MTF1_YEAST
ID MTF1_YEAST Reviewed; 341 AA.
AC P14908; D6W053;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Mitochondrial transcription factor 1;
DE EC=2.1.1.-;
DE AltName: Full=Mitochondrial transcription factor mtTFB;
DE AltName: Full=Mitochondrial-specificity factor;
DE AltName: Full=RF1023;
GN Name=MTF1; OrderedLocusNames=YMR228W; ORFNames=YM9959.10;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2853292; DOI=10.1007/bf00337714;
RA Lisowsky T., Michaelis G.;
RT "A nuclear gene essential for mitochondrial replication suppresses a defect
RT of mitochondrial transcription in Saccharomyces cerevisiae.";
RL Mol. Gen. Genet. 214:218-223(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP PROTEIN SEQUENCE OF 2-21, AND CHARACTERIZATION.
RX PubMed=1939277; DOI=10.1016/s0021-9258(18)54622-6;
RA Jang S.H., Jaehning J.A.;
RT "The yeast mitochondrial RNA polymerase specificity factor, MTF1, is
RT similar to bacterial sigma factors.";
RL J. Biol. Chem. 266:22671-22677(1991).
RN [5]
RP CHARACTERIZATION.
RX PubMed=1549466; DOI=10.1093/nar/20.5.1053;
RA Xu B., Clayton D.A.;
RT "Assignment of a yeast protein necessary for mitochondrial transcription
RT initiation.";
RL Nucleic Acids Res. 20:1053-1059(1992).
RN [6]
RP CHARACTERIZATION.
RX PubMed=8384295; DOI=10.1007/bf00282783;
RA Riemen G., Michaelis G.;
RT "A point mutation in the core subunit gene of yeast mitochondrial RNA
RT polymerase is suppressed by a high level of specificity factor MTF1.";
RL Mol. Gen. Genet. 237:49-57(1993).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16823961; DOI=10.1021/pr050477f;
RA Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A.;
RT "Toward the complete yeast mitochondrial proteome: multidimensional
RT separation techniques for mitochondrial proteomics.";
RL J. Proteome Res. 5:1543-1554(2006).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=22984289; DOI=10.1074/mcp.m112.021105;
RA Voegtle F.N., Burkhart J.M., Rao S., Gerbeth C., Hinrichs J.,
RA Martinou J.C., Chacinska A., Sickmann A., Zahedi R.P., Meisinger C.;
RT "Intermembrane space proteome of yeast mitochondria.";
RL Mol. Cell. Proteomics 11:1840-1852(2012).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RX PubMed=11567089; DOI=10.1110/ps.11201;
RA Schubot F.D., Chen C.J., Rose J.P., Dailey T.A., Dailey H.A., Wang B.-C.;
RT "Crystal structure of the transcription factor sc-mtTFB offers insights
RT into mitochondrial transcription.";
RL Protein Sci. 10:1980-1988(2001).
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.
CC -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space
CC {ECO:0000269|PubMed:16823961, ECO:0000269|PubMed:22984289}.
CC -!- MISCELLANEOUS: Present with 9380 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: Although strongly related to dimethyladenosine
CC transferase proteins, it lacks the methyltransferase activity.
CC Dimethyladenosine transferase methylates the 2 adjacent adenosines in
CC the loop of a conserved hairpin near the 3'-end of 12S mitochondrial
CC rRNA in most species. This explains why 12S rRNA is not methylated in
CC S.cerevisiae.
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; X13513; CAA31864.1; -; Genomic_DNA.
DR EMBL; Z49939; CAA90199.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10127.1; -; Genomic_DNA.
DR PIR; S57595; S57595.
DR RefSeq; NP_013955.1; NM_001182735.1.
DR PDB; 1I4W; X-ray; 2.60 A; A=2-341.
DR PDB; 6YMV; EM; 3.10 A; B=2-341.
DR PDB; 6YMW; EM; 3.71 A; B=2-341.
DR PDBsum; 1I4W; -.
DR PDBsum; 6YMV; -.
DR PDBsum; 6YMW; -.
DR AlphaFoldDB; P14908; -.
DR SASBDB; P14908; -.
DR SMR; P14908; -.
DR BioGRID; 35406; 36.
DR ComplexPortal; CPX-3146; Mitochondrial DNA-directed RNA polymerase complex.
DR DIP; DIP-1542N; -.
DR IntAct; P14908; 1.
DR MINT; P14908; -.
DR STRING; 4932.YMR228W; -.
DR iPTMnet; P14908; -.
DR MaxQB; P14908; -.
DR PaxDb; P14908; -.
DR PRIDE; P14908; -.
DR EnsemblFungi; YMR228W_mRNA; YMR228W; YMR228W.
DR GeneID; 855268; -.
DR KEGG; sce:YMR228W; -.
DR SGD; S000004841; MTF1.
DR VEuPathDB; FungiDB:YMR228W; -.
DR eggNOG; ENOG502QY7G; Eukaryota.
DR HOGENOM; CLU_034228_0_0_1; -.
DR InParanoid; P14908; -.
DR OMA; CKLSVIA; -.
DR BioCyc; YEAST:G3O-32909-MON; -.
DR EvolutionaryTrace; P14908; -.
DR PRO; PR:P14908; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P14908; protein.
DR GO; GO:0034245; C:mitochondrial DNA-directed RNA polymerase complex; IDA:SGD.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:SGD.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
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; IDA:SGD.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006390; P:mitochondrial transcription; IDA:ComplexPortal.
DR GO; GO:0032786; P:positive regulation of DNA-templated transcription, elongation; IMP:SGD.
DR GO; GO:0006391; P:transcription initiation from mitochondrial promoter; IDA:SGD.
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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; DNA-binding; Methyltransferase;
KW Mitochondrion; Reference proteome; RNA-binding; S-adenosyl-L-methionine;
KW Transcription; Transcription regulation; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1939277"
FT CHAIN 2..341
FT /note="Mitochondrial transcription factor 1"
FT /id="PRO_0000096621"
FT BINDING 23
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT BINDING 77
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT BINDING 101
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT BINDING 137
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT CONFLICT 79
FT /note="R -> S (in Ref. 1; CAA31864)"
FT /evidence="ECO:0000305"
FT CONFLICT 287..288
FT /note="QY -> PI (in Ref. 1; CAA31864)"
FT /evidence="ECO:0000305"
FT HELIX 8..11
FT /evidence="ECO:0007829|PDB:6YMV"
FT HELIX 17..19
FT /evidence="ECO:0007829|PDB:1I4W"
FT HELIX 26..36
FT /evidence="ECO:0007829|PDB:1I4W"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:1I4W"
FT TURN 45..47
FT /evidence="ECO:0007829|PDB:1I4W"
FT STRAND 49..54
FT /evidence="ECO:0007829|PDB:1I4W"
FT HELIX 59..68
FT /evidence="ECO:0007829|PDB:1I4W"
FT STRAND 71..76
FT /evidence="ECO:0007829|PDB:1I4W"
FT HELIX 80..89
FT /evidence="ECO:0007829|PDB:1I4W"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:1I4W"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:1I4W"
FT HELIX 105..111
FT /evidence="ECO:0007829|PDB:1I4W"
FT TURN 112..115
FT /evidence="ECO:0007829|PDB:1I4W"
FT STRAND 127..137
FT /evidence="ECO:0007829|PDB:1I4W"
FT HELIX 143..156
FT /evidence="ECO:0007829|PDB:1I4W"
FT HELIX 159..163
FT /evidence="ECO:0007829|PDB:1I4W"
FT STRAND 164..173
FT /evidence="ECO:0007829|PDB:1I4W"
FT HELIX 174..181
FT /evidence="ECO:0007829|PDB:1I4W"
FT HELIX 191..199
FT /evidence="ECO:0007829|PDB:1I4W"
FT STRAND 200..208
FT /evidence="ECO:0007829|PDB:1I4W"
FT HELIX 210..215
FT /evidence="ECO:0007829|PDB:1I4W"
FT HELIX 218..224
FT /evidence="ECO:0007829|PDB:1I4W"
FT HELIX 231..233
FT /evidence="ECO:0007829|PDB:1I4W"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:1I4W"
FT STRAND 242..249
FT /evidence="ECO:0007829|PDB:1I4W"
FT HELIX 256..267
FT /evidence="ECO:0007829|PDB:1I4W"
FT TURN 268..271
FT /evidence="ECO:0007829|PDB:1I4W"
FT TURN 274..276
FT /evidence="ECO:0007829|PDB:1I4W"
FT HELIX 277..280
FT /evidence="ECO:0007829|PDB:1I4W"
FT HELIX 285..289
FT /evidence="ECO:0007829|PDB:1I4W"
FT TURN 290..292
FT /evidence="ECO:0007829|PDB:1I4W"
FT TURN 297..299
FT /evidence="ECO:0007829|PDB:1I4W"
FT HELIX 303..305
FT /evidence="ECO:0007829|PDB:1I4W"
FT HELIX 308..319
FT /evidence="ECO:0007829|PDB:1I4W"
FT STRAND 327..329
FT /evidence="ECO:0007829|PDB:6YMV"
SQ SEQUENCE 341 AA; 39727 MW; B579726EE318B0B7 CRC64;
MSVPIPGIKD ISKLKFFYGF KYLWNPTVYN KIFDKLDLTK TYKHPEELKV LDLYPGVGIQ
SAIFYNKYCP RQYSLLEKRS SLYKFLNAKF EGSPLQILKR DPYDWSTYSN LIDEERIFVP
EVQSSDHIND KFLTVANVTG EGSEGLIMQW LSCIGNKNWL YRFGKVKMLL WMPSTTARKL
LARPGMHSRS KCSVVREAFT DTKLIAISDA NELKGFDSQC IEEWDPILFS AAEIWPTKGK
PIALVEMDPI DFDFDVDNWD YVTRHLMILK RTPLNTVMDS LGHGGQQYFN SRITDKDLLK
KCPIDLTNDE FIYLTKLFME WPFKPDILMD FVDMYQTEHS G
