ID   SYV_THEFY               Reviewed;         881 AA.
AC   Q47NK0;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 115.
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=Tfu_1936;
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Thermobifida.
OX   NCBI_TaxID=269800;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YX;
RX   PubMed=17209016; DOI=10.1128/jb.01899-06;
RA   Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M., DiBartolo G.,
RA   Martinez M., Lapidus A., Lucas S., Copeland A., Richardson P., Wilson D.B.,
RA   Kyrpides N.;
RT   "Genome sequence and analysis of the soil cellulolytic actinomycete
RT   Thermobifida fusca YX.";
RL   J. Bacteriol. 189:2477-2486(2007).
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; CP000088; AAZ55969.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q47NK0; -.
DR   SMR; Q47NK0; -.
DR   STRING; 269800.Tfu_1936; -.
DR   PRIDE; Q47NK0; -.
DR   EnsemblBacteria; AAZ55969; AAZ55969; Tfu_1936.
DR   KEGG; tfu:Tfu_1936; -.
DR   eggNOG; COG0525; Bacteria.
DR   HOGENOM; CLU_001493_0_2_11; -.
DR   OMA; RQWYIRN; -.
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   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..881
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_0000224616"
FT   REGION          493..526
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           76..86
FT                   /note="'HIGH' region"
FT   MOTIF           608..612
FT                   /note="'KMSKS' region"
FT   BINDING         611
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02005"
SQ   SEQUENCE   881 AA;  99445 MW;  567C9DBB98C1C8D0 CRC64;
     MGCRPRGPRG QAERAGSRCQ YHWPMTNRSR SFNVPDKPSL DGIEAKWVDV WDESGVYHFD
     RSKSREEIFA IDTPPPTVSG SLHIGHVFSY THTDTVARFQ RMNGKSVFYP MGWDDNGLPT
     ERRVQNYYGV RCDPSIPYDP DFTPPEKPDP KNQVPISRRN FIELCERLTV EDEKVFESIW
     RRLGLSVDWR YTYATIDDKS RAVAQRAFLR NLARGEAYMA EAPTLWDVTF RTAVAQAELE
     DRERPGAYHK VAFHRDGGDP IIIATTRPEL LPACVALVAH PDDERYQSLF GTTVRSPLFG
     VEVPVVAHRL ADPEKGTGIA MICTFGDVTD VTWWRELKLP TRAIIGWDGR IVADPPEGLD
     SEEGRAAYAK LAGATVHTAR QRIVEMLRES GDLIGEPEKI THPVKFFEKG DKPLEIVTTR
     QWYIRNGGRD PELREALLKR GQELDWYPEH MRTRFEHWVG GLNGDWLISR QRFFGVPFPV
     WYPLDDKGNP IYDSPILPDE SQLPVDPSSQ APEGYTEDQR GKPGGFIGDP DVMDTWATSS
     LTPQIAGGWE SDPDLFERVF PMDLRPQGQD IIRTWLFSTV VRSHFEHDCL PWKKAAISGW
     ILDPDRKKMS KSKGNVVTPL SMLEKYSSDA VRYWAASGRL GTDTALDEKQ MKIGRRLAIK
     ILNASKFALS VAGEDTVADP AAVTEPLDRS MLAVLAEVVQ DATAAFHEYD HTRALERTER
     FFWNLCDDYL ELVKARAYDP ESREGASARA ALLIALSVLH RLFAPFLPFV TEEVWSWWQD
     GSVHVAKWPS VEEFRAAAEA GDPAVLAATS EVLHTVRKAK SEAKLSMRAE VERVTVHGKQ
     AEQARLCRDD LAAAGRVTTL VFETTDDAEL RVDVELAPAE K