ID   SYV_SULAC               Reviewed;         831 AA.
AC   Q4J8X1;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 95.
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=Saci_1430;
OS   Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS   15157 / NCIMB 11770).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=330779;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX   PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA   Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA   Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT   "The genome of Sulfolobus acidocaldarius, a model organism of the
RT   Crenarchaeota.";
RL   J. Bacteriol. 187:4992-4999(2005).
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; CP000077; AAY80759.1; -; Genomic_DNA.
DR   RefSeq; WP_011278261.1; NC_007181.1.
DR   AlphaFoldDB; Q4J8X1; -.
DR   SMR; Q4J8X1; -.
DR   STRING; 330779.Saci_1430; -.
DR   EnsemblBacteria; AAY80759; AAY80759; Saci_1430.
DR   GeneID; 3473472; -.
DR   KEGG; sai:Saci_1430; -.
DR   PATRIC; fig|330779.12.peg.1377; -.
DR   eggNOG; arCOG00808; Archaea.
DR   HOGENOM; CLU_001493_0_2_2; -.
DR   OMA; FATKLWN; -.
DR   Proteomes; UP000001018; 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..831
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_0000224634"
FT   MOTIF           77..87
FT                   /note="'HIGH' region"
FT   MOTIF           564..568
FT                   /note="'KMSKS' region"
FT   BINDING         567
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02005"
SQ   SEQUENCE   831 AA;  96937 MW;  F5BECCFF405B7957 CRC64;
     MTISALELIS YYTKFLSMLS QDEINKKLEE WPKHYDPKGI ELKWQNIWMT KEFWEKVFRF
     RDEDEKSPVF VIDTPPPFTS GELHMGHAYW VTISDTIGRF KRLEGYNVLL PQGWDTQGLP
     TELKVQYKLK VPKENRELFL KKCIEWTEDM IKSMRTAMIR LGYRAEWERF EYRTYESKYR
     RIIQKSLIDM HKMGLVEMRE GPVYWCPKCE TALAQSEVGY KEEDGVLAYI LFPFVDGEGG
     VTIATTRPEL LGATQAVAVN PDDERYKSLV GRKVKIPLFD KEISIIADKA VEMTFGTGAV
     MISTYGDPQD IRWQLTYRLP VYEVVDDKGK IKNTNGLLDG LTVKEARKKI IEILKEKGYL
     IKVEKITHNV LAHTERSDCL SPIEFLIKKQ IYIKVLEWRN KLLEDYKKMK FTPQRMSYYL
     EEWIKNLEWD WNISRQRVYG TPLPFWYCDN GHLIPAPEEV LPIDPSKVNP PVEKCPHCGL
     DLKPVKDVAD VWVDSSVTVL YLTGFYDDKS RFTKTFPSSL RLQGTDIIRT WLFYTYYRTL
     ALAGNIPFKE VLINGQVLGP DGTRMSKSKG NVVSPLDKVD EYGADAIRLT LLDAKIGDDF
     PFKWDTVKSK KLLLQKLWNA GRLSYPFIGK KKINKPSKLH EIDKWILQEH KKFVQQSIEA
     YRNYDFYIVV ESIYSYFWET IADEYLELIK HRLFMEDESA IYTLSRIIKD LLILLYPIAP
     HITEEMYERL YGDKMSIALE NLPDTSDLED DGEAQKLGEY IKKATSAIRT LKIQNRLAIP
     TPISVKIYGP DDFIAKIKII EEDLKKTLKL IDIIYQENNE IKVELLSDHG S