SYV_SALCH
ID SYV_SALCH Reviewed; 951 AA.
AC Q57GC5;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 98.
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=SCH_4331;
OS Salmonella choleraesuis (strain SC-B67).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=321314;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC-B67;
RX PubMed=15781495; DOI=10.1093/nar/gki297;
RA Chiu C.-H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.-Y., Wang H.-S.,
RA Lee Y.-S.;
RT "The genome sequence of Salmonella enterica serovar Choleraesuis, a highly
RT invasive and resistant zoonotic pathogen.";
RL Nucleic Acids Res. 33:1690-1698(2005).
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; AE017220; AAX68237.1; -; Genomic_DNA.
DR RefSeq; WP_000416324.1; NC_006905.1.
DR AlphaFoldDB; Q57GC5; -.
DR SMR; Q57GC5; -.
DR EnsemblBacteria; AAX68237; AAX68237; SCH_4331.
DR KEGG; sec:SCH_4331; -.
DR HOGENOM; CLU_001493_0_2_6; -.
DR OMA; FATKLWN; -.
DR Proteomes; UP000000538; 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.
FT CHAIN 1..951
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224549"
FT COILED 882..944
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 42..52
FT /note="'HIGH' region"
FT MOTIF 554..558
FT /note="'KMSKS' region"
FT BINDING 557
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 951 AA; 108260 MW; D1F5567A32CE79D6 CRC64;
MEKTYNPQDI EQPLYEHWEK QGYFKPNGDE SKESFCIMIP PPNVTGSLHM GHAFQQTIMD
TMIRYQRMQG KNTLWQVGTD HAGIATQMVV ERKIAAEEGK TRHDYGRDAF IDKIWQWKAE
SGGTITRQMR RLGNSVDWER ERFTMDEGLS NAVKEVFVRL YKEDLIYRGK RLVNWDPKLR
TAISDLEVEN RESKGSMWHI RYPLADGAKT ADGKDYLVVA TTRPETILGD TGVAVNPEDP
RYQSLIGKFV ILPLVNRRIP IVGDEHADME KGTGCVKITP AHDFNDYEVG KRHALPMINI
LTFDGDIRES AEVFDTKGEE SDVYSSEIPA EFQKLERFAA RKAIVAAVDA LGLLEEIKPH
DLTVPYGDRG GVVIEPMLTD QWYVRADVLA KPAVEAVENG DIQFVPKQYE NMYFSWMRDI
QDWCISRQLW WGHRIPAWYD NDGNVYVGRT EDEVRQENNL GADVALRQDE DVLDTWFSSA
LWTFSTLGWP ENTDALRQFH PTSVMVSGFD IIFFWIARMI MMTMHFIKDE NGKPQVPFHT
VYMTGLIRDD EGQKMSKSKG NVIDPLDMVD GISLPELLEK RTGNMMQPQM AEKIRKRTEK
QFPNGIEPHG TDALRFTLAA LASTGRDINW DMKRLEGYRN FCNKLWNASR FVLMNTEEQD
CGFNGGEMTL SLADRWILAE FNQTVKAYRE ALDNFRFDIA AGILYEFTWN QFCDWYLELT
KPVMTGGSES ELRGTRHTLV TVLEGLLRLA HPIIPFITET IWQRVKVICG ITADTIMLQP
FPEYNAAQVD EAALADTEWL KQAIVAVRNI RAEMNIAPGK PLELLLRGCS EEAVRRVNDN
RSFLQTLARL ESITVLPADD KGPVSVTKII DGAELLIPMA GLINKDDELA RLAKEVAKIE
GEIARIEGKL SNEGFVARAP EAVIAKEREK LDSYAEAKAK LIEQQAVISA L
