ID I4H3F7_MICAE Unreviewed; 405 AA.
AC I4H3F7;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE RecName: Full=Cytosine-specific methyltransferase {ECO:0000256|RuleBase:RU000417};
DE EC=2.1.1.37 {ECO:0000256|RuleBase:RU000417};
GN ORFNames=MICAF_2060009 {ECO:0000313|EMBL:CCI16581.1};
OS Microcystis aeruginosa PCC 9807.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Microcystaceae; Microcystis.
OX NCBI_TaxID=1160283 {ECO:0000313|EMBL:CCI16581.1, ECO:0000313|Proteomes:UP000003613};
RN [1] {ECO:0000313|EMBL:CCI16581.1, ECO:0000313|Proteomes:UP000003613}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=9807 {ECO:0000313|EMBL:CCI16581.1,
RC ECO:0000313|Proteomes:UP000003613};
RA Genoscope - CEA;
RL Submitted (APR-2012) 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 -!- 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:CCI16581.1}.
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DR EMBL; CAIM01000120; CCI16581.1; -; Genomic_DNA.
DR AlphaFoldDB; I4H3F7; -.
DR HOGENOM; CLU_006958_2_1_3; -.
DR Proteomes; UP000003613; Unassembled WGS sequence.
DR GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0009036; F:type II site-specific deoxyribonuclease activity; IEA:InterPro.
DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR CDD; cd00315; Cyt_C5_DNA_methylase; 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; IPR018117; C5_DNA_meth_AS.
DR InterPro; IPR001525; C5_MeTfrase.
DR InterPro; IPR031303; C5_meth_CS.
DR InterPro; IPR019044; Restrct_endonuc_II_HindVP.
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; PF09519; RE_HindVP; 1.
DR PRINTS; PR00105; C5METTRFRASE.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
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 Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01016}; Restriction system {ECO:0000256|ARBA:ARBA00022747};
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 169
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ SEQUENCE 405 AA; 45933 MW; A6F9212C5EB9A644 CRC64;
MAKSTIFKPS LFGLKHSNRD FTQKETWGKN QFNSSFPASL CAYLDGKGLK NVDLKLDENL
KIQPAELSTK ELYGLAPDSD NLFYAFESQF GGESKMITID LFAGCGGLSL GFQKAGFTIV
AAFDNWIPAI DVYRNNFSHP IFNVDLSRES NQEILAQYNP EIIVGSPPCQ DFSSAGKRNE
GLGRASLTLT FAEIVTRVSP QWFVMENVDR IEKSKILIQA KQIFKSHGYG LTGKVINSCY
CGVPQTRKRY FLIGKMNEED DFLIDEINGN LSSKPLTVFD YMGKELDIEY YYRHPRSYQR
RAIFSIYEPS PTIRGVNRPV PKTYRQHPGD ACHLNEKLRP LTTSERSYIQ TFPKDFIFAG
TKSNLEQMIG NAVPVNLARY VGQCILNYEL KKGKKITDRQ LQLFS
//
