ID   SYV_THEAC               Reviewed;         791 AA.
AC   Q9HM29;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 110.
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=Ta0040;
OS   Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS   15155 / AMRC-C165).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Thermoplasmataceae; Thermoplasma.
OX   NCBI_TaxID=273075;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX   PubMed=11029001; DOI=10.1038/35035069;
RA   Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA   Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT   "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT   acidophilum.";
RL   Nature 407:508-513(2000).
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   -!- 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; AL445063; CAC11189.1; -; Genomic_DNA.
DR   RefSeq; WP_010900468.1; NC_002578.1.
DR   AlphaFoldDB; Q9HM29; -.
DR   SMR; Q9HM29; -.
DR   STRING; 273075.Ta0040; -.
DR   PRIDE; Q9HM29; -.
DR   EnsemblBacteria; CAC11189; CAC11189; CAC11189.
DR   GeneID; 1455707; -.
DR   KEGG; tac:Ta0040; -.
DR   eggNOG; arCOG00808; Archaea.
DR   HOGENOM; CLU_001493_0_2_2; -.
DR   OMA; FATKLWN; -.
DR   OrthoDB; 4914at2157; -.
DR   Proteomes; UP000001024; 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   Gene3D; 3.90.740.10; -; 1.
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..791
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_0000224637"
FT   MOTIF           40..50
FT                   /note="'HIGH' region"
FT   MOTIF           521..525
FT                   /note="'KMSKS' region"
FT   BINDING         524
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02005"
SQ   SEQUENCE   791 AA;  91400 MW;  0FE25F5CCCC79E12 CRC64;
     MDIDVNQMEE KWIRYWDEKD VYRFEPADRD KVFAIDTPPP TVSGKMHMGH SFSYPHIDFI
     ARYKRMRGYH VFFPWGFDDN GLPTERYVEK ETGIKPSDSN VEEFIRLCKE ISESSEKSLL
     EGWKRIGMSC YFKDYYVTSS PESIRISQSM FLDLVRKGRV YRDLAPSIRC PTCKTSISQI
     EMKDQEMHTK LVYINFSVGD RPLTIATTRP EMLGSCVAVF VNPDDARYRD LIGKEATVPI
     FGNHVRIMAD ASVDMNFGTG AEMVCTFGDQ NDLDLWKKYN LPLKISIDKD GRMTEEAGPL
     KGLSISDARK KIVEILREGG HVVKEESIKH SVNTHERCGT PIEIFIEKQW FIKYLDLKDA
     FIENGRKIEW TPEYMRVRYE NWVNGLKWDW LISRQRYYGV PFPVWYCADC GNTVYADESE
     LPVDPRIQKP SKKCDRCGST NLVPERDVMD TWATSSLTPR IALTHFGLFD KYYPEDLRGQ
     GHDIISFWAF TTIARSKIHD DRIPWFRIMI SGNVYDMYGE KMSKSKGNIV DIYSMIDKYG
     ADALRFWAST VSQGDDIRIK DQDFTRGRRT VIKMYNAKKL IDILKGDRKI RLFEDVKHPV
     NRWILTEDSR IMETITTHMD NYEVSKARTA LDTFFWNVFC DNYLEMIKPI IQKASAAGDY
     DTVDETVYTA SKVMLDVAKA YAPIMPFIAE EIYQTIDFPG RKISIHVDSW PDEKRRYSDA
     NEEVSYIVSV IDAIRSAKSA AKVSVGTRVK VASVKGRKDL IEKYRDLLSG MLRIDSMEIA
     DGDAVDATVF P