MTF1_LACKL
ID MTF1_LACKL Reviewed; 338 AA.
AC P87292;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Mitochondrial transcription factor 1;
DE EC=2.1.1.-;
DE AltName: Full=Mitochondrial transcription factor mtTFB;
GN Name=MTF1;
OS Lachancea kluyveri (Yeast) (Saccharomyces kluyveri).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=4934;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 22512 / NRRL Y-4288-3;
RX PubMed=9196077;
RA Carrodeguas J.A., Yun S., Shadel G.S., Clayton D.A., Bogenhagen D.F.;
RT "Functional conservation of yeast mtTFB despite extensive sequence
RT divergence.";
RL Gene Expr. 6:219-230(1996).
CC -!- FUNCTION: Mitochondrial transcription factor that confers selective
CC promoter recognition on the core subunit of the yeast mitochondrial RNA
CC polymerase. Interacts with DNA in a non-specific manner (By
CC 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.
CC {ECO:0000255|PROSITE-ProRule:PRU01026}.
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DR EMBL; U81619; AAC49738.1; -; Genomic_DNA.
DR AlphaFoldDB; P87292; -.
DR SMR; P87292; -.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0034246; F:mitochondrial transcription factor activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006391; P:transcription initiation from mitochondrial promoter; IEA:InterPro.
DR Gene3D; 1.10.8.100; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR001737; KsgA/Erm.
DR InterPro; IPR016586; Mtf1.
DR InterPro; IPR023165; rRNA_Ade_diMease-like_C.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR11727; PTHR11727; 1.
DR Pfam; PF00398; RrnaAD; 1.
DR PIRSF; PIRSF011649; MtTFB; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51689; SAM_RNA_A_N6_MT; 1.
PE 3: Inferred from homology;
KW DNA-binding; Methyltransferase; Mitochondrion; RNA-binding;
KW S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..338
FT /note="Mitochondrial transcription factor 1"
FT /id="PRO_0000096620"
FT BINDING 23
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT BINDING 76
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT BINDING 100
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT BINDING 136
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
SQ SEQUENCE 338 AA; 39204 MW; 96E72A785B317A33 CRC64;
MSVHIPTLNS ATKIKHYYGF KYLLNSSVHT QIYNKLQLQS TYKMDELKVL DLYPGPSQHS
AIFRNIFNPK QYVLMDSRPD FVKFIQDNFA GTSMELYQRD PYEWSSYTDM IEKEKRFVPN
RQSRDKIHNQ FLVMANLTGM IGEGLFMQWL SCIGNKNWLQ RFGRVKMLVW VPEATAHKVL
ARPGSLIRAK CSVVTEAFTD TKLVATSDSS TLQKFSSSLL EGHDPIIFST RDTWLNSGKP
ISLLEVNPID HDIDLDNWDY VTKHLLILKS TPLHTAIDSL GHGGKQYFSE KVEDKLLMDK
CPKDLTNKEF VYLTSIFNNW PFKPDIYMDF IDVFQENE
