SYV_XANOM
ID SYV_XANOM Reviewed; 980 AA.
AC Q2P7G5;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=XOO0757;
OS Xanthomonas oryzae pv. oryzae (strain MAFF 311018).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=342109;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAFF 311018;
RA Ochiai H., Inoue Y., Takeya M., Sasaki A., Kaku H.;
RT "Genome sequence of Xanthomonas oryzae pv. oryzae suggests contribution of
RT large numbers of effector genes and insertion sequences to its race
RT diversity.";
RL Jpn. Agric. Res. Q. 39:275-287(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; AP008229; BAE67512.1; -; Genomic_DNA.
DR RefSeq; WP_011407633.1; NC_007705.1.
DR AlphaFoldDB; Q2P7G5; -.
DR SMR; Q2P7G5; -.
DR KEGG; xom:XOO0757; -.
DR HOGENOM; CLU_001493_0_2_6; -.
DR OMA; FATKLWN; -.
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; -; 2.
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; 1.
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..980
FT /note="Valine--tRNA ligase"
FT /id="PRO_1000088568"
FT COILED 914..980
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 43..53
FT /note="'HIGH' region"
FT MOTIF 586..590
FT /note="'KMSKS' region"
FT BINDING 589
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 980 AA; 111006 MW; 4C6A411292E4F85D CRC64;
MTTLASSYDP SSFESRLYAQ WEAAGYFVPS DTGEPYTVLL PPPNVTGTLH MGHAFQQTLM
DALVRYHRMR GYDTLWQVGT DHAGIATEMV VSRNLALEGK GETRDSLGRE GFIAKVWEWN
AASGDTIERQ MRRLGTSSDW SRSTFTMDPQ PSAAVNEAFV RWYEQGLIYR GQRLVNWDPV
LKTAISDLEV ENVEEDGFLW SIRYPLADGV TYEHIEHDAD GNETLRETRD YLVVATTRPE
TMLGDTAVMV HPEDARYLTL HTARIVLPLT GRHVPVITDD YVDRAFGTGV VKVTPAHDFN
DYQVGERHNL PLVNLFTADA KIIDPRKQYP DDESPFVNAG IDWRELDQIQ RKRLGQHLAY
KIPAQYIGLD RYDARKLVLS ELEDLSILVE TKPHKLQVPR GDRTGQVIEP YLTDQWFVKM
DALAKRGLEL VESGQIQFVP PNWINTYRHW MENIQDWCIS RQLWWGHRIP AWFDDAGHCH
VGHDEAEVRA KHGLGAEIAL HQDSDVLETW FSSQLWPFST LGWPDSQAMA ERGFARYLPS
SVLVTGFDII FFWVARMIMA TDSFTGQVPF RDVYITGLIR DAQGQKMSKS KGNVLDPLDI
IDGISIEDLV AKRTNGLMQP RMAEKIEKAT RKEFPDGIIA HGADALRFTI AALATHGRDI
KFDLGRAEGY KNFCNKLWNA TRFVLMNTEG ARFTGVPQPR TEAEKWILAR LDKVTAETHA
HYANYRFDLL AQSLYEFAWN AFCDWFVELA KPALNNQDTD AAASTRHTLL YVLESLLRLL
HPLTPFVTEE LWQQVVPRLG ITTATISLQR FPQVGDVDTS GYATAEADVE WLKSMVSALR
RVRSELNVPP SKQVRLLLQA DTADERPRVA RFASQLSFLL KLERIDWLDA GQDTPPSAAA
IVGELTLLVP LEGLVDMDAE RMRLDKEIKR VKGEIGKCNG KLGNATFVQN APAVVVDQER
ARLADWTTQL AGLREQRGKL
