ID B6K3U8_SCHJY Unreviewed; 366 AA.
AC B6K3U8;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=rRNA adenine N(6)-methyltransferase {ECO:0000256|RuleBase:RU362106};
DE EC=2.1.1.- {ECO:0000256|RuleBase:RU362106};
GN Name=mtf1 {ECO:0000313|JaponicusDB:SJAG_03289};
GN ORFNames=SJAG_03289 {ECO:0000313|EMBL:EEB08155.1};
OS Schizosaccharomyces japonicus (strain yFS275 / FY16936) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=402676 {ECO:0000313|EMBL:EEB08155.1, ECO:0000313|Proteomes:UP000001744};
RN [1] {ECO:0000313|EMBL:EEB08155.1, ECO:0000313|Proteomes:UP000001744}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=yFS275 / FY16936 {ECO:0000313|Proteomes:UP000001744};
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(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:0000256|ARBA:ARBA00024915}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. rRNA adenine N(6)-methyltransferase family.
CC {ECO:0000256|PROSITE-ProRule:PRU01026, ECO:0000256|RuleBase:RU362106}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01026}.
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DR EMBL; KE651167; EEB08155.1; -; Genomic_DNA.
DR RefSeq; XP_002174448.1; XM_002174412.2.
DR AlphaFoldDB; B6K3U8; -.
DR STRING; 402676.B6K3U8; -.
DR EnsemblFungi; EEB08155; EEB08155; SJAG_03289.
DR GeneID; 7052459; -.
DR JaponicusDB; SJAG_03289; mtf1.
DR VEuPathDB; FungiDB:SJAG_03289; -.
DR eggNOG; ENOG502QY7G; Eukaryota.
DR HOGENOM; CLU_034228_0_0_1; -.
DR OMA; WDYVTKH; -.
DR OrthoDB; 2719760at2759; -.
DR Proteomes; UP000001744; Unassembled WGS sequence.
DR GO; GO:0000785; C:chromatin; IEA:EnsemblFungi.
DR GO; GO:0034245; C:mitochondrial DNA-directed RNA polymerase complex; IEA:EnsemblFungi.
DR GO; GO:0005634; C:nucleus; IEA:EnsemblFungi.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000179; F:rRNA (adenine-N6,N6-)-dimethyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:EnsemblFungi.
DR GO; GO:0006391; P:transcription initiation at mitochondrial promoter; IEA:EnsemblFungi.
DR Gene3D; 1.10.8.100; Ribosomal RNA adenine dimethylase-like, domain 2; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR001737; KsgA/Erm.
DR InterPro; IPR023165; rRNA_Ade_diMease-like_C.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR11727; DIMETHYLADENOSINE TRANSFERASE; 1.
DR PANTHER; PTHR11727:SF17; DIMETHYLADENOSINE TRANSFERASE 1, MITOCHONDRIAL; 1.
DR Pfam; PF00398; RrnaAD; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51689; SAM_RNA_A_N6_MT; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01026}; Reference proteome {ECO:0000313|Proteomes:UP000001744};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU01026}; rRNA processing {ECO:0000256|RuleBase:RU362106};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PROSITE-ProRule:PRU01026};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU01026}.
FT BINDING 41
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT BINDING 94
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT BINDING 120
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
SQ SEQUENCE 366 AA; 41523 MW; 3636CE502575B51C CRC64;
MTFKRLPSLT KTVLEQLKPL KLHRKDSQTQ VSHFKHVSSY LIKDELLSSV LEASGLKNAY
DNEDMTILEM SPGSGANSIA LYNYFQPKRH VLLEPRKAFF SHISSLTKNT DGRMVLHERD
GYSWATYSEL YQKHPEYFYQ QTSKEVRLGP NRRFLFTGHL PAGTPGILLG TQFVMHLIQR
DWLGILGRVR LLLWMSPELA YILLACNGYK SRSSLSVLRE LMCQIRVLAA PVEFMDTLKK
GYLHSSAVTY PVMKTISTTD EAFAPSANPL VLIDISCTSY QSDVPLDILE YVIQSLLVQK
SQPLKETVSR LCPGAENLVP LLKKRGVDIQ ESSVTASAKS LENIARIYHK WPFRPKVMTS
TLLEKP
//
