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SYV_ACTP2
ID   SYV_ACTP2               Reviewed;         954 AA.
AC   A3N2F0;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Valine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02004};
DE            EC=6.1.1.9 {ECO:0000255|HAMAP-Rule:MF_02004};
DE   AltName: Full=Valyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02004};
DE            Short=ValRS {ECO:0000255|HAMAP-Rule:MF_02004};
GN   Name=valS {ECO:0000255|HAMAP-Rule:MF_02004}; OrderedLocusNames=APL_1502;
OS   Actinobacillus pleuropneumoniae serotype 5b (strain L20).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=416269;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L20;
RX   PubMed=18065534; DOI=10.1128/jb.01845-07;
RA   Foote S.J., Bosse J.T., Bouevitch A.B., Langford P.R., Young N.M.,
RA   Nash J.H.E.;
RT   "The complete genome sequence of Actinobacillus pleuropneumoniae L20
RT   (serotype 5b).";
RL   J. Bacteriol. 190:1495-1496(2008).
CC   -!- FUNCTION: Catalyzes the attachment of valine to tRNA(Val). As ValRS can
CC       inadvertently accommodate and process structurally similar amino acids
CC       such as threonine, to avoid such errors, it has a 'posttransfer'
CC       editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-
CC       dependent manner. {ECO:0000255|HAMAP-Rule:MF_02004}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl-
CC         tRNA(Val); Xref=Rhea:RHEA:10704, Rhea:RHEA-COMP:9672, Rhea:RHEA-
CC         COMP:9708, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57762,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78537, ChEBI:CHEBI:456215; EC=6.1.1.9;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_02004};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_02004}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02004}.
CC   -!- DOMAIN: ValRS has two distinct active sites: one for aminoacylation and
CC       one for editing. The misactivated threonine is translocated from the
CC       active site to the editing site. {ECO:0000255|HAMAP-Rule:MF_02004}.
CC   -!- DOMAIN: The C-terminal coiled-coil domain is crucial for aminoacylation
CC       activity. {ECO:0000255|HAMAP-Rule:MF_02004}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       ValS type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_02004}.
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DR   EMBL; CP000569; ABN74586.1; -; Genomic_DNA.
DR   RefSeq; WP_009875208.1; NC_009053.1.
DR   AlphaFoldDB; A3N2F0; -.
DR   SMR; A3N2F0; -.
DR   STRING; 416269.APL_1502; -.
DR   EnsemblBacteria; ABN74586; ABN74586; APL_1502.
DR   KEGG; apl:APL_1502; -.
DR   PATRIC; fig|416269.6.peg.1563; -.
DR   eggNOG; COG0525; Bacteria.
DR   HOGENOM; CLU_001493_0_2_6; -.
DR   OMA; FATKLWN; -.
DR   Proteomes; UP000001432; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004832; F:valine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006438; P:valyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd07962; Anticodon_Ia_Val; 1.
DR   Gene3D; 1.10.287.380; -; 1.
DR   Gene3D; 3.40.50.620; -; 2.
DR   Gene3D; 3.90.740.10; -; 2.
DR   HAMAP; MF_02004; Val_tRNA_synth_type1; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR033705; Anticodon_Ia_Val.
DR   InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR010978; tRNA-bd_arm.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   InterPro; IPR037118; Val-tRNA_synth_C_sf.
DR   InterPro; IPR019499; Val-tRNA_synth_tRNA-bd.
DR   InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR   InterPro; IPR002303; Valyl-tRNA_ligase.
DR   PANTHER; PTHR11946; PTHR11946; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 1.
DR   Pfam; PF10458; Val_tRNA-synt_C; 1.
DR   PRINTS; PR00986; TRNASYNTHVAL.
DR   SUPFAM; SSF46589; SSF46589; 1.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   SUPFAM; SSF50677; SSF50677; 1.
DR   TIGRFAMs; TIGR00422; valS; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Coiled coil; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..954
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_1000073713"
FT   COILED          883..954
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT   MOTIF           48..58
FT                   /note="'HIGH' region"
FT   MOTIF           560..564
FT                   /note="'KMSKS' region"
FT   BINDING         563
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ   SEQUENCE   954 AA;  108817 MW;  DBE7D4B06516C787 CRC64;
     MTQNLQMADR FDSSAVEQAL YKHWEEQGYF KPTENPSLPS YCIAIPPPNV TGSLHMGHAF
     QQTLMDTLIR FNRMEGNNTL WQTGTDHAGI ATQMVVERKI AAEEGKTRHD YGREAFINKI
     WDWKAYSGGT ISQQMRRLGN SIDWDRERFT MDEGLSNAVK EVFVRLHEEG LIYRGKRLVN
     WDPKLHTAIS DLEVENKESK GSLWHFRYPL ANGAKTADGK DYLVVATTRP ETVLGDTAVA
     VHPEDERYQS LIGKTVVLPL ANREIPIVAD EYVDREFGTG VVKITPAHDF NDYEVGKRHG
     LPMVNVMTMN ADIRAEAEII GTDGKPLTTY EAKIPADYQG LERFAARKKV VADFEALGLL
     DEIKPHDLKV PYGDRGGVPI EPMLTDQWYV SVKPLAEVAT KAVEDGEIQF VPKQYENLYF
     SWMRDIQDWC ISRQLWWGHR IPAWYDEAGN VYVARSEEEV RQKHNLPADL ALRQDEDVLD
     TWFSSGLWTF STLGWPEQTK ELKMFHPTDV LITGFDIIFF WVARMIMFTM HFVKDENGKP
     QVPFKTVYVT GLIRDEQGQK MSKSKGNVLD PIDMIDGISL EDLLEKRTGN MMQPQLAEKI
     AKATRKEFEN GIAAHGTDAL RFTLAALASN GRDINWDMKR LEGYRNFCNK LWNASRFVLT
     NDKLDLSAGE VEYSLADRWI ESKFNRTVGE FREALSQYRF DLAANAIYDF TWNEFCDWYL
     ELTKPVFANG TEAQKRGASQ TLVRVLEKLL RLAHPIMPFI TEEIWQKVKG FAGIDADTIM
     LQPFPKVVKS ELDESAEMQI GWIKELIIAV RNIRAESNIA PSKGLEFLVR NVSDEQRKIL
     AENDRLLKAM AKLDSVQVLS ADENAPLSVA KLVGNVEVLI PMAGFINKEA ELARLTKEIE
     KMRGEITRIE NKLGNEAFVA KAPEAVIAKE REKMQEYQNG LEKLQTQYQA IENL
 
 
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