ID   RLMN_CALS4              Reviewed;         342 AA.
AC   Q8R9T4;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   16-JAN-2019, entry version 104.
DE   RecName: Full=Probable dual-specificity RNA methyltransferase RlmN {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=TTE1502;
OS   Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 /
OS   JCM 11007 / NBRC 100824 / MB4) (Thermoanaerobacter tengcongensis).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Caldanaerobacter.
OX   NCBI_TaxID=273068;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15242 / JCM 11007 / NBRC 100824 / MB4;
RX   PubMed=11997336; DOI=10.1101/gr.219302;
RA   Bao Q., Tian Y., Li W., Xu Z., Xuan Z., Hu S., Dong W., Yang J.,
RA   Chen Y., Xue Y., Xu Y., Lai X., Huang L., Dong X., Ma Y., Ling L.,
RA   Tan H., Chen R., Wang J., Yu J., Yang H.;
RT   "A complete sequence of the T. tengcongensis genome.";
RL   Genome Res. 12:689-700(2002).
CC   -!- FUNCTION: Specifically methylates position 2 of adenine 2503 in
CC       23S rRNA and position 2 of adenine 37 in tRNAs.
CC       {ECO:0000255|HAMAP-Rule:MF_01849}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine(2503) in 23S rRNA + 2 reduced [2Fe-2S]-
CC         [ferredoxin] + 2 S-adenosyl-L-methionine = 2-
CC         methyladenosine(2503) in 23S rRNA + 5'-deoxyadenosine + L-
CC         methionine + 2 oxidized [2Fe-2S]-[ferredoxin] + S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:42916, Rhea:RHEA-COMP:10000,
CC         Rhea:RHEA-COMP:10001, Rhea:RHEA-COMP:10152, Rhea:RHEA-
CC         COMP:10282, ChEBI:CHEBI:17319, ChEBI:CHEBI:33737,
CC         ChEBI:CHEBI:33738, ChEBI:CHEBI:57844, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:74411, ChEBI:CHEBI:74497;
CC         EC=2.1.1.192; Evidence={ECO:0000255|HAMAP-Rule:MF_01849};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine(37) in tRNA + 2 reduced [2Fe-2S]-[ferredoxin] +
CC         2 S-adenosyl-L-methionine = 2-methyladenosine(37) in tRNA + 5'-
CC         deoxyadenosine + L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin]
CC         + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:43332, Rhea:RHEA-
CC         COMP:10000, Rhea:RHEA-COMP:10001, Rhea:RHEA-COMP:10162,
CC         Rhea:RHEA-COMP:10485, ChEBI:CHEBI:17319, ChEBI:CHEBI:33737,
CC         ChEBI:CHEBI:33738, ChEBI:CHEBI:57844, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:74411, ChEBI:CHEBI:74497;
CC         EC=2.1.1.192; Evidence={ECO:0000255|HAMAP-Rule:MF_01849};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01849};
CC       Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC       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; AE008691; AAM24720.1; -; Genomic_DNA.
DR   RefSeq; WP_011025761.1; NC_003869.1.
DR   ProteinModelPortal; Q8R9T4; -.
DR   SMR; Q8R9T4; -.
DR   STRING; 273068.TTE1502; -.
DR   EnsemblBacteria; AAM24720; AAM24720; TTE1502.
DR   KEGG; tte:TTE1502; -.
DR   eggNOG; ENOG4105C55; Bacteria.
DR   eggNOG; COG0820; LUCA.
DR   HOGENOM; HOG000217991; -.
DR   KO; K06941; -.
DR   OMA; CGQLANK; -.
DR   OrthoDB; 1111428at2; -.
DR   BioCyc; TTEN273068:G1FZJ-1598-MONOMER; -.
DR   Proteomes; UP000000555; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0070040; F:rRNA (adenine-C2-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0002935; F:tRNA (adenine-C2-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0070475; P:rRNA base methylation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_01849; RNA_methyltr_RlmN; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR040072; Methyltransferase_A.
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   SFLD; SFLDF00275; adenosine_C2_methyltransferase; 1.
DR   SFLD; SFLDS00029; Radical_SAM; 1.
DR   TIGRFAMs; TIGR00048; rRNA_mod_RlmN; 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    342       Probable dual-specificity RNA
FT                                methyltransferase RlmN.
FT                                /FTId=PRO_0000350496.
FT   REGION      157    158       S-adenosyl-L-methionine binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01849}.
FT   REGION      212    214       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    331    331       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     189    189       S-adenosyl-L-methionine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01849}.
FT   BINDING     288    288       S-adenosyl-L-methionine; via amide
FT                                nitrogen and carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01849}.
FT   DISULFID    104    331       (transient). {ECO:0000255|HAMAP-
FT                                Rule:MF_01849}.
SQ   SEQUENCE   342 AA;  39453 MW;  AFBC048AEDB24289 CRC64;
     MYNLKDMTLE EMEEFFVNLG ESKFRAKQLY KWIYDKRVTD FDLMTDISKN LRAKLKEIAY
     ISELKIIERR VSQIDDTVKY LFLLEDKNII EGVAIKYKFG NTACVSTQVG CNMKCKFCAS
     AIGGKVRDLK ASEMVDQVMA IDSDYGKISN IVLMGSGEPF DNYDEVMKFI KIVNNPYGLK
     IGKRHITIST VGIVPKIYQF ADEELQVNLS ISLHAPNNEL RNELMPINRA YPLEELMKAC
     RYYIEKTNRR ITFEYALIDG VNDKKEHAYQ LVDLLKGMLC HVNLIPINYV KEIGFRKSNN
     EKVMMFKKII ENAGITCTVR RELGSDIEAA CGQLRRKYLK EG
//