accession
stringlengths 6
10
| name
stringlengths 6
11
| Full Name
stringlengths 1
147
⌀ | taxon
stringlengths 3
46
⌀ | sequence
stringlengths 16
2.75k
| function
stringlengths 6
5.51k
| AlphaFoldDB
stringlengths 6
10
|
|---|---|---|---|---|---|---|
E7FHF8
|
HYD2D_PYRFU
|
Sulfhydrogenase II subunit delta
|
Pyrococcus
|
MKLGVFELTDCGGCALNLLFLYDKLLDLLEFYEIAEFHMATSKKSREKIDVALVTGTVSTQRDLEVLRDARNRSEYLIALGTCATHGSVQGVIENSKEAYRRVYGNGKPPVKLLNPKPVTDYVPVDFAIPGCPYDKEEVFQVLIDIAKGIEPVAKDYPVCLECKLNEYECVLLKKRIPCLGPVTAGGCNAKCPSYGLGCIGCRGPSLDNNVPGMFEVLKEILPDEEIARKLRTFARW
|
Part of a bifunctional enzyme complex that functions as a hydrogen-evolving hydrogenase with sulfur-reducing activity. May play a role in hydrogen cycling during fermentative growth. Activity exhibited with NAD in addition to NADPH. The alpha and delta subunits form the hydrogenase component that catalyzes the reduction of protons to evolve hydrogen.
|
E7FHF8
|
P9WGI2
|
SIGF_MYCTO
|
Stress response/stationary phase sigma factor SigF
|
Mycobacterium tuberculosis complex
|
MTARAAGGSASRANEYADVPEMFRELVGLPAGSPEFQRHRDKIVQRCLPLADHIARRFEGRGEPRDDLIQVARVGLVNAAVRFDVKTGSDFVSFAVPTIMGEVRRHFRDNSWSVKVPRRLKELHLRLGTATADLSQRLGRAPSASELAAELGMDRAEVIEGLLAGSSYHTLSIDSGGGSDDDARAITDTLGDVDAGLDQIENREVLRPLLEALPERERTVLVLRFFDSMTQTQIAERVGISQMHVSRLLAKSLARLRDQLE
|
Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. Held in an inactive form by a cognate anti-sigma factor RsbW (UsfX) until released. Its regulon, determined following disruption, consists of 38 genes decreased in exponential phase, 187 genes decreased in early S-phase, and 277 genes decreased in late S-phase .
|
P9WGI2
|
A8H1S5
|
ENO_SHEPA
|
2-phosphoglycerate dehydratase
|
Shewanella
|
MAKIINIIGREIMDSRGNPTVEAEVHLEGGFMGMAAAPSGASTGSREALELRDGDKARYMGKGVLKAVENINGLIRDALMGKDATAQAELDQIMIDVDGTENKDKLGANAILAVSLAAAKAAAAFKGVPLYAHIADLNGTPGQYSMPVPMMNILNGGEHADNNVDIQEFMVQPVGAKSFREALRMGAEIFHSLKSVLKSKGLSTSVGDEGGFAPDLASNADALAIIKVAVEQAGYTLGTDVTLALDCAASEFYKDGQYDLSGEGKVFSANGFSDFLKSLTEQYPIASIEDGLDESDWDGWAYQTQIMGDKIQLVGDDLFVTNTKILKRGIDNGIANSILIKFNQIGSLTETLAAIRMAKEAGYTVVISHRSGETEDATIADLAVATSAGQIKTGSLCRSDRVAKYNQLLRIEEQLGEKAPYNGLKEIKGQA
|
Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.
|
A8H1S5
|
Q8JGM4
|
QSOX1_CHICK
|
Quiescin Q6
|
Gallus
|
MWRRRARSGGGGGGGGGGAAPRCRWWPAVLALLAAALPAARSRSLYSPSDPLELLGADTAERRLLGSPSAWAVEFFASWCGHCIHFAPTWRALAEDVREWRPAVMIAALDCADEANQQVCADFGITGFPTLKFFRAFSKKAEDGIRIAHPTATVADLRRAIITNLEQSGDAWPPACPPLEPASAEEVRSFFHRNTERYLALIFEQSNSFVGREVALDLLQYENVAVRRVLSSEEELVEKFGVTTFPSAYLLLRNGSFSRLPVHAEARSFYTYYLQTLSGVTRGSYRLNVTGSAINETRALQPAQADRSKVYVADLESTVHYTLRVEAGRPAVLAGAQLAALKCYVATLAKYFPGRPSVQTFLQSLDSWLRNWTEPELPRSALKEAVKNKEDASPAAVLPTNVTWVGCRGSEPHFRGYPCGLWTIFHLLTVQAAQGGPDEELPLEVLNTMRCYVKHFFGCQECAQHFEAMAAKSMDQVKSRREAVLWLWSHHNEVNARLAGGDTEDPQFPKLQWPPPDMCPQCHREERGVHTWDEAAVLSFLKEHFSLGNLYLDHAIPIPMAGEEAAASARLSTAGLREKEEEERKEEEEEGEKETEKPHREGETGRPGSSELRRPSIVRRNPRLRALGEDIVDLDSFSEQHFKSKALRAAGRHRRLSKRDTVALHHDAGWERLQVPESREEEEEGGVLRRSPWLRVLGLGFSRLDVSLCIALYFLSSMCLLGMYTFFRLRTRARKGRPGFPVA
|
Catalyzes the oxidation of sulfhydryl groups in peptide and protein thiols to disulfides with the reduction of oxygen to hydrogen peroxide. Plays a role in disulfide bond formation in a variety of extracellular proteins. In fibroblasts, required for normal incorporation of laminin into the extracellular matrix, and thereby for normal cell-cell adhesion and cell migration.
|
Q8JGM4
|
Q6MEK7
|
DUT_PARUW
|
dUTP pyrophosphatase
|
Candidatus Protochlamydia
|
MTQSYSNTLTIPTLIENEELLPFYMTPEAAGADVKAYLKESLEIPPGQSALIPTGMRLAIPEGYEIQVRPRSGLALKHQVTVLNTPGTIDADYRGEIKIILINHGTNAFIVEPGMRIAQLVLAQVLRANFVLSEELESTQRGVGGFGHTG
|
This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.
|
Q6MEK7
|
Q65Q78
|
ISPD_MANSM
|
MEP cytidylyltransferase
|
Basfia
|
MTRHSRPIIAVVPAAGVGSRMQADKPKQYLTLLGKTLLEHTLEVLLSYTPIQQIILAVAENDPYLDQLDVIRQPKIKIVQGGRDRAGSVFNGLKAITQPHAWVMVHDAARPCLTHEDLDKLLQIEDDNGGILAIPAVDTIKRASAEKQIIQTEDRSQLWQAQTPQFFRADLLYRALQQAFEHGLAVTDEASAMEFAGFRPHLVAGRSDNLKVTRPEDLKLAEFYLSRK
|
Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
|
Q65Q78
|
A8H819
|
ADD_SHEPA
|
Adenosine aminohydrolase
|
Shewanella
|
MNYLQLPKIDLHCHLDGSVRPQTVIDLAKLQDVTIPSFNVDDIKALMVAPASCPNLDEYLTRFALPVSVMQTEAALERISFELFEDAAKENVKYLEVRFGPQLHQKMSLNFEQIIGSVVKGMRRAEAQYDIKGNYILSIIKVLPKDDINDVIDAGAKFLNNGVVAFDLAASEEPGFCHEYIPYAKYALEKGYRITIHAGEQGVGQNVYDAISLLGAERIGHGIHINSHQQAYELVKTEAVALETCPSSNVQTKAVESIESHPFGDFYRDGLLVTINTDNRTVSDTTMTKELQLAAEKFNLTEADYFAIYKMSVDNAFTSDEVKLSLLKFID
|
Catalyzes the hydrolytic deamination of adenosine and 2-deoxyadenosine.
|
A8H819
|
Q295P6
|
ADAL_DROPS
|
Adenosine deaminase-like protein
|
Sophophora
|
MWKFLKEMPKVELHAHLNGSLNTNSLQDLAEKVYGNTSEEFSHLCARFVNFEKDSNLDKCFEKFAFVHELTSTAAGLQYATELVIRDFANDNIQYLELRTTPKANKNYLRRDYLRIVLDTIKRSRKKYPNILVKLLPSINRSEPVAVAEETVALALEFAKTDPDLVVGIDLSGIPTKGKFTDFCGALDLARREGLKLVIHCAEIDNPPEIKEMLSFGMSRCGHGTYLTEEDFAQMKAANIPIECCLTSNIKSGSVSSFEEHHLKRLMESDAPRVVCTDDSGVFDTSLTNEFLLVVETFNVTRDQCIDLTLEAVKHSFASEQERQQMALKVEHYVNSLQTD
|
Catalyzes the hydrolysis of the free cytosolic methylated adenosine nucleotide N(6)-methyl-AMP (N6-mAMP) to produce inositol monophosphate (IMP) and methylamine. Is required for the catabolism of cytosolic N6-mAMP, which is derived from the degradation of mRNA containing N6-methylated adenine (m6A).
|
Q295P6
|
A0A069CUU9
|
BXWO_WEIOS
|
Putative botulinum-like toxin Wo
|
Weissella
|
MDVLEMFDVNYESPILESFDSTTQSLNDVHVFMSRIQMSAYDADGEGRIEYRNLKLYEISSGIFISTDRLDTGASGVEDDHEMVDYYSSARLTREFLGESLDSQKSDYFEGIKKVFSFYKNKCNESRYIKEFFEEIQFRNICGFPKQAGTSSTDIFDQFNSVDVLLQDPVTSVWNKKVGSKKANIVIIPPATNLPITEACATAGFQPEGFPKLGSGSFFTVQFDPFFSTRFKAHETDDVALLDPTLTLLHEMTHGLHFQKGIANPVNRSGETPAWATTWGRVTGDNDAFKETPMEELLTFNKHTIDDDIEISDHLKSTYIGFLYNGRNEDDPTESVDGVYQNVSSFLNQYRGFEISSDFQHFIESCYGVKYNQESKKFIVNPRNIKRYVQDGFFIDEAKFARILNIKTRSYYTLMPDNLGVWSYRVDILNRLRETFDEDRGLLSQELDFHTALTPVVSENPALELEVAGMQRMVSLPKIKASYLPSDIKIKNFTGQKISHDTILDTNISGIIISKIKYKSDFVVDESMPRSSLNTTNYNLSPIKGTKFETDIRDKTSVKVTVSEITAPMINHVMKLDNSKVLTERPSLNEDLEETFKNTKDVYIPKTTAMMKLKEGADQTLGAVGFAVWSGQILEDLYNLAQKKEVSIDQIKDDLMSILPFYCAYKNLSAEKYEQAFANATLDAFLIFATDGGGFAGLGITVGAIAINSMYAKAETMEAYDSMFGKYVDQYQNDIKNFTLNAYVQWENNILSRLWNESRLAITGFRNMLKTVKTVMEFDATNQAYSEEDRKIIKAKCEEIFSEFPMLMQTFAKNSMTANLENASKIFNDIVWQKIKEELDQYVIDSKKYFLDSLEEAYNNGSISAESYYKYQTEAREKFVSPREVIDLYIAAHDTVVKRKRYIRRYSRKYDLATDFKGNTVHLNGLGEGTQDIQDLYGNYSVYADKKTVSTQEGHFDQTIKIAKDTNTINKVVLAVSSNNGKEYALNKDEQYTISFWLRMPVPSSSEERRIFSYSAVSGVNKEVEELILQVKNNEFVLATANLLRNSEFVIEPRIALNRWVKITIVNENTRIKVYQNDNLLGLIKDSSRKKPIAQRGTFKFYNYNVDYQLDDISYYNGTISQRDIKYTFKEDHGQFVYDHWGERLQYNKAYYLLSDDNKSAFETVYETKRLKLKSVPGVDIKYLGMNDRVYGYYGGLQFKLVPLDSKNMNNYVRWGDKFTMQSIETTNLSLAIIQDNAYFAPTQLKLISNEGKSEEEIFTFDRNIKLQNAAILVGTGNSKQGPISAYKRGYSGDLWINGARLDGYVTVVNKSNYSNDEIQEKFKWIFVPKDANWVE
|
When overexpressed the N-terminus (residues 1-476) cleaves rat synaptobrevin-2/VAMP2 between '89-Trp-|-Trp-90' in vitro. This releases the cytoplasmic domain of VAMP2 from the synaptic vesicle membrane, which would prevent the assembly of the trans-SNARE complex on the membrane and thus prevent vesicle-target membrane fusion and neurotransmitter release .
|
A0A069CUU9
|
Q3SVI1
|
PROB_NITWN
|
Gamma-glutamyl kinase
|
Nitrobacter
|
MTRPHLKKFRRIVVKVGSSLLIDSAAGKVRGEWLSALAADIAGLHGDGCDVLVVSSGAVALGRSKLKLPRGPLKLEESQAAAAVGQIALARIWSKVLADHGIGAGQILVTWQDTEERRRYLNARSTIAKLLEWRAVPVINENDTVATNEIRYGDNDRLAARVATMASADLLILLSDIDGLYDAPPHLNPDAKLITVVKRVTADIEAMAGSAASELSRGGMRTKIEAAKIATTAGTHMLIASGTIEHPLRAIMDGGPCTWFLTPANPVTARKRWIAGSLEPRGTLAIDAGAVAALRAGKSLLPAGVTRIDGHFARGDAVIVRGPNGHEIGRGLVAYDAADADRIKGRSSSDAAQLLGVRGRVEMIHRDDLVVGGPLGDSA
|
Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate.
|
Q3SVI1
|
O57415
|
RREB1_CHICK
|
Ras-responsive element-binding protein 1
|
Gallus
|
MMSAVMNVGKIAENGGTSQTVKSPSKSPAPNRIGRRNQETKEEKSSYTCPLCEKICTTQHQLTMHIRQHNTDTGGTDHSCSICGKSLSSASSLDRHMLVHSGERPYKCSVCGQSFTTNGNMHRHMKIHEKDPNSTASTTPPSPLKAKRLSSKRKFSQDAEMDREERTPAKKVVEDGQYGEGDRKEDDAYHCPVCFKDFFCKYALESHMETHPDNSLRCDICCITFRTHRGLLRHNAVIHKQLPRDPTGKPFIQNNPSIPAGFHDLGFTDFSCRKFPRISQVWCETNLRRCISEFHRFICETCNKAFPMLLALKLHTETHVMDQGRDKHKLQSTSLPSENPDQKAFMASLGLQYTKDIKPVKQEDDTQDEVQEMRLRALKSNLPQEPGSTGLLSLSPLEAATMGGPFSVLPPTKENIKLLSLQPFQKGFIIQPDSSIVVKPISNESAIELADIQQILKMASSAPPQISLPPLSKAPSVPVQSIFKHMPPLKPKPLVTPRTVVATSTPPPLISAQQASPGCISPSLPPPPLRLIKNSVETSSNSHLSQPGAKSSPSSQLLLQPKVEPLTQHEMKTQLEQDSIIEALLPLNMEAKIKQEVTEGDLKAIIAGAANKKAPTMRKVLYPCRFCDQVFAFSGVLRAHIRSHLGISPYQCNICDYIAADKAALIRHLRTHSGERPYICKICHYPGTVKANCERHLRKKHLKVTRKDIEKNIEYVTSNAAEMVDAFCSPDTVCKLCGEDLKHYRALRIHMRTHSGCQKKKPFECKECGTAFSAKRNCIHHILKQHLHVQEREIENYILVVDCSAQESHTDAPLLEDSTYMDCKPITPFLEPQNGFLLGTSSHVPIKLEPMGNFPMDFDEPLDFSQKSKNLSAVQVKQENLLVSSPLSFYDCSMEPIDLSIPKVLKRDNDIPGEARNQELASSVITDNAYNWQQCPLGFGANGNSEKNRAVGHPQPLKGSLHLTVPIISPALLGNSALLRPLRPKPPPQPLLPKPPVTKELPPLASIAQIISSVSSAPALLKTEAADASPKAASSSTGCDKSGNAKAKMTIVTAIQRDSNLPSDLTQACDPEPSPIADTGLTKKRGRKKGTKNKPKLSSGVDLESSGEFASIEKMLATTDTNKFSPFLQSTDNFKEESGQNGTSEDEKETPEDKLLRGKRNTYSDCPQKITCPYCPRVFSWASSLQRHMLTHTDSQADTEAPATGGEVLDLTSCEKEQPEEVSELPGSECSPQEEQKADSPPAEEDAEEKADEYEEGPEEDSVSNKSLDLNFASKLMDFKLAESDQSAGSSSQTERKHACDVCGKTFKFAGALSRHKKAHIREDRKDERSSEDESKSIQDDAGAPSMQDSGLEQEESPMDLKVVESPLDCEATGKENEESESISEGEGTERKSTEKSSDDKIPKTDEAKSTAKADKRKKVCTVCNKRFWSLQDLTRHMRSHTGERPYKCQTCERTFTLKHSLVRHQRIHQKVKNTRNHGKESDKEETQSRCGEDSENESSHSGTNPISENECDFAGVVGSHPSGTRSRKESLVGAAKDVPCEEERPSGQGATADLVEPAKSTQKQPAKDQEPRGSSELERPSGFIQDLLEMHNKKSPMNHILASADSTPQLLGVE
|
Transcription factor that binds specifically to the RAS-responsive elements (RRE) of gene promoters.
|
O57415
|
Q9NXL6
|
SIDT1_HUMAN
|
SID1 transmembrane family member 1
|
Homo
|
MRGCLRLALLCALPWLLLAASPGHPAKSPRQPPAPRRDPFDAARGADFDHVYSGVVNLSTENIYSFNYTSQPDQVTAVRVYVNSSSENLNYPVLVVVRQQKEVLSWQVPLLFQGLYQRSYNYQEVSRTLCPSEATNETGPLQQLIFVDVASMAPLGAQYKLLVTKLKHFQLRTNVAFHFTASPSQPQYFLYKFPKDVDSVIIKVVSEMAYPCSVVSVQNIMCPVYDLDHNVEFNGVYQSMTKKAAITLQKKDFPGEQFFVVFVIKPEDYACGGSFFIQEKENQTWNLQRKKNLEVTIVPSIKESVYVKSSLFSVFIFLSFYLGCLLVGFVHYLRFQRKSIDGSFGSNDGSGNMVASHPIAASTPEGSNYGTIDESSSSPGRQMSSSDGGPPGQSDTDSSVEESDFDTMPDIESDKNIIRTKMFLYLSDLSRKDRRIVSKKYKIYFWNIITIAVFYALPVIQLVITYQTVVNVTGNQDICYYNFLCAHPLGVLSAFNNILSNLGHVLLGFLFLLIVLRRDILHRRALEAKDIFAVEYGIPKHFGLFYAMGIALMMEGVLSACYHVCPNYSNFQFDTSFMYMIAGLCMLKLYQTRHPDINASAYSAYASFAVVIMVTVLGVVFGKNDVWFWVIFSAIHVLASLALSTQIYYMGRFKIDLGIFRRAAMVFYTDCIQQCSRPLYMDRMVLLVVGNLVNWSFALFGLIYRPRDFASYMLGIFICNLLLYLAFYIIMKLRSSEKVLPVPLFCIVATAVMWAAALYFFFQNLSSWEGTPAESREKNRECILLDFFDDHDIWHFLSATALFFSFLVLLTLDDDLDVVRRDQIPVF
|
In vitro binds long double-stranded RNA (dsRNA) (500 and 700 base pairs), but not dsRNA shorter than 300 bp. Not involved in RNA autophagy, a process in which RNA is directly imported into lysosomes in an ATP-dependent manner, and degraded.
|
Q9NXL6
|
B1IJN1
|
VATE_CLOBK
|
V-ATPase subunit E
|
Clostridium
|
MSNLENLTSKIIEDANKEAEKLLSEAKKEENEIVDEKVKKANKAKEQIIEKTKREAKTKAERVISNTHLKVRNNKLEAKQEMINKVFDEAVIKLQNLPQEEYLNFIKNSILSLDIEGDEEIIVSPNDKNKIDISFILTLNNKLKAKGKKDLLKISNENRNIKGGFILYKNGIEINNSFEALVDSLRDELEQEIIEALFS
|
Produces ATP from ADP in the presence of a proton gradient across the membrane.
|
B1IJN1
|
A9AMA4
|
ACCD_BURM1
|
Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta
|
Burkholderia cepacia complex
|
MSWLDKLLPPKIKQTDPKSRKGIPEGLWVKCPSCEAVLYRNDVDANLHVCPKCDHHMRIGARERLDALLDPEGRYEIGQEIVPVDSLKFKDSRKYPDRLKEAMDETGETDAMVVMGGAIHTLPVVAACFEFSFMGGSMGSVVGERFARGAQNALEQHVPFICFTASGGARMQESLLSLMQMAKTTAMLTKLSEAKLPFISVLTDPTMGGVSASFAFLGDVVIAEPKALIGFAGPRVIEQTVREKLPEGFQRAEFLLKTGAIDMIVDRRKMRDEIAQLLALLQRQPADALA
|
Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA.
|
A9AMA4
|
Q6CZ00
|
TUSA_PECAS
|
tRNA 2-thiouridine synthesizing protein A
|
Pectobacterium
|
MTDPFTNPDKTLDAQGLRCPEPVMMVRKTVRQMETGQTLLIIADDPATTRDIPGFCVYMEHELLAQETEQVPYRYLLRKGQ
|
Sulfur carrier protein involved in sulfur trafficking in the cell. Part of a sulfur-relay system required for 2-thiolation during synthesis of 2-thiouridine of the modified wobble base 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) in tRNA. Interacts with IscS and stimulates its cysteine desulfurase activity. Accepts an activated sulfur from IscS, which is then transferred to TusD, and thus determines the direction of sulfur flow from IscS to 2-thiouridine formation. Also appears to be involved in sulfur transfer for the biosynthesis of molybdopterin.
|
Q6CZ00
|
Q2IIL0
|
MUTL_ANADE
|
DNA mismatch repair protein MutL
|
Anaeromyxobacter
|
MPRIHVLPPGLVNQIAAGEVVERPASIVKELVENALDAGATAIGVDVEEGGLALVRVADDGSGMDRDDALLALERHATSKLRDAEGLAAIGTMGFRGEAVPAIASVSRFRLDTSPGEDGAGTRVEIEGGVLGEVAPVARPRGTTVEVRDLFFNTPARRKFMRAASTEAGHVSEAVIRLALARPDVGFTLRSGGRLVLGARAGGGLADRAGQALGREAHRHLLPVDARRGEVRVHGLICSPDHSEATGRALYLFVNGRYVRDRAAAHAVLRAFAGTLPPGRHPAGVLFVELPLDRVDVNVHPQKLEVRFAEGREVFDALFHTVAGALRTAPWLRARPQAAPAGEGPPAGGEAVAVPLAGEDAAAVLAWARAARPPEGSGATLVQPAPGAWATGRLAFPIAPAPDAGPEAAPRPEGYFAGLRYVGQHARTYLLCEAPGGTLVVIDQHASHERMLFHRLKEAFRARRIPVQPYLLPQVVTLPPAAARALEAGLAELGRLGFDAEPFGGDAFAVKGAPAALAGVDLTALLTDLGSQLADVERGSAVDDAFHDLLATMACHAAVRANQDVSPEEARALLDGLDAIDFKARCPHGRPVVFELSLADLERRVGRR
|
This protein is involved in the repair of mismatches in DNA. It is required for dam-dependent methyl-directed DNA mismatch repair. May act as a 'molecular matchmaker', a protein that promotes the formation of a stable complex between two or more DNA-binding proteins in an ATP-dependent manner without itself being part of a final effector complex.
|
Q2IIL0
|
A6SV54
|
MIAA_JANMA
|
Isopentenyl-diphosphate:tRNA isopentenyltransferase
|
Janthinobacterium
|
MSVKPLVVSIMGPTASGKTAAALAVAEKIPAEIISVDSALVYREMDIGTAKPSAEELAQVPHHLIDILDPLDSYSVMQFRQDAIRLAAEISARGKLPLLVGGTMLYFKGLKDGLDALPQADAALRAELDAEAAAIGYPAMHAKLAALDPITAERLKPNDSQRIQRALEIIALTGQPMSALLAQAPKTELPFTLLPIALEPSDRSVLHTRIATRFDAMLKGGALLDEVKALRARGDLHLGLPSMRCVGYRQSWEYLDGAYSLAELRERGIAATRQLAKRQLTWLRSMDDRHIIDCLAPDASGAILQQIEIAQNRA
|
Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
|
A6SV54
|
Q47VD1
|
HSLO_COLP3
|
Heat shock protein 33 homolog
|
Colwellia
|
MSQFNVLNRYLFTDAHARGELVQLSSSFESIIKNHNYPVGVEKLLGELLCATCLLTATLKFEGDITVQLQGDGPVGYMSVSGNNKQQMRGIAKMAEETSADTLQTLIGKGTMIITIRPNAGEAYQGVVALDEESLADCLAHYFDVSEQIPTKIWLFCDTEQQLAAGALVQLLPDGDGSTENKEQQQSDFEHLCQLTNTIKSEEVFSLEAEALLYRLYHQEQVNIFEPQMVSYLCGCSADKCLSAISQIEPSEIKAILAEHGKISMTCDYCITTYDFDELSLKSFISKVNH
|
Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress.
|
Q47VD1
|
Q2L268
|
RL18_BORA1
|
50S ribosomal protein L18
|
Bordetella
|
MDKKVTRLRRAVPTRRKITQLGVHRLSVFRSNQHIYANIISPEGDRVVVSASTLEAEVRTQLAGQSGAGGNAAAAALIGKRVAEKAKAAGIELVAFDRSGFRYHGRVKALADAAREAGLKF
|
This is one of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance.
|
Q2L268
|
O08320
|
ARGB_LACPL
|
NAG kinase
|
Lactiplantibacillus
|
MTKLIVIKIGGQAISQLSTTFFDQIAQWYQQHYQILIVHGGGPMINRLTTQLALPVHKVNGLRVTDAATLVLTKLALLGDAQPALLAKLTQHHLPVLGLNAADNQLLTGELIDYRQLGYVGRLTAVNQVQLMQLLAHHIGILAPLALTETGQWLNVNADMAATVLAQQLHAEKLVLLTDVPGIIHHGNVMTSLSPQQAQQLIRTAVITAGMQPKVQAAIAAIQTGVKQAIITNAIDQPGTAIIQEVAV
|
Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.
|
O08320
|
Q2S528
|
MURG_SALRD
|
Undecaprenyl-PP-MurNAc-pentapeptide-UDPGlcNAc GlcNAc transferase
|
Salinibacter
|
MSTRAPHILMVGGGTGGHVYPAIAIADAVRALRPDAQIVFAGTQDRLEARAVPEAGYALHPITAQGLQRRAVASNLLLPFRVAQGLVQSWRLVGAIEPDVAVGTGGYVAAPVLMAAWLRGRPLLIQEQNAYAGLTNRVLARLALRIHLAFPEAKDWVPAEHAVVSGNPTRQSLRDADPDAARAAFNVPEDGRVLLVMGGSLGSAAINGAIQRILDPLLAEGDVHVVWQTGTRYYDDLTEDLDEHPRLRVVEYIDQMGHAYAAADLAVCRAGALTCSELTVTGTPAVLVPSPNVTADHQTKNARSLERAGAAVWLDEADLDAHLETVLLDLLGNSDRRARMAEAARDRARPDAAETIARDVLALADRYRTN
|
Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II).
|
Q2S528
|
Q12HV7
|
SECB_SHEDO
|
Protein-export protein SecB
|
Shewanella
|
MAEVANNEQQEQAPQFNIQRIYTKDLSFETPNSPAVFQKEWNPEVKLDLDTRSNKLSDDVYEVVLSLTVTAKNGEETAFLCEVQQAGIFSIQGLTEQQLAHSLGAYCPNVLFPYARELVGSLVGRGTFPQLNLAPVNFDALFAQYVQQRQAAAAEAPAVEEANA
|
One of the proteins required for the normal export of preproteins out of the cell cytoplasm. It is a molecular chaperone that binds to a subset of precursor proteins, maintaining them in a translocation-competent state. It also specifically binds to its receptor SecA.
|
Q12HV7
|
P32796
|
CACP_YEAST
|
Carnitine O-acetyltransferase, mitochondrial
|
Saccharomyces
|
MRICHSRTLSNLKDLPITSRRAMHSAIVNYSTQKAQFPVETNNGEHYWAEKPNKFYQNKRPNFQGITFAKQQDLPSLPVPELKSTLDKYLQTIRPFCNDVETFERQQLLCKDFSEHMGPILQDRLKEYANDKRNWMAKFWDEQSYLQYNDPIVPYVSYFYSHMPLPNHLSKIDNDPLIKATAIISTVVKFIEAIKDESLPVEIIKGMPFCMNSFSLMFNTSRLPGKPEDNQDTNIFYSVYENNFVTIAYKGKFYKLMTHDGNDKPLSENEIWRQLYSVVFQGSQSDPKLGGIGSLTSLPRDQWREVHLELMKDPISQDSLETIHKSSFMLCLDLDQSPVTLEEKSRNCWHGDGINRFYDKSLQFLVTGNGSSGFLAEHSKMDGTPTLFLNNYVCQQLNKLDVDDFMRKVITPSSTVAMKPMELPFIITPKIHKAIESAQLQFKETIGEHDLRVWHYNKYGKTFIKRHGMSPDAFIQQVIQLAVFKYLKRQLPTYEAASTRKYFKGRTETGRSVSTASLEFVSKWQNGDVPIAEKIQALKHSAKEHSTYLKNAANGNGVDRHFFGLKNMLKSNDDQIPPLFKDPLFNYSSTWLISTSQLSSEYFDGYGWSQVNDNGFGLAYMLNNEWLHINIVNKPAKSGASVNRLHYYLSQAADEIFDALENENKRKAKL
|
Carnitine acetylase is specific for short chain fatty acids. Carnitine acetylase seems to affect the flux through the pyruvate dehydrogenase complex. It may be involved as well in the transport of acetyl-CoA into mitochondria.
|
P32796
|
Q1MMG6
|
DUT_RHIL3
|
dUTP pyrophosphatase
|
Rhizobium
|
MTIHHDLSPTLNLIRLANGEGLDLPAYESKGAAGMDLRAAVDEAAPLTLLPGKRALVPTGFIFEIPEGFEGQVRPRSGLAFKNGITCLNSPGTVDSDYRGEVKVLLANLGEEAFVISRGMRIAQMVIAPVTQMRVAEITEASETMRGAGGFGSTGV
|
This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.
|
Q1MMG6
|
Q493Q2
|
FTSW_BLOPB
|
Peptidoglycan polymerase
|
Candidatus Blochmannia
|
MRLFKTKIINRPLKLGKKKSSNIHVLYDRIFFWLLLGLIGIGFVIISSGSIPTGMRLANDPCYFIKRVIVYYSVTFLLSVIILKIPIIVWQNYSAIMLLCSCIMLITALILNNSTNGASRWIMWGTLCIQPAELSKLSFICYLANYLERKSKEVCTKFWSICKPIVIMIILAVLLLAQPDFGSIIILFITTLSILFLFGAKLCQLILVFVFNIFLIIPLIVIKPYRIQRILTFWDPWKDPFGNGYQLTQSLIAFGRGKCFGEGLGNSVLKLEYLPEAHTDFIFSILAEELGYFGAILVLFMLFIIVLRAMIIGHRALNINHRFSGILACSISMWFGLQIFINVGTVSGILPTKGLTLPFISYGGSSFLITVMASMQLLRIDFETRLSKNQAFLKCTKI
|
Peptidoglycan polymerase that is essential for cell division.
|
Q493Q2
|
B8CM26
|
SLMA_SHEPW
|
Nucleoid occlusion factor SlmA
|
Shewanella
|
MAASPKINRREHILQCLATMLETSPGQRITTAKLAAEVGVSEAALYRHFPSKARMFEGLIEFIEESLLSRINLIMDEEKDTMKRCQQLLQLLLVFAERNPGISRVLNGDALLGENERLRSRISQLFSKIETHLKQILREKSLREGQAFSIDEAVLANLLMAIAEGRIAQFVRSEFKLKPTKHFNEQWTFVQQQLLQS
|
Required for nucleoid occlusion (NO) phenomenon, which prevents Z-ring formation and cell division over the nucleoid. Acts as a DNA-associated cell division inhibitor that binds simultaneously chromosomal DNA and FtsZ, and disrupts the assembly of FtsZ polymers. SlmA-DNA-binding sequences (SBS) are dispersed on non-Ter regions of the chromosome, preventing FtsZ polymerization at these regions.
|
B8CM26
|
P42252
|
TATCD_BACSU
|
Sec-independent protein translocase protein TatCd
|
Bacillus
|
MDKKETHLIGHLEELRRRIIVTLAAFFLFLITAFLFVQDIYDWLIRDLDGKLAVLGPSEILWVYMMLSGICAIAASIPVAAYQLWRFVAPALTKTERKVTLMYIPGLFALFLAGISFGYFVLFPIVLSFLTHLSSGHFETMFTADRYFRFMVNLSLPFGFLFEMPLVVMFLTRLGILNPYRLAKARKLSYFLLIVVSILITPPDFISDFLVMIPLLVLFEVSVTLSAFVYKKRMREETAAAA
|
Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. Required for PhoD secretion. TatCd promotes membrane localization of TatAd via domain specific interactions. TatCd is required for stabile production of TatAd as well as for its maintenance.
|
P42252
|
Q0T894
|
GUAC_SHIF8
|
Guanosine 5'-monophosphate oxidoreductase
|
Shigella
|
MRIEEDLKLGFKDVLIRPKRSTLKSRSDVELERQFTFKHSGQSWSGVPIIAANMDTVGTFSMASALASFDILTAVHKHFSVEEWQAFINNSSADVLKHVMVSTGTSDADFEKTKQILDLNPALNFVCIDVANGYSEHFVQFVAKAREAWPTKTICAGNVVTGEMCEELILSGADIVKVGIGPGSVCTTRVKTGVGYPQLSAVIECADAAHGLGGMIVSDGGCTTPGDVAKAFGGGADFVMLGGMLAGHEESGGRIVEENGEKFMLFYGMSSESAMKRHVGGVAEYRAAEGKTVKLPLRGPVENTARDILGGLRSACTYVGASRLKELTKRTTFIRVLEQENRIFNNL
|
Catalyzes the irreversible NADPH-dependent deamination of GMP to IMP. It functions in the conversion of nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and in maintaining the intracellular balance of A and G nucleotides.
|
Q0T894
|
A4FVX8
|
RS19_METM5
|
30S ribosomal protein S19
|
Methanococcus
|
MARQKKYSGKGGARKKNKQKQNVAPRRRVEFKYKGFTLEELQEMPIKKFMEIVPSRQRRTMARGITPKQRKLVMKIKKARRLTNRGKEARVIRTHCRDFVITPEMIGLTFGIYNGKEFKEIKLVEETVGRFLGEMAPTRAVVQHGSPGMGATRGSMFVPIK
|
Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA.
|
A4FVX8
|
Q2P192
|
TRHO_XANOM
|
tRNA hydroxylation protein O
|
Xanthomonas
|
MITNTAAYQFVTIQHPQTLAASVLAQAEQQALKGSVLIAEEGINLFLAGDAEQIGAFYAWLQADARFARMRIKYSESAYQPFARLKVKIKPEIISFRRDDASPLQGRAPSVTPAVLREWLRNGQDDRGRPLVLLDTRNAQEVVYGTFQGALTLPIDTFTELPGALESHRAALADATVVSFCTGGIRCEKAALWMQADGMDNVLQLEGGILGYFEEVGGEGYDGRCFVFDERVALDPELKPLVDAERPAKTGKI
|
Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs.
|
Q2P192
|
P34116
|
G13B_DICDI
|
Cell surface glycoprotein gp138B
|
Dictyostelium
|
MKIILTLSIFLICFLQLGQSVIDPSQNEVMSDLLFNLYGYDKSLDPCNSNSVECDDINSTSTIKTVISLNLPTPLQEYVITQDLTPLQNLTYMELYEKIYLTLSFFKNINKLTQLETIVTLSFNVTIPDDTIFPASLETFSIYKPSVPLSIAIFGSNIKNLYVNSPLTGYSIPTLINVNPYLENLQLPVTYYSGFPSNISLAFPNLQYLTIYVNNDMDQNNYHNFSISNIGVFKNLKGLDIEFTDSYNPQEFSINSFLSNVPVIDSLYIYGQGVTIDPSVGIIDLSYVKSKKFLSINIQESSLLNNCKGKSFKSPKKAYFRSNYNTFSYACIDFSNLAYFYDYYNEYEQYLPNIDNAPLLNEIYISESVVVGDIPESYCRINYLGLNYNQLNGTAPSCILCLGGNRGGDIVLPNPLLNFNKTSEPYCPTFKIDQNYTNLVATDGIGKLIITGTNLGWYGNDITPITANSKLAITIPKGVGTNKSITVTFQNGEQRTFNYSYVPPFIKSYGFLELDSNKYLTINGTGFDFENPNIITINGQQITFSIALGGGDNDGLIALPIDELPNFDSETKFTVSTLVGGQSSNEVTFYYFNSINITEEKLVLNNTGGSVDINGSFGTNNISLVSISINGTNCLVTSYTNSKLTIQYPSKQVGDNYVLTLNVGGYAVNLVVEYIEGGETPTPSTTPSTTPSTTPSTTPSSTPTQSPGDDGSTSSTLSISFYLITLLLLTQQFI
|
Involved in the sexual cell fusion of D.discoideum.
|
P34116
|
P44849
|
Y736_HAEIN
|
Uncharacterized sodium-dependent transporter HI_0736
|
Haemophilus
|
MAHSAPKAQKRETFSGRRAFILAAIGSAVGLGNIWRFPYTTYENGGGAFIIPYLIALLTAGIPLLFLDYAIGHRHRGGAPLSYRRFSPHFEVFGWWQMMVNVIIGLYYAVVLGWAASYTYFSFTGAWGDKPIDFFIGKFLKMGDIKNGISFEFVGMVTAPLIAMWIVALGVLSMGVQKGIAKVSSVLMPVLVVMFMVLVIYSLFLPGAAKGLDALFTPDWSKLSNPSVWIAAYGQIFFSLSIGFGIMVTYASYLKKESDLTGSGLVVGFANSSFEVLAGIGVFAALGFIATAQGQEVSEVAKGGIGLAFFAFPTIINKAPFGEVLGMLFFGSLTFAALTSFISVIEVIISAIQDKIRISRGKVTFIVGVPMMLVSVILFGTTTGLPMLDVFDKFVNYFGIVAVAFASLIAIVANEKLGLLGNHLNETSSFKVGFFWRLCIVLTSGVLAFMLFSEGAKVFSEGYEGYPNWFVNTFGWGMSISLLVVACFLSRLKWKSETKLTIDETKGE
|
Putative sodium-dependent transporter.
|
P44849
|
B4Q2J2
|
UBE2S_DROYA
|
Ubiquitin-protein ligase S
|
Sophophora
|
MSSQYSNVENLSPQTIRQVMRELQEMETTPPEGIKVLINESDVTDIQALIDGPAGTPYAAGVFRVKLTLNKDFPQTPPKAYFLTKIFHPNVAANGEICVNTLKKDWKPDLGIKHILLTIKCLLIVPNPESALNEEAGKMLLERYDDYSQRARMMTEIHAQPAKCGVGASGDAKDDDGPSTKKHAGLDKKLQDKKKEKLLKEKKRMLKRL
|
Catalyzes the covalent attachment of ubiquitin to other proteins. Acts as an essential factor of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated ubiquitin ligase that controls progression through mitosis. Acts by specifically elongating polyubiquitin chains initiated by the E2 enzyme vih/UbcH10 on APC/C substrates, enhancing the degradation of APC/C substrates by the proteasome and promoting mitotic exit.
|
B4Q2J2
|
Q5QW45
|
XGPT_IDILO
|
Xanthine phosphoribosyltransferase
|
Idiomarina
|
MGWHSNREFFVSWEELHRATRELARRQLPAEQYKGIIAVSRGGLVPAAIVSRELNIRVVDCVAVSSYDHTEQRDDLQVMKDVTATEDGEGFLVVDDLVDTGNTMKFLRERLPKAKFVTVYAKPSGMEMVDDFVADLAQDTWIHFPWDMHLHYIEPLAGQES
|
Purine salvage pathway enzyme that catalyzes the transfer of the ribosyl-5-phosphate group from 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to the N9 position of the 6-oxopurines guanine and xanthine to form the corresponding ribonucleotides GMP (guanosine 5'-monophosphate) and XMP (xanthosine 5'-monophosphate), with the release of PPi. To a lesser extent, also acts on hypoxanthine.
|
Q5QW45
|
Q8RI39
|
POTA_FUSNN
|
Spermidine/putrescine import ATP-binding protein PotA
|
Fusobacterium
|
MEKKDINIVNVNKSFDGVQILKDINLKIEQGEFFSIIGPSGCGKTTLLRMIAGFISPDSGAIYLGDENIVNLPPNLRNVNTIFQKYALFPHLNVFENVAFPLRLKKVDEKTINEEVNKYLKLVGLEEHSTKKVSQLSGGQQQRISIARALINKPGVLLLDEPLSALDAKLRQNLLIELDLIHDEVGITFIFITHDQQEALSISDRIAVMNAGKVLQVGTPAEVYEAPADTFVADFLGENNFFSGKVTEIINEELAKINLEGIGEIIIELDKKVKIGDKVTISLRPEKIKLSKNEIKKTKNYMNSAAVYVDEYIYSGFQSKYYVHLKNNEKLKFKIFMQHAAFFDDNDEKAIWWDEDAYITWDAYDGYLVEVESEKK
|
Part of the ABC transporter complex PotABCD involved in spermidine/putrescine import. Responsible for energy coupling to the transport system.
|
Q8RI39
|
Q2SJZ8
|
PURT_HAHCH
|
Phosphoribosylglycinamide formyltransferase 2
|
Hahella
|
MVRIGTPLTDVATRAMLLGSGELGKEVAIELQRFGVEVIAVDRYSNAPAMQVAHRAHVIDMLDPKQLRALIELERPDFIIPEIEAIATAELLELERSGFNVVPSARAANLTMNREGIRRLAAEELGLSTSPYAFAADFESFRDAVSSIGVPCVVKPIMSSSGKGQSVIHSDGDVERAWRYAQEGGRAGQGKVIVEGFVDFDYEVTLLTLRHAGGTSFCDPIGHLQVDGDYRVSWQPHPMSAIALGAAQDIAEKVTVALGGCGIFGVELFVKGDEVYFSEVSPRPHDTGLVTLVSQNLSEFALHARALLGLPVPLIKQTGASASVALLVEGDSSRVCFSSLEAALCHPEVQLRLFGKPEVHGKRRMGVVLAQSENLDEARKLAQKAVDSIVVELGPDIKQE
|
Involved in the de novo purine biosynthesis. Catalyzes the transfer of formate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR). Formate is provided by PurU via hydrolysis of 10-formyl-tetrahydrofolate.
|
Q2SJZ8
|
Q6FV04
|
RU2A_CANGA
|
U2 small nuclear ribonucleoprotein A'
|
Nakaseomyces/Candida clade
|
MKFTPGAVEDAPSYYVDHDNGKYNTQKCVILRNLGLEGDDIAMPASLNHLAKPTHILDLTNNDLVFFPDLHHRDDIETLLLSKNRLMVLDAALLPSKLKSLSLAFNGIENFETLIPLSHCPSTVRDLVLIGNPICHLSEYRQRILALVPSLEVLDFKLVSQAEKAQAVKDHVAVMKKIKEDNRQIHQRKKKALAAEVDGKNTFGRNTKSLTEAAKVTKPRDKTIEVMNTVVGKLTEEKKKKIREQLANASSMEELERLERLLTGGV
|
Involved in pre-mRNA splicing.
|
Q6FV04
|
O74311
|
NAA30_SCHPO
|
NatC catalytic subunit
|
Schizosaccharomyces
|
MVTIVPYSHQYLKDICQLIQKDLSEPYSKYVYRYFVHQWPEFSFVALDNDRFIGAVICKQDVHRGTTLRGYIAMLAIVKEYRGQGIATKLTQASLDVMKNRGAQEIVLETEVDNEAAMSFYERLGFCRYKRLYRYYLNGTDAFRYILYPN
|
Catalytic component of the NatC N-terminal acetyltransferase.
|
O74311
|
B9DX64
|
ATPD_CLOK1
|
F-type ATPase subunit delta
|
Clostridium
|
MYEYLDRRYALALYKIAEEKGKVEEYLEELKDVTDIINNDTQFLEFIEHPEISTAEKKKTFINVFKGKISEDILSFLLILIDKGRINQLYSKLKEMGKIYLENHNTVIATVKTVIPLEDDERETLTEKLRRKFNKEVLIKEELDPEIIGGVYVEVNNMVIDGTVKSKLSEMKKIMLKGEQR
|
This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction.
|
B9DX64
|
Q7U6W9
|
PCXA_PARMW
|
Proton extrusion protein PcxA
|
Parasynechococcus marenigrum
|
MAARNWIGLFSRGEGNNLTNALERGYEAALLIQSLELEFYADRKVRPELELSVPRSVQATVLRRFHAALQICRSSLSTVTPNRGQLDPQELRQLQLIETVVSRYSGKRSSSKSGMSTAPELLPRSLLGVFDSVRRQLDPSSEESVVAGFRRRRDSTLASLRILLLLVLVPLLVQQVSNTYIVGPAVERLSPDLSFLSYPKPQLEEVAVEKLRIYKEELEFDALLKGQEPLSSDLLVIKLRERAQELKQEADQESVQAIKNVLADLAGLMAFVVVCLVSRDQLRVLRGFLDEAIYGLSDSAKAFAIILFTDIFVGYHSPEGWTVLLDGIAHHFGLPTQENFILLFIATFPVILATIFKYWIFRYLNRVSPSSVATLKGMNGGG
|
Involved in light-induced Na(+)-dependent proton extrusion. Also seems to be involved in CO(2) transport.
|
Q7U6W9
|
Q8PNI0
|
GLO2_XANAC
|
Glyoxalase II
|
Xanthomonas
|
MRLIALPAFDDNYIWALVAADGRAIIVDPGQAEPVLAAAQRQGLVPSAVLLTHHHGDHIGGVAELQQRWPDLALFGPADERIPTNAHHVGRGERLRLLDVEFQVIKVPGHTRSHIAFLADGHLFSGDTLFSLGCGRMFEGTAPQMFDSLQRLASLPGETLVCCGHEYTLANAAFALHVDPTNAALQRRQQEAQAMRHAARPTLPISLKSELATNPFLRTSHPEIRAAVAPRAASALSSEVDIFAELRRWKDEFRA
|
Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
|
Q8PNI0
|
D2Y2B4
|
H13A6_CYRHA
|
Hainantoxin-XIII.6
|
Haplopelma
|
MKTAIFTVVLALAVFAVLSFGWEANEKALSEEFTELIHEKEAASEAEARECRYFWGECHDHMPCCDWLVCRYKWPITYNICVWNRTFPEK
|
Ion channel inhibitor.
|
D2Y2B4
|
A1QZ99
|
MRAY_BORT9
|
UDP-MurNAc-pentapeptide phosphotransferase
|
Borrelia
|
MFCLLGLRLLKYITFRTAYATIFAFLLALIFGPFIILRLKKLKLDQILRKDGPKRHLSEKIGIPTMGGILIFFCVLVSLFFWIDFWNIYFLIILFVMVSFACLGFMDDLLKIKRKNSDGLNPRFKIYGQILFSCISVTMLYYFGDEHVSIIYFPFFKSLKLDLGVLYIPFGMFILISASNSFNLTDGLDGLAIGLSIVVTGALVIIAYLASRVDFAFYLNIPNIKGAEELVVFLGALLGGSFGFLWFNAYPAKIMMGDTGSLSIGAVLGMTALILKSEILFAILAGVFVVETLSVIIQVVVYKHTKKRVFKMAPLHHHFEELGWSEMQVVIRFWIIGLIFAIIALSTLKIR
|
Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I.
|
A1QZ99
|
Q8TJZ5
|
CFBA_METAC
|
Sirohydrochlorin nickelchelatase
|
Methanosarcina
|
MTEKLGILAIGHGSKLPYNKEVVSQIADYIAQKHSDVVVRAGFMENSEPTLEEAIAGFAGTGVTKIAAVPVFLASGVHITKDIPGILSLDEKGCGILNIDGKDVPLCYAKPLGADELIADLVFKRVQEAL
|
Catalyzes the insertion of Co(2+) into sirohydrochlorin as part of the anaerobic pathway to cobalamin biosynthesis (Potential). Involved in the biosynthesis of the unique nickel-containing tetrapyrrole coenzyme F430, the prosthetic group of methyl-coenzyme M reductase (MCR), which plays a key role in methanogenesis and anaerobic methane oxidation . Catalyzes the insertion of Ni(2+) into sirohydrochlorin to yield Ni-sirohydrochlorin .
|
Q8TJZ5
|
A3CMJ2
|
LEUC_STRSV
|
Isopropylmalate isomerase
|
Streptococcus
|
MAGKSIFDKLWERHLITGEEGQPQLMYVDQHYIHEVTSPQAFQGLRDAGRKVRRPDLTFGTFDHNVPTVNIYDIRDVISKAQIDKLSENVKDFGIEHAAHGSELQGIVHMVGPETGKTQPGKFIVCGDSHTATHGAFGAIAFGIGTSEVEHVFATQTIWQVKPKKMLVKFTGVPPKGVYSKDFILALIARYGVAAGVGHVVEYAGDAIDHLTMEERMTICNMSIEFGSKMGIMNPDQKTYDYVKGRPGAPKDFEAAVADWKTLVSDPDAVYDKVIEIDVSELAPMVTWGTNPSMGVEFGAAFPEIRDMNDERAYNYMDLSPGKKAEDIDLGYIFIGSCTNARLSDLQLAAKFVAGKHIAPNLTAIVVPGSRPVKRAAEKMGLDKIFMDAGFEWRDPGCSMCLGMNPDKVPDGVHCASTSNRNFEDRQGFGAKTHLCSPAMAAAAAIAGRFVDVRQLPEVQ
|
Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
|
A3CMJ2
|
B0TLA6
|
RECF_SHEHH
|
DNA replication and repair protein RecF
|
Shewanella
|
MSLTRLHIETFRNISLAQLDPGDGLNLIYGQNGSGKTSILEAIYFLGMGRSFRSHLSQRVIQHNDDKLTLFANLSVCEQESKIGLRRFRNGETEVKINGDNIKRLSTLAETLPIQVITPESFSLLFEGPKSRRQFIDWGAFHSDKSFHLAWANVRRILKQRNQLLKNQVSYSQIQYWDKELVRYSEQVTEIRKQYVDSLNEQLKGIIGEFLPLVEVKVSFTRGWDSKTDFGQLLETQYLRDVAAGNTGSGPHKADLRLRVGVLPVQDALSRGQLKLLVCALRIAQGKLLKQQTDKNSIYLVDDLPSELDAQHRKLLLQQLMDTGAQVFVTAIEPAAIVDSLATPPSKMFHVEQGCVTVIDKPTRE
|
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.
|
B0TLA6
|
Q1QIN5
|
LPXK_NITHX
|
Lipid A 4'-kinase
|
Nitrobacter
|
MHEPAFWHRPSSLLSRLLMPVGALYGAVAARRLMRTGMRAGVPVICVGNYHVGGAGKTPTVIALAGILRSLGETPVVLSRGYGGRLHGPVHVDPHRHTAADVGDEPLMMAWTIPVIVSRQRAAGIAPARALGASVILMDDGFQNPALAKDISLIVIDRARGLGNGQVFPAGPLRAPLPPQLARTDALVIVGFGPAADDVAASIGARGGLVLPARLIPDDASVVALRGRRVYAFAGIGDPQRFFRSLRACGIDVAAERAFPDHHPFSQRDVADLQTAAERDGLTLVTTEKDLARLRNSEDLAAFAQAVVAFAVTLAFDDEAVLRSFLTDRIGRARR
|
Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA).
|
Q1QIN5
|
Q39230
|
SYSC_ARATH
|
Seryl-tRNA(Ser/Sec) synthetase
|
Arabidopsis
|
MLDINLFREEKGNNPEIIRESQRRRFASVEIVDEIIKLDKEWRQRQFEVDSFRKEFNKLNKQVAQLKIKKEDASEIIQQTEKNKQDSTAKEAEVREAYAALKAKLEQVGNLVHDSVPVDKDEANNLVIKLWGEKRFSTPGLKLKNHVDLVELLGIADTKRGAEIAGARGFFLKGDGLMLNQALINFGLTFLKKRGFTGLQPPFFMRKDVMAKCAQLAQFDEELYKVTGEGDDKYLIATAEQPLCAYHIDEWIHPTELPLRYAGYSSCFRKEAGSHGRDTLGIFRVHQFEKIEQFCITGPNENASWEMLDEMMKNSEDFYQALKLPYQIVSIVSGALNDAAAKKYDLEAWFPSSETFRELVSCSNCTDYQARRLEIRYGQKKSNEQTKQYVHMLNSTLTATERTICCILENYQREDGVDIPEVLQPFMGGETFLPFKAKPVVADTKGKKSKA
|
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).
|
Q39230
|
Q7Z624
|
CMKMT_HUMAN
|
Calmodulin-lysine N-methyltransferase
|
Homo
|
MESRVADAGTGETARAAGGSPAVGCTTRGPVVSAPLGAARWKLLRQVLKQKHLDDCLRHVSVRRFESFNLFSVTEGKERETEEEVGAWVQYTSIFCPEYSISLRHNSGSLNVEDVLTSFDNTGNVCIWPSEEVLAYYCLKHNNIFRALAVCELGGGMTCLAGLMVAISADVKEVLLTDGNEKAIRNVQDIITRNQKAGVFKTQKISSCVLRWDNETDVSQLEGHFDIVMCADCLFLDQYRASLVDAIKRLLQPRGKAMVFAPRRGNTLNQFCNLAEKAGFCIQRHENYDEHISNFHSKLKKENPDIYEENLHYPLLLILTKHG
|
Catalyzes the trimethylation of 'Lys-116' in calmodulin.
|
Q7Z624
|
A6U6T5
|
PDXH_SINMW
|
Pyridoxal 5'-phosphate synthase
|
Sinorhizobium
|
MTANELTTGDFTEASEPFSLFGTWLKEAEKSEVNDPNAVALATVDPDGMPNARMVLLKGFDERGFVFYTNFESQKGQEILATRKAAMCFHWKSLRRQVRLRGPVEVVPDVEADEYFVSRPRGSRIGAWASKQSRPLESRFALEKAVAEYTARHAIGEIPRPDYWSGFRIRPLSIEFWHDRPFRLHDRLEFRRKAPDGDWTKVRMYP
|
Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
|
A6U6T5
|
Q9SZA4
|
CDC21_ARATH
|
Cell division cycle 20.1, cofactor of APC complex
|
Arabidopsis
|
MDAGMNNTSSHYKTQARCPLQEHFLPRKPSKENLDRFIPNRSAMNFDYAHFALTEGRKGKDQTAAVSSPSKEAYRKQLAETMNLNHTRILAFRNKPQAPVELLPSNHSASLHQQPKSVKPRRYIPQTSERTLDAPDIVDDFYLNLLDWGSANVLAIALDHTVYLWDASTGSTSELVTIDEEKGPVTSINWAPDGRHVAVGLNNSEVQLWDSASNRQLRTLKGGHQSRVGSLAWNNHILTTGGMDGLIINNDVRIRSPIVETYRGHTQEVCGLKWSGSGQQLASGGNDNVVHIWDRSVASSNSTTQWLHRLEEHTSAVKALAWCPFQANLLATGGGGGDRTIKFWNTHTGACLNSVDTGSQVCSLLWSKNERELLSSHGFTQNQLTLWKYPSMVKMAELTGHTSRVLYMAQSPDGCTVASAAGDETLRFWNVFGVPETAKKAAPKAVSEPFSHVNRIR
|
Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle.
|
Q9SZA4
|
A0ZZ20
|
ATPA_GOSBA
|
F-ATPase subunit alpha
|
Gossypium
|
MVTIRADEISNIIRERIEQYNREVKIVNTGTVLQVGDGIARIHGLDEVMAGELVEFEEGTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGKIAQIPVSEAYLGRVINALAKPIDGWGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIFGDRQTGKTAVATDTILNQQGQNVICVYVAIGQKASSVAQVVTTFQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRERHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKSSSQLGEGSMTALPIVETQSGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKSKLELAQFAELEAFAQFASDLDKATQNQLARGQRLRELLKQSQSAPLTVAEQISTIYTGTNGYLDSLEIGQVRKFLVELRTYLKTNKPQFQEIISSTKTFTEEAETLLKDAIQDQMERFRLQEQL
|
Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
|
A0ZZ20
|
B1AHY7
|
DNAA_UREP2
|
Chromosomal replication initiator protein DnaA
|
Ureaplasma
|
MANNYQTLYDSAIKRIPYDLISDQAYAILQNAKTHKVCDGVLYIIVANAFEKSIINGNFINIISKYLSEEFKKENIVNFEFIIDNEKLLINSNFLIKETNIKNRFNFSDELLRYNFNNLVISNFNQKAIKAIENLFSNNYDNSSMCNPLFLFGKVGVGKTHIVAAAGNRFANSNPNLKIYYYEGQDFFRKFCSASLKGTSYVEEFKKEIASADLLIFEDIQNIQSRDSTAELFFNIFNDIKLNGGKIILTSDRTPNELNGFHNRIISRLASGLQCKISQPDKNEAIKIINNWFEFKKKYQITDEAKEYIAEGFHTDIRQMIGNLKQICFWADNDTNKDLIITKDYVIECSVENEIPLNIVVKKQFKPEQIIEIVAKELNIKTDLIKSSIRKNNIVWARDIVCYILKNKLNLTLTDIGKLLNGREHTTISHSISKVQKILDDENSQEALQINLIINKF
|
Plays an important role in the initiation and regulation of chromosomal replication. Binds to the origin of replication; it binds specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'-TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids.
|
B1AHY7
|
A2RI74
|
DPPA_LACLM
|
Dipeptide-binding protein
|
Lactococcus cremoris subsp. cremoris
|
MKQAKIIGLSTVIALSGIILVACGSKTSEQKNIQFSIPTDVASLDTTILTDQYSYDVAGNVEEGLTRVDSKGNAALALAKSIDVSKDGLTYTVTLKDNLKWSNGDKLTAKDFVYSWKRAVDPKTGSEYAYLMGAVSGANDIISGKSSLDTLGIKAESDTEFTVTLAQPTPYFKFLLSEPVYYPLDQKVVDKYGKQYGTSSDKTVYNGPFMFKSDKAWTGTNKNFSIYANPNYYDKSAVKSKQIDFQVISNANTGAQLYKQGKLDFTLLSTTDLINANKKTEGYTVFKQARTDYIEYNQSGKNASSPDAQKALANQDIRQALNLATNRAEVVKTALPGSTAATSFTPVGMSKTSTGEDFATYAKQDYSYDPTKAKELWAKGLKELGLTKLSLSLEAAGDLAPSEATANFLQTAYQQNLPGLTVNLKLVPFKQRLNDAQNGNFDMVLSGWGGDYAEPSTFLQLFTTGQSYNDGKFSSKTYDDAFKAATTTPDVLEPAKVDEHYKAAEAALYEGSYINPIDFQANPALMNPKITGLEFHSTGLAYDLKSAYIK
|
Part of the ABC transporter DppABCDF involved in dipeptide transport . Binds di- and tripeptides with high affinity. Requires a free N-terminal alpha-amino group and an alpha-peptide bound contiguous with the N-terminal amino group, has a strong selectivity for L-residues, and shows preference for dipeptides containing methionine or arginine, followed by hydrophobic tripeptides consisting of leucine or valine residues .
|
A2RI74
|
P43187
|
ALLB3_BETPN
|
Allergen Bet v III
|
Betula
|
MPCSTEAMEKAGHGHASTPRKRSLSNSSFRLRSESLNTLRLRRIFDLFDKNSDGIITVDELSRALNLLGLETDLSELESTVKSFTREGNIGLQFEDFISLHQSLNDSYFAYGGEDEDDNEEDMRKSILSQEEADSFGGFKVFDEDGDGYISARELQMVLGKLGFSEGSEIDRVEKMIVSVDSNRDGRVDFFEFKDMMRSVLVRSS
|
Could be involved in calcium metabolism in pollen. Binds 3 calcium ions.
|
P43187
|
P01111
|
RASN_HUMAN
|
Transforming protein N-Ras
|
Homo
|
MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNSKSFADINLYREQIKRVKDSDDVPMVLVGNKCDLPTRTVDTKQAHELAKSYGIPFIETSAKTRQGVEDAFYTLVREIRQYRMKKLNSSDDGTQGCMGLPCVVM
|
Ras proteins bind GDP/GTP and possess intrinsic GTPase activity.
|
P01111
|
Q9HNI2
|
GLNA_HALSA
|
Glutamine synthetase I alpha
|
Halobacterium
|
MTNGDSSSSALTDNERAVLDDIEAQGIDFLRLQFTDILGTVKNVSIPAHQAEKAFTEGIYFDGSSIEGFVRIQESDMRLDPDPETFAVLPWRSNGDGGSARLICDVVDREGNAFAGGPRQVLKNVLARADDMGYSVSIGPEPEFFLFEKDDDGNATTTAHDQGGYFDLAPKDLASDIRREIIFTLEAMGFEIEASHHEVARGQHEINFKYDDALTTADNIATFRAVVRAVAEQHDVHATFMPKPIGEINGSGMHSHISLFDEDGENVFADNDDEFNLSETAYQFMGGVLEHAPAFTAVTNPTVNSYKRLVPGYEAPVYIAWSGVNRSALIRVPDAAGVSARFEIRSPDPSCNPYLALAAVIAAGLDGIDTDADPGDAVREDIYEFDEDKRDAYGIDTLPGHLGDAVTALESDPVMQDALGEHVCEKFAEAKRHEYAEYKASVSEWETDRYLEKF
|
Glutamine synthetase (GS) is an unusual multitasking protein that functions as an enzyme, a transcription coregulator, and a chaperone in ammonium assimilation and in the regulation of genes involved in nitrogen metabolism. It catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia. Feedback-inhibited GlnA also interacts with and regulates the activity of the transcriptional regulator TnrA. During nitrogen limitation, TnrA is in its DNA-binding active state and turns on the transcription of genes required for nitrogen assimilation. Under conditions of nitrogen excess, feedback-inhibited GlnA forms a stable complex with TnrA, which inhibits its DNA-binding activity. In contrast, feedback-inhibited GlnA acts as a chaperone to stabilize the DNA-binding activity of GlnR, which represses the transcription of nitrogen assimilation genes.
|
Q9HNI2
|
G1CWH8
|
CYC12_CLITE
|
Cliotide T12
|
Clitoria
|
MASLRIAPLALFFFLAASVMFTVEKTEAGIPCGESCVFIPCITGAIGCSCKSKVCYRDHVIAAEAKTMDDHHLLCQSHEDCITKGTGNFCASFPEQDIKYGWCFRAESEGFMLKDHLKMSVPN
|
Probably participates in a plant defense mechanism.
|
G1CWH8
|
Q8K989
|
CLPX_BUCAP
|
ATP-dependent Clp protease ATP-binding subunit ClpX
|
Buchnera
|
MTDKSKDNSKKLLQCSFCGKNQKEVKKLIAGPAVYICDECIRLCNNIIQETKTTKKIEDDELSYLPTPHEIKKHLDNYVIGQNHTKKVLSVAVYNHYQRIRNVSKNKDNVELGKSNILLIGPTGSGKTLLAETLAKLLNVPFSIADATTLTEAGYVGEDVENVIQKLLQKCEYNVKKAELGIVYIDEIDKISRKSDNPSITRDVSGEGVQQALLKLIEGTLASIPPQGGRKHPQQEFLQVNTANILFICAGAFSELSKIISKRIDTGNTIGFNCNLKKQKKKKSEQYFLQQVQSKDLIKFGLIPEFIGRLPIITILKELNETALVQILCKPKNALIKQYQTLFNLEKVKLEFTKEAVTSIAKKALSKKTGARGLRSIIENILLDIMYELPSMKNVEKILIDESVVNSHSLPKIIYEEKNKSKKASGE
|
ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP.
|
Q8K989
|
Q1LZB3
|
S2533_BOVIN
|
Solute carrier family 25 member 33
|
Bos
|
MATGTQQKENTLLHLFAGGCGGTVGAIFTCPLEVIKTRLQSSRLALRTVYYPQVHLGTISGAGVVRQTSVTPGLLQVLKSILEKEGPRSLFRGLGPNLVGVAPSRAVYFACYSKAKEQFNGVFVPNSNIVHVFSAGSAAFVTNSLMNPIWMVKTRMQLERKVRGSKQMNTLQCARYVYQTEGIRGFYRGLTASYAGISETIICFAIYESLKKYLKEAPLASSTNGTEKNSTNFFGLMAAAALSKGCASCVAYPHEVIRTRLREEGSKYKSFVQTARLVFREEGYLAFYRGLFAQLIRQIPNTAIVLSTYELIVYLLEDHAQ
|
Mitochondrial transporter that imports/exports pyrimidine nucleotides into and from mitochondria. Transports preferentially uracil, thymine, and cytosine (deoxy)nucleoside di- and triphosphates by an antiport mechanism. Also transports guanine but not adenine (deoxy)nucleotides. Is inhibited strongly by pyridoxal 5'-phosphate, 4,7-diphenyl-1,10-phenanthroline, tannic acid, and mercurials (mercury dichloride, mersalyl acid, p-hydroxymercuribenzoate). Participates in mitochondrial genome maintenance, regulation of mitochondrial membrane potential and mitochondrial respiration. Upon INS or IGF1 stimulation regulates cell growth and proliferation by controlling mitochondrial DNA replication and transcription, the ratio of mitochondria-to nuclear-encoded components of the electron transport chain resulting in control of mitochondrial ROS production. Participates in dendritic cell endocytosis and may associate with mitochondrial oxidative phosphorylation.
|
Q1LZB3
|
Q8D795
|
FABV2_VIBVU
|
Enoyl-[acyl-carrier-protein] reductase [NADH] 2
|
Vibrio
|
MRIEPIIQGVVARSAHPFGCEAAIKKQIAFVKNAPQISQGPKRVLILGASSGFGLAARIALTFGGAQADTIGVSFERGPSEKGTGSAGWYNNVFFKREAEKEGRIAINIVGDAFASETRTQVIEAIETYFEGEVDLVIYSLATGMRPISNQPGEFWRSVIKPFGQTVTGASFDLEHDRWIDTTLESATEEEALHTIKVMGGEDWESWIDTLINAESIAQGCQTIAFSYVGPEITHPIYLDGTLGRAKIDLHQTSHSLNLKLANFDGAAYATVCKALVTKASVFIPALSPYLLALYRVMKDEKCHEGCIEQMQRLFATKLYGQDHISVDGERLVRMDDWELAPHIQNKVNQILEEMDANNFQVIGDYQGFKNEFLQLNGFGFDEVDYSQDIDLQTILKLTP
|
Involved in the final reduction of the elongation cycle of fatty acid synthesis (FAS II). Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP).
|
Q8D795
|
A3N319
|
RL7_ACTP2
|
50S ribosomal protein L7/L12
|
Actinobacillus
|
MSLTNEQLIEAIASKSVSEIVELIAAMEEKFGVSAAAAVAAAPAAGAAAAEEKTEFDVILAEAGANKVAVIKAVRGATGLGLKEAKDLVESAPAALKEGISKPEAEALKKELEEAGAKVEIK
|
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation.
|
A3N319
|
B8ZNX4
|
COAD_STRPJ
|
Pantetheine-phosphate adenylyltransferase
|
Streptococcus
|
MSDKIGLFTGSFDPMTNGHLDMIERASRLFDKLYVGIFFNPHKQGFLPLENRKRGLEKAVKHLGNVKVVSSHDELVVDVAKRLGATCLVRGLRNASDLQYEASFDYYNHQLSSDIETIYLHSRPEHLYISSSGVRELLKFGQDIACYVPESILEEIRNEKKD
|
Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
|
B8ZNX4
|
Q631P8
|
MURB2_BACCZ
|
UDP-N-acetylmuramate dehydrogenase 2
|
Bacillus cereus group
|
MNMQEVYEYLSTVLPEGHVKQDEMLKNHTHIKVGGKADVFVAPTNYDEIQEVIKYANKYNIPVTFLGNGSNVIIKDGGIRGITVSLIHITGVTVTGTTIVAQCGAAIIDVSRIALDHNLTGLEFACGIPGSVGGALYMNAGAYGGEISFVLTEAVVMTGDGELRTLTKEAFEFGYRKSVFANNHYIILEARFELEEGVHEEIKAKMDDLTFKRESKQPLEYPSCGSVFKRPPNNFAGKLIQDSGLQGKRIGGVEVSLKHAGFMVNVDNGTAQDYIDLIHFVQKTVEEKFGVKLEREVRIIGEDKE
|
Cell wall formation.
|
Q631P8
|
B9L1Z5
|
FPG_THERP
|
DNA-(apurinic or apyrimidinic site) lyase MutM
|
Thermomicrobium
|
MPELPEVETIRRTLAPVLIGALVIGALRGEHPEDILLDPWPVFARRVRRHRIVALERRGKYLAARFEDGDRLVIHLGMTGELRLSHPATAPGKHCHLALVLRSLRPLPPSLVDQRQRFLLRYLDIRRFGRIALLDQAGWETFTARLGPEPLDPTLDPRALWSRLRERRTAIKAALLDQALLAGIGNIYADEALFQARLHPARRCQTLSLDEVERLLVALRTVLSAAIENAGTTIRDYRDGQGRAGSFQSRLQVYGKPAGTPCPRCGTGLARIRIAGRSSVFCPRCQPLH
|
Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates.
|
B9L1Z5
|
Q4A5Y8
|
RL7_MYCS5
|
50S ribosomal protein L7/L12
|
Mycoplasmopsis
|
MAKLTKETFVESLKEMSIKEVMELVEAMKEEFGVDPAAAVAVAAAPGEAAEAAKTSVKVVLKADNGKKVQIIKAVKDLLGGSLMDAKKIVDNLPAVVKENIKPEEAEPIRAALVEAGAEVSVE
|
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation.
|
Q4A5Y8
|
Q1RHA4
|
ERA_RICBR
|
GTPase Era
|
belli group
|
MTKQIQKTVSVCIIGRPNSGKSTLLNRIIGEKLSIVTPKVQTTRSIITGIITLNDTQIILYDTPGIFEPKGTLEKAMVRCAWSSLHSADIVMLIIDSLKPLDSITHDILNKLRSLNVVPVFLLNKIDVESKYIDDTKAFLAENYSDSLLFPISAISGENVDKLLEYITSKAKIAPWLYEEDDITDLPMRFIAAEITREQLFLGLQQELPYKLTVQTEKWEELKDKSVKINQIIVVSRESYKTIILGKNGSKIKELGAKSRMQMQQFFGFPVHLFLFVKVQELWEDNSDYYEYMKI
|
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.
|
Q1RHA4
|
B1YHQ9
|
PANB_EXIS2
|
Ketopantoate hydroxymethyltransferase
|
Exiguobacterium
|
MHTMTPLLKKQQAGEKLVMLTAYDYPSAKLAEAGHVDLLLVGDSLGNVILGYDSTIAVTVDDMVHHAKAVRRGAPATFMVVDMPFASYHGSFDRTLEAAARIFQESGADALKLEGAGDILTTIRRLTEAGMPCVAHLGLTPQSVGVLEGFKVQGKSLAAAEQLIADSLAAEQAGAKMLVLECVPHPLAKRVQELLTIPVIGIGAGADVAGQVLVYHDILTYGVGRLPKFVKAYADWNTSGTEAIARYVEDVKNGTFPELAHSFLMDEELIGALYGGFKE
|
Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
|
B1YHQ9
|
B8EAI0
|
PDXH_SHEB2
|
Pyridoxal 5'-phosphate synthase
|
Shewanella
|
MTDLSDIRREYAKGGLRRADLPQNPMDLFELWMTQARDAELSDPTAMCVATVDEHGQPFQRIVLLKRFDDTGFVFFTNLGSRKAQQIAANNKVSLHFPWHPLERQVSVLGEAQALSTAEVLKYFMTRPKDSQIAAWVSQQSSKLSARQVLEGKFFEMKAKFAKGDVPLPSFWGGYLVRPSSIEFWQGGEHRLHDRFIYARHDAEWEIDRLAP
|
Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
|
B8EAI0
|
Q83HZ6
|
PYRH_TROW8
|
Uridine monophosphate kinase
|
Tropheryma
|
MASRRVLLKLSGESFGGGAPLVDPDVVSAIASEIVRVSKTIQIAIVVGGGNYFRGAELSRRGMARDRADYMGMLGTVINALALQDFLEQAGGDTRVQSAISMSQVAELYVPRRAERHLTKGRVVIFAAGAGMPYFSTDTVAVQRALEIKADIVLIAKNGVDGVYTDDPQINPNAKKIYKITYREALERGLRVVDSAALGLCMEHGLPMRVFGMESLRDAVSGLKVGTELSQ
|
Catalyzes the reversible phosphorylation of UMP to UDP.
|
Q83HZ6
|
Q0KE78
|
RECA_CUPNH
|
Recombinase A
|
Cupriavidus
|
MDDKKAGAGVSAEKQKALAAALSQIEKQFGKGSIMRLGDGEVEKDIQVVSTGSLGLDIALGVGGLPRGRVVEIYGPESSGKTTLTLQVVAEMQKLGGTCAFIDAEHALDVSYANKLGVNVGDLLISQPDTGEQALEITDALVRSGSIDLIVIDSVAALVPKAEIEGEMGDSLPGLQARLMSQALRKLTGTIKRTNCLVIFINQIRMKIGVMFGSPETTTGGNALKFYASVRLDIRRIGSIKKGDDVIGNETKVKVVKNKVSPPFREAFFDILYGQGISRQGEIIDLGVDAKIVEKSGAWYSYNGDKIGQGKDNAREYLRENPDIADEIENKVRAALGVVAMNPTAAATPVAVED
|
Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage.
|
Q0KE78
|
Q8DEQ3
|
TRMN6_VIBVU
|
tRNA m6A37 methyltransferase
|
Vibrio
|
MKSGTLKTKGFKFKQFSIASSNSGMPVSTDGVLLGAWADFHHCQNLLDIGTGTGLLSLMCAQRYVHLSITAVDIDAHAMEAAQENFSHSPWHSRLQLQHGDVLKLNFTHRFDGIICNPPYFNSGEQAQATQRATARHTDTLAHDALLLRCRELLTPNGKANFVLPLTEGEQFLQLAQQQGWHLHRLCRVKPSPNKPVHRLLFELGLSTATTSEEHLTINDGSTYSAAFVKLCQDFYLKM
|
Specifically methylates the adenine in position 37 of tRNA(1)(Val) (anticodon cmo5UAC).
|
Q8DEQ3
|
P07951
|
TPM2_HUMAN
|
Tropomyosin-2
|
Homo
|
MDAIKKKMQMLKLDKENAIDRAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKEAQEKLEQAEKKATDAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDRKYEEVARKLVILEGELERSEERAEVAESKCGDLEEELKIVTNNLKSLEAQADKYSTKEDKYEEEIKLLEEKLKEAETRAEFAERSVAKLEKTIDDLEDEVYAQKMKYKAISEELDNALNDITSL
|
Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments. The non-muscle isoform may have a role in agonist-mediated receptor internalization.
|
P07951
|
Q8D8V3
|
HCP_VIBVU
|
Prismane protein
|
Vibrio
|
MFCIQCEQTIQTPAVKGCSFAQGMCGKTAEVSDLQDVLVYSLQGVSYWATQAHRYGIINDEINQWAPKAFFSTLTNVNFDPERILQLTSQAAQFKAQLKDQVLTASSLANSPLSEVPAVAEFELPENAQAILAFAPQVAVNRGKEGVHEDVIGLRLLCLYGLKGAAAYMEHARVLEQTNNDIYAEYHEIMAWLGTDPEDLGELLDCSMRIGLMNYKVMEMLDHGETATFGHPVPTAVNVKPVKGKCILVSGHDLHDLEKILQQTEGKGINVYTNGEMLPAHGYPELNKYPHLVGNYGSAWQNQQKEFANFPGAIVMTSNCLLNPNVGQYADRLFTRSIVGWPGVAHIEDDDFSAVIESALAQPGFQHDEIEHMITVGFGRNALMNAAPAVIDQVKQGNIKHFFLVGGCDGDKAERSYYTDFTEAAPEDTLILTLACGKFRFNKNTFGDINGIPRLLDVGQCNDAYSAIQLALALAQEFDCGINELPLTLVLSWFEQKAIVILLTLFALGVKGIYTGPTAPAFLTPNLIAIIQEKFDMRSIGNVQDDLNTILAA
|
Catalyzes the reduction of hydroxylamine to form NH(3) and H(2)O.
|
Q8D8V3
|
Q8GYD9
|
SDE3_ARATH
|
Silencing defective protein 3
|
Arabidopsis
|
MSVSGYKSDDEYSVIADKGEIGFIDYQNDGSSGCYNPFDEGPVVVSVPFPFKKEKPQSVTVGETSFDSFTVKNTMDEPVDLWTKIYASNPEDSFTLSILKPPSKDSDLKERQCFYETFTLEDRMLEPGDTLTIWVSCKPKDIGLHTTVVTVDWGSDRVERVVFLLAEDKISSSLTSNRPYSRSRRAPKKDFAVDDYVKGSRPSKVVERSFRNRLPLYEIPKEIREMIENKEFPDDLNEGLTARNYANYYKTLLIMEELQLEEDMRAYDMENVSMKRRGIYLSLEVPGLAERRPSLVHGDFIFVRHAYDDGTDHAYQGFVHRVEADEVHMKFASEFHQRHTAGSVYNVRFTYNRINTRRLYQAVDAAEMLDPNFLFPSLHSGKRMIKTKPFVPISPALNAEQICSIEMVLGCKGAPPYVIHGPPGTGKTMTLVEAIVQLYTTQRNARVLVCAPSNSAADHILEKLLCLEGVRIKDNEIFRLNAATRSYEEIKPEIIRFCFFDELIFKCPPLKALTRYKLVVSTYMSASLLNAEGVNRGHFTHILLDEAGQASEPENMIAVSNLCLTETVVVLAGDPRQLGPVIYSRDAESLGLGKSYLERLFECDYYCEGDENYVTKLVKNYRCHPEILDLPSKLFYDGELVASKEDTDSVLASLNFLPNKEFPMVFYGIQGCDEREGNNPSWFNRIEISKVIETIKRLTANDCVQEEDIGVITPYRQQVMKIKEVLDRLDMTEVKVGSVEQFQGQEKQVIIISTVRSTIKHNEFDRAYCLGFLSNPRRFNVAITRAISLLVIIGNPHIICKDMNWNKLLWRCVDNNAYQGCGLPEQEEFVEEPFKQEGSSNGPQYPPEAEWNNSGELNNGGANENGEWSDGWNNNGGTKEKNEWSDGWNSNGGGTKKKDEWSDGWDNNGGTNGINQEGSSNAPQDPQEAEWNDSGEVKNGGTKEKDVRSDGWNNNGGKNEKEECCDGWKDGGSGEEIKNGGKFETRGDFVAKEEDEWSDGWK
|
Probable RNA helicase required for post-transcriptional gene silencing (PTGS), a process that provides protection in plants against virus infection and can suppress expression of transgenes. Plays a central role in RNA interference (RNAi) process, a process that mediates mRNA destruction of translational repression. Required for the assembly of the RISC complex, a complex required for target RNA destruction or repression. May be required in the RISC assembly to unwind miRNAs, in the production of single-stranded miRNA from the double-stranded miRNA, a key step in RISC formation. Involved in the amplification of sense-PTGS (S-PTGS), leading to siRNA production. Required for the maintenance but not the initiation of tobacco rattle virus (TRV)-mediated silencing, probably by mediating/maintaining DNA methylation and chromatin-based transcriptional gene silencing at some genomic locations.
|
Q8GYD9
|
Q2M218
|
ZN630_HUMAN
|
Zinc finger protein 630
|
Homo
|
MIESQEPVTFEDVAVDFTQEEWQQLNPAQKTLHRDVMLETYNHLVSVGCSGIKPDVIFKLEHGKDPWIIESELSRWIYPDRVKGLESSQQIISGELLFQREILERAPKDNSLYSVLKIWHIDNQMDRYQGNQDRVLRQVTVISRETLTDEMGSKYSAFGKMFNRCTDLAPLSQKFHKFDSCENSLKSNSDLLNYNRSYARKNPTKRFRCGRPPKYNASCSVPEKEGFIHTGMEPYGDSQCEKVLSHKQAHVQYKKFQAREKPNVCSMCGKAFIKKSQLIIHQRIHTGEKPYVCGDCRKAFSEKSHLIVHQRIHTGEKPYECTKYGRAFSRKSPFTVHQRVHTGEKPYECFECPKAFSQKSHLIIHQRVHTREKPFECSECRKAFCEMSHLFIHQITHTGKKPYECTECGKTFPRKTQLIIHQRTHTGEKPYKCGECGKTFCQQSHLIGHQRIHTGEKPYVCTDCGKAFSQKSHLTGHQRLHTGEKPYMCTECGKSFSQKSPLIIHQRIHTGEKPYQCGECGKTFSQKSLLIIHLRVHTGEKPYECTECGRAFSLKSHLILHQRGHTGEKPYECSECGKAFCGKSPLIIHQKTHPREKTPECAESGMTFFWKSQMITYQRRHTGEKPSRCSDCGKAFCQHVYFTGHQNPYRKDTLYIC
|
May be involved in transcriptional regulation.
|
Q2M218
|
Q71VU0
|
INLJ_LISMF
|
Internalin J
|
Listeria
|
MKTSKIIIASLVSLTLVSNPILTFAATNDVIDSTTEITTDKEISSTQPTIKTTLKAGQTQSFNDWFPDDNFASEVAAAFEMQATDTISEEQLATLTSLDCHNSSIADMTGIEKLTGLTKLICTYNNITTLDLSQNTNLTYLACDSNKLTNLDVTPLTKLTYLNCDTNKLTKIDVSQNPLLTYLNCARNTLTEIDVSHNTQLTELDCHLNKKITKLDVTPQTQLTTLDCSFNKITALDVSQNKLLNRLNCDTNNITKLDLNQNIQLTFLNCSSNKLTEIDVTPLTQLTYFDCSVNPLTELDVSTLSKLTTLHCIQTDLLEIDLTHNTQLIYFQAEGCRKIKELDVTHNTQLYLLDCQAAGITELDLSQNPKLVYLYLNNTELTKLDVSHNTKLKSLSCVNAHIQDFSSVGKIPVLNNNLDAEGQTITMPKETLTNNSLTIAVSPDLLDQFGNPMNIEPGDGGVYDQATNTITWENLSTDNPAVTYTFTSENGAIVGTVTTPFEAPQPIKGEDVTVHYLDDKGEKLAADEVLSGNLDDPYTSSAKDIPDYTLTTTPDNATGTFTTTSQSVTYVYTKNIVAAEPVTVNYVDDTGKTLAPSETLNGNVGDTYNATAKQIDGYTLSTTPNNATGTFNTSSQTVTYVYTKNIVAAEPVTVNYVDDTGKTLAPSETLNGNVGDTYNATAKQIDGYTLSAEPTNATGQFTSSAQTVNYIYTKNPAPEKGVVEIHYVDENNKQLSSATKISGTVGDNYTTEPKNIDGYTLTTTPDNATGTFNTSSQTVTYVYTKNIVAAEPVTVNYVDANGKTLAPSETLNGTIGDTYNATAKQIDGYTLSAEPTNATGQFTNSAQTVNYIYTKNTNIDQPLPDKKTTKPSNLKTTEVKKASDTLPKTGDSTPWKSALLGVFLSSTALVIWKKKK
|
Involved in several steps of L.monocytogenes infection, probably improves adhesin to host cells.
|
Q71VU0
|
O65272
|
KEA2_ARATH
|
K(+) efflux antiporter 2, chloroplastic
|
Arabidopsis
|
MDFASSVQRQSMFHGGADFASYCLPNRMISAKLCPKGLGGTRFWDPMIDSKVRSAIRSKRNVSYRSSLTLNADFNGRFYGHLLPAKPQNVPLGFRLLCQSSDSVGDLVGNDRNLEFAEGSDDREVTFSKEEKDTREQDSAPSLEELRDLLNKATKELEVASLNSTMFEEKAQRISEVAIALKDEAASAWNDVNQTLNVVQEAVDEESVAKEAVQKATMALSLAEARLQVALESLEAEGYNTSEESEVRDGVKDKEEALLSAKADIKECQENLASCEEQLRRLQVKKDELQKEVDRLNEAAERAQISALKAEEDVANIMVLAEQAVAFELEATQRVNDAEIALQRAEKTLFGSQTQETTQGKVLDGKNTIVGEDEVLSEIVDVSHQAERDLVVVGVSSDVGTQSYESDNENGKPTADFAKEAEGEAEKSKNVVLTKKQEVQKDLPRESSSHNGTKTSLKKSSRFFPASFFSSNGDGTATVFESLVESAKQQWPKLILGFTLLGAGVAIYSNGVGRNNQLPQQPNIVSTSAEDVSSSTKPLIRQMQKLPKRIKKLLEMFPQQEVNEEEASLLDVLWLLLASVIFVPLFQKIPGGSPVLGYLAAGILIGPYGLSIIRNVHGTKAIAEFGVVFLLFNIGLELSVERLSSMKKYVFGLGSAQVLVTAAVIGLITHYVAGQAGPAAIVIGNGLALSSTAVVLQVLQERGESTSRHGRATFSVLLFQDLAVVVLLILIPLISPNSSKGGIGFQAIAEALGLAAIKAAVAITGIIAGGRLLLRPIYKQIAENRNAEIFSANTLLVILGTSLLTARAGLSMALGAFLAGLLLAETEFSLQVESDIAPYRGLLLGLFFMTVGMSIDPKLLLANFPLIMGTLGLLLVGKTILVVIIGKLFGISIISAVRVGLLLAPGGEFAFVAFGEAVNQGIMTPQLSSLLFLVVGISMALTPWLAAGGQLIASRFELQDVRSLLPVESETDDLQGHIIICGFGRIGQIIAQLLSERLIPFVALDVSSDRVAIGRSLDLPVYFGDAGSREVLHKIGADRACAAAIALDTPGANYRCVWALSKYFPNVKTFVRAHDVDHGLNLEKAGATAVVPETLEPSLQLAAAVLAQAKLPTSEIATTINEFRSRHLSELAELCEASGSSLGYGFSRSTSKPKPPSPSETSDDNQIIEGTLAI
|
Electroneutral K(+)/H(+) antiporter modulating monovalent cation and pH homeostasis in plastids . Transports K(+) and Cs(+) preferentially relative to Na(+) or Li(+) . May function in osmotic adjustment .
|
O65272
|
P31801
|
CHAA_ECOLI
|
Na(+)/H(+) exchanger
|
Escherichia
|
MSNAQEAVKTRHKETSLIFPVLALVVLFLWGSSQTLPVVIAINLLALIGILSSAFSVVRHADVLAHRLGEPYGSLILSLSVVILEVSLISALMATGDAAPTLMRDTLYSIIMIVTGGLVGFSLLLGGRKFATQYMNLFGIKQYLIALFPLAIIVLVFPMALPAANFSTGQALLVALISAAMYGVFLLIQTKTHQSLFVYEHEDDSDDDDPHHGKPSAHSSLWHAIWLIIHLIAVIAVTKMNASSLETLLDSMNAPVAFTGFLVALLILSPEGLGALKAVLNNQVQRAMNLFFGSVLATISLTVPVVTLIAFMTGNELQFALGAPEMVVMVASLVLCHISFSTGRTNVLNGAAHLALFAAYLMTIFA
|
Sodium exporter that functions mainly at alkaline pH . Can also function as a potassium/proton and calcium/proton antiporter at alkaline pH . Does not play a major role in calcium export . The K(+)/H(+) antiporter activity may enable E.coli to adapt to K(+) salinity stress and to maintain K(+) homeostasis .
|
P31801
|
Q8ZQ59
|
PIPB_SALTY
|
Secreted effector protein PipB
|
Salmonella
|
MPITNASPENILRYLHAAGTGTKEAMKSATSPRGILEWFVNFFTCGGVRRSNERWFREVIGKLTTSLLYVNKNAFFDGNKIFLEDVNGCTICLSCGAASENTDPMVIIEVNKNGKTVTDKVDSERFWNVCRMLKLMSKHNIQQPDSLITEDGFLNLRGVNLAHKDFQGEDLSKIDASNADFRETTLSNVNLVGANLCCANLHAVNLMGSNMTKANLTHADLTCANMSGVNLTAAILFGSDLTDTKLNGAKLDKIALTLAKALTGADLTGSQHTPTPLPDYNDRTLFPHPIF
|
Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. Does not appear to be required for the formation or the maintenance of either Salmonella-containing vacuole (SCV) or the Salmonella-induced filaments (Sifs). Not required for intracellular replication in phagocytic cells.
|
Q8ZQ59
|
A4WDE0
|
LEPA_ENT38
|
Ribosomal back-translocase LepA
|
Enterobacter
|
MKNIRNFSIIAHIDHGKSTLSDRIIQICGGLSDREMEAQVLDSMDLERERGITIKAQSVTLDYKAADGETYQLNFIDTPGHVDFSYEVSRSLAACEGALLVVDAGQGVEAQTLANCYTAMEMELEVVPVLNKIDLPAADPERVAEEIEDIVGIDATDAVRCSAKTGVGVPDVLERLVRDIPPPEGDVDAPLQALIIDSWFDNYLGVVSLVRIKNGTMRKGDKIKVMSTGQVYNADRLGIFTPKQVDRTELRCGEVGWLVCAIKDILGAPVGDTLTQARNPADKALPGFKKVKPQVYAGLFPVSSDDYENFRDALGKLSLNDASLFYEPESSTALGFGFRCGFLGLLHMEIIQERLEREYDLDLITTAPTVVYEVETTNKEVIYVDSPSKLPPLNNIEELREPIAECHMLLPQEFLGNVITLCIEKRGVQTNMVYHGNQVALTYEIPMAEVVLDFFDRLKSTSRGYASLDYNFKRFQASNMVRVDVLINSERVDALALITHNDNAPYRGRELVEKMKELIPRQQFDIAIQAAIGNHIIARATVKQLRKNVLAKCYGGDVSRKKKLLQKQKDGKKRMKQVGNVELPQEAFLAILHVGKDGK
|
Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP-dependent manner.
|
A4WDE0
|
A2C0H2
|
PETD_PROM1
|
17 kDa polypeptide
|
Prochlorococcus
|
MSTLKKPDLTDTKLRAKLAKGMGHNYYGEPAWPNDLLYIFPVVILGTIACVVGLAVLDPAFLGDKANPFATPLEILPEWYLYPVFQILRVVPNKLLGIALQTLIPLGLMILPFIENINKFANPFRRPVAMSLFLFGTVLTMYLGIGACLPIDKSLTLGLF
|
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.
|
A2C0H2
|
Q5TKG3
|
CAX1B_ORYSJ
|
OsCAX1b
|
Oryza sativa
|
MPVSRMMMESNTMAKEMAVRHHLLPGSPRRRTAHNLSSSSLRKSSDASLLHKVPCAALRSLLANLNDVLLTTRLFLLFPAVLLAIAATYLHFGQVWVFVLSLIGLVPLAERLSFLTEQIAFYTGPTVGGLLNATFGNVTEVIIALLALREGKIEVVKCSLLGSILSNLLLVLGTSLFLAGIANLRAHQPYDTKQAHVNTALLMLAVLCHSLPLMLRYAVTSGDHAIVSGDAALHLSRACSILMLIAYLAYLFFQLNTHRQLFEPQQVEDDDDDDLVIAQDDEPVLGFSSAMIWLALMTLLTALLSGYVVSTIEAASESWELSVSFISIILLPIVGNAAEHAGAVIFALKNKMDITLGVSLGSATQISMFVVPVSVIVAWTMGIPMDLDFNLLETGSLFLAILVTAFTLQEGESHYLKGLILVLCYAVISVCFFVIRRRSAGGTDGVHHLDVIV
|
Vacuolar cation/proton exchanger (CAX). Translocates Ca(2+) and other metal ions into vacuoles using the proton gradient formed by H(+)-ATPase and H(+)-pyrophosphatase.
|
Q5TKG3
|
B7M0D7
|
CAIT_ECO8A
|
L-carnitine/gamma-butyrobetaine antiporter
|
Escherichia
|
MKNEKRKTGIEPKVFFPPLIIVGILCWLTVRDLDAANVVINAVFSYVTNVWGWAFEWYMVVMLFGWFWLVFGPYAKKRLGNEPPEFSTASWIFMMFASCTSAAVLFWGSIEIYYYISTPPFGLEPNSTGAKELGLAYSLFHWGPLPWATYSFLSVAFAYFFFVRKMEVIRPSSTLVPLVGEKHAKGLFGTIVDNFYLVALIFAMGTSLGLATPLVTECMQWLFGIPHTLQLDAIIITCWIILNAICVACGLQKGVRIASDVRSYLSFLMLGWVFIVSGASFIMNYFTDSVGMLLMYLPRMLFYTDPIAKGGFPQGWTVFYWAWWVIYAIQMSIFLARISRGRTVRELCFGMVLGLTASTWILWTVLGSNTLLLIDKNIINIPNLIEQYGVARAIIETWAALPLSTATIWGFFILCFIATVTLVNACSYTLAMSTCREVRDGEEPPLLVRIGWSILVGIIGIVLLALGGLKPIQTAIIAGGCPLFFVNIMVTLSFIKDAKQNWKD
|
Catalyzes the exchange of L-carnitine for gamma-butyrobetaine.
|
B7M0D7
|
P37322
|
BLC3_PSEAI
|
Carbenicillinase 3
|
Pseudomonas
|
MKFLLAFSLLIPSVVFASSSKFQQVEQDVKAIEVSLSARIGVSVLDTQNGEYWDYNGNQRFPLTSTFKTIACAKLLYDAEQGKVNPNSTVEIKKADLVTYSPVIEKQVGQAITLDDACFATMTTSDNTAANIILSAVGGPKGVTDFLRQIGDKETRLDRIEPDLNEGKLGDLRDTTTPKAIASTLNKLLFGSALSEMNQKKLESWMVNNQVTGNLLRSVLPAGWNIADRSGAGGFGARSITAVVWSEHQAPIIVSIYLAQTQASMAERNDAIVKIGHSIFDVYTSQSR
|
Hydrolyzes both carbenicillin and oxacillin.
|
P37322
|
C0M821
|
RSMG_STRE4
|
16S rRNA 7-methylguanosine methyltransferase
|
Streptococcus
|
MTPQAFYLVLEQAGFALTNHQKEQFDTYFKLLVDWNRKINLTAITEENEVYLKHFYDSVAPLLQGYIPNEPLRLLDIGAGAGFPSIPMKIMFPKLDVTIIDSLNKRIHFLQLLAKELGLEGVHFYHGRAEDFGQDKQFRGQFDLVTARAVARMQILSELTIPFLKIKGKLIALKAQAADQELEEAKKALQLLFAKVLDHQPYQLPNGDGRYITLVEKKKETPNKYPRKAGIPNKKPL
|
Specifically methylates the N7 position of a guanine in 16S rRNA.
|
C0M821
|
A8FPD5
|
ENGB_SHESH
|
Probable GTP-binding protein EngB
|
Shewanella
|
MSESCIDFRKAKFLISAPDIAHLNEHLPGDAGVEIAFAGRSNAGKSSALNLLTDQKSLARTSRTPGRTQLINIFELDENRRLVDLPGYGFAQVPLALKKKWQESLGEYLQERQCLGGMVVLMDIRHPLKDLDMQMIAWALESEIPVLALLTKADKLKQSERMKMVNEVRKHLGDFDDRVKVEPFSSLKGIGKAKVLGILNEWCHPQWLTDAIADAETEEE
|
Necessary for normal cell division and for the maintenance of normal septation.
|
A8FPD5
|
A8F9S1
|
AROK_BACP2
|
Shikimate kinase
|
Bacillus
|
MKINREIPVRQRNIVLIGFMGVGKTTIGQLVAKKLYRDFIDVDQEIEKKYNMTIPEMFQQKGEAFFRQAEKDYIVDLCEHTQLKIVSLGGGAFKQEEIKRACLKHCTVLFLDLSWENWKQRLDILIENRPVLHNRTLDEMKELFEERREIYSLHNSRVETDHLEAEEVANYIVDTLKLGWDLYSK
|
Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
|
A8F9S1
|
Q1IX82
|
RL14_DEIGD
|
50S ribosomal protein L14
|
Deinococcus
|
MIMPQTRLDVADNSGARELMCIRVLNSGIGGKGLTKGGGGNKRYAHVGDIIVASVKDAAPRGAVKAGDVVKAVVVRTSHAIKRADGSTIRFDKNAAVIINNQGEPRGTRVFGPVARELRDRRFMKIVSLAPEVL
|
Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome.
|
Q1IX82
|
Q5SCV8
|
ATPB_HUPLU
|
F-ATPase subunit beta
|
Huperzia
|
MEINPFALGVSTLVEKNVGYITQIIGPVLDVAFPPGKMPNIYNSSIIKGKNPAGQEMNVTCEVQQLLGNNKVRAVAMSATDGLTREMKVVDTGAPLSVPVGEATLGRIFNVLGEPVDNLGSVDAGTTSPIHRSAPAFAQSDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESKVINEQNISESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNKQDVLLFIDNILRFVQAGSEVSALLGRMPSAVGYQPTLGTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPSDSTPTMLQPWIVGEQHYETAQEVKQTLQRYKELQDIIAILGLDESSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVTLVETIKGFQMILSGELDNLPEQAFYLVGDINEATAKAATSQVEN
|
Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.
|
Q5SCV8
|
A6L330
|
END4_PHOV8
|
Endonuclease IV
|
Phocaeicola
|
MKKIGAHVSVSGGVEMAPVNALGIGADAFALFTKNQRQWVAKPLSVESVTLFKENCEKEGFDARYVLPHDSYLINLGHPDEEGLEKSRAAFLDEMQRCELLGLKMLNFHPGSHLNKISIEKCLDRIAESVNMTLDKTTGVTAVIENTAGQGSNVGNEFWHLRYIIDKVEDKSRVGVCLDTCHTYTAGYDIVNEYDRVFTEFDEVVGRNYLCAIHLNDSKKPLGSRVDRHDSIGKGLIGIDFFRRFMQDSRFDDMPVILETPDDTIWRDEIKMLRSFES
|
Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate.
|
A6L330
|
A0T0J1
|
RK5_PHATC
|
50S ribosomal protein L5, chloroplastic
|
Phaeodactylum
|
MLNQHSLEEIAEIHNLLGNIKQEYEIGIKPLLIKNSPKLFKNPHTVPKLKKIQINRGLGLAAQNTNLLKKNIEEFEKIAGQKPLITRSKKAIAGFKIREDMELGLSVTLRGEKMYTFLTKLLFFTFAQIRDFRGLSLRSFDKAGNYTLGLKEQLIFPEIDYDDVDQIQGFTINIILEHGSPKYRAESIDKILNGMILFKFLRFPLNDCGYYDKYEAFSDINRNWDKKRHLKRKRWSQE
|
Binds 5S rRNA, forms part of the central protuberance of the 50S subunit.
|
A0T0J1
|
Q57705
|
TYW1_METJA
|
tRNA wyosine derivatives biosynthesis protein Taw1
|
Methanocaldococcus
|
MIPEEIYKILRKQRYQIDGHTAVKLCGWVRKKMLEDKNCYKSKFYGIETHRCIQCTPSVIWCQQNCIFCWRVLPRDIGIDISQIKEPKWEEPEVVYEKILAMHKRIIMGYAGVLDRVGEKKFKEALEPKHVAISLSGEPTLYPYLDELIKIFHKNGFTTFVVSNGILTDVIEKIEPTQLYISLDAYDLDSYRRICGGKKEYWESILNTLDILKEKKRTCIRTTLIRGYNDDILKFVELYERADVHFIELKSYMHVGYSQKRLKKEDMLQHDEILKLAKMLDENSSYKLIDDSEDSRVALLQNENRKINPKL
|
Component of the wyosine derivatives biosynthesis pathway that catalyzes the condensation of N-methylguanine with 2 carbon atoms from pyruvate to form the tricyclic 4-demethylwyosine (imG-14) on guanosine-37 of tRNA(Phe).
|
Q57705
|
Q4ZUZ4
|
LEU3_PSEU2
|
Beta-IPM dehydrogenase
|
Pseudomonas syringae
|
MSKQILILPGDGIGPEIMTEAVKVLELANEKYQLGFELTHDVIGGAAIDKHGVPLADETLERARAADAVLLGAVGGPKWDTIERDIRPERGLLKIRSQLGLFGNLRPAILYPQLADASSLKPEIVAGLDIMIVRELTGGIYFGAPRGTRVLDNGERQAYDTLPYSESEIRRIAKVGFDMAMVRGKKLCSVDKANVLASSQLWREIVEQVARDYPEVELSHMYVDNAAMQLVRAPKQFDVIVTDNLFGDILSDQASMLTGSIGMLPSASLDTANKGMYEPCHGSAPDIAGKGIANPLATILSVSMMLRYSFNLTDAADAIEKAVSLVLDQGIRTGDIWSEGKVKVGTQEMGDAVVAALRNL
|
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.
|
Q4ZUZ4
|
Q96334
|
PSBP_BRAJU
|
OEC 23 kDa subunit
|
Brassica
|
EDDTSTVSRRLALTLLVGAAAVGSKVSPADAAYGEAANVFGKPKTNTDFTAINGDGFQVQVPAKWNPSREVEYPGQVLRYEDNFDATSNLNVMVTPTDKKSITDYGSPEEFLSQVNYLLGKQAYFGETACEGGFDNNAVATANILETNIQDVGGKPYYYLSVLTRTADEDEGGKHQLITATVNGGKLYICKAQAGDKRWFKGANKFVEKAATSFSVA
|
May be involved in the regulation of photosystem II.
|
Q96334
|
A1JT25
|
SELA_YERE8
|
Selenocysteinyl-tRNA(Sec) synthase
|
Yersinia
|
MSAEPHHLYSQLPAIDSLLRAPEMAPLLDEYGAALLTENLRLMQAEAREYIRQFHTLADWCADWPAALRHRLNQRQPALKPVFNLSGTVLHTNLGRAPLAESAIAAVTDAMRGAVTLEYSLSGAGRGHRDRAVADLLCELTGAEDACIVNNNAAAVFLMLTVMAAGKQVVVSRGELVEIGGAFRIPDVMRQAGCELVEVGTTNRTHLKDYRQAISEHTGLLMKVHTSNYSIEGFTASVAEQQLAALGHEFAIPTATDLGSGSLVDMTRYGLPAEPMPQQLIAAGVDLVTFSGDKLLGGPQAGIILGKKQWIDQLQQHPLKRVLRADKMTLAALDATLRLYQQPDRLTELLPTMRLLTRPAQDIAESAQRVLAALNGSYAADFTLAVESCWSQIGSGSLPVDRLPSWAVTFTPKDGSGSALEALTVRWRGLAKPIIGRVADGRLWLDLRCLEDEAALLRELAP
|
Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis.
|
A1JT25
|
O59801
|
SKI2_SCHPO
|
Putative ATP-dependent RNA helicase C550.03c
|
Schizosaccharomyces
|
MSSKLVDAINEVAVSNKDKIELDGIKDDSFDGHLSITEATYDVDTFLKPSPALSKDWIRKLQKKWDREITYKGLYEYPETLARTQIRFQRHGLEGKIMGYKEVPELIEDLNSKNSSSFLRKPSSKNEFVRGSTSNIPFLADDSDVDAIAGEPSVKMALYGEDGLLQVPPGFSRGLSMTATSTTDNLNDEFDPEKWDTKKVKSSNRNFVTIHELNEHLKNVNSKHSEIDDLLPDKRSIVSLPPSTLNLHKQPDYAHVVDSSAPIENFQQLVPEMALDFPFELDNFQKEAIYHLEMGDSVFVAAHTSAGKTVVAEYAIALAQKHMTKAIYTSPIKALSNQKFRDFKHKFEDVGILTGDVQVNPEGSCLLMTTEILRSMLYRGADLIRDVEFVIFDEVHYVNDLERGVVWEEVIIMLPPHVTLILLSATVPNTKEFASWVGRTKKKNIYVISTLKRPVPLEHYLWVKQNMFKIVDQHGRFLMDGYKSANDALKKPDKPVIAKDNKNSARGRGAARGRGVQTNMMRGRGSAKSVERRDANTWVHLIGHLHKQNLLPVIVFVFSKKRCEEYVDTLTNRDLNNHQEKSEVHVVIEKAVARLKKEDRLLPQIGRMREMLSRGLAVHHGGLLPIIKEIVEILFQRGLVKVLFATETFAMGVNMPAKSVVFSGTQKHDGRNFRDLLPGEYTQCSGRAGRRGLDVTGTVIILSRSELPDTASLRHMIMGPSSKLISQFRLTYNMILNLLRVETLRIEDMIKRSFSENVNQTLVPQHEEKIKSFEEKLSALKKEMSDVDLKEIKSCLLSSESFKEYTKKMHFRAITTANGKRIFKDGRVIVFQQLDFTRTVGVLLGTSIRTNASDCTLEVAYLNPQNNLKRPSDLLAFADAFNDVYDNAIFDESNQFKYGLINLSGIERVCNTILRIDSGGIRDRRGGAFRKLSEQFASIKKFSDLLFEEVNWSKVRDFEFCEAFEKRNFLQNKLSGNPIISTPNFLTHFALAYQEYELESNIDNLSSYISDQNLELLPDYEQRIKVLQELGYIDAERTVLLKGRVACEINSTSELVLTELILENSLADFSCEETIALLSAFVFDEKTEVEPTISPHLQKGKEMILSVAEKVNQIQEHYQVLYFNEGNDFESQPRFGLMEVCYEWARGMSFNRITDLTDVLEGSIVRTIIRLDEVLRECRGAARVVGDSSMYTKMEECQNLIRRNIVFCPSLYM
|
RNA helicase component of the SKI complex involved in 3'-mRNA degradation pathway.
|
O59801
|
Q07512
|
FLS_PETHY
|
Flavonol synthase/flavanone 3-hydroxylase
|
Petunia
|
MKTAQGVSATLTMEVARVQAIASLSKCMDTIPSEYIRSENEQPAATTLHGVVLQVPVIDLRDPDENKMVKLIADASKEWGIFQLINHGIPDEAIADLQKVGKEFFEHVPQEEKELIAKTPGSNDIEGYGTSLQKEVEGKKGWVDHLFHKIWPPSAVNYRYWPKNPPSYREANEEYGKRMREVVDRIFKSLSLGLGLEGHEMIEAAGGDEIVYLLKINYYPPCPRPDLALGVVAHTDMSYITILVPNEVQGLQVFKDGHWYDVKYIPNALIVHIGDQVEILSNGKYKSVYHRTTVNKDKTRMSWPVFLEPPSEHEVGPIPKLLSEANPPKFKTKKYKDYVYCKLNKLPQ
|
Catalyzes the formation of flavonols from dihydroflavonols. It can act on dihydrokaempferol to produce kaempferol, on dihydroquercetin to produce quercitin and on dihydromyricetin to produce myricetin.
|
Q07512
|
Q18J40
|
MSRA_HALWD
|
Peptide-methionine (S)-S-oxide reductase
|
Haloquadratum
|
MSETATVGGGCFWCTEAAMKELAGVNTVTSGYAGGDIDNPTYKQVCSGTTDHAEVVQIEYDPTKIEYSELLEVFFATHDPTQLNRQGPDVGTQYRSIILTHTAEQRATAEAYIEALNDHYDDAIVTEIESLERFWSAEEYHQDYFEKNPSDAYCRMHAQPKVEKVRETFTEKLT
|
Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
|
Q18J40
|
A8AXZ6
|
AROD_STRGC
|
Type I dehydroquinase
|
Streptococcus
|
MKLVVSVTPRNLEEAQQIDAQRFVDADLIEWRADFLEKEEILKVAPAIFEKFAGRELIFTLRTKDEGGHIQLSDDEYVEMIKKVAQLYQPDYVDFEYFSHKDKIDEMLEFPNLVLSYHNFEETPENMMEILSELTSLTPKAVKVSVMANSGQDVLDLMNYTRGFKTLNPEQEYVTISMGRVGRISRIASDLTGSSWSFASLDEATAPGQISLSSMKKIRDILNEN
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Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate.
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A8AXZ6
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