ID   HEMK_RICBR              Reviewed;         556 AA.
AC   Q1RH40;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 22.
DE   RecName: Full=Bifunctional methyltransferase;
DE   Includes:
DE     RecName: Full=HemK protein homolog;
DE              EC=2.1.1.-;
DE   Includes:
DE     RecName: Full=tRNA (guanine-N(7)-)-methyltransferase;
DE              EC=2.1.1.33;
DE     AltName: Full=tRNA(m7G46)-methyltransferase;
GN   Name=hemK; OrderedLocusNames=RBE_1243;
OS   Rickettsia bellii (strain RML369-C).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia.
OX   NCBI_TaxID=336407;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA   Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA   Fournier P.-E., Claverie J.-M., Raoult D.;
RT   "Genome sequence of Rickettsia bellii illuminates the role of amoebae
RT   in gene exchanges between intracellular pathogens.";
RL   PLoS Genet. 2:733-744(2006).
CC   -!- FUNCTION: Catalyzes the formation of N(7)-methylguanine at
CC       position 46 (m7G46) in tRNA (By similarity).
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + tRNA = S-adenosyl-L-
CC       homocysteine + tRNA containing N(7)-methylguanine.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the hemK family.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the
CC       methyltransferase superfamily. TrmB family.
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DR   EMBL; CP000087; ABE05324.1; -; Genomic_DNA.
DR   RefSeq; YP_538413.1; -.
DR   GeneID; 3996337; -.
DR   GenomeReviews; CP000087_GR; RBE_1243.
DR   KEGG; rbe:RBE_1243; -.
DR   HOGENOM; Q1RH40; -.
DR   OMA; Q1RH40; IGVEVYL.
DR   BioCyc; RBEL336407:RBE_1243-MON; -.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008276; F:protein methyltransferase activity; IEA:InterPro.
DR   GO; GO:0008176; F:tRNA (guanine-N7-)-methyltransferase activity; IEA:HAMAP.
DR   GO; GO:0006479; P:protein amino acid methylation; IEA:InterPro.
DR   GO; GO:0006400; P:tRNA modification; IEA:HAMAP.
DR   HAMAP; MF_01057; fused; 1.
DR   InterPro; IPR004556; Modification_methylase_HemK.
DR   InterPro; IPR002052; N6_adenine_Mtase_CS.
DR   InterPro; IPR019874; Release_fac_Glu-N5_MeTfrase.
DR   InterPro; IPR007848; Small_mtfrase.
DR   InterPro; IPR003358; tRNA_(Gua-N-7)_MeTrfase.
DR   Pfam; PF02390; Methyltransf_4; 1.
DR   Pfam; PF05175; MTS; 1.
DR   TIGRFAMs; TIGR00536; hemK_fam; 1.
DR   TIGRFAMs; TIGR03534; RF_mod_HemK; 1.
DR   PROSITE; PS00092; N6_MTASE; UNKNOWN_1.
PE   3: Inferred from homology;
KW   Complete proteome; Methyltransferase; S-adenosyl-L-methionine;
KW   Transferase; tRNA processing.
FT   CHAIN         1    556       Bifunctional methyltransferase.
FT                                /FTId=PRO_0000288434.
FT   REGION      348    399       Insert.
FT   BINDING     403    403       S-adenosyl-L-methionine (By similarity).
FT   BINDING     428    428       S-adenosyl-L-methionine (By similarity).
FT   BINDING     455    455       S-adenosyl-L-methionine (By similarity).
FT   BINDING     477    477       S-adenosyl-L-methionine (By similarity).
FT   BINDING     481    481       Substrate (By similarity).
FT   BINDING     513    513       Substrate (Potential).
SQ   SEQUENCE   556 AA;  63993 MW;  EA14666271E6FE1E CRC64;
     MQYSIQKFLN EGAYKLQHIG INNPKLEARI LLQHAINKPY EYLLANPEKQ LNQLEIEAVE
     KVLERRLKHE PIAYILGTKE FYSREFIVNK HVLIPRNDTE ILIDVVLQYH SQHSLCHSSN
     GGNPDKKQLD SVVKPRNNIK SSNILELGTG SGCISISLLL ELPNSQITAT DISIDAIEVA
     KSNAIKHDVT DRLQIIHSNW FENIGKQKFD LIVSNPPYIS INEKPEMAIE TINYEPSIAL
     FAEEDGLLSY KIIAENAKKF LKQNGKIILE IGYKQADQVS QIFLDHGYVI DNIHQDLQSH
     NRVIEISLIQ LNRSYARRIG KSLSGIQQNL LDNELPKYLF SKEKLIGKNY NSCKIKSNYT
     KFNLEKSKES VSRGAERIKI REHLRTYKED VANFSSSTSI FLEIGFGMGE HFINQAKMNP
     DKLFIGVEVY LNGVANVLKL AEEQNITNFL LFPNNLDFIL HDLPNNSLDR IYILFPDPWI
     KNRQKKKRIL NKERLTILQT KLKNKGSLIF TSDIENYFEE VVELIKQNGN FQITNEDNYS
     KPHDNYIITK IPPKSY
//