ID K1W551_TRIAC Unreviewed; 513 AA.
AC K1W551;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=DNA (cytosine-5-)-methyltransferase {ECO:0000256|ARBA:ARBA00011975};
DE EC=2.1.1.37 {ECO:0000256|ARBA:ARBA00011975};
GN ORFNames=A1Q2_01636 {ECO:0000313|EMBL:EKD04053.1};
OS Trichosporon asahii var. asahii (strain CBS 8904) (Yeast).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Trichosporonales; Trichosporonaceae; Trichosporon.
OX NCBI_TaxID=1220162 {ECO:0000313|EMBL:EKD04053.1, ECO:0000313|Proteomes:UP000006757};
RN [1] {ECO:0000313|EMBL:EKD04053.1, ECO:0000313|Proteomes:UP000006757}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 8904 {ECO:0000313|EMBL:EKD04053.1,
RC ECO:0000313|Proteomes:UP000006757};
RX PubMed=23193141; DOI=10.1128/EC.00264-12;
RA Yang R.Y., Li H.T., Zhu H., Zhou G.P., Wang M., Wang L.;
RT "Genome sequence of the Trichosporon asahii environmental strain CBS
RT 8904.";
RL Eukaryot. Cell 11:1586-1587(2012).
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:EKD04053.1}.
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DR EMBL; AMBO01000235; EKD04053.1; -; Genomic_DNA.
DR AlphaFoldDB; K1W551; -.
DR STRING; 1220162.K1W551; -.
DR eggNOG; ENOG502QPKK; Eukaryota.
DR HOGENOM; CLU_479132_0_0_1; -.
DR InParanoid; K1W551; -.
DR OrthoDB; 317994at2759; -.
DR Proteomes; UP000006757; Unassembled WGS sequence.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR001525; C5_MeTfrase.
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 PRINTS; PR00105; C5METTRFRASE.
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:UP000006757};
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 ACT_SITE 302
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ SEQUENCE 513 AA; 56834 MW; 29C3984776632D3A CRC64;
MPPIRHGKQR PAGQRIKLGD VVSFTHHDET TYGVVTSLVG GEVHVQHLVS TAFGPMRAHR
RCSTPDSVKL TTLPSPKWVK EDGCLRHPLP GCDSCHHRDL RRRQRQLIFL DDGNAVKYRG
EVYHIGELVF RRSETKGEPW AVGIVKDFKK DGIVVQDELC ITPSRRTWLY VELRGKGVIN
LPTHLSLSYP CFKLEHRQRE DGAIIPLQRP KGPCECIFAE ARRTTALKEL RPPAVGLYAG
GGGSALGLSE HFELKLAVDT EDSCVQTLRA NFPATRVLQR EVGSLTAADI GEVSLLVAGP
PCQAFTRANH NRKVDARGHE PARLLRLISQ TLPQLVLIEN VPGIKDRCGS DDVAWNAAED
VVRSLLGLGY QVRWAVLDAA SYGAPQYRKR LFVLGAMTGT PLPRFPEPTH ANARPASTIF
LGEVFSSHDG TGAFPPVTAE QAVGDLPAWE YKLGGVYDPL KTEVGMRRCD VGPPRSRYAE
RLQRPDRRAR EHLTVGCSAD DYERCAHWKT SSS
//
