ID   SYV_PSESM               Reviewed;         948 AA.
AC   Q887M3;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 107.
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=PSPTO_1268;
OS   Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=223283;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-871 / DC3000;
RX   PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA   Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA   Gwinn M.L., Dodson R.J., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA   Daugherty S.C., Brinkac L.M., Beanan M.J., Haft D.H., Nelson W.C.,
RA   Davidsen T.M., Zafar N., Zhou L., Liu J., Yuan Q., Khouri H.M.,
RA   Fedorova N.B., Tran B., Russell D., Berry K.J., Utterback T.R.,
RA   Van Aken S.E., Feldblyum T.V., D'Ascenzo M., Deng W.-L., Ramos A.R.,
RA   Alfano J.R., Cartinhour S., Chatterjee A.K., Delaney T.P., Lazarowitz S.G.,
RA   Martin G.B., Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M.,
RA   Collmer A.;
RT   "The complete genome sequence of the Arabidopsis and tomato pathogen
RT   Pseudomonas syringae pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(2003).
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; AE016853; AAO54793.1; -; Genomic_DNA.
DR   RefSeq; NP_791098.1; NC_004578.1.
DR   RefSeq; WP_011103493.1; NC_004578.1.
DR   AlphaFoldDB; Q887M3; -.
DR   SMR; Q887M3; -.
DR   STRING; 223283.PSPTO_1268; -.
DR   PRIDE; Q887M3; -.
DR   EnsemblBacteria; AAO54793; AAO54793; PSPTO_1268.
DR   GeneID; 1182904; -.
DR   KEGG; pst:PSPTO_1268; -.
DR   PATRIC; fig|223283.9.peg.1290; -.
DR   eggNOG; COG0525; Bacteria.
DR   HOGENOM; CLU_001493_0_2_6; -.
DR   OMA; FATKLWN; -.
DR   OrthoDB; 32262at2; -.
DR   PhylomeDB; Q887M3; -.
DR   Proteomes; UP000002515; 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; 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..948
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_0000224540"
FT   COILED          879..945
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT   MOTIF           40..50
FT                   /note="'HIGH' region"
FT   MOTIF           551..555
FT                   /note="'KMSKS' region"
FT   BINDING         554
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ   SEQUENCE   948 AA;  107067 MW;  333037CCC42249D6 CRC64;
     MDKTYQPHAI ETSWYQTWES ENYFAPQGAG DSYTIMIPPP NVTGSLHMGH GFNNAIMDAL
     IRFRRMQGRN TLWQPGTDHA GIATQMLVER RLEAQGVSRH ELGREKFLDK IWEWKAESGG
     NISRQIRRLG SSVDWSRERF TMDDGLSDAV KEAFVRLHED GLIYRGKRLV NWDTKLHTAI
     SDLEVENHDE KGHLWNLRYP LADGAKTAEG LDYLIVATTR PETMLGDAAV AVNPQDERYK
     ALIGKFVELP LVGRRIPIIA DDYCDPEFGT GCVKITPAHD FNDYEVGKRH NLPLLNIFDK
     NANVLPAAQV FNLDGKLNES VDGTLPAAYA GLDRFEARKQ IVAAFDAAGL LVSIDDHALK
     VPKGDRSGTI IEPWLTDQWY VSTKPLAEPA IAAVEDGRIA FVPKQYENMY FSWMRDIQDW
     CISRQLWWGH RIPAWYDESG KVYVGRDEAE VRAKNNLGPE IALQQDNDVL DTWFSSGLWT
     FSTLGWPEKT KALETFHSTD VLVTGFDIIF FWVARMIMLT LHLVKNEDGT PQVPFKTVYV
     HGLVRDGQGQ KMSKSKGNVL DPLDIVDGID LETLVEKRTS GLMQPQLAKK IEKQTRQEFA
     DGIASYGTDA LRFTFCSLAS TGRDIKFDMG RVEGYRNFCN KIWNAARYVL DKGEDCGQNG
     EAVELSLADR WIISQLQRTE AEVTRQLDQF RFDLAAQALY EFIWNQYCDW YLELSKPVLW
     DETASIERQR GTRRTLVRVL EVALRLAHPF MPFITEEIWQ RLAPLAGVEG KTIMLQPWPV
     ANEARIDQAA EDDIEWLKGL MLAVRNIRGE MNIGPGKPLQ LFLKNVSADD QRRLSENDYL
     LRKLAKLESM TVLTDGAEAP LSATALVGDM EVLVPMAGLI DKGAELARLD KEIQRLQGEV
     QRVGGKLSNA AFVDKAPPDV IAKERAKLTE AEQALGKLAE QHARIASL