ID   SYM1_ACAM1              Reviewed;         558 AA.
AC   A8ZQ66;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   16-JUN-2009, entry version 13.
DE   RecName: Full=Methionyl-tRNA synthetase 1;
DE            EC=6.1.1.10;
DE   AltName: Full=Methionine--tRNA ligase 1;
DE            Short=MetRS 1;
GN   Name=metG1; OrderedLocusNames=AM1_F0085;
OS   Acaryochloris marina (strain MBIC 11017).
OG   Plasmid pREB6.
OC   Bacteria; Cyanobacteria; Acaryochloris.
OX   NCBI_TaxID=329726;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18252824; DOI=10.1073/pnas.0709772105;
RA   Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J.,
RA   Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D.,
RA   Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M.,
RA   Shimada Y., Taylor H.L., Tomo T., Tsuchiya T., Wang Z.T., Raymond J.,
RA   Mimuro M., Blankenship R.E., Touchman J.W.;
RT   "Niche adaptation and genome expansion in the chlorophyll d-producing
RT   cyanobacterium Acaryochloris marina.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008).
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; CP000843; ABW33099.1; -; Genomic_DNA.
DR   RefSeq; YP_001522389.1; -.
DR   GeneID; 5687006; -.
DR   GenomeReviews; CP000843_GR; AM1_F0085.
DR   KEGG; amr:AM1_F0085; -.
DR   OMA; A8ZQ66; YINGIKH.
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; FALSE_NEG.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Metal-binding; Nucleotide-binding; Plasmid;
KW   Protein biosynthesis; Zinc.
FT   CHAIN         1    558       Methionyl-tRNA synthetase 1.
FT                                /FTId=PRO_0000331770.
FT   MOTIF        10     20       "HIGH" region.
FT   MOTIF       332    336       "KMSKS" region.
FT   METAL       142    142       Zinc (By similarity).
FT   METAL       145    145       Zinc (By similarity).
FT   METAL       155    155       Zinc (By similarity).
FT   METAL       158    158       Zinc (By similarity).
FT   BINDING     335    335       ATP (By similarity).
SQ   SEQUENCE   558 AA;  64196 MW;  A6481D3ED2FF1293 CRC64;
     MRYLITSALP YINGIKHLGN LVGSMLPADI YARFLRQEGE EVLYICATDE HGTPAEIAAI
     DAGLEVAEFC AKQYHKQKEI YKRFGLSFDY FGRTSAPENH ELTQYFYQQL AKQNFIEERE
     ISQFYALDDQ RFLPDRYVTG TCPHCGYEQA RGDQCENCTK VLTPTELIKP RSTISGSTHL
     ELRTSRHLFL RLDKLSDEVR NWVDKQTQWS TLTKSIALKW LNEGLKSRCI TRDLVWGVPV
     PTEGFERKVF YVWFDAPIGY ISATKAWGDI TNNDWECWWK ESDDVHYTQF MAKDNLPFHT
     IMWPATILGS REPWKMVDYI KGFNWLNYYG GKFSTSSQRG VFLDQALEIA SADNWRYMLI
     ANAPESADSA FTWEQFQKQV NKELADNLGN FVNRILKFTA SRFGMTLPEG GTPGDAEAEL
     QVTCNELVEK LRKYLHNLEF RRATETLNAL WRTGNQYIDV RAPWVLFKTD QDETAMVIRT
     CVNLIRLYAI SSAPFIPHTT QALFDALQLT DVERRHTMTE ASDLTLLAAG RSFMVPAPLF
     QKIDDDLVAE LKAQYGGE
//