ID   TFB1M_MACFA             Reviewed;         345 AA.
AC   Q2PG46;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 69.
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            Short=mtTFB1;
DE   AltName: Full=S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase 1;
DE   Flags: Precursor;
GN   Name=TFB1M; ORFNames=QccE-11267;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RA   Osada N., Hida M., Kusuda J., Tanuma R., Iseki K., Hirai M., Terao K.,
RA   Suzuki Y., Sugano S., Hashimoto K.;
RT   "Isolation of full-length cDNA clones from macaque brain cDNA libraries.";
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase which
CC       specifically dimethylates mitochondrial 12S rRNA at the conserved stem
CC       loop. Also required for basal transcription of mitochondrial DNA,
CC       probably via its interaction with POLRMT and TFAM. Stimulates
CC       transcription independently of the methyltransferase activity (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with mitochondrial RNA polymerase POLRMT. Interacts
CC       with TFAM (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:0000255|PROSITE-ProRule:PRU01026}.
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DR   EMBL; AB220391; BAE72924.1; -; mRNA.
DR   RefSeq; NP_001270403.1; NM_001283474.1.
DR   AlphaFoldDB; Q2PG46; -.
DR   SMR; Q2PG46; -.
DR   STRING; 9541.XP_005552248.1; -.
DR   Ensembl; ENSMFAT00000068242; ENSMFAP00000017700; ENSMFAG00000031968.
DR   GeneID; 102130743; -.
DR   CTD; 51106; -.
DR   eggNOG; KOG0821; Eukaryota.
DR   GeneTree; ENSGT00950000183142; -.
DR   OrthoDB; 628543at2759; -.
DR   Proteomes; UP000233100; Chromosome 4.
DR   Bgee; ENSMFAG00000031968; Expressed in thymus and 13 other tissues.
DR   GO; GO:0042645; C:mitochondrial nucleoid; IEA:Ensembl.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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   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; 1.
DR   Pfam; PF00398; RrnaAD; 1.
DR   SMART; SM00650; rADc; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR00755; ksgA; 1.
DR   PROSITE; PS01131; RRNA_A_DIMETH; 1.
DR   PROSITE; PS51689; SAM_RNA_A_N6_MT; 1.
PE   2: Evidence at transcript level;
KW   DNA-binding; Methyltransferase; Mitochondrion; Reference proteome;
KW   RNA-binding; rRNA processing; S-adenosyl-L-methionine; Transcription;
KW   Transcription regulation; Transferase; Transit peptide.
FT   TRANSIT         1..27
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..345
FT                   /note="Dimethyladenosine transferase 1, mitochondrial"
FT                   /id="PRO_0000273172"
FT   BINDING         35..38
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         36
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT   BINDING         38
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT   BINDING         63
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT   BINDING         85
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT   BINDING         111
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT   BINDING         141
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
SQ   SEQUENCE   345 AA;  39480 MW;  293CD4488648052E CRC64;
     MAAPGKLSTC RLPPLPTIRE IIKLFRLQAT KQLSQNFLLD LRLTDKIVRK AGNLANAYVY
     EVGPGPGGIT RSILNADVAE LLVVEKDTRF IPGLQMLSEA APGKLRIVHG DVLTFKVEKA
     FSESLKRPWE DDPPNVHIIG NLPFSVSTPL IIKWLENISC RDGPFVYGRT QMTLTFQKEV
     AERLAANTGS KQRSRLSVMA QYLCNVRHIF TIPGRAFVPK PEVDVGVVHF TPLIQPKIEQ
     PFKLVEKVVQ NVFQFRRKYC HRGLGMLFPE AQRLENTGRL LELADIDPTL RPRQLSISHF
     KSLCEVYRRM CDEDPQLFAY NFREELRQRK IKKKEKQDDA KSYRL