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Database: UniProt
Entry: A0A0S4LJN1_9BACT
LinkDB: A0A0S4LJN1_9BACT
Original site: A0A0S4LJN1_9BACT 
ID   A0A0S4LJN1_9BACT        Unreviewed;       654 AA.
AC   A0A0S4LJN1;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
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=COMA2_30069 {ECO:0000313|EMBL:CUS37086.1};
OS   Candidatus Nitrospira nitrificans.
OC   Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC   Nitrospira.
OX   NCBI_TaxID=1742973 {ECO:0000313|EMBL:CUS37086.1, ECO:0000313|Proteomes:UP000198736};
RN   [1] {ECO:0000313|Proteomes:UP000198736}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Luecker S., Luecker S.;
RL   Submitted (OCT-2015) 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; CZPZ01000023; CUS37086.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S4LJN1; -.
DR   STRING; 1742973.COMA2_30069; -.
DR   Proteomes; UP000198736; 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; 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   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:CUS37086.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198736};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CUS37086.1}.
FT   DOMAIN          13..85
FT                   /note="N6 adenine-specific DNA methyltransferase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12161"
FT   DOMAIN          111..426
FT                   /note="DNA methylase adenine-specific"
FT                   /evidence="ECO:0000259|Pfam:PF02384"
SQ   SEQUENCE   654 AA;  73699 MW;  9E0279D8CB50329C CRC64;
     MNKAKIVHQD PALRQAAGQD FYNTSKFTLR DLKARASQQQ LKADFGAYLD GFSPNVQDIL
     EKFEFRNQIP RLSKSDALGT LINKFLSPDI NLSPNPVKNP DGSVKHPGLD NHAMGTIFEE
     LVRRFNEENN EEAGEHWTPR DAVKLMAKLI FLPIADQIKS GTYLLYDGAC GTGGMLTVAE
     ETLQQLAAEH NKKVAAHLYG QEINAETYAI AKADFLLKGE GEAADNIVGG PEYSTLANDA
     FPSREFDFML SNPPYGKSWK SDLERLGGKE GIKDSRFVIQ HAGEAEYSLI TRSSDGQMLF
     LANMLSKMKH KTKLGSRIAE VHNGSSLFTG DAGQGESNIR RWIIENDWLE GIVALPLNMF
     YNTGIATYIW VLANRKSAHR KGKVQLIDAT QWFKPLRKNL GKKNCELSED DITRICDTFI
     DFKETEQSKI FPNETFGYWK VTIERPLRLR VDLDAQSLSA FRTICEEEEE APLSNLAERV
     AGQLGPGPHL NFNEFVKTVE ADAEKHNIKL TGARKKLLKD QLAKRDETAA EVIRKIHKPG
     KNKPDPLRGL FETTIDGKLC VTEYEPDTDL RDTEQIPLLE DGGIEAFIRR EVLPHVPDAW
     YDAESVKTGY EISFTRYFYK PQPLRLLEEI RADIMALEKE MEGLLGEIIG DTRR
//
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