TFB1M_RAT
ID TFB1M_RAT Reviewed; 345 AA.
AC Q811P6; Q6IRI6;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 106.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=New England Deaconess Hospital;
RA Antinozzi P.A.;
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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; AY198392; AAO42744.1; -; mRNA.
DR EMBL; BC070907; AAH70907.1; -; mRNA.
DR RefSeq; NP_852139.2; NM_181474.2.
DR AlphaFoldDB; Q811P6; -.
DR SMR; Q811P6; -.
DR STRING; 10116.ENSRNOP00000022397; -.
DR PaxDb; Q811P6; -.
DR PRIDE; Q811P6; -.
DR GeneID; 308140; -.
DR KEGG; rno:308140; -.
DR UCSC; RGD:727795; rat.
DR CTD; 51106; -.
DR RGD; 727795; Tfb1m.
DR eggNOG; KOG0821; Eukaryota.
DR InParanoid; Q811P6; -.
DR OrthoDB; 628543at2759; -.
DR PhylomeDB; Q811P6; -.
DR TreeFam; TF300798; -.
DR PRO; PR:Q811P6; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0042645; C:mitochondrial nucleoid; ISO:RGD.
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; ISO:RGD.
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; 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_0000273175"
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"
FT CONFLICT 343
FT /note="W -> C (in Ref. 2; AAH70907)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 345 AA; 39181 MW; 49877D17E79BB91A CRC64;
MAASGKLGTF RLPPLPTIRE IIKLFGLRAA KQLSQNFLLD LRLTDKIVRK AGSLADVYVY
EVGPGPGGIT RSILNADIAE LLVVEKDTRF IPGLQMLSDA APGKLRIVHG DVLTYKIEKA
FPDNIRRQWE DDPPNVHIIG NLPFSVSTPL IIKWLENISL KNGPFVYGRT KMTLTFQKEV
AERLVATTGS KQRSRLSIMA QYLCNVEHLF TIPGKAFVPK PEVDVGVVHL MPLVQPKIKQ
PFKLVEKVVQ NVFQFRRKYC HRGLGMLFPE AQRLESTGRL LQLADIDPTL RPTHLSLMHF
KSLCDVYRKM CDEDPQLFAY NFREELKQKK RKGQEKDGDS ESWGF
