ID A0A1Y1YP97_9FUNG Unreviewed; 1236 AA.
AC A0A1Y1YP97;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 13-SEP-2023, entry version 25.
DE RecName: Full=Cytosine-specific methyltransferase {ECO:0000256|RuleBase:RU000417};
DE EC=2.1.1.37 {ECO:0000256|RuleBase:RU000417};
GN ORFNames=K493DRAFT_279253 {ECO:0000313|EMBL:ORX99839.1};
OS Basidiobolus meristosporus CBS 931.73.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota;
OC Entomophthoromycotina; Basidiobolomycetes; Basidiobolales; Basidiobolaceae;
OC Basidiobolus.
OX NCBI_TaxID=1314790 {ECO:0000313|EMBL:ORX99839.1, ECO:0000313|Proteomes:UP000193498};
RN [1] {ECO:0000313|EMBL:ORX99839.1, ECO:0000313|Proteomes:UP000193498}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 931.73 {ECO:0000313|EMBL:ORX99839.1,
RC ECO:0000313|Proteomes:UP000193498};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) 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}.
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:ORX99839.1}.
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DR EMBL; MCFE01000091; ORX99839.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1YP97; -.
DR STRING; 1314790.A0A1Y1YP97; -.
DR InParanoid; A0A1Y1YP97; -.
DR OrthoDB; 1215898at2759; -.
DR Proteomes; UP000193498; 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; 2.
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; 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; 1.
DR Pfam; PF12047; DNMT1-RFD; 1.
DR PIRSF; PIRSF037404; DNMT1; 4.
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; 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:UP000193498};
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 438..551
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT DOMAIN 597..725
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..56
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 856
FT /evidence="ECO:0000256|PIRSR:PIRSR037404-1,
FT ECO:0000256|PROSITE-ProRule:PRU01016"
SQ SEQUENCE 1236 AA; 140618 MW; A6FD63342589B5AC CRC64;
MDGDNDSISN LQTDSSDEFL SESKLVKRPQ RTQAKKRTKL ELDDDDDDDV KMKVEPKPAS
KLSVPRYKCP AEEILENEHL EIFGEEPSEV DDLHIPCRTL DDFVIYDVAR NNQIVSIEEI
DEEGRELRAS GNVQAIMVSD DGPRDGGNVI EEEDDDEDFE IDENGDLNQT APSRSQRVKL
STIFYWEVQL LDNGMSAIWL RTQYSWYKLV RPTEKYERFY IDIFKRIRLA NLLITKMVNN
TTATYQDFLS SMNQSPVGSS NSDDIGVRFY EQDIINNIDY ICEEINVYLE DQDDYTIFNS
PLLHKLTEIR NQDEGIGMVR EPKPIDVRDS ATRKTIRKIK KSEPEENPAC VTSHIRNLAK
GLFTRHIVMS KHLADVVAEI EEVKKTGDSS IIEDAVVEVI PQKRRGNLCK DKKVSWIGES
VGSLRSKTYY SGAQIGEVEL AIGDCVALDT RATEPDLVKI QYMYQDTFGV KYIHGRTLMS
GKKTVLEDVS HPFELFLVDQ CDTWKMSSIV KKCELKFLEP EEVEPQQQPH PDFYFIRYWY
DPLSPTFEDI AKHELLPNGG KKLKRCYACD LERLEESKKF PHSVNKKGVR GFVFKGYEYH
LYDFVYLLPS APYGPYDIGQ IVEILSSQED MSDLSTVKIR RLARCDTLLP KYTSKTPQTN
FDRKDARQLY ITEQYVTVNI AKLEGTCWVQ HQDTISDLDA YKDQVDTFYI SGHRAHISGK
EPLEDIRASS IRICGACQSA RDTNERHAKR LQRKRKPLAA LDIFSGCGGL TCGLKQSGVV
ETKYAIEFYS SAALSFERNF PGANVYNQCA NLLLDRAIAV HHRGEELPPI KDHMNRVMPE
MPAPQDVDFI YCGPPCQGFS GINRYKKAND IKNSLIATSL SYVDYYRPEY FLLENVRGML
AFKLGGEQDG TNRIKGGIKM GVVKFILRAL TSMGYQTRFS VQQAGHHGLP QSRRRLFFWG
AKRGSNLPEF PQPSNCFPKQ GTLNINLPNG KSFTAIKRTI GHAPHFPVTV ADAICDLPGF
EYRNPEAVYK VEDPRPSIFK KLPVASGGYI GSMEMDYTNP PLTEYQRQLR RNAHKLHNHV
TRGFNDLTTE RICRVPMWAG ADHSNLPEKL KPWCLSSPDS AASRHNGWKG LFGRLDFDGH
FQTALTDMQP MGKQGTVIHP NQERVLTVRE CARAQGFPDD FIFHSFNKQD VKDLHRQVGN
AVPPPLAAAL GRQLKAALME ALTDESESDD EEPPED
//