ID   A0A0E3V5E1_9BACT        Unreviewed;       353 AA.
AC   A0A0E3V5E1;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   18-JAN-2017, entry version 11.
DE   RecName: Full=Probable dual-specificity RNA methyltransferase RlmN {ECO:0000256|HAMAP-Rule:MF_01849};
DE            EC=2.1.1.192 {ECO:0000256|HAMAP-Rule:MF_01849};
DE   AltName: Full=23S rRNA (adenine(2503)-C(2))-methyltransferase {ECO:0000256|HAMAP-Rule:MF_01849};
DE   AltName: Full=23S rRNA m2A2503 methyltransferase {ECO:0000256|HAMAP-Rule:MF_01849};
DE   AltName: Full=Ribosomal RNA large subunit methyltransferase N {ECO:0000256|HAMAP-Rule:MF_01849};
DE   AltName: Full=tRNA (adenine(37)-C(2))-methyltransferase {ECO:0000256|HAMAP-Rule:MF_01849};
DE   AltName: Full=tRNA m2A37 methyltransferase {ECO:0000256|HAMAP-Rule:MF_01849};
GN   Name=rlmN {ECO:0000256|HAMAP-Rule:MF_01849};
GN   ORFNames=SD10_00325 {ECO:0000313|EMBL:AKD53576.1};
OS   Spirosoma radiotolerans.
OC   Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cytophagaceae;
OC   Spirosoma.
OX   NCBI_TaxID=1379870 {ECO:0000313|EMBL:AKD53576.1, ECO:0000313|Proteomes:UP000033054};
RN   [1] {ECO:0000313|EMBL:AKD53576.1, ECO:0000313|Proteomes:UP000033054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DG5A {ECO:0000313|EMBL:AKD53576.1};
RX   PubMed=24748440; DOI=10.1007/s00284-014-0584-x;
RA   Lee J.J., Srinivasan S., Lim S., Joe M., Im S., Bae S.I., Park K.R.,
RA   Han J.H., Park S.H., Joo B.M., Park S.J., Kim M.K.;
RT   "Spirosoma radiotolerans sp. nov., a gamma-radiation-resistant
RT   bacterium isolated from gamma ray-irradiated soil.";
RL   Curr. Microbiol. 69:286-291(2014).
CC   -!- FUNCTION: Specifically methylates position 2 of adenine 2503 in
CC       23S rRNA and position 2 of adenine 37 in tRNAs.
CC       {ECO:0000256|SAAS:SAAS00536189}.
CC   -!- CATALYTIC ACTIVITY: 2 S-adenosyl-L-methionine + adenine(2503) in
CC       23S rRNA + 2 reduced [2Fe-2S] ferredoxin = S-adenosyl-L-
CC       homocysteine + L-methionine + 5'-deoxyadenosine + 2-
CC       methyladenine(2503) in 23S rRNA + 2 oxidized [2Fe-2S] ferredoxin.
CC       {ECO:0000256|HAMAP-Rule:MF_01849, ECO:0000256|SAAS:SAAS00536154}.
CC   -!- CATALYTIC ACTIVITY: 2 S-adenosyl-L-methionine + adenine(37) in
CC       tRNA + 2 reduced [2Fe-2S] ferredoxin = S-adenosyl-L-homocysteine +
CC       L-methionine + 5'-deoxyadenosine + 2-methyladenine(37) in tRNA + 2
CC       oxidized [2Fe-2S] ferredoxin. {ECO:0000256|HAMAP-Rule:MF_01849,
CC       ECO:0000256|SAAS:SAAS00536173}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01849,
CC       ECO:0000256|SAAS:SAAS00385725}.
CC   -!- MISCELLANEOUS: Reaction proceeds by a ping-pong mechanism
CC       involving intermediate methylation of a conserved cysteine
CC       residue. {ECO:0000256|HAMAP-Rule:MF_01849}.
CC   -!- SIMILARITY: Belongs to the radical SAM superfamily. RlmN family.
CC       {ECO:0000256|HAMAP-Rule:MF_01849, ECO:0000256|SAAS:SAAS00571858}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01849}.
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DR   EMBL; CP010429; AKD53576.1; -; Genomic_DNA.
DR   RefSeq; WP_046375163.1; NZ_CP010429.1.
DR   EnsemblBacteria; AKD53576; AKD53576; SD10_00325.
DR   KEGG; srd:SD10_00325; -.
DR   KO; K06941; -.
DR   Proteomes; UP000033054; Chromosome.
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; rRNA_mod_RlmN; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|HAMAP-Rule:MF_01849,
KW   ECO:0000256|SAAS:SAAS00463035};
KW   Complete proteome {ECO:0000313|Proteomes:UP000033054};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01849,
KW   ECO:0000256|SAAS:SAAS00462865};
KW   Disulfide bond {ECO:0000256|HAMAP-Rule:MF_01849,
KW   ECO:0000256|SAAS:SAAS00536144};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_01849, ECO:0000256|SAAS:SAAS00462960};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_01849,
KW   ECO:0000256|SAAS:SAAS00462907};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01849,
KW   ECO:0000256|SAAS:SAAS00462842};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_01849,
KW   ECO:0000256|SAAS:SAAS00462825, ECO:0000313|EMBL:AKD53576.1};
KW   rRNA processing {ECO:0000256|HAMAP-Rule:MF_01849,
KW   ECO:0000256|SAAS:SAAS00536180};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_01849,
KW   ECO:0000256|SAAS:SAAS00462941};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01849,
KW   ECO:0000256|SAAS:SAAS00463018, ECO:0000313|EMBL:AKD53576.1};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_01849,
KW   ECO:0000256|SAAS:SAAS00536153}.
FT   DOMAIN      116    285       Radical_SAM. {ECO:0000259|Pfam:PF04055}.
FT   REGION      172    173       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01849}.
FT   REGION      227    229       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01849}.
FT   ACT_SITE     91     91       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01849}.
FT   ACT_SITE    346    346       S-methylcysteine intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_01849}.
FT   METAL       121    121       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|HAMAP-Rule:MF_01849}.
FT   METAL       125    125       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|HAMAP-Rule:MF_01849}.
FT   METAL       128    128       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|HAMAP-Rule:MF_01849}.
FT   BINDING     204    204       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01849}.
FT   BINDING     303    303       S-adenosyl-L-methionine; via amide
FT                                nitrogen and carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01849}.
SQ   SEQUENCE   353 AA;  39882 MW;  56F9D646434E2EDB CRC64;
     MKQDIRKLTA VQLKDWFAKN NQQGFRAKQV HEWLWKKSAL SFEQMTNLSL PTRELLNEHF
     EIRSLTVDQQ QRSNDGTIKS SFRLFDGNLV EGVLIPALRT DARDDGPSDR MTACVSSQVG
     CSLTCKFCAT GYMDRKRNLD AAEIYDQVVA IDRQAKENYD ASLTNIVYMG MGEPLLNYKN
     VLESVDRITS PDGLGMSPKR ITVSTAGIAK MIRQLGDDEV KFNLALSLHA ANDLKRDQIM
     PINESNTLEV LGDALTYFYK KTGTRVTFEY ILFYNFNDTL QDALELWKFT KRVPAKINII
     EYNPIAEASF KNTDPQTLDK FAGFLESKGV TVNVRRSRGK DIDAACGQLA GKK
//