TFB1M_PONAB
ID TFB1M_PONAB Reviewed; 343 AA.
AC Q5R4V9;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 78.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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; CR861132; CAH93207.1; -; mRNA.
DR RefSeq; NP_001126887.1; NM_001133415.1.
DR AlphaFoldDB; Q5R4V9; -.
DR SMR; Q5R4V9; -.
DR STRING; 9601.ENSPPYP00000019173; -.
DR GeneID; 100173901; -.
DR KEGG; pon:100173901; -.
DR CTD; 51106; -.
DR eggNOG; KOG0821; Eukaryota.
DR InParanoid; Q5R4V9; -.
DR OrthoDB; 628543at2759; -.
DR Proteomes; UP000001595; Unplaced.
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; 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..343
FT /note="Dimethyladenosine transferase 1, mitochondrial"
FT /id="PRO_0000273174"
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 343 AA; 39083 MW; 58B4301C983FBB95 CRC64;
MAASGKLSTW RLPPLPTIRE IIKLLRVQAA KQLSQNFLLD LRLTDKIVRK AGNLTNAYVY
EVGPGPGGIT RSILNADVAE LLVVEKDTRF VPGLQMLSDA APGKLRIVHG DVLTFKVEKA
FSESLKRPWE DDPPDVHIIG NLPFSVSTPL IIKWLENISC RDGPFVYGRT QMTLTFQKEV
AERLAANTGS KQRSRLSVMA QYLCNVRHIF TIPGRAFVPK PEVDVGVVHF TPLIQPKIEQ
PFKLVEKVVQ NVFQFRRKYC HRGLRMLFPE AQRLESTGRL LELADVDPTL RPCQPSISHF
KSLCDVYRKM CDEDPQLFAY NFREELKQRK SKNEEKEEDD AEN
