ID A0A1I0Y389_9BACT Unreviewed; 540 AA.
AC A0A1I0Y389;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
GN ORFNames=SAMN04489723_10472 {ECO:0000313|EMBL:SFB07357.1};
OS Algoriphagus aquimarinus.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Algoriphagus.
OX NCBI_TaxID=237018 {ECO:0000313|EMBL:SFB07357.1, ECO:0000313|Proteomes:UP000198790};
RN [1] {ECO:0000313|EMBL:SFB07357.1, ECO:0000313|Proteomes:UP000198790}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23399 {ECO:0000313|EMBL:SFB07357.1,
RC ECO:0000313|Proteomes:UP000198790};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyadenosine in DNA + S-adenosyl-L-methionine = an
CC N(6)-methyl-2'-deoxyadenosine in DNA + H(+) + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:15197, Rhea:RHEA-COMP:12418, Rhea:RHEA-
CC COMP:12419, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:90615, ChEBI:CHEBI:90616; EC=2.1.1.72;
CC Evidence={ECO:0000256|ARBA:ARBA00001279};
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DR EMBL; FOKK01000004; SFB07357.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0Y389; -.
DR STRING; 237018.SAMN04489723_10472; -.
DR OrthoDB; 9814572at2; -.
DR Proteomes; UP000198790; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro.
DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC.
DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR003356; DNA_methylase_A-5.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR42933:SF1; SITE-SPECIFIC DNA-METHYLTRANSFERASE (ADENINE-SPECIFIC); 1.
DR PANTHER; PTHR42933; SLR6095 PROTEIN; 1.
DR Pfam; PF02384; N6_Mtase; 1.
DR PRINTS; PR00507; N12N6MTFRASE.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 4: Predicted;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Reference proteome {ECO:0000313|Proteomes:UP000198790};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 179..494
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 540 AA; 61308 MW; 6EF4145323DBC0DD CRC64;
MTDNHLFESK TKLLIDGLKS TCANYGLGND GNEFKIITQV FLYKFLNDKF IYELKKLKPN
LAAAEHLDEA IRMIPEAEYE LLMLQLNEGT ARLQPEQFIS RLYQRQSEPK FSEIFDNTLL
AIAKENSDIF SVITEEGEKI VLFENISKYI TDKRDDFCKS IINKLVHFSF EEIFKEKFDF
FATIFEYLIK DYNTNSGGKY AEYFTPHAVS KIMARCLVQD EVSNVSCYDP SAGSGTLLMN
LAHQIGEDRC MIYSQDISQK SSNLLRLNLI LNNLVHSIPN IVKGNTILEP YHKKADGHLQ
KFDYIVSNPP FKLDFSDFVA DLDTKQNNER FFAGIPNVPA KKLESMAIYL MFLQHIMYSL
SPTGKAAIVV PTGFITAQSG IEKKIRERMV KDKMLAGVVS MPSNIFATTG TNVSVIFLDK
QNKGDVILID ASNLGTTVKE GKNQKTLLST AEEDRIIATF SEKKAEEDFS VLVSYDEIEA
KNYSLSAGQY FEVKIEYVDI TQDEFQAKLG SYQQNLALLF ADSKDLEIEI HENLKGLKYA
//
