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Database: UniProt
Entry: A0A433X8V0_9BACL
LinkDB: A0A433X8V0_9BACL
Original site: A0A433X8V0_9BACL 
ID   A0A433X8V0_9BACL        Unreviewed;       515 AA.
AC   A0A433X8V0;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 16.
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=EJP77_11615 {ECO:0000313|EMBL:RUT30482.1};
OS   Paenibacillus zeisoli.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=2496267 {ECO:0000313|EMBL:RUT30482.1, ECO:0000313|Proteomes:UP000272464};
RN   [1] {ECO:0000313|EMBL:RUT30482.1, ECO:0000313|Proteomes:UP000272464}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3-5-3 {ECO:0000313|EMBL:RUT30482.1,
RC   ECO:0000313|Proteomes:UP000272464};
RA   Sun L., Chen Z.;
RL   Submitted (DEC-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   -!- 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:RUT30482.1}.
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DR   EMBL; RZNX01000004; RUT30482.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A433X8V0; -.
DR   OrthoDB; 9814572at2; -.
DR   Proteomes; UP000272464; 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:InterPro.
DR   CDD; cd02440; AdoMet_MTases; 1.
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; IPR004546; Restrct_endonuc_T1M.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR038333; T1MK-like_N_sf.
DR   NCBIfam; TIGR00497; hsdM; 1.
DR   PANTHER; PTHR42933:SF1; SITE-SPECIFIC DNA-METHYLTRANSFERASE (ADENINE-SPECIFIC); 1.
DR   PANTHER; PTHR42933; SLR6095 PROTEIN; 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   4: Predicted;
KW   Methyltransferase {ECO:0000313|EMBL:RUT30482.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000272464};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW   Transferase {ECO:0000313|EMBL:RUT30482.1}.
FT   DOMAIN          10..157
FT                   /note="N6 adenine-specific DNA methyltransferase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12161"
FT   DOMAIN          171..481
FT                   /note="DNA methylase adenine-specific"
FT                   /evidence="ECO:0000259|Pfam:PF02384"
SQ   SEQUENCE   515 AA;  57396 MW;  9C29807DD3047C92 CRC64;
     MSSAAQRAEL QSQIWKIAND VRGSVDGWDF KQYVLGTLFY RFISENFSNY IEAGDESIKY
     ADLPDDIITK EIKEDAIKTK GYFIYPSQLF SNIAKTANTN ESLNTDLAAI FSAIENSANG
     YPSELDIKGL FADFDTTSNR LGNTVKDKNS RLAAVIKGVE GLNFKGFEDS QIDLFGDAYE
     YLISNYAANA GKSGGEFFTP QSVSKLIAQL AIHKLTTINK IYDPAAGSGS LLLQAKKQFD
     AHIIEDGFYG QEINHTTYNL ARMNMFLHNI NYDKFNIAFG NTLLNPQFGD EKPFDAIVSN
     PPYSINWSGS DDPTLINDER FAPAGVLAPK SKADFAFVLH TLNYLSSKGR ASIVCFPGIF
     YRGGAEQKIR KYLIDNNFVE TVISLAPNLF YGTSIAVNIL VLSKHKADTK TQFIDASGVD
     FYKKATNNNI LTDEHIEQIM KIFDSKEEVD HVAKSVDYDA IVQKDYNLSV STYVEPKNTR
     EVIDINELNA EIKTTVAKID QLRAEIDDII EVVES
//
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