SYV_SHEON
ID SYV_SHEON Reviewed; 958 AA.
AC Q8EBS5;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 112.
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=SO_3424;
OS Shewanella oneidensis (strain MR-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=211586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-1;
RX PubMed=12368813; DOI=10.1038/nbt749;
RA Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A.,
RA Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J.,
RA Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J.,
RA Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V.,
RA Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
RT "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT Shewanella oneidensis.";
RL Nat. Biotechnol. 20:1118-1123(2002).
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; AE014299; AAN56421.1; -; Genomic_DNA.
DR RefSeq; NP_718977.1; NC_004347.2.
DR RefSeq; WP_011073282.1; NZ_CP053946.1.
DR AlphaFoldDB; Q8EBS5; -.
DR SMR; Q8EBS5; -.
DR STRING; 211586.SO_3424; -.
DR PaxDb; Q8EBS5; -.
DR KEGG; son:SO_3424; -.
DR PATRIC; fig|211586.12.peg.3319; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_6; -.
DR OMA; FATKLWN; -.
DR OrthoDB; 32262at2; -.
DR PhylomeDB; Q8EBS5; -.
DR BioCyc; SONE211586:G1GMP-3188-MON; -.
DR Proteomes; UP000008186; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006438; P:valyl-tRNA aminoacylation; IBA:GO_Central.
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..958
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224553"
FT COILED 887..956
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 42..52
FT /note="'HIGH' region"
FT MOTIF 554..558
FT /note="'KMSKS' region"
FT BINDING 557
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 958 AA; 108756 MW; 5130AB5F18BD4803 CRC64;
MEKTYDPQSI EQTLYQNWEE KGYFKPHGDA SQGNYCIMIP PPNVTGSLHM GHAFQDTIMD
TLIRYQRMKG KNTLWQVGTD HAGIATQMLV ERKLEAEEGK SRHDLGRDVF MEKVWEWKAQ
SGGTITKQLR RMGASVDWDR ERFTMDEGLS KAVQEVFVRL YEDDLIYRGK RLVNWDPKLH
TAISDLEVEN KEKQGHMWHL RYPLADGELT ADGKDYLEVA TTRPETMLGD SAVAVHPDDE
RYQALIGKYI LLPIVNRRIP IVADDYVDMA FGTGCVKITP AHDFNDYEVG KRHKLPMFNV
LTLDAAIRSS AEVVNTDGTI NTSLDGSLPE RYAGLDRFKA RDAIVAEFET LGLLEKIAPH
GLKVPYGDRS GVVIEPMLTD QWYVAVAPMA KTAIEAVENG DIKFVPQQYE NMYFSWMRDI
QDWCISRQLW WGHRIPAWYD TNGKVYVGRT EAEVRAKHDI DDAIALRQDE DVLDTWFSSA
LWTFSTLGWP DNVEDLKTFH PTDVLVTGFD IIFFWVARMI MMTMHFIKDE DGKPQVPFKT
VYVTGLIRDE AGNKMSKSKG NVLDPLDMID GIDLETLVEK RTGNMMQPQL AAKIEKSTRK
EFENGIEAHG TDALRFTLAA MASTGRDINW DMKRLDGYRS FCNKLWNASR YVLMNTEGQD
CGPNSPDYQG GEMELSLADR WIIDLFNQTV KTYDEHMASY RFDLAANTLY EFTWNQFCDW
YLELTKPVLQ NGTEAQMRGT RHTLVNVLEA MQRLMHPMMP YITETIWQRV KPLTGVQGDT
IMLAPFPAFD AAKVDATAMA DLEWVKQVIV AVRNIRAELN IAPSKPLNAL LRGVSAQDKA
RIEANQAFFA TLARLESMTI LGEGETAPMS TTGLIGEMEL LIPMAGLVDV AAEMARIDKQ
LEKLTQEIAR IEGKLSNEGF VAKAPPAVID KERAKMADLS RDIDKLTEQK AEFAKLEA
