SYV_MALP2
ID SYV_MALP2 Reviewed; 869 AA.
AC Q8EX08;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 117.
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=MYPE420;
OS Malacoplasma penetrans (strain HF-2) (Mycoplasma penetrans).
OC Bacteria; Tenericutes; Mycoplasmoidales; Mycoplasmoidaceae; Malacoplasma.
OX NCBI_TaxID=272633;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HF-2;
RX PubMed=12466555; DOI=10.1093/nar/gkf667;
RA Sasaki Y., Ishikawa J., Yamashita A., Oshima K., Kenri T., Furuya K.,
RA Yoshino C., Horino A., Shiba T., Sasaki T., Hattori M.;
RT "The complete genomic sequence of Mycoplasma penetrans, an intracellular
RT bacterial pathogen in humans.";
RL Nucleic Acids Res. 30:5293-5300(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 -!- SEQUENCE CAUTION:
CC Sequence=BAC43832.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BA000026; BAC43832.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q8EX08; -.
DR SMR; Q8EX08; -.
DR STRING; 272633.26453500; -.
DR PRIDE; Q8EX08; -.
DR EnsemblBacteria; BAC43832; BAC43832; BAC43832.
DR KEGG; mpe:MYPE420; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_14; -.
DR OMA; FATKLWN; -.
DR Proteomes; UP000002522; 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; -; 3.
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..869
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224513"
FT COILED 797..869
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 51..61
FT /note="'HIGH' region"
FT MOTIF 523..527
FT /note="'KMSKS' region"
FT BINDING 526
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 869 AA; 102214 MW; 5E13DF819EC67349 CRC64;
MSNIKNNNDL SKKYDHKICE QQFSLWTTQK ELNKKNLKAN KNSYSILLPP PNVTGNLHLG
HALNGTIQDC LIRFNNLKGL SAYWICGMDH AGIATQTKYE KYLRENKISN KDKSRDEKVA
DLFEWSQNVG NNIRNQWKNM GFFLDYENEH FTLEKKSNEM VNQVFVKMYN DGLIYRSKTL
VNWDIKLQSA ISNIEVIKKE VETNLYYIRY YLSNSKDYLL VATTRPETIF VDECLVVNPK
DKRYKNYINK FAINPLTNKE IKIIADEYVD IQFGTGVMKC TPAHDFNDYE LGKKYKLNII
SCFNEDGTTN NYAVGFENLK IADARVKCVE YLEKNNLLEK VEKTISNVGF SERTNAVVEP
MMSEQWFVKV SEYSKKVIEL QKSSKKIQFF PIKFEKNLIN WMTNLNDWCI SRQLWWGHQI
PVWYKKDSKE IYVGTKPPKN EELYVRDNDV LDTWFSSGLW PITTTDALKS KDALFPTNVL
VTGFDIIFFW VFRMMFFSLY LKKEVPFKHC YITGLIRDEH NNKMSKSLGN GVDPNDVIEK
YGADALRLFL LSSSSPGEDL CYVEEKVKSC WGFINKLWNS FRYVEMNSSD FNFDEDKTPK
NLEDFDKWIL NKFNKAYSEF LQQFNKYNFL VSIKKILDFT WDDFCNTYIE LSKNRTSNQE
SKLWVLNYLI KKILILFHPM CPFVTSNLYD NFKFKTKDSI LLERLDFKKI SNLKESSIED
VLQIINKIRI FNFENKIPNN KVIDIHLEVL NPKLFKISDE VINILNTAKI NIVKQDIKSL
KPDYVENNYL IFILNKEDLL GSNNEANNIE KIKKEIEFVK SEISRCNGML SNKSFIEKAP
KEKIELEKSK KEKHEMKLKE LEKLLSSHK
