SYV_STRM5
ID SYV_STRM5 Reviewed; 942 AA.
AC B4SJ70;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=Smal_0533;
OS Stenotrophomonas maltophilia (strain R551-3).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX NCBI_TaxID=391008;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R551-3;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Taghavi S.,
RA Monchy S., Newman L., Vangronsveld J., van der Lelie D., Richardson P.;
RT "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001111; ACF50238.1; -; Genomic_DNA.
DR RefSeq; WP_012510004.1; NC_011071.1.
DR AlphaFoldDB; B4SJ70; -.
DR SMR; B4SJ70; -.
DR STRING; 391008.Smal_0533; -.
DR EnsemblBacteria; ACF50238; ACF50238; Smal_0533.
DR KEGG; smt:Smal_0533; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_6; -.
DR OMA; FATKLWN; -.
DR OrthoDB; 32262at2; -.
DR BioCyc; SMAL391008:SMAL_RS02725-MON; -.
DR Proteomes; UP000001867; 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..942
FT /note="Valine--tRNA ligase"
FT /id="PRO_1000189245"
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; 106318 MW; 407E0685912208AD CRC64;
MTQLASSYDP KSFETDLYEA WEKAGHFKPS GTGEPYTILL PPPNVTGTLH MGHAFQQTLM
DALVRYHRMR GYDTLWQVGT DHAGIATEMV VSRNLALEGK GETRDSLGRE GFIGKVWEWK
QQSGDIIERQ MRRLGTSADW SRSTFTMDPQ PSAAVNEAFV RWYEQGLIYR GQRLVNWDPV
LKTAISDLEV ESAEEDGFLW SIAYTLDDGL SYEHVERDAD GVETLRETRD YLVVATTRPE
TLLGDTAVMV HPEDARYAHL IGKSVVLPLT GRRVPVIADD YVDRAFGTGV VKVTPAHDFN
DYEVGVRHSL PMINLFTPVA ALNENAPERF QGLDRYAARK AVLAELEDLG ILVETKAHKL
QVPRGDRTGQ VIEPYLTDQW FVKMDDLAKR GLELVEDGSI SFVPPNWINT YRHWMNNIQD
WCISRQLWWG HRIPAWFDEA TGSCYVGRSE EEVRAKHSLG SDVVLNQESD VLETWFSSQL
WPFSTLGWPN EQAMAERGFD RYLPSSVLIT GFDIIFFWVA RMIMATDNLV GKIPFKDVYF
TGLIRDGQGQ KMSKSKGNVL DPLDIIDGIS IDDLVAKRTG GLMQPKMVEK IEKATRKEFP
DGIAAHGADA LRFTIAALAT HGRDIKFDMN RAEGYKNFCN KLWNASRFTL MNTEGAAFTG
MPTPRTDAER WILSRLAAVS SEAQGHYANY RFDLLAQCLY EFAWNEFCDW FLELSKPALN
GADAADAEST RHTLLYVLEA LLRLLHPLTP FITEQLWQQL APRLGLAETT LSLRPYPTAA
EFEGDFAQAE ADVEWLKAVI SAVRRVRSEL NVAPSKQVPL RLQAGLEQDR VRIERFSASL
SFLLKLDSIQ WLAEGESAPP AAAAIVGELK LLVPLEGLVD LDAERVRLDK EIARVEVEKE
KSETKLAKFT DKVPPAVVEQ ERVRLVDWNT QLAGLREQRA KL
