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Database: UniProt
Entry: A0A0F8DFA1_CERFI
LinkDB: A0A0F8DFA1_CERFI
Original site: A0A0F8DFA1_CERFI 
ID   A0A0F8DFA1_CERFI        Unreviewed;       922 AA.
AC   A0A0F8DFA1;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=rRNA adenine N(6)-methyltransferase {ECO:0000256|RuleBase:RU362106};
DE            EC=2.1.1.- {ECO:0000256|RuleBase:RU362106};
GN   ORFNames=CFO_g3022 {ECO:0000313|EMBL:KKF94639.1};
OS   Ceratocystis fimbriata f. sp. platani.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Microascales; Ceratocystidaceae; Ceratocystis.
OX   NCBI_TaxID=88771 {ECO:0000313|EMBL:KKF94639.1, ECO:0000313|Proteomes:UP000034841};
RN   [1] {ECO:0000313|EMBL:KKF94639.1, ECO:0000313|Proteomes:UP000034841}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFO {ECO:0000313|EMBL:KKF94639.1,
RC   ECO:0000313|Proteomes:UP000034841};
RA   Belbahri L.;
RT   "Genome sequence of Ceratocystis platani, a major pathogen of plane
RT   trees.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU362106}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KKF94639.1}.
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DR   EMBL; LBBL01000146; KKF94639.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F8DFA1; -.
DR   Proteomes; UP000034841; Unassembled WGS sequence.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
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; IPR017956; AT_hook_DNA-bd_motif.
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   SMART; SM00384; AT_hook; 7.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000256|RuleBase:RU362106};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034841};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW   rRNA processing {ECO:0000256|RuleBase:RU362106};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|RuleBase:RU362106};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362106}.
FT   REGION          285..312
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          411..622
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        417..445
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        446..562
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        569..622
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   922 AA;  106443 MW;  32817FF11F6AFE6E CRC64;
     MATGRPTQKL ATHHVRITNE ISKWLYESGL YRVTSSKAST KKPPPKVEKN RVHIINEEFV
     DQIITYLGDS LDRHKGCDLL DINPGVGIWS KALHKVLEPR KHIMMEPDGD FYAEHLKPLT
     DKPNVEIVHK HGVIWDDVYS TLDMLPEQKP VPRTGPVERN DTLLITMNLG TYPKKKYQSY
     ESVSALILHQ IMTSVRTRSM FQKYGLVRML VWTNDEEKRA YIPKNIFSRR RAAIDTEAAL
     EYIHEVVGSD DMSSETRANL IQLRQPTRLM ALQLESGRVV AEKMKKAGRV YPKDRQSDIT
     KQLEKNTPEE RRKDQEYIDR IISGLIKRRE YITEYEKQYP KPEPADMQEN DPTNYFLAGD
     LVKFRSKFFM TLPDNETGLV SKKPQLYGIS KPRDAPRRLI DNEEVEALKR LAEVEGTDEM
     DEDENEEEDI EKEIEQEEEE EEGEGEEEVK PKKRSRSKKI VEAKEDPEEE AKPKRRSRSK
     KAAEAEEDAE EEAKPKRRSR SKKAVEAEED AEEEAKPKRR SRSKKATEVE EDAGEEAKPK
     RRSRSKKAAE VAEQEEVEAK PAKRRGRKKK AALEAEETGE EEEPKPKRCS HSKNAVEISK
     ETESNSDGSK PEKPKRGRPT RAAVLAKEQE RDELLQKLQE EAAKAQVVTK PQPQPQEEQG
     VQAAEVLDRS ALTVPRSTRY MPAPPSPTAI VKQIFGPNYK GTVRDIREWL ARAYNQMWVE
     LREKYRSGEY TMEQYMEGHK LLNDEINLSH INYIATTRLH VDEHHCFNQD EPVLLWDRRE
     YEPLITKPHD VFPDVPMTLL DIQPKSMHPL LRDNVNQACL VFDVLTMAMI NSSGEMGKLL
     DKMWPGAADG CLPNMPEAVN LKRYGIPIEV KGTAITTMTG RRMNQEQYYE MLEAWQKWPF
     RPTYAQLICH HTEEPPNVPD QE
//
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