ID A0A1B7VYS1_APHFL Unreviewed; 433 AA.
AC A0A1B7VYS1;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-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=AN481_06575 {ECO:0000313|EMBL:OBQ26146.1};
OS Aphanizomenon flos-aquae LD13.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Aphanizomenonaceae;
OC Aphanizomenon.
OX NCBI_TaxID=1710894 {ECO:0000313|EMBL:OBQ26146.1, ECO:0000313|Proteomes:UP000092382};
RN [1] {ECO:0000313|EMBL:OBQ26146.1, ECO:0000313|Proteomes:UP000092382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MDT13 {ECO:0000313|EMBL:OBQ26146.1};
RA Driscoll C.;
RT "Whole genome shotgun sequence assembly of Aphanizomenon flos-aquae
RT UKL13.";
RL Submitted (SEP-2015) 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, 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:OBQ26146.1}.
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DR EMBL; LJOY01000015; OBQ26146.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B7VYS1; -.
DR STRING; 1803587.GCA_001593825_03805; -.
DR PATRIC; fig|1710894.3.peg.2846; -.
DR Proteomes; UP000092382; Unassembled WGS sequence.
DR GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IEA:UniProtKB-EC.
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; IPR001525; C5_MeTfrase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR NCBIfam; TIGR00675; dcm; 1.
DR PANTHER; PTHR46098; TRNA (CYTOSINE(38)-C(5))-METHYLTRANSFERASE; 1.
DR PANTHER; PTHR46098:SF1; TRNA (CYTOSINE(38)-C(5))-METHYLTRANSFERASE; 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}; 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 75
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ SEQUENCE 433 AA; 49340 MW; DC9C40A3FD336B10 CRC64;
MIRFIDLFAG IGGMRLGFQQ ACDVLGIESQ CVLSSEIDKR AIETYKLNFD DQPMGDIRKI
DIISEFDFML AGFPCQPFSY AGKQQGFGDT RGTLFFEIER LLTSYQPQAF LLENVRGLTT
HDQGRTFNTI INSLEKLGYG IHYLLLNSSN FGVPQNRVRI YILGLLGKKP KITINSDRGA
TDSHTFKEQL YQLSLFADPY LVVKVKDILE QKVSENYYLS KNFEQQLFDA VDGQFEKLHG
VRLIDFRGGN SLHSWDLGIK GKCTKDERDF MAALMSHRRH KEFGNHQDGK SLTIEQIKTF
FDNENMENII YSLIEKKYLK EINGRYNPVS GNMSFEVFKF LDPESISITL TSSDANKLGI
VQNGKPRRIT PRECARLQGF PECYIVHQDD NAAYKQFGNA VTVPVIQAIV EDFIKNNSIT
KANLFSSVIP MVR
//
