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Protein

Mitochondrial transcription factor 1

Gene

MTF1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Mitochondrial transcription factor that confers selective promoter recognition on the core subunit of the yeast mitochondrial RNA polymerase. Interacts with DNA in a non-specific manner.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei23 – 231S-adenosyl-L-methionine; via amide nitrogenPROSITE-ProRule annotation
Binding sitei77 – 771S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei101 – 1011S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei137 – 1371S-adenosyl-L-methioninePROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

  • transcription initiation from mitochondrial promoter Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, RNA-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciYEAST:G3O-32909-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Mitochondrial transcription factor 1 (EC:2.1.1.-)
Alternative name(s):
Mitochondrial transcription factor mtTFB
Mitochondrial-specificity factor
RF1023
Gene namesi
Name:MTF1
Ordered Locus Names:YMR228W
ORF Names:YM9959.10
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIII

Organism-specific databases

EuPathDBiFungiDB:YMR228W.
SGDiS000004841. MTF1.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial DNA-directed RNA polymerase complex Source: SGD
  • mitochondrial intermembrane space Source: SGD
  • mitochondrial matrix Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 341340Mitochondrial transcription factor 1PRO_0000096621Add
BLAST

Proteomic databases

MaxQBiP14908.

PTM databases

iPTMnetiP14908.

Interactioni

Protein-protein interaction databases

BioGridi35406. 24 interactions.
DIPiDIP-1542N.
IntActiP14908. 1 interaction.
MINTiMINT-403802.

Structurei

Secondary structure

1
341
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi17 – 193Combined sources
Helixi26 – 3611Combined sources
Helixi38 – 403Combined sources
Turni45 – 473Combined sources
Beta strandi49 – 546Combined sources
Helixi59 – 6810Combined sources
Beta strandi71 – 766Combined sources
Helixi80 – 8910Combined sources
Turni90 – 923Combined sources
Beta strandi96 – 983Combined sources
Helixi105 – 1117Combined sources
Turni112 – 1154Combined sources
Beta strandi127 – 13711Combined sources
Helixi143 – 15614Combined sources
Helixi159 – 1635Combined sources
Beta strandi164 – 17310Combined sources
Helixi174 – 1818Combined sources
Helixi191 – 1999Combined sources
Beta strandi200 – 2089Combined sources
Helixi210 – 2156Combined sources
Helixi218 – 2247Combined sources
Helixi231 – 2333Combined sources
Beta strandi234 – 2363Combined sources
Beta strandi242 – 2498Combined sources
Helixi256 – 26712Combined sources
Turni268 – 2714Combined sources
Turni274 – 2763Combined sources
Helixi277 – 2804Combined sources
Helixi285 – 2895Combined sources
Turni290 – 2923Combined sources
Turni297 – 2993Combined sources
Helixi303 – 3053Combined sources
Helixi308 – 31912Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1I4WX-ray2.60A2-341[»]
ProteinModelPortaliP14908.
SMRiP14908. Positions 4-325.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14908.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi157 – 19640Arg/Lys-rich (basic)Add
BLAST
Compositional biasi209 – 23325Asp/Glu-rich (acidic)Add
BLAST
Compositional biasi246 – 26015Asp/Glu-rich (acidic)Add
BLAST

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. rRNA adenine N(6)-methyltransferase family.PROSITE-ProRule annotation

Phylogenomic databases

HOGENOMiHOG000074718.
InParanoidiP14908.
KOiK15267.
OMAiPRNHILI.
OrthoDBiEOG78PVKN.

Family and domain databases

Gene3Di1.10.8.100. 1 hit.
3.40.50.150. 1 hit.
InterProiIPR001737. KsgA/Erm.
IPR016586. Mtf1.
IPR023165. rRNA_Ade_diMease-like.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR11727. PTHR11727. 2 hits.
PfamiPF00398. RrnaAD. 1 hit.
[Graphical view]
PIRSFiPIRSF011649. MtTFB. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51689. SAM_RNA_A_N6_MT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P14908-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVPIPGIKD ISKLKFFYGF KYLWNPTVYN KIFDKLDLTK TYKHPEELKV
60 70 80 90 100
LDLYPGVGIQ SAIFYNKYCP RQYSLLEKRS SLYKFLNAKF EGSPLQILKR
110 120 130 140 150
DPYDWSTYSN LIDEERIFVP EVQSSDHIND KFLTVANVTG EGSEGLIMQW
160 170 180 190 200
LSCIGNKNWL YRFGKVKMLL WMPSTTARKL LARPGMHSRS KCSVVREAFT
210 220 230 240 250
DTKLIAISDA NELKGFDSQC IEEWDPILFS AAEIWPTKGK PIALVEMDPI
260 270 280 290 300
DFDFDVDNWD YVTRHLMILK RTPLNTVMDS LGHGGQQYFN SRITDKDLLK
310 320 330 340
KCPIDLTNDE FIYLTKLFME WPFKPDILMD FVDMYQTEHS G
Length:341
Mass (Da):39,727
Last modified:January 23, 2007 - v4
Checksum:iB579726EE318B0B7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti79 – 791R → S in CAA31864 (PubMed:2853292).Curated
Sequence conflicti287 – 2882QY → PI in CAA31864 (PubMed:2853292).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X13513 Genomic DNA. Translation: CAA31864.1.
Z49939 Genomic DNA. Translation: CAA90199.1.
BK006946 Genomic DNA. Translation: DAA10127.1.
PIRiS57595.
RefSeqiNP_013955.1. NM_001182735.1.

Genome annotation databases

EnsemblFungiiYMR228W; YMR228W; YMR228W.
GeneIDi855268.
KEGGisce:YMR228W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X13513 Genomic DNA. Translation: CAA31864.1.
Z49939 Genomic DNA. Translation: CAA90199.1.
BK006946 Genomic DNA. Translation: DAA10127.1.
PIRiS57595.
RefSeqiNP_013955.1. NM_001182735.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1I4WX-ray2.60A2-341[»]
ProteinModelPortaliP14908.
SMRiP14908. Positions 4-325.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35406. 24 interactions.
DIPiDIP-1542N.
IntActiP14908. 1 interaction.
MINTiMINT-403802.

PTM databases

iPTMnetiP14908.

Proteomic databases

MaxQBiP14908.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYMR228W; YMR228W; YMR228W.
GeneIDi855268.
KEGGisce:YMR228W.

Organism-specific databases

EuPathDBiFungiDB:YMR228W.
SGDiS000004841. MTF1.

Phylogenomic databases

HOGENOMiHOG000074718.
InParanoidiP14908.
KOiK15267.
OMAiPRNHILI.
OrthoDBiEOG78PVKN.

Enzyme and pathway databases

BioCyciYEAST:G3O-32909-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP14908.
PROiP14908.

Family and domain databases

Gene3Di1.10.8.100. 1 hit.
3.40.50.150. 1 hit.
InterProiIPR001737. KsgA/Erm.
IPR016586. Mtf1.
IPR023165. rRNA_Ade_diMease-like.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR11727. PTHR11727. 2 hits.
PfamiPF00398. RrnaAD. 1 hit.
[Graphical view]
PIRSFiPIRSF011649. MtTFB. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51689. SAM_RNA_A_N6_MT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A nuclear gene essential for mitochondrial replication suppresses a defect of mitochondrial transcription in Saccharomyces cerevisiae."
    Lisowsky T., Michaelis G.
    Mol. Gen. Genet. 214:218-223(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "The yeast mitochondrial RNA polymerase specificity factor, MTF1, is similar to bacterial sigma factors."
    Jang S.H., Jaehning J.A.
    J. Biol. Chem. 266:22671-22677(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-21, CHARACTERIZATION.
  5. "Assignment of a yeast protein necessary for mitochondrial transcription initiation."
    Xu B., Clayton D.A.
    Nucleic Acids Res. 20:1053-1059(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  6. "A point mutation in the core subunit gene of yeast mitochondrial RNA polymerase is suppressed by a high level of specificity factor MTF1."
    Riemen G., Michaelis G.
    Mol. Gen. Genet. 237:49-57(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "Crystal structure of the transcription factor sc-mtTFB offers insights into mitochondrial transcription."
    Schubot F.D., Chen C.J., Rose J.P., Dailey T.A., Dailey H.A., Wang B.-C.
    Protein Sci. 10:1980-1988(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).

Entry informationi

Entry nameiMTF1_YEAST
AccessioniPrimary (citable) accession number: P14908
Secondary accession number(s): D6W053
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 147 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 9380 molecules/cell in log phase SD medium.1 Publication
Although strongly related to dimethyladenosine transferase proteins, it lacks the methyltransferase activity. Dimethyladenosine transferase methylates the 2 adjacent adenosines in the loop of a conserved hairpin near the 3'-end of 12S mitochondrial rRNA in most species. This explains why 12S rRNA is not methylated in S.cerevisiae.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XIII
    Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.