ID W6QTC4_PENRF Unreviewed; 573 AA.
AC W6QTC4;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=DNA (cytosine-5-)-methyltransferase {ECO:0000256|ARBA:ARBA00011975};
DE EC=2.1.1.37 {ECO:0000256|ARBA:ARBA00011975};
GN ORFNames=PROQFM164_S06g000335 {ECO:0000313|EMBL:CDM37374.1};
OS Penicillium roqueforti (strain FM164).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1365484 {ECO:0000313|EMBL:CDM37374.1};
RN [1] {ECO:0000313|EMBL:CDM37374.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FM164 {ECO:0000313|EMBL:CDM37374.1};
RX PubMed=24407037; DOI=10.1038/ncomms3876;
RA Cheeseman K., Ropars J., Renault P., Dupont J., Gouzy J., Branca A.,
RA Abraham A.L., Ceppi M., Conseiller E., Debuchy R., Malagnac F., Goarin A.,
RA Silar P., Lacoste S., Sallet E., Bensimon A., Giraud T., Brygoo Y.;
RT "Multiple recent horizontal transfers of a large genomic region in cheese
RT making fungi.";
RL Nat. Commun. 5:2876-2876(2014).
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; HG792020; CDM37374.1; -; Genomic_DNA.
DR AlphaFoldDB; W6QTC4; -.
DR STRING; 1365484.W6QTC4; -.
DR OMA; KPRVHTM; -.
DR OrthoDB; 1948937at2759; -.
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; 2.
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};
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 57..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 340
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ SEQUENCE 573 AA; 63684 MW; D810F7A923875D40 CRC64;
MQEASHTFQP TEKLQIVIDL TCDDETNQAI EELTSEMTHV GAASVIVAGD DLASDRSSSG
NSSLISNQSA SCSPTPETMQ QEIDIGGVVF KPGISLELED GSFLRVKDMI PQPHDLLFFG
RHLYRTTHPE AKTYLPKLNN ELVWLTQKTD LISIKKVRRV VSIRFTNYRT DFNNLTPGDE
LTCRLKLTIR QNGVVIIPGN APLSAEQCAI EWLTFAESDP GLGKRANQLR AEWRGHTVPF
GEARVSSMAR DLERQGVIDL TVPDRAYTFG DAYCGAGGVS CGAKQAGVKL QWAVDIDKHA
LETYQLNFDD VEVEHSDFFS FLTNDPKFLR VDIAHCSPPC QTWSPAHTVP CPRDDANSAC
VFSAGSLIRE SRPRVLTMEE TMGLPQRFPV IFNRVVLDMV EFGYSVRWSV LGCDEYGVPQ
ERKRLLLIAA GPGEALPHYA QPTHGMPGHG LRPRETISST IDNIPPDAED HNVEAALARW
ALSHRPSFDR HSLARTITCG GGEYNYHPSG TRPYTSREMA LLQTFPLDFQ FAGRFMRKQI
GNAVPPLFAK AIYGEIVKSL YKTDTEEAMG IFH
//
