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Database: UniProt
Entry: A0A0N1LEI7_9SPHN
LinkDB: A0A0N1LEI7_9SPHN
Original site: A0A0N1LEI7_9SPHN 
ID   A0A0N1LEI7_9SPHN        Unreviewed;       483 AA.
AC   A0A0N1LEI7;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, 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=IP68_15275 {ECO:0000313|EMBL:KPF73890.1};
OS   Blastomonas sp. AAP25.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Blastomonas.
OX   NCBI_TaxID=1523416 {ECO:0000313|EMBL:KPF73890.1, ECO:0000313|Proteomes:UP000037930};
RN   [1] {ECO:0000313|EMBL:KPF73890.1, ECO:0000313|Proteomes:UP000037930}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AAP25 {ECO:0000313|EMBL:KPF73890.1,
RC   ECO:0000313|Proteomes:UP000037930};
RA   Zeng Y., Feng F., Liu Y., Koblizek M.;
RT   "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT   Revealed by High-throughput Strain Identification and Genome Sequencing.";
RL   Submitted (AUG-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};
CC   -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00006594}.
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:KPF73890.1}.
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DR   EMBL; LJHP01000022; KPF73890.1; -; Genomic_DNA.
DR   RefSeq; WP_054135865.1; NZ_LJHP01000022.1.
DR   AlphaFoldDB; A0A0N1LEI7; -.
DR   PATRIC; fig|1523416.3.peg.1926; -.
DR   OrthoDB; 9806213at2; -.
DR   Proteomes; UP000037930; Unassembled WGS sequence.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0004519; F:endonuclease activity; 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   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:SF4; TYPE I RESTRICTION ENZYME ECOKI 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   3: Inferred from homology;
KW   Endonuclease {ECO:0000313|EMBL:KPF73890.1};
KW   Hydrolase {ECO:0000313|EMBL:KPF73890.1};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Nuclease {ECO:0000313|EMBL:KPF73890.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037930};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          13..105
FT                   /note="N6 adenine-specific DNA methyltransferase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12161"
FT   DOMAIN          153..452
FT                   /note="DNA methylase adenine-specific"
FT                   /evidence="ECO:0000259|Pfam:PF02384"
SQ   SEQUENCE   483 AA;  54457 MW;  E160BAEAA63E4FF4 CRC64;
     MFENAFNNID RAMRNDEGLA SELDYAEQTS WLLFLKYLDD FEAEMEDEAE LEGREYQPIL
     DPQYRWDVWA APKKDTGEID HQVAMTGQDL VDFVNGELFP YLKGFHAAAH DADTIEYKIG
     EIFTEIINRF RSGYSLREVI DIVDTLDFGS SKAKHELSDL YETRIKRMGN AGRNGGEYYT
     PRPLIRAMIK VVDPKIGETI YDGAAGSAGF LCEAFDYLRR PDLSAAEWDI LQRKTFYGQE
     KKSLAYVLGV MNMILHGIEA PQIRHTNTLT ENVMDIQQAD RHDIVLANPP FGGGERKEVQ
     QNFPIKSGET AYLFLQHFIR KLKAGGRGAV VIKNTFLSNT DNASVELRKE LLTSCNLHTV
     LDCPGGTFQG AGVKTVVLFF EKGAPTRQVW YYQLDPGRSL GKTNPLNDAD LAEFVAFQPD
     KADSAKSWTV SVGELDKGTW DLSVRNPSAP EEAPLRAPEQ IIADMLARDE ETRKILEEIR
     GML
//
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