MTF1_SCHPO
ID MTF1_SCHPO Reviewed; 366 AA.
AC Q9US51;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Mitochondrial transcription factor 1;
DE EC=2.1.1.-;
GN Name=mtf1; ORFNames=SPAC1002.08c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3]
RP FUNCTION.
RX PubMed=21357609; DOI=10.1093/nar/gkr103;
RA Jiang H., Sun W., Wang Z., Zhang J., Chen D., Murchie A.I.;
RT "Identification and characterization of the mitochondrial RNA polymerase
RT and transcription factor in the fission yeast Schizosaccharomyces pombe.";
RL Nucleic Acids Res. 39:5119-5130(2011).
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 {ECO:0000269|PubMed:21357609}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:16823372}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU329670; CAB65608.1; -; Genomic_DNA.
DR RefSeq; NP_593495.1; NM_001018929.2.
DR AlphaFoldDB; Q9US51; -.
DR SMR; Q9US51; -.
DR BioGRID; 279699; 4.
DR STRING; 4896.SPAC1002.08c.1; -.
DR MaxQB; Q9US51; -.
DR PaxDb; Q9US51; -.
DR EnsemblFungi; SPAC1002.08c.1; SPAC1002.08c.1:pep; SPAC1002.08c.
DR GeneID; 2543271; -.
DR KEGG; spo:SPAC1002.08c; -.
DR PomBase; SPAC1002.08c; mtf1.
DR VEuPathDB; FungiDB:SPAC1002.08c; -.
DR eggNOG; ENOG502QY7G; Eukaryota.
DR HOGENOM; CLU_034228_0_0_1; -.
DR InParanoid; Q9US51; -.
DR OMA; CKLSVIA; -.
DR PhylomeDB; Q9US51; -.
DR PRO; PR:Q9US51; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0034245; C:mitochondrial DNA-directed RNA polymerase complex; IDA:PomBase.
DR GO; GO:0005759; C:mitochondrial matrix; ISO:PomBase.
DR GO; GO:0005739; C:mitochondrion; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016433; F:rRNA (adenine) methyltransferase activity; ISM:PomBase.
DR GO; GO:0006390; P:mitochondrial transcription; EXP:PomBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:PomBase.
DR GO; GO:0006391; P:transcription initiation from mitochondrial promoter; IMP:PomBase.
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; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR11727; PTHR11727; 1.
DR Pfam; PF00398; RrnaAD; 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; Reference proteome;
KW RNA-binding; S-adenosyl-L-methionine; Transcription;
KW Transcription regulation; Transferase.
FT CHAIN 1..366
FT /note="Mitochondrial transcription factor 1"
FT /id="PRO_0000316606"
FT BINDING 38
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT BINDING 91
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT BINDING 117
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
SQ SEQUENCE 366 AA; 41198 MW; 29923DDD861B75E3 CRC64;
MKLPKILYDA AAFGGPRSTG FVKILNLNGR SSYKSSYLVN QNLMDEALVK SNLLKEYNSE
KMTILEMAPG PGVTTTSLFN YFQPKSHVVL ESREVFSKPL QKLCTLSDGR IKWVHQDGYY
WQTYEDVYVS KVLDPRIQTE EEQKLSPHRE LLFFAHLPHG YAGLLFVSQI LDFLSARDWL
GIFGRVRVLL WLPCSPTVTL LGSRGFSKRS KTSVFREAFT DSRVLAASES TLQKLCMGYS
KEAKENYQIS PNPLLVSPTP ITSEPHKEDL TLVEMCSKPQ DKQLSIPVFE SIVRILLTCK
ATSLSKSIYY LGPGAETLLP SFTQCGINID MPVGLLSAAD FLTISKIIQK YPFKHHLHLG
TIIEDS