDILILPGYVQACRALMIAASVLGLPAILLLLTVLPCIRMGHEPGVAKYRRAQLAGVLLILLALCAIVATIWFPVCAHREITIVSFGYSLYAGWIGAVMCLVGGCVIVCCSGDAQSFGENRFYYSSGSSSPTHAKSAHV
Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity.
Q60771
Q07H98
RUVB_RHOP5
Holliday junction ATP-dependent DNA helicase RuvB
Rhodopseudomonas
MTPPSRIVTPERRADDVGDTALRPQTLAEFVGQQQARANLQIFIDAARKRQEALDHVLFVGPPGLGKTTLAQIVARELGVGFRATSGPVIAKAGDLAALLTNLEERDVLFIDEIHRLSPAVEEVLYPAMEDFQLDLIIGEGPAARSVKIELSKFTLVGATTRAGLLTNPLRDRFGIPIRLNFYTVEELEGIVSRGARVLGTGITPDGANEIARRARGTPRIAGRLLRRVRDFASAADAAAIDRRIADHALSALEVDAAGLDAMDRRYLSTIALNYGGGPVGVETMAAALSEPRDAIEDIIEPFLIQCGYLQRTPRGRLLTSHAFKHLGLAEPSREASQFGLFGGDEE
The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing.
Q07H98
B8DC19
DAPB_LISMH
4-hydroxy-tetrahydrodipicolinate reductase
Listeria
MRVAVSGFKGRMGHEVVKTVLREADLELVAVLDHEPKEKNINEIVEFSSLDVPVFGNLSEMLEEIKPDCVVDFTTPKVGYSNTKTILEHGVRAVVGTTGFTPEQISELRSIAESKKIGALIAPNFAVGAVLMMQFAQKAAKYFPNVEIIELHHDNKLDAPSGTAVKTAEMMAETREFVKQGAADEVELIEGARGSEYEGMRIHSVRLPGLVAHQEVIFGAEGQGLTIRHDSYDRISFMSGVALSVRKTKELETLIYGLENILD
Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
B8DC19
Q43497
MDAR_SOLLC
Ascorbate free radical reductase
Solanum subgen. Lycopersicon
MAEKSFKYVIVGGGVSAGYAAREFAKQGVKPGELAIISKEAVAPYERPALSKAYLFPEGAARLPGFHVCVGSGGERQLPEWYAEKGISLILSTEIVKADLASKTLVSAAGESFKYQTLVIATGTTVLKLSDFGVQGADSKNIFYLREIDDADQLVEALKAKKNGKAVVVGGGYIGLELSAVLRLNNIEVNMVYPEPWCMPRLFTEGIAAFYEGYYKNKGVNIIKGTVAVGFDTHPNGEVKEVKLKDGRVLEADIVVVGVGARPLTTLFKGQVEEEKGGIKTDAFFKTSVPDVYAVGDVATFPLKMYNEIRRVEHVDHSRKSAEQAVKAIFASEQGKSVDEYDYLPYFYSRAFDLSWQFYGDNVGETVLFGDADPNSATHKFGQYWIKDGKIVGAFLESGSPEENKAIAKVAKVQPPATLDQLAQEGISFASKI
Catalyzes the conversion of monodehydroascorbate to ascorbate, oxidizing NADH in the process.
Q43497
P60009
ACT_CANGA
Actin
Nakaseomyces/Candida clade
MDSEVAALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGIMVGMGQKDSYVGDEAQSKRGILTLRYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPMNPKSNREKMTQIMFETFNVPAFYVSIQAVLSLYSSGRTTGIVLDSGDGVTHVVPIYAGFSLPHAILRIDLAGRDLTDYLMKILSERGYSFSTTAEREIVRDIKEKLCYVALDFEQEMQTAAQSSSIEKSYELPDGQVITIGNERFRAPEALFHPSVLGLESAGIDQTTYNSIMKCDVDVRKELYGNIVMSGGTTMFPGIAERMQKEITALAPSSMKVKIIAPPERKYSVWIGGSILASLTTFQQMWISKQEYDESGPSIVHHKCF
Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
P60009
B6J5D4
RL23_COXB1
50S ribosomal protein L23
Coxiella
MNEERLFKILLAPHISEKGALTTGQYVFEVMPDATKPEIKRAVEKQFNVTVKSVRTCNVKGKTTRFRQVRGRRKNWKKAYVMLAPGSEIDIAAGE
One of the early assembly proteins it binds 23S rRNA. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the ribosome. Forms the main docking site for trigger factor binding to the ribosome.
B6J5D4
Q10058
YAM3_SCHPO
Putative oxidoreductase C1F5.03c
Schizosaccharomyces
MSNSRNIVIVGGGITGVSCLYFLAHHPSFNRDRDTITLFESAGIASAASGKASGFLSLEWHGPSTSSLAALSYNLHKELSDQYDGVNKWGYRALDTWSIKADENCQQPDKLPEGIEWIAPSIVENVTRLGNKKNSGQVHPYKFCHAIYEEASKVANVTLVKGHVLSVDENEVEYRLIGDDYAPDEEEEITSAEELHTIHSMEATHIIVAAGPWTPQLIPNLRISGARIHSITIDLPIKLNGNAVFSEITYKDGTIAAPEFYAREDELYVCGEFDDEPLPELSSDTKVDQDKCALIKQCANHFHQIIRDSPVKVRQACYLPISNATGAPVIGKIGSSIYVAAAHGCWGITLGPGTGKVLSELILDGAVTSANIDLLDPEGSLE
Putative oxidoreductase that negatively regulates the retrieval of cargo from late endosomes to the Golgi.
Q10058
Q9Z0S1
BPNT1_MOUSE
PAP-inositol 1,4-phosphatase
Mus
MASSHTVLMRLVASAYSIAQKAGTIVRCVIAEGDLGIVQKTSATDLQTKADRLVQMSICSSLARKFPKLTIIGEEDLPPGEVDQELIEDGQWEEILKQPCPSQYSAIKEEDLVVWVDPLDGTKEYTEGLLDNVTVLIGIAYEGKAIAGIINQPYYNYQAGPDAALGRTIWGVLGLGAFGFQLKEAPAGKHIITTTRSHSNQLVTDCISAMNPDTVLRVGGAGNKIIQLIEGKASAYVFASPGCKKWDTCAPEVILHAVGGKLTDIHGNALQYNKEVKHMNSAGVLAALRNYEYYASHVPESVKNALIP
Converts adenosine 3'-phosphate 5'-phosphosulfate (PAPS) to adenosine 5'-phosphosulfate (APS) and 3'(2')-phosphoadenosine 5'- phosphate (PAP) to AMP. Has 1000-fold lower activity towards inositol 1,4-bisphosphate (Ins(1,4)P2) and inositol 1,3,4-trisphosphate (Ins(1,3,4)P3), but does not hydrolyze Ins(1)P, Ins(3,4)P2, Ins(1,3,4,5)P4 or InsP6.
Q9Z0S1
B2I605
ERA_XYLF2
GTPase Era
Xylella
MTQTVPYRCGRIAVIGRPNVGKSTLTNALVGTKISIVSNRPQTTRHRLLGIATFPEGQIILVDTPGLHREQKHPMNRLMNRTARGSLEDVDAALLVTESTHWNEEDTLAYNLLNDTGIPVVLVINKIDRFKDKSALLPFLTHINENHTFATIHPVSALKRKGLKTLVSDLLALLPEGGPMFSEDEITDRSQRFLASELVREQVMRQLGKELPYATTVEIEYFTENTGLFRIGALIWVERESQKAIVIGKGGVRLKEIGVKARQQMERLFQTKVFLETWVRVRKDWSNNEAALKTFGYE
An essential GTPase that binds both GDP and GTP, with rapid nucleotide exchange. Plays a role in 16S rRNA processing and 30S ribosomal subunit biogenesis and possibly also in cell cycle regulation and energy metabolism.
B2I605
C0HJW7
MANA_LABPU
Alpha-mannosidase
Lablab
LVSSGQLEFIDGGVQIDPFGHSAVQAYFEVNDNSLPVQDNVELFDYNVQERVNDFVAAALSQANITRVNALYSTPSIYTDAKYATNEYWPLKTDDFFPYADRFNSGPNTDSLADALAIAQHHDAVTGTEKLAIGYQEAEELVSSSLACVQDSDGLEIESQLLPQQKVSVPPLGFSTYTVLTAKYDETGQASGAYLFRPDGTWHGNAKLTVLDGPVLDEVHQQINPWIYQITRSVLVDRPLGGSSLQDGQIELYYRIDPLGEGAKWRRSFGQEIYSPLLLAFAEQDDQDEW
Liberates mannose from p-nitrophenyl-alpha-D-mannoside.
C0HJW7
Q5HKP0
HIS5_STAEQ
ImGP synthase subunit HisH
Staphylococcus
MIAIIDYGLGNISNVTRAIQHLGYDVILTCDDKDVQKAEAIVLPGVGHFQDAMHSIEEKSIKDMLKNIHDKPIIGICLGMQLLFQHSAEGDVSGLELVPGNIVPIQSSHPIPHLGWNELKSTHPLLQSDVYFVHSYQAEMSEYVVAYADYGTKIPGVIQYRNYIGIQFHPEKSGTYGLEILNQALKGGFIND
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.
Q5HKP0
C4LAE6
GLYA_TOLAT
Serine hydroxymethyltransferase
Tolumonas
MLKRDMNIADYDPELWASIVEETQRQEEHIELIASENYTSPRVMQAQGSQLTNKYAEGYPGKRYYGGCEFVDKTETLAIERAKALFGAVYANVQPHSGSQANAAVYMALLKPGDTVLGMNLAHGGHLTHGSPVNFSGKLYNIVPYGIDASGKIDYVELERLALEHKPKMVLGGFSAYSGVVDWAKMREIADKVGAYLFVDMAHVAGLVAAGVYPNPVPHAHVVTSTTHKTLAGPRGGLILSAVNDEELHKKLNSAVFPGTQGGPLMHVIAGKAVAFKEAMEPEFKAYQQQVVKNSKAMVEVFLARGYKIVSGGTENHLFLVDFTDRELTGKEADAALGLANITVNKNSVPNDPRSPFVTSGIRIGSPSITRRGFKEAEAKELAGWICDVLDNRTDEAVIAATRAKVLDICKRLPVYA
Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.
C4LAE6
Q96TA2
YMEL1_HUMAN
YME1-like protein 1
Homo
MFSLSSTVQPQVTVPLSHLINAFHTPKNTSVSLSGVSVSQNQHRDVVPEHEAPSSECMFSDFLTKLNIVSIGKGKIFEGYRSMFMEPAKRMKKSLDTTDNWHIRPEPFSLSIPPSLNLRDLGLSELKIGQIDQLVENLLPGFCKGKNISSHWHTSHVSAQSFFENKYGNLDIFSTLRSSCLYRHHSRALQSICSDLQYWPVFIQSRGFKTLKSRTRRLQSTSERLAETQNIAPSFVKGFLLRDRGSDVESLDKLMKTKNIPEAHQDAFKTGFAEGFLKAQALTQKTNDSLRRTRLILFVLLLFGIYGLLKNPFLSVRFRTTTGLDSAVDPVQMKNVTFEHVKGVEEAKQELQEVVEFLKNPQKFTILGGKLPKGILLVGPPGTGKTLLARAVAGEADVPFYYASGSEFDEMFVGVGASRIRNLFREAKANAPCVIFIDELDSVGGKRIESPMHPYSRQTINQLLAEMDGFKPNEGVIIIGATNFPEALDNALIRPGRFDMQVTVPRPDVKGRTEILKWYLNKIKFDQSVDPEIIARGTVGFSGAELENLVNQAALKAAVDGKEMVTMKELEFSKDKILMGPERRSVEIDNKNKTITAYHESGHAIIAYYTKDAMPINKATIMPRGPTLGHVSLLPENDRWNETRAQLLAQMDVSMGGRVAEELIFGTDHITTGASSDFDNATKIAKRMVTKFGMSEKLGVMTYSDTGKLSPETQSAIEQEIRILLRDSYERAKHILKTHAKEHKNLAEALLTYETLDAKEIQIVLEGKKLEVR
ATP-dependent metalloprotease that catalyzes the degradation of folded and unfolded proteins with a suitable degron sequence in the mitochondrial intermembrane region . Plays an important role in regulating mitochondrial morphology and function by cleaving OPA1 at position S2, giving rise to a form of OPA1 that promotes maintenance of normal mitochondrial structure and mitochondrial protein metabolism . Ensures cell proliferation, maintains normal cristae morphology and complex I respiration activity, promotes antiapoptotic activity and protects mitochondria from the accumulation of oxidatively damaged membrane proteins . Required for normal, constitutive degradation of PRELID1 . Catalyzes the degradation of OMA1 in response to membrane depolarization . Required to control the accumulation of nonassembled respiratory chain subunits (NDUFB6, OX4 and ND1) .
Q96TA2
Q6MEE8
ISPD_PARUW
MEP cytidylyltransferase
Candidatus Protochlamydia
MEHQLIPFTVVLLAGGMGTRMKNLIPKQYLTIQEKPIALHSFEKLASMPEIEQMIVVCEPQYEQLFTVYKLNKPLIFARPGLRRQDSLWNGIKLIAGNPLVCIHDSARPFIEIDRIRQTVAEAEKWGAAVLGVRVKATIKICEEKQFIVNTPNRAFLWEMQTPQIVRLKLLYDGFSVAQKNELTVSDDVSLVELIDKPVKVVEGSYLNIKITTPEDLLIAQSILKNHALL
Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
Q6MEE8
B5XVW1
FADI_KLEP3
Fatty acid oxidation complex subunit beta
Klebsiella
MSQALPLITRQGDRIAIVRGLRTPFARQATVFHGVPAVDLGKMVVGEMLARSDIPADVIEQLVFGQVVQMPEAPNIAREIVLGTGMSVHTDAYSVSRACATSFQAVANVAESLMAGTIRAGIAGGADSSSVLPIGVSKTLARTLVDANKARTLSQKLKLFSRLRPRDLLPVPPAVAEYSTGLRMGDTAEQMAKSWGITREQQDALAHRSHQLAAKAWEEGKLSAEVMTAYAPPFREPLEQDNNIRKNSTLADYQKLRPAFDRKHGTVTAANSTPLTDGAAAVILMTESRAKELGLTPLGYLRSYAFTAIDVWQDMLLGPAWSTPLALERAGLTLADLTLIDMHEAFAAQTLANLQCLASERFAREVLGRSQATGEVDESKFNVLGGSIAYGHPFAATGARMITQTLHELRRRGGGFGLVTACAAGGLGAAMIVEAE
Catalyzes the final step of fatty acid oxidation in which acetyl-CoA is released and the CoA ester of a fatty acid two carbons shorter is formed.
B5XVW1
O82531
PSB1_PETHY
20S proteasome subunit beta-6
Petunia
MTKQQANWSPYDNNGGTCVAVAGADYCVIAADTRMSTGYNILTRDYSKIIKLADKCVMASSGFQADVRALQKVLASRHLIYQHQHNKQMSCPAMGQLLSNTLYYKRFFPYYSFNVLGGLDSEGKGCVFTYDAVGSYERVGYSSQGSGSTLIMPFLDNQLKSPSPLLLPAQDAVTPLSEAEAIDLVKTCFASATERDIYTGDRLEIVILNASGIRREEMELRKD
Non-catalytic component of the proteasome, a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity.
O82531
Q6GDC5
HIS1_STAAR
ATP phosphoribosyltransferase
Staphylococcus
MLRIAIAKGRLMDSLINYLDAIEFTTLSETLKNRERQLLLSVDNIECILVKGSDVPIYVEQGIADIGIVGSDILDERHYNVNNLLNMPFGACHFAVAAKPETTNYRKIATSYVHTAETYFKSKGIDVELIKLNGSVELACVVDMVDGIVDIVQTGTTLKANGLVEKQHISDINARLITNKAAYFKKSQLIEQFIRSLEVSIANA
Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity.
Q6GDC5
P51299
RK18_PORPU
50S ribosomal protein L18, chloroplastic
Porphyra
MKINSKQTRIHKHRRVRKKVQGTASRPRLCVFRSNKHIYAQVIDDIKGITLVAASSINLKLQSSITLGSNCEASRSVGKTLAERSIKEGIENVVFDRGGKLYHGRVEALAEAAKEAGMVF
Binds 5S rRNA, forms part of the central protuberance of the 50S subunit.
P51299
Q9RRC1
MOAC_DEIRA
Molybdenum cofactor biosynthesis protein C
Deinococcus
MSDPQGDAPQLTHFVGGQPRMVDVSAKAPTTRTARAEAWVLLPPESRAALLAGQTPKGDPLSVARLAGLAGSKRTADLIFLCHPIPVTSAEVDVTLKDAGIHITALVKTTAPTGVEMEALTAVTVAALNVYDMLKATSKAIEVSGVRLLSKTGGKSGDYQAAERPPQP
Catalyzes the conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP).
Q9RRC1
P97813
PLD2_MOUSE
Phosphatidylcholine-hydrolyzing phospholipase D2
Mus
MTVTQKNLFPYGDYLNSSQLHMEPDEVDTLREGEDPADRMHPYLAIYDLQPLKAHPLVFAPGVPVIAQVVGTERYTSGSKVGTCTLYSVRLTHGDFTWTTKKKFRHFQELHRDLQRHKVLMSLLPLARFAVTHSPAREAAAEDIPSLPRGGSEGSARHTASKQKYLENYLNRLLTMSFYRNYHAMTEFLEVSQLSFIPDLGSKGLEGVIRKRSGGHRVPGFTFCGRDQVCYRWSKRWLVVKDSFLLYMRPETGAISFVQLFDPGFEVQVGKRSTETRYGVRIDTSHRSLILKCSSYRQARWWGQEITELAQGSGRDFLQLHQHDSYAPPRPGTLARWFVNGAGYFAAVADAILRAQEEIFITDWWLSPEIYLKRPAHSDDWRLDIMLKRKAEEGVRVSILLFKEVELALGINSGYSKRTLMLLHPNIKVMRHPDLVTLWAHHEKLLVVDQVVAFLGGLDLAFGRWDDVQYRLTDLGDPSEPVHLQTPTLGSDPAATPDLSHNQFFWLGKDYSNLITKDWVQLDRPFEDFIDRETTPRMPWRDVGVVVHGVAARDLARHFIQRWNFTKTTKARYKTPLYPYLLPKSTSTANNLPFMIPGGQCATVQVLRSVDRWSAGTLENSILNAYLHTIRESQHFLYIENQFFISCSDGRTVLNKVGDEIVDRILKAHEQGQCFRVYLLLPLLPGFEGDISTGGGNSIQAILHFTYRTLCRGEHSILHRLKAAMGTAWRDYMSICGLRTHGELGGHPISELIYIHSKMLIADDRTVIIGSANINDRSLLGKRDSELAILIKDTEMEPSLMDGVEYQAGRFALSLRKHCFSVILGANTWPDLDLRDPVCDDFFQLWQETAENNATIYEQIFRCLPSNATRSLRALREYVAVESLATVSPSLAQSELAHIQGHLVHFPLKFLEDESLLPPLGSKEGMIPLEVWT
Function as phospholipase selective for phosphatidylcholine . May have a role in signal-induced cytoskeletal regulation and/or endocytosis .
P97813
Q3V522
CYF_ACOCL
Cytochrome f
Acorus
MQNRNTFSWVKEQMTRFISVSIMIYVITRTSIANAYPIFAQQGYENPREATGRIVCANCHLANKPVDIEVPQAVLPDTVFEAVVRIPYDKQLKQVLANGKKGSLNVGAVLILPEGFELAPPDRISPEMKEKMGNLAFQSYRPTKKNIIVIGPVPGQKYSEIVFPILSPDPATKKDVHFLKYPIYVGGNRGRGQIYPDGSKSNNTVYNATAAGVVSRILRKEKGGYEITIADASDGHQVVDIIPPGPELLVSEGESIKLDQPLTSNPNVGGFGQGDAEIVLQDPLRVQGLLFFLASVILAQIFLVLKKKQFEKVQLYEMNF
Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
Q3V522
B2GUZ2
SKA3_RAT
Spindle and kinetochore-associated protein 3
Rattus
MNPIQSFHCKLRSLATVLDGETARLLRALDGEDSEDFEDSSARILCDLYSEVQTLKDDVNAHLDKARLESRESTHFIKAAKVLMKKNSADIIKLREFFQKYGYQARDKEDSACEHRVSNSSPGLAVCKDTQEPGVKQELSEPRVPRGSAPEEPLRSPQLSDFGLQRYMVSQGPANPRQETVSLKEDRASETTPAKDPSVQVLKTPRCALKMDDFECVTPKLEHFGISEYTMCLNEDYTMGLKNMKSIKSSPLSGVGGEAVETGPVTSDNSFAIPGPMIQQLEKNDVEYINSPLPPKFCTPGLKIPSSMDSTDLVSIDYPLSKPNSSPTDLEDKDCAPLILNSDECYQSFADPHSPTITSYENFTTPSPPKVTAIPEDILQMLKYNSNLASPIDVKAMPLRRGFTSKGQSTRGAANKENW
Component of the SKA1 complex, a microtubule-binding subcomplex of the outer kinetochore that is essential for proper chromosome segregation. The SKA1 complex is a direct component of the kinetochore-microtubule interface and directly associates with microtubules as oligomeric assemblies. The complex facilitates the processive movement of microspheres along a microtubule in a depolymerization-coupled manner. In the complex, it mediates the microtubule-stimulated oligomerization. Affinity for microtubules is synergistically enhanced in the presence of the ndc-80 complex and may allow the ndc-80 complex to track depolymerizing microtubules.
B2GUZ2
Q75A44
LDB17_ASHGO
Protein LDB17
Eremothecium
MALKPPYSPESGGASRSRTQTETVHFWEYLESLLDAADCTSEAQVNSALVAYVKTASERYGEYLVEDRDFYRVALLLLRAPLYERNKSFCISKMLSLLSIDLLEMSMKFVISYILLCECKADSSSLDHVLDYQGFTVIYNKLYEHFAYLHRYSDDEETTFEANITELDEEINEELRKISTVLLDLLFQILKYSKCELANLQRVDDFFVYYMMVSLRSDTVEDMYNNAKFRLLLALNEQYMISNHKAGLENKVYAYLMNHTASKQFVELLLLQFNRTVDKSLQIMMCKIIYLILTSRDEIAMDYFYLNDLHVVTDVLIRNLTNISEDEEVLRNTFLRILDLILRKTEWTQSHYREQELLELLEYLCSVDNLCSSGNVKSEHMSTTKLAFKCRQAIRQLKVEQKKSRDAAAAPAPRPKTPEPRFERTDSHMSVPMDKITRAIGRSPFASPPPPPPSRRV
May be involved in protein-linked oligosaccharide phosphorylation.
Q75A44
Q6HCY5
HDOX_BACHK
Iron-responsive surface determinant
Bacillus cereus group
MIIVTNTAKITKGNGHKLIDRFNKVGQVETMPGFLGLEVLLTQNTVDYDEVTISTRWNAKEDFQGWTKSPAFKDAHSHQGGMPDYILDNKITYYNVEVVRMPMAAAQ
Allows bacterial pathogens to use the host heme as an iron source. Catalyzes the oxidative degradation of the heme macrocyclic porphyrin ring to the biliverdin in the presence of a suitable electron donor such as ascorbate or NADPH--cytochrome P450 reductase, with subsequent release of free iron.
Q6HCY5
P30362
ASPG_LUPAR
Isoaspartyl peptidase/L-asparaginase subunit beta
Lupinus
PPERRKPREEGLRHCLQIGVEALKARKSPLDVVELVVRELENNEHFNAGIGSVLTNSGTVEMEASIMDGKSMKCGAVSGLSTVLNPISLARLVMEKTPHMYLAFQGAQDFAKQQGVETVDSSHFITAENVERLKLAIEANRVQIDYSQYNYTQPVQDDAEKELPVANGDSQIGTVGCVAVDSQGNLASATSTGGLVNKMVGRIGDTPLIGAGTYANELCAVSATGKGEAIIQATVARDVAALMEFKGLSLKEAADYVVHERTPKGTVGLIAVSAAGEIAMPFNTTGMFRACATEDGNSEIAIWPPA
Degrades proteins damaged by L-isoaspartyl residue formation (also known as beta-Asp residues). Also has L-asparaginase activity, which is used to liberate stored nitrogen during seed development.
P30362
Q57E41
UVRC_BRUAB
Excinuclease ABC subunit C
Brucella
MPDTAGLSGPDIINAFVKRLPNNPGVYRMFNSDGGVLYVGKARNLKKRVSNYARGIGHSNRITRMIRETVTMEFVVTRTETEALLLEANLIKRLRPRFNVLMRDDKSFPYILLTGGHRAPGIFKHRGARSRKGDYFGPFASAGAVGRTINALQRAFLLRTCTDSVFETRTRPCLLYQIKRCSAPCTYEISDEDYAGLVAEAKAFLSGKSQSVKDHLAAAMQAASADLDFEHAAVYRDRLAALSHVQSHQGINPQTVEEADVFAIHQEGGMTCIQVFFFRTGQNWGNRAYFPKADSSLGPAEVLGAFLSQFYDDKPCPKLVLLSETVEEQSLITEALSTRAGHKVQVSVPQRGEKKELVQHALTNAREALGRRLAETSSQARLLQGLAETFGLPRAPRRIEVYDNSHIMGTNAVGGMIVAGPEGFVKNQYRKFNIRSTDITPGDDFGMMREVIERRFSRLVKEHGTPAGEVKNPDAFPAWPDVILIDGGQGQVGAVRQILGEMGISDLVTAIGIAKGVDREAGRERFFMEGKQPFTLPPRDPVLYFIQRLRDEAHRFAIGTHRARRKKEIVRNPLDEIAGIGPTRKRALLHHFGTAKAVSRAAVEDLMQIDGISEAMARAIHDHFRDK
The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision.
Q57E41
Q979Q5
SYP_THEVO
Prolyl-tRNA synthetase
Thermoplasma
MENKKENFSEWYNEIVTISDLSDKRYPIKGMNVWRPYGWKIMKLIDNIIRNAVDKHSFDEVNFPVLISRGMLEVEFEHIRGFENEIYWVTKGGKEKLEEELALRPTSESAMYPMFSLWVRSHADLPLKIYQIVSVYRYETKHTRSFIRIREIHFFEAHTAHESYEDAEKQMDEYRIIWTEIADALCLPFLYDQRPEWDKFPGAMYTIAFDTVMPSGRSLQIGTIHQYGTNFSKNYDIKYLKEDGTFEYVHQTTFGMSERLLAAIIGIHGDDKGLILPPAIAPIQVVIVPIPGEGVERYAKDIETTLNGIGIRCHVDNRDNYTPGYKYNDWEMRGVPLRIEVGERELKEKTVTLAARNIRGKKTVQREKLVYEVPDMLDLVKEKITEDAKKTFNSLVVSASSLDDFKKEGLIKAFWCGSKECSDKIENETEKSALGFNLNNDETGKCIVCGKAGKLAIFSRSY
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).
Q979Q5
Q39043
BIP2_ARATH
Luminal-binding protein 2
Arabidopsis
MARSFGANSTVVLAIIFFGCLFAFSTAKEEATKLGSVIGIDLGTTYSCVGVYKNGHVEIIANDQGNRITPSWVGFTDSERLIGEAAKNQAAVNPERTVFDVKRLIGRKFEDKEVQKDRKLVPYQIVNKDGKPYIQVKIKDGETKVFSPEEISAMILTKMKETAEAYLGKKIKDAVVTVPAYFNDAQRQATKDAGVIAGLNVARIINEPTAAAIAYGLDKKGGEKNILVFDLGGGTFDVSVLTIDNGVFEVLSTNGDTHLGGEDFDHRIMEYFIKLIKKKHQKDISKDNKALGKLRRECERAKRALSSQHQVRVEIESLFDGVDLSEPLTRARFEELNNDLFRKTMGPVKKAMDDAGLQKSQIDEIVLVGGSTRIPKVQQLLKDFFEGKEPNKGVNPDEAVAYGAAVQGGILSGEGGDETKDILLLDVAPLTLGIETVGGVMTKLIPRNTVIPTKKSQVFTTYQDQQTTVSIQVFEGERSLTKDCRLLGKFDLTGVPPAPRGTPQIEVTFEVDANGILNVKAEDKASGKSEKITITNEKGRLSQEEIDRMVKEAEEFAEEDKKVKEKIDARNALETYVYNMKNQVSDKDKLADKLEGDEKEKIEAATKEALEWLDENQNSEKEEYDEKLKEVEAVCNPIITAVYQRSGGAPGAGGESSTEEEDESHDEL
In cooperation with other chaperones, Hsp70s are key components that facilitate folding of de novo synthesized proteins, assist translocation of precursor proteins into organelles, and are responsible for degradation of damaged protein under stress conditions (Probable). Involved in polar nuclei fusion during female gametophyte development and is essential for the regulation of endosperm nuclei proliferation . Involved in sperm nuclear fusion with central cell polar nuclei at fertilization, which is critical for normal endosperm nuclear proliferation . Required for pollen development and pollen tube growth .
Q39043
G3XCZ8
PIGA_PSEAE
Heme oxygenase PigA
Pseudomonas
MDTLAPESTRQNLRSQRLNLLTNEPHQRLESLVKSKEPFASRDNFARFVAAQYLFQHDLEPLYRNEALARLFPGLASRARDDAARADLADLGHPVPEGDQSVREADLSLAEALGWLFVSEGSKLGAAFLFKKAAALELDENFGARHLAEPEGGRAQGWKSFVAILDGIELNEEEERLAAKGASDAFNRFGDLLERTFA
Involved in heme degradation. Catalyzes the degradation of heme to biliverdin, with the release of iron. Forms biliverdin delta (70%) and beta (30%).
G3XCZ8
B8QHP5
CP52N_STABO
Cytochrome P450 monooxygenase CYP52-N1
Starmerella
MILYAVLGAFAAFLLYMDVLYPFVIYPLRARWHKCGYIPRDLSWPLGIPLTLVVLSKLRKDMLLQFMAAQDLSRPYKTSLRQFLGKWVIATRDPENIKAVLSTKFNDFSLKERGNRMRHVIGDGIFTQDGAPWKHSRDMLRPQFTKDQISRVELLSHHIDVLIREIRKSGGNVELQRLFHLMTMDTATHFLFGESVGSLEVSGESKGIEITDPKTGEIVNTVDFVESYTFANKFALKKIILNDLEFLADLTEPSYKWHLRRVHTVMDHYVQLALKATEKYDPDDDSEKGEYYFSHELAKLTRDPLSLRDQLFNILIAGRDTTAATLSYAFHYLTKNPAIYAKVREDVLTVFPNGDASLATYEDLRKAKYLQMVIKEVLRLAPAVPLNTRAAVRDTYLPRGGGPAGNLPVFVPKGTAVNYPTYILHRDPDIYGADAYEFNPERWRPENKLPNSPMYSWGYIPFNGGPRICIGQQFALTEIALTMIKLVLEFERLEPADDFEPNLQDKSSLTVMVGGSGVRVKLS
Catalyzes the terminal (at the omega-position) hydroxylation of a fatty acid. Probably involved in alkane metabolism. Linoleic acid is the preferred substrate, but it acts on various other C-16, C-18 and C-20 saturated and unsaturated fatty acids, namely palmitic, palmitoleic, stearic, oleic, alpha-linoleic, arachidonic and myristic acid.
B8QHP5
P84047
H4_ASEAQ
Histone H4
Asellus
MTGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG
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.
P84047
Q820G1
CH10_STRAW
Chaperonin-10
Streptomyces
MTTASSKVAIKPLEDRIVVQPLDAEQTTASGLVIPDTAKEKPQEGVVLAVGPGRFEDGNRLPLDVTVGDVVLYSKYGGTEVKYNGEEYLVLSARDVLAIVEK
Together with the chaperonin GroEL, 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. GroES binds to the apical surface of the GroEL ring, thereby capping the opening of the GroEL channel.
Q820G1
Q0IC27
ISPF_SYNS3
2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
unclassified Synechococcus
MTSSVPSLRIGNGYDVHRLVPDRPLILGGQLLEHPAGLGLDGHSDADVLVHAIMDALLGALSLGDIGKYFPPSDPQWKGADSLVLLEQVVALVKARGWGVVNVDAVLIAERPKLKPHIEAMRSAIALRIGVAPDQVGVKATTNEQLGPEGREEGISCQAVALLQAL
Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP).
Q0IC27
Q7VQH1
CYSI_BLOFL
Sulfite reductase [NADPH] hemoprotein beta-component
Candidatus Blochmannia
MIMLKYNNKLLSDNERIKKNSNFLRGTIEKDLDNNLTGGFNVDNAQLIRFHGMYQQDDRDVRLERMNQKLEPLINMMLRCRLPGGVITSQQWLNIDNFSEEQTLYSSIRLTTRQTFQLHGILKPKLKGIHQLLNKLGLDSIATAGDVNRNVICTANPMESKVHYQIWELSKKISEHLLPKSKAYAEIWLNEKKIESIDSEPILSSVYLPRKFKIAIAVPPVNDVDVYANDLGLVAIKDNTGNLIGFNVLIGGGLAMTYGDKSTYPRMASEFGYINLQDILKIVESVITVQRDWGDRYNRRHAKTKYTLVKVGIDILKKEIENRSGLKFSPMYPYKFTERGDKFGWIRGINQDYWHLTLFIENGRVCNTSNILIKKGLSEIAKVHSGFFRITTNQNLIISEIHQDKKDIIEDLLKQYGLLGDFVTSQRKSSMACVAFPTCPLAMAEAERFLPAFVTKVEHVMSKYNLQRDAIILRVTGCPNGCARAMLAEIGLTGRGIGRYNLYLGGNKNGTRIPRLYKENITEDEILHVLDITIGDWAKNRKTQESYGDYVVRAGIVRAVINSEEDFYL
Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate.
Q7VQH1
Q313H2
DXR_OLEA2
2-C-methyl-D-erythritol 4-phosphate synthase
Oleidesulfovibrio
MNGYISPLPDAAWNSRFPRSLVLLGSTGSIGTSALRVVERQPELFRITALAGARNVRLLARQAAAYRPPHLAVINGNAADELASLLPAGYRPRIHTGQEGYEFLAALPEADCVLSAQVGAAGLRATVAAARAGKTIALANKESLVLAGGLIRRLCHETGASVLPVDSEHNAIFQALQGHDAAQMRRIILTASGGPFRGRDRTFLQSVTREQALNHPNWSMGAKISIDSATLMNKGLEVIEACHLYNAPLEKVEVVVHPQSIIHSLVEYNDGSQIAHMGTPDMRIAIAYCLGWPRVMHTGVEPLDLLSVGSLTFESPDISLFPCLELARKAYAGGNGLPVVLNAANEVAVDLFLQGAIAFLDIPRLIEAAMQAHDAAPHQNMYDEVESILTLDKTTRRVTADLAGARG
Catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).
Q313H2