SYV_METTH
ID SYV_METTH Reviewed; 877 AA.
AC O26861;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Valine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02005};
DE EC=6.1.1.9 {ECO:0000255|HAMAP-Rule:MF_02005};
DE AltName: Full=Valyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02005};
DE Short=ValRS {ECO:0000255|HAMAP-Rule:MF_02005};
GN Name=valS {ECO:0000255|HAMAP-Rule:MF_02005}; OrderedLocusNames=MTH_767;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(1997).
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_02005}.
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_02005};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02005}.
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_02005}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC ValS type 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_02005}.
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DR EMBL; AE000666; AAB85270.1; -; Genomic_DNA.
DR PIR; E69202; E69202.
DR RefSeq; WP_048060895.1; NC_000916.1.
DR AlphaFoldDB; O26861; -.
DR SMR; O26861; -.
DR STRING; 187420.MTH_767; -.
DR PRIDE; O26861; -.
DR EnsemblBacteria; AAB85270; AAB85270; MTH_767.
DR GeneID; 24853900; -.
DR KEGG; mth:MTH_767; -.
DR PATRIC; fig|187420.15.peg.755; -.
DR HOGENOM; CLU_001493_0_2_2; -.
DR OMA; FATKLWN; -.
DR Proteomes; UP000005223; 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; 3.40.50.620; -; 2.
DR HAMAP; MF_02005; Val_tRNA_synth_type2; 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; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR InterPro; IPR022874; Valine-tRNA_ligase_type_2.
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 PRINTS; PR00986; TRNASYNTHVAL.
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; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..877
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000106250"
FT MOTIF 46..56
FT /note="'HIGH' region"
FT MOTIF 529..533
FT /note="'KMSKS' region"
FT BINDING 532
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02005"
SQ SEQUENCE 877 AA; 100946 MW; B939720D6D8FF0DB CRC64;
MTDNQIPKDY NHKNEVKWQK KWQEEDIYRF IGSGTKPRYI IDTPPPYPTG SIHMGHVLNW
VYMDIIARFK RMRGFDVLFP QGWDCHGLPT EVKVEETHNI KKSDVSREEF RRLCVELTQE
NIRMMKEQMQ RLGFSQDWNH EFVTMTPEYM RRTQLSFLRM YRDGLIYQGV HPVNWCPRCE
TAIAFAEVEY IENETNLNYV RFPVEGADEH ITIATTRPEL MAACVAVVVH PDDERFREFE
DKLIEVPLFG QKVKLIKDPE VDPEFGTGAV MVCTFGDKTD VSWVNRHGLD VIDAIDERGY
MTEAAGKYQG LTIAECKEKI VEDLENEGFL LKKEPVRQNV GTCWRCKTPI EILVKKQWFV
AVKKLIPQVR EAAEEMKWVP GHMKTRLLNW TGSMDWDWCI SRQRIFATPI PVWYCSECGR
VHVADEEMLP VDPTRDGPGI TCECGSTEFI GEEDVLDTWM DSSISPLSVA GWPDESYREL
FPADLRPQGH DIIRTWAFYT ILRCMALTGE KPFSEIVING MVFGEDGHKM SKSRGNVIAP
EEVLEDYGAD ALRLWAAGSV PGSDVPFAWK DVKYGYKFLR KFWNAFRFIS IHLTENPEVE
ARPMDRWILS RLMNLVAEVT ESLDDYNFAA AVNRVQTFIW HDFCDEYIEA VKYRLYSDED
PESRMAAQNT LRMVLDTCLR LLAPVAPHFT EEVHQHVGEG SIHLRGWPEH IPEIVDPEIE
RSGDLAVEII GEIRRFKSSS KMPLNAPLKA ATIYTDNESA EMIKPFLDDI AGTMNIGDIS
LVAGKPEITE RAVELEPRME KIGPEFRSDA PAIISWLTGA DPHEVYEEIQ RNGEIEVEGN
RLTMDHISFR KEVIGTAGER VDVLNLDEPE VIIEIVR
