ID   SYV_RICTY               Reviewed;         814 AA.
AC   Q68W50;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 102.
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=RT0682;
OS   Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=257363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-144 / Wilmington;
RX   PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA   McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA   McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA   Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA   Yu X.-J., Walker D.H., Weinstock G.M.;
RT   "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT   of other Rickettsiae.";
RL   J. Bacteriol. 186:5842-5855(2004).
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; AE017197; AAU04142.1; -; Genomic_DNA.
DR   RefSeq; WP_011191119.1; NC_006142.1.
DR   AlphaFoldDB; Q68W50; -.
DR   SMR; Q68W50; -.
DR   STRING; 257363.RT0682; -.
DR   EnsemblBacteria; AAU04142; AAU04142; RT0682.
DR   KEGG; rty:RT0682; -.
DR   eggNOG; COG0525; Bacteria.
DR   HOGENOM; CLU_001493_0_2_5; -.
DR   OMA; RQWYIRN; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000000604; 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   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.
FT   CHAIN           1..814
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_0000224615"
FT   MOTIF           46..56
FT                   /note="'HIGH' region"
FT   MOTIF           536..540
FT                   /note="'KMSKS' region"
FT   BINDING         539
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02005"
SQ   SEQUENCE   814 AA;  94426 MW;  9E8770F2EAEFD792 CRC64;
     MKEFPKHYNF IENEKKWQHI WQELQIYAYN PNMSKEGIYI VDTPPPTVSG QLHIGHIYSY
     TQTDFIVRFQ RMIGKNIFYP IGFDDNGLPT ERLVEKQKQI KAYNMERDEF IKICQEVVQN
     EEAKFRNLFK QIALSVDWSL EYQTISPLSR KISQMSFLDL LHKGEVYRAN QPILWDTVDG
     TALAQADIED KQKISSMNYI MFKTEQGDKL TIATTRPELL PACVAVFYHP DDGRYKHLAD
     KSAITPLFNE KVPILADPLV QQDKGTGLVM CCTFGDQTDI TWWKSHNLPL KTIITKKGTI
     NFPHKIDLDG LTIKEARTKI IDILKEQNLL TKQEEITQTV KCAERSGAPL EILTVTQWFI
     KTITHKEALL KRTNELNWYP KNMQMRLENW INSLSWDWCI SRQRYFGVPF PIWYSKRIGE
     EGKILYADIS QLPVDPLKDL PIGYSKEEVD PDLDVMDTWA TSSVSPQLST YGISEDFAIN
     KVRHDKLFPM DLRPQAHEII RTWAFYTILK SHLHQNILPW KNIMVSGWCL AEDRSKMSKS
     KGNVLVPEKL LERYGADVIR YWSANSKLGA DTAYSEDIMK NGKRLVNKLW NAAKFVSIHF
     DKLTSEDKKV SLCAIKEKIT HEFDQWIINK LVALVKLATN ALQNYEYANA IYLTEKFFWS
     IFCDNYLEIS KTRSYDEGNK NPQGQYSSIL TSYHVMQTLL KLFAPFMPHI TEELYQILYS
     KNSIHIQGNW VNYGDLNYDI DVQGPEGLLT ILDIVRKFKA EYNLSIKAPI KLLEVSGIIL
     STELVEDLKN VTSAEAIQFE MKDDKIKVNI KLFV