TFB1M_DROPS
ID TFB1M_DROPS Reviewed; 337 AA.
AC Q2LZ79;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 76.
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=mtTFB1; ORFNames=GA20255;
OS Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=46245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MV2-25 / Tucson 14011-0121.94;
RX PubMed=15632085; DOI=10.1101/gr.3059305;
RA Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA Weinstock G.M., Gibbs R.A.;
RT "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT gene, and cis-element evolution.";
RL Genome Res. 15:1-18(2005).
CC -!- FUNCTION: Probable S-adenosyl-L-methionine-dependent methyltransferase
CC which specifically dimethylates mitochondrial 12S rRNA at the conserved
CC stem loop. {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; CH379069; EAL29629.2; -; Genomic_DNA.
DR RefSeq; XP_001353894.2; XM_001353858.3.
DR AlphaFoldDB; Q2LZ79; -.
DR SMR; Q2LZ79; -.
DR STRING; 7237.FBpp0274186; -.
DR PRIDE; Q2LZ79; -.
DR EnsemblMetazoa; FBtr0275748; FBpp0274186; FBgn0080250.
DR GeneID; 4813779; -.
DR KEGG; dpo:Dpse_GA20255; -.
DR eggNOG; KOG0821; Eukaryota.
DR HOGENOM; CLU_041220_7_0_1; -.
DR InParanoid; Q2LZ79; -.
DR OMA; RIEQPFK; -.
DR Proteomes; UP000001819; Chromosome X.
DR Bgee; FBgn0080250; Expressed in female reproductive system and 2 other tissues.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR GO; GO:0034246; F:mitochondrial transcription factor activity; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000179; F:rRNA (adenine-N6,N6-)-dimethyltransferase activity; IEA:InterPro.
DR GO; GO:0006390; P:mitochondrial transcription; ISS:UniProtKB.
DR GO; GO:0006417; P:regulation of translation; IEA:EnsemblMetazoa.
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; Transferase; Transit peptide.
FT TRANSIT 1..84
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 85..337
FT /note="Dimethyladenosine transferase 1, mitochondrial"
FT /id="PRO_0000273184"
FT BINDING 38..41
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 39
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT BINDING 41
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT BINDING 67
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT BINDING 89
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT BINDING 118
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT BINDING 140
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
SQ SEQUENCE 337 AA; 38581 MW; 236CCA329B06C531 CRC64;
MSQVTARVLN SGMRLPPLPT IRELVKLYKL QAMKQLSQNF LMDERLTDKI VKSAGRIDPR
DIVLEVGPGP GGITRSILRR QPQRLILVEK DRRFGETLQL LRECASPLDM QVDIYYDDIL
RFNIEQHIPD TTQRIHLIGN LPFSISTRLL INWYADLAAR RGAFRRNDTC MTLTFQKEVA
ERICAPVGSE QRCRLSVMSQ IWTEPVMKFI IPGKAFVPKP QVDVGVVKLI PLKQPKTQLP
FSLVERVVRH IFSMRQKYCR RGYGTLLPPD SREETTQTLF QRADVRDTLR SFELSVPQCL
RLADAYAEYI KEHPEVEAYD YRGPKNPDVS GAAAASS
