SYV_RICFE
ID SYV_RICFE Reviewed; 859 AA.
AC Q4UMX8;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Valine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02005};
DE EC=6.1.1.9 {ECO:0000255|HAMAP-Rule:MF_02005};
DE AltName: Full=Valyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02005};
DE Short=ValRS {ECO:0000255|HAMAP-Rule:MF_02005};
GN Name=valS {ECO:0000255|HAMAP-Rule:MF_02005}; OrderedLocusNames=RF_0229;
OS Rickettsia felis (strain ATCC VR-1525 / URRWXCal2) (Rickettsia azadi).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=315456;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-1525 / URRWXCal2;
RX PubMed=15984913; DOI=10.1371/journal.pbio.0030248;
RA Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E.,
RA Parinello H., Claverie J.-M., Raoult D.;
RT "The genome sequence of Rickettsia felis identifies the first putative
RT conjugative plasmid in an obligate intracellular parasite.";
RL PLoS Biol. 3:1-12(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_02005}.
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_02005};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_02005}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02005}.
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_02005}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC ValS type 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_02005}.
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DR EMBL; CP000053; AAY61080.1; -; Genomic_DNA.
DR RefSeq; WP_011270581.1; NC_007109.1.
DR AlphaFoldDB; Q4UMX8; -.
DR SMR; Q4UMX8; -.
DR STRING; 315456.RF_0229; -.
DR PRIDE; Q4UMX8; -.
DR EnsemblBacteria; AAY61080; AAY61080; RF_0229.
DR KEGG; rfe:RF_0229; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_5; -.
DR OMA; RQWYIRN; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000008548; 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; 3.40.50.620; -; 2.
DR HAMAP; MF_02005; Val_tRNA_synth_type2; 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; IPR005728; Rickett_RPE.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR InterPro; IPR022874; Valine-tRNA_ligase_type_2.
DR InterPro; IPR002303; Valyl-tRNA_ligase.
DR PANTHER; PTHR11946; PTHR11946; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 1.
DR PRINTS; PR00986; TRNASYNTHVAL.
DR SUPFAM; SSF47323; SSF47323; 1.
DR SUPFAM; SSF50677; SSF50677; 1.
DR TIGRFAMs; TIGR01045; RPE1; 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; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..859
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224614"
FT MOTIF 46..56
FT /note="'HIGH' region"
FT MOTIF 583..587
FT /note="'KMSKS' region"
FT BINDING 586
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02005"
SQ SEQUENCE 859 AA; 99399 MW; C0D8F6ABC525946F CRC64;
MKEFPKNYNF TENEKKWQQI WQEKQIYAYD PNISKDEIYV VDTPPPTVSG QLHIGHVYSY
TQTDFIVRFQ RMMGKNIFYP MGFDDNGLPT ERLVEKQKQI KAYNMSRSEF IKICEEVVAS
EEEKFRSLFN QIALSVDWSL EYQTISPLSR KISQMSFLDL VKKGEVYRND QPILWDPVDG
TALAQADIDD KEKTSFMNYI TFEIEEDDRP FSKFAYREEF VGNTEHSTAA YIKVREDAST
GLTHKLPLEV EFGKRSITIA TTRPELLPAC VAVFYHPDDK RYKHLAGKSA ITPLFNGKVP
LLADPLVQQD KGTGLVMCCT FGDQTDITWW KTHNLPLKTI VTKKGTIDFP HDIAIDGLKI
KEARTKIIDI LKEQNLLTKQ EEITHTVKCA ERSGAPLEIL TVPQWFVKTI SHKEALLKRA
SELNWHPKNM KIRLESWINS ISWDWCISRQ RYFGVPFPVW YSKRVGEEGK ILYADISQLP
VDPLKDLPIG YSKEEVEPDL DVMDTWATSS VSPQLSTHGI SDDFTVNKER HDKLFPMELR
PQAHEIIRTW AFYTILKAHL HQNTLPWKNI MVSGWCLAED RSKMSKSKGN VLVPEKLLEQ
YGSDVIRYWS ANSKLGADTA YSEDVMKNGK RLVNKLWNAA KFVSIHFEKL KDKDKQAKLL
DVKEKITNEF DQWMINKLVE LVKLATNELQ NYEYANAMHL TEKFFWAIFC DNYLEISKNR
AYDEENKNPS GQYSSILTLY HTMQILLKLF APFMPHITEE LYQILYSDKS VHEKGNWVNY
GDLNYKIDAK GAEGLLEILD IVRKFKAEKN LSIKAPIKLL EVSGIELSAE LTEDLKNVTS
AEEIQFEDQG DKIKVNVIL
