SYV_CHLMU
ID SYV_CHLMU Reviewed; 939 AA.
AC Q9PK91;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 125.
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=TC_0576;
OS Chlamydia muridarum (strain MoPn / Nigg).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=243161;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MoPn / Nigg;
RX PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA Salzberg S.L., Eisen J.A., Fraser C.M.;
RT "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT AR39.";
RL Nucleic Acids Res. 28:1397-1406(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_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; AE002160; AAF39411.1; -; Genomic_DNA.
DR PIR; H81686; H81686.
DR RefSeq; WP_010230885.1; NZ_CP027217.1.
DR AlphaFoldDB; Q9PK91; -.
DR SMR; Q9PK91; -.
DR STRING; 243161.TC_0576; -.
DR EnsemblBacteria; AAF39411; AAF39411; TC_0576.
DR GeneID; 1245935; -.
DR KEGG; cmu:TC_0576; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_0; -.
DR OMA; FATKLWN; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000000800; 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.
FT CHAIN 1..939
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000106220"
FT COILED 873..939
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 47..57
FT /note="'HIGH' region"
FT MOTIF 563..567
FT /note="'KMSKS' region"
FT BINDING 566
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 939 AA; 107122 MW; 1D141FA682187869 CRC64;
MNEDQFPKAY DPKSSESGVY SFWERSGMFI ADANSKKPAY SIVMPPPNVT GILHMGHALV
NTLQDMLIRY KRMKGFEVCW VPGTDHAGIA TQTVVERHLR SSLGKRRTDF SREEFLKHVW
EWKEKSQNVI LSQLRQLGCS CDWSRQRFTM DPEANRAVKK AFKVLFDKGV IYRGYYLVNW
DPILQTALAD DEVEYEEREG WLYYIRYPVV NSEEFITVAT TRPETLLGDT AIAVSPEDER
YSHLIGAKVI VPFVDREIPI IGDFSVDASF GTGAVKITPA HDKDDYRTGM NHRLPMINIL
TPTGEINENG GIFTGLAKES ARENIITSLE ALGLFVRKEA YSSRVGVSYR SGAIIEPYLS
KQWFVSVDSF RESLREFVNS KEINLFPPEF IRNYLTWVNN LKDWCISRQL WWGHRIPVWH
NKHDEEYVIC FDGDGVPEEV AQDPESWYQD PDVLDTWFSS GLWPLTCFGW PEESADLRKF
YPTSVLVTGH DILFFWVTRM VLMCSAMVDT KPFADVFLHG LIFGKSYKQY DDNGEWTYVS
GDQKREYDKG KALPKNVVAK WEKLSKSKGN VIDPIEMIDM YGADAVRFTL CSCANRGEQI
DLDYRLFEEY KNFVNKLWNG ARFIFGHISE LTSRDLEEGV NKDLLGLEDF YILDRFNELL
ALIDSHYNCY SFDKIAALAY DFFKNDLCST YLEIIKPTLF GKQGNDEQRA TKRKLLATLL
VNILGVLHPI VPYITETLFQ KIKTTLGVVG DGLGDAVTGH AVSMLRSEAC MIAGYPQPIE
LSFPQGLRES FAIAEKLVYT IRNIRGEMQL DPRDLLQAFI ISSEKKELLD ACIPIMCALG
GIKTIEQLSE APKDCIFSLG VVEGIQVGVI LPAEHLAKEH ARLEKEKIRL ENSIESLSKL
LASEDFRTRA NPNLVQAKED ALRNSRQELQ SILDKIASL
