SYV_CUPPJ
ID SYV_CUPPJ Reviewed; 955 AA.
AC Q474E1;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
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=Reut_A0863;
OS Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator
OS (strain JMP 134)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=264198;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JMP134 / LMG 1197;
RX PubMed=20339589; DOI=10.1371/journal.pone.0009729;
RA Lykidis A., Perez-Pantoja D., Ledger T., Mavromatis K., Anderson I.J.,
RA Ivanova N.N., Hooper S.D., Lapidus A., Lucas S., Gonzalez B.,
RA Kyrpides N.C.;
RT "The complete multipartite genome sequence of Cupriavidus necator JMP134, a
RT versatile pollutant degrader.";
RL PLoS ONE 5:E9729-E9729(2010).
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; CP000090; AAZ60242.1; -; Genomic_DNA.
DR RefSeq; WP_011297047.1; NC_007347.1.
DR AlphaFoldDB; Q474E1; -.
DR SMR; Q474E1; -.
DR STRING; 264198.Reut_A0863; -.
DR EnsemblBacteria; AAZ60242; AAZ60242; Reut_A0863.
DR KEGG; reu:Reut_A0863; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_4; -.
DR OMA; FATKLWN; -.
DR OrthoDB; 32262at2; -.
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; -; 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.
FT CHAIN 1..955
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224542"
FT COILED 926..955
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 49..59
FT /note="'HIGH' region"
FT MOTIF 549..553
FT /note="'KMSKS' region"
FT BINDING 552
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 955 AA; 106658 MW; 0FF724513CA586C5 CRC64;
MTAQDQSLAK SFEPAAIEAK WGPEWEKRGI AQPTFDPAKP DFAIQLPPPN VTGTLHMGHA
FNQTIMDGLT RHARMLGANT LWVPGTDHAG IATQIVVERQ LEAQGVSRHD LGREKFTEKV
WAWKEESGST ITRQVRRMGA SIDWTREYFT MSPDMSKAVT EVFVRLHEQG LIYRGKRLVN
WDPVLGTAVS DLEVDSVEED GFLWHIRYPL VEADAKGGLT HLTVATTRPE TMLGDVAVMV
HPEDERYAHL IGKEVELPLT GRRIPVIADE YVDREFGTGV VKVTPAHDFN DYAVGQRHNL
PQISILTLDA KITADAPGNY AGQDRYDARK AIVADLEAQG LLVETKKHKL MTPRSERTGS
AIEPMLTDQW FVAMSKPAPE GTFYPGRSIA EVALDAVQSG EIKLVPENWN STYNQWLANI
QDWCISRQLW WGHQIPAWYD DAGNCFVART EEEAQAKAKA AGSTGALRRE EDVLDTWFSS
ALVPFSSLGW PEETPELKHF LPSSVLVTGY DIIFFWVARM VMMTKHFTGQ VPFHTVYVHG
LVRDSEGKKM SKSEGNTLDP VDLIDGIDLD TLLKKRTTGL RRPKDAPKIE KKTKKEFPEG
IPAFGADALR FTFASLATLG RNINFDTGRC EGYRNFCNKL WNATRFVLMN TEGHDCGMGP
CNNDCGPDGY LHFSQADRWI VSLLQRVEAD VEKGFAEYRF DNIASAIYKF VWDEYCDWYL
ELAKVQIQTG TEAQQRATRR TLLRVLETVL RLAHPIIPFI TEELWQKVAP LAGRAKGDGT
ESLALQAYPL PAMAKIDEAA EQWVAQLKAV VDACRNLRGE MNISPAQRIP LYAQGDTEFL
REASAHIQAL AKLSEVRVFE DDATLQAEGA GAPVAIVGGN HLLLKIEIDV AAERVRLSKE
IERIGGEIGK CRGKLSNESF VAKAPPAVVA QETQRLSDFE QTLAKLQDQL QRLPA
