ID   SYM_STRPQ               Reviewed;         665 AA.
AC   P0DG49; P59080;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 1.
DT   03-AUG-2022, entry version 57.
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; OrderedLocusNames=SPs1557;
OS   Streptococcus pyogenes serotype M3 (strain SSI-1).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=193567;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SSI-1;
RX   PubMed=12799345; DOI=10.1101/gr.1096703;
RA   Nakagawa I., Kurokawa K., Yamashita A., Nakata M., Tomiyasu Y.,
RA   Okahashi N., Kawabata S., Yamazaki K., Shiba T., Yasunaga T., Hayashi H.,
RA   Hattori M., Hamada S.;
RT   "Genome sequence of an M3 strain of Streptococcus pyogenes reveals a large-
RT   scale genomic rearrangement in invasive strains and new insights into phage
RT   evolution.";
RL   Genome Res. 13:1042-1055(2003).
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   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       MetG type 2B subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC64652.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BA000034; BAC64652.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; P0DG49; -.
DR   SMR; P0DG49; -.
DR   KEGG; sps:SPs1557; -.
DR   HOGENOM; CLU_009710_9_4_9; -.
DR   OMA; SDMHGTP; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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: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; 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; 1.
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; PS50886; TRBD; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; RNA-binding; tRNA-binding.
FT   CHAIN           1..665
FT                   /note="Methionine--tRNA ligase"
FT                   /id="PRO_0000411614"
FT   DOMAIN          562..665
FT                   /note="tRNA-binding"
FT   MOTIF           12..22
FT                   /note="'HIGH' region"
FT   MOTIF           308..312
FT                   /note="'KMSKS' region"
FT   BINDING         311
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   665 AA;  74885 MW;  AD5140C0C91BCFE6 CRC64;
     MKKPFYITTP IYYPSGKLHI GSAYTTIACD VLARYKRLMG HEVFYLTGLD EHGQKIQTKA
     KEAGITPQTY VDNMAKDVKA LWQLLDISYD KFIRTTDDYH EEVVAAVFEK LLAQDDIYLG
     EYSGWYSVSD EEFFTESQLK EVFRDEDGQV IGGIAPSGHE VEWVSEESYF LRLSKYADRL
     VAFFKERPDF IQPDGRMNEM VKNFIEPGLE DLAVSRTTFT WGVPVPSDPK HVVYVWIDAL
     LNYATALGYG QANHANFDKF WNGTVFHMVG KDILRFHSIY WPILLMMLDL PMPDRLIAHG
     WFVMKDGKMS KSKGNVVYPE MLVERFGLDP LRYYLMRSLP VGSDGTFTPE DYVGRINYEL
     ANDLGNLLNR TVAMINKYFD GTVPAYVDNG TAFDADLSQV IDAQLADYHK HMEAVDYPRA
     LEAVWTIIAR TNKYIDETAP WVLAKEDGDK AQLASVMAHL AASLRVVAHV IQPFMMETSA
     AIMAQLGLAP VSDLSTLALA DFPANTKVVA KGTPIFPRLD MEAEIDYIKA QMGDSSAISQ
     EKEWVPEEVA LKSEKDVITF ETFDAVEIRV AEVKEVSKVE GSEKLLRFRV DAGDGQDRQI
     LSGIAKCYPN EQELVGKKLQ IVANLKPRKM MKKYISQGMI LSAEHGDQLT VLTVDSSVPN
     GSIIG