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Database: UniProt
Entry: A0A1B9GL16_9TREE
LinkDB: A0A1B9GL16_9TREE
Original site: A0A1B9GL16_9TREE 
ID   A0A1B9GL16_9TREE        Unreviewed;       902 AA.
AC   A0A1B9GL16;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=DNA (cytosine-5-)-methyltransferase {ECO:0000256|ARBA:ARBA00011975};
DE            EC=2.1.1.37 {ECO:0000256|ARBA:ARBA00011975};
GN   ORFNames=I316_06668 {ECO:0000313|EMBL:OCF31663.1};
OS   Kwoniella heveanensis BCC8398.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Kwoniella.
OX   NCBI_TaxID=1296120 {ECO:0000313|EMBL:OCF31663.1, ECO:0000313|Proteomes:UP000092666};
RN   [1] {ECO:0000313|EMBL:OCF31663.1, ECO:0000313|Proteomes:UP000092666}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCC8398 {ECO:0000313|EMBL:OCF31663.1,
RC   ECO:0000313|Proteomes:UP000092666};
RG   The Broad Institute Genome Sequencing Platform;
RA   Cuomo C., Litvintseva A., Chen Y., Heitman J., Sun S., Springer D.,
RA   Dromer F., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A.,
RA   Alvarado L., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA   Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA   Murphy C., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Cryptococcus heveanensis BCC8398.";
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000092666}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCC8398 {ECO:0000313|Proteomes:UP000092666};
RA   Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D.,
RA   Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S., Birren B.;
RT   "Evolution of pathogenesis and genome organization in the Tremellales.";
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. C5-methyltransferase family. {ECO:0000256|PROSITE-
CC       ProRule:PRU01016}.
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DR   EMBL; KV700132; OCF31663.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1B9GL16; -.
DR   STRING; 1296120.A0A1B9GL16; -.
DR   Proteomes; UP000092666; Unassembled WGS sequence.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 2.30.30.490; -; 1.
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; IPR043151; BAH_sf.
DR   InterPro; IPR001525; C5_MeTfrase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR10629; CYTOSINE-SPECIFIC METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR10629:SF52; DNA (CYTOSINE-5)-METHYLTRANSFERASE 1; 1.
DR   Pfam; PF00145; DNA_methylase; 2.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51679; SAM_MT_C5; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01016}; Reference proteome {ECO:0000313|Proteomes:UP000092666};
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   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          26..115
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          514..538
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          712..735
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        79..111
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        517..538
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        513
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ   SEQUENCE   902 AA;  100131 MW;  278E305700EF182B CRC64;
     MSDPRRSSRP STSLGKRMRA LSVISVISEE DEEESAGADT SKRDSKARSS EQALPPSPTD
     RVKRARSDTS RVAKAPIKAT ETPSTTPWTS TSNQTHHSRV TGRSDNRAVW STDRNPIHPG
     EEVAVKVDGV DDAIRLSSAP YDLILIRSIY TLKFHDSGIP SKSYVHAQYL DKPTSIDGRS
     ARSYRQGELF LKHANCQDFA LKLIIEGTKL DFELIKSSAT RRRDTKHFAQ FVDEWTASTI
     RVPSPALDFH GCDACHSRDK KQYAEVVTIE KDAVRVGEER YHLFDFVFID PGVQGAPYMI
     GHLISWTEKK GSVEVNLRMM ERIQEVPGMS AYVSERHLVA SHKHLFFPAT RIVGTAFVFG
     SEDALRKGAP GCKSAFWCTH RLIENDRGRE VSLPLQTPLK SCSSCLNLQC HYRHDIKSCL
     EAARFPAADC YSGAGGFLLP GLDIFDWQSA CDIDVVACET LRRLKPKVPK LKIHHGSVEE
     LLHRSLDRDA HDTSSRRFPA RGSTFLLTGG PPCQGHSRAS HANNNTNGEN SSKAGPTDDR
     NSEMFVFLAL VAHTLPYVVI LENVGAFKDD KAELSQENAD GNFARRAMRE LTSMGSVQLM
     LSSLQTLLTD STYRVARRYA VRLAVINSRA YGSPQDRHRC FILAVQRGLP LPELPAPTHA
     VPSPMATVFK DKNGRAMPFY LGDRRATRGT GIHPPVTISD AISDLPVFEY HSRGTDQRPR
     RPIFSGSRDP AKGNGTKCGF AKPVAYASPP LNDFQRAKRG SNTQVNDHYT SYCTPGALDI
     IFNRSKLPNA RGCERRAVSN EGFSTLLTNS APGGKSTAVI HPSQERKFTT AERKRAMGWP
     DCFKLAGTPL DQDRLTGNGV CFESVEAIYQ SIVETIILPW WIKAGKPKER VYEKFVADYP
     IL
//
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