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Database: UniProt
Entry: D5BJQ3_ZUNPS
LinkDB: D5BJQ3_ZUNPS
Original site: D5BJQ3_ZUNPS 
ID   D5BJQ3_ZUNPS            Unreviewed;       521 AA.
AC   D5BJQ3;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   24-JAN-2024, entry version 61.
DE   RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE            EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
GN   OrderedLocusNames=ZPR_3435 {ECO:0000313|EMBL:ADF53751.1};
OS   Zunongwangia profunda (strain DSM 18752 / CCTCC AB 206139 / SM-A87) (Wangia
OS   profunda).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Zunongwangia.
OX   NCBI_TaxID=655815 {ECO:0000313|EMBL:ADF53751.1, ECO:0000313|Proteomes:UP000001654};
RN   [1] {ECO:0000313|EMBL:ADF53751.1, ECO:0000313|Proteomes:UP000001654}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18752 / CCTCC AB 206139 / SM-A87
RC   {ECO:0000313|Proteomes:UP000001654};
RX   PubMed=20398413; DOI=10.1186/1471-2164-11-247;
RA   Qin Q.L., Zhang X.Y., Wang X.M., Liu G.M., Chen X.L., Xie B.B., Dang H.Y.,
RA   Zhou B.C., Yu J., Zhang Y.Z.;
RT   "The complete genome of Zunongwangia profunda SM-A87 reveals its adaptation
RT   to the deep-sea environment and ecological role in sedimentary organic
RT   nitrogen degradation.";
RL   BMC Genomics 11:247-247(2010).
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; CP001650; ADF53751.1; -; Genomic_DNA.
DR   RefSeq; WP_013072839.1; NC_014041.1.
DR   AlphaFoldDB; D5BJQ3; -.
DR   STRING; 655815.ZPR_3435; -.
DR   REBASE; 25827; M.ZprORF3435P.
DR   KEGG; zpr:ZPR_3435; -.
DR   eggNOG; COG0286; Bacteria.
DR   HOGENOM; CLU_013049_4_1_10; -.
DR   OMA; EMARTQH; -.
DR   OrthoDB; 9814572at2; -.
DR   Proteomes; UP000001654; Chromosome.
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   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; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR038333; T1MK-like_N_sf.
DR   PANTHER; PTHR42998; TYPE I RESTRICTION ENZYME HINDVIIP M PROTEIN-RELATED; 1.
DR   PANTHER; PTHR42998:SF1; TYPE I RESTRICTION ENZYME HINDVIIP M PROTEIN-RELATED; 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.
PE   4: Predicted;
KW   Methyltransferase {ECO:0000313|EMBL:ADF53751.1};
KW   Transferase {ECO:0000313|EMBL:ADF53751.1}.
FT   DOMAIN          12..138
FT                   /note="N6 adenine-specific DNA methyltransferase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12161"
FT   DOMAIN          151..476
FT                   /note="DNA methylase adenine-specific"
FT                   /evidence="ECO:0000259|Pfam:PF02384"
SQ   SEQUENCE   521 AA;  59930 MW;  47F03821D3C2D012 CRC64;
     MAKKKTTKEK SIEESLWDAA NKLRGSIEPS EYKHVVLGLI FLKFASDKFE VRREELIAEG
     KEKYLEMKDF YNMKNVFFLA ETSRWNYLIK NAKQDDIALK IDTALNQIEK NNPSLKGALP
     DNYFSRLGLD KSKLSALLDT INKIDTQKDK SQDIVGRVYE YFLSKFALAE GKGKGEFYTP
     KSIVNLIAEM IEPYKGIIYD PACGSGGMFV QSIKFIESHH GSKREISIYG QEYTNTTYKL
     AKMNLAIRGI SANLGDKAAD TFSNDQHKDL KADYIMANPP FNQKDWRGPQ ELIDDPRWQG
     YEVPPKSNAN YGWILNMVSK LSDDGVAGFI LANGALSGGG EEYKIRRKLV ENNLVEAIII
     LPQNMFYTTN ISVTVWILNR NKTAHTRSIG DEERHYRDRH EEVLFMDLRQ NGEPFEKKFI
     QFSGTQIKDI ARTYHDWQQE DTNYKDIPEY CYSATKADIE KKDFSLVPSK YIEFVNRDEN
     IDFDTKMAGL QTELTDLLQQ EEDSKKELLD VFKELGYAIK L
//
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