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
//