AC MF_01228; DC Protein; auto TR HAMAP; MF_01228; -; 1; level=0 XX Names: Met_tRNA_synth_type2 XX ID SYM DE RecName: Full=Methionine--tRNA ligase; DE EC=6.1.1.10; DE AltName: Full=Methionyl-tRNA synthetase; DE Short=MetRS; GN Name=metG; XX 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. 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; case and and and ( or or ) CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Note=Binds 1 zinc ion per subunit.; end case case CC -!- SUBUNIT: Homodimer. end case case not and CC -!- SUBUNIT: Monomer. end case CC -!- SUBCELLULAR LOCATION: Cytoplasm. case and and and ( or or ) CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. CC MetG type 2A subfamily. end case case not CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. CC MetG type 2B subfamily. end case XX DR Pfam; PF00133; tRNA-synt_1; 1; trigger=no DR PRINTS; PR01041; TRNASYNTHMET; 1; trigger=no DR NCBIfam; TIGR00398; MetG; 1; trigger=no DR NCBIfam; TIGR00399; MetG_C_term; 1; trigger=no DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1; trigger=no DR PROSITE; PS50886; TRBD; 0-1; trigger=yes XX KW Cytoplasm KW Aminoacyl-tRNA synthetase KW Protein biosynthesis KW Ligase KW ATP-binding KW Nucleotide-binding case KW RNA-binding KW tRNA-binding end case case and and and ( or or ) KW Metal-binding KW Zinc end case XX GO GO:0005524; F:ATP binding GO GO:0004825; F:methionine-tRNA ligase activity GO GO:0006431; P:methionyl-tRNA aminoacylation GO GO:0005737; C:cytoplasm XX FT From: SYM_THET8 (P23395) FT MOTIF 12..22 FT /note="'HIGH' region" FT Condition: [YDFAS]-Y-x(5)-H-[LIV]-G-[SHN] FT MOTIF 297..301 FT /note="'KMSKS' region" FT Condition: K-[MI]-[SG]-K-[ST] FT BINDING 127 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Condition: C FT BINDING 130 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Condition: C FT BINDING 144 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Condition: C FT BINDING 147 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Condition: [HC] FT From: SYM_SYNY3 (Q55729) case not FT BINDING 152 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Condition: [HC] end case FT From: SYM_MYCGE (P47267) case not FT BINDING 147 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Condition: [HC] end case FT BINDING 300 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Condition: K XX Size: 497-683; Related: MF_00098; Template: P23395; P9WFU5; P23920; Scope: Bacteria Fusion: Nter: None Cter: None Duplicate: in CLOPE Plasmid: None Comments: Subfamily 2a links 1 zinc ion ion (shown in THET8) whereas subfamily 2b does not (shown in MYCTU). Possible wrong starts in AQUAE and SYNY3. XX # Revision 1.41 2023/06/01 //