SYM_THEVB
ID SYM_THEVB Reviewed; 529 AA.
AC P59081;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2002, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Methionine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_01228};
DE EC=6.1.1.10 {ECO:0000255|HAMAP-Rule:MF_01228};
DE AltName: Full=Methionyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_01228};
DE Short=MetRS {ECO:0000255|HAMAP-Rule:MF_01228};
GN Name=metG {ECO:0000255|HAMAP-Rule:MF_01228}; Synonyms=metS;
GN OrderedLocusNames=tlr0750;
OS Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC Thermosynechococcus.
OX NCBI_TaxID=197221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takeuchi C., Yamada M., Tabata S.;
RT "Complete genome structure of the thermophilic cyanobacterium
RT Thermosynechococcus elongatus BP-1.";
RL DNA Res. 9:123-130(2002).
CC -!- FUNCTION: Is required not only for elongation of protein synthesis but
CC also for the initiation of all mRNA translation through initiator
CC tRNA(fMet) aminoacylation. {ECO:0000255|HAMAP-Rule:MF_01228}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-
CC methionyl-tRNA(Met); Xref=Rhea:RHEA:13481, Rhea:RHEA-COMP:9667,
CC Rhea:RHEA-COMP:9698, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57844, ChEBI:CHEBI:78442, ChEBI:CHEBI:78530,
CC ChEBI:CHEBI:456215; EC=6.1.1.10; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01228};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01228};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01228};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01228}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01228}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC MetG type 2A subfamily. {ECO:0000255|HAMAP-Rule:MF_01228}.
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DR EMBL; BA000039; BAC08301.1; -; Genomic_DNA.
DR RefSeq; NP_681539.1; NC_004113.1.
DR RefSeq; WP_011056597.1; NC_004113.1.
DR AlphaFoldDB; P59081; -.
DR SMR; P59081; -.
DR STRING; 197221.22294471; -.
DR EnsemblBacteria; BAC08301; BAC08301; BAC08301.
DR KEGG; tel:tlr0750; -.
DR PATRIC; fig|197221.4.peg.790; -.
DR eggNOG; COG0143; Bacteria.
DR OMA; SDMHGTP; -.
DR OrthoDB; 761140at2; -.
DR Proteomes; UP000000440; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004825; F:methionine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006431; P:methionyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd07957; Anticodon_Ia_Met; 1.
DR CDD; cd00814; MetRS_core; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_01228; Met_tRNA_synth_type2; 1.
DR InterPro; IPR041872; Anticodon_Met.
DR InterPro; IPR014758; Met-tRNA_synth.
DR InterPro; IPR023457; Met-tRNA_synth_2.
DR InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
DR InterPro; IPR033911; MetRS_core.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR PANTHER; PTHR43326; PTHR43326; 1.
DR Pfam; PF19303; Anticodon_3; 1.
DR Pfam; PF09334; tRNA-synt_1g; 2.
DR PRINTS; PR01041; TRNASYNTHMET.
DR SUPFAM; SSF47323; SSF47323; 1.
DR TIGRFAMs; TIGR00398; metG; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Metal-binding;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome; Zinc.
FT CHAIN 1..529
FT /note="Methionine--tRNA ligase"
FT /id="PRO_0000139260"
FT MOTIF 12..22
FT /note="'HIGH' region"
FT MOTIF 301..305
FT /note="'KMSKS' region"
FT BINDING 127
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01228"
FT BINDING 130
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01228"
FT BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01228"
FT BINDING 148
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01228"
FT BINDING 304
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01228"
SQ SEQUENCE 529 AA; 60336 MW; 9E1BD88CF6F0D2AB CRC64;
MSPHFSLTTP LYYVNALPHI GSAYTTIAAD VLARFYRLQG YQVRFITGTD EHGQKIERTA
QQRGLSPQAH CDEIAAGFQA LWQQLNIHYD RFSRTTSPRH HAIVNEFFQR VWDNGDIYLG
QQQGWYCVEC EEFKEERELL EGRRCPIHVN RTVEWRDERN YFFRLSKYQQ ALLDHYAEHP
DFVQPPSRRN EVLSFIERGL QDFSISRVNL AWGFPVPTDP EQTLYVWFDA LLGYVTALLE
PEDEPTLANA LKTWWPINLH IIGKDILRFH GISWPAMLMS AGLPLPEQIF VHGFLTKDGQ
KMGKSLGNTL DPFALVAQYG ADAVRYYFMK EVEFGRDGDF SETRFVTILN ADLANDLGNL
LNRTLKMAWK YTDGKVPNVQ GAAIPREHPL RQLAEHLSQT YGQGYRQLAF HEVCQQALTL
ARAGNKFLDE EAPWKRYRAG ETAAVAEILY CVLESVRLVA YVLAPIIPQL SEAIYGQLGY
SIRFNGSIAP DLLGDRQAQW GVLPASQPLA NPEPIFQKLL LPATVADSP
