ID   SYV_PYRAE               Reviewed;         799 AA.
AC   Q8ZVG2;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Valine--tRNA ligase;
DE            EC=6.1.1.9;
DE   AltName: Full=Valyl-tRNA synthetase;
DE            Short=ValRS;
GN   Name=valS; OrderedLocusNames=PAE2297;
OS   Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP
OS   104966 / NBRC 100827 / IM2).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=178306;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2;
RX   PubMed=11792869; DOI=10.1073/pnas.241636498;
RA   Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I.,
RA   Miller J.H.;
RT   "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT   aerophilum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002).
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 (By similarity). {ECO:0000250}.
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       ValS type 2 subfamily. {ECO:0000305}.
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DR   EMBL; AE009441; AAL64094.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8ZVG2; -.
DR   SMR; Q8ZVG2; -.
DR   STRING; 178306.PAE2297; -.
DR   EnsemblBacteria; AAL64094; AAL64094; PAE2297.
DR   KEGG; pai:PAE2297; -.
DR   PATRIC; fig|178306.9.peg.1710; -.
DR   eggNOG; arCOG00808; Archaea.
DR   HOGENOM; CLU_001493_0_2_2; -.
DR   InParanoid; Q8ZVG2; -.
DR   OMA; FATKLWN; -.
DR   Proteomes; UP000002439; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004832; F:valine-tRNA ligase activity; IBA:GO_Central.
DR   GO; GO:0006438; P:valyl-tRNA aminoacylation; IBA:GO_Central.
DR   CDD; cd07962; Anticodon_Ia_Val; 1.
DR   Gene3D; 3.40.50.620; -; 2.
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; 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.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..799
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_0000224631"
FT   BINDING         536
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   799 AA;  93224 MW;  E480A051DC2C5906 CRC64;
     MAHRLPTRWD IKWEEELLKL WEKEGRFKTK ISGSRPVFVI DTPPPYLSSN RPHIGQTASY
     AHFDMIARFL RMRGVDVIFP FYLDRNGLPI EVQVEKKYGV VAHEIPREKF IKMCKEELDS
     YEGEFVSSLR RWGLSFDYWP NGTDSPEYRR MTQKTFIELW HKGLVYEAER PTPWCPRCRT
     ALAEPEIEYR EEETYLNYIK FKVKETGEDI IIATTRPELL PATVAVIFHP DDSRYTRLNG
     MHAVVPPEGQ VVPILPHKAA NPNFGSGLVM ISTFGDTRDL MIVNELKLPI RIIIDEGGRI
     KTGKYAGVSI REARAKIIED LKNAGLLVKQ ERLVHNVPVC WRCKTPLEII VTRELFIKQI
     EFKEKLIELA GKMEFKPPEY RQVLIDWIKS LELDWPVSRR RYYATEIPIW WCAKPNGERV
     PLLPKGGEYY VPWRDEPPPE VKEACKDGRL EGDTRVFDTW FDSSISWMYA SGVTKDFNAF
     SKVYPHSIMR PQGYDIIRTW LYYSLLRAYL LYGDVPFRYV RINGMGLDEK GEAMHKSKGN
     VIDLLAPVEK YGADPVRFWA AAAGRLGTDY RYNENVIREG KEFLTKVWNI SRFVLSFPEP
     QQKPQLAPVD RALLARLYDV AKKVITAYSE FDVYEPAHAL YNFIWHEFAD HYIELVKSRA
     YNREGVFTEE EQRAAIWTLY TAWRYSLKLL APIMPFVTDK IWREAYGRSI HDEMIEDPPE
     EWKEGDQALF HLVKKINSAV WRYKNRRGMS LADRLDAVLY VSELAMQAAK DLKYMHKVSD
     VRPGRGAEQI DDEGLVWLG