ID   F3YA05_MELPT            Unreviewed;       357 AA.
AC   F3YA05;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   18-APR-2012, entry version 7.
DE   RecName: Full=Ribosomal RNA large subunit methyltransferase N;
DE            EC=2.1.1.192;
DE   AltName: Full=23S rRNA (adenine(2503)-C(2))-methyltransferase;
DE   AltName: Full=23S rRNA m2A2503 methyltransferase;
GN   Name=rlmN;
OS   Melissococcus plutonius (strain ATCC 35311 / CIP 104052 / LMG 20360 /
OS   NCIMB 702443).
OC   Bacteria; Firmicutes; Lactobacillales; Enterococcaceae; Melissococcus.
OX   NCBI_TaxID=940190;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35311 / CIP 104052 / LMG 20360 / NCIMB 702443;
RX   PubMed=21622755; DOI=10.1128/JB.05151-11;
RA   Okumura K., Arai R., Okura M., Kirikae T., Takamatsu D., Osaki M.,
RA   Miyoshi-Akiyama T.;
RT   "Complete genome sequence of Melissococcus plutonius ATCC 35311.";
RL   J. Bacteriol. 193:4029-4030(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 35311;
RA   Okumura K., Arai R., Osaki M., Okura M., Kirikae T., Takamatsu D.,
RA   Akiyama T.;
RT   "Whole genome sequence of Melissococcus plutonius ATCC 35311.";
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Specifically methylates position 2 of adenine 2503 in
CC       23S rRNA (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   -!- 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 (By similarity).
CC   -!- SIMILARITY: Belongs to the radical SAM superfamily. RlmN family.
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DR   EMBL; AP012200; BAK21333.1; -; Genomic_DNA.
DR   RefSeq; YP_004456142.1; NC_015516.1.
DR   GeneID; 10595697; -.
DR   KEGG; mps:MPTP_0871; -.
DR   PATRIC; 54620483; VBIMelPlu182073_0862.
DR   KO; K06941; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0005506; F:iron ion binding; IEA:HAMAP.
DR   GO; GO:0070040; F:rRNA (adenine-C2-)-methyltransferase activity; IEA:EC.
DR   HAMAP; MF_01849; 23SrRNA_methyltr_N; 1; -.
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; Iron; Iron-sulfur;
KW   Metal-binding; Methyltransferase; rRNA processing;
KW   S-adenosyl-L-methionine; Transferase.
FT   METAL       117    117       Iron-sulfur (4Fe-4S-S-AdoMet) (By
FT                                similarity).
FT   METAL       121    121       Iron-sulfur (4Fe-4S-S-AdoMet) (By
FT                                similarity).
FT   METAL       124    124       Iron-sulfur (4Fe-4S-S-AdoMet) (By
FT                                similarity).
SQ   SEQUENCE   357 AA;  41257 MW;  DA5A183BC03A79B1 CRC64;
     MEKDIMQKQT IYGLTKEALV NWFLENGEKK FRANQVWEWL YIKRVESFED MTNLSKTLIS
     LLDQHFVIQV LRQTIIQEAK DGTVKYLFEL PDKNMIETVL MRQEYGLSVC VTTQVGCNMG
     CTFCASGLLK KNRNLTAGEI VAQIMMVQRY FDQRKLGERV SHVVVMGIGE PFDNYEQLMQ
     FIQIINDEKG LAIGARHLTV STCGLVPQIK KFAQTGLQVN LAISLHASNN QIRSSIMRIN
     HTFPIEKLMQ TIDEYIEQTN RRVTFEYIML QKVNDYPEHA QELADLLKDK KKLAYVNLIP
     YNPVNEHDQY CRSEKASVLK FYDILKKNGI NCVIRKEHGT DIDAACGQLR SKQLTKK
//