ID A0A0D0B4K0_9AGAR Unreviewed; 1047 AA.
AC A0A0D0B4K0;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 13-SEP-2023, entry version 35.
DE RecName: Full=Cytosine-specific methyltransferase {ECO:0000256|RuleBase:RU000417};
DE EC=2.1.1.37 {ECO:0000256|RuleBase:RU000417};
GN ORFNames=GYMLUDRAFT_98175 {ECO:0000313|EMBL:KIK58230.1};
OS Collybiopsis luxurians FD-317 M1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Omphalotaceae; Collybiopsis;
OC Collybiopsis luxurians.
OX NCBI_TaxID=944289 {ECO:0000313|EMBL:KIK58230.1, ECO:0000313|Proteomes:UP000053593};
RN [1] {ECO:0000313|EMBL:KIK58230.1, ECO:0000313|Proteomes:UP000053593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FD-317 M1 {ECO:0000313|EMBL:KIK58230.1,
RC ECO:0000313|Proteomes:UP000053593};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (APR-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; KN834786; KIK58230.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D0B4K0; -.
DR HOGENOM; CLU_008262_0_0_1; -.
DR OrthoDB; 317994at2759; -.
DR Proteomes; UP000053593; 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 CDD; cd04370; BAH; 1.
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; IPR031303; C5_meth_CS.
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; 1.
DR Pfam; PF00145; DNA_methylase; 1.
DR PIRSF; PIRSF037404; DNMT1; 4.
DR PRINTS; PR00105; C5METTRFRASE.
DR SMART; SM00439; BAH; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51038; BAH; 1.
DR PROSITE; PS00094; C5_MTASE_1; 1.
DR PROSITE; PS00095; C5_MTASE_2; 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:UP000053593};
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 235..376
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT REGION 1..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1015..1047
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..57
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..159
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 647
FT /evidence="ECO:0000256|PIRSR:PIRSR037404-1,
FT ECO:0000256|PROSITE-ProRule:PRU01016"
SQ SEQUENCE 1047 AA; 118555 MW; E7414BDB52282F2B CRC64;
MEGSSKLVDR GGSLKTKDNA RSAHELAMPS GSSSATFVRD HEEGTETEPE EGFSKPMSRR
LEAVVIPVSS QGKPSSKKAI GKQKQLTPKS QSATPSIPSP SKSRRPTSSK LSTPASTRFR
QYYEDDNSDS DYSSSDSSHS SEESDVPKRS RDKDSAAKDS MKPTLTPIVN RVVQGFFNLK
FRVAELDSGK KPGKSQWKSM KYDVHKGNPE KVEFENELES EDNKVYYKSV ILDGERYKIG
DIVMVQPGED ARKGRQKNFA SDAAQSVNDY ANKYWFIRIR YFYEEFDRKS GRLRMFHGQW
FEHGSKTFLQ QTSHSRALYL TNSCGDAPLS SIYRKCDVKF PKLGEQEEED DHDSDGDQFF
CQYVWDDNKD LSFLDLPSEE QITEDLAFAP AYRACHSCVL EERAEFFKEV QYSKENGCVS
HYGIDYHVDD FIYLRPSGKE QSDLLEKAQI VKILPPGSNS SPKLIVRKMN NPERKSNLDE
HLLEFSKATE TVSFEDVNGK FYVARYSQTS EKLPKWIRED DHFFVDKNTS LSQCSQCLDD
HKKLLEKRKN VGPPLRALEL FSGAGGLGSG LDASGYVKTV AAVEWDKHAA ETYKTNHPQT
AVFCQDVNKL LHDISNDENV QSLPRGGKTR RFPRPGDIDL ISGGPPCQAF SMANHHPKEN
DIRATLPFSQ LSFTEMYLPP YFLLENVVGI LNFRLRGVLK GRSLSGGIKH GVFKLIVRTL
MALGYQVHVK VLQAANYGAP QGRQRVIFLA AKQGLKIPDF PIPTHVFRAN NHKLLENDDL
ILYKPTRSPD DSRSFAPFRT VSCSEAIGDL AGFDWENPHR TIKATDKDKL EAKIRSKSLP
SFPAGPRNKL PGFETCEYAH SPMNAYQKLV REDMEDEVKE HVTPTFSEHI IECSTTVPLQ
PRASHLDIPE RLHRKKKKDP QPIFYGRLDG NECFKTAMTR CAPNTKASYL LHFSQKRMLT
VREYARAQGF PDRYTFMKSY TVYEANLAYK QIGNAVPVPL ALALGKSLGD ALVVEREREE
ERERKGSAYV DRRDEDENEG SERSVEV
//
