SYV_CHLTA
ID SYV_CHLTA Reviewed; 939 AA.
AC Q3KM60;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 108.
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=CTA_0324;
OS Chlamydia trachomatis serovar A (strain ATCC VR-571B / DSM 19440 / HAR-13).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=315277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-571B / DSM 19440 / HAR-13;
RX PubMed=16177312; DOI=10.1128/iai.73.10.6407-6418.2005;
RA Carlson J.H., Porcella S.F., McClarty G., Caldwell H.D.;
RT "Comparative genomic analysis of Chlamydia trachomatis oculotropic and
RT genitotropic strains.";
RL Infect. Immun. 73:6407-6418(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_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; CP000051; AAX50562.1; -; Genomic_DNA.
DR RefSeq; WP_011324675.1; NC_007429.1.
DR AlphaFoldDB; Q3KM60; -.
DR SMR; Q3KM60; -.
DR EnsemblBacteria; AAX50562; AAX50562; CTA_0324.
DR KEGG; cta:CTA_0324; -.
DR HOGENOM; CLU_001493_0_2_0; -.
DR OMA; FATKLWN; -.
DR Proteomes; UP000002532; 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_1000216263"
FT COILED 874..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; 107018 MW; D8C030F21BFC3B99 CRC64;
MNEDQFPKAY DPKSSETGVY SFWERSGIFV ANASSEKPAY SIVMPPPNVT GILHMGHALV
NTLQDTLIRY KRMQGFEVCW VPGTDHAGIA TQTVVERHLK ASLGKQRTDF SREEFLKHVW
DWKEKSQNVI LSQLRQLGCS CDWSRQRFTM DPGANRAVKK AFKILFDKGV IYRGYYLVNW
DPILQTALAD DEVEYEERDG WLYYIRYQVV NSEEFITVAT TRPETLLGDT AIAVSPEDLR
YSHLIGAKVV VPFVNREIPI IGDFSVDASF GTGAVKITPA HDKDDYKTGM NHQLPMINIL
TPTGEINENG GIFTGLSREV ARENIITSLE ALGLFVKKEA YSSRVGVSYR SGAIIEPYLS
KQWFVSVDSF RDSLRGFVNS EEIRIFPPEF VRNYLTWVNN LKDWCISRQL WWGHRIPVWH
NKHDENVICF DGEGGPEEVM RDPESWYQDP DVLDTWFSSG LWPLTCFGWP DENSLDLKKF
YPTAVLVTGH DILFFWVTRM VLMCSAMVDT EPFSDVFLHG LIFGKSYREY DEKGEWFYVS
GERKRDYDKG KALPKNVVAK WEKLSKSKGN VIDPIEMIEA YGADAVRLTL CSCANRGEQI
DLDYHLFEEY KNFINKLWNG ARFIFGHISE LTSRDLEEGV NQDLLGLEDF YILDRFNELL
DLIDGHYNCY SFDKIASLAY DFFKNDLCST YLEIIKPTLF GKQDSDQQRA TKRKLLATLL
INILGVLHPI VPYITETLFQ KLKATLGTVE NGKGDSVTGH AVSMLRSEAC MVAEYPKPIH
VAFPQGLRES FGIAERLVYT IRNIRGEMQL DPREPLQAFV ISSEKKELVD VCIPIMCALG
GVKTVEQLAE APKDSIFSLG VVEGIQVGVI LPPEHLAKER VRLEKEKTRL EKSIDSVSKL
LASEDFRTRA NPSLVQAKKD SLRNSQRELQ SILDKLASL
