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Database: UniProt
Entry: A0A0S2I3P5_9BACT
LinkDB: A0A0S2I3P5_9BACT
Original site: A0A0S2I3P5_9BACT 
ID   A0A0S2I3P5_9BACT        Unreviewed;      1073 AA.
AC   A0A0S2I3P5;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
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=L21SP5_03166 {ECO:0000313|EMBL:ALO16781.1};
OS   Salinivirga cyanobacteriivorans.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Salinivirgaceae;
OC   Salinivirga.
OX   NCBI_TaxID=1307839 {ECO:0000313|EMBL:ALO16781.1, ECO:0000313|Proteomes:UP000064893};
RN   [1] {ECO:0000313|EMBL:ALO16781.1, ECO:0000313|Proteomes:UP000064893}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L21-Spi-D4 {ECO:0000313|EMBL:ALO16781.1,
RC   ECO:0000313|Proteomes:UP000064893};
RA   Spring S., Bunk B., Sproer C., Klenk H.-P.;
RT   "Description and complete genome sequence of a novel strain predominating
RT   in hypersaline microbial mats and representing a new family of the
RT   Bacteriodetes phylum.";
RL   Submitted (NOV-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; CP013118; ALO16781.1; -; Genomic_DNA.
DR   RefSeq; WP_057954132.1; NZ_CP013118.1.
DR   AlphaFoldDB; A0A0S2I3P5; -.
DR   REBASE; 131154; BspD4ORF3166P.
DR   KEGG; blq:L21SP5_03166; -.
DR   PATRIC; fig|1307839.3.peg.3328; -.
DR   OrthoDB; 9759819at2; -.
DR   Proteomes; UP000064893; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0006306; P:DNA methylation; IEA:InterPro.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR003356; DNA_methylase_A-5.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR041635; Type_ISP_LLaBIII_C.
DR   PANTHER; PTHR33841; DNA METHYLTRANSFERASE YEEA-RELATED; 1.
DR   PANTHER; PTHR33841:SF5; TYPE II METHYLTRANSFERASE M.HINDII; 1.
DR   Pfam; PF02384; N6_Mtase; 1.
DR   Pfam; PF18135; Type_ISP_C; 1.
DR   PRINTS; PR00507; N12N6MTFRASE.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000313|EMBL:ALO16781.1};
KW   Helicase {ECO:0000313|EMBL:ALO16781.1};
KW   Hydrolase {ECO:0000313|EMBL:ALO16781.1};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Nucleotide-binding {ECO:0000313|EMBL:ALO16781.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000064893};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          295..509
FT                   /note="DNA methylase adenine-specific"
FT                   /evidence="ECO:0000259|Pfam:PF02384"
FT   DOMAIN          693..1065
FT                   /note="Type ISP restriction-modification enzyme LLaBIII C-
FT                   terminal specificity"
FT                   /evidence="ECO:0000259|Pfam:PF18135"
SQ   SEQUENCE   1073 AA;  124358 MW;  6E05FF06EFD68E54 CRC64;
     MIQTYLNKIN TRFKNGISKE HSYRGDLETL IRELVPGIEI TNEPANVTDC GNPDYVITKG
     KIPIGYIEAK DIGKDLNNKG YKEQFDRYRN ALENLIITDY TWFQFFQNGE LVHEIRIGEI
     ENNQIKPLNG NFAQFTNLIQ NFATFIGQTI KSPKKLAEMM AAKAKLLQNI LENAVTSDEE
     TQENTSLQGQ YKTFQNILIH DLTPKGFADI YAQTLAYGMF AARLHDTTLE DFSRQEAAEL
     IPKSNPFLRK LFGYVAGPDI DERIKRTVDN LADVFRATNI RELLKNFGKT TQTHDPIIHF
     YETFLAEYDP KLRKTRGVWY TPEPVVNFIV CAVDDILKTE FNLPDGLADT TKTKIKVPVA
     GSKKPMEKEV HKVQILDPAT GTGTFLAEVV KFIYNKKFKA MQGAWSSYVD EHLIPRLNGF
     ELLMASYSMA HLKLDMLLQE TGYNPTKTQR FNIYLTNSLE EHHPDTGTLF SNWLSTEANE
     ANHIKRDTPV MCVIGNPPYS GESSNKGEWI MNLMEDYKRE PGGKEKLKER NPKWINDDYV
     KFLRYGQYYI EKNGSGVLAY INPHGFLDNP TFRGMRWNLL KTYDKIYTID LHGNSKKKET
     APDGSLDFNV FDIQQGVSIN IFVKTGKKQV NKLANVLHYD LYGKRDFKYD FLNKKSIQSI
     DFNELTNVAP MYFMVQKDFE AQKTYDEGFL VSKLFSLSNV GIVTSRDEFT IHQSKEEVKS
     TIDEFLSLED EDARKKFNLG KDVRDWKVSY AKADLNKYYP DKGSFTKISY RPFDDKWTFF
     TGKSKGFHCY PRKEVMQHFL KDENIGLVVA RQCASDWRYI FISKLIGEFN LTGTAGRYGS
     GNYFPLYLYP DTQNDGMYAI EKLSKKGSKP NLNMKIVVQI EEKLGLDFES EKSANKNKFA
     PIDLLDYIYA VLHSPSYRKK YKEFLKTDFP RIPYPKYKET FWNLVELGKQ IREIHLLESS
     KVEEYITSYP KDGDNTITRK IAQKDWEITD TKKQLGRIWI NDEQYFENIP LVAWEFYIGG
     YQPAQKWLKD RAPKKGEPGR TLSYEDILHY QKIIVALTET DWLMQEVDKI EFE
//
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