ID A0A068RV47_9FUNG Unreviewed; 891 AA.
AC A0A068RV47;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, 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=LCOR_04292.1 {ECO:0000313|EMBL:CDH52856.1};
OS Lichtheimia corymbifera JMRC:FSU:9682.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Lichtheimiaceae; Lichtheimia.
OX NCBI_TaxID=1263082 {ECO:0000313|EMBL:CDH52856.1, ECO:0000313|Proteomes:UP000027586};
RN [1] {ECO:0000313|EMBL:CDH52856.1, ECO:0000313|Proteomes:UP000027586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JMRC:FSU:9682 {ECO:0000313|Proteomes:UP000027586};
RA Schwartze V.U., Winter S., Shelest E., Marcet-Houben M., Horn F.,
RA Wehner S., Hoffmann K., Riege K., Sammeth M., Nowrousian M., Valiante V.,
RA Linde J., Jacobsen I.D., Marz M., Brakhage A.A., Gabaldon T., Bocker S.,
RA Voigt K.;
RT "Gene expansion shapes genome architecture in the human pathogen
RT Lichtheimia corymbifera: an evolutionary genomics analysis in the ancient
RT terrestrial Mucorales (Mucoromycotina).";
RL Submitted (AUG-2013) 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:CDH52856.1}.
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DR EMBL; CBTN010000015; CDH52856.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A068RV47; -.
DR STRING; 1263082.A0A068RV47; -.
DR VEuPathDB; FungiDB:LCOR_04292.1; -.
DR OrthoDB; 1215898at2759; -.
DR Proteomes; UP000027586; 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 GO; GO:0043130; F:ubiquitin binding; IEA:InterPro.
DR CDD; cd14279; CUE; 1.
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; IPR003892; CUE.
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 PRINTS; PR00105; C5METTRFRASE.
DR SMART; SM00439; BAH; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51038; BAH; 2.
DR PROSITE; PS00094; C5_MTASE_1; 1.
DR PROSITE; PS51140; CUE; 1.
DR PROSITE; PS51679; SAM_MT_C5; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
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:UP000027586};
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 1..44
FT /note="CUE"
FT /evidence="ECO:0000259|PROSITE:PS51140"
FT DOMAIN 149..262
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT DOMAIN 297..421
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT COILED 25..52
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 535
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ SEQUENCE 891 AA; 102191 MW; B33EA408A61A3272 CRC64;
MTIDNIEPLA NTFPEIEQCD IVDVLAACEN DMDRATDRLT DLRDRMDSKR GREELSQHVV
PLKKLKKPKK NYKDANDTCI TAHISFIAKD MFIRKMINIT EAAEEAHYQQ IMNDGNINKE
NTMAVTWHGR PIKRENGRTY YSAAIVDGEI LELGDTVYMR TGDEEPWFAL IMSFFDGPDA
DYQFHARFFS HGRETVLDEL AGERELFLLD NCEDNDLYSV MGKANVIRMD GDIEEPTAFT
KKDWWFYRLW YDPDDAIFED VDLHEDPDVC LSCRAKEEEK AREQPKWEDG SVKYQGVEYH
VHDFIYTLIG PESKPYVIAQ IVSIDASRHI IHIQTMTRDE DSSKLDHYDL IDNGSEAPYK
DSRMLTMTTQ RQRISLEELE GKCWVEEIGN IEDVKEYKKS PDNFYTNDTI THCQPCREKR
EENEELWEQF YDSANKLSAL DIFAGCGGLT VGMDNTGVIE TTHSIEFNPD AAKTFQRNFP
DSTVHNQCAN VLLARAIASH HQNIELEPLD DFHGKPLRPM PGPNDIDFIY CGPPCQGFSD
LNQHKKPGEI KNTLVCSAMS YVDFYRPSYF LLENVRGLVS YKLGKDRINN GVLKFIIRCL
TSMGYQVRFA VLQAAQYGVP QTRRRLFVWG AKIGKHLPKF PQPMTCTDYA TNTIIRFADG
TEVSHVTRTG KRAPLSMVTV GDTISDLPAF DYECSNARPN VRTYNAVLQP PGKIRQRYTI
PPKTDFQTWL RGDTEELRNH VTRAFNEVNV QRICAIKMEP KADHNCLPQE LIPWALDRRN
PAAQRHNFWP GLFGRLDYNE QFQTAVTELN PLSKQGTVIH PNQHRVLSVR EAARSQGFPD
WFIFKAISKK KPSQKVTAMY MQVGNAVPVP LAAALGNGLK NAMFEDWLQD Q
//
