ID   TFB1M_XENTR             Reviewed;         346 AA.
AC   Q28HM1;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=TTpA018f13.1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Tadpole;
RG   Sanger Xenopus tropicalis EST/cDNA project;
RL   Submitted (OCT-2006) 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; CR760823; CAJ83142.1; -; mRNA.
DR   RefSeq; NP_001016494.1; NM_001016494.2.
DR   RefSeq; XP_012827224.1; XM_012971770.2.
DR   AlphaFoldDB; Q28HM1; -.
DR   SMR; Q28HM1; -.
DR   STRING; 8364.ENSXETP00000017166; -.
DR   PaxDb; Q28HM1; -.
DR   GeneID; 549248; -.
DR   KEGG; xtr:549248; -.
DR   CTD; 51106; -.
DR   Xenbase; XB-GENE-5721420; tfb1m.
DR   eggNOG; KOG0821; Eukaryota.
DR   InParanoid; Q28HM1; -.
DR   OrthoDB; 628543at2759; -.
DR   Proteomes; UP000008143; Chromosome 10.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000007852; Expressed in egg cell and 19 other tissues.
DR   GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0034246; F:mitochondrial transcription factor activity; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0000179; F:rRNA (adenine-N6,N6-)-dimethyltransferase activity; IBA:GO_Central.
DR   GO; GO:0031167; P:rRNA methylation; IBA:GO_Central.
DR   GO; GO:0006391; P:transcription initiation from mitochondrial promoter; IBA:GO_Central.
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..346
FT                   /note="Dimethyladenosine transferase 1, mitochondrial"
FT                   /id="PRO_0000273177"
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   346 AA;  39570 MW;  C339B2E1DCF9034C CRC64;
     MATQGVLAKY RLPPLPTIGE IIKLFNLRAE KQLSQNFLLD LKLTDKIVRK AGNLQNAYVC
     EVGPGPGGIT RSILNAGVEE LLVVEKDTRF IPGLKMLNEA SSGKVQIVHG DILTYRMDRA
     FPKHLKKPWD DDPPNVHIIG NLPFSVSTPL IIKWLEQLAD RTGPFTYGRT QMTLTFQKEV
     AERLTASTSS KQRSRLSIMA QNLCNVKNCF TIPGRAFVPK PEVDVGVVHF TPFIQPKIEQ
     PFKVVEKVVR SVFQFRRKYC HHGVSILFPE ESRLKCTEQM LRLADVDPTL RPTELTMTHF
     KKLCNVYREM CDQNPNLFAY NFREELRMRK LQGKTTEEGE EDDLQR