ID A0A165D0I2_9BASI Unreviewed; 1059 AA.
AC A0A165D0I2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 13-SEP-2023, entry version 29.
DE RecName: Full=Cytosine-specific methyltransferase {ECO:0000256|RuleBase:RU000417};
DE EC=2.1.1.37 {ECO:0000256|RuleBase:RU000417};
GN ORFNames=CALCODRAFT_503094 {ECO:0000313|EMBL:KZT51804.1};
OS Calocera cornea HHB12733.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Calocera.
OX NCBI_TaxID=1353952 {ECO:0000313|EMBL:KZT51804.1, ECO:0000313|Proteomes:UP000076842};
RN [1] {ECO:0000313|EMBL:KZT51804.1, ECO:0000313|Proteomes:UP000076842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12733 {ECO:0000313|EMBL:KZT51804.1,
RC ECO:0000313|Proteomes:UP000076842};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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; KV424090; KZT51804.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165D0I2; -.
DR STRING; 1353952.A0A165D0I2; -.
DR InParanoid; A0A165D0I2; -.
DR OrthoDB; 317994at2759; -.
DR Proteomes; UP000076842; 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; -; 1.
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; 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; PF00145; DNA_methylase; 1.
DR Pfam; PF12047; DNMT1-RFD; 1.
DR PIRSF; PIRSF037404; DNMT1; 3.
DR PRINTS; PR00105; C5METTRFRASE.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51038; BAH; 1.
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:UP000076842};
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 404..528
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT REGION 37..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 298..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 661
FT /evidence="ECO:0000256|PIRSR:PIRSR037404-1,
FT ECO:0000256|PROSITE-ProRule:PRU01016"
SQ SEQUENCE 1059 AA; 119238 MW; E9014B4AB5FAAE0C CRC64;
MTSSRKRHLS DDSEIYSIAG GLRAASVLSN LSTTFSRLSV DPGSFSSRNY EHLEPAHKRP
KSTNRFEVPE NCILEAEDLV LEGEGVDSDE SQDDDEEPSL PIRLLDSFVV FDEANHGTMM
PLSGLEAPDS DLRIYGVVKP MFVGDDEYVE YDEEGTPSDN AERVEFVSTA IFLYYLESDP
MKPLVWLKTQ YSWLILDRPS PEYRVHYYEF WKARYVCRLA LMTTSEGRSY FDLEFSELQQ
TEPGGAVNLR GRPFSQTRVL REISGKEETV EDLLSDAVES GWDNAYAVMP ELYPRKTKTS
LSRNRVKDQT YQPAESRIRS HPHQAQTKKS FRPFFTPAVE RLASRLGLRG SARRIASAPV
HDRSQISILD SLEDSIEEAA KGDLEGVWGL DDDRVGGPSP HPQEPYHVHD FVYIRGLNDR
EGNQPFRIGQ IRDFRGSDRD PRVIVRLFAR WDDLNGVPDE GILRPKDSCH LCATRVHHNL
STLDLRGLCV VRHHEELSEA STTRHPGEQG FYVKYICSAE RLTGPLTKNN FLLLRPNDLQ
QCANSRCKDR RHSRNKVLKE PLKCLELFHG AGGLSLGLEQ AGCIVTKWVV DASPSAHATF
RANFPDAAAI LQDTNEVLRR AVDLSEGKDP PPLYQIGSHT ERCPELPRPG EVDIIIGGPP
CQGFSRLNSF ATANDKRNTL IGNALSYVDF FQPRFVLLEN VRPLLHMSST LRRNGSDEEE
VVENAFAKLI VGFLVERGYQ VRFKVLQAVQ YGAPQERNRV IFMAALRGET LPEFPLPTHT
WRSKVGPGLG VLRDEEGGAP HPYITVEDAI SDLPPFHWDW DERGLRKDPD LPRPDELRVP
GITRNRKRET RGYIHPVAYT GPPKTAYQRL IRGDCEEVQH HATHTFSVKY VERICNIPPP
QPELGIPEGL DWRAMCMALI PADVAHPHGR IVGDTNINRD AKFARVYASR PAQTVVTTLQ
PGGRMTRILH YSQYRVLSAR ENARLQGFPD SFKFVAPKNN LTEVGCGAST LPEPCSNAQS
DLSPYRKRCP NSSSVSARPA IQQGTAWGRA RLRLRGAGD
//
