ID   SYM_ALKHC               Reviewed;         660 AA.
AC   Q9KGK8;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 133.
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=BH0053;
OS   Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS   / JCM 9153 / C-125) (Bacillus halodurans).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX   NCBI_TaxID=272558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX   PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA   Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA   Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT   "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT   and genomic sequence comparison with Bacillus subtilis.";
RL   Nucleic Acids Res. 28:4317-4331(2000).
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}.
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DR   EMBL; BA000004; BAB03772.1; -; Genomic_DNA.
DR   PIR; E83656; E83656.
DR   RefSeq; WP_010896237.1; NC_002570.2.
DR   AlphaFoldDB; Q9KGK8; -.
DR   SMR; Q9KGK8; -.
DR   STRING; 272558.10172665; -.
DR   EnsemblBacteria; BAB03772; BAB03772; BAB03772.
DR   KEGG; bha:BH0053; -.
DR   eggNOG; COG0073; Bacteria.
DR   eggNOG; COG0143; Bacteria.
DR   HOGENOM; CLU_009710_9_4_9; -.
DR   OMA; SDMHGTP; -.
DR   OrthoDB; 761140at2; -.
DR   Proteomes; UP000001258; 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; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR041872; Anticodon_Met.
DR   InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
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; PF08264; Anticodon_1; 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; PS00178; AA_TRNA_LIGASE_I; 1.
DR   PROSITE; PS50886; TRBD; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome; RNA-binding;
KW   tRNA-binding.
FT   CHAIN           1..660
FT                   /note="Methionine--tRNA ligase"
FT                   /id="PRO_0000139209"
FT   DOMAIN          560..660
FT                   /note="tRNA-binding"
FT   REGION          535..554
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           15..25
FT                   /note="'HIGH' region"
FT   MOTIF           311..315
FT                   /note="'KMSKS' region"
FT   BINDING         314
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   660 AA;  75192 MW;  EC3408645728A536 CRC64;
     MSKEQKTFYL TTPIYYPSDK LHIGHAYTTV AGDAMARYKR LRGYNVMYLT GTDEHGQKIE
     QKAEAKGLTP KQFVDEIVSG IQDLWKKLDI SYDDFIRTTE ERHIKVVQQI FEQLLDQGDI
     YLGDYEGWYS IPDETFYTET QLVDKEYDAD GNLIGGKSPD SGHPVEKVRE QSYFFRMSKY
     ADRLLQFYEE NPQFIQPESR KNEMINNFIK PGLEDLAVSR TSFTWGVPVP RDPKHVVYVW
     IDALSNYITA LGYGSDQQEK YENYWPADVH LVGKEIVRFH TIYWPIMLMA LDLPLPKKVF
     GHGWLLMKDG KMSKSKGNVV DPVPLIDRYG LDALRYYLLR EVPFGSDGVF TPEAFVERVN
     YDLANDLGNL LNRTVAMIEK YFDGKIPSYV KDGTPFDADL VELVYSTVKK VEDAMEEMEF
     SIALTAIGQL ISRTNKYIDE TQPWVLAKDE SKREQLGAAM YHLAESIRYV SVLLQPFMTK
     APQKIWEQLG IDSSLTTWES LETFGQIPGN TNVQKGQPLF PRLDVEEEVA HIKSLMGGSK
     KPEEAPKDEK EESDEITIDD FSKVELRIAE VIDAEPVKKA DRLLKIQLDL GYEKRQVVSG
     IAKYYSPSDL IGKKVICVTN LKPVKLRGEL SQGMILAGSE GDQLRLATVD GALPNGSLVK