ID   A0A0E3V5E1_9BACT        Unreviewed;       353 AA.
AC   A0A0E3V5E1;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   29-SEP-2021, entry version 29.
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,
RC   ECO:0000313|Proteomes:UP000033054};
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 bacterium
RT   isolated from gamma ray-irradiated soil.";
RL   Curr. Microbiol. 69:286-291(2014).
CC   -!- FUNCTION: Specifically methylates position 2 of adenine 2503 in 23S
CC       rRNA and position 2 of adenine 37 in tRNAs. {ECO:0000256|HAMAP-
CC       Rule:MF_01849}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine(2503) in 23S rRNA + 2 reduced [2Fe-2S]-[ferredoxin]
CC         + 2 S-adenosyl-L-methionine = 2-methyladenosine(2503) in 23S rRNA +
CC         5'-deoxyadenosine + L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin] +
CC         S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:42916, Rhea:RHEA-
CC         COMP:10000, Rhea:RHEA-COMP:10001, Rhea:RHEA-COMP:10152, Rhea:RHEA-
CC         COMP:10282, ChEBI:CHEBI:17319, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC         ChEBI:CHEBI:57844, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:74411, ChEBI:CHEBI:74497; EC=2.1.1.192;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01849};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine(37) in tRNA + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-
CC         adenosyl-L-methionine = 2-methyladenosine(37) in tRNA + 5'-
CC         deoxyadenosine + L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin] + S-
CC         adenosyl-L-homocysteine; Xref=Rhea:RHEA:43332, Rhea:RHEA-COMP:10000,
CC         Rhea:RHEA-COMP:10001, Rhea:RHEA-COMP:10162, Rhea:RHEA-COMP:10485,
CC         ChEBI:CHEBI:17319, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC         ChEBI:CHEBI:57844, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:74411, ChEBI:CHEBI:74497; EC=2.1.1.192;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01849};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|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:0000256|HAMAP-Rule:MF_01849};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_01849}.
CC   -!- MISCELLANEOUS: Reaction proceeds by a ping-pong mechanism involving
CC       intermediate methylation of a conserved cysteine residue.
CC       {ECO:0000256|HAMAP-Rule:MF_01849}.
CC   -!- SIMILARITY: Belongs to the radical SAM superfamily. RlmN family.
CC       {ECO:0000256|HAMAP-Rule:MF_01849}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       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   PATRIC; fig|1379870.5.peg.71; -.
DR   HOGENOM; CLU_029101_0_1_10; -.
DR   OrthoDB; 1111428at2; -.
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-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   TIGRFAMs; TIGR00048; rRNA_mod_RlmN; 1.
DR   PROSITE; PS51918; RADICAL_SAM; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_01849};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01849};
KW   Disulfide bond {ECO:0000256|HAMAP-Rule:MF_01849};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01849};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW   Rule:MF_01849};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01849};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW   Rule:MF_01849}; Reference proteome {ECO:0000313|Proteomes:UP000033054};
KW   rRNA processing {ECO:0000256|ARBA:ARBA00022552, ECO:0000256|HAMAP-
KW   Rule:MF_01849};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW   Rule:MF_01849};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01849}; tRNA processing {ECO:0000256|HAMAP-Rule:MF_01849}.
FT   DOMAIN          107..341
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
FT   REGION          172..173
FT                   /note="S-adenosyl-L-methionine binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01849"
FT   REGION          227..229
FT                   /note="S-adenosyl-L-methionine binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01849"
FT   ACT_SITE        91
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01849"
FT   ACT_SITE        346
FT                   /note="S-methylcysteine intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01849"
FT   METAL           121
FT                   /note="Iron-sulfur (4Fe-4S-S-AdoMet)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01849"
FT   METAL           125
FT                   /note="Iron-sulfur (4Fe-4S-S-AdoMet)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01849"
FT   METAL           128
FT                   /note="Iron-sulfur (4Fe-4S-S-AdoMet)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01849"
FT   BINDING         204
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01849"
FT   BINDING         303
FT                   /note="S-adenosyl-L-methionine; via amide nitrogen and
FT                   carbonyl oxygen"
FT                   /evidence="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
//