ID   SYM_BLOPB               Reviewed;         555 AA.
AC   Q492J8;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 39.
DE   RecName: Full=Methionyl-tRNA synthetase;
DE            EC=6.1.1.10;
DE   AltName: Full=Methionine--tRNA ligase;
DE            Short=MetRS;
GN   Name=metG; OrderedLocusNames=BPEN_486;
OS   Blochmannia pennsylvanicus (strain BPEN).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; ant endosymbionts; Candidatus Blochmannia.
OX   NCBI_TaxID=291272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16077009; DOI=10.1101/gr.3771305;
RA   Degnan P.H., Lazarus A.B., Wernegreen J.J.;
RT   "Genome sequence of Blochmannia pennsylvanicus indicates parallel
RT   evolutionary trends among bacterial mutualists of insects.";
RL   Genome Res. 15:1023-1033(2005).
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   -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family. MetG type 1 subfamily.
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DR   EMBL; CP000016; AAZ41101.1; -; Genomic_DNA.
DR   RefSeq; YP_277978.1; -.
DR   GeneID; 3562993; -.
DR   GenomeReviews; CP000016_GR; BPEN_486.
DR   KEGG; bpn:BPEN_486; -.
DR   HOGENOM; Q492J8; -.
DR   OMA; Q492J8; DFSWREF.
DR   BioCyc; CBLO291272:BPEN_486-MON; -.
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:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006431; P:methionyl-tRNA aminoacylation; IEA:HAMAP.
DR   HAMAP; MF_00098; -; 1.
DR   InterPro; IPR015413; aa-tRNA-synt_I.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002304; Met-tRNA-synth_Ia.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR014758; tRNA-synt_met_N.
DR   Gene3D; G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1.
DR   Pfam; PF09334; tRNA-synt_1g; 1.
DR   PRINTS; PR01041; TRNASYNTHMET.
DR   TIGRFAMs; TIGR00398; metG; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Metal-binding; Nucleotide-binding; Protein biosynthesis; Zinc.
FT   CHAIN         1    555       Methionyl-tRNA synthetase.
FT                                /FTId=PRO_0000331784.
FT   MOTIF        13     23       "HIGH" region.
FT   MOTIF       330    334       "KMSKS" region.
FT   METAL       144    144       Zinc (By similarity).
FT   METAL       147    147       Zinc (By similarity).
FT   METAL       157    157       Zinc (By similarity).
FT   METAL       160    160       Zinc (By similarity).
FT   BINDING     333    333       ATP (By similarity).
SQ   SEQUENCE   555 AA;  64541 MW;  6A7A4215AAF8BB56 CRC64;
     MTTKKMLVTC ALPYANGSLH IGHMLEHIQA DIWVRYQRMQ GNCVYFICAD DAHGTAIMLK
     SQQLNIAPEQ MIAQIRQEHQ RDCYKFGISY DNYYSTHSDE TRELLHDIYS RLNTRGFIKS
     KFISQLYDSK KNMFLPDRFV KGICPKCKKD DQYGDNCAAC GTIYTSLELI NPKSVISGTS
     PIIRKSEHLF FDLPAFTDTL RTWIRSGSIQ KEVANKVEEW FKLGLKKWDI SRDAPYFGFK
     IPNSSEKYFY VWMDAPVGYM GTFKNLCKKN KNISFNDFWG SNSKTDLYHF IGKDIIYFHC
     LFWPAVLSGS QFRKPTNIFV HGHVTLNGSK ISKSKGTCIN VSTYLSCLNP DYLRYYYATK
     LSSHANDIDL NLSDFITRVN SDIINKILNL ASRNSGFIHQ YYNGHLSNTL THPLIYNMFI
     ESRHYIGKLF QKREFNYAMR EIMKLADEAN RYIDKHAPWH IAKKIDRRQE ALSIYSMGIQ
     LFRVLMIYLK PVLPKLANYS ECFLNTRLTW GSLSAPLSNH RINKFKIIFS RIHPDQIASM
     TNKSQLHERL TDNNV
//