ID   A0A1K1N626_SELRU        Unreviewed;      1059 AA.
AC   A0A1K1N626;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, 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=SAMN02910323_1201 {ECO:0000313|EMBL:SFW30811.1};
OS   Selenomonas ruminantium.
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC   Selenomonas.
OX   NCBI_TaxID=971 {ECO:0000313|EMBL:SFW30811.1, ECO:0000313|Proteomes:UP000182958};
RN   [1] {ECO:0000313|Proteomes:UP000182958}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C3 {ECO:0000313|Proteomes:UP000182958};
RA   Varghese N., Submissions S.;
RL   Submitted (NOV-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 N(4)/N(6)-methyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00006594}.
CC   -!- SIMILARITY: Belongs to the type-I restriction system S methylase
CC       family. {ECO:0000256|ARBA:ARBA00010923}.
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DR   EMBL; FPJA01000005; SFW30811.1; -; Genomic_DNA.
DR   RefSeq; WP_072305899.1; NZ_FPJA01000005.1.
DR   AlphaFoldDB; A0A1K1N626; -.
DR   Proteomes; UP000182958; 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; 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; IPR000055; Restrct_endonuc_typeI_TRD.
DR   InterPro; IPR044946; Restrct_endonuc_typeI_TRD_sf.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR42933; SLR6095 PROTEIN; 1.
DR   PANTHER; PTHR42933:SF4; TYPE I RESTRICTION ENZYME ECOKI METHYLASE SUBUNIT; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Reference proteome {ECO:0000313|Proteomes:UP000182958};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          404..679
FT                   /note="DNA methylase adenine-specific"
FT                   /evidence="ECO:0000259|Pfam:PF02384"
FT   DOMAIN          893..1028
FT                   /note="Type I restriction modification DNA specificity"
FT                   /evidence="ECO:0000259|Pfam:PF01420"
FT   COILED          1028..1055
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1059 AA;  122566 MW;  B48D6E92392212B2 CRC64;
     MITIKNFVKA LQLMRFTESD GWYAKYFPDY DVYLKVDLEN KKLYYPDAIK GRERNDFFDD
     AHKENMVVFE CVNRLLEKGY RPEHIELEKE WHLGHDAKGG RADICVTDPN GKMLFIIECK
     TAGREYEAEL RQINVDGGQL FSYWQQERGC EWLLLYASDL EDDRLSYRTD SISCIDDSNV
     QIARKQDSSI KVYEDAHTTE ELFSVWDETY EKRLFDDVVF RDDTVAYEIG AKPLRKKDLR
     DFSEGDKIVN RFEEILRHNN VSDKENAFNR LVALFICKLV DEIQKGEDDI VEFQYKVGTD
     TYENLQDRLQ RLHRDGMEKF MREEIFYVAD DYAENLIQQY TGQKRTKLIA ELKKTLRILK
     FYTNNDFAFK DVHNEELFYQ NGKILVEVVQ LFEAYRIIGS NDLQTLGDLF EQLLSKGFKQ
     NEGQFFTPIP ITRFIWDSLP LKKVFQRNER EYPKIIDYAC GAGHFLTQGY EAINDFLHLE
     DRAWVADKLY GVEKDYRLAR VSKISLFMHG AGNGNIVFGD GLENYTDKNI SPRSFDILVA
     NPPYAVSAFK PHLKLKDNDF SILSKISNNG SEIETLFVER IAQLLKPQGV AAVVLPSSIL
     NKENESFIAA RESLLQNFRL RAIVQLGSKT FGATGTNTVV LFLEKFAEPP KKIDLCSDSV
     QAILTAQSLE DWEDKEILAA YLAKIHTQRE SYSEFVTRQR NYDDWHDVPY LDAYYKAFIA
     SSEYGTKVKQ KGYQALPDDK KMEWCNYHFY DFALSREAEK LLYFSLAYGQ STLIITAPND
     NKGQEKFLGY GWSNRKGQEG IQIKKLGGLM YNPQDREAVN TLAALVRASF GTEEEVSGDL
     GEYYHYLSVT DMLDFSGVDF NKAIKTTKIR HQVLKEGMTA YKLDSKEFSV SIGNRVVAAE
     IEEDGEYPVY SANVFEEFGR INKQNLTDFS QPSVIWGIDG DWMVNYLPEN YPFYPTDHCG
     VIRVNTDKIL PKYLALALQV EGEYERFSRS NRASTTRIKN LTVEIPDVEV QGRIVEKIES
     IDKQIALLGE MNLSKKDMQA KIDELRNEKE SVIEKHFKC
//