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Full Name
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147
⌀
taxon
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46
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sequence
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2.75k
function
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5.51k
AlphaFoldDB
stringlengths
6
10
P07051
ROLC_NICGL
Protein ROL C
Nicotiana
MAEVDLCALFFNLRVKDVTSSDELKKHILSASDERNPLTEPGENQSMDVDEEGGTRDPGILYLYVDCPTMMQCFYGTSFPYNSRHGALLTNLPPYQKDVSLSEVSRGLRQASGFFGYEDPIRSAYFAALSFPGHVAKLDEQMELTSTNGESLTFDLYASDQLRLEPGAWVRHGECKFGMN
Hydrolyzes cytokinin glucosides thus liberating free cytokinins.
P07051
A6UWL8
ARGC_META3
N-acetyl-glutamate semialdehyde dehydrogenase
Methanococcus
MVTISIIGGTGYTGSELLRILLNHPQVEIKHITSRKMDGVNITKVHPNLKNIKNIDNLVFENISPSNLDSDFVFCATPHGASMKIVPELYETGSKIIDLSGDYRFEDLSLYEKWYNLTHTGELPAVYGLPELHRNEIKKAQLVANPGCFPTGSILALAPLVKEGIIENRIIVDSKTGVSGAGVNPSETTHYPSVNENILPYKMTTHRHSPEIEKELEKLNISNNIKLSFTPHLAPLTRGILSTTHSYLKNTDIDRDIIIDIYNEFYKNEPFVRIFEEGAPTLTGVRGSNFCDIGGFEIDRHGRIVVVSAIDNLVKGASGQAIHNLNLMAGFNETESLLYGGLKP
Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.
A6UWL8
Q7PS09
MTNB_ANOGA
Probable methylthioribulose-1-phosphate dehydratase
Anopheles
MASGRSSIYQDLSEEHPRKLIPELCKQFYNLGWVTGTGGGISIKLDDEIYIAPSGVQKERIQPDDLFIQNIEGDDLQTPPDYKKLTKSQCTPLFMLAYKERSAGAVIHTHSPAAVMTTLLWPGKEFRCTHLEMIKGIYDYELNRNLMYDEELVVPIIENTLFEKDLEESMANALRDYPGTSAILVRRHGVYVWGHNWQKAKTMAECYDYLFSLAVEMHKVGLDANAVPKRY
Catalyzes the dehydration of methylthioribulose-1-phosphate (MTRu-1-P) into 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P).
Q7PS09
Q9C8G9
AB1C_ARATH
Multidrug resistance-associated protein 1
Arabidopsis
MGFEPLDWYCKPVPNGVWTKTVDYAFGAYTPCAIDSFVLGISHLVLLILCLYRLWLITKDHKVDKFCLRSKWFSYFLALLAAYATAEPLFRLVMRISVLDLDGAGFPPYEAFMLVLEAFAWGSALVMTVVETKTYIHELRWYVRFAVIYALVGDMVLLNLVLSVKEYYGSFKLYLYISEVAVQVAFGTLLFVYFPNLDPYPGYTPVGTENSEDYEYEELPGGENICPERHANLFDSIFFSWLNPLMTLGSKRPLTEKDVWHLDTWDKTETLMRSFQKSWDKELEKPKPWLLRALNNSLGGRFWWGGFWKIGNDCSQFVGPLLLNELLKSMQLNEPAWIGYIYAISIFVGVVLGVLCEAQYFQNVMRVGYRLRSALIAAVFRKSLRLTNEGRKKFQTGKITNLMTTDAESLQQICQSLHTMWSAPFRIIVALVLLYQQLGVASIIGALFLVLMFPIQTVIISKTQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDELSWFRKAQLLSAFNMFILNSIPVLVTVVSFGVFSLLGGDLTPARAFTSLSLFSVLRFPLFMLPNIITQMVNANVSLNRLEEVLSTEERVLLPNPPIEPGQPAISIRNGYFSWDSKADRPTLSNINLDIPLGSLVAVVGSTGEGKTSLISAMLGELPARSDATVTLRGSVAYVPQVSWIFNATVRDNILFGAPFDQEKYERVIDVTALQHDLELLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVCILDDPLSALDAHVGQQVFEKCIKRELGQTTRVLVTNQLHFLSQVDKILLVHEGTVKEEGTYEELCHSGPLFQRLMENAGKVEDYSEENGEAEVDQTSVKPVENGNANNLQKDGIETKNSKEGNSVLVKREERETGVVSWKVLERYQNALGGAWVVMMLVICYVLTQVFRVSSSTWLSEWTDSGTPKTHGPLFYNIVYALLSFGQVSVTLINSYWLIMSSLYAAKKMHDAMLGSILRAPMVFFQTNPLGRIINRFAKDMGDIDRTVAVFVNMFMGSIAQLLSTVILIGIVSTLSLWAIMPLLVVFYGAYLYYQNTSREIKRMDSTTRSPVYAQFGEALNGLSSIRAYKAYDRMAEINGRSMDNNIRFTLVNMAANRWLGIRLEVLGGLMVWLTASLAVMQNGKAANQQAYASTMGLLLSYALSITSSLTAVLRLASLAENSLNSVERVGNYIEIPSEAPLVIENNRPPPGWPSSGSIKFEDVVLRYRPELPPVLHGVSFLISPMDKVGIVGRTGAGKSSLLNALFRIVELEKGRILIDECDIGRFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFSEHNDADLWESLERAHLKDTIRRNPLGLDAEVTEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDVLIQKTIREEFKSCTMLIIAHRLNTIIDCDKVLVLDSGKVQEFSSPENLLSNGESSFSKMVQSTGTANAEYLRSITLENKRTREANGDDSQPLEGQRKWQASSRWAAAAQFALAVSLTSSHNDLQSLEIEDDNSILKKTKDAVVTLRSVLEGKHDKEIEDSLNQSDISRERWWPSLYKMVEGLAVMSRLARNRMQHPDYNLEGKSFDWDNVEM
Pump for glutathione S-conjugates. Mediates the transport of S-(2,4-dinitrophenyl)-glutathione (DNP-GS), GSSG, cyanidin 3-glucoside-GS (C3G-GS) and metolachlor-GS (MOC-GS).
Q9C8G9
Q81G11
LEU3_BACCR
Beta-IPM dehydrogenase
Bacillus cereus group
MEKRIVCLAGDGVGPEVMESAKEVLHMVERLYGHHFHLQDEYFGGVAIDLTGQPLPQRTLAACLASDAVLLGAVGGPRWDSAKERPEKGLLALRKGLGVFANVRPVTVESATAHLSPLKNADEIDFVVVRELTGGIYFSYPKERTEEVATDTLTYHRHEIERIVSYAFQLANKRKKKVTSIDKANVLESSKLWRTVTEEVALRYPNVEVEHILVDAAAMELIRNPGRFDVIVTENLFGDILSDEASVLAGSLGMLPSASHAEKGPSLYEPIHGSAPDIAGKNKANPIAMMRSVAMMLGQSFGLTREGYAIEEAVSAVLKSGKCTADIGGTETTTSFTKAVIQEMEEQALVGRGR
Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate.
Q81G11
Q4L890
RS13_STAHJ
30S ribosomal protein S13
Staphylococcus
MARIAGVDIPREKRIVISLTYVYGIGTSTAKKIVEEANVSADTRVKDLTDDELGRIREVVDSYKVEGDLRREQNLNIKRLMEISSYRGIRHRRGLPVRGQKTKNNARTRKGPVKTVANKKK
Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA. In the 70S ribosome it contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit (bridge B1b), connecting the 2 subunits; these bridges are implicated in subunit movement. Contacts the tRNAs in the A and P-sites.
Q4L890
Q8RPZ9
RL20_AZOVI
50S ribosomal protein L20
Azotobacter
MARVKRGVIARRRHKKILKLAKGYYGARSRVFRVAKQAVIKAGQYAYRDRRQRKRQFRALWIARINAGDRQNGLSYSRLIAGLKKATIEIDRKVLSDLAVNEKAAFAAIVEKAKAVLA
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.
Q8RPZ9
A8GV67
DNAJ_RICB8
Chaperone protein DnaJ
belli group
MSQDYYQILGVSKTANSADLKKAYHKLAKQYHPDNAAAGDTNAEKKFKEINAAYEVLKDEQKRAAYDRFGHDAFQNQQARGGAGSQGGHPFGADINDIFGDFFSDFMGGGGRRKPTSSKVRGSDLKYNLTINLEEAFHGVEKNISFSSEVKCDTCHGSGSEKGETTTTCDACGGVGATRVQQGFFMIEQTCHKCQGNGQIIKNPCKKCHGLGRYHKQRNLSVNIPAGVENGTRIRHPGEGEAGIRGGNNGDLYVDIAIKPHDIYKVDGANLHCKLPISFVNAALGGEVAVPVIEGGKVNLTIPAGTQNGDQLRLCGKGMSKIRSTIRGDMLAHVHVEVPKNLSKRQRELLEELRGESANEKENDGSFFNKMKSLWS
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.
A8GV67
P02674
FIBA1_PETMA
Fibrinogen alpha-1 chain
Petromyzon
QVCIADDISLRGPRLTEQRSAGQGSCASATADLCVHGDWGRKCPNGCRMQGLMSHAEKDIGKRIGDLTERLARLGRLYTQVHTDFRAVSDTSGQTLNEHNELEVRYSEVLRELERRIIHLQRRINMQLQQLTLLQHNIKTQVSQILRVEVDIDVALRTCKGSCARYLEYRLDKEKNLQLEKAASYIANLKFERFEEVVVEETLNRRVETSSHAFQPTHGQGTPQPGHGTHSLSATSSITSAPNFVPHRQPTYVDHGRLSNPNEVAHSASSSSTHTSSSSSPSQPVSRDSAFPLPGSNTGTSEWDFNFHDESTPGNGPRDEAAASSSAHSPSTASHDTATSTTSFSSGTSGKDVAPLGTGVTHDGGVRTSGSLMDGGSSDTGTGGVSKTTTFTGSAQGGSWSTGGSTATNTGSAQGGSWSTGGRTEPNTGSGQGGSWGTGGRTEPNTGSGQGGSWGTGGRTEPNTGSGQGGSWGTGGRTEPNTGSAQGGSWGTGGRTEPNTGSAQGGSWGTGGRTEPNTGSAQGGSWSTGGRTEPNTGSAKGGSWGTGGRTEPNTGSAKGGSWSTGGRTEPNTGSAKGGSWGTGGRTEPNTGSAQGGSWGTGGRTEPNTGSAQGGSWGTGGRTEPNTGSAQGGSWGTGGRTEPNTGSAQGGSWGTGGRTEPNTGSAQGGSWSTGGRTEPNTGSGQGGSWGTGGRTEPNTGSGQGGSWSTGGRTEPNTGSGQGGSWGTGGRTEPNTGSAQGGSWGTGGRTEPNTGSAQGGSWGTGGSTATNTGSAQGGGGYAAGGTGAQTGSGSTSTHSAHSASGGMSSLDMLPALPDFGTWDMPDHSDIFSRRRVSTSSTTSSSSGGGHAGAAAGGGGDGASRFGSLFTTDFGPEFHEEFRSMLPGASRLSSSSSSSTRSTSSTSGGKVVTESVVTKVLSNGTTITHHTKHVSTSDGTGAASDGVSPLLTGRKTKAARSRRAKATRP
Fibrinogen has a double function: yielding monomers that polymerize into fibrin and acting as a cofactor in platelet aggregation.
P02674
Q9DC70
NDUS7_MOUSE
NADH-ubiquinone oxidoreductase 20 kDa subunit
Mus
MAALAAPGLLSVRILGLRTAQVQLRRVHQSVATEGPSPSPSPSLSSTQSAVSKAGAGAVVPKLSHLPRSRAEYVVTKLDDLINWARRSSLWPMTFGLACCAVEMMHMAAPRYDMDRFGVVFRASPRQADVMIVAGTLTNKMAPALRKVYDQMPEPRYVVSMGSCANGGGYYHYSYSVVRGCDRIVPVDIYVPGCPPTAEALLYGILQLQRKIKREQKLKIWYRR
Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity of complex I.
Q9DC70
A1R037
CHED_BORT9
Probable chemoreceptor glutamine deamidase CheD
Borrelia
MLNHFNFKLKRDVTIIVPGEAFVSNDRVISTILGSCVSVVLYDGVRRLIGVNHYVLVKSDSVVDVLQKGRYGVYAIPMLIDAMIENGASKSNLKAKLFGGANFMAKGTIRVGVENSEFAVNSLTKYGIPVVAQDFDQSKSRKIFVFPENFKVVVEYPDGAKIF
Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis.
A1R037
B2S007
HSLV_BORHD
ATP-dependent protease subunit HslV
Borrelia
MSFKGTTVIAIRRGGKTAVAADGQVTFGYTVLKSNAVKIRKLVNGRILAGFAGSTSDAITLFEKFEEKVKAREDGIIDIKRAAVELAKDWRSDKILHKLEAMMLVADSENILLISGTGDVVEPEEDVISIGSGGNYAYSAALAYMENKKLSAADIAFKSLKVAAKVCIYTNSNIVLEEIS
Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
B2S007
P51503
ZNF80_GORGO
Zinc finger protein 80
Gorilla
MSPKGDGLGTVDGLHSQVLQEQVSTGDNLHECDSQGPSKDTLVREGKTYKCKECGKVFNKNSLLVRHHQIHAGVKTYECQECGKAFHEKVDFVRHMRIHSGEKPCKCVECGKVFNRRSHLLCYRQIHTGEKPYECSECGKTFSYHSVFIQHRMTHTGEKLFGCKECGKTFYYNSSLTRHMKIHTGEKPYKCGECGKTFTYHSVFFRHSMTHTAGKPYECKECGKGFYYSYSLTRHTRSHTGEKPYECLEHRKAFGYHSAFAQQSKIHSGGKNL
May be involved in transcriptional regulation.
P51503
Q88YZ4
FABH1_LACPL
3-oxoacyl-[acyl-carrier-protein] synthase III 1
Lactiplantibacillus
MPTYTKLTAMGQYVPGRVVDNDELAAIMDTSDEWIQAHTGIKTRHYAMNDENTSDLATQVAQQLLQKSGLAASAIDLILVTTITPDALTPATACLVQANIGADNAFAFDLSAACAGFTFGLATADKFIRSGQYQNVMVISAEVNSKMMDFQDRTAAVFFGDGAGGALLQATDNPDENSLIAEKLESQGNATVIHSGRVRPITEVAATNYPQTDAFYQVGRDVFQFATTVVPEQMRGLIASAQLTPSDLQYVICHQANLRIIEKIAANLALPMTKFPHNVDHYGNTSSAGVAMALANVFDTLTGPVLLTAFGGGLAYGSVLIKK
Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids.
Q88YZ4
Q8U0C0
LEUC2_PYRFU
Isopropylmalate isomerase 2
Pyrococcus
MTLIEEILGGKSGESVVRRVDLVYAHDGTMPLIIEAFNKVFATVRARAYIFFDHVYPAPTVKIANLQKEIRDFAKRHRIPVIEGQGISHQLVVEMGLTENSKIVVGADSHTPTLGALGVFAVGMGATDVAVILGLGKTWFRIPESVGVILEGNPSRYVMATDVILHLLSLLKDYDMNYRAVEFFNVPFSLDERLTLTNFVVEANAKTGIIGEEYTGDGYVKELEIELNSLNPLVAKPHNPANVVPVEEVEGTKIDQVFIGSCTNGRFEQISKAAEILEGEKVAVRTIVGPASMNVYKRMIEEGVARKLIEAGAVILPPGCGPCLGRHMGVVGDGEIVLSTTNRNFRGRMGSPNAQIYLSNPITAAVSALYGEITNPEGAI
Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
Q8U0C0
Q1KVX6
CHLN_TETOB
Light-independent protochlorophyllide reductase subunit N
Tetradesmus
MTILLEEKEKLTFECETGNYHTFCPISCVSWLYQKIEDSFFLVIGTKTCGYFLQNALGVMIFAEPRYAMAELEESDISAKLNDYKELKRLCFQIKEDRNPSVIVWIGTCTTEIIKMDLEGMAPELERELGIPIVVARANGLDYAFTQGEDTVLAAMAQRCPSLPLNVEEKSQNSLFNQSSNSPENLKTLNTKKDTFQNSTENSKTFSAEKKKTQNPFEFFKSLEEFFPSFSIQNNKKETILSKNSFVPFVEVEKNMYPLESSENSKAESFYHLLREGEQTNQNSELVKPKLVLFGSLPNTVATQLKLELNRQGIEISGWLPSTRYSDLPILDTNTYVCGVNPFLSRTATTLMRRRKCKLISAPFPIGPDGTKAWIEKICSIYGKKPIGLEERETKIWEGLEDSLKLVRGKSVFFMGDNLLEISLARFLIRCGMIVYEIGIPYLDQRFQAAELALLEKTCFEMNVPVPRIVEKPDNYYQISRIRELQPDLVITGMAHANPLEARNITTKWSVEFTFAQIHGFTNAREILDLVTRPLRRNQNINSFSEFFGSTTSTFVQNQF
Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (ChlN-ChlB) is the catalytic component of the complex.
Q1KVX6
C1C8T6
ALR_STRP7
Alanine racemase
Streptococcus
MKASPHRPTKALIHLGAIRQNIQQMGAHIPQGTLKWAVVKANAYGHGAVAVAKAIQDDVDGFCVSNIDEAIELRQAGLSKPILILGVSEIEAVALAKEYDFTLTVAGLEWIQALLDKEVDLTGLTVHLKIDSGMGRIGFREVSEVEQAQDLLQKHGVCVEGIFTHFATADEESDDYFNAQLERFKTILASMKEVPELVHASNSATTLWHVETIFNAVRMGDAMYGLNPSGAVLDLPYDLIPALTLESALVHVKTVPAGACMGYGATYQADSEQVIATVPIGYADGWTRDMQNFSVLVDGQACPIVGRVSMDQITIRLPKLYPLGTKVTLIGSNGDKEITATQVATYRVTINYEVVCLLSDRIPREYY
Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids.
C1C8T6
Q2L008
PIMT_BORA1
Protein-beta-aspartate methyltransferase
Bordetella
MRKPVGSKDGSGVYSRQGLDGYTPANSNTRISTATLPRPEPLRPAASSANLGLNSDRLRLAMVQRLRQMGITDDRVLDAMAAVPRHTFVDEALASRAYEDAALPIGHSQTISQPWVVARMIAAVCEARAPSRVLEVGAGCGYQAAVLAQFVREVHSIERIRGLYELARANLRALRLSTRVRLIYGDGTQGVPGVAPFDAIVVAAAGLAIPQALLNQLAPGGRLIAPEGSTSQRLVLIERTGTASWKRMELEAVRFVPLKAGIQS
Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins.
Q2L008
A8G9L4
SYI_SERP5
Isoleucyl-tRNA synthetase
Serratia
MSDYKNTLNLPETGFPMRGDLAKREPGMLQRWYEQDLYGMIRTAKKGKKSFILHDGPPYANGSIHIGHSVNKILKDIIIKSKGMSGFDSPYIPGWDCHGLPIELKVEQLYGKPGEKLTAAEFRIKCREYAAEQVEGQKKDFIRLGVLGDWDRPYLTMDFKTEANIIRALGKIISNGHLLKGAKPVHWCTDCRSSLAEAEVEYYDKTSPSIDVAFHAVDAAAVATKFGVTRFNGPVSLVIWTTTPWTLPANRAISLHPEFAYQLVQVEGQCLILAAELVESVMKRAGITHWEVLGSCKGADLELMRFEHPFMGFDVPAIMGEHVTLDAGTGAVHTAGGHGPDDFVISQKYGLEIANPVGPNGCYLTGTHPLLDGKFVFKANDLIVDLLREKDALLHVEKLVHSYPCCWRHKTPIIFRATPQWFISMDQKGLRKQSLEEIKGVQWIPEWGQARIETMVANRPDWCISRQRTWGVPMSLFVHKDTEQLHPRSVELMEEVAKRVEQDGIQAWWDLDAADILGADAADYVKVPDTLDVWFDSGSTHSSVVDVRPEFNGHGADMYLEGSDQHRGWFMSSLMISTAMKGKAPYKEVLTHGFTVDGQGRKMSKSIGNTISPQDVMNKLGGDILRLWVASTDYTGEIAVSDEILKRSADSYRRIRNTARFLLANLNGFEPSTDCVAPEEMVVLDRWAVGRALAAQQDIEKAYANYDFHEVVQRLMQFCSVEMGSFYLDIIKDRQYTAKSDSVARRSCQTALFHIAEALVRWMAPIMSFTADEIWAFLPGKRAQYVFTEEWYDGLFGLAEGEGMNDSFWAELLKVRGEVNKVLEQARADKRLGGSLEAAVTLYADSELAERLNSLQDELRFVLLTSGARVAPLADAPADAQAAELVKGLKIAFSTAEGEKCPRCWHYTTDIGLVAEHADLCGRCVVNVAGDGEKRKFA
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).
A8G9L4
Q29118
CSF2_PIG
Colony-stimulating factor
Sus
MWLQNLLLLGTVVCSISAPTRPPSPVTRPWQHVDAIKEALSLLNNSNDTAAVMNETVDVVCEMFDPQEPTCVQTRLNLYKQGLRGSLTRLKSPLTLLAKHYEQHCPLTEETSCETQSITFKSFKDSLNKFLFTIPFDCWGPVKK
Cytokine that stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes.
Q29118
Q8MCP4
MATK_MELID
Intron maturase
Melilotus
MKEYQVYLERARSRQQDFLYPLIFREYIYGLAYSQNFNRSIFVENLGYDNKYSLLIVKRLITRMYQQNHLIISANDSNKNPFLGYNKNFYSQIISEGFAIVVEIPFFLELSSSLEEPEIIKSYKNVRSIHSIFPFLEDKLTHLNYVSDIRIPYPIHLEILVQILRYWVKDAPFFHLLRLFLYNFCNWNSFITTKKSISTFSKSNPRLFLFLYHFYVCEYESIFLFLRNKSSHLRLKSFSVFFERIFFYAKREHLVEVFAKDFSYTLTFFKDPLIHYVRYQGKCILASKNAPFLMNKWKHYFIHLWQGFFDVWSQPRTININQLSEHSFQLLGYFLNVRLNRSVVRSQMLQNTFLIEIVSKKLDIIVPIIPLIRSLAKAKFCNVLGHPISKPVWADSSDFDIIDRFLRICRNLSHYYNGSSKKKSLYQIKYILRLSCIKTLACKHKSTVRAFLKRSGSEELLEAFFTEEEEILSLIFPRDSSTLHRLNRNRIWYLDILFSNDLVNDE
Usually encoded in the trnK tRNA gene intron. Probably assists in splicing its own and other chloroplast group II introns.
Q8MCP4
Q9WXZ6
PLSX_THEMA
Phosphate-acyl-ACP acyltransferase
Thermotoga
MKIAIDVMGGDRAPDEILKGALLASKEVEGEIVLIGPEEIVKNKGLPFVSASEIVKMDDPPLEVLRKKNSSMHMGLKLLSEGKVDAFVSAGATGPLFLGATSIVGKLEGIERPALGVAVPSLKGATVLIDAGANAKVRPEHLVDFAFMGIAYSKVLGAENPRVGLLNMGSEENKGPDDIKRAYQLLKEFLGDTFFGNVEGHDINLGTVDVVVADGFSGNVALKTMEGTAKLVTSVLKESIKDGGFLSLLGALLMKRSFDKMKEKLDPRSYGGTFILGVKGIVVKAHGSSDAKAIKHAIKVAEKGIRVNIVQEIERGISHVRNSGDGR
Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
Q9WXZ6
P0DJG6
VSP_CROVV
Snake venom serine protease
Crotalus
VIGGDECNINEHRFLVALYDPDGFLSGGIL
Snake venom serine protease that catalyzes the hydrolysis of arginine esters, kallikrein substrates Pro-Phe-Arg-MCA and Z-Phe-Arg-MCA. Cleaves kininogen analogs to release bradykinin. Induces contraction of the isolated rat uterus directly at high concentrations, but provokes more forceful contractions when injected in presence of bovine plasma. Shows capillary permeability-increasing activity and hypotensive activity on the anesthetized rat.
P0DJG6
Q12PB3
RECR_SHEDO
Recombination protein RecR
Shewanella
MKFSPLVDELIQALKGLPGVGPKSAQRMAFNLLERDRKVGLKLAESLKNAMTDVGHCQSCRTFTEQSLCPICASHKRGASGVICVVETPADVLAIEAGGHFNGRYFVLLGHLSPLDGVGPEELGLSLLEQHLQTLDVTELILATNPTVEGDATAHFIADMARRHKVIISRIAHGVPVGGELEYVDSTTLALSFNGRIAL
May play a role in DNA repair. It seems to be involved in an RecBC-independent recombinational process of DNA repair. It may act with RecF and RecO.
Q12PB3
H6VC06
VKTK2_DABRR
Daboia russelii Kunitz Inhibitor-II
Daboia
MSSGGLLLLLGLLTLWAELTPISGHDRPTFCNLAPESGRCRAHLRRIYYNLESNKCEVFFYGGCGGNDNNFSTWDECRHTCVGK
Serine protease inhibitor that inhibits plasmin (90%) (Ki=0.19 nM), trypsin (70%), FXIa/F11 (37%) (Ki=6 nM) and FXa/F10 (20%), and prolonges the activated partial thromboplastin time. This antifibrinolytic property has been confirmed by a fibrin plate assay. Shows less antifibrinolytic activity that aprotinin. In vivo, reduces the bleeding time in a murine bleeding model, and prevents the increase of fibrin(ogen) degradation products in coagulation-stimulated mice.
H6VC06
B2KAT6
YBEY_ELUMP
Endoribonuclease YbeY
Elusimicrobium
MIINVFYKTKVPSHFRKTSLFKAGVSAALGKFASKKGEVNLIFVDGKEIHKINKEFLNHDYKTDVISFNYPFPQKGGEGLPFGDIFVCYDVAKENASLYGQGVLKEMLTYAVHGALHLAGMDDATPKERSAMDDETGRIILKI
Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
B2KAT6
A3MYI9
BIOB_ACTP2
Biotin synthase
Actinobacillus
MTTYNLRLKAKSELTPHPTAQYWRKCQVEELFEMPFMELIFKAAQVHREHFDPQAIQLSTLLSIKTGGCPEECEYCPQSARYDTGLEKQVMMDVEEIVEKAKIAKARGASRFCMGAAWRGPKPKDIKVVSEIIGAVKALGLETCGTFGLLEDGMAEDLKQAGLDYYNHNLDTDPERYNKIVHTRNHDDRMDTLGKVRHAGLKVCCGGIVGMNETRPERAGLIASLANLDPQPESVPINQLIKVEGTPLENAEDLDWTEFVRTIAVARITMPKSYVRLSAGRTSMPEAMQTLCFMAGANSIFYGEKLLTTCNPEEDSDRLLMDKLDLYPLAYEPSDA
Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.
A3MYI9
A1KBU9
MURB_AZOSB
UDP-N-acetylmuramate dehydrogenase
Azoarcus
MNIAPPLAITTDADLGPLNTFGLPARAARLLRVRGEEDVRALLAEPGWRGEPRLVLGGGSNLVLRGDFAGTVLKVEIAGRRLVGVREDADGAAWIVEAGAGECWHDFVRWTLAQGWPGLENLSLIPGTVGAAPIQNIGAYGVELTERFDALDAIDLDSGETRSFDRTTCAFGYRDSVFKRAAGRWLVLRVRFRLPQAWAPVGRYADVAAELAARGIAAPGAADISDAVIAIRRRKLPDPAKIGNAGSFFKNPVVDAAAWARLAAAHPEAPHYPQRDGSIKLAAGWLIEQAGWKGRNLGPVGCYERQALVLVNRGGACGEDVARLAAAIQADVEARFGIRLEPEPVFV
Cell wall formation.
A1KBU9
O34707
YTPB_BACSU
Tetraprenyl-beta-curcumene synthase
Bacillus
MTVPEHPFGLMAKVYRDIFPLVHQELDIWKQKSESIHNSELKAQATASIRDKTFHCEGGGILALLSGSQKQKCVEFIIAYQTISDYLDNLCDRSTSLDPQDFRMLHASMQDALTVGAELQNYYQFREEQDDSGYLHELVKTCQRVLGSIEHYDMIKPYLLELCGYYCDLQVHKHVIEHERVPRLEKWFTQYESELPEMEWYEFSACAGSTLGIFCLVAYSFQPDFTESTAKKIRDSYFPYIQGLHILLDYLIDQEEDLLEGDLNFCSYYQSHEEMMDRLEHFIHKADEHLQGIPHENFHRLINRGLLGVYLSDDKVAGQKEMGRLAKKLIKASGKTSLFFYINGRAYRKFQKMSWMKNSKKKAQIIC
Catalyzes the transformation of a linear C35 prenyl diphosphate chain to form tetraprenyl-beta-curcumene.
O34707
Q4UMZ0
QUEC_RICFE
Queuosine biosynthesis protein QueC
spotted fever group
MKKAVILVSGGADSATVLAIAREMGYEIHAMSFNYGQRNNAELRKVKELIKEYNVKQHKIVYIDLRAFGGSALTDNNIDVPHYHDVNELPEDVPVTYVPARNTIFLSYALGYAEVIGAKDIFIGVHTSDSANYPDCRPEYIKSFEEMANLATNIGNRITIHTPLIDMAKEQIIKTGLELGVDYKNTISCYDPTEDDLSCGNCLACMIRLDAFKKNNVQDPINYV
Catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)).
Q4UMZ0
P0CY82
CA427_CONBU
Kappa-conotoxin-like Bu27
Textilia
ASDGRNAVVHERAPELVVTATTTCCGYDPMTICPPCMCTHSCPPKRKPGRRND
Kappa-conotoxins bind and inhibit voltage-gated potassium channels.
P0CY82
A3QET2
GLO2_SHELP
Glyoxalase II
Shewanella
MHTVTPIPAFNDNYIWLIHAKDSGGHYVVDPGDAKAVLDYLEQHQIVLDGILITHHHSDHTGGIAELQASHDHKLTVYGPDNENIKGINHPISGQTESVKPEKLDSDAAVFHLPGHTLGHIAYLIDDHLFCGDTLFSAGCGRLFEGTPAQMHHSLQTLAQLDETTLVYPAHEYTQANLAFALTVENDNEALIAHAAKVKQLRDQNLPSLPSSIGLEKQINPFLRPEQASIKQNLSCHFAQDVTDDGTSFTLLRQWKDNFL
Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
A3QET2
B1G898
APIBP_PARG4
D-apiose binding SBP
Paraburkholderia
MKASKRWVALAAATLTLFTATGTAQAANLIAIITPSHDNPFFKAEADTANARAKALGYDTIVLVHDDDANKQSNLVDTAIARGAKAIILDNAGSEASISAVRKAKAAGIPSFLIDREINATGIAVSQIVSNNYQGAQLGGRAFVKALGEKGNYVELVGREADINAGIRSKGYHDVIDQFPNMKMVERQSANWSQTEAYRVMETILQSHPDVKGVIAGNDTMAMGASAALKAAKRSDVIVVGFDGSNDVRDAIMRNDIRATVLQPAALAATEAVEQADKYMKTGSTGKPEKQLINCSLITKANAGKLDMFALR
Part of an ABC transporter complex involved in D-apiose import (Probable). Binds D-apiose, D-ribose and D-ribulose .
B1G898
C5Y8Z8
GATA_SORBI
Glutamyl-tRNA(Gln) amidotransferase subunit A, chloroplastic/mitochondrial
Sorghum
MPPPLQAHRLLISHRRLPSPARRRFTAASSLQSAPATTLAPGPATSSILSIRESLLSGERTAADITSEYLSRLRRTEPSLRSFIHVADAAAEREAEELDRRIASGEKDAVGPLAGVLVGVKDNLCTANMPSTGGSRILDGYRPAYDATAVRRLQEAGAIVVGKTNLDEFGMGSTTEGSAFQVTTNPWDDSRVPGGSSGGSASAVSARQCVVSLGSDTGGSVRQPASFCGVVGLKPTYGRVSRFGLMAYASSLDVVGCFGSSVFDTATILSVVAGHDKMDSTSSSQVVPDYASELVSLDLLESKPLAGLRIGIIQETLGEGVANGVISSIKGAASHLEQLGSVVEEVSLPSFSLGLPAYYILASSEASSNLSRYDGIRYGRQFSADDLNELYGESRANGLGHEVKMRILMGTYALSAGYYDAYYKRAQQVRTLVKESFKDALERYDILISPAAPSAAYKIGEKINDPLAMYAGDILTVNVNLAGLPALVVPCGFVEGGPAGLPVGLQLIGSPFCEGNLLRVGHIFEQTLQNLSFVPPLLAES
Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in chloroplasts and mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
C5Y8Z8
A1S3W9
NHAA_SHEAM
Sodium/proton antiporter NhaA
Shewanella
MEKAIRNFLSQESAGGILLLVAVALAMLLANSPLSGLYQGFLNTEMQVRFGALDINKPLLLWINDGLMALFFLLIGLEVKRELLEGALSSPSKASLPTFAAIGGMLVPAAIYLFFNFDDPVTKVGWAIPAATDIAFALGIMALLGNRVPVALKVFLLALAIIDDLGVIVIIALFYSTDLSMLSLVIAAIAVTGLVALNRKGVTSLAPYGVLGIILWIAVLKSGVHATLAGVVIAFCIPLRAKDGSSPSEHLEHSLHPWSNFLILPVFAFANAGVPLGNVGFDSILSPVPVGIALGLLLGKPIGVLLFSYAAVKLRLAELPKGIGWHQIAPVAVMCGIGFTMSMFIASLAFEHGGELYGDLARIGILLGSLFAAVIGYFWLSKVLPKAGERI
Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons.
A1S3W9
P9WKI5
Y3410_MYCTU
Uncharacterized oxidoreductase Rv3410c
Mycobacterium tuberculosis complex
MVEIGMGRTARRTYELSEISIVPSRRTRSSKDVSTAWQLDAYRFEIPVVAHPTDALVSPEFAIELGRLGGLGVLNGEGLIGRHLDVEAKIAQLLEAAAADPEPSTAIRLLQELHAAPLNPDLLGAAVARIREAGVTTAVRVSPQNAQWLTPVLVAAGIDLLVIQGTIVSAERVASDGEPLNLKTFISELDIPVVAGGVLDHRTALHLMRTGAAGVIVGYGSTQGVTTTDEVLGISVPMATAIADAAAARRDYLDETGGRYVHVLADGDIHTSGELAKAIACGADAVVLGTPLAESAEALGEGWFWPAAAAHPSLPRGALLQIAVGERPPLARVLGGPSDDPFGGLNLVGGLRRSMAKAGYCDLKEFQKVGLTVGG
Has no inosine-5'-monophosphate dehydrogenase activity.
P9WKI5
P18208
GLBM_TYLHE
Giant extracellular hemoglobin linker 2 chain
Tylorrhynchus
DDCVCPGGREWASVASKADSQEARVNRLAGRVEALAENLRAGGDRLSHYKSEFRELEFRVDELEGNGCEPRHFQCGGSAMECISDLLTCDGSPDCANGADEDSDVCHIPPIAGTLLVGHLNTDHDFCTKRKPNEFDLFISSVQRSSYFQSRLKVKGNLQIKYTAEGRDQEDVLQVKGYYNFGTHQLVILPPEDDRLGIVCNFRAGNDDRCRAHIVHEASLEHCGDDFVFVKEDDHH
Acts as a linker for the assembly of heme-containing chains in the construction of giant hemoglobin.
P18208
P47627
ERA_MYCGE
GTPase Era
Mycoplasma
MKVLKVGVLGPTNAGKSTLINFLHNDDSLMVSSMNNTTLLSISTEVINQANKNIVFIDVPGFTEKKHSNYELITKEIRKALSGIDVLLLVVRSDQNNKIEFLKTQLQQLKRYQNLTRIFLINKFHQKSLSEVNKAIILEEFKPQKTIEINLLKFDKNLFWSIFKQVELRYNIFRKDINFIDANNDDFKILEGLREQIIFYCKNEIPHIARIEIIEKSFNKEKNLLKIHLVISVPKLSQKKIIIGKNAEMIKAIGIATRKKLLNHFDCDIFIDIFVKTEKQKLPVYSFLSK
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.
P47627
P81413
CDC6_PYRFU
ORC1-type DNA replication protein
Pyrococcus
MNEGEHQIKLDELFEKLLRARKIFKNKDVLRHSYTPKDLPHRHEQIETLAQILVPVLRGETPSNIFVYGKTGTGKTVTVKFVTEELKRISEKYNIPVDVIYINCEIVDTHYRVLANIVNYFKDETGIEVPMVGWPTDEVYAKLKQVIDMKERFVIIVLDEIDKLVKKSGDEVLYSLTRINTELKRAKVSVIGISNDLKFKEYLDPRVLSSLSEEEVVFPPYDANQLRDILTQRAEEAFYPGVLDEGVIPLCAALAAREHGDARKALDLLRVAGEIAEREGASKVTEKHVWKAQEKIEQDMMEEVIKTLPLQSKVLLYAIVLLDENGDLPANTGDVYAVYRELCEYIDLEPLTQRRISDLINELDMLGIINAKVVSKGRYGRTKEIRLNVTSYKIRNVLRYDYSIQPLLTISLKSEQRRLI
Involved in regulation of DNA replication. May play essential roles in origin recognition and cell cycle control of replication. Binds specifically to the oriC region, which alters the topological structure of the DNA and introduces localized melting of the DNA duplex. May recruit the MCM helicase onto the oriC region. Shows weak ATPase activity in the absence of DNA.
P81413
Q7VQC9
RL15_BLOFL
50S ribosomal protein L15
Candidatus Blochmannia
MFSLNTIAPALGAKRVGKRVARGIGSGFGKTAGRGHKGQKSRSGCKIKVSFEGGQTPLHRRLPKFGFKSRKSIVTQEITLFDLSRIPENVIDLNVLKKYDIVSRKIRFVKIIMSGTFDKPVIIRNLRISKGARDLIKSVGGRIEEGE
Binds to the 23S rRNA.
Q7VQC9
Q05A36
MEX3C_MOUSE
RING-type E3 ubiquitin transferase MEX3C
Mus
MPSGSSAALALALAAAPAPLPQPPPLPPPPPAGGPELEGDGLLLRERLAALGLDDPSPAEPGAPALRAAAVAAAAAAQCQARRATGLAPEEPGRLATSETAELELEVDEEEGEEAELDGELLEEEELEEAEEEDRPSLLLLSPPAATASQTQPIPGGPLGSVLLPAAGFDAREAAAAGVLYGGDDAQGMMAAMLSHAYGPGGGGAAAAALNGEQAALLRRKSVNTTECVPVPSSEHVAEIVGRQGCKIKALRAKTNTYIKTPVRGEEPIFVVTGRKEDVAMAKREILSAAEHFSMIRASRNKNGPALGGLSCSPNLPGQTTVQVRVPYRVVGLVVGPKGATIKRIQQQTHTYIVTPSRDKEPVFEVTGMPENVDRAREEIEMHIAMRTGNYIELNEENDFHYNGTDVSFEGGTLGSAWLSSNPVPPSRARMMSNYRNDSSSSLGSGSTDSYFGSNRLADFSPTSPFSTGNFWFGDTLPSVGSEDLTVDSPAFDSLPTSAQTIWTPFEPVNPLSGFGSDPSGNMKTQRRGSQPSTPRLSPTFPESIEHPLARRVRSDPPSTGNHVGLPIYIPAFSNGTNSYSSSNGGSTSSSPPESRRKHDCVICFENEVIAALVPCGHNLFCMECANKICEKRTPSCPVCQTAVTQAIQIHS
RNA-binding protein. May be involved in post-transcriptional regulatory mechanisms, modulating levels of some mRNAs by promoting their degradation in a way involving ubiquitin ligase activity. May act as suppressor of replication stress and chromosome missegregation.
Q05A36
A8Z332
RS11_STAAT
30S ribosomal protein S11
Staphylococcus
MARKQVSRKRRVKKNIENGVAHIRSTFNNTIVTITDEFGNALSWSSAGALGFKGSKKSTPFAAQMASETASKSAMEHGLKTVEVTVKGPGPGRESAIRALQSAGLEVTAIRDVTPVPHNGCRPPKRRRV
Located on the platform of the 30S subunit, it bridges several disparate RNA helices of the 16S rRNA. Forms part of the Shine-Dalgarno cleft in the 70S ribosome.
A8Z332
B4SRY3
PANB_STRM5
Ketopantoate hydroxymethyltransferase
Stenotrophomonas maltophilia group
MSTHADSKPWTVPALAEAKRNGQKLVMLTAYDAGFARTFDANGVDLILIGDSLGMVVQGHDSTLPVTVADMVYHTRAVARVLQRALLVADLPFGADATPERALDASLQLLQAGAEMVKIEGAGFKVDIIRYLVEREIPVCAHLGLTPQSVLRLGGFKIQGRGDAARQLVEDARAVAAAGASIMVLECVPTPVAAEVTAAVDVPTIGIGAGPQCDGQVLVLHDFLGLDSGHRRPKFVKDFLAEGGSVAGATRAYADAVRDGSFPDEQHAYAQ
Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
B4SRY3
P10477
CELE_ACET2
CtCE2
Acetivibrio
MKKIVSLVCVLVMLVSILGSFSVVAASPVKGFQVSGTKLLDASGNELVMRGMRDISAIDLVKEIKIGWNLGNTLDAPTETAWGNPRTTKAMIEKVREMGFNAVRVPVTWDTHIGPAPDYKIDEAWLNRVEEVVNYVLDCGMYAIINVHHDNTWIIPTYANEQRSKEKLVKVWEQIATRFKDYDDHLLFETMNEPREVGSPMEWMGGTYENRDVINRFNLAVVNTIRASGGNNDKRFILVPTNAATGLDVALNDLVIPNNDSRVIVSIHAYSPYFFAMDVNGTSYWGSDYDKASLTSELDAIYNRFVKNGRAVIIGEFGTIDKNNLSSRVAHAEHYAREAVSRGIAVFWWDNGYYNPGDAETYALLNRKTLSWYYPEIVQALMRGAGVEPLVSPTPTPTLMPTPSPTVTANILYGDVNGDGKINSTDCTMLKRYILRGIEEFPSPSGIIAADVNADLKINSTDLVLMKKYLLRSIDKFPAEDSQTPDEDNPGILYNGRFDFSDPNGPKCAWSGSNVELNFYGTEASVTIKSGGENWFQAIVDGNPLPPFSVNATTSTVKLVSGLAEGAHHLVLWKRTEASLGEVQFLGFDFGSGKLLAAPKPLERKIEFIGDSITCAYGNEGTSKEQSFTPKNENSYMSYAAITARNLNASANMIAWSGIGLTMNYGGAPGPLIMDRYPYTLPYSGVRWDFSKYVPQVVVINLGTNDFSTSFADKTKFVTAYKNLISEVRRNYPDAHIFCCVGPMLWGTGLDLCRSYVTEVVNDCNRSGDLKVYFVEFPQQDGSTGYGEDWHPSIATHQLMAERLTAEIKNKLGW
Multifunctional enzyme involved in the degradation of plant cell wall polysaccharides. Displays endoglucanase activity against carboxymethyl cellulose (CMC) and barley beta-glucan . Also catalyzes the deacetylation of acetylated birchwood xylan and glucomannan, with a preference for the latter, and of the synthetic substrate 4-nitrophenyl acetate (4-NPAc) .
P10477
B2HVR7
URED_ACIBC
Urease accessory protein UreD
Acinetobacter calcoaceticus/baumannii complex
MNRIQQTFQTSSAPFWYAQLELGFCYENSRTIMSHRKHYGPVRVQKMLWPEKTGVCHAIIVHPPAGIAGGDHLTFQIETERQAHAVITTPGAGKWYRTNGKHAFQHIYLNVKDDSILEWMPQETMLFDGALAHSETDIHLEQTASFIGWDMLVLGRQARAENFVQGSYHNQFKLWRKNKLLVADTLYFEGGDRWLSSCLGMNNQAVMASFWAVPPEKFRSSFYLEQHIELIRELIMRMDVPVTLTLLEDVLCARFLGNDVRRCHDAFAAIRAKLRRYWFDLDEEFPRIWKT
Required for maturation of urease via the functional incorporation of the urease nickel metallocenter.
B2HVR7
A3PLP3
HYPA_CERS1
Hydrogenase maturation factor HypA
Cereibacter
MHEMSLCEGIRGIVEDQARRHGFATVKVLRLEIGRFAGVEKAALGFAFDVVMRGSAAEGARLEILDLPGRALCYDCGEEAAIEDRFDPCPLCGGGRLMPVGGDEMRIKDMEVQ
Involved in the maturation of [NiFe] hydrogenases. Required for nickel insertion into the metal center of the hydrogenase.
A3PLP3
P29469
MCM2_YEAST
Minichromosome maintenance protein 2
Saccharomyces
MSDNRRRRREEDDSDSENELPPSSPQQHFRGGMNPVSSPIGSPDMINPEGDDNEVDDVPDIDEVEEQMNEVDLMDDNMYEDYAADHNRDRYDPDQVDDREQQELSLSERRRIDAQLNERDRLLRNVAYIDDEDEEQEGAAQLDEMGLPVQRRRRRRQYEDLENSDDDLLSDMDIDPLREELTLESLSNVKANSYSEWITQPNVSRTIARELKSFLLEYTDETGRSVYGARIRTLGEMNSESLEVNYRHLAESKAILALFLAKCPEEMLKIFDLVAMEATELHYPDYARIHSEIHVRISDFPTIYSLRELRESNLSSLVRVTGVVTRRTGVFPQLKYVKFNCLKCGSILGPFFQDSNEEIRISFCTNCKSKGPFRVNGEKTVYRNYQRVTLQEAPGTVPPGRLPRHREVILLADLVDVSKPGEEVEVTGIYKNNYDGNLNAKNGFPVFATIIEANSIKRREGNTANEGEEGLDVFSWTEEEEREFRKISRDRGIIDKIISSMAPSIYGHRDIKTAVACSLFGGVPKNVNGKHSIRGDINVLLLGDPGTAKSQILKYVEKTAHRAVFATGQGASAVGLTASVRKDPITKEWTLEGGALVLADKGVCLIDEFDKMNDQDRTSIHEAMEQQSISISKAGIVTTLQARCSIIAAANPNGGRYNSTLPLAQNVSLTEPILSRFDILCVVRDLVDEEADERLATFVVDSHVRSHPENDEDREGEELKNNGESAIEQGEDEINEQLNARQRRLQRQRKKEEEISPIPQELLMKYIHYARTKIYPKLHQMDMDKVSRVYADLRRESISTGSFPITVRHLESILRIAESFAKMRLSEFVSSYDLDRAIKVVVDSFVDAQKVSVRRQLRRSFAIYTLGH
Acts as component of the MCM2-7 complex (MCM complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity; specifically the MCM2-MCM5 association is proposed to be reversible and to mediate a open ring conformation which may facilitate DNA loading. Once loaded onto DNA, double hexamers can slide on dsDNA in the absence of ATPase activity. Necessary for cell growth.
P29469
B8J5H5
RNPH_ANAD2
tRNA nucleotidyltransferase
Anaeromyxobacter
MRKNGRGELDLRPILLEPRVSKHAEGSCLVRFGDTHVLCTASVDEKVPPHVYGTGAGWVTAEYGMLPRSTHERMQREAARGKQTGRTLEIQRLVGRALRAAVDLRAIGPRTVTLDCDVIQADGGTRTAAITGAYVALVQAVRGIQKRRQLAQDPVKRSVAAVSVGIVAGQVHLDLDYDEDSTAEVDMNVVATGDGALVEVQGTAEGKPFPRAELDRMLDAALAGLSRLKELQEAALRTP
Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation.
B8J5H5
P75548
HPRK_MYCPN
HPr(Ser) kinase/phosphorylase
Mycoplasma
MKKLLVKELIEQFQDCVNLIDGHTNTSNVIRVPGLKRVVFEMLGLFSSQIGSVAILGKREFGFLSQKTLVEQQQILHNLLKLNPPAIILTKSFTDPTVLLQVNQTYQVPILKTDFFSTELSFTVETYINEQFATVAQIHGVLLEVFGVGVLLTGRSGIGKSECALDLINKNHLFVGDDAIEIYRLGNRLFGRAQEVAKKFMEIRGLGIINVERFYGLQITKQRTEIQLMVNLLSLEKQTTVTFERLGTELKKQRLLGVDLSFYEIPISPGRKTSEIIESAVIDFKLKHSGYNSALDFIENQKAILKRKKDES
Is a metabolite-sensitive enzyme that catalyzes the ATP-as well as probably the pyrophosphate-dependent phosphorylation of Ser-47 in HPr, a phosphocarrier protein of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS). HprK/P also catalyzes the pyrophosphate-producing, inorganic phosphate-dependent dephosphorylation (phosphorolysis) of seryl-phosphorylated HPr (P-Ser-HPr). The regulatory role of HPrK/P in the physiology of M.pneumoniae is not known yet.
P75548
P49113
IL8_CAVPO
Neutrophil attractant protein 1
Cavia
MPSQLRVAVLAAFLLSAVLCEGMVVTKLVSELRCQCIKIHTTPFHPKFIKELKVIESGPRCANSEIIVKLSDNRQLCLDPKKKWVQDVVSMFLKRTESQDS
Chemotactic factor that mediates inflammatory response by attracting neutrophils, basophils, and T-cells to clear pathogens and protect the host from infection. Also plays an important role in neutrophil activation. Released in response to an inflammatory stimulus, exerts its effect by binding to the G-protein-coupled receptors CXCR1 and CXCR2, primarily found in neutrophils, monocytes and endothelial cells. G-protein heterotrimer (alpha, beta, gamma subunits) constitutively binds to CXCR1/CXCR2 receptor and activation by IL8 leads to beta and gamma subunits release from Galpha (GNAI2 in neutrophils) and activation of several downstream signaling pathways including PI3K and MAPK pathways.
P49113
B0S909
RECF_LEPBA
DNA replication and repair protein RecF
Leptospira
MFLKKIYIKNFRNHEETQLTFKSRLVFFIGNNGEGKTNLLESISLLSYLKSFRESDQNQLLRWDTSDTFIRAEFESEGNEYLFEYGIEHSQTKRKKLKVNGEEFKKISDYVGYFRSIVMSPPDILIIEDGNVERRRFLDAFISSTNRYYLKQLIEYERLIKQRNAALKKENASDREIGIWDEPIIEHDSEIREIRTKTIQSLAGYFHQNLLQLSSGKDPYFLTYKPNITSKEEHKQKLIDNLRKDKAIGYTSCGNHRDTLPIGFDDKDLSGFGSQGQKRSAVIALKTACFQMIRDTTGEAPVLLIDDIIRELDVKRREYFVNLISECGQAFFTTTDLEGINEYVGNLTVDKEIYIIDSGKVKVFTEI
The RecF protein is involved in DNA metabolism; it is required for DNA replication and normal SOS inducibility. RecF binds preferentially to single-stranded, linear DNA. It also seems to bind ATP.
B0S909
Q3T122
EIF3D_BOVIN
eIF-3-zeta
Bos
MAKFMTPVIQDNPSGWGPCAVPEQFRDMPYQPFSKGDRLGKVADWTGATYQDKRYTNKYSSQFGGGSQYAYFHEEDETSFQLVDTARTQKTAYQRNRMRFAQRNLRRDKDRRNMLQFNLQTLPKSAKQKERERIRLQKKFQKQFGVRQKWDQKSQKPRDSSVEVRSDWEVKEEMDFPQLMKMRYLEVSEPQDIECCGALEYYDKAFDRITTRSEKPLRSIKRIFHTVTTTDDPVIRKLAKTQGNVFATDAILATLMSCTRSVYSWDIVVQRVGSKLFFDKRDNSDFDLLTVSETANEPPQDEGNSFNSPRNLAMEATYINHNFSQQCLRMGKERYNFPNPNPFVEDDMDKNEIASVAYRYRRWKLGDDIDLIVRCEHDGVMTGANGEVSFINIKTLNEWDSRHCNGVDWRQKLDSQRGAVIATELKNNSYKLARWTCCALLAGSEYLKLGYVSRYHVKDSSRHVILGTQQFKPNEFASQINLSVENAWGILRCVIDICMKLEEGKYLILKDPNKQVIRVYSLPDGTFSSDEDDEEEEEEEEEEEEEEA
mRNA cap-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, a complex required for several steps in the initiation of protein synthesis of a specialized repertoire of mRNAs. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression. In the eIF-3 complex, EIF3D specifically recognizes and binds the 7-methylguanosine cap of a subset of mRNAs.
Q3T122
Q27665
PFKA_HAECO
Phosphohexokinase
Haemonchus
MSLKRNIRRLDSIVPTAGREGSDIQFNLYKGRGVAVFTSGGDSQGMNGAVHSVVRMGIYLGCKVCFINEGYQGMVDGGDNIVEASWNSGSDIIQKGGTIIGSARCTDLRQREGRMKAAYNLIEKGITNLVVIGGDGSLIGANQFRKDWPGLVKELVDTKKITPEAAKSYPNIQIVGLVGSIDNDFCGTDMTIGTDSALQRIIESIDAVVATAQSHQRAFVVEVMGRHCGYLALVAALACEADFCFIPEWPPPVNWREILCKKLQEMRAEGQRLNIIVVAEDDDRDGTPISSDLVKDVVAKTLKYDTRVTVLGHVQRGGSPSAFDRLLGCRMGAEAVLALMEMNEESEPCVISIMVTRWYVPLMQCVERTKAVQKAMSEKDWELAVKLRGRSFQRNLETYKLLTKLRTVEKDNLSGGQNFNVAVMNVGAPAGGMNAAVRSFVRMAIVPSLYSLRYEDSFEGLANGAFKKFQWGDVTNWVMHGGSFLGTQKQLPNEKNVPLIAEQLRKHNIQALLLVGGFEAYHSTLILSKNREKYPEFCIPLCVIPCTISNNVPGTSISLGSDTAINEICTMIDKIKQSATGTKRRVFIIETMGGYCGYLATLSALASGADNAYIFEEKFTVEISLRRGSHRCKMAQGVQRYLIVRNEYANKNFTTEFVKQLFAEEGKGEFSTRINILGHAQQGGSPTPFDRNMGTKLAARALEYIITQIKESMVNGVVSTKSPERATLLGLTGRRVVFTPVEELAAETDFDKRLPCDQWWLKLRPLLRILAKHTSIYHTEAMEDTEDYD
Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
Q27665
Q5VJ42
CYB_GALSE
Ubiquinol-cytochrome-c reductase complex cytochrome b subunit
Galago
MTNIRKQHPLAKMINHSFIDLPAPSNISSWWNFGSLLGLCLMIQIITGLFLAMHYTSDTSTAFSSVTHICRDVNYGWIIRYLHANGASMFFICLFMHIGRGLYYGSFTFLETWNIGIILLFTVMATAFMGYVLPWGQMSFWGATVITNLLSAIPYMGTGLVEWIWGGFSVDKATLTRFFAFHFILPFIIAALAMIHLLFLHETGSNNPSGISSDSDKIPFHPYYTIKDLLGVILLLVSLFSLVLFSPDLLGDPDNYIPANPLNTPPHIKPEWYFLFAYAILRSIPNKLGGVLALVSSILILALIPHLHTAKQQSMMFRPLSQCLYWMLVADLFTLTWIGGQPVENPFITIGQTASIIYFLIILILMPLTNLLENKLLKW
Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
Q5VJ42
Q7VXF8
PAND_BORPE
Aspartate 1-decarboxylase alpha chain
Bordetella
MQRIMLRAKLHRVTVTEADLHYEGSCGIDEDLLDAAGMREFERIELYNVTNGERFDTYIIKAARGSGAISLNGAAARRAQVGDLLIICTYGPMSEEQSAAHKPQVVLVDDANRVKEIRKFPA
Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
Q7VXF8
A8AVE2
GATA_STRGC
Glutamyl-tRNA(Gln) amidotransferase subunit A
Streptococcus
MTFNHKTIEELHDLLVKKEISAVELTQATLADIKEREGAVDSFITVSEEEALAKAAALDAKGIDADNLMSGIPLAVKDNISTKGILTTAASKMLYNYKPIFDATSVEKLYGKDMIIVGKTNMDEFAMGGSSENSYFKTTKNAWDGSKVPGGSSGGSATAVASGQVRLSLGSDTGGSIRQPASFNGVVGLKPTYGRVSRFGLIAFGSSLDQIGPFSQTVKENAQLLNVISGNDPKDSTSSQEAVPDFTNKIGQDIKGMKIALPKEYMGEGIDSKVKETILAAAKHLESLGAIVEEVSLPHSKYGVAVYYIIASSEASSNLQRFDGIRYGYRAEDIENLEDVYVKSRSEGFGEEVKRRIMLGTFSLSSGYYDAYFKKAGQVRTLIMQDFAKVFEKYDLILGPTAPTVAYDLGSQNQDPVAMYLADLLTIPVNLAGLPGISIPAGFADGLPVGLQLIGNHFDEATIYQAAAAFEATTDYHKQQPVIFGGEK
Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
A8AVE2
P81569
DEFD4_SPIOL
So-D4
Spinacia
MFFSSKKCKTVSKTFRGPCVRNA
Antimicrobial peptide. Active against Fusarium spp., Gram-positive and Gram-negative bacterial pathogens.
P81569
Q5P7G7
RF1_AROAE
Peptide chain release factor 1
Aromatoleum
MKQSIRDKLELLTHRLAELDRELSSGDAVRDMDGFRSLGRERAEIEPVVALYGAYRQAEADCESARAMLADAEMRELAESELETGAVRLQALEAELQCALLPCDPSDERNLFLEVRAGTGGDEASLFAGDLLRMYTRYAERQRWKVEIVSSSPSDLGGYKEVILRIAGAGAYSKLKFESGGHRVQRIPVTETQGRIHTSACTVAVMPEADEVEAVNINPADLRIDTFRASGAGGQHINKTDSAVRITHLPTGIVVECQDDRSQHRNRAQAMSVLAARIQDRQLREQQAREAATRKSLVGSGDRSERIRTYNYPQGRVTDHRINLTLYKLDAVMQGDLDELVDALTREHQADQLAALGGG
Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.
Q5P7G7
C6HI66
MAP2_AJECH
Peptidase M
Histoplasma
MGSKTPGNHRRDPNESSRPPAIDAINPPKQAAASGLVHGSLEGESQKRNKRKKKKKKKNTKELEILQTTPPRVALANIFRSQRYPEAEIVKYSSDNDNLQRTTAEELRHLSVLNAMDDEFLNDYRNAAEVHRQVRQYVQTIIKPGIALSQLAQEIEDGVRALTNHQGLETGDALKAGMAFPTGLCLNNIAAHWTPNPGAKEVILQYDDVLKIDFGVHVNGRIVDSAFTMAFNPVYDNLLAAVKNATNTGLKEAGIDARIAHISETIQEVMESYEVELNRKVIPVKAVRNITGHNILHYKIHGDKQVPFVKTQTNQRMEEGDVFAIETFGSTGKAYLDDATGIYGYGYDENASTAGLHHSSAKSLLKTIKENFGTLVFSRRYLERLGVQRYHLGMRSLVTNGIVQSYAPLVDVPGSYVAQFEHTVLLRPNCKEVISRGDDY
Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val).
C6HI66
C0SVM5
BBX19_ARATH
Protein SALT TOLERANCE HOMOLOG 5
Arabidopsis
MRILCDACENAAAIIFCAADEAALCRPCDEKVHMCNKLASRHVRVGLAEPSNAPCCDICENAPAFFYCEIDGSSLCLQCDMVVHVGGKRTHGRFLLLRQRIEFPGDKPKENNTRDNLQNQRVSTNGNGEANGKIDDEMIDLNANPQRVHEPSSNNNGIDVNNENNHEPAGLVPVGPFKRESEK
Acts as negative regulator of seedling photomorphogenesis.
C0SVM5
A5PKN5
BBS12_XENLA
Bardet-Biedl syndrome 12 protein homolog
Xenopus
MAIRGHKGLQQLLSMATSVNSFLGPMKSYKFIFDQITHESILTSSSFRLLENLDLTSAIGQLLNETIQAHHKSYKTGTTTLFFMVGAWSSAVQECLHLGIPVSLIVSVMLDGLNSCIGHVHSLQVSLVSQVTSDCTNIKTNGINHSNYSASGDQGNCSSELENNPLPRVSNMRTASEFPVAFHKKPLPLCTGTNLYKTQRRRLFHSRHLAEDLSFFQDVPERPQTTTLNNETLDGLAKGLAHGYQPVMNLVKNAVCLHCAEIKENSLDKSSFNISRLETCSLPGLSEEHTTVSFGYTTLVPTESAAVITHLNGKPLRILLVDGELTESHRHLGFDNPDNVKMVFEHAGNEKHNLEDSWISRAYEKIIQANINLILVRGDVCPFLLKQCIHRNILIVTQVKQNILQAFSECTGAEPVTYLTQINCCSVGNEAFVTLCTRANSIIEVSQKIVISITAKKLNLITATLSSRIPSTMQSIEDQFLTCAYRLHHALQEGNVFYGGGAIELLCIHHLQKLVQESSSSFYAYDNAQFHCLSSWMTESATFYRAAIIGCLAKGWYKYISVLLCNMGGFLSELDAVTFIENELQNISHHSSPIDYVRDQYSKKDLFNDEMGISISHHSLPVYDNVTPKLEAWRRALHLVLTVLQTDAEVITNSATQNQILMSETSNGEYLFL
Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis.
A5PKN5
B9MQJ8
RNPH_CALBD
tRNA nucleotidyltransferase
Caldicellulosiruptor
MRQDQRAYNEIRPIKITRNFIKYAEGSCLIEMGNTKVIVTATIDDKVPPFKKGSGEGWITAEYSMLPRATQQRNVRDINKLRLSGRSHEIQRLIGRALRAGINFKALGERVIIIDCDVIQADGGTRTASITGGFIAMFDACKKLYDEKIIENFPVTDFVAAVSVGICDGVEMLDLCFEEDSKAAVDMNLVMNDKGEFIEIQGTAEGAPFSWEQFQKLLELGKQGIQKIIEVQKEVLGQDCELVGSVPKDEKTSRCDQE
Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation.
B9MQJ8
B5M9L6
LSD18_STRLS
Lasalocid biosynthesis protein Lsd18
Streptomyces
MTNTRSAVVLGGGMAGMLVSSMLARHVGSVTVIDRDAFPAGPDLRKGVPQARHAHILWSGGARIVEELLPGTTDRLLGAGAHRIGIPDGQVSYTAYGWQHRFPEAQFMIACSRALLDWTVREETLREERIALVEKTEVLALLGDAGRVTGVRVRDQESGEEREVPADLVVDTTGRGSPSKRLLAELGLPAPEEEFVDSGMVYATRLFRAPEAAATNFPLVSVHADHRAGRPGCNAVLMPIEDGRWIVTVSGTRGGEPPADDEGFARFARDGVRHPLVGELIAKAQPLTSVERSRSTVNRRLHYDRLATWPEGLVVLGDAVAAFNPVYGHGMSAAAHSVLALRSQLGQRAFQPGLARAAQRAIAVAVDDAWVLATSHDIGYPGCRTQTRDPRLTRHAGERQRVTDLVGLTATRNQVVNRAAVALNTLSAGMASMQDPAVMAAVRRGPEVPAPTEPPLRPDEVARLVSGAGVTA
May catalyze the stereoselective double epoxidation reaction leading to bisepoxyprelasalocid A, a bisepoxide intermediate in the biosynthesis of the polyether antibiotic lasalocid A.
B5M9L6
Q7VQE5
RL2_BLOFL
50S ribosomal protein L2
Candidatus Blochmannia
MSVIKCNPTSPGRRHVVKLVNGGLYKGKPYSSLLSKKVANSSKGRNNYGRITMRHIGSGHKQRYRIIDFKRNKDDVFAVVERMEYDPNRSANIALIVYKDGERRYILAPRNLNVGNKIISGLNVPISPGNSLPLSNIPVGSIIHNVEMKVGKGGQLARSAGTYVQIVSRDGEYIILRLRSGEIRKVRCECRATIGEVGNNEHMLRALGKAGASRWRGIRPTVRGTAMNPIDHPHGGGEGKNFGKHPVSPWGVQTKGKRTRSNKRTDKFILCRRKKK
One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome.
Q7VQE5
A3D7B5
RLMD_SHEB5
23S rRNA(m5U1939)-methyltransferase
Shewanella
MAQFFKAKPNSSKQLSAKLSLSVNQLDHLGAGIAQHQGKVVFIPGALPDETVTVQFTEQKKNYARAKLIKVDTPSSERVEPECPHYHTCGGCDLQHMSLSGQREHKEAALLDIMAKFAGAEGGTLSPELTGEGWHYRRRARLATLFDKNTKHLSLGFRAASSSNVVPISQCQVLAKPLSDLIVPFAKLLNQLTAKASLGHLELIAADNGHFAVLRITKALNDKDLAKLSAFAEQHQIHICLQDNEGQFQGVGAELVLPVYQLLDDKAESDAVSLSFTPGNFVQVNGQINKAMVAQAMDWLAPALDERILDLFCGMGNFSLPLAKMGADVIGVEGVAEMVTQARVNAKANNLDKLTFFHGDLSADLSLEPWMGKIDKLLLDPARAGAFESLQWLKKMKPRKVVYVSCNPASLARDSAVLLERGYRLQQLGLIDMFPQTHHIEAMALFELTK
Catalyzes the formation of 5-methyl-uridine at position 1939 (m5U1939) in 23S rRNA.
A3D7B5
B8D9W6
NFUA_BUCA5
Fe/S biogenesis protein NfuA
Buchnera
MINISKKAQEHFTSLLSNEPENTQIRVFIVNPGTPNAECGVAFCPENEIELSDIQLKYDGFFVYVNKDTISYLKNSVIDLVTDKIGSQLTLKAPYAKNNFSKKVSSSLEEKVKCFLNLEINPQLSMHGGRVELMKIDENGIAAIQFSGGCNGCSMIGSTLKETVEKKLLSSFSEIKKVYDETHHLHGQHSFY
Involved in iron-sulfur cluster biogenesis. Binds a 4Fe-4S cluster, can transfer this cluster to apoproteins, and thereby intervenes in the maturation of Fe/S proteins. Could also act as a scaffold/chaperone for damaged Fe/S proteins.
B8D9W6
Q8DBG3
GLND_VIBVU
[Protein-PII]-UMP uridylyl-removing enzyme
Vibrio
MAFQSPLTFNDEQLTVAQLKSQLDLFANAQKQAFLNHHPVTDLVLSRAEYMDLLLTRLWRYYGFSEIHNISLVAVGGYGRGELHPLSDIDILVLSKHKLPGELETKLSEFITLLWDLRLEVGHAVRTVEECAAIGREDLTVATNLQEARLLCGSENTFQDLKKVVLSDSFWPSETFYRAKIQEQRERHARYHDTTYNLEPDIKSTPGGLRDIHTLSWVARRHFGATSLLEMSRYGFLTDAEYRELVECQDFLWRVRFALHIELKRYDNRLTFAHQIQVAEHLGFKGEGNRGIEMMMKEFYRTLRRVAELNKMLLKLFDQAIINGGETEPAVIINEDFQRRGRLIEARKPALFQARPETILDMFLHIANDSTIDSVSPPTLRQLRTARRRLNKFLHTIPEAREKFMELVRHPNALHRAFSLMHKLGVLAAYLPQWSQIVGQMQFDLFHVYTVDEHSVRLLNHINTFSYAKNHDKHPICCEVYPRLQKKELLLLAAIFHDIGKGRGGDHSEIGEKEAYDFCIEHGLSKPEAKLVSWLVRHHLLMSVTAQRRDIYDPEVITEFAKQVRDEERLEYLVCLTVADICATNPELWNSWKRTLLAELFYSTQRALRRGLENPVDVRERIRHNQQLASALLRKEGFTAREIEVLWQRFKADYFLRHTHKQIAWHCEHILRMDNPEQPLVLMSKKATRGGTEVFVYTKDQHALFATVVAELDRRNFNVHDAQIMSSKDGYVLDTFMVLDQHGQAIDVDNHKAVIKHLMHVLADGRPTKVKTRRTPYKLQHFKVKTKVDFLPTKSKKRTLMELVALDTPGLLAITGATFADMGFNLHGAKITTIGERAEDLFILTSENGGRLSEEQELQLREKLIHNIAELAP
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism.
Q8DBG3
A1A875
QUEA_ECOK1
Queuosine biosynthesis protein QueA
Escherichia
MRVTDFSFELPESLIAHYPMPERSSCRLLSLDGPTGALTHGTFTDLLDKLNPGDLLVFNNTRVIPARLFGRKASGGKIEVLVERMLDEKRILAHIRASKAPKPGAELLLGDDESINATMTARHGALFEVEFNDDRSVLDILNSIGHIPLPPYIDRPDEDADRELYQTVYSEKPGAVAAPTAGLHFDEPLLEKLRAKGVEMAFVTLHVGAGTFQPVRVDTIEDHIMHSEYAEVPQDVVEAVLAAKARGNRVIAVGTTSVRSLESAAQAAKNDLIEPFFDDTQIFIYPGFQYKVVDALVTNFHLPESTLIMLVSAFAGYQHTMNAYKAAVEEKYRFFSYGDAMFITYNPQAINERVGE
Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA).
A1A875
Q5FM04
RECR_LACAC
Recombination protein RecR
Lactobacillus
MQYPLPIAHLIDAYMKLPGIGEKTATRLAFYTMDMPQEDVEDFSKALIQVKQDIHQCPICGNITEKEICDICSNPNRDQTTIMVVEQPKDLMALEEMGEYDGLYHVLHGVLSPMDGIGPEEVNIKSLITRLQKNDDVKEVILALNSTPEGESTSMYISKLIKPAGIKVTRLAAGLSVGSDIEYANSITLKRAVQGRTTL
May play a role in DNA repair. It seems to be involved in an RecBC-independent recombinational process of DNA repair. It may act with RecF and RecO.
Q5FM04
C1CLK8
ATPA_STRZP
F-ATPase subunit alpha
Streptococcus
MAINAQEISALIKQQIENFKPNFDVTETGVVTYIGDGIARAHGLENVMSGELLNFENGSYGMAQNLESTDVGIIILGDFTDIREGDTIRRTGKIMEVPVGESLIGRVVDPLGRPVDGLGEIHTDKTRPVEAPAPGVMQRKSVSEPLQTGLKAIDALVPIGRGQRELIIGDRQTGKTTIAIDTILNQKDQDMICIYVAIGQKESTVRTQVETLRQYGALDYTIVVTASASQPSPLLFLAPYTGVAMAEEFMYQGKHVLIVYDDLSKQAVAYRELSLLLRRPPGREAFPGDVFYLHSRLLERSAKVSDELGGGSITALPFIETQAGDISAYIATNVISITDGQIFLGDGLFNAGIRPAIDAGSSVSRVGGSAQIKAMKKVAGTLRIDLASYRELEAFTKFGSDLDAATQAKLNRGRRTVEVLKQPVHKPLPVEKQVTILYALTHGFLDTVPVDDIVRFEEEFHTFFDAQHPEILETIRDTKDLPEEAVLDAAITEFLNQSSFQ
Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
C1CLK8
Q4UMV4
EX7L_RICFE
Exodeoxyribonuclease VII large subunit
spotted fever group
MLDNFIANQATKEFSVSEISNKIKELLENNFGYIKVKGEISGLKIASSGHAYFNLKENTAILACTCWRPILAKIKFPLNDGMEVVISGKLSSYAGNSRYQLSVDNLQPAGLGAMLQILNERKARLEKEGLFNKIRIPIPFLPDKIGVITSITGAVIKDIIHRIRERFPTRIIIWPVSVQGENSGNEIAEAIEGFNNLEEINKPSVIIVARGGGSIEDLWSFNDEILVRAAYNSKIPIISAVGHEVDYTLIDLAADKRAPTPTAAAEFAVPVRSILNNTLQSYEKILLNNTSRLIKYHEQNIINYDKIHRYLSHYMNNKQQLLDETGFNLLDALPCFIELQETKIKSFSKERVNPAKILNYKTLELTHQTAYLSKSANNTLKNFEYKLELNSTLLASLDYNNVLKRGFAIVKGETGNFLSSKITAANEKIFNIKFSDGEIKVVRNTVIASD
Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Q4UMV4
Q8UBB7
UGPC2_AGRFC
sn-glycerol-3-phosphate import ATP-binding protein UgpC 2
Agrobacterium tumefaciens complex
MAQIDIRQVRKSYGKTPTLHGVDLSFDSGEFVVILGPSGCGKSTLLRMIAGLEEITSGEIAIGGRVVNTLEPRERGCAMVFQNYALYPHMSVAANIGYALKVAGVPKAERQRRIEETAKIVGLSDYLERKPAALSGGQRQRVAMARAIIREPAVFLFDEPLSNLDAKLRVSMRAEIRKLHQRLSATSIFVTHDQVEAMTLADRLVVMNKGNVEQVGHPLDIYHRPASTFVASFIGSPAMNLFTTKVEVETPAVILSGTPVKLFPETALELRGRNVTVGIRPEQCVVSMDGPGVPAIVDFVEELGSGRIVHADIAGETFSAAIGEDLLVKPGQRIHLDLPTAHLHFFDPATGKRIETEGTAETARSKNETLLAV
Part of the ABC transporter complex UgpABCE involved in sn-glycerol-3-phosphate import. Responsible for energy coupling to the transport system.
Q8UBB7
B1XRS9
RS20_POLNS
30S ribosomal protein S20
Polynucleobacter
MANTVQARKRARQAVKQNEHNSSLRSKLRTSIKAVRKAIEAGDKAAAAKVFAATQSTIDKIADKKIAHKNTAARQKSRLSAAIKAMAA
Binds directly to 16S ribosomal RNA.
B1XRS9
A6W6U5
ISPE_KINRD
4-(cytidine-5'-diphospho)-2-C-methyl-D-erythritol kinase
Kineococcus
MPGSPDPAPPELASVTARAPAKVNLLLQVGPRRDDGYHDLVTVFQAVSLHEEVTVTPADEFGITVEGVGGTDVGGVPLDGTNLALRAARLLAERAGVDRAVHVHVRKEVPVAGGMAGGSADAAAALVACDSLWRLRLGLDALAELGAELGSDVPFGLHGRTAVGTGRGEHLVPVLTGASSAWVFVLAEGGLSTPAVFAECDRRREATGHDAPPGRLEAVEAALRGGDVDALGAALSNDLQDAACALDPALAGTVAAGRRAGAVAGIVSGSGPTVALLARSPAAARRLALDLEPLFGAERLRTATGPAPGARVLEAVSTPSPGGRS
Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
A6W6U5
P02025
HBB_HYLLA
Hemoglobin beta chain
Hylobates
VHLTPEEKSAVTALWGKVNVDEVGGEALGRLLVVYPWTQRFFESFGDLSTPDAVMGNPKVKAHGKKVLGAFSDGLAHLDNLKGTFAQLSELHCDKLHVDPENFRLLGNVLVCVLAHHFGKEFTPQVQAAYQKVVAGVANALAHKYH
Involved in oxygen transport from the lung to the various peripheral tissues.
P02025
A4IM31
PYRC_GEOTN
Dihydroorotase
Geobacillus
MAMWLKNGMSFNENGQLVRTHIKIEHGNIAAIHHEQLFEANGEDVIDVGGKLIAPGLIDVHVHLREPGGEAKETIETGTLAAAKGGFTTVAAMPNTNPVPDRKEQMEWLARRIQETAHVRVLPYASITLGQKGEELTDFAALKEAGAFAFTDDGVGVQSAGMMFEAMKRAAALDMAIVAHCEDDTLKNGGAVHDGDFARRYGIAGIPSVCEAVHIARDVLLAEATGCHYHVCHISTKESVRVVRDAKRAGICVTAEVTPHHLLLCDEDIPRLDANYKMNPPLRSRADREALIEGLLDGTIDFIATDHAPHTAAEKAKGMEAAPFGIVGLETAFPLLYTHFVKKNVFTLKQLVDWLTIKPAQCFGLQTGRLEVGAPADITVIDLETEEPIDPETFASKGNNTPFAGWRCQGWPVMTFVGGTLVWEKGRA
Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate.
A4IM31
Q3SGJ3
MINE_THIDA
Cell division topological specificity factor
Thiobacillus
MSWLSLIFGEKKSTASVAKERLQLIIAHERVGLSGRDFLPDLQKDLVAVISKYVKIDPDDIKVGLEKQGNYEVIEVNIVLPEMR
Prevents the cell division inhibition by proteins MinC and MinD at internal division sites while permitting inhibition at polar sites. This ensures cell division at the proper site by restricting the formation of a division septum at the midpoint of the long axis of the cell.
Q3SGJ3
Q8CW73
TORA_ECOL6
Trimethylamine-N-oxide reductase 1
Escherichia
MNNNDLFQASRRRFLAQLGGLTVAGMLGTSLLTPRRATAAQAATEAVISKEGILTGSHWGAIRATVKDGRFVAAKPFELDKYPSKMIAGLPDHVHNAARIRYPMVRVDWLRKRHLSDTSQRGDNRFVRVSWDEALDMFYEELERVQKTHGPSALLTASGWQSTGMFHNASGMLAKAIALHGNSVGTGGDYSTGAAQVILPRVVGSMEVYEQQTSWPLVLQNSKTIVLWGSDLLKNQQANWWCPDHDVYEYYEQLKAKVAAGEIEVISIDPVVTSTHEYLGREHVKHIAVNPQTDVPLQLALAHTLYSENLYDKNFLANYCVGFEQFLPYLLGEKDGQPKDAAWAEKLTGIDAETIRGLARQMAANRTQIIAGWCVQRMQHGEQWAWMIVVLAAMLGQIGLPGGGFGFGWHYNGAGTPGRKGVILSGFSGSTSIPPVHDNSDYKGYSSTIPIARFIDAILEPGKVINWNGKSVKLPPLKMCIFAGTNPFHRHQQINRIIEGWRKLETVIAIDNQWTSTCRFADIVLPATTQFERNDLDQYGNHSNRGIIAMKQVVPPQFEARNDFDIFRELCRRFNREEAFTEGLDEMGWLKRIWQEGVQQGKGRGVHLPAFNDFWNNKEYVEFDHPQMFVRHQAFREDPDLEPLGTPSGLIEIYSKTIADMNYDDCQGHPMWFEKIERSHGGPGSQKYPLHLQSVHPDFRLHSQLCESETLRQQYTVAGKEPVFISPKDASARGIRHGDVVRVFNVRGQVLAGAVVSDRYAPGVARIHEGAWYDPDKGGEPGALCKYGNPNVLTIDIGTSQLAQATSAHTTLVEIEKYNGTVEQVTAFNGPVEMVAQCEYVPASQVKS
Reduces trimethylamine-N-oxide (TMAO) into trimethylamine; an anaerobic reaction coupled to energy-yielding reactions.
Q8CW73
P24955
CYB_DAMDA
Ubiquinol-cytochrome-c reductase complex cytochrome b subunit
Dama
MINIRKTHPLMKIVNNAFIDLPAPSNISSWWNFGSLLGICLILQILTGLFLAMHYTSDTMTAFSSVTHICRDVNYGWIIRYMHANGASMFFICLFIHVGRGLYYGSYTFLETWNIGVILLFTVMATAFVGYVLPWGQMSFWGATVITNLLSAIPYIGTNLVEWIWGGFSVDKATLTRFFAFHFILPFIIAALAMVHLLFLHETGSNNPTGIPSDVDKIPFHPYYTIKDILGILFLFLFLMTLVLFAPDLLGDPDKYTPANPLNTPPHIKPEWYFLFAYAILRSIPNKLGGVLALVSSILILILMPFLHTSKQRSMMFRPFSQCLFWVLVADLLTLTWIGGQPVEYPFITIGQLASILYFLIILVLMPATSTIENNLLKW
Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
P24955
Q72QL9
TPIS_LEPIC
Triose-phosphate isomerase
Leptospira
MRKTIIAGNWKMNLSLKEAVFLAHSIREKIPSISKDKVSMVFPSTLHLENVSKILEGSSVIVGAQNCYHSGLAAFTGETSPDQLKEIGVKVVMVGHSERRQFLGESNFFCNDKIRFLLKNEFTVLYCVGETLSERESGKTLEVLSSQIREGLKGIDSVFFSNLILAYEPVWAIGTGKVATPSQAQEVHSFIRKEISGLFVGASSISESISILYGGSVKPDNIQDLLKEKDIDGGLVGGASQKISSFAGLF
Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
Q72QL9
B2A397
IF2_NATTJ
Translation initiation factor IF-2
Natranaerobius
MEKIRVYQLAKEIGLESKELVTTLQELDISVKNHMSTLSEEEADTVRELYTESSAKDEDNKDETSQQQDEKQEDKKEQGTTTDKPLVAPPITVGELAEQIGVESTSIITKLISKGVMANINQNLEEDSLEYLAQEFDFVVTQEEPEEDEKSEEDRIIEQIRSEEPKGEPLERAPVVTVMGHVDHGKTSILDSIRKTKSIEKEAGGITQHIGASRVLYNDKTVVFLDTPGHEAFTEMRARGAHVTDIAILVVAADDGVMPQTVEAINHAKSAGVPIIVAINKTDKPDANPDRVKQELTEYNLVTEEWGGDTICVSVSAVQNEGIDELLEMVQLVAEMNELTSYPQNTGKGTVIEAKLDKGRGPVATVLVEDGTLKVGDSVLCGSTFGNIRAMVDDRGKRLKQANPVTPVEILGLENIPEAGDEFQVVPDEKMAREIAKKKQEKEREEKLKRSQSVSLDNLFDQIKEGEQKELNIIVKGDVRGSVEALRESLLKLNDNEHEIKVNVIHAGVGTVSESDIMLAVASNAIIIGFNVRPDPNARKAAEREQIDMRVYRVIYEAIEDVKAAMAGLLDPEYKEVVQGQIEVRQLFKVSRIGTIAGCYVTDGYIRNNSYIRVIRDGRVIHEGNIKNLKRFQDDVKEVQQGYECGILLEKFNDLKEGDIFEAYTYEEISPDV
One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex.
B2A397
Q46FW1
MNTP_METBF
Putative manganese efflux pump MntP
Methanosarcina
MSFLTNFLLGLGLSMDAFAVSMSSSTTIRPFHQKDALKLAVFFGGFQAFMPVLGWLGGSAVSGFVSNYASWIAFGLLTFIGGKMIYEALYGDPDGKINSLNYSVLLMLAIATSIDALAVGISFAFLNTPILEPVIIIGCVTFVMSFCGAVLGHRIGHFFEHEVEIIGGLILIGIGGKILAEHLLWI
Probably functions as a manganese efflux pump.
Q46FW1
Q32DU5
GLPB_SHIDS
Anaerobic glycerol-3-phosphate dehydrogenase subunit B
Shigella
MRFDTVIMGGGLAGLLCGLQLQKHGLRSAIVTRGQSALHFSSGSLDLLSHLPDGQAVTDIHSGLESLRQQAPAHPYSLLGPQRVLDLACQAQALIAKSGAQLQGSVELPHQRITPLGTLRSTWLSSPEVPVWPLPAKKICVVGISGLMDFQAHLAAASLRELDLAVETAEIELPELDVLRNNATEFRAVNIARFLDNEENWPLLLDALIPVANTCEMILIPACFGLADDKLWRWLNEKLPCSLMLLPTLPPSVLSIRLQNQLQRQFVRQGGVWMPGDEVKKVTCKNGVVNEIWTRNHADIPLRPRFAVLASGSFFSGGLVAERNGIREPILGLDVLQTATRGEWYKEDFFAPQPWQQFGVTTDQTLRPSQAGQTIENLFAIGSVLGGFDPIAQGCGGGVCAVSALHAAQQIAQRAGGQQ
Conversion of glycerol 3-phosphate to dihydroxyacetone. Uses fumarate or nitrate as electron acceptor.
Q32DU5
P02582
ACT1_MAIZE
Actin-1
Zea
MADEDIQPIVCDNGTGMVKAGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDAYVGDEAQAKRGILTLKYPIEHGIVNNWDDMENWHHTFYNELRVSPEDHPVLLTEAPLNPKANREKMTQIMFETFECPAMYVAIEAVLSLYASGRTTGIVMDSGDGVSHTVPIYEGYTLPHAILRLDLAGRDLTDHLMKILTERGYSLTTSAEREIVRDIKEKLAYVALDYEQELETAKSSSSVEKSYEMPDGQVITIGSERFRCPEVLFQPSLVGMESPSVHEATYNSIMKCDVDIRKDLYGNVVLSGGFTMFPGIADRMSKEITSLVPSSMKVKVVAPPRRKYSVWIGGSILASLSTFQQMWISKGEYDETGPGIVHMKCF
Essential component of cell cytoskeleton; plays an important role in cytoplasmic streaming, cell shape determination, cell division, organelle movement and extension growth.
P02582
Q9H5J0
ZBTB3_HUMAN
Zinc finger and BTB domain-containing protein 3
Homo
MLREFSKWGVEASPGKAWERKRSLLRGAVGRYRGATGGDLFWAPFPSWGTMEFPEHSQQLLQSLREQRSQGFLCDCTVMVGSTQFLAHRAVLASCSPFFQLFYKERELDKRDLVCIHNEIVTAPAFGLLLDFMYAGQLTLRGDTPVEDVLAAASYLHMNDIVKVCKRRLQARALAEADSTKKEEETNSQLPSLEFLSSTSRGTQPSLASAETSGHWGKGEWKGSAAPSPTVRPPDEPPMSSGADTTQPGMEVDAPHLRAPHPPVADVSLASPSSSTETIPTNYFSSGISAVSLEPLPSLDVGPESLRVVEPKDPGGPLQGFYPPASAPTSAPAPVSAPVPSQAPAPAEAELVQVKVEAIVISDEETDVSDEQPQGPERAFPSGGAVYGAQPSQPEAFEDPGAAGLEEVGPSDHFLPTDPHLPYHLLPGAGQYHRGLVTSPLPAPASLHEPLYLSSEYEAAPGSFGVFTEDVPTCKTCGKTFSCSYTLRRHATVHTRERPYECRYCLRSYTQSGDLYRHIRKAHNEDLAKRSKPDPEVGPLLGVQPLPGSPTADRQSSSGGGPPKDFVLAPKTNI
May be involved in transcriptional regulation.
Q9H5J0
O25343
DAPD_HELPY
Tetrahydropicolinate succinylase
Helicobacter
MINKFKNFVSNYQQSNHYKEPLGFGIARVDIAPISKKILCATYPVLNWKDENLGSYAVFCNSLSKEKILKESASERVIEIDESFVLKALDFYTPFLNEAYSNKMAHKNIQVVLELLKALEENRLKNSDGESLYRLVILYEDKPCESVESAYMKLLALSLGKAPLRSLNLEGIFNQLSNAAWSGNKPYELEWLRMNEVALKMRDHFPSIDFIDKFPRYLMQLIPEFDNIRLLDSSKTRFGAYLGTGGYTQMPGASYVNFNAGAMGVCMNEGRISSSVVVGAGTDIGGGASVLGVLSGGNNNPISIGKNCLLGANSVTGISLGDGCIVDAGVAILAGSVIEIEENEFKKLLEVNSALEKHANNLYKGKELSGKNGVHFRSNSQNGKLIAFRSVKKIELNQNLH
Catalyzes the conversion of the cyclic tetrahydrodipicolinate (THDP) into the acyclic N-succinyl-L-2-amino-6-oxopimelate using succinyl-CoA.
O25343
Q3Z974
RL16_DEHM1
50S ribosomal protein L16
Dehalococcoides
MLQPKRVKFRKVQRGRRDGAAHKGNTVAFGEFALQSLEAGWITARQIEATRRAITRYIRRGGQVWIRIFPDKPITKKPAETRQGGGKGAPEEWVAVVRRGRIMFEIGGVTPEAAKEAMRLASYKMPVKTRFVARDVPAAAEETEVAEAE
Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs.
Q3Z974
A3NWS4
SYE_BURP0
Glutamyl-tRNA synthetase
pseudomallei group
MTRPVRTRFAPSPTGFIHLGNIRSALYPWAFARKMKGTFVLRIEDTDLERSTEASVDAILEGMAWLGLDYDEGPYYQMQRMDRYREVLAQMLEKDLVYPCYMSTEELDALRERQRAAGEKPRYDGTWRPEPGKVLPEPPAGVTPVLRFRNPLTGSVVWDDAVKGRVEISNEELDDLVIARPDGTPTYNFCVVVDDLDMGITHVIRGDDHVNNTPRQINILRALGGEVPVYAHLPTVLNEQGEKMSKRHGAMSVMGYRDAGYLPEAVLNYLARLGWSHGDAEIFSREQFVEWFDLEHLGKSPAQYDHNKLNWLNNHYIKEADDARLAELAKPFFAALGIDADTIARGPDLVGVMGLMKDRASTVKEIAENSTMFYRAPAPDAQALAQHVTDAVRPALAEFAAALKTAEWTKEAIAAALKAVLGAHKLKMPQLAMPVRLLVAGTTHTPSIDAVLLLFGRDVVVSRLAAALA
Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
A3NWS4
Q6CKX3
EIF3I_KLULA
Eukaryotic translation initiation factor 3 39 kDa subunit homolog
Kluyveromyces
MRPIVLKGHERPLTQVKFNRDGDLVFACSKDSVASIWYAINGERLGTLDDHSGTIWSIDVDESTTYALTGGADFCFKIWKVATGVAVHSVSTRSPVLRVEFSPDGSKLLIVLDAVMGHIGSIVVYSLIRNENGEIVNVKEEPDYEITTIEQATKVFVASWSYNGKYIIAGHEDGQISAYYGENGEFVQAKKIHEKSIKDIQFSPDRTYFITSSRDSVASLVDVDTFEVLKTYKADCPLNSASITPLKEFVILGGGQDAKDVTTTSAREGKFEARIYHKVFQDEIGRVKGHFGPLNYVAVSPTGTSYASGGEDGYIRLHHFDKSYFDFKYDVEKTFEVERRQQLQKQE
Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation.
Q6CKX3
C6TEX6
FEN1_SOYBN
Flap structure-specific endonuclease 1
Glycine subgen. Soja
MGIKGLTKLLADNAPKSMKENKFESYFGRKIAIDASMSIYQFLIVVGRSGTEMLTNEAGEVTSHLQGMFSRTIRLLEAGIKPVYVFDGKPPDLKKQELAKRYSKRAEATEDLSEALETANKEDIEKFSKRTVKVTKQHNDDCKRLLRLMGVPVVEAPSEAEAQCAALCKAGKVYGVVSEDMDSLTFGAPKFLRHLMDPSSKKIPVMEFEVAKILEELNMTMDQFIDLCILSGCDYCDSIRGIGGLTALKLIRQHGSIENIPENLNKERYQIPDNWPYQEARRLFKEPLVITDEKELDIKWSSPDEEGLITFLVNENGFNRDRVTKAIEKIKVAKNKSSQGRLESFFKPTANPSVPIKRKETPVNNAKETNKKTKAGGGKKKK
Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. It enters the flap from the 5'-end and then tracks to cleave the flap base, leaving a nick for ligation. Also involved in the long patch base excision repair (LP-BER) pathway, by cleaving within the apurinic/apyrimidinic (AP) site-terminated flap. Acts as a genome stabilization factor that prevents flaps from equilibrating into structures that lead to duplications and deletions. Also possesses 5'-3' exonuclease activity on nicked or gapped double-stranded DNA, and exhibits RNase H activity. Also involved in replication and repair of rDNA and in repairing mitochondrial DNA.
C6TEX6
Q1R0I0
RS12_CHRSD
30S ribosomal protein S12
Chromohalobacter
MATINQLVRKPRKRPVAKSDVPALQSCPQKRGVCTRVYTTTPKKPNSALRKVCRVRLTNGYEVASYIGGEGHNLQEHSVVLIRGGRVKDLPGVRYHTVRGALDTSGVQNRRQGRSKYGTKRPKS
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.
Q1R0I0
B4L7F0
RS3A_DROMO
40S ribosomal protein S3a
Drosophila
MAVGKNKGLSKGGKKGGKKKVVDPFSRKDWYDVKAPNMFQTRQIGKTLVNRTQGQRIASDYLKGRVFEVSLADLQKDIDPERSFRKFRLIAEDVQDRNVLCNFHGMDLTTDKYRSMVKKWQTLIEAIVEAKTVDGYLLRVFCIGFTFKDQQSQRKTCYAQQSQVRKIRARMTDIITNEVSGADLKQLVNKLALDSIAKDIEKSCQRIYPLHDVYIRKVKVLKKPRFDISKLLELHGDGGGKTTEAVVSAEGAVIDRPEGYEPPVQEAV
Essential for oogenesis; required for late follicle cell development.
B4L7F0
Q3LS63
DPP5_ASPNG
Dipeptidyl-peptidase V
Aspergillus subgen. Circumdati
MGALQWLSITAAAASAVSALTPEQMIGAPRRTEVIPNPSGDTGLFSTSQWSFDTHSESTWWSLIDLESGETTTLTDDSDIEEIIWLGSDSSTLLYINSTNAQVPGGVELWIADSSDFANYKAASLSAGFLGIKSTVTDSGDVHFILRGKSYPNGTAYNDQLAETYPSTARIYDSIFVRHWDTYLTTASHAVFSGTLQSSTSDDGNVQYTSSGGLTNLVNPVKGAESPFPPFGGNDDYDLSPDGKWVTFKSKAPELPLANNTAAYVYLVPHDGSATAFAVNGPDSPATPEGVEGESNNPVFSPDSDKIAYFQMATNTYESDRNVLYVYSIADDTITPLAKDWDRSPSSVTWVDGDNLVVASQDLGRTRLFAIPGDAGTTSSPRTFTDGGSVSAQYVLSNSTLLVTSSAFWTSWSVYTASPDEGVINTLASANEIDPELSGLSSSDFEEFYFDGNWTTLQGWITYPQDFDSSKKYPLAFLIHGGPEDAWADEWNLKWHSKVFADQGYVVVQPNPTGSTGFGQQLTDAIQLNWTAGAAYDDLTKAWQYVHDTYDFIDTDNGVAAGPSFGAFMITWIQGDDFGRKFKALVSHDGPFIGDAWVETDELWFVEHEFNGTFWQARDAFHNTDPSGPSRVLAYSTPQLVIHSDKDYRIPVANGIGLFNTLQERGVPSRFLNFPDEDHWVTGQENSLVWYQQVLGWINRYSGVGGSNPDAIALEDTVNPVVDLNP
Extracellular dipeptidyl-peptidase which removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini.
Q3LS63
Q06SH3
EFTU_STIHE
Elongation factor Tu, chloroplastic
Stigeoclonium
MARAKFERKKPHVNIGTIGHVDHGKTTLTAAITMALAARGGATGRKYDEIDSAPEEKARGITINAAHVEYETENRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTTEHVLLAKQVGVPAIVVFLNKADQVDDPELLELVELEVRDILDKYGFASDEVQILSGSALLALEALVENPNIKPGDSEWVDKIYNLMATVDEHIPTPKREMDKPFLLAVEDVFSITGRGTVATGRVERGTLKVNETVEIIGLRDTKTTTVTAIEMFQKTLDETIAGDNVGILLRGVQKKDIERGMVIAKPGTILPHTLFEGQVYVLTAEEGGRKSGFFKGYQPQFYVRTTDVTGKILDFSYIKQRNPSELSTMHSNPMVCPGDYVNMKIQLITPIAIEKGMRFAIREGGRTVGAGMVLEILES
This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
Q06SH3
C4KH27
GCSPA_SULIK
Glycine dehydrogenase (aminomethyl-transferring) subunit 1
Sulfolobus
MYKHPWLPNLDLIDEMLKEIGVNSLDELFNDIPAEIKINRLLNVAKGKPLSEYEIEKEINEKVKKNVELQAPPFIGAGICPHYIPNVVKFIIGRSEFYTSYTPYQPEISQGLLQALFEYQSLMAELLDMDVVNASMYDWGSALAEAVLMANRINGKKTVLVPENANPFHKEVVRTWIGGKGIKIEEVKYDKNSGELDLEDLEKKSNIDDISAIYIQQPNFFGIFESNIEHVIDVAKHKRALSIVGVNPLSLGLIKPPGSYEADIVVGDGQELGLPLNFGGPLMGVFAVRWDMSLVRQMPGRIVGITKDTNGKMGFTLILQTREQFIKREKATSNITTNEALLAIANAVYLSLLGKEGMRELAEEIYFRSHYAAKKLTEIDNVSMPFRSDFFEEFAIRFPIEYDKISNKLKERKLQGGLKLSDYTSLFCVTEVHDKKSIDLLVSTIQEMINGVETS
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.
C4KH27
Q4URM3
RNH_XANC8
Ribonuclease H
Xanthomonas
MKSIEVHTDGSCLGNPGPGGWAALLRYNGREKELAGGEANSTNNRMELMAAIMALETLTEPCQILLHTDSQYVRQGITEWMPGWVRRGWKTSGGDPVKNRELWERLHAATQRHSIEWRWVKGHNGDPDNERVDVLARNQAIAQRGGLATS
Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Q4URM3
A7GSJ5
DXS_BACCN
1-deoxyxylulose-5-phosphate synthase
Bacillus cereus group
MDLTQIQNPSFLKDMSISELEELSEDIRKFLIEELSQTGGHIAPNLGVVELTIALHTLFDSPKDKFLWDVGHQSYVHKILTGRAKEFRTLRQYKGLCGFPKRCESEHDVWETGHSSTSLSAAMGMALARDLKKTDEYVIPIIGDGALTGGMALEALNHIGHEKTDMIVILNDNEMSIAPNVGALHNVLGRLRTAGKYQWVKDELEYILKKIPAVGGKVAATAEKIKDSLKYLLVSGVFFEELGFTYLGPVDGHDYEKLFETLQYAKKTKGPVLVHVITKKGKGYKPAESDVIGTWHGTGPYKIESGDFVKPKEVAPAWSAVVSETVRKLARVDERIVAITPAMPVGSKLEKFHQEFPNRMIDVGIAEQHATTMAAGMATQGMKPFLAIYSTFLQRAYDQVVHDICRQNLNVFIGIDRSGLVGADGETHQGVFDIAFLRHLPNIVLMMPKDENEGQHLVYTAMQYEDGPIALRYPRGNGLGVPMDDEFKVIPIGTWETLREGTQAAIVTFGTTIPMAMEAAERLGKAGVSVKVVNARFIKPMDEAYLHDLLGKNIPILTIEEACLIGGFGSGVMEFAAEHGYHSALIERMGIPDYFIEHGSVTKLLEEIGLTTDAVVDRIHTMIPSKQKRA
Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-xylulose-5-phosphate (DXP).
A7GSJ5
Q99P99
HDAC4_RAT
Histone deacetylase 4
Rattus
MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPAAVPMDLRLDHQFSLPLEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCMSSDPRYWYGKTQHSSLDQSSPPQSGVSASYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVATALKKRPLDVTDSACSSAPGSGPSSPNSSSGNVSTENGIAPTVPSTPAETSLAHRLVTREGSVAPLPLYTSPSLPNITLGLPATGPAAGAAGQQDAERLALPALQQRISLFPGTHLTPYLSTSPLERDGGAAHNPLLQHMVLLEQPPTQTPLVTGLGALPLHTQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLHLSKMISKPSEPPRQPESHPEETEEELREHQALLDEPYLDRLPGQKEPSLAGVQVKQEPIESEEEEVEATREAEPSQRPATEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGSHRPLSRAQSSPASATFPMSVQEPPTKPRFTTGLVYDTLMLKHQCTCGNTNSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSSLTSVFVRLPCGGVGVDSDTIWNEVHSSGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAIAAKLLQQRLNVSKILIVDWDVHHGNGTQQAFYNDPNVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIANEFAPDVVLVSSGFDAVEGHPTPLGGYNLSAKCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELEPLPEKVLHQRPNANAVHSMEKVMGIHSEYWRCLQRLSPTVGHSLIEAQKCENEEAETVTAMASLSVGVKPAEKRSEEEPMEEEPPL
Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Involved in muscle maturation via its interaction with the myocyte enhancer factors such as MEF2A, MEF2C and MEF2D. Deacetylates HSPA1A and HSPA1B at 'Lys-77' leading to their preferential binding to co-chaperone STUB1.
Q99P99
Q2NQM2
RL3_SODGM
50S ribosomal protein L3
Sodalis
MKGLIGRKVGMTRIFTEDGVSIPVTVIEIEANRVTQVKDLENDGYRAIQVTAGTKKANRVIKPEAGHFAKAGVEAGRGLWEFRVEDGEEVTVGQSITVELFADVKKVDVTGTSKGKGFAGTVKRWNFRTQDATHGNSLSHRVPGSIGQNQTPGKVFKGKKMAGQLGNERVTVQSLDVVRVDVERNLLLVKGAVPGATGGDLIVKPAVKA
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.
Q2NQM2
Q3JTS8
PSTB_BURP1
Phosphate-transporting ATPase
pseudomallei group
MNMAESHLDPSKLATGPAGFGAAAGQRPLAPLNAKIEVKNLNFFYNQFHALKNINLSIPEGKVTAFIGPSGCGKSTLLRTFNKMYALYPEQRAEGEIVMDGENLLQSKLDISLLRARIGMVFQKPTPFPMSIYDNIAFGVKMFERLTRSEMDDRVEWALTKAALWNEVKDKLSQSGYGLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELIAELKSDYTVVIVTHNMQQAARCSDYTAYMYLGELIEFGETEKIFIKPARKETEDYITGRFG
Part of the ABC transporter complex PstSACB involved in phosphate import. Responsible for energy coupling to the transport system.
Q3JTS8