ID   TFB1M_VERVE             Reviewed;         343 AA.
AC   Q1A705;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Dimethyladenosine transferase 1, mitochondrial;
DE            EC=2.1.1.-;
DE   AltName: Full=Mitochondrial 12S rRNA dimethylase 1;
DE   AltName: Full=Mitochondrial transcription factor B1;
DE   AltName: Full=S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase 1;
DE   Flags: Precursor;
OS   Vermamoeba vermiformis (Amoeba) (Hartmannella vermiformis).
OC   Eukaryota; Amoebozoa; Tubulinea; Echinamoebida; Vermamoeba.
OX   NCBI_TaxID=5778;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=16533820; DOI=10.1093/molbev/msk001;
RA   Shutt T.E., Gray M.W.;
RT   "Homologs of mitochondrial transcription factor B, sparsely distributed
RT   within the eukaryotic radiation, are likely derived from the
RT   dimethyladenosine methyltransferase of the mitochondrial endosymbiont.";
RL   Mol. Biol. Evol. 23:1169-1179(2006).
CC   -!- FUNCTION: Probable S-adenosyl-L-methionine-dependent methyltransferase
CC       which specifically dimethylates mitochondrial 12S rRNA at the conserved
CC       stem loop. Also required for basal transcription of mitochondrial DNA.
CC       Stimulates transcription independently of the methyltransferase
CC       activity (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. rRNA adenine N(6)-methyltransferase family. KsgA
CC       subfamily. {ECO:0000305}.
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DR   EMBL; DQ295025; ABB97064.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1A705; -.
DR   SMR; Q1A705; -.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0000179; F:rRNA (adenine-N6,N6-)-dimethyltransferase activity; IEA:InterPro.
DR   Gene3D; 1.10.8.100; -; 1.
DR   Gene3D; 3.40.50.150; -; 1.
DR   HAMAP; MF_00607; 16SrRNA_methyltr_A; 1.
DR   InterPro; IPR001737; KsgA/Erm.
DR   InterPro; IPR023165; rRNA_Ade_diMease-like_C.
DR   InterPro; IPR020596; rRNA_Ade_Mease_Trfase_CS.
DR   InterPro; IPR020598; rRNA_Ade_methylase_Trfase_N.
DR   InterPro; IPR011530; rRNA_adenine_dimethylase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR11727; PTHR11727; 2.
DR   Pfam; PF00398; RrnaAD; 2.
DR   SMART; SM00650; rADc; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS01131; RRNA_A_DIMETH; 1.
DR   PROSITE; PS51689; SAM_RNA_A_N6_MT; 1.
PE   3: Inferred from homology;
KW   Methyltransferase; Mitochondrion; RNA-binding; rRNA processing;
KW   S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW   Transferase; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..343
FT                   /note="Dimethyladenosine transferase 1, mitochondrial"
FT                   /id="PRO_0000273186"
FT   BINDING         28..31
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         29
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         31
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         56
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         78
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         133
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         169
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   343 AA;  38523 MW;  884E8369D24E8851 CRC64;
     MTMRLPPLPT IGELIRLFGL SAKQQLSQNF LLDLNITDKI VRSSGDLTNK TVIEVGPGPG
     GLTRSILKAG AKKLVVIEKD RRFLPALEVL RHAAGNIDGS PWEEAFLTKS EMDAKRYMSY
     APNKSRMQIV MNDVLRVDEQ EILQHIHAPI DSNDKTQWEN MAPITIIGNL PFAISTELTI
     KWLKQIQGRH GAFRFGRAEF ILMFQKEVAD RLIANPGTKQ YSRLTVMTQQ LCSVKKLSDI
     PGSAFVPKPD VDASLVSMVP RVTPLGVNVP TPTLEYVCRQ VFGQRRKMIN NSVKTLGPEA
     EILLARAHID PTLRPEQLTV PQWCDLARAY QQWENKPQWA PAL