ID   SYV_RICPR               Reviewed;         814 AA.
AC   Q9ZCN6;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 112.
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=RP687;
OS   Rickettsia prowazekii (strain Madrid E).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=272947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Madrid E;
RX   PubMed=9823893; DOI=10.1038/24094;
RA   Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA   Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA   Kurland C.G.;
RT   "The genome sequence of Rickettsia prowazekii and the origin of
RT   mitochondria.";
RL   Nature 396:133-140(1998).
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; AJ235272; CAA15124.1; -; Genomic_DNA.
DR   PIR; B71675; B71675.
DR   RefSeq; NP_221048.1; NC_000963.1.
DR   RefSeq; WP_004599517.1; NC_000963.1.
DR   AlphaFoldDB; Q9ZCN6; -.
DR   SMR; Q9ZCN6; -.
DR   STRING; 272947.RP687; -.
DR   EnsemblBacteria; CAA15124; CAA15124; CAA15124.
DR   KEGG; rpr:RP687; -.
DR   PATRIC; fig|272947.5.peg.709; -.
DR   eggNOG; COG0525; Bacteria.
DR   HOGENOM; CLU_001493_0_2_5; -.
DR   OMA; RQWYIRN; -.
DR   Proteomes; UP000002480; 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; Reference proteome.
FT   CHAIN           1..814
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_0000106246"
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;  94516 MW;  E2BF221D8AA167E0 CRC64;
     MKEFPKHYNF TENEKKWQNI WQELQIYAYD PNISKAEIYI VDTPPPTVSG QLHIGHIYSY
     TQTDFIVRFQ RMIGKNIFYP IGFDDNGLPT ERLVEKQKQI KAYNMERDEF IKICLEVVKN
     EEAKFRSLFK QIALSVDWSL EYQTISPLSR KISQMSFLDL LHKGEVYRAN QPILWDTVDG
     TALAQADIED KQKISSMNYI TFKTEQGDQL TIATTRPELL PACVAVFYHP DDVRYKHLAD
     KSAITPLFNE KVPILADPLV QQDKGTGLVM CCTFGDQTDI TWWKSHNLPL KTIITKKGTI
     NFPHKLDIDG LTIKEARTKI IDILKEQSLL TKQEEIIQTV KCAERSGAPL EILTVTQWFI
     KTITHKEALL KRTNELNWYP KNMKMRLENW INSLSWDWCI SRQRYFGVPF PIWYSKRIGE
     EGKILYADIS QLPVDPLKDL PIGYSKEEVD PDLDVMDTWA TSSVSPQLST YGISEDLAIN
     KVRHDKLFPM DLRPQAHEII RTWAFYTILK SHLHQNILPW KNIMVSGWCL AEDRSKMSKS
     KGNVLVPEKL LERYGADVIR YWSANSKLGA DTAYSEDVMK NGKRLVNKLW NAAKFVSIHF
     DKLTSEDKKV SLFDIKEKIT NEFDQWMINK LVALVKLATN ALQNYEYANA IYLTEKFFWS
     IFCDNYLEIS KTRSYDEANK NPQGQYSSIL TLYHIMQTLL KLFAPFMPHI TEELYQILYN
     KNSIHMQGNW INYGDLNYEI DVQGPEGLLE ILDIVRKFKA EYNLSIKAPI KLLEVSGIVL
     STELVEDLKN VTSAEEIQFK AKDDQIKVNI KLFV