SYV_LACLA
ID SYV_LACLA Reviewed; 880 AA.
AC Q9CDP6;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 110.
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=LL2173;
GN ORFNames=L0351;
OS Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=272623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL1403;
RX PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "The complete genome sequence of the lactic acid bacterium Lactococcus
RT lactis ssp. lactis IL1403.";
RL Genome Res. 11:731-753(2001).
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; AE005176; AAK06271.1; -; Genomic_DNA.
DR PIR; E86896; E86896.
DR RefSeq; NP_268330.1; NC_002662.1.
DR RefSeq; WP_010906358.1; NC_002662.1.
DR AlphaFoldDB; Q9CDP6; -.
DR SMR; Q9CDP6; -.
DR STRING; 272623.L0351; -.
DR PaxDb; Q9CDP6; -.
DR PRIDE; Q9CDP6; -.
DR EnsemblBacteria; AAK06271; AAK06271; L0351.
DR KEGG; lla:L0351; -.
DR PATRIC; fig|272623.7.peg.2333; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_9; -.
DR OMA; FATKLWN; -.
DR Proteomes; UP000002196; 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 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..880
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224493"
FT COILED 808..880
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 46..56
FT /note="'HIGH' region"
FT MOTIF 520..524
FT /note="'KMSKS' region"
FT BINDING 523
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 880 AA; 100538 MW; 3D230091DB3D8001 CRC64;
MTNELTPKFN PTEVEAGRYE KWLEADVFKP SGNPDAEPYS IVIPPPNVTG KLHLGHAWDT
TLQDIIIRQK RMQGFDTLWL PGMDHAGIAT QAKVAARLAE DGILPQDLGR EKFLDKVWEW
KDEYATTIKE QWGKMGISVD YSRERFTLDE GLSQAVRKVF VQLYNKGWIY RGEKLINWDP
KAMTALSDIE VIHKEIDGAF YHITYQIEGS DEFVEIATTR PETFLGDTAV IVNEKDERYK
HLVGKNVILP IINRVIPILT DDHADMEKGT GVVKITPAHD PNDFEVAMRH DLPMINMMNN
DGTINENGGK YEGLDRFEAR KQIVADLKEL GQLVDIKPVR HEVGHSERTG VVVEPRLSTQ
WFVKMDELAK NAIANQTTED AVEFYPPRFN DTFMQWMENV HDWVISRQLW WGHQIPAWYN
EAGEMYVGEE APEGEGWTQD EDVLDTWFSS ALWPFSTMGW PDENSADFIR YFPTSTLVTG
YDIIFFWVSR MIFQSLEFTG KSPFHNVLIH GLIRDEEGRK MSKSLGNGID PMDVIEKYGA
DALRWFLSNG SAPGQDVRFS YDKMDAAWNF INKIWNVSRY ILMNAEDISA DAVSSALTKV
ANKTAGNVTD RWILTRLNDT VERVTEQMDK FEFGVAGHIL YNFIWDEFAN WYLELTKEVM
FGEDEAEKDI TRAVLLHVLD QVLRLLHPIM PFFTEEIFEK LPNTSGSIVV AEYPKVRPEF
NDDKASEGVA MLIELITAVR NIRAEVNTPL SKAVPMLIKS EHADFLNAVS PYISRFTNPS
ELTIAKDLAV PEQAMSAVIT GAELYLPLAG LINIEEEIAR LEKELAKWQK ELDLVNKKLG
NERFVANAKA EVVQKEKDKL ADYQEKFDTV KARIAELKEN
