ID   SYV_PICTO               Reviewed;         768 AA.
AC   Q6L1N5;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 105.
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=PTO0532;
OS   Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC
OS   100828).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Picrophilaceae; Picrophilus.
OX   NCBI_TaxID=263820;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828;
RX   PubMed=15184674; DOI=10.1073/pnas.0401356101;
RA   Fuetterer O., Angelov A., Liesegang H., Gottschalk G., Schleper C.,
RA   Schepers B., Dock C., Antranikian G., Liebl W.;
RT   "Genome sequence of Picrophilus torridus and its implications for life
RT   around pH 0.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9091-9096(2004).
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; AE017261; AAT43117.1; -; Genomic_DNA.
DR   RefSeq; WP_011177333.1; NC_005877.1.
DR   AlphaFoldDB; Q6L1N5; -.
DR   SMR; Q6L1N5; -.
DR   STRING; 263820.PTO0532; -.
DR   EnsemblBacteria; AAT43117; AAT43117; PTO0532.
DR   GeneID; 2845375; -.
DR   KEGG; pto:PTO0532; -.
DR   PATRIC; fig|263820.9.peg.560; -.
DR   eggNOG; arCOG00808; Archaea.
DR   HOGENOM; CLU_001493_0_2_2; -.
DR   OMA; FATKLWN; -.
DR   OrthoDB; 4914at2157; -.
DR   Proteomes; UP000000438; 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; Reference proteome.
FT   CHAIN           1..768
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_0000224630"
FT   MOTIF           37..47
FT                   /note="'HIGH' region"
FT   MOTIF           510..514
FT                   /note="'KMSKS' region"
FT   BINDING         513
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02005"
SQ   SEQUENCE   768 AA;  89456 MW;  EE8EEDF079DF3DA3 CRC64;
     MLDINEMENK WKDYWFNNDV FKFRPGNKIF IIDTPPPTVS GKMHMGHAYS YPHQDFMARY
     MRMKGFSVYY PWGFDDNGLP TERYVEKERH VTIRNTPLDE YIKICREASR DAEKILLKNW
     YDLGLSCDFK NYIETSSDFS TRISQELFID LVLNNRAYRA EAPVIRCPTC NTAISQIDMK
     DTEIDTDLVY INFSGIEIAT TRPELLGACV ALVVNPNDPR YKKIINSEVV VPLYNYTVRI
     ISDDSIDMNF GTGAEMLCTF GDQHDLELWR KYNPGTRIII KNDLIDDGII IKGLSVKEAR
     KEIIKKLKEN NYLIKTERIK HSVNTHERCG TPVEIIISKQ WYIKDLDIKD ELLDLGNRIE
     WIPDYMKTRY QNWVSGLKWD WCISRQRYYG IPFPVWYCKD CGGIVLADKS ELPVDPRLSG
     TNKRCSCGSG NLEPETDVMD TWATSSISVT LYLMHINSMN LYPADVRFQG HDIITSWAFT
     TILRSYLHYR DVPWKKIFIS GNVYDPYGEK MSKSKGNIIE PSTIIEKYGA DALRFWASTT
     MPGENIKIRE QDLVRGRKTV IKLYNSARLV LMLSDNIKGS MDNIISQVNR WILTKFEKTL
     KNVTELMDGY YFSRARSELD NFFWNIFCDN YLEIIKSEIK RYPEETAAVS RFLMENIIKM
     YSPIMPFITE ELYHEFNKDS LSVSLEKYPE YNEDYIFDGA EDFDYIIDII NKIRAIKSNM
     KMSMAAPISI SLKGNEKIIN DSAEIIKSVM HVENLKISNS DNIEIEVQ