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SYV_PSE14
ID   SYV_PSE14               Reviewed;         948 AA.
AC   Q48MF2;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 96.
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=PSPPH_1153;
OS   Pseudomonas savastanoi pv. phaseolicola (strain 1448A / Race 6)
OS   (Pseudomonas syringae pv. phaseolicola (strain 1448A / Race 6)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=264730;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1448A / Race 6;
RX   PubMed=16159782; DOI=10.1128/jb.187.18.6488-6498.2005;
RA   Joardar V., Lindeberg M., Jackson R.W., Selengut J., Dodson R.,
RA   Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S., Gwinn Giglio M.,
RA   Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A., Crabtree J.,
RA   Creasy T., Davidsen T.M., Haft D.H., Zafar N., Zhou L., Halpin R.,
RA   Holley T., Khouri H.M., Feldblyum T.V., White O., Fraser C.M.,
RA   Chatterjee A.K., Cartinhour S., Schneider D., Mansfield J.W., Collmer A.,
RA   Buell R.;
RT   "Whole-genome sequence analysis of Pseudomonas syringae pv. phaseolicola
RT   1448A reveals divergence among pathovars in genes involved in virulence and
RT   transposition.";
RL   J. Bacteriol. 187:6488-6498(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; CP000058; AAZ33987.1; -; Genomic_DNA.
DR   RefSeq; WP_011167924.1; NC_005773.3.
DR   AlphaFoldDB; Q48MF2; -.
DR   SMR; Q48MF2; -.
DR   STRING; 264730.PSPPH_1153; -.
DR   EnsemblBacteria; AAZ33987; AAZ33987; PSPPH_1153.
DR   KEGG; psp:PSPPH_1153; -.
DR   eggNOG; COG0525; Bacteria.
DR   HOGENOM; CLU_001493_0_2_6; -.
DR   OMA; FATKLWN; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000000551; 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.
FT   CHAIN           1..948
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_0000224538"
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;  107027 MW;  DB00BD7BA6624B31 CRC64;
     MDKTYQPHAI ETSWYQTWES ENYFAPQGVG DSYTIMIPPP NVTGSLHMGH GFNNAIMDAL
     IRFRRMQGRN TLWQPGTDHA GIATQMLVER RLEAQGISRH ELGREKFLDK IWEWKAESGG
     NISRQIRRLG SSVDWSRERF TMDDGLSDAV KEAFVRLHED GLIYRGKRLV NWDTKLHTAI
     SDLEVENHDE KGHLWNLRYP LADGAKTAEG LDYLIVATTR PETMLGDAAV AVNPQDERYK
     ALIGKFVELP LVGRRIPIIA DDYCDPEFGT GCVKITPAHD FNDYEVGKRH NLPLLNIFDK
     NANVLAAAQV FNLDGTLNES VDGSLPAAYA GLDRFEARKQ IVAAFDAAGL LVSVDDHALK
     VPKGDRSGTI IEPWLTDQWY VSTKPLAEPA IAAVEDGRIA FVPKQYENMY FSWMRDIQDW
     CISRQLWWGH RIPAWYDESG KVYVGRDEAE VRAKNNLGPE IALQQDNDVL DTWFSSGLWT
     FSTLGWPEKT KALETFHSTD VLVTGFDIIF FWVARMIMLT MHLVKNEDGT PQVPFKTVYV
     HGLVRDGQGQ KMSKSKGNVL DPLDIVDGID LETLVEKRTS GLMQPQLAKK IEKQTRQEFA
     DGIASYGTDA LRFTFCSLAS TGRDIKFDMG RVEGYRNFCN KIWNAARYVL DKGEDCGQNG
     EAVELSLADR WIISQLQRTE AEVTRQLDQF RFDLAAQALY EFIWNQYCDW YLELSKPVLW
     DETAPVERQR GTRRTLVRVL EVALRLAHPF MPFITEEIWQ RLAPLAGAQG KTIMLQPWPV
     ANEARIDQAA EDDIEWLKGL MLAVRNIRGE MNIGPGKPLQ LFLKNVSAED QRRLSENDYL
     LKKLAKLESM TVLTEGAEAP LSATALVGDM EVLVPMAGLI DKGAELARLD KEIQRLQGEV
     QRVGGKLSNA AFVDKAPPEV IAKERAKLTE AEQALGKLAE QHARIASL
 
 
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