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SYM_STRP6
ID   SYM_STRP6               Reviewed;         665 AA.
AC   Q5XDK8;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 2.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Methionine--tRNA ligase;
DE            EC=6.1.1.10;
DE   AltName: Full=Methionyl-tRNA synthetase;
DE            Short=MetRS;
GN   Name=metG; OrderedLocusNames=M6_Spy0370;
OS   Streptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=286636;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-946 / MGAS10394;
RX   PubMed=15272401; DOI=10.1086/422697;
RA   Banks D.J., Porcella S.F., Barbian K.D., Beres S.B., Philips L.E.,
RA   Voyich J.M., DeLeo F.R., Martin J.M., Somerville G.A., Musser J.M.;
RT   "Progress toward characterization of the group A Streptococcus metagenome:
RT   complete genome sequence of a macrolide-resistant serotype M6 strain.";
RL   J. Infect. Dis. 190:727-738(2004).
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=AAT86505.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000003; AAT86505.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q5XDK8; -.
DR   SMR; Q5XDK8; -.
DR   EnsemblBacteria; AAT86505; AAT86505; M6_Spy0370.
DR   KEGG; spa:M6_Spy0370; -.
DR   HOGENOM; CLU_009710_9_4_9; -.
DR   OMA; SDMHGTP; -.
DR   Proteomes; UP000001167; Chromosome.
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_0000139254"
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;  74882 MW;  97A97A348D87E28E CRC64;
     MKKPFYITTP IYYPSGKLHI GSAYTTIACD VLARYKRLMG HEVFYLTGLD EHGQKIQTKA
     KEAGITPQTY VDNMAKDVKA LWQLLDISYD TFIRTTDDYH 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 TAFDADLSQL IDAQLADYHK HMEAVDYPRA
     LEAVWTIIAR TNKYIDETAP WVLAKEDGDK AQLASVMAHL AASLRVVAHV IQPFMMETSA
     AIMAQLGLAP VSDLSTLALA DFPANTKVVA KGTPIFPRLD MEAEIDYIKA QMGDSSAISQ
     EKEWVPEEVA LKSEKDVITF ETFDAVEIRV AEVKEVSKVE GSEKLLRFRV DAGDGQDRQI
     LSGIAKCYPN EQELVGKKLQ IVANLKPRKM MKQYISQGMI LSAEHGDQLT VLTVDPSVPN
     GSIIG
 
 
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