ID A0A420DF25_9FLAO Unreviewed; 688 AA.
AC A0A420DF25;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
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=BXY80_2714 {ECO:0000313|EMBL:RKE90247.1};
OS Ichthyenterobacterium magnum.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Ichthyenterobacterium.
OX NCBI_TaxID=1230530 {ECO:0000313|EMBL:RKE90247.1, ECO:0000313|Proteomes:UP000284892};
RN [1] {ECO:0000313|EMBL:RKE90247.1, ECO:0000313|Proteomes:UP000284892}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26283 {ECO:0000313|EMBL:RKE90247.1,
RC ECO:0000313|Proteomes:UP000284892};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (SEP-2018) 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 -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC {ECO:0000256|ARBA:ARBA00006594}.
CC -!- SIMILARITY: Belongs to the type-I restriction system S methylase
CC family. {ECO:0000256|ARBA:ARBA00010923}.
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:RKE90247.1}.
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DR EMBL; RAQJ01000008; RKE90247.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A420DF25; -.
DR Proteomes; UP000284892; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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; 1.10.287.1120; Bipartite methylase S protein; 1.
DR Gene3D; 3.90.220.20; DNA methylase specificity domains; 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; IPR000055; Restrct_endonuc_typeI_TRD.
DR InterPro; IPR044946; Restrct_endonuc_typeI_TRD_sf.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR038333; T1MK-like_N_sf.
DR PANTHER; PTHR42933; SLR6095 PROTEIN; 1.
DR PANTHER; PTHR42933:SF4; TYPE I RESTRICTION ENZYME ECOKI METHYLASE SUBUNIT; 1.
DR Pfam; PF12161; HsdM_N; 1.
DR Pfam; PF01420; Methylase_S; 1.
DR Pfam; PF02384; N6_Mtase; 1.
DR PRINTS; PR00507; N12N6MTFRASE.
DR SUPFAM; SSF116734; DNA methylase specificity domain; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:RKE90247.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000284892};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 21..140
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 153..456
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
FT DOMAIN 495..656
FT /note="Type I restriction modification DNA specificity"
FT /evidence="ECO:0000259|Pfam:PF01420"
SQ SEQUENCE 688 AA; 78977 MW; BF03908F7F1A4362 CRC64;
MFEQTFKNID DLLYKDSGAD SELDYIGQTS WVMFLRYLDE LEQDKADEAE LKGEEYKFIL
DEEYRWPNWA MPKGADGKLD HHKAMTGPDL VQFVDNRLFP YLAEFKQKAD NPKTIEYKIG
EIFSELKNKI QSGYNLREIL EYADELPFRA STDKHELSHL YESKIKNMGN AGRNGGQYYT
PRPLIRAMIN VVDPQIGEKI YDGAAGSCGF LCEAYEYMYE RMEKTTDNLK TLQEETLYGK
EKKNLAYVIG IMNMILHGIE APNIIHVNTL GENIRDIQEK NRYHVILANP PFGGKERKEV
QQNFDIKTGE TASLFLQHFI KSLKAGGRAA IVIKNTFLSN ADNASISLRK HLLESCDLHT
ILDLPVGTFT GVGQKTVVLF FTKGSPTKKI WTYELKVDRS LGKRSPLADN DLVEFLEKQN
NFEVSDNSWF THVSEIDENS FDLKISNPNK ADEISDRLPN DIVEEITSLN DETNQLLNDG
FFQRYLQALD SNRQEEWEIS TLGQSCDFFN GKAHEKAIDI NGDFVVVNSK FISTEGEVRK
FTQNQIFPLF ENDVVLVMSD VPNGKALAKC FLIDEDDKYS LNQRICAIRS DRFNSKFLYY
QLNRNKHYLK FNNGENQTNL RKSDILDCPL IIPPIEIQNQ IVEVLDRMKE ITDQVELNIK
ANSALIEELK LSVSGLPFLI ENNELAEN
//
