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Database: UniProt/SWISS-PROT
Entry: RLMN_THIDA
LinkDB: RLMN_THIDA
Original site: RLMN_THIDA 
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-OCT-2014, entry version 64.
DE   RecName: Full=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=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. {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; 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; HEGSKFE; -.
DR   OrthoDB; EOG6DJZ2N; -.
DR   BioCyc; TDEN292415:GHWG-605-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; 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   TIGRFAMs; TIGR00048; TIGR00048; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Complete proteome; Cytoplasm; Disulfide bond; Iron;
KW   Iron-sulfur; Metal-binding; Methyltransferase; Reference proteome;
KW   rRNA processing; S-adenosyl-L-methionine; Transferase;
KW   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.
FT                                {ECO:0000255|HAMAP-Rule:MF_01849}.
FT   REGION      229    231       S-adenosyl-L-methionine binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01849}.
FT   ACT_SITE     91     91       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       111    111       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000255|HAMAP-Rule:MF_01849}.
FT   METAL       115    115       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000255|HAMAP-Rule:MF_01849}.
FT   METAL       118    118       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    104    349       (transient). {ECO:0000255|HAMAP-
FT                                Rule:MF_01849}.
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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