ID   SYV_TROWT               Reviewed;         856 AA.
AC   Q83G51;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 110.
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=TWT_478;
OS   Tropheryma whipplei (strain Twist) (Whipple's bacillus).
OC   Bacteria; Actinobacteria; Micrococcales; Tropherymataceae; Tropheryma.
OX   NCBI_TaxID=203267;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Twist;
RX   PubMed=12902375; DOI=10.1101/gr.1474603;
RA   Raoult D., Ogata H., Audic S., Robert C., Suhre K., Drancourt M.,
RA   Claverie J.-M.;
RT   "Tropheryma whipplei twist: a human pathogenic Actinobacteria with a
RT   reduced genome.";
RL   Genome Res. 13:1800-1809(2003).
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   -!- SUBUNIT: Monomer. {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; AE014184; AAO44575.1; -; Genomic_DNA.
DR   RefSeq; WP_011102600.1; NC_004572.3.
DR   AlphaFoldDB; Q83G51; -.
DR   SMR; Q83G51; -.
DR   STRING; 203267.TWT_478; -.
DR   EnsemblBacteria; AAO44575; AAO44575; TWT_478.
DR   KEGG; twh:TWT_478; -.
DR   eggNOG; COG0525; Bacteria.
DR   HOGENOM; CLU_001493_0_2_11; -.
DR   OMA; RQWYIRN; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000002200; 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; 3.40.50.620; -; 2.
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   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..856
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_0000224618"
FT   MOTIF           47..57
FT                   /note="'HIGH' region"
FT   MOTIF           578..582
FT                   /note="'KMSKS' region"
FT   BINDING         581
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02005"
SQ   SEQUENCE   856 AA;  97538 MW;  BA9687B7B1E246B9 CRC64;
     MNIPDKPSLE GLEEKWSKLW KSSKIYNFEL EQVSAKQDVY SIDTPPPTAS GVLHIGHVFS
     YTHTDIIARF QRMQGKIVFY PMGWDDNGLP TERRVQNYFS VRCDPSLPYC QNLKLAQINN
     DSMARSISRR NFIELCQQLS EEDERKFEEL WNYLGLSVDW SQTYRTIDDD AIHLSQHFFL
     ENVNSGAAYQ DWAPTLWDVT YRTAVAQAEI EERQITGFYY RLAFENENAT VEIETTRPEL
     LAGCVALVAH PDDNRYKHLF GSHVITPVFD VKVPVLPHRA AQPDKGSGIA MVCTFGDITD
     VQWWRDLNLQ SCPIIDASGR VVPDAPDPIV SERGRRAFAT LSGKTLSAAK KHTLEMLISE
     KSIIGEPRKI THPVKFFEKG DKPLEILLTR QWYIRNGYSD NALTERLIEL GKQLQWYPKT
     MLRRYEGWLT GLNSDWLISR QRFLGVPFPI WYQTDDRGNA KFDDPIFPDR KDLPLDPTIA
     VPRGYSENQR GAPNGFVAET DVMDTWATSS LTPQLAGKYL KNPKLFEAIF PYSLRPQGQD
     IIRTWLFSSI IRSEYAHATA PWKSTAISGF ILDPDRKKMS KSKGNAKTPK DILDRYGADA
     VRYWAACARL GVDTALDVEN PTQIKIGRRL ALKVLNAARF VVHLHKNKET YSGQPDMKRC
     YPIDFAAISN PLDLSLLKQL DQTIEQSTNA LKNFDHSKAL DTTETFFWNF CDNYVEIVKD
     RAYAGDESAL TTLLVVTNIV IKLLAPFIPY ATEEAWSWFN ETSVHTQSWP ETLKLHSGDI
     ELLKIACSFM SLVRGGKTEA KLSQKTEIAY LKIALPNPEI IMPIMDDLRR AGKIDKCELI
     DGDAQILAIE YGEISR