SYV_LACAC
ID SYV_LACAC Reviewed; 879 AA.
AC Q5FKW5;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 98.
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=LBA0794;
OS Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=272621;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700396 / NCK56 / N2 / NCFM;
RX PubMed=15671160; DOI=10.1073/pnas.0409188102;
RA Altermann E., Russell W.M., Azcarate-Peril M.A., Barrangou R., Buck B.L.,
RA McAuliffe O., Souther N., Dobson A., Duong T., Callanan M., Lick S.,
RA Hamrick A., Cano R., Klaenhammer T.R.;
RT "Complete genome sequence of the probiotic lactic acid bacterium
RT Lactobacillus acidophilus NCFM.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:3906-3912(2005).
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; CP000033; AAV42659.1; -; Genomic_DNA.
DR RefSeq; WP_011254252.1; NC_006814.3.
DR RefSeq; YP_193690.1; NC_006814.3.
DR AlphaFoldDB; Q5FKW5; -.
DR SMR; Q5FKW5; -.
DR STRING; 272621.LBA0794; -.
DR PRIDE; Q5FKW5; -.
DR EnsemblBacteria; AAV42659; AAV42659; LBA0794.
DR GeneID; 56942423; -.
DR KEGG; lac:LBA0794; -.
DR PATRIC; fig|272621.13.peg.756; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_9; -.
DR OMA; FATKLWN; -.
DR BioCyc; LACI272621:G1G49-809-MON; -.
DR Proteomes; UP000006381; 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..879
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224489"
FT COILED 806..879
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 45..55
FT /note="'HIGH' region"
FT MOTIF 521..525
FT /note="'KMSKS' region"
FT BINDING 524
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 879 AA; 101629 MW; AC7197C5E44DD4ED CRC64;
MTDLAPKYNP NEVEKGRYQE WLDEDLFKPS GDKKAHPYSI VIPPPNVTGK LHLGHAWDTA
IQDTLIRFKR MEGYDTLYLP GMDHAGIATQ AKVEAKLRKQ GKDRHEMGRE AFVKQVWDWK
DEYANIIKSQ WSKLGLSLDY SRERFTLDKG LSKAVKKVFV QLYNEGLIYR GEYIINWDPT
LETALSDIEV IHKDDKGAFY HVKYPFADGS GFVEIATTRP ETMFGDTAVA VAPGDPRYKD
IVGKELILPL VGRHIPIIED QHVDPEFGTG LVKITPAHDP NDFQVGNRHN LKRINVMNDD
GTMNEEAGKY AGMDRFECRE ALVKDLKEEG YLIKVEPIVH SVGHSERSGV QVEPRLSKQW
FVKMKPLADK VLENQKSEGK VNFVPERFEQ TLNHWMENVH DWVISRQLWW GHRIPAWYNK
KTGETYVGEE APKDIENWEQ DPDVLDTWFS SALWPFSTMG WPDTDNPDFK RYFPTNALVT
GYDIIFFWVS RMIFQSLHFT KERPFKDVVL HGLIRDEQGR KMSKSLGNGI DPMDVIDKYG
ADALRWFLLN GTAPGQDTRF SYTKMDAAWN FINKIWNVSR FVIMNLPEDA KPAHMPDTSK
FDLSDKWIFD RLNHTIGEVT RLFGEYQFGE AGREAYNFIW NDFCDWYIEI SKVALNGDDE
ELKARKQENL IWILDQILRL MHPIMPFVTE KLWLSMPHEG KSIMTASYPV THKEFENKTA
DQEMDFLIEV IKAVRNIRME VNAPMSSEID IMIKLDDLNN KHILDENVDY VENFLHPKKL
EVSADIEAPK LAKTAVIPGA QIFVPLTELV NVDEELAKME KEAKRLEDEV ARCEKKLSNK
GFVDHAPEAV VNKEKEKMAD YESQLSGVRE RIQDLKESK
