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-MAY-2013, entry version 50.
DE RecName: Full=Probable dual-specificity RNA methyltransferase RlmN;
DE EC=2.1.1.-;
DE EC=2.1.1.192;
DE AltName: Full=23S rRNA (adenine(2503)-C(2))-methyltransferase;
DE AltName: Full=23S rRNA m2A2503 methyltransferase;
DE AltName: Full=Ribosomal RNA large subunit methyltransferase N;
DE AltName: Full=tRNA (adenine(37)-C(2))-methyltransferase;
DE AltName: Full=tRNA m2A37 methyltransferase;
GN Name=rlmN; 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 (By similarity).
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 -!- 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.
CC -!- COFACTOR: Binds 1 4Fe-4S cluster. The cluster is coordinated with
CC 3 cysteines and an exchangeable S-adenosyl-L-methionine (By
CC similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (Potential).
CC -!- MISCELLANEOUS: Reaction proceeds by a ping-pong mechanism
CC involving intermediate methylation of a conserved cysteine residue
CC (By similarity).
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. RlmN family.
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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; MACDFCA; -.
DR ProtClustDB; PRK14455; -.
DR BioCyc; BTHU412694:GH1W-3311-MONOMER; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:HAMAP.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070040; F:rRNA (adenine-C2-)-methyltransferase activity; IEA:HAMAP.
DR GO; GO:0019843; F:rRNA binding; IEA:HAMAP.
DR GO; GO:0002935; F:tRNA (adenine-C2-)-methyltransferase activity; IEA:HAMAP.
DR GO; GO:0000049; F:tRNA binding; IEA:HAMAP.
DR GO; GO:0070475; P:rRNA base methylation; IEA: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; IPR004383; rRNA_lsu_MTrfase_RlmN.
DR InterPro; IPR007197; rSAM.
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 (By
FT similarity).
FT REGION 230 232 S-adenosyl-L-methionine binding (By
FT similarity).
FT ACT_SITE 105 105 Proton acceptor (Potential).
FT ACT_SITE 349 349 S-methylcysteine intermediate (By
FT similarity).
FT METAL 125 125 Iron-sulfur (4Fe-4S-S-AdoMet) (By
FT similarity).
FT METAL 129 129 Iron-sulfur (4Fe-4S-S-AdoMet) (By
FT similarity).
FT METAL 132 132 Iron-sulfur (4Fe-4S-S-AdoMet) (By
FT similarity).
FT BINDING 207 207 S-adenosyl-L-methionine (By similarity).
FT BINDING 306 306 S-adenosyl-L-methionine; via amide
FT nitrogen and carbonyl oxygen (By
FT similarity).
FT DISULFID 118 349 (transient) (By similarity).
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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