ID   SYV_BURPS               Reviewed;         955 AA.
AC   Q63TI8;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 101.
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=BPSL1980;
OS   Burkholderia pseudomallei (strain K96243).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=272560;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K96243;
RX   PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA   Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M.,
RA   Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D.,
RA   Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A.,
RA   Brown N.F., Challis G.L., Cherevach I., Chillingworth T., Cronin A.,
RA   Crossett B., Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z.,
RA   Hauser H., Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S.,
RA   Price C., Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M.,
RA   Simmonds M., Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M.,
RA   Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT   "Genomic plasticity of the causative agent of melioidosis, Burkholderia
RT   pseudomallei.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(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; BX571965; CAH35979.1; -; Genomic_DNA.
DR   RefSeq; WP_004521705.1; NZ_CP009538.1.
DR   RefSeq; YP_108578.1; NC_006350.1.
DR   AlphaFoldDB; Q63TI8; -.
DR   SMR; Q63TI8; -.
DR   STRING; 272560.BPSL1980; -.
DR   EnsemblBacteria; CAH35979; CAH35979; BPSL1980.
DR   GeneID; 56526346; -.
DR   KEGG; bps:BPSL1980; -.
DR   PATRIC; fig|272560.51.peg.4132; -.
DR   eggNOG; COG0525; Bacteria.
DR   OMA; FATKLWN; -.
DR   Proteomes; UP000000605; 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; Reference proteome.
FT   CHAIN           1..955
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_0000224453"
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;  106726 MW;  FA96C0FA6861576C 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 TGLMNPKQAA TIEKKTRKEF PDGIPAFGTD
     ALRFTMASMA TLGRNVNFDL ARCEGYRNFC NKLWNATRFV LMNCEGHDCG FDKPEVCGAG
     DCGPGGYLDF SPADRWIVSL MQRVEADIAK GFADYRFDNI ANAIYKFVWD EYCDWYLELA
     KVQIQNGTPE QQRATRRTLL RVLETVLRLA HPIIPFITEA LWQKVAPLAG RYPAGKAEGE
     ASLMVQAYPV AEPKKLDEAC EQWAAELKAV VDACRNLRGE MNLSPATKVP LLAAGDAAQL
     QAFAPYVQAL ARLSEVRVLP DEAALDADAH GAPIAIVGGN KLVLKVEIDV AAERERLSKE
     IARLEGEIVK CNAKLGNEAF VAKAPPAVVA QEQKRLAEFQ STLTKLGAQL ARLPA