ID   SYV_RICPU               Reviewed;         812 AA.
AC   C4K2L1;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 69.
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=RPR_06530;
OS   Rickettsia peacockii (strain Rustic).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=562019;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rustic;
RX   PubMed=20027221; DOI=10.1371/journal.pone.0008361;
RA   Felsheim R.F., Kurtti T.J., Munderloh U.G.;
RT   "Genome sequence of the endosymbiont Rickettsia peacockii and comparison
RT   with virulent Rickettsia rickettsii: identification of virulence factors.";
RL   PLoS ONE 4:E8361-E8361(2009).
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; CP001227; ACR47808.1; -; Genomic_DNA.
DR   AlphaFoldDB; C4K2L1; -.
DR   SMR; C4K2L1; -.
DR   EnsemblBacteria; ACR47808; ACR47808; RPR_06530.
DR   KEGG; rpk:RPR_06530; -.
DR   HOGENOM; CLU_001493_0_2_5; -.
DR   OMA; RQWYIRN; -.
DR   Proteomes; UP000005015; 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_1000216266"
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;  94346 MW;  E8EC7BD07BBDA1C2 CRC64;
     MKEFPKNYNF TENEKKWQQI WQEKQIYAYN PNVAKEETYV IDTPPPTVSG QLHIGHVYSY
     TQTDFIVRFQ RMMGKNIFYP MGFDDNGLPT ERLVEKQKQI KAYNMDRSEF IKICEEVVES
     EEEKFRSLFN QIALSVDWSL EYQTISPLSR KISQMSFLDL VQKEEIYLTN QPILWDPVDG
     TALAQADIED KEKTSFMNYI TFKTEQGDPL TIATTRPELL PACVAVFYHP DDGRYKHLAG
     KSAITPLFNE QVPLLADPLV RQDKGTGLVM CCTFGDQTDI TWWKTHNLPL KTIITKKGTI
     DFQHETSIDG LKIKEARTKI IDILKEQELL IKQEDITHTV KCAERSGAPL EILTVPQWFV
     KTISHKEELL KRANELNWHP KNMKIRLENW INAISWDWCI SRQRYFGVPF PVWYSKRVGE
     EGKILYADVT QLPIDPLKDL PMGYSKEEVE PDYDVMDTWA TSSVSPQLST HGISDDFAVN
     KDRHDKLFPM DLRPQAHEII RTWAFYTILK AHLHQNTLPW KNIMISGWCL AEDRSKMSKS
     KGNVLVPEKL LEQYGSDVIR YWSANSKLGA DTAYSEDVMK NGKRLVNKLW NAAKFVFIHF
     DKLKGEDKKA SLLDIKEKIT NEFDKWMVNK LVELVKLATN ELQNYEYAHA MHLTEKFFWV
     VFCDNYLEIS KTRSYDEEHK NPQGQYSSIL TLYHVMQTLL KLFAPFMPHI TEELYQILYS
     KNSIHVKGSW VNYSDLNYEI NAKGAEGLLE ILDIVRKFKA EKNLSIKAPI KLLEVSGIVL
     SAELAEDLKN VTSAEEIQFE MKDDKIKVNI IL