SYV_JANMA
ID SYV_JANMA Reviewed; 965 AA.
AC A6SUQ8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
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=mma_0315;
OS Janthinobacterium sp. (strain Marseille) (Minibacterium massiliensis).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Janthinobacterium.
OX NCBI_TaxID=375286;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Marseille;
RX PubMed=17722982; DOI=10.1371/journal.pgen.0030138;
RA Audic S., Robert C., Campagna B., Parinello H., Claverie J.-M., Raoult D.,
RA Drancourt M.;
RT "Genome analysis of Minibacterium massiliensis highlights the convergent
RT evolution of water-living bacteria.";
RL PLoS Genet. 3:1454-1463(2007).
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; CP000269; ABR88574.1; -; Genomic_DNA.
DR RefSeq; WP_012078180.1; NC_009659.1.
DR AlphaFoldDB; A6SUQ8; -.
DR SMR; A6SUQ8; -.
DR STRING; 375286.mma_0315; -.
DR EnsemblBacteria; ABR88574; ABR88574; mma_0315.
DR KEGG; mms:mma_0315; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_4; -.
DR OMA; FATKLWN; -.
DR OrthoDB; 32262at2; -.
DR BioCyc; JSP375286:MMA_RS01650-MON; -.
DR Proteomes; UP000006388; 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..965
FT /note="Valine--tRNA ligase"
FT /id="PRO_1000022167"
FT COILED 803..835
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT COILED 900..965
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 44..54
FT /note="'HIGH' region"
FT MOTIF 559..563
FT /note="'KMSKS' region"
FT BINDING 562
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 965 AA; 108440 MW; 78093D6C28F052AC CRC64;
MELAKSFDPA DIEAFWRTEW EKRGYYTATT DADKPAFSIQ LPPPNVTGTL HLGHGFNQTI
MDGLTRYHRM RGFNTAWIPG TDHAGIATQI VVERQLDAQK ITRHDLGREK FVEKVWEWKE
KSGSTITGQI RRLGASPDWS REYFTMDEPR SKTVTEVFVR LVEQGLIYRG KRLVNWDPVL
GTAVSDLEVV SEEEDGQMWN IRYPLADGSS YKFPIAFDEA GNATEWEERN FIVVATTRPE
TMLGDVAVAV DPTDTRYQHL VGKLLTLPLC ERTIPIIADD YVDKEFGTGC VKITPAHDFN
DYAVGQRHNL DKISILTLDA KINENAPAAY QGLDRFAARK QIVADLDAQG LLELVKPHKL
MVPRGDRTNT VIEPMLTDQW FVAMSKPAPE GTYFPGKSIT EVALEKVANG EIKMLPENWT
NTYNQWLNNI QDWCISRQLW WGHQIPAWYD SEGKVYVARN EDEAKAKATA AGYNGPLTRD
EDVLDTWFSS ALVPFSTLGW PEETPDFKTF LPSSVLVTGF DIIFFWVARM VMMTTHFTGK
VPFKTVYVHG LIRDSSGQKM SKSKGNTLDP IDLIDGINVD ELVAKRTVGL MNPKQAASIE
KSTRKEFPAG ISAYGTDALR FTMASYASLG RNINFDLSRC EGYRNFCNKL WNATRFVLMN
CEGHDCGFRD APCAAGDCDP GGYTDFSQAD RWIVSKLQRT EADIAKGFAD YRFDNIAASL
YQFIWDEYCD WYLEVAKVQI QTGTEAQQRA TRRTLLRVLE TILRLAHPVI PFITEALWQT
VAPLTGYKPN PAGDSIMLQP YPEAQAGKID EQAENWMAEL KAMTDACRNL RGEMQLSPAL
RVPLIMEASD PTQAARLQSF APYLQALAKL SEVNVADKLP ESPAPVSIVG TAKLMLKVEI
DVAAERERLS KEIARLDGEI TKANSKLGNE SFVARAPAQV VAQEKERVAN FSATLNKLRE
QFAKL
