SYV_BURMA
ID SYV_BURMA Reviewed; 955 AA.
AC Q62KW5;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=BMA0927;
OS Burkholderia mallei (strain ATCC 23344).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=243160;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23344;
RX PubMed=15377793; DOI=10.1073/pnas.0403306101;
RA Nierman W.C., DeShazer D., Kim H.S., Tettelin H., Nelson K.E.,
RA Feldblyum T.V., Ulrich R.L., Ronning C.M., Brinkac L.M., Daugherty S.C.,
RA Davidsen T.D., DeBoy R.T., Dimitrov G., Dodson R.J., Durkin A.S.,
RA Gwinn M.L., Haft D.H., Khouri H.M., Kolonay J.F., Madupu R., Mohammoud Y.,
RA Nelson W.C., Radune D., Romero C.M., Sarria S., Selengut J., Shamblin C.,
RA Sullivan S.A., White O., Yu Y., Zafar N., Zhou L., Fraser C.M.;
RT "Structural flexibility in the Burkholderia mallei genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14246-14251(2004).
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; CP000010; AAU49461.1; -; Genomic_DNA.
DR RefSeq; WP_004191922.1; NC_006348.1.
DR RefSeq; YP_102654.1; NC_006348.1.
DR AlphaFoldDB; Q62KW5; -.
DR SMR; Q62KW5; -.
DR STRING; 243160.BMA0927; -.
DR PRIDE; Q62KW5; -.
DR EnsemblBacteria; AAU49461; AAU49461; BMA0927.
DR GeneID; 56595417; -.
DR KEGG; bma:BMA0927; -.
DR PATRIC; fig|243160.12.peg.960; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_4; -.
DR OMA; FATKLWN; -.
DR Proteomes; UP000006693; Chromosome 1.
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; 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..955
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224452"
FT COILED 887..953
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 47..57
FT /note="'HIGH' region"
FT MOTIF 542..546
FT /note="'KMSKS' region"
FT BINDING 545
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 955 AA; 106744 MW; C2CB6E83B59C937D CRC64;
MSDTTLAKSF EPQTIESQWG PEWEKRGYAT PALDPSRPDF SIQLPPPNVT GTLHMGHAFN
QTIMDGLVRY HRMLGHNTLW VPGTDHAGIA TQIVVERQLD AQGVSRHDLG REKFVERVWE
WKERSGSTIT GQVRRIGASP DWSREYFTMN DKMSEAVREV FVRLYEQGLI YRGKRLVNWD
PVLLTAVSDL EVVSEEENGH LWHIRYPLAD GSGHLSVATT RPETMLGDVA VMVHPEDERY
RHLVGRHVKL PLCEREIPII ADDYVDREFG TGVVKVTPAH DFNDYQVGLR HALAPIEILT
LDAKINDNAP AAYRGLDRFD ARKAIVDELD AQGLLESVKP HKLMVPRGDR TGVVIEPMLT
DQWFVAMTKP APQGTFHPGK SITEVSLEVV RRGEIKFVPE NWTTTYYQWL ENIQDWCISR
QLWWGHQIPA WYGENGEIFV ARNEEDARAQ AAAKGYTGAL KRDDDVLDTW FSSALVPFSS
LGWPNETPEM KHFLPSSVLV TGFDIIFFWV ARMVMMTTHF TGKVPFGTVY VHGLVRDAEG
QKMSKSKGNT LDPIDIVDGI GLDALVAKRT TGLMNPRQAA TIEKKTRKEF PDGIPAFGTD
ALRFTMASMA TLGRNVNFDL ARCEGYRNFC NKLWNATRFV LMNCEGHDCG FDKPEVCGAG
DCGPGGYLDF SPADRWIVSL MQRVEADIAK GFADYRFDNI ANAIYKFVWD EYCDWYLELA
KVQIQNGTSE QQRATRRTLL RVLETVLRLA HPIIPFITEA LWQKVAPLAG RYPAGKAEGE
ASLMVQAYPV AEPKKLDEAC EQWAAELKAV VDACRNLRGE MNLSPATKVP LLAAGDAAQL
QAFAPYVQAL ARLSEVRVLP DEAALDADAH GAPIAIVGGN KLVLKVEIDV AAERERLSKE
IARLEGEIVK CNAKLGNEAF VAKAPPAVVA QEQKRLAEFQ STLTKLGAQL ARLPA
