ID   SYM_BORBU               Reviewed;         734 AA.
AC   Q44951;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 2.
DT   16-JUN-2009, entry version 72.
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=BB_0587;
OS   Borrelia burgdorferi (Lyme disease spirochete).
OC   Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Borrelia;
OC   Borrelia burgdorferi group.
OX   NCBI_TaxID=139;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35210 / B31 / CIP 102532 / DSM 4680;
RX   MEDLINE=98065943; PubMed=9403685; DOI=10.1038/37551;
RA   Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA   Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K.,
RA   Gwinn M.L., Dougherty B.A., Tomb J.-F., Fleischmann R.D.,
RA   Richardson D.L., Peterson J.D., Kerlavage A.R., Quackenbush J.,
RA   Salzberg S.L., Hanson M., van Vugt R., Palmer N., Adams M.D.,
RA   Gocayne J.D., Weidman J.F., Utterback T.R., Watthey L., McDonald L.A.,
RA   Artiach P., Bowman C., Garland S.A., Fujii C., Cotton M.D., Horst K.,
RA   Roberts K.M., Hatch B., Smith H.O., Venter J.C.;
RT   "Genomic sequence of a Lyme disease spirochaete, Borrelia
RT   burgdorferi.";
RL   Nature 390:580-586(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 246-360.
RC   STRAIN=212;
RX   MEDLINE=95111614; PubMed=7812434;
RA   Ojaimi C., Davidson B.E., Saint-Girons I., Old I.G.;
RT   "Conservation of gene arrangement and an unusual organization of rRNA
RT   genes in the linear chromosomes of the Lyme disease spirochaetes
RT   Borrelia burgdorferi, B. garinii and B. afzelii.";
RL   Microbiology 140:2931-2940(1994).
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.
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; AE000783; AAB91520.1; -; Genomic_DNA.
DR   EMBL; L32146; AAC41404.1; -; Genomic_DNA.
DR   PIR; B70173; B70173.
DR   RefSeq; NP_212721.1; -.
DR   HSSP; Q9V011; 1MKH.
DR   GeneID; 1195434; -.
DR   GenomeReviews; AE000783_GR; BB_0587.
DR   KEGG; bbu:BB0587; -.
DR   NMPDR; fig|224326.1.peg.971; -.
DR   TIGR; BB_0587; -.
DR   HOGENOM; Q44951; -.
DR   OMA; Q44951; SAYQPEQ.
DR   BioCyc; BBUR224326:BB_0587-MON; -.
DR   BRENDA; 6.1.1.10; 142596.
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    734       Methionyl-tRNA synthetase.
FT                                /FTId=PRO_0000139107.
FT   DOMAIN      570    675       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   734 AA;  85215 MW;  585508811CED9CFB CRC64;
     MKKMNLVTAA LPYVNNIPHL GNLVQVLSAD AFARYSKMSG IETLYVCGTD EYGTATETKA
     LIENTTPLEL CNKYYEIHKS IYKWFNIEFD IFGRTTNKNH QDIVQNFFLQ LEKNGYIKER
     ETEQFYCNKD SMFLADRYVI GECPECQSMA KGDQCDNCSK LLNPTDLINP KCIICKNKPI
     LKKTNHLYLD LPKIKTKLEK WIKNPDTSKN WNTNALKMTK AFLRDGLKER AITRDLKWGI
     PVPKKGFENK VFYVWFDAPI GYISITKNII KNWESWWKNN DQVNLVQFIG KDNILFHTII
     FPCIEIGSEE NWTILNQLSS SEYLNYENLK FSKSEGTGIF GNDAITTGIP SDIWRFYIYY
     NRPEKSDFQF MWQDLMERVN TELIDNFSNL VNRVLTFQRK FFGDVIETIE IQNKFWKQIT
     PKYNKILNLF KKTELKSALK EILKISSLGN KIFQDNEPWK RKNNSPQETK ELISNLIYLI
     RDLSILMMPF IPETSKKIQQ FFGNSYQFST KILGTKSGIK KIEFTEILFN KLEQKKINNL
     KLKYSGDKNM KENEQAENLP IAKEQPENLF REKVLLRVVK INKIERNPEA KNLFILKLDD
     GTNKDKQIVS GLEGYYTEEE LLGKHIIIVD NLKPAKFRGI KSEGMLIAAE DKNKNFKVII
     VEDSIQNPIA GERIILENDQ NKDLACPPKI DINKFLKANI VAENGELKIN GINLILENSK
     NKILSKDIPN GTVC
//