ID A0A1A7R1T2_9FLAO Unreviewed; 476 AA.
AC A0A1A7R1T2;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=LX77_02884 {ECO:0000313|EMBL:RAJ21130.1};
OS Gelidibacter algens.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Gelidibacter.
OX NCBI_TaxID=49280 {ECO:0000313|EMBL:RAJ21130.1, ECO:0000313|Proteomes:UP000248987};
RN [1] {ECO:0000313|EMBL:RAJ21130.1, ECO:0000313|Proteomes:UP000248987}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12408 {ECO:0000313|EMBL:RAJ21130.1,
RC ECO:0000313|Proteomes:UP000248987};
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 (JUN-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 -!- 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:RAJ21130.1}.
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DR EMBL; QLLQ01000012; RAJ21130.1; -; Genomic_DNA.
DR RefSeq; WP_066433182.1; NZ_QLLQ01000012.1.
DR AlphaFoldDB; A0A1A7R1T2; -.
DR STRING; 49280.A9996_08530; -.
DR REBASE; 171056; M.Gal536ORF8530P.
DR OrthoDB; 9814572at2; -.
DR Proteomes; UP000248987; 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; 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; 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 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 6..128
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 139..439
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 476 AA; 54594 MW; AC7B9541B9474188 CRC64;
MSNITTNIKG IRDIMRKDTG VDGDAQRISQ MVWMLFMKIF ADKEEEWEIT LDNYESPIPE
NLKWQNWAAD DEGLTGDALM DFIDNKLFPA LKDLDITISP QAHIIRSVFD DTYNYMKNGT
LFRQVINVID QIDFNSTTER HLFNDIYETI LKELQSAGSS GEYYTPRAVT QFMVDMINPQ
LGESVLDPAC GTGGFLTCTI DHIREQVKTP KDREIMQNSI RGVEKKPLPH LLCTTNLMLN
GFDLPAVRRD NLLSKPYADW GAKDKLDIIV TNPPFGGVEE DGTETNFPQK FRTKETADLF
LALIIKLLKN NGRCAIVLPD GTLFGEGMKT RLKEELLERC NLHTIVRLPN GVFNPYTSIK
TNLLFFEKGT PTKDIWYFEH PYPEGVKSYN KGKPIHIKEF DLEKAWWDNR EENENAWKVS
IDDIKKRNFN LDIKNPHQEA DDLASPEELL AKFEATEKKI SSIQDEIINV LTEALK
//
