SYV_CHLFF
ID SYV_CHLFF Reviewed; 940 AA.
AC Q255D3;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 102.
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=CF0333;
OS Chlamydia felis (strain Fe/C-56) (Chlamydophila felis).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=264202;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fe/C-56;
RX PubMed=16766509; DOI=10.1093/dnares/dsi027;
RA Azuma Y., Hirakawa H., Yamashita A., Cai Y., Rahman M.A., Suzuki H.,
RA Mitaku S., Toh H., Goto S., Murakami T., Sugi K., Hayashi H., Fukushi H.,
RA Hattori M., Kuhara S., Shirai M.;
RT "Genome sequence of the cat pathogen, Chlamydophila felis.";
RL DNA Res. 13:15-23(2006).
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; AP006861; BAE81105.1; -; Genomic_DNA.
DR RefSeq; WP_011457885.1; NC_007899.1.
DR AlphaFoldDB; Q255D3; -.
DR SMR; Q255D3; -.
DR STRING; 264202.CF0333; -.
DR KEGG; cfe:CF0333; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_0; -.
DR OMA; FATKLWN; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000001260; 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; 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 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..940
FT /note="Valine--tRNA ligase"
FT /id="PRO_1000216261"
FT COILED 872..938
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 47..57
FT /note="'HIGH' region"
FT MOTIF 564..568
FT /note="'KMSKS' region"
FT BINDING 567
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 940 AA; 107117 MW; 7161423A2B4DCEB8 CRC64;
MEEDVFPKAY DPKGLEDKLY AFWEDAGMFT AQSASNKPPY AIIMPPPNVT GILHMGHALV
NTLQDVLIRY KRMSGFEVCW VPGTDHAGIA TQTVVERHLY SSLGKRRIDF SREEFLEYVW
EWKEKSEGII LSQLRQLGCS CDWSRLRFTM EPLASRAVKK AFKVLFDRGH IYRGYYLVNW
DPVLQTALAD DEVEYEEKDG WLYYIRYRVV DSSDEIIVAT TRPETLLGDT AIAISPDDER
YSHLLGAKVH LPFVDREIPI IGDMSVDPLF GTGAVKITPA HDRDDYRTGI NHNLPLVNIL
TPTGKINENG GIFAGLSKEK ARDDIITALD AMGLFVKKEP YTLRVGVSYR SGAVIEPYLS
KQWFVSVDSF RDSLREFVAS DSIKIFPPEF TRNYLSWVNN LRDWCISRQL WWGHRIPVWY
HKSDEDRIIC YDGEGLPEEV AQDPDSWDQD PDVLDTWFSS GLWPLTCLGW PDVEAKDLKK
FYPTSVLITG HDILFFWVTR MVLLCSAMVG EKPFSDVFLH GLIFGKSYKR YNNLGEWTYI
SGEEKHAYDM GKPLPKDVTA KWEKLSKSKG NVIDPLEMID KYGADAVRMA LCSCANRGEQ
IDLDYRLFEE YKNFANKIWN GARFIFGHIS NLTGKDLADG INQNLLGLED YYILDGFNRL
LKELESAYQS YAFDRVTTMA YEFFRNDFCS TYIEIIKPTL YGKQGNDEDR LTKQKLLAVL
LVNILGVLHP IAPFVTETLF LKLKEAIGVI VDASSDEITA HALNMLRADS YVLAPYPQAM
RITIPDNLHA SFALAERLVY TIRNIRGEMQ LDPRASLEAF VICPEGVSVD TYVPMMCALG
GLSSVEHLTE EPKDRVYSLG VVEGIRLGVF VPIEQITKEK NRLEKEKIRL EKAIESVSRL
LGSENFRAKA NPDLVSAKEE ALKNNRMELQ SILDKLASFS
