ID RLMN_THIDA Reviewed; 372 AA.
AC Q3SL73;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 01-MAY-2013, entry version 58.
DE RecName: Full=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=Tbd_0591;
OS Thiobacillus denitrificans (strain ATCC 25259).
OC Bacteria; Proteobacteria; Betaproteobacteria; Hydrogenophilales;
OC Hydrogenophilaceae; Thiobacillus.
OX NCBI_TaxID=292415;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25259;
RX PubMed=16452431; DOI=10.1128/JB.188.4.1473-1488.2006;
RA Beller H.R., Chain P.S., Letain T.E., Chakicherla A., Larimer F.W.,
RA Richardson P.M., Coleman M.A., Wood A.P., Kelly D.P.;
RT "The genome sequence of the obligately chemolithoautotrophic,
RT facultatively anaerobic bacterium Thiobacillus denitrificans.";
RL J. Bacteriol. 188:1473-1488(2006).
CC -!- FUNCTION: Specifically methylates position 2 of adenine 2503 in
CC 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503
CC modification seems to play a crucial role in the proofreading step
CC occurring at the peptidyl transferase center and thus would serve
CC to optimize ribosomal fidelity (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; CP000116; AAZ96544.1; -; Genomic_DNA.
DR RefSeq; YP_314349.1; NC_007404.1.
DR ProteinModelPortal; Q3SL73; -.
DR STRING; 292415.Tbd_0591; -.
DR EnsemblBacteria; AAZ96544; AAZ96544; Tbd_0591.
DR GeneID; 3673701; -.
DR KEGG; tbd:Tbd_0591; -.
DR PATRIC; 23967339; VBIThiDen82923_0591.
DR eggNOG; COG0820; -.
DR HOGENOM; HOG000217992; -.
DR KO; K06941; -.
DR OMA; MACDFCA; -.
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; IPR004383; rRNA_lsu_MTrfase_RlmN.
DR InterPro; IPR007197; rSAM.
DR Pfam; PF04055; Radical_SAM; 1.
DR PIRSF; PIRSF006004; CHP00048; 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 1 372 Dual-specificity RNA methyltransferase
FT RlmN.
FT /FTId=PRO_0000350505.
FT REGION 175 176 S-adenosyl-L-methionine binding (By
FT similarity).
FT REGION 229 231 S-adenosyl-L-methionine binding (By
FT similarity).
FT ACT_SITE 91 91 Proton acceptor (Potential).
FT ACT_SITE 349 349 S-methylcysteine intermediate (By
FT similarity).
FT METAL 111 111 Iron-sulfur (4Fe-4S-S-AdoMet) (By
FT similarity).
FT METAL 115 115 Iron-sulfur (4Fe-4S-S-AdoMet) (By
FT similarity).
FT METAL 118 118 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 104 349 (transient) (By similarity).
SQ SEQUENCE 372 AA; 41198 MW; 50FE5FA2C75E60BB CRC64;
MPQNLLDFDL AGLTAWFGER GEKPFRARQV FHWIHQAGVT DFAQMTDIAK SLREKLQNEA
VVQAPAINFA HLSADGTRKW LFDVGVGNGI ETVFIPEDDR GTLCVSSQVG CALECTFCST
GRQGFNRNLT VAEIVGQLWV AQHSLKREPN RTASDHGAGE IAERPVTNVV MMGMGEPLAN
FENVVTALGV MLDDHAYGLS RRRVTVSTSG LVPAMDRLAE RCPVALAVSL HAPNDALRDQ
IVPINRKYPL AELMAACRRY LVHAPRDFIT FEYVMLAGVN DQPEHARQLI ALTRDVPCKF
NLIPFNPFPD SGYEKPRAEA MRVFREILQD AGYVVTTRKT RGDDIDAACG QLAGRVADRS
GRVMKRVHRE AA
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