ID   SYV_RICRS               Reviewed;         812 AA.
AC   A8GTB4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   03-AUG-2022, entry version 76.
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=A1G_05850;
OS   Rickettsia rickettsii (strain Sheila Smith).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=392021;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sheila Smith;
RA   Madan A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA   Sanchez A., Dasch G., Eremeeva M.;
RT   "Complete genome sequence of Rickettsia rickettsii.";
RL   Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000848; ABV76639.1; -; Genomic_DNA.
DR   RefSeq; WP_012151193.1; NC_009882.1.
DR   AlphaFoldDB; A8GTB4; -.
DR   SMR; A8GTB4; -.
DR   EnsemblBacteria; ABV76639; ABV76639; A1G_05850.
DR   GeneID; 45539571; -.
DR   KEGG; rri:A1G_05850; -.
DR   HOGENOM; CLU_001493_0_2_5; -.
DR   OMA; RQWYIRN; -.
DR   Proteomes; UP000006832; 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_1000022185"
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;  94266 MW;  BD1DAC36DC522DA5 CRC64;
     MKEFPKNYNF TENEKKWQQI WQEKQIYAYN PNVAKEETYV IDTPPPTVSG QLHIGHVYSY
     TQTDFIVRFQ RMMGKNIFYP MGFDDNGLPT ERLVEKQKQI KAYNMERSEF IKICEEVVES
     EEEKFRSLFN QIALSVDWSL EYQTISPLSR KISQMSFLDL VQKEEIYRTN QPILWDPVDG
     TALAQADIED KEQTSFMNYI TFKTEQGDPL TIATTRPELL PACVAVFYHP DDGRYKHLAG
     KSAITPLFNE QVPLLADPLV RQDKGTGLVM CCTFGDQTDI TWWKTHNLPL KTIITKKGTI
     DCQHETSIDG LKIKEARTKI IAILKEQELL IKQEDITHTV KCAERSGAPL EILTVPQWFV
     KTISHKEELL KRANELNWHP KNMKIRLENW INAISWDWCI SRQRYFGVPF PVWYSKRVGE
     EGKILYADIT QLPIDPLKDL PMGYSKEEVE PDYDVMDTWA TSSVSPQLST HGISDDFAVN
     KDRHDKLFPM DLRPQAHEII RTWAFYTILK AHLHQNTLPW KNIMISGWCL AEDRSKMSKS
     KGNVLVPEKL LEQYGSDVIR YWSANSKLGA DTAYSEDVMK NGKRLVNKLW SAAKFVFIHF
     DKLKGEDKKA SLLDIKEKIT NEFDKWMVNK LVELVKLATN ELQNYEYANA MHLTEKFFWV
     VFCDNYLEIS KTRSYDEEHK NPQGQYSSIL TLYHVMQTLL KLFAPFMPHI TEELYQILYS
     ENSIHVKGSW VNYSDLNYEI NAKGAEGLLE ILDIVRKFKA EKNLSIKAPI KLLEVSGIVL
     SAELAEDLKN VTSADEIQFE MKDDKIKVNI IL