ID   A0A225TNJ3_9NOCA        Unreviewed;       369 AA.
AC   A0A225TNJ3;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   07-NOV-2018, entry version 4.
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=B9C99_06460 {ECO:0000313|EMBL:OWY82457.1};
OS   Rhodococcus sp. BUPNP1.
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=1432786 {ECO:0000313|EMBL:OWY82457.1, ECO:0000313|Proteomes:UP000198201};
RN   [1] {ECO:0000313|EMBL:OWY82457.1, ECO:0000313|Proteomes:UP000198201}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BUPNP1 {ECO:0000313|EMBL:OWY82457.1,
RC   ECO:0000313|Proteomes:UP000198201};
RA   Sengupta K., Whitworth D.E., Swain M., Saha P.;
RT   "Rhodococcus sp. BUPNP1, whole genome shotgun sequence.";
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
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:SAAS01075366}.
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:SAAS01075355}.
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:SAAS01075335}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01849,
CC       ECO:0000256|SAAS:SAAS01075369}.
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:SAAS01075361}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01849}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:OWY82457.1}.
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DR   EMBL; NERM01000005; OWY82457.1; -; Genomic_DNA.
DR   RefSeq; WP_016691228.1; NZ_NERM01000005.1.
DR   Proteomes; UP000198201; 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; 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; SFLDG01062; methyltransferase_(Class_A); 1.
DR   SFLD; SFLDS00029; Radical_SAM; 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:SAAS01075359};
KW   Complete proteome {ECO:0000313|Proteomes:UP000198201};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01849,
KW   ECO:0000256|SAAS:SAAS01075336};
KW   Disulfide bond {ECO:0000256|HAMAP-Rule:MF_01849,
KW   ECO:0000256|SAAS:SAAS01075368};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_01849, ECO:0000256|SAAS:SAAS01075349};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_01849,
KW   ECO:0000256|SAAS:SAAS01075344};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01849,
KW   ECO:0000256|SAAS:SAAS01075339};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_01849,
KW   ECO:0000256|SAAS:SAAS01075338, ECO:0000313|EMBL:OWY82457.1};
KW   rRNA processing {ECO:0000256|HAMAP-Rule:MF_01849,
KW   ECO:0000256|SAAS:SAAS01075357};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_01849,
KW   ECO:0000256|SAAS:SAAS01075340};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01849,
KW   ECO:0000256|SAAS:SAAS01075354, ECO:0000313|EMBL:OWY82457.1};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_01849,
KW   ECO:0000256|SAAS:SAAS01075343}.
FT   DOMAIN      123    296       Radical_SAM. {ECO:0000259|Pfam:PF04055}.
FT   REGION      183    184       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01849}.
FT   REGION      240    242       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01849}.
FT   ACT_SITE    108    108       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01849}.
FT   ACT_SITE    362    362       S-methylcysteine intermediate.
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   METAL       132    132       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|HAMAP-Rule:MF_01849}.
FT   METAL       135    135       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|HAMAP-Rule:MF_01849}.
FT   BINDING     217    217       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01849}.
FT   BINDING     319    319       S-adenosyl-L-methionine; via amide
FT                                nitrogen and carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01849}.
SQ   SEQUENCE   369 AA;  39756 MW;  E49A17C46BFA30CE CRC64;
     MASSLPLVFD APKRGLPPRH LADLDADQRR DAVRELGLPA FRADQLARQY YGRLEADPAK
     MTDLPAAVRD KVGEALFPPL LSAVRHIACD GGETRKTLWR AHDGTLLESV LMRYPDRATL
     CISSQAGCGM ACPFCATGQG GLDRNLSTAE IVDQVRAAAA ALRDGDVAGG PGRLSNVVFM
     GMGEPLANYK RVVAAVRRIT SPAPEGLGLS QRSVTVSTVG LAPAIRRLAD EGLSVTLAVS
     LHTPDDELRD TLVPVNNRWS VAEVLEAARY YADKTGRRVS IEYALIRDVN DQPWRADMLG
     KKLHKALGSL VHVNLIPLNP TPGSEWDASP KDVEREFVRR VQAQGVSCTV RDTRGQEIAA
     ACGQLAAEG
//