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Database: UniProt
Entry: A0A2V1INP7_9BACT
LinkDB: A0A2V1INP7_9BACT
Original site: A0A2V1INP7_9BACT 
ID   A0A2V1INP7_9BACT        Unreviewed;       867 AA.
AC   A0A2V1INP7;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-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=C5O23_09325 {ECO:0000313|EMBL:PWB01556.1};
OS   Duncaniella muris.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae;
OC   Duncaniella.
OX   NCBI_TaxID=2094150 {ECO:0000313|EMBL:PWB01556.1, ECO:0000313|Proteomes:UP000244905};
RN   [1] {ECO:0000313|Proteomes:UP000244905}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 103720 {ECO:0000313|Proteomes:UP000244905};
RA   Clavel T., Strowig T.;
RL   Submitted (FEB-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:PWB01556.1}.
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DR   EMBL; PUEC01000020; PWB01556.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V1INP7; -.
DR   Proteomes; UP000244905; 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; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Reference proteome {ECO:0000313|Proteomes:UP000244905};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          6..152
FT                   /note="N6 adenine-specific DNA methyltransferase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12161"
FT   DOMAIN          163..483
FT                   /note="DNA methylase adenine-specific"
FT                   /evidence="ECO:0000259|Pfam:PF02384"
FT   REGION          308..327
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          664..691
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   867 AA;  99129 MW;  2DAB12BC56FB7B94 CRC64;
     MNKQQLASKI WASANKMRSK IEANEYKDYI LGFIFYRYLS TEIENFYRTE GWSDEDMPSL
     EEDIDPEYTE YVRKNRGYFI GYKNLFSTWL NKGNDFGVKD VSEALSAFNR LIYPTHKKVF
     SGIFDTLETG LKNLGDSDTT RSSAISKLIQ LIKDIPMDGN QGYDVLGYIY EYLISNFAAS
     AGKKAGEFYT PHEVSVLMAE IVAHHLRDRE KIEIYDPTSG SGSLLITIGR AVAKHNDSPD
     NIKYYAQELK RNTYNLTRMN LVMRGIKPNN IITRNGDTLE HGSDWPMFED DDKETSYEYR
     PMDAVVSNPP YSQEWDRPSD KDSDPRYKDY GLAPKKKADY AFLLHDLYHL KSDGIMAIVL
     PHGVLFRPGD EAEIRRNLIE QNKIEAIIGL PADIFFGTPI ATIVMVLKAN RDNTDVLFID
     ASKYASKDGK KKKLQASDIK RIFDAVTTRP ASIDKFARLV SLKEILENEY DLNIPKYVDS
     SDAVEKWDLY SSLLGGVPRT EIELLKDYWE VMPALKSTLF PEGEYVECLS DNVGDTIRNH
     DDIKKFQAAY NSAFGDYEQY LIAQLIYGMM TLNVAKEVDI LGEDLFNRLS SVPLLDRYAA
     FQALSDCWEQ TATDIEIIQT EGREVLRKIE PNMVMVKNGE DEDEIQKGWK GRIMPFKLVQ
     KTLLPEYLDR VNELQEQLAE TVGEVSALLE ETGEDDAEIL NEDGDAFDNK KVKVQLKLML
     KEYKKRKYTD LPDFPEGSIE AHVVTLTKNA DEQKRLKAEV KDALRELEEK TIFTIESLTE
     EQIRELLRLK WIMPVVDAVK AEHTNVITSL IDKVEALVVK YAVTLNDVEK SISESESKLS
     DMVVSLRGND FDMKALESFK NLLNHGK
//
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