ID   F3YA05_MELPT            Unreviewed;       357 AA.
AC   F3YA05;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   28-NOV-2012, entry version 10.
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=MPTP_0871;
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 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 (By similarity).
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; 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   BioCyc; MPLU940190:GH20-1021-MONOMER; -.
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   GO; GO:0001510; P:RNA methylation; IEA:GOC.
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; Disulfide bond; Iron;
KW   Iron-sulfur; Metal-binding; Methyltransferase; rRNA processing;
KW   S-adenosyl-L-methionine; Transferase; tRNA processing.
FT   REGION      169    170       S-adenosyl-L-methionine binding (By
FT                                similarity).
FT   REGION      224    226       S-adenosyl-L-methionine binding (By
FT                                similarity).
FT   ACT_SITE     97     97       Proton acceptor (By similarity).
FT   ACT_SITE    346    346       S-methylcysteine intermediate (By
FT                                similarity).
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).
FT   BINDING     201    201       S-adenosyl-L-methionine (By similarity).
FT   BINDING     302    302       S-adenosyl-L-methionine; via amide
FT                                nitrogen and carbonyl oxygen (By
FT                                similarity).
FT   DISULFID    110    346       (transient) (By 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
//