SYV_STRMU
ID SYV_STRMU Reviewed; 883 AA.
AC Q8DSL1;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Valine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02004};
DE EC=6.1.1.9 {ECO:0000255|HAMAP-Rule:MF_02004};
DE AltName: Full=Valyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02004};
DE Short=ValRS {ECO:0000255|HAMAP-Rule:MF_02004};
GN Name=valS {ECO:0000255|HAMAP-Rule:MF_02004}; OrderedLocusNames=SMU_1770;
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159;
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(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. {ECO:0000255|HAMAP-Rule:MF_02004}.
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_02004};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_02004}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02004}.
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_02004}.
CC -!- DOMAIN: The C-terminal coiled-coil domain is crucial for aminoacylation
CC activity. {ECO:0000255|HAMAP-Rule:MF_02004}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC ValS type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_02004}.
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DR EMBL; AE014133; AAN59398.1; -; Genomic_DNA.
DR RefSeq; NP_722092.1; NC_004350.2.
DR RefSeq; WP_002352358.1; NC_004350.2.
DR AlphaFoldDB; Q8DSL1; -.
DR SMR; Q8DSL1; -.
DR STRING; 210007.SMU_1770; -.
DR PRIDE; Q8DSL1; -.
DR EnsemblBacteria; AAN59398; AAN59398; SMU_1770.
DR KEGG; smu:SMU_1770; -.
DR PATRIC; fig|210007.7.peg.1580; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_9; -.
DR OMA; FATKLWN; -.
DR PhylomeDB; Q8DSL1; -.
DR Proteomes; UP000002512; 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; 1.10.287.380; -; 1.
DR Gene3D; 3.40.50.620; -; 2.
DR Gene3D; 3.90.740.10; -; 1.
DR HAMAP; MF_02004; Val_tRNA_synth_type1; 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; IPR010978; tRNA-bd_arm.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR InterPro; IPR037118; Val-tRNA_synth_C_sf.
DR InterPro; IPR019499; Val-tRNA_synth_tRNA-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; 2.
DR Pfam; PF10458; Val_tRNA-synt_C; 1.
DR PRINTS; PR00986; TRNASYNTHVAL.
DR SUPFAM; SSF46589; SSF46589; 1.
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; Coiled coil; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..883
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224573"
FT COILED 809..883
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 46..56
FT /note="'HIGH' region"
FT MOTIF 520..524
FT /note="'KMSKS' region"
FT BINDING 523
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 883 AA; 100935 MW; 4ACCEAACC06FA33D CRC64;
MSTQLSPKYN PAEVEADRYQ KWLDADVFKP SGDQKAKPYS IVIPPPNVTG KLHLGHAWDT
TLPDIIIRQK RMQGFDTLWL PGMDHAGIAT QAKVEARLAE DGISRYDLGR EKFLDKVWEW
KDEYAATIKE QWGKMGISVD YSRERFTLDE GLSKAVRKVF VELYKKGWIY RGEFIINWDP
KARTALSDIE VIHKDVEGAF YHMNYMLEDG SRALEVATTR PETMFGDTAV AVNPNDDRYK
DLIGQNVILP IVNKLIPIVA DEHADPEFGT GVVKITPAHD PNDFLVGQRH NLPQVNVMND
DGTMNELAGE FAGMDRFEAR KATVKKLEEI GALVEIEKMT HSVGHSERTG VPIEPRLSTQ
WFVKMDQLAK NAIANQDTDD KVDFYPPRFN DTFLQWMENV HDWVISRQLW WGHQIPAWYN
ADGDMYVGEE APEGDGWKQD EDVLDTWFSS ALWPFSTMGW PDTDSEDFKR YFPTSTLVTG
YDIIFFWVSR MIFQSLEFTG CRPFQNVLIH GLIRDEQGRK MSKSLGNGID PMDVVDKYGA
DALRWFLSNG SAPGQDVRFS YEKMDAAWNF INKIWNISRY ILMNNEGLSL DQASKNVVLV
TNGKAGNVTD RWILHNLNET IAKVTENFDK FEFGVAGHIL YNFIWDEFAD WYVELTKEVL
YSEDEAEKVI TRSVLLYTLD KILRLLHPIM PFVTEEIFGQ YADGSIVTAA YPTVNPAFEN
QTAHSGVESL KDLIRAVRNA RAEVNVAPSK PITILVKTSD SNLEDFFKAN VNYIKRFTNP
ETLEISSAIA TPELAMSAVI TGAEIFLPLA DLLNVEEELA RLNKELAKWQ KELDIVAKKL
SNDRFVQNAK PEIVQKERDK QIDYQTKYDA TVERIKEMEK LIK
