ID   A0A073IMR2_9BACT        Unreviewed;       553 AA.
AC   A0A073IMR2;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   07-APR-2021, entry version 37.
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=EH55_08130 {ECO:0000313|EMBL:KEJ91633.1};
OS   Synergistes jonesii.
OC   Bacteria; Synergistetes; Synergistia; Synergistales; Synergistaceae;
OC   Synergistes.
OX   NCBI_TaxID=2754 {ECO:0000313|EMBL:KEJ91633.1, ECO:0000313|Proteomes:UP000027665};
RN   [1] {ECO:0000313|EMBL:KEJ91633.1, ECO:0000313|Proteomes:UP000027665}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=78-1 {ECO:0000313|EMBL:KEJ91633.1,
RC   ECO:0000313|Proteomes:UP000027665};
RA   Coil D.A., Eisen J.A., Holland-Moritz H.E.;
RT   "Draft Genome Sequence of Synergistes jonesii.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KEJ91633.1}.
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DR   EMBL; JMKI01000038; KEJ91633.1; -; Genomic_DNA.
DR   RefSeq; WP_070110155.1; NZ_JQEL01000045.1.
DR   STRING; 2754.EH55_08130; -.
DR   EnsemblBacteria; KEJ91633; KEJ91633; EH55_08130.
DR   eggNOG; COG0820; Bacteria.
DR   Proteomes; UP000027665; Unassembled WGS sequence.
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; IPR006638; Elp3/MiaB/NifB.
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   SFLD; SFLDF00275; adenosine_C2_methyltransferase; 1.
DR   SFLD; SFLDS00029; Radical_SAM; 1.
DR   SMART; SM00729; Elp3; 1.
DR   TIGRFAMs; TIGR00048; rRNA_mod_RlmN; 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:UP000027665};
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};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW   Rule:MF_01849}.
FT   DOMAIN          104..312
FT                   /note="Elp3"
FT                   /evidence="ECO:0000259|SMART:SM00729"
FT   REGION          161..162
FT                   /note="S-adenosyl-L-methionine binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01849"
FT   REGION          216..218
FT                   /note="S-adenosyl-L-methionine binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01849"
FT   REGION          390..553
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        432..519
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        94
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01849"
FT   ACT_SITE        334
FT                   /note="S-methylcysteine intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01849"
FT   METAL           114
FT                   /note="Iron-sulfur (4Fe-4S-S-AdoMet)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01849"
FT   METAL           118
FT                   /note="Iron-sulfur (4Fe-4S-S-AdoMet)"
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   BINDING         193
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01849"
FT   BINDING         292
FT                   /note="S-adenosyl-L-methionine; via amide nitrogen and
FT                   carbonyl oxygen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01849"
SQ   SEQUENCE   553 AA;  61058 MW;  5D01DDCF3FB9F424 CRC64;
     MAEKKYALDF DFGEWEKYIT ESLGEPKFRA GQICGWLWQK RVCDPAEMTN LSKELRAELA
     EKLDFACPAL VREQRSRDGT KKFLWRLRDG ETVESVLIKE GDRLTLCVST QVGCPLHCSF
     CATGLSGFAR NLSAGEIAGQ LLAAEKQIGR EINNVVYMGM GEPLLNVDSV LKSVRMLNDP
     KMRNLGRRHI TISTSGVIPG IEELAASGLG VRLAVSLHAA DDELRSLLMP VNQTYPASEL
     RDAMQKYQAA TGDRITIEYA LFGGVNDGVE RARELVRYLK GIHVFVNLIP ANDVAGRCEK
     PKAEDVLRFR SVLESAGFEC EIRSERGADI DAACGQLRRK AHGGEAAPEG GARTLAKAAV
     PPRVDKSDEW KEKSAARVKG AKKDFPALRA NEKKKAFSPS GGFVAYPGKR VRAQRPAGEK
     SYGAPNFGEK RGGRGNARDF ETPLGARSRD EHAELRRGGK TDEARQDHRT RREEENHFER
     GVAAKHGYAE ARAEKFDTRR PRKSGSCAPE KDSSRQRPRG KAKNGAGRGA ADADSAFWKF
     YLRPKKSARG KKP
//