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Database: UniProt/TrEMBL
Entry: Q5WLX1_BACSK
LinkDB: Q5WLX1_BACSK
Original site: Q5WLX1_BACSK 
ID   Q5WLX1_BACSK            Unreviewed;       655 AA.
AC   Q5WLX1;
DT   23-NOV-2004, integrated into UniProtKB/TrEMBL.
DT   23-NOV-2004, sequence version 1.
DT   01-MAY-2013, entry version 70.
DE   RecName: Full=Methionine--tRNA ligase;
DE            EC=6.1.1.10;
DE   AltName: Full=Methionyl-tRNA synthetase;
GN   Name=metS; Synonyms=metG; OrderedLocusNames=ABC0061;
OS   Bacillus clausii (strain KSM-K16).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=66692;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KSM-K16;
RA   Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y.,
RA   Kawai S., Ito S., Horikoshi K.;
RT   "The complete genome sequence of the alkaliphilic Bacillus clausii
RT   KSM-K16.";
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Is required not only for elongation of protein synthesis
CC       but also for the initiation of all mRNA translation through
CC       initiator tRNA(fMet) aminoacylation (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + L-methionine + tRNA(Met) = AMP +
CC       diphosphate + L-methionyl-tRNA(Met).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Contains 1 tRNA-binding domain.
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DR   EMBL; AP006627; BAD62604.1; -; Genomic_DNA.
DR   RefSeq; YP_173565.1; NC_006582.1.
DR   ProteinModelPortal; Q5WLX1; -.
DR   STRING; 66692.ABC0061; -.
DR   EnsemblBacteria; BAD62604; BAD62604; ABC0061.
DR   GeneID; 3204439; -.
DR   KEGG; bcl:ABC0061; -.
DR   PATRIC; 18919262; VBIBacCla58185_0064.
DR   eggNOG; COG0143; -.
DR   HOGENOM; HOG000200401; -.
DR   KO; K01874; -.
DR   OMA; RINYDLA; -.
DR   ProtClustDB; PRK12267; -.
DR   BioCyc; BCLA66692:GHMP-62-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0004825; F:methionine-tRNA ligase activity; IEA:HAMAP.
DR   GO; GO:0000049; F:tRNA binding; IEA:HAMAP.
DR   GO; GO:0006431; P:methionyl-tRNA aminoacylation; IEA:HAMAP.
DR   Gene3D; 2.40.50.140; -; 1.
DR   Gene3D; 3.40.50.620; -; 2.
DR   HAMAP; MF_01228; Met_tRNA_synth_type2; 1; -.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR004495; Met-tRNA-synth_Ia_bsu_C.
DR   InterPro; IPR014758; Met-tRNA_synth.
DR   InterPro; IPR023457; Met-tRNA_synth_2.
DR   InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
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_1a_anticodon-bd.
DR   InterPro; IPR013155; V/L/I-tRNA-synth_anticodon-bd.
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; SSF50249; Nucleic_acid_OB; 1.
DR   SUPFAM; SSF47323; tRNAsyn_1a_bind; 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; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Protein biosynthesis; RNA-binding;
KW   tRNA-binding.
FT   DOMAIN      555    655       tRNA-binding (By similarity).
FT   MOTIF        13     23       "HIGH" region (By similarity).
FT   MOTIF       309    313       "KMSKS" region (By similarity).
FT   METAL       128    128       Zinc (By similarity).
FT   METAL       161    161       Zinc (By similarity).
SQ   SEQUENCE   655 AA;  74168 MW;  B1B794E496B5BC58 CRC64;
     MSEKTFYITT PIYYPSGKLH IGHTYTTVAG DAMARYKRLR GYDVRYLTGT DEHGQKIEQK
     AKEKGISPLE YTNEMVKPIK ELWKKLDISH DDFIRTTEKR HTNMVEKIFE QLVEQGDIYL
     GEYEGWYCVS DETFYGEREL VDPIKDESGN IIGGKSPDSG HPVEKVREKS YFFRMSKYAD
     RLLAFYEENP DFIQPASRKN EMINNFIKPG LQDLAVSRTS FTWGVKVPSN PKHVVYVWID
     ALTNYITALG YGTADDTLYQ KYWPADVHLV GKDILRFHTI YWPIMLMALD LPLPKKVFGH
     GWFLTKDGKM SKSKGNVVDP APLIDHFGLD AIRYYLLREV PFGADGVFTP EAFVERVNYD
     LANDLGNLLN RTVAMINKYF NGEIPAYVKS ASPFDEDLLD LVQATITKVE DAMEEMEFSI
     ALAAIWQLVS RTNKYIDETQ PWMLAKEEDN RELLGSVMYH LAESLRIISV LIRPFMTRTP
     AKIWAQLGID ESLAGWESIR VFGQLPAGTK VSKGEPVFPR LDVEKEVDYI VELMGGKADP
     EPEEIEDENE ITIDDFSKVE LKVAEVTAAE PVEGADRLLK IQLDLGTETR QVVSGIAKYY
     APSDLVGKKV ICVTNLKPVK LRGELSQGMI LAGSKGKKLQ LATVDGDLPN GAQVK
//
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