TFB1M_MOUSE
ID TFB1M_MOUSE Reviewed; 345 AA.
AC Q8JZM0;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 135.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=129;
RX PubMed=12068295; DOI=10.1038/ng909;
RA Falkenberg M., Gaspari M., Rantanen A., Trifunovic A., Larsson N.-G.,
RA Gustafsson C.M.;
RT "Mitochondrial transcription factors B1 and B2 activate transcription of
RT human mtDNA.";
RL Nat. Genet. 31:289-294(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary gland;
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).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=12532263; DOI=10.1007/s00335-002-2218-z;
RA Rantanen A., Gaspari M., Falkenberg M., Gustafsson C.M., Larsson N.-G.;
RT "Characterization of the mouse genes for mitochondrial transcription
RT factors B1 and B2.";
RL Mamm. Genome 14:1-6(2003).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH
RP S-ADENOSYL-L-METHIONINE.
RX PubMed=23804760; DOI=10.1093/nar/gkt547;
RA Guja K.E., Venkataraman K., Yakubovskaya E., Shi H., Mejia E.,
RA Hambardjieva E., Karzai A.W., Garcia-Diaz M.;
RT "Structural basis for S-adenosylmethionine binding and methyltransferase
RT activity by mitochondrial transcription factor B1.";
RL Nucleic Acids Res. 41:7947-7959(2013).
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 -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:12532263}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. rRNA adenine N(6)-methyltransferase family. KsgA
CC subfamily. {ECO:0000305}.
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DR EMBL; AF508971; AAM33651.1; -; mRNA.
DR EMBL; BC032930; AAH32930.1; -; mRNA.
DR CCDS; CCDS28363.1; -.
DR RefSeq; NP_666186.1; NM_146074.1.
DR PDB; 4GC5; X-ray; 1.80 A; A=1-345.
DR PDB; 4GC9; X-ray; 2.10 A; A=1-345.
DR PDBsum; 4GC5; -.
DR PDBsum; 4GC9; -.
DR AlphaFoldDB; Q8JZM0; -.
DR SMR; Q8JZM0; -.
DR BioGRID; 230274; 2.
DR STRING; 10090.ENSMUSP00000035291; -.
DR iPTMnet; Q8JZM0; -.
DR PhosphoSitePlus; Q8JZM0; -.
DR EPD; Q8JZM0; -.
DR MaxQB; Q8JZM0; -.
DR PaxDb; Q8JZM0; -.
DR PeptideAtlas; Q8JZM0; -.
DR PRIDE; Q8JZM0; -.
DR ProteomicsDB; 259017; -.
DR Antibodypedia; 33417; 209 antibodies from 28 providers.
DR DNASU; 224481; -.
DR Ensembl; ENSMUST00000041003; ENSMUSP00000035291; ENSMUSG00000036983.
DR GeneID; 224481; -.
DR KEGG; mmu:224481; -.
DR UCSC; uc008aes.1; mouse.
DR CTD; 51106; -.
DR MGI; MGI:2146851; Tfb1m.
DR VEuPathDB; HostDB:ENSMUSG00000036983; -.
DR eggNOG; KOG0821; Eukaryota.
DR GeneTree; ENSGT00950000183142; -.
DR HOGENOM; CLU_041220_7_0_1; -.
DR InParanoid; Q8JZM0; -.
DR OMA; RIEQPFK; -.
DR OrthoDB; 628543at2759; -.
DR PhylomeDB; Q8JZM0; -.
DR TreeFam; TF300798; -.
DR BioGRID-ORCS; 224481; 21 hits in 73 CRISPR screens.
DR ChiTaRS; Tfb1m; mouse.
DR PRO; PR:Q8JZM0; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q8JZM0; protein.
DR Bgee; ENSMUSG00000036983; Expressed in lumbar dorsal root ganglion and 244 other tissues.
DR Genevisible; Q8JZM0; MM.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0042645; C:mitochondrial nucleoid; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
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:MGI.
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 HAMAP; MF_00607; 16SrRNA_methyltr_A; 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 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Methyltransferase; Mitochondrion;
KW Reference proteome; RNA-binding; rRNA processing; S-adenosyl-L-methionine;
KW Transcription; 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_0000273173"
FT BINDING 35..38
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT BINDING 36
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 38
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 63
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 85
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:23804760"
FT BINDING 111
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:23804760"
FT BINDING 141
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT HELIX 18..30
FT /evidence="ECO:0007829|PDB:4GC5"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:4GC5"
FT HELIX 41..51
FT /evidence="ECO:0007829|PDB:4GC5"
FT STRAND 58..62
FT /evidence="ECO:0007829|PDB:4GC5"
FT TURN 65..67
FT /evidence="ECO:0007829|PDB:4GC5"
FT HELIX 68..74
FT /evidence="ECO:0007829|PDB:4GC5"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:4GC5"
FT STRAND 79..84
FT /evidence="ECO:0007829|PDB:4GC5"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:4GC5"
FT HELIX 91..100
FT /evidence="ECO:0007829|PDB:4GC5"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:4GC5"
FT STRAND 105..108
FT /evidence="ECO:0007829|PDB:4GC5"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:4GC5"
FT TURN 118..120
FT /evidence="ECO:0007829|PDB:4GC5"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:4GC5"
FT STRAND 135..140
FT /evidence="ECO:0007829|PDB:4GC5"
FT HELIX 144..160
FT /evidence="ECO:0007829|PDB:4GC5"
FT HELIX 163..167
FT /evidence="ECO:0007829|PDB:4GC5"
FT STRAND 171..177
FT /evidence="ECO:0007829|PDB:4GC5"
FT HELIX 178..185
FT /evidence="ECO:0007829|PDB:4GC5"
FT HELIX 195..201
FT /evidence="ECO:0007829|PDB:4GC5"
FT STRAND 204..212
FT /evidence="ECO:0007829|PDB:4GC5"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:4GC5"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:4GC5"
FT STRAND 225..232
FT /evidence="ECO:0007829|PDB:4GC5"
FT HELIX 242..253
FT /evidence="ECO:0007829|PDB:4GC5"
FT HELIX 260..264
FT /evidence="ECO:0007829|PDB:4GC5"
FT HELIX 265..267
FT /evidence="ECO:0007829|PDB:4GC5"
FT HELIX 270..272
FT /evidence="ECO:0007829|PDB:4GC5"
FT HELIX 273..284
FT /evidence="ECO:0007829|PDB:4GC5"
FT HELIX 292..294
FT /evidence="ECO:0007829|PDB:4GC5"
FT HELIX 297..313
FT /evidence="ECO:0007829|PDB:4GC5"
FT HELIX 317..319
FT /evidence="ECO:0007829|PDB:4GC5"
FT HELIX 322..326
FT /evidence="ECO:0007829|PDB:4GC5"
SQ SEQUENCE 345 AA; 38962 MW; 97BF51EC95328AD5 CRC64;
MAASGKLGTF RLPPLPTIRE IIKLFGLRAV KQLSQNFLLD LRLTDKIVRK AGSLADVYVY
EVGPGPGGIT RSILNANVAE LLVVEKDTRF IPGLQMLSDA APGKLRIVHG DVLTYKIEKA
FPGNIRRQWE DDPPNVHIIG NLPFSVSTPL IIKWLENISL KDGPFVYGRT KMTLTFQKEV
AERLVATTGS KQHSRLSIMA QYLCNVEHLF TIPGKAFVPK PKVDVGVVHL TPLIEPKIKQ
PFKLVEKVVQ NAFQFRRKYC HRGLGMLFPE AQRLESTGRL LQLADIDPTL RPTHLSLMHF
KSLCDVYRKM CDEDPQLFTY NFREELKQKK SKGQEKDGDP ESCGF
