SYV_THEVO
ID SYV_THEVO Reviewed; 790 AA.
AC Q97CR9;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, 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=TV0032;
GN ORFNames=TVG0034869;
OS Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC
OS 15438 / GSS1).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1;
RX PubMed=11121031; DOI=10.1073/pnas.97.26.14257;
RA Kawashima T., Amano N., Koike H., Makino S., Higuchi S., Kawashima-Ohya Y.,
RA Watanabe K., Yamazaki M., Kanehori K., Kawamoto T., Nunoshiba T.,
RA Yamamoto Y., Aramaki H., Makino K., Suzuki M.;
RT "Archaeal adaptation to higher temperatures revealed by genomic sequence of
RT Thermoplasma volcanium.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:14257-14262(2000).
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; BA000011; BAB59174.1; -; Genomic_DNA.
DR RefSeq; WP_010916289.1; NC_002689.2.
DR AlphaFoldDB; Q97CR9; -.
DR SMR; Q97CR9; -.
DR STRING; 273116.14324246; -.
DR PRIDE; Q97CR9; -.
DR EnsemblBacteria; BAB59174; BAB59174; BAB59174.
DR GeneID; 1441518; -.
DR KEGG; tvo:TVG0034869; -.
DR eggNOG; arCOG00808; Archaea.
DR HOGENOM; CLU_001493_0_2_2; -.
DR OMA; FATKLWN; -.
DR OrthoDB; 4914at2157; -.
DR PhylomeDB; Q97CR9; -.
DR Proteomes; UP000001017; 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.
FT CHAIN 1..790
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224638"
FT MOTIF 40..50
FT /note="'HIGH' region"
FT MOTIF 521..525
FT /note="'KMSKS' region"
FT BINDING 524
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02005"
SQ SEQUENCE 790 AA; 91205 MW; C4FFCA069E8753CF CRC64;
MDLDIDQMEK KWLKYWEDND IYTFIPSERE KVFTIDTPPP TVSGKMHMGH SFSYSHIDFI
ARYKRMRGYH VFFPWGFDDN GLATERYVEK ETGIKPTDGN VEHFINLCRE FSQASEKALI
EGWKRMGMSC YFKDYYVTSS PESVKISQSM FLDLVKKNRV YRDLAPTIRC PTCKTSISQI
EMKDEMLKSK LVYINFDVEG SKLTIATSRP ELLGSCVALF VNNEDERYKN IIGREATVPL
FGHKVPIMGD ESIDKDFGTG AEMVCTFGDQ NDLDLWKKYS LPLRISIDKD GKMNENAGPL
NGLSINDGRK KIIELLKSEG FVVKEEDIKH SVNTHERCGT PVEIFIEKQW FIRYLDLKKD
FIDSGRAVKW IPDYMRTRYE NWVNGLKWDW CISRQRYYGV PFPVWYCSDC GNTVFADDKD
LPVDPRLQPP SKRCDKCGSS NLVPERDVMD TWATSSLTPR IALSHFGLFD KYYPEDLRGQ
GHDIISFWAF TTIARSKIHD NTIPWLTLMI SGNVFDMYGE KMSKSKGNIV DIYAITDKYG
ADALRFWAST VSQGEDIRVK EQDFVRGRRT VIKMYNANRL IDILRNGRPL KNVDEPKHPV
NLWILTEESK VVKLVTDSMD NYEVSKARSA LDVFFWNTFC DNYLEMIKAI VQAANEKNDL
GTVDETIYTA SKVMRDVVKM YAPIMPFITE EIYQSIEIEG KKKSVHIDCW PMENREYVEA
SEVRYVTSII DKIRAAKSNA KVSVGTPVRK ALIKCNASIA EKYRDMLSRM MRIGSIDIED
SDKLEVSVEP
