SYV_BRUME
ID SYV_BRUME Reviewed; 910 AA.
AC Q8YGX8;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, 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}; OrderedLocusNames=BMEI1027;
OS Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=224914;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=16M / ATCC 23456 / NCTC 10094;
RX PubMed=11756688; DOI=10.1073/pnas.221575398;
RA DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J.,
RA Haselkorn R., Kyrpides N.C., Overbeek R.;
RT "The genome sequence of the facultative intracellular pathogen Brucella
RT melitensis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE008917; AAL52208.1; -; Genomic_DNA.
DR PIR; AE3380; AE3380.
DR RefSeq; WP_004686808.1; NZ_GG703778.1.
DR AlphaFoldDB; Q8YGX8; -.
DR SMR; Q8YGX8; -.
DR STRING; 224914.BMEI1027; -.
DR PRIDE; Q8YGX8; -.
DR EnsemblBacteria; AAL52208; AAL52208; BMEI1027.
DR GeneID; 29593855; -.
DR KEGG; bme:BMEI1027; -.
DR PATRIC; fig|224914.52.peg.405; -.
DR eggNOG; COG0525; Bacteria.
DR OMA; FATKLWN; -.
DR PhylomeDB; Q8YGX8; -.
DR Proteomes; UP000000419; Chromosome I.
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.
FT CHAIN 1..910
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224450"
FT COILED 842..910
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 45..55
FT /note="'HIGH' region"
FT MOTIF 554..558
FT /note="'KMSKS' region"
FT BINDING 557
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 910 AA; 102679 MW; D279DD073A3B14C2 CRC64;
MLEKTYDAAA TEPKIAERWE EAGAFKAGAG AKPGADPFAV VIPPPNVTGS LHMGHALNNT
IQDIMVRFER MRGKNVLWQP GMDHAGIATQ MVVERQLAER KEPNRHAMGR EKFIERIWQW
KAESGGMISN QLRRLGASCD WSRERFTMDE GLSRAVLEVF VTLYKQGLIY RDKRLVNWDP
KLLTAISDIE VESREIKGHL WHFRYPLENV PFDPENPHTY IIVATTRPET MLGDTGVAVN
PKDERYHALV GNDVILPLVG RHIPIVADDY ADPEAGSGTV KITPAHDFND FEVGKRNNLR
AINILTPEAA ITLKDNVDFL EDLELTAELK ALIVELDGMD RFAARKRIVE LMDERGYLEK
IDDHTHAVPH GDRGGVPIEP YLTDQWYVNA GELAKPAMAA VRDGRTQIVP KNWEKTYFDW
MENIQPWCVS RQLWWGHQIP AWYGPDSHCF VEKSEAEAKA AARAHYGEDV ALERDTDVLD
TWFSSALWPF STLGWPDKTP ELATYYPTSV LVTGFDILFF WVARMMMMGL HFMEEIPFHT
VYLHALVRDK HGAKMSKSKG NVIDPLELMD EYGADALRFT LAIMAAQGRD VKLDPARIAG
YRNFGTKLWN ATRFAQMNGV KLAPDFRPEN AKLAVNRWIL TELTRATRAV TEGIATYRFN
EAAGAAYRFV WNQFCDWYLE FLKPIFMGDD EAAKAEAQAT AAYCLDQVYK LLHPFMPFMT
EELWSLTASE GKKRDTVLAL AEWPELSFED EDAAADINWL VDLVTGIRSV RAEMNVPAGA
IAPVVVLDAN KVTVDRFARH DAAIKRLARV ERISFEQQAP KGAAQMLLGE ATICIPLGSL
IDLQAEAARL AKEAGKIAAE MDRIEKKLAN EKFVANAREE VVEAERERLL ELKEAAQRVA
TAESRIRDAS
