SYV_CHLT2
ID SYV_CHLT2 Reviewed; 939 AA.
AC B0B7L8;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 84.
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=CTL0554;
OS Chlamydia trachomatis serovar L2 (strain 434/Bu / ATCC VR-902B).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=471472;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=434/Bu / ATCC VR-902B;
RX PubMed=18032721; DOI=10.1101/gr.7020108;
RA Thomson N.R., Holden M.T.G., Carder C., Lennard N., Lockey S.J., Marsh P.,
RA Skipp P., O'Connor C.D., Goodhead I., Norbertzcak H., Harris B., Ormond D.,
RA Rance R., Quail M.A., Parkhill J., Stephens R.S., Clarke I.N.;
RT "Chlamydia trachomatis: genome sequence analysis of lymphogranuloma
RT venereum isolates.";
RL Genome Res. 18:161-171(2008).
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; AM884176; CAP03994.1; -; Genomic_DNA.
DR RefSeq; WP_009873710.1; NC_010287.1.
DR RefSeq; YP_001654630.1; NC_010287.1.
DR AlphaFoldDB; B0B7L8; -.
DR SMR; B0B7L8; -.
DR EnsemblBacteria; CAP03994; CAP03994; CTL0554.
DR KEGG; ctb:CTL0554; -.
DR PATRIC; fig|471472.4.peg.595; -.
DR HOGENOM; CLU_001493_0_2_0; -.
DR OMA; FATKLWN; -.
DR Proteomes; UP000000795; 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_1000216262"
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; 107103 MW; 9AFD87208168625B CRC64;
MNEDQFPKAY DPKSSETGVY SFWERSGMFV ANASSEKPAY SIVMPPPNVT GILHMGHALV
NTLQDTLIRY KRMQGFEVCW VPGTDHAGIA TQTVVERHLK ASLGKRRTDF SREEFLKHVW
DWKEKSQNVI LSQLRQLGCS CDWSRQRFTM DPGANRAVKK AFKILFDKGV IYRGYYLVNW
DPILQTALAD DEVEYEERDG WLYYIRYQVV NSEEFITVAT TRPETLLGDT AIAVSPEDQR
YSHLIGAKVV VPFVNREIPI IGDFSVDASF GTGAVKITPA HDKDDYKTGM NHQLPMINIL
TSTGEINENG GIFTGLSREV ARENIITSLE ALGLFVKKEA YSSRVGVSYR SGAIIEPYLS
KQWFVSVDSF RDSLREFVNS EEIRIFPPEF VRNYLTWVNN LKDWCISRQL WWGHRIPVWH
NKHDENVICF DGEGGPEEVM RDPESWYQDP DVLDTWFSSG LWPLTCFGWP DEDSLDLKKF
YPTAVLVTGH DILFFWVTRM VLMCSAMVDT EPFSDVFLHG LIFGKSYREY DEKGEWFYVS
GERKRDYDKG KALPKNVVAK WEKLSKSKGN VIDPIEMIEA YGADAVRLTL CSCANRGEQI
DLDYRLFEEY KNFINKLWNG ARFIFGHISE LTSRDLEEGV NQDLLGLEDF YILDRFNELL
DLIDGHYNCY SFDKIASLAY DFFKNDLCST YLEIIKPTLF GKQGSDQQRA TKRKLLATLL
INILGVLHPI VPYITETLFQ KLKATLGTVE NGKGDSVTGH AVSMLRSEAC MVAEYPKPIH
VAFPQGLRES FGIAERLVYT IRNIRGEMQL DPREPLQAFV ISSEKKELVD VCIPIMCALG
GVKTVEQLAE APKDSIFSLG VVEGIQVGVI LPPEHLAKER VRLEKEKTRL EKSIDSVSKL
LASEDFRTRA NPSLVQAKKD SLRNSQRELQ SILDKLASL
