SYV_GRAFK
ID SYV_GRAFK Reviewed; 876 AA.
AC A0M5I5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=GFO_2933;
OS Gramella forsetii (strain KT0803).
OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Gramella.
OX NCBI_TaxID=411154;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KT0803;
RX PubMed=17107561; DOI=10.1111/j.1462-2920.2006.01152.x;
RA Bauer M., Kube M., Teeling H., Richter M., Lombardot T., Allers E.,
RA Wuerdemann C.A., Quast C., Kuhl H., Knaust F., Woebken D., Bischof K.,
RA Mussmann M., Choudhuri J.V., Meyer F., Reinhardt R., Amann R.I.,
RA Gloeckner F.O.;
RT "Whole genome analysis of the marine Bacteroidetes'Gramella forsetii'
RT reveals adaptations to degradation of polymeric organic matter.";
RL Environ. Microbiol. 8:2201-2213(2006).
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; CU207366; CAL67880.1; -; Genomic_DNA.
DR RefSeq; WP_011710781.1; NC_008571.1.
DR AlphaFoldDB; A0M5I5; -.
DR SMR; A0M5I5; -.
DR STRING; 411154.GFO_2933; -.
DR PRIDE; A0M5I5; -.
DR EnsemblBacteria; CAL67880; CAL67880; GFO_2933.
DR KEGG; gfo:GFO_2933; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_10; -.
DR OMA; FATKLWN; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000000755; 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.
FT CHAIN 1..876
FT /note="Valine--tRNA ligase"
FT /id="PRO_1000022165"
FT COILED 847..876
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 43..53
FT /note="'HIGH' region"
FT MOTIF 534..538
FT /note="'KMSKS' region"
FT BINDING 537
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 876 AA; 100797 MW; FA7FE20877C6FC5A CRC64;
MAIASQYNAK KVEDKWYDYW MKNNYFHSEV DDREPYTIVI PPPNVTGVLH MGHMLNNTIQ
DVLVRRARLK GLNACWVPGT DHASIATEAK VVAKLKAEGI DKNDLTREEF LQHAWEWTHK
HGGIILQQLK HLGASCDWER TKFTMDDDMS ASVIKVFVDL YEKGLVYRGY RMVNWDPQAK
TTLSDEEVNY EERNGKLYHL KYKIDGTEDY LTIATTRPET ILGDTAICIN PNDERFTHLK
GKKAIVPICN RTIPIIEDEY VDMEFGTGCL KVTPAHDEND KNLGDKHDLD VIDIFNDDAT
LNNYGLHYEG KDRFVVRAEI VEELELYGFL DKVEDHINKV GTSERTGAVI EPKLSDQWFL
KMKEMAQPAI KAVLGDDINL VPEKFLNTYR HWMENVRDWN ISRQLWWGHQ IPAYFYGKGK
NDFVVAETLN QAVLKAREVT GNAELQASDL TQDKDALDTW FSSWLWPMSV FNGILEPENK
EIEYYYPTND LVTAPEILFF WVARMIMAGY EYRGERPFKN VYLTGIVRDK QRRKMSKSLG
NSPDPLGLIE QYGADGVRVG MLLSSPAGND LMFDEDLCKQ GSGFTNKIWN AFRLVKGWEI
SEKIEQPETA KMAINWYTAR FQKTIREIED HYSKYRISDA LMSTYKLIWD DYCSWFLEMV
KPGYGEPMDA KTYKAIIAIL EENLKILHPF MPFVTEEIWQ EITERTPEEA LIIAKWPVEK
EFDETIIKEF SHAAEVIAGV RKIRKDKNIS FKNEIDFSVL NNENTSKTFD GVISKMGNIS
NLEYVTGSVD GALSFRVRSN EYFIPIAGAI DVEAEKEKIQ EELNYTEGFL KSVDKKLSNE
RFVNNAPEKV VAIEKAKKAD AEAKIEALKA SLKSLS
