SYV_BACLD
ID SYV_BACLD Reviewed; 880 AA.
AC Q65GK8; Q62S16;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 115.
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=BLi02938, BL00631;
OS Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 /
OS NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=279010;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX PubMed=15383718; DOI=10.1159/000079829;
RA Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P.,
RA Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.;
RT "The complete genome sequence of Bacillus licheniformis DSM13, an organism
RT with great industrial potential.";
RL J. Mol. Microbiol. Biotechnol. 7:204-211(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77;
RA Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J.,
RA Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B.,
RA Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A.,
RA Bolotin A., Lapidus A., Galleron N., Ehrlich S.D., Berka R.M.;
RT "Complete genome sequence of the industrial bacterium Bacillus
RT licheniformis and comparisons with closely related Bacillus species.";
RL Genome Biol. 5:R77.1-R77.12(2004).
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; AE017333; AAU41806.1; -; Genomic_DNA.
DR EMBL; CP000002; AAU24444.1; -; Genomic_DNA.
DR RefSeq; WP_009329289.1; NC_006322.1.
DR AlphaFoldDB; Q65GK8; -.
DR SMR; Q65GK8; -.
DR STRING; 279010.BL00631; -.
DR EnsemblBacteria; AAU24444; AAU24444; BL00631.
DR KEGG; bld:BLi02938; -.
DR KEGG; bli:BL00631; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_9; -.
DR OMA; FATKLWN; -.
DR OrthoDB; 32262at2; -.
DR BioCyc; BLIC279010:BLI_RS14535-MON; -.
DR Proteomes; UP000000606; 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; -; 3.
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..880
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224435"
FT COILED 809..880
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 49..59
FT /note="'HIGH' region"
FT MOTIF 525..529
FT /note="'KMSKS' region"
FT BINDING 528
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 880 AA; 101888 MW; 059404916742E163 CRC64;
MDNQELTMPT KYDPSAVEKD RYDYWVNGKF FEAKNDPEKE PYTVVIPPPN VTGKLHLGHA
WDSTLQDIVT RMKRMQGYDV LWLPGMDHAG IATQAKVEAK LREEGKTRYD LGREKFLEET
WNWKEEYADF IRSQWAKLGL GLDYSRERFT LDEGLSKAVR EVFVKLYEKG LIYRGEYIIN
WDPATKTALS DIEVIYKDVQ GAFYHMRYPL KDGSGSIEIA TTRPETMLGD TAVAVHPEDE
RYKHLIGKTV ILPITGREIP IVGDDYVDME FGSGAVKITP AHDPNDFEIG NRHNLERILV
MNEDGTMNDN ALQYKGMDRF ECRKQIVKDL QEEGVLFKIE EHTHSVGHSE RSGAVVEPYL
STQWFVQMQP LADAAIELQK SEGKVNFVPD RFEKTYLHWM ENIRDWCISR QLWWGHRIPA
WYHKETGEIY VGVEAPEDAE NWEQDKDVLD TWFSSALWPF STMGWPDIDE EDFKRYYPTN
VLVTGYDIIF FWVSRMIFQG IEFTGERPFK DVLIHGLIRD DQGRKMSKSL GNGVDPMDVI
DKYGADSLRY FLATGSSPGQ DLRFSFEKVE STWNFANKIW NASRFALMNM DGMTYEELDL
SGEKSVADKW ILTRLNETIE TVTQLADKYE FGEVGRHLYN FIWDDFCDWY IEMAKLPLYG
EDEAAKKTTR SILAYVLDQT MRLLHPFMPF LTEEIWQHLP HEGESITVAK WPEAVKEYTD
TEAAADMKLL VEVIRAVRNI RSEVNTPLSK QIELYIKTST PEIAERLEEN RSYVERFTNP
SLLQIGTDIQ AVDKAMTAVV SGAELILPLE GLINIDEEIS RLQKELDKLT KEVERVQKKL
SNEGFMKKAP AHVIEEERAK EADYTAKREA VEKRIAELKN
