SYV_CHLTR
ID SYV_CHLTR Reviewed; 939 AA.
AC O84304;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 123.
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=CT_302;
OS Chlamydia trachomatis (strain D/UW-3/Cx).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=272561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D/UW-3/Cx;
RX PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT trachomatis.";
RL Science 282:754-759(1998).
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; AE001273; AAC67895.1; -; Genomic_DNA.
DR PIR; H71532; H71532.
DR RefSeq; NP_219807.1; NC_000117.1.
DR RefSeq; WP_009872283.1; NC_000117.1.
DR AlphaFoldDB; O84304; -.
DR SMR; O84304; -.
DR STRING; 813.O172_01620; -.
DR PRIDE; O84304; -.
DR EnsemblBacteria; AAC67895; AAC67895; CT_302.
DR GeneID; 884822; -.
DR KEGG; ctr:CT_302; -.
DR PATRIC; fig|272561.5.peg.323; -.
DR HOGENOM; CLU_001493_0_2_0; -.
DR InParanoid; O84304; -.
DR OMA; FATKLWN; -.
DR Proteomes; UP000000431; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006438; P:valyl-tRNA aminoacylation; IBA:GO_Central.
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..939
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000106222"
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; 107036 MW; CEB8449DC7BB9066 CRC64;
MNEDQFPKAY DPKSSETGVY SFWERSGMFV 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
