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Probable dual-specificity RNA methyltransferase RlmN (EC 2.1.1.192) (23S rRNA (adenine(2503)-C(2))-methyltransferase) (23S rRNA m2A2503 methyltransferase) (Ribosomal RNA large subunit methyltransferase N) (tRNA (adenine(37)-C(2))-methyltransferase) (tRNA m2A37 methyltransferase)

 RLMN_TREPA              Reviewed;         340 AA.
O83107;
02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
22-NOV-2017, entry version 116.
RecName: Full=Probable dual-specificity RNA methyltransferase RlmN {ECO:0000255|HAMAP-Rule:MF_01849};
EC=2.1.1.192 {ECO:0000255|HAMAP-Rule:MF_01849};
AltName: Full=23S rRNA (adenine(2503)-C(2))-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01849};
AltName: Full=23S rRNA m2A2503 methyltransferase {ECO:0000255|HAMAP-Rule:MF_01849};
AltName: Full=Ribosomal RNA large subunit methyltransferase N {ECO:0000255|HAMAP-Rule:MF_01849};
AltName: Full=tRNA (adenine(37)-C(2))-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01849};
AltName: Full=tRNA m2A37 methyltransferase {ECO:0000255|HAMAP-Rule:MF_01849};
Name=rlmN {ECO:0000255|HAMAP-Rule:MF_01849};
OrderedLocusNames=TP_0068;
Treponema pallidum (strain Nichols).
Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Treponema.
NCBI_TaxID=243276;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Nichols;
PubMed=9665876; DOI=10.1126/science.281.5375.375;
Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M.,
Utterback T.R., McDonald L.A., Artiach P., Bowman C., Cotton M.D.,
Fujii C., Garland S.A., Hatch B., Horst K., Roberts K.M., Sandusky M.,
Weidman J.F., Smith H.O., Venter J.C.;
"Complete genome sequence of Treponema pallidum, the syphilis
spirochete.";
Science 281:375-388(1998).
-!- FUNCTION: Specifically methylates position 2 of adenine 2503 in
23S rRNA and position 2 of adenine 37 in tRNAs.
{ECO:0000255|HAMAP-Rule:MF_01849}.
-!- CATALYTIC ACTIVITY: 2 S-adenosyl-L-methionine + adenine(2503) in
23S rRNA + 2 reduced [2Fe-2S] ferredoxin = S-adenosyl-L-
homocysteine + L-methionine + 5'-deoxyadenosine + 2-
methyladenine(2503) in 23S rRNA + 2 oxidized [2Fe-2S] ferredoxin.
{ECO:0000255|HAMAP-Rule:MF_01849}.
-!- CATALYTIC ACTIVITY: 2 S-adenosyl-L-methionine + adenine(37) in
tRNA + 2 reduced [2Fe-2S] ferredoxin = S-adenosyl-L-homocysteine +
L-methionine + 5'-deoxyadenosine + 2-methyladenine(37) in tRNA + 2
oxidized [2Fe-2S] ferredoxin. {ECO:0000255|HAMAP-Rule:MF_01849}.
-!- COFACTOR:
Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
Evidence={ECO:0000255|HAMAP-Rule:MF_01849};
Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
cysteines and an exchangeable S-adenosyl-L-methionine.
{ECO:0000255|HAMAP-Rule:MF_01849};
-!- INTERACTION:
O83970:dnaZX2; NbExp=2; IntAct=EBI-1585371, EBI-1582351;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01849}.
-!- MISCELLANEOUS: Reaction proceeds by a ping-pong mechanism
involving intermediate methylation of a conserved cysteine
residue. {ECO:0000255|HAMAP-Rule:MF_01849}.
-!- SIMILARITY: Belongs to the radical SAM superfamily. RlmN family.
{ECO:0000255|HAMAP-Rule:MF_01849}.
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EMBL; AE000520; AAC65061.1; -; Genomic_DNA.
PIR; D71371; D71371.
RefSeq; WP_010881517.1; NC_021490.2.
ProteinModelPortal; O83107; -.
SMR; O83107; -.
IntAct; O83107; 7.
STRING; 243276.TP0068; -.
EnsemblBacteria; AAC65061; AAC65061; TP_0068.
GeneID; 34331620; -.
KEGG; tpa:TP_0068; -.
eggNOG; ENOG4105C55; Bacteria.
eggNOG; COG0820; LUCA.
KO; K06941; -.
OMA; CGQLANK; -.
Proteomes; UP000000811; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0070040; F:rRNA (adenine-C2-)-methyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0070475; P:rRNA base methylation; IEA:InterPro.
GO; GO:0030488; P:tRNA methylation; IEA:InterPro.
Gene3D; 3.20.20.70; -; 1.
HAMAP; MF_01849; RNA_methyltr_RlmN; 1.
InterPro; IPR013785; Aldolase_TIM.
InterPro; IPR027492; RNA_MTrfase_RlmN.
InterPro; IPR004383; rRNA_lsu_MTrfase_RlmN/Cfr.
InterPro; IPR007197; rSAM.
PANTHER; PTHR30544; PTHR30544; 1.
Pfam; PF04055; Radical_SAM; 1.
PIRSF; PIRSF006004; CHP00048; 1.
SFLD; SFLDF00275; adenosine_C2_methyltransferase; 1.
SFLD; SFLDS00029; Radical_SAM; 1.
TIGRFAMs; TIGR00048; rRNA_mod_RlmN; 1.
1: Evidence at protein level;
4Fe-4S; Complete proteome; Cytoplasm; Disulfide bond; Iron;
Iron-sulfur; Metal-binding; Methyltransferase; Reference proteome;
rRNA processing; S-adenosyl-L-methionine; Transferase;
tRNA processing.
CHAIN 1 340 Probable dual-specificity RNA
methyltransferase RlmN.
/FTId=PRO_0000350509.
REGION 157 158 S-adenosyl-L-methionine binding.
{ECO:0000255|HAMAP-Rule:MF_01849}.
REGION 212 214 S-adenosyl-L-methionine binding.
{ECO:0000255|HAMAP-Rule:MF_01849}.
ACT_SITE 90 90 Proton acceptor. {ECO:0000255|HAMAP-
Rule:MF_01849}.
ACT_SITE 331 331 S-methylcysteine intermediate.
{ECO:0000255|HAMAP-Rule:MF_01849}.
METAL 111 111 Iron-sulfur (4Fe-4S-S-AdoMet).
{ECO:0000255|HAMAP-Rule:MF_01849}.
METAL 115 115 Iron-sulfur (4Fe-4S-S-AdoMet).
{ECO:0000255|HAMAP-Rule:MF_01849}.
METAL 118 118 Iron-sulfur (4Fe-4S-S-AdoMet).
{ECO:0000255|HAMAP-Rule:MF_01849}.
BINDING 189 189 S-adenosyl-L-methionine.
{ECO:0000255|HAMAP-Rule:MF_01849}.
BINDING 288 288 S-adenosyl-L-methionine; via amide
nitrogen and carbonyl oxygen.
{ECO:0000255|HAMAP-Rule:MF_01849}.
DISULFID 104 331 (transient). {ECO:0000255|HAMAP-
Rule:MF_01849}.
SEQUENCE 340 AA; 37520 MW; 4F1F0332758CF721 CRC64;
MEWCCALSGL LPEEIQKVCA FAERFRGVQV FRWIAAGCTD FHAMSDLSSE TRARLARACV
ISDTRVYTTL RDVDGTLKLG IELKDKRRVE AVLLVDQVSR KTACLSCQVG CPMACAFCQT
GQLGFARNLS ASEIVEQFLH LERCVGTLDN VVFMGMGEPM LNLDAVCRAI EILSHPQGRD
LSEKRITIST SGHCRGIYSL ADRALQVRLA VSLTTANAPL RARLMPRAAH DSLAKLKSAI
RYFNEKSGKR VTLELALMRG VNTSERHAQE VIDFAHGLNV HVNLIPWNPV ASIHFETPRE
VEVAHFEALL MRARIPVTRR YQRGNGIGGA CGQLGKTAGV


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