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Database: UniProt
Entry: A0A285NIG5_9PSED
LinkDB: A0A285NIG5_9PSED
Original site: A0A285NIG5_9PSED 
ID   A0A285NIG5_9PSED        Unreviewed;       944 AA.
AC   A0A285NIG5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, 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   ORFNames=SAMN05660463_01120 {ECO:0000313|EMBL:SNZ08703.1};
OS   Pseudomonas sp. URIL14HWK12:I9.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1261633 {ECO:0000313|EMBL:SNZ08703.1, ECO:0000313|Proteomes:UP000232228};
RN   [1] {ECO:0000313|EMBL:SNZ08703.1, ECO:0000313|Proteomes:UP000232228}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=URIL14HWK12:I9 {ECO:0000313|EMBL:SNZ08703.1,
RC   ECO:0000313|Proteomes:UP000232228};
RA   Ehlers B., Leendertz F.H.;
RL   Submitted (SEP-2017) 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; OBEM01000002; SNZ08703.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A285NIG5; -.
DR   OrthoDB; 9784823at2; -.
DR   Proteomes; UP000232228; 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   Gene3D; 3.90.220.20; DNA methylase specificity domains; 1.
DR   Gene3D; 3.30.950.30; Schlafen, AAA domain; 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; IPR044946; Restrct_endonuc_typeI_TRD_sf.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR007421; Schlafen_AlbA_2_dom.
DR   InterPro; IPR038461; Schlafen_AlbA_2_dom_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   Pfam; PF04326; SLFN_AlbA_2; 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   4: Predicted;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:SNZ08703.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000232228};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          10..141
FT                   /note="N6 adenine-specific DNA methyltransferase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12161"
FT   DOMAIN          156..453
FT                   /note="DNA methylase adenine-specific"
FT                   /evidence="ECO:0000259|Pfam:PF02384"
FT   DOMAIN          797..929
FT                   /note="Schlafen AlbA-2"
FT                   /evidence="ECO:0000259|Pfam:PF04326"
SQ   SEQUENCE   944 AA;  105891 MW;  7B09453B777F0B5D CRC64;
     MNTENHSQTA AFLWSIADLL RGDFKQSQYG RIILPFTLLR RMECELAPTK DEVIKQTFAH
     EGRPDTVREM FLRRATGHLQ FFNASPLTLA TLSNTQTAAD LTSYVQAFST DARDIFEHFH
     FEGFVQQLAR ANLLYQVVQR FAATDLSPER ISNFGMGLIF EELIHKFSES SNETVGEHFT
     PRDIARLTTS LVITEQDGKL APNSIVTIYD PTAGTGGFLS EGNGYIQSIS NKVTVSLYGQ
     DINSESYAIC KANMLIKGQD ITSVKLGNTL SNDQLAEKSF DFMLSNPPFG VEWKKIQKQI
     TDEYTEKGFD GRFGPGLPRV SDGSLLFLLH LVSKMRDPRD GGSRIGIILN GSPMFTGGAG
     SGESEIRRYL LQNDLVEAVV ALPADMFYNT SIATYLLVMS NRKSADRIGK VQLIDASTIY
     APMRKSIRNK RKFFAEEQVA EIIKLYEAFK DGSNSKILFN TELGYQSITI ERPLRLSFSV
     TPTKLAAYER FKGSEQVELL GKVKGWFDNF PDFLIAAGIK SLTQGAEKAV LACFGERDPN
     AKPMLKNNGE FIADIYGRKL VSVPLSQSVE DYFDREIRPY AEDSWLAPPS GDKTDRKIGI
     IGYEINFNRF KVQGQIERLE SQYKSYSSSS LGHLAMAVID GGRVEQLLHR ENSLYFNKKG
     SPRVKSVLNV DSKSHKDYIQ VVIGKEAVAD YIVTFFHSEL GALCLAACMQ GVTVKYFRSD
     DLDRIVVALP SLDEQKEIVN TSRKLKSLKE AIERFDSEVA LNPTSSSSLN HRLDGMLEVI
     GRLTVEDKIR NIIRMGETDV TELKSSFSLD IKKQEKADYI EDASLKTVVA FLNTDGGSLL
     IGVSDDGELL GLNDEINRFH KGSKDKFLLY FKNKLKSRVG EQYYPFISTK LVILDGKNVL
     WIDCKSSVNP CYLYGQDFYV RTNPATDKLE GPKLVEYVKN HFGY
//
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