ID   SYV_SALTO               Reviewed;         860 AA.
AC   A4X0V0;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 93.
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=Strop_0015;
OS   Salinispora tropica (strain ATCC BAA-916 / DSM 44818 / CNB-440).
OC   Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC   Salinispora.
OX   NCBI_TaxID=369723;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-916 / DSM 44818 / CNB-440;
RX   PubMed=17563368; DOI=10.1073/pnas.0700962104;
RA   Udwary D.W., Zeigler L., Asolkar R.N., Singan V., Lapidus A., Fenical W.,
RA   Jensen P.R., Moore B.S.;
RT   "Genome sequencing reveals complex secondary metabolome in the marine
RT   actinomycete Salinispora tropica.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:10376-10381(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}.
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; CP000667; ABP52500.1; -; Genomic_DNA.
DR   RefSeq; WP_011903937.1; NC_009380.1.
DR   AlphaFoldDB; A4X0V0; -.
DR   SMR; A4X0V0; -.
DR   STRING; 369723.Strop_0015; -.
DR   EnsemblBacteria; ABP52500; ABP52500; Strop_0015.
DR   KEGG; stp:Strop_0015; -.
DR   PATRIC; fig|369723.5.peg.15; -.
DR   eggNOG; COG0525; Bacteria.
DR   HOGENOM; CLU_001493_0_2_11; -.
DR   OMA; RQWYIRN; -.
DR   Proteomes; UP000000235; 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   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..860
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_1000088571"
FT   REGION          469..491
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           43..53
FT                   /note="'HIGH' region"
FT   MOTIF           574..578
FT                   /note="'KMSKS' region"
FT   BINDING         577
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02005"
SQ   SEQUENCE   860 AA;  95775 MW;  B83612E2219E8A90 CRC64;
     MPAKASLEGI EKVWSRVWEQ NGTYRFDRSV TRSEVYSVDT PPPTVSGALH VGHVFSYTHS
     DAIARFQRMR GRAVFYPMGW DDNGLPTERR VQNYYGVRCD PSLPYDPGYT PPAEPPSRPQ
     PISRRNFVEL CRNLTELDEQ AFEALWRHLG LSVDWSLTYA TIDDRSRAIS QRAFLRNLAR
     GEAYLADAPT LWDVTFRTAV AQAELEDRER QGTYYRLAFH SATGDKIYVE TTRPELLPAC
     VALVAHPDDE RYQHLLGSTA VSPLFGVPVP IRAHPLAQPD KGSGIAMICT FGDLTDVLWW
     RELALPTRPV MGRDGRLLPE PPPGIVNADA VAAYQTLAGL TAFSAKAKVV ELLRAAGDLE
     IAPRPTTQTV KFYEKGDKPL EIITTRQWYV RNGGRDTELR SALVHRGREL TWSPEFMRSR
     YENWVEGLSG DWVISRQRFF GVPIPVWYPL DDSGEPDYAH PILPDDVALP VDPSSDAPTG
     YQESQRNQPG GFMADPDVMD TWATSSLTPE IAGGWTVDDD LFARVFPMDL RPQAHEIIRT
     WLFATVLRSH QEFNCLPWTT VLLSGWILDP DRKKMSKSKG NTVTPMALLE KYGSDAVRYW
     AVSGRPGTDT AFDTGQMKIG RRLAIKILNA TTFVLRFGSP TLLAPHMAHV TEPLDRSMLA
     RLASVVDSAT TGFTQHDYTR SLECTEQFFW SFCDDYLELV KERAYGEPDD RAVRSAHAAL
     ALALHTLLRL FAPMLPFVTE EAWSWWQEGS VHRAAWPTGQ ELVGPDVSAE ANRSTEASGS
     GEAGTDLLGL ASDVLAAIRR AKSEAKQSMR APVAQLTLRG RASDLAAFAL VSRDVRAAGV
     VREVDTAEAD TPLTPEITLG