ID A0A1W2TVA7_ROSNE Unreviewed; 766 AA.
AC A0A1W2TVA7;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=DNA (cytosine-5-)-methyltransferase {ECO:0000256|ARBA:ARBA00011975};
DE EC=2.1.1.37 {ECO:0000256|ARBA:ARBA00011975};
GN ORFNames=SAMD00023353_8600260 {ECO:0000313|EMBL:GAP92566.2};
OS Rosellinia necatrix (White root-rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Xylariaceae; Rosellinia.
OX NCBI_TaxID=77044 {ECO:0000313|EMBL:GAP92566.2};
RN [1] {ECO:0000313|EMBL:GAP92566.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W97 {ECO:0000313|EMBL:GAP92566.2};
RA Kanematsu S.;
RT "Draft genome sequence of Rosellinia necatrix.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. C5-methyltransferase family. {ECO:0000256|PROSITE-
CC ProRule:PRU01016}.
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DR EMBL; DF977531; GAP92566.2; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W2TVA7; -.
DR STRING; 77044.A0A1W2TVA7; -.
DR OMA; CCYWSPA; -.
DR OrthoDB; 1948937at2759; -.
DR Proteomes; UP000054516; Unassembled WGS sequence.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 3.90.120.10; DNA Methylase, subunit A, domain 2; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR001525; C5_MeTfrase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR10629; CYTOSINE-SPECIFIC METHYLTRANSFERASE; 1.
DR PANTHER; PTHR10629:SF52; DNA (CYTOSINE-5)-METHYLTRANSFERASE 1; 1.
DR Pfam; PF00145; DNA_methylase; 1.
DR PRINTS; PR00105; C5METTRFRASE.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51679; SAM_MT_C5; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01016}; Reference proteome {ECO:0000313|Proteomes:UP000054516};
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 REGION 73..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 653..766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..684
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 704..718
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 412
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ SEQUENCE 766 AA; 86504 MW; D7A96D730E4BB8E5 CRC64;
MRNSLRAEAV VKSAWGADAE DTQIEAESAV IENRLRDLPD RLRQGLIIID QDDDEDEEEH
EREAIPALAD IIDLTDDAPG PEQRSKDQPV RNPPIPSHES LEFYYFDGLI KIERGSTVEI
QALEQPQLFK TSFLHVQHIF RTSDGVKLHG IPLTRMRNLR GRLPRLRNEV AMILHVDNDD
KRPEEVQAAI EVSVADVIKI RHCHFTNADF PQHRTVLGIH KSITDLEQYG VLMCRWRCIF
RYRNSATRIA HFGQTKSKGR CNAAPVEYVI EHLNARQASK KRFEVSEAGR FNVWRGGKVR
GGDYDPENKN SPITGPLVQL DAKADSEVVL IEKKPGQKYT FGDMFCGAGG ASCGAQKAGF
HIKIACDHHL GACRTYSKVF PEADLVMSDI FDFITRDTAK TRVDVLHLSP PCQFWSPAHT
CAGANDDANI AVLFSCHELI RELRPRIFTL EQTFGILLPK FEYYFNALVH GFTRNDYSVR
WKVVDLVDWG SPAARKRLVM IGSCPGEALP PFPRATHVAP GGGGKGKWKR RRRSHVTVAK
MLGRIPRDAW RHDDMHRPRE MARKRLARWD ADVTLRRCIT TNGGYGNYHP SGRRDFTLRE
YATLQTFPVG YPFQNPDRKR QIGNAFPPKA VKALYAHLRG WLEGQDRVYA VENEPVDRDD
PDVSFFDLGS SDDEDDDGDE DEDVEYVGSQ RLPSPSIGSN RGGEEEEEES DEDMDLDYGP
CIDVNQGPHV WPPIDLTTAD DDDDDDGSGG TDDNARAWVD LTGEDK
//
