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Database: UniProt/SWISS-PROT
Entry: RLMN_BACAH
LinkDB: RLMN_BACAH
Original site: RLMN_BACAH 
ID   RLMN_BACAH              Reviewed;         362 AA.
AC   A0RHN7;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   01-OCT-2014, entry version 56.
DE   RecName: Full=Probable dual-specificity RNA methyltransferase RlmN {ECO:0000255|HAMAP-Rule:MF_01849};
DE            EC=2.1.1.- {ECO:0000255|HAMAP-Rule:MF_01849};
DE            EC=2.1.1.192 {ECO:0000255|HAMAP-Rule:MF_01849};
DE   AltName: Full=23S rRNA (adenine(2503)-C(2))-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01849};
DE   AltName: Full=23S rRNA m2A2503 methyltransferase {ECO:0000255|HAMAP-Rule:MF_01849};
DE   AltName: Full=Ribosomal RNA large subunit methyltransferase N {ECO:0000255|HAMAP-Rule:MF_01849};
DE   AltName: Full=tRNA (adenine(37)-C(2))-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01849};
DE   AltName: Full=tRNA m2A37 methyltransferase {ECO:0000255|HAMAP-Rule:MF_01849};
GN   Name=rlmN {ECO:0000255|HAMAP-Rule:MF_01849};
GN   OrderedLocusNames=BALH_3495;
OS   Bacillus thuringiensis (strain Al Hakam).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=412694;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Al Hakam;
RX   PubMed=17337577; DOI=10.1128/JB.00241-07;
RA   Challacombe J.F., Altherr M.R., Xie G., Bhotika S.S., Brown N.,
RA   Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O.,
RA   Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T.,
RA   Goodwin L.A., Green L.D., Han C.S., Hill K.K., Hitchcock P.,
RA   Jackson P.J., Keim P., Kewalramani A.R., Longmire J., Lucas S.,
RA   Malfatti S., Martinez D., McMurry K., Meincke L.J., Misra M.,
RA   Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B.,
RA   Reilly L.P., Richardson P., Robinson D.L., Saunders E., Tapia R.,
RA   Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O.,
RA   Wills P.L., Gilna P., Brettin T.S.;
RT   "The complete genome sequence of Bacillus thuringiensis Al Hakam.";
RL   J. Bacteriol. 189:3680-3681(2007).
CC   -!- FUNCTION: Specifically methylates position 2 of adenine 2503 in
CC       23S rRNA and position 2 of adenine 37 in tRNAs.
CC       {ECO:0000255|HAMAP-Rule:MF_01849}.
CC   -!- CATALYTIC ACTIVITY: 2 S-adenosyl-L-methionine + adenine(2503) in
CC       23S rRNA = S-adenosyl-L-homocysteine + L-methionine + 5'-
CC       deoxyadenosine + 2-methyladenine(2503) in 23S rRNA.
CC       {ECO:0000255|HAMAP-Rule:MF_01849}.
CC   -!- CATALYTIC ACTIVITY: 2 S-adenosyl-L-methionine + adenine(37) in
CC       tRNA = S-adenosyl-L-homocysteine + L-methionine + 5'-
CC       deoxyadenosine + 2-methyladenine(37) in tRNA. {ECO:0000255|HAMAP-
CC       Rule:MF_01849}.
CC   -!- COFACTOR: Binds 1 4Fe-4S cluster. The cluster is coordinated with
CC       3 cysteines and an exchangeable S-adenosyl-L-methionine.
CC       {ECO:0000255|HAMAP-Rule:MF_01849}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01849}.
CC   -!- MISCELLANEOUS: Reaction proceeds by a ping-pong mechanism
CC       involving intermediate methylation of a conserved cysteine
CC       residue. {ECO:0000255|HAMAP-Rule:MF_01849}.
CC   -!- SIMILARITY: Belongs to the radical SAM superfamily. RlmN family.
CC       {ECO:0000255|HAMAP-Rule:MF_01849}.
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DR   EMBL; CP000485; ABK86730.1; -; Genomic_DNA.
DR   RefSeq; YP_896237.1; NC_008600.1.
DR   ProteinModelPortal; A0RHN7; -.
DR   STRING; 412694.BALH_3495; -.
DR   EnsemblBacteria; ABK86730; ABK86730; BALH_3495.
DR   GeneID; 4542707; -.
DR   KEGG; btl:BALH_3495; -.
DR   PATRIC; 18999741; VBIBacThu63319_3870.
DR   eggNOG; COG0820; -.
DR   HOGENOM; HOG000217991; -.
DR   KO; K06941; -.
DR   OMA; PEAPYAK; -.
DR   OrthoDB; EOG6DJZ2N; -.
DR   BioCyc; BTHU412694:GH1W-3423-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0070040; F:rRNA (adenine-C2-)-methyltransferase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0002935; F:tRNA (adenine-C2-)-methyltransferase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0070475; P:rRNA base methylation; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_01849; RNA_methyltr_RlmN; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR006638; Elp3/MiaB/NifB.
DR   InterPro; IPR027492; RNA_MTrfase_RlmN.
DR   InterPro; IPR004383; rRNA_lsu_MTrfase_RlmN/Cfr.
DR   InterPro; IPR007197; rSAM.
DR   PANTHER; PTHR30544; PTHR30544; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   PIRSF; PIRSF006004; CHP00048; 1.
DR   SMART; SM00729; Elp3; 1.
DR   TIGRFAMs; TIGR00048; TIGR00048; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Complete proteome; Cytoplasm; Disulfide bond; Iron;
KW   Iron-sulfur; Metal-binding; Methyltransferase; rRNA processing;
KW   S-adenosyl-L-methionine; Transferase; tRNA processing.
FT   CHAIN         1    362       Probable dual-specificity RNA
FT                                methyltransferase RlmN.
FT                                /FTId=PRO_0000350037.
FT   REGION      175    176       S-adenosyl-L-methionine binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01849}.
FT   REGION      230    232       S-adenosyl-L-methionine binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01849}.
FT   ACT_SITE    105    105       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01849}.
FT   ACT_SITE    349    349       S-methylcysteine intermediate.
FT                                {ECO:0000255|HAMAP-Rule:MF_01849}.
FT   METAL       125    125       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000255|HAMAP-Rule:MF_01849}.
FT   METAL       129    129       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000255|HAMAP-Rule:MF_01849}.
FT   METAL       132    132       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000255|HAMAP-Rule:MF_01849}.
FT   BINDING     207    207       S-adenosyl-L-methionine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01849}.
FT   BINDING     306    306       S-adenosyl-L-methionine; via amide
FT                                nitrogen and carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01849}.
FT   DISULFID    118    349       (transient). {ECO:0000255|HAMAP-
FT                                Rule:MF_01849}.
SQ   SEQUENCE   362 AA;  41553 MW;  5D1D0D3E937245BD CRC64;
     METTVRKQKK NLETKKPSIY SLQLHEMQDW LKEQGEPKFR AGQIFDWLYK KRVKNYEDMS
     NLSKGLREKL SNSFDITTLN TLVKQTSSDG TIKFLFQLYD GYSIETVLMR HEYGNSICVT
     TQVGCRIGCT FCASTLGGLK RNLEAGEIVA QVVEVQRALD ESEERVSSLV VMGIGEPFDN
     YDNLMGFLRI INHEKGLHIG ARHMTVSTSG IIPKIYKFAE EDLQINFAIS LHAPNSELRS
     KLMPINRAYK LPDLMEAIKY YVNRTGRRIT FEYGLFGGEN DQVEHAEELA ALLKGVKCHV
     NLIPVNYVPE RDYVRTPREQ IFLFEKTLKD RGVNVTIRRE QGHDIDAACG QLRAKERKEE
     TR
//
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