ID   A0A1L7FBM1_9PSEU        Unreviewed;       676 AA.
AC   A0A1L7FBM1;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
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=UA75_21050 {ECO:0000313|EMBL:APU22199.1};
OS   Actinoalloteichus sp. GBA129-24.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Actinoalloteichus.
OX   NCBI_TaxID=1612551 {ECO:0000313|EMBL:APU22199.1, ECO:0000313|Proteomes:UP000185506};
RN   [1] {ECO:0000313|EMBL:APU22199.1, ECO:0000313|Proteomes:UP000185506}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GBA129-24 {ECO:0000313|EMBL:APU22199.1,
RC   ECO:0000313|Proteomes:UP000185506};
RA   Ruckert C., Nouioui I., Willmese J., van Wezel G., Klenk H.-P.,
RA   Kalinowski J., Zotchev S.B.;
RT   "Complete genome sequence of Actinoalloteichus fjordicus DSM 46856
RT   (=GBA129-24).";
RL   Submitted (JUN-2016) 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};
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DR   EMBL; CP016077; APU22199.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1L7FBM1; -.
DR   STRING; 1612551.UA75_21050; -.
DR   REBASE; 182734; M.Asp12924ORF21050P.
DR   KEGG; acti:UA75_21050; -.
DR   OrthoDB; 9784823at2; -.
DR   Proteomes; UP000185506; Chromosome.
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   CDD; cd02440; AdoMet_MTases; 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; IPR003356; DNA_methylase_A-5.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR044946; Restrct_endonuc_typeI_TRD_sf.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR42998:SF1; TYPE I RESTRICTION ENZYME HINDI METHYLASE SUBUNIT; 1.
DR   PANTHER; PTHR42998; TYPE I RESTRICTION ENZYME HINDVIIP M PROTEIN-RELATED; 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   4: Predicted;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Methyltransferase {ECO:0000313|EMBL:APU22199.1};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW   Transferase {ECO:0000313|EMBL:APU22199.1}.
FT   DOMAIN          194..413
FT                   /note="DNA methylase adenine-specific"
FT                   /evidence="ECO:0000259|Pfam:PF02384"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   676 AA;  72710 MW;  393E3D6FDCFFBAC0 CRC64;
     MTEDISPRRR HPAGDSSEPA VGPGDAGAPP PEAATVAAGD IARLAGVGKA AVSNWRRRFD
     DFPDAVGGSA ASPLYALADV ENWLRRHGKN FEVPLREQLW PRVRGAADDL RLGAFVASLG
     AFLVFHQRAG HTWRPTDEVG LLDAVLADAP ELSETVRALW QGPQEDVLRT LVELVESEGH
     VAAFDFLYER HRDAHARRAV YTSPELAELM VRVAGIDGGT VLDPSCGTGT LLLTAYDCGA
     SEILGQEPDD VVATLARIRL LLRGAAPDIV VGDALRADAH GDRRADAVVV NPPFNERSWG
     YDELVGDLRW EYGQPPRGES ELAWVQHCLA HVDSAGIVVA AMPGAVADRR SGRRIRGNLL
     RAGVLRAVIS SAELGMSADG TATEPDLWVF RKGTESTTPS HVLMVGRSQD AEQAWQAFAE
     DPAADLPESC RAVRIIDLLD DVVDLTPTRW LPVEPDTAVA ASFTPVVAEL RAALGRLTDA
     LPDLDVHSDT AERAMTTVGE LVRSGLITMF QAPTRMPTDT GSLPVLTLDD LNRGTVPSGH
     CEQTGDTVLI QPGDVIVPMI PREPLVRLAV EAGAALGPRL LLFRANQDRI VPGFLAAHLR
     FAANTVGGRA GTTGSRPEVR RTPIPRISLQ EQQQYGKAFD RMTAFEDALR QTARLGESLV
     RRGFTGLADG TLRSAR
//