SYV_GRABC
ID SYV_GRABC Reviewed; 896 AA.
AC Q0BTM1;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 95.
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};
GN OrderedLocusNames=GbCGDNIH1_0933;
OS Granulibacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Granulibacter.
OX NCBI_TaxID=391165;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1260 / CGDNIH1;
RX PubMed=17827295; DOI=10.1128/jb.00793-07;
RA Greenberg D.E., Porcella S.F., Zelazny A.M., Virtaneva K., Sturdevant D.E.,
RA Kupko J.J. III, Barbian K.D., Babar A., Dorward D.W., Holland S.M.;
RT "Genome sequence analysis of the emerging human pathogenic acetic acid
RT bacterium Granulibacter bethesdensis.";
RL J. Bacteriol. 189:8727-8736(2007).
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; CP000394; ABI61831.1; -; Genomic_DNA.
DR AlphaFoldDB; Q0BTM1; -.
DR SMR; Q0BTM1; -.
DR STRING; 391165.GbCGDNIH1_0933; -.
DR EnsemblBacteria; ABI61831; ABI61831; GbCGDNIH1_0933.
DR KEGG; gbe:GbCGDNIH1_0933; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_5; -.
DR OMA; FATKLWN; -.
DR Proteomes; UP000001963; 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; Reference proteome.
FT CHAIN 1..896
FT /note="Valine--tRNA ligase"
FT /id="PRO_1000088562"
FT COILED 830..896
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 48..58
FT /note="'HIGH' region"
FT MOTIF 543..547
FT /note="'KMSKS' region"
FT BINDING 546
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 896 AA; 100289 MW; 612DB78973229A5F CRC64;
MYERAMLSKN FDHAANEQRI YAGWEHGGAF AANPASSATP FTIMIPPPNV TGSLHMGHAL
TFTLQDSLVR WRRMQGRDVL WQPGTDHAGI ATQMVVERLL ASEGSPGRRE IGRDAFLDRV
WRWKAESGGN ITHQLRRLGA SLDWGRERFT MDEGLSAAVR DVFVTLYRQG LIYRDRRLVN
WDPQLQTAIS DLEVESREVR GNLWHIRYPL EDGEGSIIVA TTRPETMLGD SAVAVHPEDE
RYTALIGKCV ILPLTGRRIP IVADTYSDPE KGTGAVKITP AHDFNDFAVG RRHDLPMPSI
MDREGRITLA EITCTEATDI ADPAFVTGLE GQERFAARKA IVARLEEMGF LETIETHTHH
VPHGDRSGVP IEPLLTTQWF CNAAELAKPA VAAVESGDTR FVPKQWENTF FAWLRDIQPW
CISRQLWWGH RIPAWYAPDG SVYVAATAEE AQAAYGGSET LTQDEDVLDT WFSSALWPFS
TLGWPEDDSI LSRYYPTDVL ITGFDIIFFW VARMMMMGLH IQKQVPFRDV YIHGLVRDER
GQKMSKSKGN VIDPLALIEA HGADPMRFAI CLLAGPGRDI KLGPKRVEDA SRFVTKLWNA
SVFCERNGVK PEPGFDPATV TLPLSRWILA SADDAIRAAT QALEAYRFDD YAATCYRFVW
NTFCDWFVEL AKPILLATDT PEAAEIKAVA AHVLGVVLRL LHPAMPYVTE TLWDHFGYGP
EFSLIRAPWP EVGVSDPARE AARQEIDWLV RLIGEVRTVR NEMNVPPSTL TPILLKDAVA
ETVARAERWR DQIARLARAS SVTSLEGALP KGSAQAVLDE AILVIPLEGV IDLDAERTRL
TRERDKARDE AAKVVRKLEN ADFVARAKPE VVEENRDRLA ALEADIARLG AALERL
