SYV_THEKO
ID SYV_THEKO Reviewed; 888 AA.
AC Q5JGN7;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Valine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02005};
DE EC=6.1.1.9 {ECO:0000255|HAMAP-Rule:MF_02005};
DE AltName: Full=Valyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02005};
DE Short=ValRS {ECO:0000255|HAMAP-Rule:MF_02005};
GN Name=valS {ECO:0000255|HAMAP-Rule:MF_02005}; OrderedLocusNames=TK1274;
OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Pyrococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL Genome Res. 15:352-363(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_02005}.
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_02005};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02005}.
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_02005}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC ValS type 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_02005}.
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DR EMBL; AP006878; BAD85463.1; -; Genomic_DNA.
DR RefSeq; WP_011250225.1; NC_006624.1.
DR AlphaFoldDB; Q5JGN7; -.
DR SMR; Q5JGN7; -.
DR STRING; 69014.TK1274; -.
DR EnsemblBacteria; BAD85463; BAD85463; TK1274.
DR GeneID; 3235319; -.
DR KEGG; tko:TK1274; -.
DR PATRIC; fig|69014.16.peg.1246; -.
DR eggNOG; arCOG00808; Archaea.
DR HOGENOM; CLU_001493_0_2_2; -.
DR InParanoid; Q5JGN7; -.
DR OMA; FATKLWN; -.
DR OrthoDB; 4914at2157; -.
DR PhylomeDB; Q5JGN7; -.
DR Proteomes; UP000000536; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006438; P:valyl-tRNA aminoacylation; IBA:GO_Central.
DR CDD; cd07962; Anticodon_Ia_Val; 1.
DR Gene3D; 3.40.50.620; -; 2.
DR Gene3D; 3.90.740.10; -; 1.
DR HAMAP; MF_02005; Val_tRNA_synth_type2; 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; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR InterPro; IPR022874; Valine-tRNA_ligase_type_2.
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 PRINTS; PR00986; TRNASYNTHVAL.
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; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..888
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224633"
FT MOTIF 43..53
FT /note="'HIGH' region"
FT MOTIF 534..538
FT /note="'KMSKS' region"
FT BINDING 537
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02005"
SQ SEQUENCE 888 AA; 103464 MW; 4487F64695A4F82B CRC64;
MLPKNYDPNE IEPKWQKFWL DEKIYKYELD EKKPSYAIDT PPPFTSGTLH LGHVLSHTWI
DIIARYKRMT GYNVLFPQGF DNHGLPTELK VEKEFGISKD QPEKFLQKCI EWTWQAIEAM
RNQFIRIGYS ADWDLEYHTM DDWYKAAVQK SLIEFYKKGM LYQAEHPVYW CPRCRTSLAK
AEVGYVEEDG FLYYIKLPLA DGSGHVPIAT TRPELMPACV AVFVHPEDER YKHVVGKKVK
LPIFEREVPV LADEDVDPSF GTGAVYNCTY GDEQDVVWQK RYNLPVIIAI NEDGTMNENA
GPYAGLKTEE ARKKIAEDLE KMGLLYKKEK IRHRVLRHTE RSSCMAPIEL LPKKQWFIKV
KDFTDEIVKV AEQINWYPPD MFLRLKDWAE SMDWDWVISR QRVFGTPIPF WVCDNGEIIL
PNEEDLPVDP RFEKPPRKCS DGSEPKPVTD VLDCWVDSSI TPLIITKWHE AIKGDEEGKK
WFEHNFPTAL RPQGTDIIRT WAFYTIFRTW VLTGEKPWHD ILINGMVAGP DGRKMSKSYG
NVVAPDEVIP KYGADALRLW TALAPPGEDH PFKWETVDYN YRFLQKVWNI YRFAERHLEN
FDPASAPEEL EPLDRWILSR LHRLIKFATE EMEKYRFNLL TRELITFVWH EVADDYIEMI
KYRLYGDDEE SKLKAKAALY ELLYNVMLLL APFVPHITEE LYQNLFRERI GAKSVHLLEW
PKYSEARIDE EAEKLGELAR EIVGAMRRYK NSHGLSLNAK LKHVAIYTTD SYEVLKTIEK
DIAGTMNIEK LEIIKGEPEL EERIIEIKPN FKTVGPRYGK LVPKITAYLK ENAEEVAKAL
KESGKIEFEV DGQKVELTKD DIVLRKAVFS EGEEVETAVV GDAVILFF
