ID A0A0L6WSG3_9AGAR Unreviewed; 1313 AA.
AC A0A0L6WSG3;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Cytosine-specific methyltransferase {ECO:0000256|RuleBase:RU000417};
DE EC=2.1.1.37 {ECO:0000256|RuleBase:RU000417};
GN ORFNames=J132_00843 {ECO:0000313|EMBL:KNZ78480.1};
OS Termitomyces sp. J132.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Tricholomatineae; Lyophyllaceae;
OC Termitomyces.
OX NCBI_TaxID=1306850 {ECO:0000313|EMBL:KNZ78480.1, ECO:0000313|Proteomes:UP000053712};
RN [1] {ECO:0000313|Proteomes:UP000053712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J132 {ECO:0000313|Proteomes:UP000053712};
RA Hu H., Poulsen M.;
RT "The genome of Termitomyces.";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5-
CC methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:13681, Rhea:RHEA-COMP:11369, Rhea:RHEA-COMP:11370,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:85452, ChEBI:CHEBI:85454; EC=2.1.1.37;
CC Evidence={ECO:0000256|RuleBase:RU000417};
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, ECO:0000256|RuleBase:RU000416}.
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DR EMBL; KQ412478; KNZ78480.1; -; Genomic_DNA.
DR STRING; 1306850.A0A0L6WSG3; -.
DR OrthoDB; 317994at2759; -.
DR Proteomes; UP000053712; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR Gene3D; 2.30.30.490; -; 2.
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; IPR001025; BAH_dom.
DR InterPro; IPR043151; BAH_sf.
DR InterPro; IPR018117; C5_DNA_meth_AS.
DR InterPro; IPR001525; C5_MeTfrase.
DR InterPro; IPR022702; Cytosine_MeTrfase1_RFD.
DR InterPro; IPR017198; DNMT1-like.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR NCBIfam; TIGR00675; dcm; 1.
DR PANTHER; PTHR10629; CYTOSINE-SPECIFIC METHYLTRANSFERASE; 1.
DR PANTHER; PTHR10629:SF52; DNA (CYTOSINE-5)-METHYLTRANSFERASE 1; 1.
DR Pfam; PF01426; BAH; 2.
DR Pfam; PF00145; DNA_methylase; 2.
DR Pfam; PF12047; DNMT1-RFD; 1.
DR PIRSF; PIRSF037404; DNMT1; 5.
DR PRINTS; PR00105; C5METTRFRASE.
DR SMART; SM00439; BAH; 2.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51038; BAH; 2.
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:UP000053712};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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 425..565
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT DOMAIN 606..725
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT REGION 322..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 855
FT /evidence="ECO:0000256|PIRSR:PIRSR037404-1,
FT ECO:0000256|PROSITE-ProRule:PRU01016"
SQ SEQUENCE 1313 AA; 147268 MW; AB6E21F2293B8BA1 CRC64;
MIGLSPPQLG STLPISPTVS DFEDASRHDI RDVFKAQYLR ASPTVSDFMV NDTSATLAPS
DDETMSWPSK TSRLPIASGS NVTLEDIEGP VLYEAPVDAI PEDDNLLIPG ETSLDPLENS
ASQDDVPVRV LDDFSIFDMS SNELVPIAGL LGLGYGSRKF GASGSVRAWI DQDQDELGDD
DESDEDLENL ERVKLSTILE FDIHSISEAT GNPDSKIYIR TKYAWYILHM PTEEYRPDRH
ASYEEFLEKL SDVEGDSSAR EEVLASLQML GRVLTEADIQ SEDVKAYVAA NLPEMCDDYD
IPINSVRLAS EYLQLDLSDG EDFEPKSKSL PKSRSKRIST KSTLSDKEME VLKHRNTTYV
TPIVSQIMKN LFSVPLHFAE IPRIEDDPDV ITEIDNVKTH HSDPTSMKWG QAEGNLYTSL
NMDGVEYHAG DDVMVVPGDD EDQKRALISE TDASQSPNSY ANHLWFCKIC YFFEKNVNGK
RVKMFHGQWF IHGSKTILQE TAHSKSLFLL NTCEDNPAAS IFKKCNITMM GAGDVEQPDD
GQPHANDFHC ALAYDEKEAS FTDLPSEEEM TKLLEHDTCI ACALRKRGEQ LDELVMTSDG
YSRHGIHYHP NDFIYIRSRG RTTGLLDIAQ IVMMEVEGRN FQLTVQMFER PSKPQNSKGG
LPWDDRRLYL TDNEQIIYDI DLVDGMCFVR QLTDADEIDE WVTQDDHFYV NQIIDGRTGK
PRDLDNRAVR KCDTCWRERR RKQEEQQKLL MRNGPIRCLE LFSGAGGLGT GLDLSGFVET
KYAVEFSPSA AATYAKNHPN ATVYCQDSNK LLQQAYETGK GETPEPLLSG MDGKTRLPPM
PRRGDVDMIS GGPPCQSFSR ANHNPVPDDV RSTLPGNMLG FVETYDPQYF LLENVAGLLT
HRLMSTRSKH KRTLVGGIQG GMVKFIKRTL IALGYQVRCK VLQATQYGAP QSRRRVIFWG
AKRGLTIPDY PVPMYASAKG MNRSTLPTGM LEPMSRSRDS EFMHHCAPLR AVSVDDAISD
LPPFDWISPH KILPCTSKDK QAVRLRIEQG IPQFTATQAA RMPLPGFPEG TEYLTEPQNR
YQKWLRRGMG EDEVVEGHYT KFFTPSVVEA TVAVPLKPGA THRDIPEALR PKHMQIETSK
SFYGRLDGDG QFKCTMTNAA PNSKESWLLH PHVEQQKRIM SVRELARSQG FPDDYEFMSE
DQSQNGQRLV VNQIRQIGNA VPVPFALCLG KSLGGALLKD WERDRERRER EGSVVYLLDA
GDFGVVAAAR GEVAVYTGAD ADVGCDAWCA LDPLEIWVRV GWEKDGDLPK LVP
//
