SYV_HAEDU
ID SYV_HAEDU Reviewed; 961 AA.
AC Q7VN93;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=HD_0669;
OS Haemophilus ducreyi (strain 35000HP / ATCC 700724).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=233412;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=35000HP / ATCC 700724;
RA Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L.,
RA Nguyen D., Wang J., Forst C., Hood L.;
RT "The complete genome sequence of Haemophilus ducreyi.";
RL Submitted (JUN-2003) 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; AE017143; AAP95593.1; -; Genomic_DNA.
DR RefSeq; WP_010944645.1; NC_002940.2.
DR AlphaFoldDB; Q7VN93; -.
DR SMR; Q7VN93; -.
DR STRING; 233412.HD_0669; -.
DR EnsemblBacteria; AAP95593; AAP95593; HD_0669.
DR KEGG; hdu:HD_0669; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_6; -.
DR OMA; FATKLWN; -.
DR Proteomes; UP000001022; 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..961
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224485"
FT COILED 892..961
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 48..58
FT /note="'HIGH' region"
FT MOTIF 560..564
FT /note="'KMSKS' region"
FT BINDING 563
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 961 AA; 108975 MW; EFDFADCA41C9238B CRC64;
MTQKFEMADR FDASAVEQAL YQHWEEQGYF KPSENPAVPS YCIAIPPPNV TGSLHMGHAF
QQTLMDTLIR FNRMEGNNTL WQAGTDHAGI ATQMVVERKI AAEEGKTRHD YGREAFINKI
WDWKAYSGGT ISQQMRRLGN SIDWQRERFT MDDGLSNAVK EVFVRLHEQG LIYRGKRLVN
WDPKLHTAIS DLEVENKESK GSLWHFRYPL SNGVKTADGK DYLIVATTRP ETVLGDTAVA
VHPEDERYQS LIGKTVLLPL ANREIPIIAD EYVDREFGTG VVKITPAHDF NDYEVGKRHA
LPMVNVMTMN ADIRQTAEVL GPDGKPLNTY QAIIPADYQG LERFTARKKV VADFEALALL
DEIKPHDLKV PYGDRGGVPI EPMLTDQWYV SVKPLAEVAT KAVENGEIQF VPKQYENLYF
SWMRDIQDWC ISRQLWWGHR IPAWYDESGN VYVARTEAEV RIKHNLPLDL PLTQDEDVLD
TWFSSGLWTF STLGWPEQTK ELKMFHTTDV LITGFDIIFF WVARMIMFTM HFIKDENGKP
QVPFKTVYVT GLIRDEQGQK MSKSKGNVLD PIDMIDGISL ADLLEKRTGN MMQPQLAEKI
AKATRKEFAA TPTLPAGGIA AHGTDALRFT LAALASNGRD INWDMKRLEG YRNFCNKLWN
ASRFVLTNDK LDLSAGEVEY SLADRWIESS FNRTVGEFRE ALTQYRFDLA ANAIYEFTWN
QFCDWYLELT KPVFANGSDA QKRATSKTLV SLLEKLLRLA HPIMPFITEE IWQKVKHFAG
VEGDSIMLQP FPIVEQAKLD ADAEQQINWL KELIIAVRNI RAEANIAPSK ALDLLVRNVT
QQQAVILSEN QLLLTAMAKL TSISVLTAGE QAPLSVAKLV GQVEVLVPMA GFINKDTELA
RLSKEIDKLH NEVMRIESKL SNEAFVAKAP EAVISKERAK MAEYQSGIEK LQAQFKAIEA
L
