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Database: UniProt
Entry: A0A1D2IA54_9ACTN
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Original site: A0A1D2IA54_9ACTN 
ID   A0A1D2IA54_9ACTN        Unreviewed;       836 AA.
AC   A0A1D2IA54;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-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   Name=hsdM {ECO:0000313|EMBL:ODA71345.1};
GN   ORFNames=APS67_004513 {ECO:0000313|EMBL:ODA71345.1};
OS   Streptomyces sp. AVP053U2.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1737066 {ECO:0000313|EMBL:ODA71345.1, ECO:0000313|Proteomes:UP000054731};
RN   [1] {ECO:0000313|EMBL:ODA71345.1, ECO:0000313|Proteomes:UP000054731}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AVP053U2 {ECO:0000313|EMBL:ODA71345.1,
RC   ECO:0000313|Proteomes:UP000054731};
RA   Olsen C.W., Carey S., Hinshaw L., Karasin A.I.;
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};
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:ODA71345.1}.
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DR   EMBL; LMTQ02000027; ODA71345.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1D2IA54; -.
DR   REBASE; 169700; M.Ssp53U2ORF4513P.
DR   Proteomes; UP000054731; 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: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; cd16961; RMtype1_S_TRD-CR_like; 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; IPR000055; Restrct_endonuc_typeI_TRD.
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; PF01420; Methylase_S; 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   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Methyltransferase {ECO:0000313|EMBL:ODA71345.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054731};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW   Transferase {ECO:0000313|EMBL:ODA71345.1}.
FT   DOMAIN          264..563
FT                   /note="DNA methylase adenine-specific"
FT                   /evidence="ECO:0000259|Pfam:PF02384"
FT   DOMAIN          619..792
FT                   /note="Type I restriction modification DNA specificity"
FT                   /evidence="ECO:0000259|Pfam:PF01420"
SQ   SEQUENCE   836 AA;  89935 MW;  7039BD90AA366201 CRC64;
     MRSCCHMTAL PSITAIESAS AAVRAVERGS MRIRKYQQQQ LVSRAAIAEM AGVQRSAITN
     WERRYTDFPS PTRAGGTDYY YLSDALTWLK GRSVPPRARR DDEGADATYA DRARTALVAA
     SEAEAVEDLE AEGFPAAPGT AGDETDGEHL SPADILFREQ DEGQWGSGSR IGFLYLLFSL
     VYLRWAQPRR WAVVRRAAAQ GQAGTHIHRF LPAVAQHVEQ TLAAQGVTSA MAVRLEDLAP
     RSPQAIVRLL DKIESSGRGS FTELLGHHAL EAGLGSRDAF TPPGVARLLA ALLGSSAAQS
     LYDPNGRGGE LLSAVLAARP EQGNEAGGGI PAVTIGSAHP GTRDLAAMNL MVHGARPELL
     NLTGTTRPWT EGHRRRRADL VLTNPPFNVP AVPVDADWWT YGEPPASNAN LAWPQYAVMS
     LNEGGRAAVL MPNSAATSSN LKEQRIRHAL VDRGAVECVI ALPAKMFSAT TISVNVWILK
     PEAQERSSGE VLFIDASGLA TEVSRKLSVL EADDCALIAA AYHSWRGTGG NGAFLPDSRL
     PCAAVRRDVV NAAGSSLRPA DYARPARRPN VDAEALTDPY GALLRSREEA GRADVLADSR
     VAGFRQLGGG LGLPIDTAPD DWEWRNLGEL CELQAGPSPS LLPKDAYVLG GVVPVVQPKH
     LRDRRVADAR GTAVPYDKAQ RLRRFALQEG DILCARTGTV GPVAHVRAGQ VGWLFGSNLI
     RLHRFAPEVC PAYLLAYLSL SRTTEWIKSR SEKTTVPSIS KADLQALPVY LPTWSEQKRI
     AGALGALDEQ IARHLEVAWA ATQVHKELAE QLVGLVALQG PTAPASADTF PERTSR
//
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