ID   SYM_BORAP               Reviewed;         724 AA.
AC   Q0SMS1;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-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=BAPKO_0618;
OS   Borrelia afzelii (strain PKo).
OC   Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Borrelia;
OC   Borrelia burgdorferi group.
OX   NCBI_TaxID=390236;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16914037; DOI=10.1186/1471-2164-7-211;
RA   Gloeckner G., Schulte-Spechtel U., Schilhabel M., Felder M.,
RA   Suehnel J., Wilske B., Platzer M.;
RT   "Comparative genome analysis: selection pressure on the Borrelia vls
RT   cassettes is essential for infectivity.";
RL   BMC Genomics 7:211-211(2006).
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; CP000395; ABH01857.1; -; Genomic_DNA.
DR   RefSeq; YP_710033.1; -.
DR   GeneID; 4227921; -.
DR   GenomeReviews; CP000395_GR; BAPKO_0618.
DR   KEGG; baf:BAPKO_0618; -.
DR   HOGENOM; Q0SMS1; -.
DR   OMA; Q0SMS1; SAYQPEQ.
DR   BioCyc; BAFZ390236:BAPKO_0618-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: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    724       Methionyl-tRNA synthetase.
FT                                /FTId=PRO_0000331786.
FT   DOMAIN      560    665       tRNA-binding.
FT   MOTIF        12     22       "HIGH" region.
FT   MOTIF       330    334       "KMSKS" region.
FT   METAL       143    143       Zinc (By similarity).
FT   METAL       146    146       Zinc (By similarity).
FT   METAL       155    155       Zinc (By similarity).
FT   METAL       158    158       Zinc (By similarity).
FT   BINDING     333    333       ATP (By similarity).
SQ   SEQUENCE   724 AA;  84391 MW;  3D8839B7529646D9 CRC64;
     MKKMNLITAA LPYVNNIPHL GNLVQVLSAD AFARYSKMSG IETLYICGTD EYGTATETKA
     LIEKTTPLEL CNKYYEIHKS IYKWFNIEFD IFGRTTNKHH QETVQNFFLK LEKNGYIKER
     ETEQFFCNKD LIFLADRYVI GECPECQSMA KGDQCDNCSK LLNPTDLINP KCIICKNKPI
     LKKTNHLYID LPKIKTKLEK WIKNPTTSKN WNTNALKMTN AFLRDGLKER AITRDLKWGI
     PVPKKGYENK VFYVWFDAPI GYISITKNIV KNWESWWKNN KQVNLVQFIG KDNILFHTIM
     FPCIKIGSKE NWTTLNQLSS SEYLNYENLK FSKSEGTGIF GNDVITTGIP SDVWRFYIYY
     NRPEKSDFQF IWQDLMERVN TELIDNFSNL VNRVLTFQKK FFGDVIETIE IQHKFWEQIT
     PKYNKILNLF KNTELKSALK EILKISSFGN KIFQDNEPWK RKESSPQEIK ELILNLIYLI
     RDLSILMMPF IPETSKKIQQ FFGNSYQFST KILGTKSGIK KIEFVEILFN KLEQKKINDL
     RLKYSGEKNM KEKEQPENLF REKVLLRVVK INKIERNPEA KNLFILKLDD GTNKDKQIVS
     SLEGYYTEEE LLGKHIIIVD NLKPAKFRGI KSEGMLIAAE DKNKNFKIII VEDSIKNPIA
     GERIILENDQ NKDLTCPPKI DINKFSKANI ITENGELKIN GINLILEHSK NKILSKDIPN
     GIVC
//