SYV_RALSO
ID SYV_RALSO Reviewed; 968 AA.
AC Q8XX80;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 111.
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=RSc2236;
GN ORFNames=RS01363;
OS Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=267608;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GMI1000;
RX PubMed=11823852; DOI=10.1038/415497a;
RA Salanoubat M., Genin S., Artiguenave F., Gouzy J., Mangenot S., Arlat M.,
RA Billault A., Brottier P., Camus J.-C., Cattolico L., Chandler M.,
RA Choisne N., Claudel-Renard C., Cunnac S., Demange N., Gaspin C., Lavie M.,
RA Moisan A., Robert C., Saurin W., Schiex T., Siguier P., Thebault P.,
RA Whalen M., Wincker P., Levy M., Weissenbach J., Boucher C.A.;
RT "Genome sequence of the plant pathogen Ralstonia solanacearum.";
RL Nature 415:497-502(2002).
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; AL646052; CAD15943.1; -; Genomic_DNA.
DR RefSeq; WP_011002164.1; NC_003295.1.
DR AlphaFoldDB; Q8XX80; -.
DR SMR; Q8XX80; -.
DR STRING; 267608.RSc2236; -.
DR EnsemblBacteria; CAD15943; CAD15943; RSc2236.
DR GeneID; 60501749; -.
DR KEGG; rso:RSc2236; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_4; -.
DR OMA; FATKLWN; -.
DR Proteomes; UP000001436; 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; -; 1.
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..968
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224543"
FT COILED 800..831
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT COILED 898..963
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 49..59
FT /note="'HIGH' region"
FT MOTIF 559..563
FT /note="'KMSKS' region"
FT BINDING 562
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 968 AA; 107892 MW; B88582D1C6CDEF20 CRC64;
MTDPNQSLAK SFEPAAIEQK WSAAWEAMGI SRATLEAGRP DFCIQLPPPN VTGTLHMGHA
FNQTIMDGLA RHARMQGANT LWVPGTDHAG IATQIVVERQ LDAQGISRHD LGRPAFVDKV
WEWKEQSGST ITRQIRRMGA SIDWEREYFT MDPKMSRAVS DVFVRLYEQG LIYRGKRLVN
WDPVLGTAVS DLEVVSEEED GALWHIRYPL AQPDAKTGLT HLTVATTRPE TMLGDVAVMV
HPEDERYAHL IGQAVRLPLS GEADALDTAQ WREIPIIGDE YVDRAFGTGV VKVTPGHDFN
DYAVGQRHGL PQISVLTLEA KIADTAPATY RGIDRFEARK RIVVDLETLG LLAEVKKHTL
MVPRGDRTGV IIEPMLTDQW FVAMSKPAPE GTRFPGRSIA EVALDAVQGG KIKLVPEQWV
NTYNQWLNNI QDWCISRQLW WGHQIPAWYD EAGNVYVART EEEARAQAAA KGHTGAIKRD
DDVLDTWFSA ALVPFSSLGW PADTPELKHF LPSTVLVTGY DIIFFWVARM VMMTLHFTGE
VPFQTVYVHG LVRDSEGKKM SKSEGNTLDP VDLIDGIALE PLLVKRTTGL RRPKDAPNVE
KRTRKEFPDG IPAFGADALR FTFASLATLG RNINFDSSRC EGYRNFCNKL WNATRFVLMN
TEGQDCGLQE CVGDCGPEGA LHFSPADRWI VSLLQRVETE VEKGFADYRF DNIASAIYKF
VWDEYCDWYL ELAKVQIQTG TPAQQRATRR TLLRVLETVL RLAHPIIPFI TEELWQKVAP
MAGRAKGDGT ESLAQQEYPR AVLAKIDEQA EQWVQQLKAL VDACRNLRGE MSLSPAQRVP
LYAHGDAEFL QAAAPYVQAL GKLSEVKVYT DAAAMEQDGA GAPVAIVGEN KLLLKIEIDV
AAEHARLSKE IDRLRGEIVK CEGKLGNESF VARAPAAVVE QEQKRLADFK ATLGKLEAQI
ARLPVQTA
