ID   SYV_STRMK               Reviewed;         942 AA.
AC   B2FMS2;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 87.
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=Smlt0673;
OS   Stenotrophomonas maltophilia (strain K279a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=522373;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K279a;
RX   PubMed=18419807; DOI=10.1186/gb-2008-9-4-r74;
RA   Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A.,
RA   Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N., Adlem E.,
RA   Kerhornou A., Lord A., Murphy L., Seeger K., Squares R., Rutter S.,
RA   Quail M.A., Rajandream M.A., Harris D., Churcher C., Bentley S.D.,
RA   Parkhill J., Thomson N.R., Avison M.B.;
RT   "The complete genome, comparative and functional analysis of
RT   Stenotrophomonas maltophilia reveals an organism heavily shielded by drug
RT   resistance determinants.";
RL   Genome Biol. 9:R74.1-R74.13(2008).
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; AM743169; CAQ44255.1; -; Genomic_DNA.
DR   RefSeq; WP_012479102.1; NC_010943.1.
DR   AlphaFoldDB; B2FMS2; -.
DR   SMR; B2FMS2; -.
DR   STRING; 522373.Smlt0673; -.
DR   EnsemblBacteria; CAQ44255; CAQ44255; Smlt0673.
DR   KEGG; sml:Smlt0673; -.
DR   PATRIC; fig|522373.3.peg.643; -.
DR   eggNOG; COG0525; Bacteria.
DR   HOGENOM; CLU_001493_0_2_6; -.
DR   OMA; FATKLWN; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000008840; 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; -; 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; Reference proteome.
FT   CHAIN           1..942
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_1000189246"
FT   COILED          876..942
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT   MOTIF           43..53
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   942 AA;  106207 MW;  DB401EFE09A7A830 CRC64;
     MTQLASSYDP KSFETDLYEA WEKAGHFKPS GTGEPYTILL PPPNVTGTLH MGHAFQQTLM
     DALVRYHRMR GYDTLWQVGT DHAGIATEMV VSRNLALEGK GETRDSLGRE GFIGKVWEWK
     QQSGDTIERQ MRRLGTSADW SRSTFTMDPQ PSAAVNEAFV RWYEQGLIYR GQRLVNWDPV
     LKTAISDLEV ESAEEDGFLW SIAYTLDEGL SYEHVERDAD GVETLRETRD YLVVATTRPE
     TLLGDTAVMV HPEDKRYAHL IGKSVVLPLT GRRVPVIADD YVDRAFGTGV VKVTPAHDFN
     DYEVGVRHSL PMINLFTPVA ALNENAPERF QGLDRYAARK AVLAELEDLG ILVETKAHKL
     QVPRGDRTGQ VIEPYLTDQW FVKMDDLAKR GLELVEDGSI SFVPPNWINT YRHWMNNIQD
     WCISRQLWWG HRIPAWFDEA TGSCYVGRSE EEVRAKHNLG SDVVLNQESD VLETWFSSQL
     WPFSTLGWPN EQAMAERGFD RYLPSSVLIT GFDIIFFWVA RMIMATDNLV GKIPFKDVYF
     TGLIRDGQGQ KMSKSKGNVL DPLDIIDGIT IDDLVAKRTG GLMQPKMVEK IEKATRKEFP
     DGIAAHGADA LRFTIAALAT HGRDIKFDMN RAEGYKNFCN KLWNASRFAL MNTEGAAFTG
     VPRPRTDAER WILARLAATT AEAQGHFAAY RFDLLAQCLY EFAWNAFCDW FLELSKPALN
     GADAADAEST RHTLLYVLEA LLRLLHPLTP FITEQLWQQL APRLGLAETT LSLRPYPTAA
     EFEGDFAQAE ADVEWLKAVI SAVRRVRSEL NVAPSKLVPL RLQAGLEQDR VRIERFSASL
     SFLLKLDSIQ WLAEGESAPP AAAAIVGELK LLVPLEGLVD LDAERVRLDK EIARVEAEKE
     KSETKLAKFT DKVPPAVVEQ ERVRLADWNT QLAGLREQRA KL