ID   SYM_GEOSE               Reviewed;         649 AA.
AC   P23920;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Methionine--tRNA ligase;
DE            EC=6.1.1.10;
DE   AltName: Full=Methionyl-tRNA synthetase;
DE            Short=MetRS;
GN   Name=metG; Synonyms=metS;
OS   Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=1422;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 1518;
RX   PubMed=1852609; DOI=10.1093/nar/19.13.3673;
RA   Mechulam Y., Schmitt E., Panvert M., Schmitter J.-M., Lapadat-Tapolsky M.,
RA   Meinnel T., Dessen P., Blanquet S., Fayat G.;
RT   "Methionyl-tRNA synthetase from Bacillus stearothermophilus: structural and
RT   functional identities with the Escherichia coli enzyme.";
RL   Nucleic Acids Res. 19:3673-3681(1991).
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:0000250}.
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;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC       Note=Binds 1 zinc ion per subunit.;
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       MetG type 2A subfamily. {ECO:0000305}.
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DR   EMBL; X57925; CAA40999.1; -; Genomic_DNA.
DR   PIR; S16682; S16682.
DR   AlphaFoldDB; P23920; -.
DR   SMR; P23920; -.
DR   ChEMBL; CHEMBL1641342; -.
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:0000049; F:tRNA binding; IEA:UniProtKB-KW.
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   CDD; cd02800; tRNA_bind_EcMetRS_like; 1.
DR   Gene3D; 2.40.50.140; -; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_01228; Met_tRNA_synth_type2; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR041872; Anticodon_Met.
DR   InterPro; IPR004495; Met-tRNA-synth_bsu_C.
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; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR002547; tRNA-bd_dom.
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   Pfam; PF01588; tRNA_bind; 1.
DR   PRINTS; PR01041; TRNASYNTHMET.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   TIGRFAMs; TIGR00398; metG; 1.
DR   TIGRFAMs; TIGR00399; metG_C_term; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR   PROSITE; PS50886; TRBD; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Metal-binding;
KW   Nucleotide-binding; Protein biosynthesis; RNA-binding; tRNA-binding; Zinc.
FT   CHAIN           1..649
FT                   /note="Methionine--tRNA ligase"
FT                   /id="PRO_0000139210"
FT   DOMAIN          555..647
FT                   /note="tRNA-binding"
FT   MOTIF           13..23
FT                   /note="'HIGH' region"
FT   MOTIF           298..302
FT                   /note="'KMSKS' region"
FT   BINDING         128
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         131
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         145
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         148
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         301
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   649 AA;  74354 MW;  BDF5DCCA79B21A89 CRC64;
     MEKKTFYLTT PIYYPSDKLH IGHAYTTVAG DAMARYKRLR GYDVMYLTGT DEHGQKIQRK
     AQEKGVTPQQ YVDDIVAGIQ ELWRKLDISY DDFIRTTQER HKKIVEKIFA RLVEQGDIYL
     GEYEGWYCTP CESFYTERQL VDGNCPDCGR PVEKVKEESY FFRMSKYVDR LLQYYEENPD
     FIQPESRKNE MINNFIKPGL EDLAVSRTTF DWGIKVPGDP KHVIYVWIDA LANYITALGY
     GTDNDEKFRK YWPADVHLVG KEIVRFHTIY WPIMLMALGL PLPKKVFGHG WLLMKDGKMS
     KSKGNVVDPV MIIDRYGLDA LRYYLLREVP FGSDGVFTPE GFIERINYDL ANDLGNLLHR
     TVAMIEKYFG GAIPPYRGPK TPFDRDLSET AREVVRQYEE AMERMEFSVA LSAVWQLIGR
     TNKYIDETQP WVLAKEESKR EELASVMAHL AESLRYTAVL LQPFLTRTPE RIFTQLGISD
     RSLKEWDSLY DFGLIPEGTN VQKGEPLFPR LDIGVEVEYI KAHMQGGKPA EAAKEEKQAA
     RAEEISIDDF AKVDLRVAEV VQPERMKNAD KLLKLQLDLG GEKRQVISGI AEFYKPEELI
     GKKVICVANL KPAKLRGEWS EGMILAGGSG GGFSLATVDQ HVPNGTKIK