ID A0A1V8UQF2_9PEZI Unreviewed; 1176 AA.
AC A0A1V8UQF2;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=DNA (cytosine-5-)-methyltransferase {ECO:0000256|ARBA:ARBA00011975};
DE EC=2.1.1.37 {ECO:0000256|ARBA:ARBA00011975};
GN ORFNames=B0A51_06283 {ECO:0000313|EMBL:OQO25959.1};
OS Rachicladosporium sp. CCFEE 5018.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Cladosporiales; Cladosporiaceae; Rachicladosporium.
OX NCBI_TaxID=1974281 {ECO:0000313|EMBL:OQO25959.1, ECO:0000313|Proteomes:UP000192386};
RN [1] {ECO:0000313|Proteomes:UP000192386}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCFEE 5018 {ECO:0000313|Proteomes:UP000192386};
RA Coleine C., Masonjones S., Stajich J.E.;
RT "Genomes of endolithic fungi from Antarctica.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. C5-methyltransferase family. {ECO:0000256|PROSITE-
CC ProRule:PRU01016}.
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:OQO25959.1}.
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DR EMBL; NAEU01000237; OQO25959.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V8UQF2; -.
DR STRING; 1974281.A0A1V8UQF2; -.
DR Proteomes; UP000192386; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 2.30.30.490; -; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR001025; BAH_dom.
DR InterPro; IPR043151; BAH_sf.
DR InterPro; IPR018117; C5_DNA_meth_AS.
DR InterPro; IPR001525; C5_MeTfrase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR10629; CYTOSINE-SPECIFIC METHYLTRANSFERASE; 1.
DR PANTHER; PTHR10629:SF54; DNA METHYLTRANSFERASE DIM-2; 1.
DR Pfam; PF00145; DNA_methylase; 1.
DR PRINTS; PR00105; C5METTRFRASE.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51038; BAH; 1.
DR PROSITE; PS00094; C5_MTASE_1; 1.
DR PROSITE; PS51679; SAM_MT_C5; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01016}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000192386};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PROSITE-ProRule:PRU01016};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU01016}.
FT DOMAIN 411..528
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT REGION 1..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1053..1076
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1106..1176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1118..1132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1133..1148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 752
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ SEQUENCE 1176 AA; 130937 MW; E626F5D40103F921 CRC64;
MPPTRERRQS TKAAESAISQ EIDDRPWKRR KITRGGGAEF LERPTRVVRP QRSVVIDLDS
DDDSASSAPA PGHDPSRESQ AVDDAPPDCA IVRTYPPAQP SSCFSGWEAP TDAQKSSEAD
ALEDLLSCLQ GLEQPEEFNY IELSDFTIYR PPDVRLHHDM CALSRLQVLG IDRLLFNGVL
SVGDQRRFVQ GVPFGILTID YDESVRFDTR KRACLQSFRG HRADVWYRLG EPADEYRRYS
DPFNWLATFT AFFLEYLEQH GCKAVTLADF RSHFFQWLQA THGSLHEFPA WHAQCKLDDF
RSSITANFDY LNKECHSLGL VPGRLWAEVN PADLRAIPKQ VNDELKTVVT PFVHDMFKHM
YFATHLRQKT ASNSLLSQIA TRKRSMALTP LNSRPTTLPT VMDVAAVEGP LVIRPGDVVQ
IPPDPKSTWR GLDAWFVYVQ DVRGEHMDVI WLYHSSHTTL DESAYYPFQN ELFMSDNCRC
GQDAEPIDQV IRKVDVRWFM TDPNSISQAD FFVRQKYRSV LEDFVTLRSS DFTCECHLDN
DTAQWEECCA TYNIGDYVLF REGISDDHAL VPAQVTAFDR VERKVCLESL QCALGHAIRP
NELIETGNIC AVSPTAIDRK CTITRYCSRN AVNFPFDRDG AGDHYYIIDE ATKVVPGSYT
PSIAPMRGLG MFCGGGNLDR GLEECGAVEV KYALDWAEHA LHSYRANVDD PATVSYFLGS
VNDYLAQAMK GSTKAGIATI GEVDLISAGS PCPGFSPMQP DKQSQKASQM ASLVASVVSY
VDFYTPRYLI LENVVSMTNT LHFAQDQNVF TQIIAGLVAL GYQTQQFLMD AWSYGSSQQR
SRVFIIASAP GLPPLEAPPH THAHAKQVQK KGLGRASNGE IIGVRRDDWT PFAHVSTTAS
TAHLPNIGDA TVDLCPAFPD HRTTTEETAR SRDSLASVPT RPYEMSLQKA VHRGLITSGS
AYEWVKSYDP NSIRGRPDGK SYQRVAPDGL FPSLMTKLAL QDGKNEARIA QGFRPHEVII
GSPGQQMKIV GNSVDRWVAF ALGLHLRKSW DARPKDEDEA PGRGMQSINV KPTPEQLRAI
DHEVDEVRAG GFKAIRRRLL TVEAASTASG MSSRRASIPE EAEADGESTP RATSYERKSA
SITPSRGTLD GATEAHGLLT PIQREGSNLE SAIMIE
//