SYV_BRADU
ID SYV_BRADU Reviewed; 958 AA.
AC Q89LR8;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 111.
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=blr4475;
OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS NBRC 14792 / USDA 110).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium.
OX NCBI_TaxID=224911;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT Bradyrhizobium japonicum USDA110.";
RL DNA Res. 9:189-197(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}.
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DR EMBL; BA000040; BAC49740.1; -; Genomic_DNA.
DR RefSeq; NP_771115.1; NC_004463.1.
DR RefSeq; WP_011087247.1; NZ_CP011360.1.
DR AlphaFoldDB; Q89LR8; -.
DR SMR; Q89LR8; -.
DR STRING; 224911.27352738; -.
DR PRIDE; Q89LR8; -.
DR EnsemblBacteria; BAC49740; BAC49740; BAC49740.
DR GeneID; 64024220; -.
DR KEGG; bja:blr4475; -.
DR PATRIC; fig|224911.44.peg.4248; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_5; -.
DR InParanoid; Q89LR8; -.
DR OMA; FATKLWN; -.
DR PhylomeDB; Q89LR8; -.
DR Proteomes; UP000002526; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006438; P:valyl-tRNA aminoacylation; IBA:GO_Central.
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..958
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224449"
FT COILED 892..958
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 45..55
FT /note="'HIGH' region"
FT MOTIF 571..575
FT /note="'KMSKS' region"
FT BINDING 574
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 958 AA; 108671 MW; 37899FE401C556F1 CRC64;
MIEKNYQPAD IEARMSVVWE DSLAFKAGRP DRRDAVPFTI VIPPPNVTGS LHMGHALNNT
LQDILCRFER MRGRDVLWQP GTDHAGIATQ MVVERQLMER QQPGRREMGR EKFLERVWQW
KAESGDTIIN QLKRLGASCD WSRERFTMDE GLSKAVIKVF VELHRDGLIY KDKRLVNWDT
KLLTAISDLE VQQTEVKGSL WYLRYPIEGK TFSPEDPSSF IVVATTRPET MLGDTGVAVH
PDDERYQKLI GKHVILPLVG RKVEIVADDY SDPEKGSGAV KVTPAHDFND FEVGNRHGLR
RISVLDKEGC LDLLDNEDYL RDLPEGAAQF AEEFNKVDRF VARKRIVERL ESFGFVERIE
PHTHMVPHGD RSNSVIEPYL TDQWYVDAKT LAKPAIAAVR SGETSFVPKN WEKTYFEWME
NIQPWCISRQ LWWGHQIPAW YGPDGKVFVA ETEEEAISHA LGYYVEQEVI TAEQGREMAL
DRNKREGFIT RDEDVLDTWF SSALWPFSTL GWPEDAPEVQ RYYPTNALVT GFDIIFFWVA
RMMMMGLHFM KEVPFSTIYI HALVRDEKGA KMSKSKGNVI DPLHLIDEYG ADALRFTLAA
MAAQGRDIKL ATSRVEGYRN FATKLWNASR FAEMNHCAVP EGFEPAKAKE TLNRWIAHES
AHTTREVTEA IEAYRFNDAA GAIYRFVWNV YCDWYVELAK PVLLGPDSPA KDETRAMVAW
ARDEILKLLH PFMPFITEEL WEVTAKRDGL LALAAWPLKP AEPTPEQLAM FAAAAGPTDP
LISPALIVPI FDHADFTDPK AEAEIGWVID LVTQIRSVRA EMNIPPATLT ALVLAGASAE
TRERAPRWTD VIKRMARLSD ISFADRAPDG AVQLLVRGEV AALPLKGVID VAAERTRLDK
EIGKADADIK RAESKLANEK FVANAAEEVV EEEREKREAA LARKAKLLEA LERLKQAS
