ID   SYV_CHLCV               Reviewed;         940 AA.
AC   Q822K4;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Valine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02004};
DE            EC=6.1.1.9 {ECO:0000255|HAMAP-Rule:MF_02004};
DE   AltName: Full=Valyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02004};
DE            Short=ValRS {ECO:0000255|HAMAP-Rule:MF_02004};
GN   Name=valS {ECO:0000255|HAMAP-Rule:MF_02004}; OrderedLocusNames=CCA_00678;
OS   Chlamydia caviae (strain ATCC VR-813 / DSM 19441 / 03DC25 / GPIC)
OS   (Chlamydophila caviae).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=227941;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-813 / DSM 19441 / 03DC25 / GPIC;
RX   PubMed=12682364; DOI=10.1093/nar/gkg321;
RA   Read T.D., Myers G.S.A., Brunham R.C., Nelson W.C., Paulsen I.T.,
RA   Heidelberg J.F., Holtzapple E.K., Khouri H.M., Federova N.B., Carty H.A.,
RA   Umayam L.A., Haft D.H., Peterson J.D., Beanan M.J., White O.,
RA   Salzberg S.L., Hsia R.-C., McClarty G., Rank R.G., Bavoil P.M.,
RA   Fraser C.M.;
RT   "Genome sequence of Chlamydophila caviae (Chlamydia psittaci GPIC):
RT   examining the role of niche-specific genes in the evolution of the
RT   Chlamydiaceae.";
RL   Nucleic Acids Res. 31:2134-2147(2003).
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_02004}.
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_02004};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_02004}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02004}.
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_02004}.
CC   -!- DOMAIN: The C-terminal coiled-coil domain is crucial for aminoacylation
CC       activity. {ECO:0000255|HAMAP-Rule:MF_02004}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       ValS type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_02004}.
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DR   EMBL; AE015925; AAP05420.1; -; Genomic_DNA.
DR   RefSeq; WP_011006635.1; NC_003361.3.
DR   AlphaFoldDB; Q822K4; -.
DR   SMR; Q822K4; -.
DR   STRING; 227941.CCA_00678; -.
DR   EnsemblBacteria; AAP05420; AAP05420; CCA_00678.
DR   KEGG; cca:CCA_00678; -.
DR   eggNOG; COG0525; Bacteria.
DR   HOGENOM; CLU_001493_0_2_0; -.
DR   OMA; FATKLWN; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000002193; 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; 1.10.287.380; -; 1.
DR   Gene3D; 3.40.50.620; -; 2.
DR   Gene3D; 3.90.740.10; -; 1.
DR   HAMAP; MF_02004; Val_tRNA_synth_type1; 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; IPR010978; tRNA-bd_arm.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   InterPro; IPR037118; Val-tRNA_synth_C_sf.
DR   InterPro; IPR019499; Val-tRNA_synth_tRNA-bd.
DR   InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR   InterPro; IPR002303; Valyl-tRNA_ligase.
DR   PANTHER; PTHR11946; PTHR11946; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 2.
DR   Pfam; PF10458; Val_tRNA-synt_C; 1.
DR   PRINTS; PR00986; TRNASYNTHVAL.
DR   SUPFAM; SSF46589; SSF46589; 1.
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; Coiled coil; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..940
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_0000224458"
FT   COILED          872..938
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT   MOTIF           47..57
FT                   /note="'HIGH' region"
FT   MOTIF           564..568
FT                   /note="'KMSKS' region"
FT   BINDING         567
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ   SEQUENCE   940 AA;  107370 MW;  493BD25B020E967E CRC64;
     MEEDEFSKAY DPKGLEDKLY AFWEGSGMFT AQSASDKPPY AIIMPPPNVT GILHMGHALV
     NTLQDVLIRY KRMSGFEVCW VPGTDHAGIA TQTVVERHLY ASLGKRRIDF SREEFIKHVW
     EWKEKSEGVI LSQLRQLGCS CDWSRLRFTM EPLANRAVKK AFKALFDKGH IYRGYYLVNW
     DPVLQTALAD DEVEYEEKDG WLYYIRYKVV DSSEEIIVAT TRPETLLGDT AIAISPDDER
     YSHLLGAKVH LPFVDREIPI IGDMSVDPLF GTGAVKITPA HDRDDYRTGI NHNLPMVNIL
     APTGEINENG GIFAGLSKEK AREDIITALE AMGLFVKKEP YKLRVGVSYR SGAVIEPYLS
     KQWFVSVESF RDSLREFVAN DSIKIFPPEF TRNYLSWVNN LRDWCISRQL WWGHRIPVWY
     HKSDEDRILC YDGEGIPEEV AQDPDSWYQD PDVLDTWFSS GLWPLTCLGW PDVESGDLEK
     FYPTAVLITG HDILFFWVTR MVLLCSAMVE EKPFSDVFLH GLIFGKSYKR YNDLGEWTYI
     SGEEKHAYDM GKALPKDVVA KWEKLSKSKG NVIDPLEMIG KYGADAVRMT LCSCANRGEQ
     IDLDYRLFEE YKNFANKIWN GARFIFGHIS NLTSKDLVYG IDKDLLGLED FYILDGFNQL
     LKQLESAYQS YAFDKITTMA YEFFRNDFCS TYIEIIKPTL YGKQGNEEDR LTKQKLLAVL
     LVNILGVLHP ITPFVTETLF LKLKATLGDV DAPCADTITA HALDMLRAES YVVAPYPQAI
     DIAIPKDLHE SFALAERLVY TIRNIRGEMQ LDPRASLEVF VICPEGISIE TYVPMMCALG
     GIASLEYLSE EPKDRVYSLG VVEGIRLGVF VPMEHITKER NRLEKEKMRL ENSIESVSRL
     LSSESFRAKA NPDLVRSKEE TLKNNRMELQ SILDKLASFS