ID A0A2U1E4N0_9FIRM Unreviewed; 867 AA.
AC A0A2U1E4N0;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=C7381_104145 {ECO:0000313|EMBL:PVY94639.1};
OS Ezakiella coagulans.
OC Bacteria; Bacillota; Tissierellia; Ezakiella.
OX NCBI_TaxID=46507 {ECO:0000313|EMBL:PVY94639.1, ECO:0000313|Proteomes:UP000245793};
RN [1] {ECO:0000313|EMBL:PVY94639.1, ECO:0000313|Proteomes:UP000245793}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20705 {ECO:0000313|EMBL:PVY94639.1,
RC ECO:0000313|Proteomes:UP000245793};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (APR-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 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:PVY94639.1}.
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DR EMBL; QEKV01000004; PVY94639.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U1E4N0; -.
DR Proteomes; UP000245793; 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:0006306; P:DNA methylation; IEA:InterPro.
DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR Gene3D; 3.90.220.20; DNA methylase specificity domains; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR003356; DNA_methylase_A-5.
DR InterPro; IPR000055; Restrct_endonuc_typeI_TRD.
DR InterPro; IPR044946; Restrct_endonuc_typeI_TRD_sf.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR42933:SF1; SITE-SPECIFIC DNA-METHYLTRANSFERASE (ADENINE-SPECIFIC); 1.
DR PANTHER; PTHR42933; SLR6095 PROTEIN; 1.
DR Pfam; PF01420; Methylase_S; 1.
DR Pfam; PF02384; N6_Mtase; 2.
DR PRINTS; PR00507; N12N6MTFRASE.
DR SUPFAM; SSF116734; DNA methylase specificity domain; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:PVY94639.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000245793};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 335..482
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
FT DOMAIN 487..623
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
FT DOMAIN 690..851
FT /note="Type I restriction modification DNA specificity"
FT /evidence="ECO:0000259|Pfam:PF01420"
SQ SEQUENCE 867 AA; 99037 MW; 22195A69D0ACA08D CRC64;
MIEKWKLEDD VNDFVKNTLS EIDLKKLKDY NVESGMSEYM KDALKGSAKT KTKTNFGKPD
FHIEKYDIPV IFEDKLGSKK LISKNKDGIK NDEKSIRNFA TNGAIHYATQ MIASGKYKEV
VAIGVAGDNE ENVKFDIYYV FGSSFKSVKR MDEYFNIDFL ENKKTFSHFY KDCVLTEEEK
HEILITSRTL LQKYAGELNK LMHNHNITAP QRVLYVSGML LSMQDIVDEN GNMIQRGLIP
EDLLGAKTDT KRDGILITNQ IKEYLKQKQI KQEKVDLMLS SFSEISKDNQ RDEPTDLDKL
VSKLLDKEAS TNKQIFTYIF NNIFMSIDAM AGHLDIMGEM YSEFLKYALG DGKEIGIVLT
PPYVTKMMAE MLNVNKDSRT MDLATGSAGF LISSMEIMID DANKTFGKDT SKANKKIEEI
KKEQLLGVEL NAEMFTLAAT NMILRGDGSS NIRKGNTFRT PEELYTNFKS NRLLLNPPFS
FEENGMPFIR FGLSKMEKGG LAAIIIQDSA GSGRAVSSNQ EILKNNTLLA SIKMPVDLFI
PMAGVQTSIY VFEAGTPHDY EKTVKFIDFR NDGYKRTKRG LNEIDSPTER YQDIIKIYKA
GKNAKVNENL WDIDEIYIED FISDGGNDWN FEQHKKIDTK PKLEDFKNTV ADYIAWEVSN
ILKSEESTSK KSLIPRLEKL EKEFIESGGE WKEYKVGDLF DIHPTKNYGL TNVKLFETKG
ETPIIVNSSL NNGVGGYVDL DPLEKKGIIT FSDTTTADSI FYQPRDFIGY SHIQGMYPYD
SENWTKKSML YFCSAFKRST QGLFDYANKF NREKAREILV ALPFLNGKIN FSYMEKFIEE
LEADRIEELE AYLMATGLKD YKLTKED
//
