ID   SYM_ALHEH               Reviewed;         675 AA.
AC   Q0AAG6;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   16-JUN-2009, entry version 24.
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=Mlg_0817;
OS   Alkalilimnicola ehrlichei (strain MLHE-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Alkalilimnicola.
OX   NCBI_TaxID=187272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Sims D., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Oremland R.S., Hoeft S.E., Switzer-Blum J., Kulp T.,
RA   King G., Tabita R., Witte B., Santini J.M., Basu P., Hollibaugh J.T.,
RA   Xie G., Stolz J.F., Richardson P.;
RT   "Complete sequence of Alkalilimnicola ehrilichei MLHE-1.";
RL   Submitted (AUG-2006) 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   -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family. MetG type 1 subfamily.
CC   -!- SIMILARITY: Contains 1 tRNA-binding domain.
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DR   EMBL; CP000453; ABI56171.1; -; Genomic_DNA.
DR   RefSeq; YP_741661.1; -.
DR   GeneID; 4270648; -.
DR   GenomeReviews; CP000453_GR; Mlg_0817.
DR   KEGG; aeh:Mlg_0817; -.
DR   HOGENOM; Q0AAG6; -.
DR   OMA; Q0AAG6; SAYQPEQ.
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:UniProtKB-KW.
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; IPR004495; Met-tRNA-synth_Ia_bsu_C.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR014758; tRNA-synt_met_N.
DR   InterPro; IPR002547; tRNA_bd.
DR   Gene3D; G3DSA:2.40.50.140; OB_NA_bd_sub; 1.
DR   Gene3D; G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1.
DR   Pfam; PF09334; tRNA-synt_1g; 1.
DR   Pfam; PF01588; tRNA_bind; 1.
DR   PRINTS; PR01041; TRNASYNTHMET.
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; Metal-binding; Nucleotide-binding; Protein biosynthesis;
KW   RNA-binding; tRNA-binding; Zinc.
FT   CHAIN         1    675       Methionyl-tRNA synthetase.
FT                                /FTId=PRO_0000331777.
FT   DOMAIN      574    675       tRNA-binding.
FT   MOTIF        12     22       "HIGH" region.
FT   MOTIF       328    332       "KMSKS" region.
FT   METAL       143    143       Zinc (By similarity).
FT   METAL       146    146       Zinc (By similarity).
FT   METAL       156    156       Zinc (By similarity).
FT   METAL       159    159       Zinc (By similarity).
FT   BINDING     331    331       ATP (By similarity).
SQ   SEQUENCE   675 AA;  76942 MW;  F7E4C82EEDE1A7AC CRC64;
     MTRKILVTSA LPYANGPIHL GHLVEYIQTD IWARFQRLRG HDCHYVCADD AHGTPIMLKA
     RERGITPEAL IAEVGEEHQR DFADFLIEFD NYHTTHSDEN RYFAELIYSR LNQAGHIDRK
     VIKQAYDPKL EMFLPDRYIK GECPRCGAED QYGDSCEACG ATYTPAELKN AVSVVSGERP
     VERESEHYFF RLQDFEAMLR EWASPEHLQA EVANKLAEWF KEGLRSWDIS RDAPYFGFRI
     PDTEDKYFYV WLDAPIGYMA SFKHLCERKG LDFDDWWGPD STAELYHFIG KDIIYFHALF
     WPAMLHGAGF RKPTEICAHG FLTVNGQKMS KSRGTFIMAR TWLDHLNPEY LRYYFAAKLS
     ASVHDLDLSL DDFTQRVNAD LVGKLVNIAS RCAGFIHKRF EGRLGETLDD PALYRQFTAA
     GEHIAELYEK REFSRAMREI MALADQANQY VDEQKPWVLA KQEDQADRVQ DICTQGLNLF
     RVLVVYLKPV LPRLAADAEA FLNLPEQCWA DAKTPLLDHG IRKFKPLMTR VDPDRVQAML
     EDSKKTLQPK GEPQAAEAGP LTSDPIAEQI EIGDFAKVDL RIARIEQAEH VEGADKLLRL
     QLDLGGETRQ VFAGIKQAYR PEDLEGRLTV MAANLKPRKM KFGVSEGMVL AAGPGGSDLY
     LLEPHQGAQP GMRVK
//