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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}.
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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
 
 
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