SYV_SYNC1
ID SYV_SYNC1 Reviewed; 899 AA.
AC Q3A253;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=Pcar_2315;
OS Syntrophotalea carbinolica (strain DSM 2380 / NBRC 103641 / GraBd1)
OS (Pelobacter carbinolicus).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Syntrophotaleaceae; Syntrophotalea.
OX NCBI_TaxID=338963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2380 / NBRC 103641 / GraBd1;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chertkov O., Schmutz J., Larimer F.,
RA Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Pelobacter carbinolicus DSM 2380.";
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
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 -!- SEQUENCE CAUTION:
CC Sequence=ABA89554.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000142; ABA89554.2; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q3A253; -.
DR SMR; Q3A253; -.
DR STRING; 338963.Pcar_2315; -.
DR EnsemblBacteria; ABA89554; ABA89554; Pcar_2315.
DR KEGG; pca:Pcar_2315; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_7; -.
DR OMA; FATKLWN; -.
DR Proteomes; UP000002534; 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..899
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224526"
FT COILED 827..898
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 60..70
FT /note="'HIGH' region"
FT MOTIF 539..543
FT /note="'KMSKS' region"
FT BINDING 542
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 899 AA; 102025 MW; 5146B0163772A960 CRC64;
MSQSCMFCPK DELPMEPKLP KGYEPHDVEA KWYEFWTENG LFHADENSPK NPFSIVIPPP
NVTGVLHMGH ALNNTLQDIL ARWKRMDGHE VLWQPGTDHA GIATQNVVEK QLAAEGSSRH
DLGREGFVDR VWQWRTESGG QIINQLKRLG ASCDWERERF TMDEGLSRAV REVFVTLYEE
GLIYRDNRLI NWCPRCHTAL SDLEVEHQDQ KGNLWHLRYP VVGTDRHLVV ATTRPETMLG
DTAVAVHPED ERYADLIGKF IMLPLMDRQI PIIADEYVDK EFGSGAVKIT PAHDFNDFEI
GKRHDLEFIN IFDESGVVNG NGGRYQGLER FEARTRVLAD LDAAGLLEQT EEHLNAVGEC
YRCKTVIEPY MSLQWYVNVQ PLAEKAIEAV QTGQTRIIPQ QWEKTYFEWM FNIRDWCISR
QIWWGHRIPA WFCAACNEVT VSREDPTACS HCGATELRQE TDVLDTWFSS ALWPFSTMGW
PDKTVALEKF YPTSCLVTGF DILFFWVARM MMMGLKFMGQ VPFKDVYIHA LVRDAQGQKM
SKSKGNVIDP LTVIDEYGTD AFRFTLAAFA AQGRDVKLSV DRIAGYRNFV NKLWNASRFA
LMNLEDFDPS GIDLDDCQLT LAERWILTRL IDVAAETGKA LEEYKFNEAA SVLYAFTWHE
FCDWYIELSK DDLYGEDAAR KATSQAVLYT VLEQLLRLLH PLMPFVTEEI WQALPGERPA
VSIMSAAFST VSELPEDRQG ASHMERIMDV IKGVRNIRGE MNVPPGKRIA AVLDCKTSKA
AEVMAAGEGY IKSLARIDDL AFGVAVERPA QAATQVAGDI EILLPLAGLI DLDEEQKRLN
KEIAKVEKDV LMFSKKLSNE SFLAKAPAAV LEKDRQKLAD AEEKLSILKQ GLEKLAALQ
