ID   A0A1Q5GI41_9ACTN        Unreviewed;       922 AA.
AC   A0A1Q5GI41;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, 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=AMK22_23330 {ECO:0000313|EMBL:OKJ32225.1};
OS   Streptomyces sp. CB01580.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1703933 {ECO:0000313|EMBL:OKJ32225.1, ECO:0000313|Proteomes:UP000186318};
RN   [1] {ECO:0000313|EMBL:OKJ32225.1, ECO:0000313|Proteomes:UP000186318}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CB01580 {ECO:0000313|EMBL:OKJ32225.1,
RC   ECO:0000313|Proteomes:UP000186318};
RX   PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA   Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA   Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA   Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT   "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL   MBio 7:e02104-e02116(2016).
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:OKJ32225.1}.
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DR   EMBL; LIXJ01000018; OKJ32225.1; -; Genomic_DNA.
DR   RefSeq; WP_073788220.1; NZ_LIXJ01000018.1.
DR   AlphaFoldDB; A0A1Q5GI41; -.
DR   STRING; 1703933.AMK22_23330; -.
DR   OrthoDB; 9784823at2; -.
DR   Proteomes; UP000186318; 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:SF3; TYPE I RESTRICTION ENZYME MJAVIII 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   4: Predicted;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:OKJ32225.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186318};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          9..137
FT                   /note="N6 adenine-specific DNA methyltransferase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12161"
FT   DOMAIN          173..479
FT                   /note="DNA methylase adenine-specific"
FT                   /evidence="ECO:0000259|Pfam:PF02384"
FT   REGION          59..78
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        62..78
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   922 AA;  101132 MW;  F418CCBD600CB795 CRC64;
     MAKLTLDQLE RHLFAAADIL RGTMDAAEYR DFLLVLLFLK RANDEFDAAR DRIIAQEMAQ
     GASREEAEEE ADEPSHYTRD RIIYVPEQAR WAQLAGAVDD VATSYLQPAL DALEGHQGNE
     RLRGLFGHVN FNRIGGGGGT GTSAAKLADK RLAALIGHFG SLRLRGEDFE FPDVIGAAYE
     YLLKDFADSA GAKGGEFYTP RAVVRMMVEL ARPQANQHVY DPCVGSGGML IHTKEYIEEH
     GGDTEDLALA GQDANNGSWV MATMNMLFHG ASDFDLRTGD TLTNPLHIDK SYDVVLSNPP
     FSMDYKADDL PDLDGRMKYG YTSEKGKADL MFLQHMLYMV EGRGGSVFTV MPHGVLFRSG
     AEGDIRARLI EDDLLEAVIG LPSNIFYGTG IPACVLVLRA RGEKHPDRQG KVLFINADRE
     FHSERAQNVL LPEHVEKIVS TFHDEVGDGS GVPRFARWVK RVELEENAYN LNIRRYVDNT
     PPPEPQDVRA HLSGGVPKSE IAAEEKAKLL EAYQVRITDL FADRGPDSAY VDFLPEDRRP
     DAERLTALAE RRERELWDAF DKWWAVETEQ IASLAPYEDD DRTEFEKRSQ LARLRADLID
     SFRKLLLNVD LLDRYALAGA VAGWWQDARN ELKALAGNGF KGVVEGWVDT VEAMLEPEPN
     PWTGGARKRS GAERRQAYGH KVVARIAPDF LRELAEADAL KATLDAKVKA AEEAEAARAA
     AAAGVVEDDG EASGEPGALG PAMAEALLSE ADLKKLKKER TAAGKAVKAL EEAFYPLDGM
     GGAAKAAARL AAAKKKGAGK AAQPAAVAAA GQTALDVTVT GADADVDSGT DAGAEEERPT
     PRLHEVRDAL DEAGAREIVL GILREDLAAK LEGHVVRRRR ELIDAYAGWE RKYLVSLRDI
     EARREAASKR LEGFLEELGY VG
//