ID   TFB1M_XENLA             Reviewed;         344 AA.
AC   Q7T0W5;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 81.
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;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (AUG-2003) 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       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:0000255|PROSITE-ProRule:PRU01026}.
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DR   EMBL; BC056010; AAH56010.1; -; mRNA.
DR   RefSeq; NP_001079850.1; NM_001086381.1.
DR   AlphaFoldDB; Q7T0W5; -.
DR   SMR; Q7T0W5; -.
DR   DNASU; 379540; -.
DR   GeneID; 379540; -.
DR   KEGG; xla:379540; -.
DR   CTD; 379540; -.
DR   Xenbase; XB-GENE-6255481; tfb1m.L.
DR   OrthoDB; 628543at2759; -.
DR   Proteomes; UP000186698; Chromosome 9_10L.
DR   Bgee; 379540; Expressed in oocyte and 19 other tissues.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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; 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; 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..344
FT                   /note="Dimethyladenosine transferase 1, mitochondrial"
FT                   /id="PRO_0000273176"
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   344 AA;  39432 MW;  2D2F1BC04600F14F CRC64;
     MATPGALAKF RLPPLPTIGE IVKLFNLRAE KQLSQNFLLD LKLTDKIVRR AGNLQNAYVC
     EVGPGPGGIT RSILNAGVEE LLVVEKDTRF IPGLKMLNEA SGGKVRTVHG DILTYRMDRA
     FPKHLIKSWD DEPPNVHIIG NLPFSVSTPL IIKWLEQVAD RTGPFTYGRT QMTLTFQQEV
     AERLTASTKN KQRSRLSIMS QYLCNVKNCF TIPGRAFIPK PKVDVGVVHL TPFVQPKIEQ
     PFKLVEKVVR CIFQFRRKYC HHGVSILFPE EIRIQLTEQM LRLADVDPTL RPTELTMTHF
     KKLCNVYREM CDQNPHLFSY NYREELRMKK LQGKSTEEED DLLQ