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Database: UniProt
Entry: A0A080M6T6_9PROT
LinkDB: A0A080M6T6_9PROT
Original site: A0A080M6T6_9PROT 
ID   A0A080M6T6_9PROT        Unreviewed;       527 AA.
AC   A0A080M6T6;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 28.
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=AW06_002251 {ECO:0000313|EMBL:KFB76681.1};
OS   Candidatus Accumulibacter cognatus.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Candidatus Accumulibacter.
OX   NCBI_TaxID=2954383 {ECO:0000313|EMBL:KFB76681.1, ECO:0000313|Proteomes:UP000021315};
RN   [1] {ECO:0000313|EMBL:KFB76681.1, ECO:0000313|Proteomes:UP000021315}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK-02 {ECO:0000313|Proteomes:UP000021315};
RA   Skennerton C.T., Barr J.J., Slater F.R., Bond P.L., Tyson G.W.;
RT   "Expanding our view of genomic diversity in Candidatus Accumulibacter
RT   clades.";
RL   Submitted (FEB-2014) 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};
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:KFB76681.1}.
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DR   EMBL; JDST02000048; KFB76681.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A080M6T6; -.
DR   STRING; 1453999.AW06_002251; -.
DR   Proteomes; UP000021315; 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; 1.20.1260.30; -; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR022749; D12N6_MeTrfase_N.
DR   InterPro; IPR003356; DNA_methylase_A-5.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR004546; Restrct_endonuc_T1M.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR038333; T1MK-like_N_sf.
DR   NCBIfam; TIGR00497; hsdM; 1.
DR   PANTHER; PTHR42933:SF1; SITE-SPECIFIC DNA-METHYLTRANSFERASE (ADENINE-SPECIFIC); 1.
DR   PANTHER; PTHR42933; SLR6095 PROTEIN; 1.
DR   Pfam; PF12161; HsdM_N; 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   ECO:0000313|EMBL:KFB76681.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000021315};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KFB76681.1}.
FT   DOMAIN          13..166
FT                   /note="N6 adenine-specific DNA methyltransferase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12161"
FT   DOMAIN          182..490
FT                   /note="DNA methylase adenine-specific"
FT                   /evidence="ECO:0000259|Pfam:PF02384"
SQ   SEQUENCE   527 AA;  58244 MW;  3ABBD32B70ABF653 CRC64;
     MANNNKEAER AELHKTIWRI ANDLRGSVDG WDFKTYVLGM LFYRFISENL ASYLNEQERK
     AGTPDFDYAR LSDADAEFGR VETVKEKGFY ILPSELFANV RARARHDANL NETLSRIFAD
     IEGSATGSDS ENDIKGLFDD LDVNSSKLGP TVAKRNEKLV KLLDAIGDLP LASTEGGFTE
     NTIDLFGDAY EYLMTMYAST AGKSGGEFFT PQEVSELLAR ITVVGKSEVN KVYDPACGSG
     SLLLKFVKVL GHDKVRQGFF GQEINLTTYN LCRINMFLHD VNFEKFDIAH GDTLTDPAHW
     DDEPFEAIVS NPPYSIKWDG DANPLLINDP RFAPAGVLAP KSKADLAFTM HILSWLAVNG
     TAAIVEFPGV LYRGGAEQKI RQYLIDNNYV DAVIQLPPDL FFGTTIATCI IVLKKSKHDN
     ATLFIDASAE FVRSGNKNKL LPEHHQKILD AYTGRKNIAH FARLVDNGDI AANGYNIAVS
     SYVEQADTSE AVDIAALNAE IARIVARQAE LRTQIDAIVA DLEGESE
//
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