TFB1M_CAEEL
ID TFB1M_CAEEL Reviewed; 367 AA.
AC P91424;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 136.
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 AltName: Full=S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase 1;
DE Flags: Precursor;
GN Name=tfbm-1; ORFNames=T03F1.7;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Probable S-adenosyl-L-methionine-dependent methyltransferase
CC which specifically dimethylates mitochondrial 12S rRNA at the conserved
CC stem 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FO080917; CCD67792.1; -; Genomic_DNA.
DR PIR; T29195; T29195.
DR RefSeq; NP_491242.2; NM_058841.6.
DR AlphaFoldDB; P91424; -.
DR SMR; P91424; -.
DR BioGRID; 52696; 1.
DR STRING; 6239.T03F1.7; -.
DR EPD; P91424; -.
DR PaxDb; P91424; -.
DR PeptideAtlas; P91424; -.
DR EnsemblMetazoa; T03F1.7.1; T03F1.7.1; WBGene00020189.
DR GeneID; 188022; -.
DR KEGG; cel:CELE_T03F1.7; -.
DR UCSC; T03F1.7; c. elegans.
DR CTD; 188022; -.
DR WormBase; T03F1.7; CE30685; WBGene00020189; tfbm-1.
DR eggNOG; KOG0821; Eukaryota.
DR GeneTree; ENSGT00950000183142; -.
DR HOGENOM; CLU_041220_7_0_1; -.
DR InParanoid; P91424; -.
DR OMA; RIEQPFK; -.
DR OrthoDB; 628543at2759; -.
DR PhylomeDB; P91424; -.
DR PRO; PR:P91424; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00020189; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
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; 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 3: Inferred from homology;
KW Methyltransferase; Mitochondrion; Reference proteome; RNA-binding;
KW rRNA processing; S-adenosyl-L-methionine; Transcription;
KW Transcription regulation; Transferase; Transit peptide.
FT TRANSIT 1..16
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 17..367
FT /note="Dimethyladenosine transferase 1, mitochondrial"
FT /id="PRO_0000273182"
FT BINDING 30..33
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 31
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT BINDING 33
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT BINDING 58
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT BINDING 80
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT BINDING 106
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 367 AA; 41893 MW; FD2419FC6548F1BC CRC64;
MASASRLPPL PALRDFIHMY RLRAKKILSQ NYLMDMNITR KIAKHAKVIE KDWVIEIGPG
PGGITRAILE AGASRLDVVE IDNRFIPPLQ HLAEAADSRM FIHHQDALRT EIGDIWKNET
ARPESVDWHD SNLPAMHVIG NLPFNIASPL IIKYLRDMSY RRGVWQYGRV PLTLTFQLEV
AKRLCSPIAC DTRSRISIMS QYVAEPKMVF QISGSCFVPR PQVDVGVVRF VPRKTPLVNT
SFEVLEKVCR QVFHYRQKYV TKGLKTLYPE ELEDELSDDL LKKCRIDPTT TSIRLGIEQF
ADLAEGYNEQ CIRYPGLFLY DYTNKLHNLE DLSKEPNALP PPVPIFAPAP TIDSADNTWS
LKNFNCS
