ID   SYV_RICBR               Reviewed;         812 AA.
AC   Q1RJ74;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 100.
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=RBE_0509;
OS   Rickettsia bellii (strain RML369-C).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX   NCBI_TaxID=336407;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RML369-C;
RX   PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA   Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA   Fournier P.-E., Claverie J.-M., Raoult D.;
RT   "Genome sequence of Rickettsia bellii illuminates the role of amoebae in
RT   gene exchanges between intracellular pathogens.";
RL   PLoS Genet. 2:733-744(2006).
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; CP000087; ABE04590.1; -; Genomic_DNA.
DR   RefSeq; WP_011477181.1; NC_007940.1.
DR   AlphaFoldDB; Q1RJ74; -.
DR   SMR; Q1RJ74; -.
DR   STRING; 336407.RBE_0509; -.
DR   EnsemblBacteria; ABE04590; ABE04590; RBE_0509.
DR   KEGG; rbe:RBE_0509; -.
DR   eggNOG; COG0525; Bacteria.
DR   HOGENOM; CLU_001493_0_2_5; -.
DR   OMA; RQWYIRN; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000001951; 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..812
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_0000272363"
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   812 AA;  94328 MW;  4AFE1D05DBE0D43A CRC64;
     MKEFPKNYNF IESEKKWQKI WQEKQIYAYD ENIAKDETFV VDTPPPTVSG QLHIGHVYSY
     TQTDFIVRFQ RMMGKNIFYP MGFDDNGLPT ERLVEKQRQV KAYNMGREEF INICNEVVAS
     EEEKFRSLFN QIALSVDWNL EYQTISPLSR KISQMSFLDL VKKGEVYRNN QPILWDPVDG
     TALAQADIED KEKTSFMNYI TFKTEANDEF TIATTRPELL PACVAVFYHP DDKRYQHLAG
     KFAVTPLFNV KVPLLADPLV QQDKGTGLVM CCTFGDQTDI TWWKTHNLPL NTIITKKGTI
     DFPHEIGIDG LKIKEARAKI IDILKEQELF VKQEEITQTV KCAERSGAPL EVLTVPQWFV
     KTISHKDELL KRANELNWHP KNMKIRLDNW INAISWDWCI SRQRYFGVPF PVWYSKRIGE
     EGKILYADIS QLPVDPLKDL PIGYSKYEVE PDLDVMDTWA TSSVSPQLST WGISDEFAVN
     KDRHGKLFPM DLRPQAHEII RTWAFYTILK AHLHQNTLPW KNIMVSGWCL AEDRSKMSKS
     KGNVLVPEKL LEQYGSDVIR YWSANSKLGA DTAYSEDVMK NGKRLVNKLW NAAKFVSQHF
     DKLSDEDKKT NLIDVKEKIT HEFDQWIINK LVELVNNATN ELQNYEYANA MHLTEKFFWS
     VFCDNYLEIS KTRAYDEENK NPSGQYSSVL TLYHVMQTLL KLFAPFMPHI TEELYQILYS
     ENSIHIKGNW INYGNLNYKI DAKQPERLLE ILDHVRKFKA EKNLSIKAEV QLLEVSGIEL
     SKELTSDLKN VTSAKEVKFK PTNDEIKVSI LT