ID   SYM_BACFR               Reviewed;         679 AA.
AC   Q64MP7;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 2.
DT   02-SEP-2026, entry version 129.
DE   RecName: Full=Methionine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00098};
DE            EC=6.1.1.10 {ECO:0000255|HAMAP-Rule:MF_00098};
DE   AltName: Full=Methionyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00098};
DE            Short=MetRS {ECO:0000255|HAMAP-Rule:MF_00098};
GN   Name=metG {ECO:0000255|HAMAP-Rule:MF_00098}; OrderedLocusNames=BF4503;
OS   Bacteroides fragilis (strain YCH46).
OC   Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
OC   Bacteroidaceae; Bacteroides.
OX   NCBI_TaxID=295405;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YCH46;
RX   PubMed=15466707; DOI=10.1073/pnas.0404172101;
RA   Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N.,
RA   Kuhara S., Hattori M., Hayashi T., Ohnishi Y.;
RT   "Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions
RT   regulating cell surface adaptation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004).
CC   -!- FUNCTION: Catalyzes the attachment of L-methionine to tRNA(Met). Is
CC       required not only for elongation of protein synthesis but also for the
CC       initiation of all mRNA translation through initiator tRNA(fMet)
CC       aminoacylation. {ECO:0000255|HAMAP-Rule:MF_00098}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=tRNA(Met) + L-methionine + ATP = L-methionyl-tRNA(Met) + AMP +
CC         diphosphate; Xref=Rhea:RHEA:13481, Rhea:RHEA-COMP:9667, Rhea:RHEA-
CC         COMP:9698, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57844,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78530, ChEBI:CHEBI:456215;
CC         EC=6.1.1.10; Evidence={ECO:0000255|HAMAP-Rule:MF_00098};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13482;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00098};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00098};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00098};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00098}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00098}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       MetG type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_00098}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD51240.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AP006841; BAD51240.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_005791925.1; NC_006347.1.
DR   AlphaFoldDB; Q64MP7; -.
DR   SMR; Q64MP7; -.
DR   STRING; 295405.BF4503; -.
DR   KEGG; bfr:BF4503; -.
DR   PATRIC; fig|295405.11.peg.4335; -.
DR   HOGENOM; CLU_009710_1_2_10; -.
DR   OrthoDB; 9810191at2; -.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004825; F:methionine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; IEA:InterPro.
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   FunFam; 1.10.730.10:FF:000030; Methionine--tRNA ligase; 1.
DR   FunFam; 2.20.28.20:FF:000001; Methionine--tRNA ligase; 1.
DR   FunFam; 2.40.50.140:FF:000042; Methionine--tRNA ligase; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   Gene3D; 1.10.730.10; Isoleucyl-tRNA Synthetase, Domain 1; 1.
DR   Gene3D; 2.20.28.20; Methionyl-tRNA synthetase, Zn-domain; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   HAMAP; MF_00098; Met_tRNA_synth_type1; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR041872; Anticodon_Met.
DR   InterPro; IPR004495; Met-tRNA-synth_bsu_C.
DR   InterPro; IPR023458; Met-tRNA_ligase_1.
DR   InterPro; IPR014758; Met-tRNA_synth.
DR   InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
DR   InterPro; IPR033911; MetRS_core.
DR   InterPro; IPR029038; MetRS_Zn.
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   NCBIfam; TIGR00398; metG; 1.
DR   NCBIfam; TIGR00399; metG_C_term; 1.
DR   NCBIfam; NF001100; PRK00133.1; 1.
DR   PANTHER; PTHR45765; METHIONINE--TRNA LIGASE; 1.
DR   PANTHER; PTHR45765:SF1; METHIONINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR   Pfam; PF19303; Anticodon_3; 1.
DR   Pfam; PF09334; tRNA-synt_1g; 1.
DR   Pfam; PF01588; tRNA_bind; 1.
DR   PRINTS; PR01041; TRNASYNTHMET.
DR   SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF57770; Methionyl-tRNA synthetase (MetRS), Zn-domain; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 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..679
FT                   /note="Methionine--tRNA ligase"
FT                   /id="PRO_0000139101"
FT   DOMAIN          578..679
FT                   /note="tRNA-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00098"
FT   MOTIF           15..25
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00098"
FT   MOTIF           332..336
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00098"
FT   BINDING         147
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00098"
FT   BINDING         150
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00098"
FT   BINDING         160
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00098"
FT   BINDING         163
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00098"
FT   BINDING         335
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00098"
SQ   SEQUENCE   679 AA;  77595 MW;  790D69EF7F69799F CRC64;
     MEKNFKRTTV TSALPYANGP VHIGHLAGVY VPADIYVRYL RLKKEDVLFI GGSDEHGVPI
     TIRAKKEGIT PQDVVDRYHF LIKKSFEEFG ISFDVYSRTS SKTHHELASD FFKKLYEKGE
     FIEKTSEQYY DEEAHQFLAD RYITGECPHC HSEGAYGDQC EKCGTSLSPT DLINPKSAIS
     GSKPVMKETK HWYLPLDKHE TWLRQWILEE HKEWRPNVYG QCKSWLDMGL QPRAVSRDLD
     WGIPVPVEGA EGKVLYVWFD APIGYISNTK ELLPDSWETW WKDPETRLVH FIGKDNIVFH
     CIVFPAMLKA EGSYILPDNV PSNEFLNLEG DKISTSRNWA VWLHEYLEDF PGKQDVLRYV
     LTANAPETKD NDFTWKDFQA RNNNELVAVY GNFVNRAMVL TQKYFEGKVP AAGELTDYDK
     ETLKEFSDVK AEVEKLLNVF KFRDAQKEAM NLARIGNKYL ADTEPWKLAK TDMERVGTIL
     NISLQLVANL AIAFEPFLPF SSERLRQMLN MDSFDWAELG RNDLLPAGHQ LNKPELLFEK
     IEDATIEAQV QKLLDTKKAN EEANYKAKPI RANIEFDDFM KLDIRVGTVL ECQKVPKADK
     LLQFKIDDGL ETRTIVSGIA QHYKPEELVG KQVCFIANLA PRKLKGIVSE GMILSAENND
     GSLAVVMPGR EVKPGSEVK
//