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Database: UniProt
Entry: I3Z345_BELBD
LinkDB: I3Z345_BELBD
Original site: I3Z345_BELBD 
ID   I3Z345_BELBD            Unreviewed;       478 AA.
AC   I3Z345;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE            EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
GN   OrderedLocusNames=Belba_1022 {ECO:0000313|EMBL:AFL83663.1};
OS   Belliella baltica (strain DSM 15883 / CIP 108006 / LMG 21964 / BA134).
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC   Belliella.
OX   NCBI_TaxID=866536 {ECO:0000313|EMBL:AFL83663.1, ECO:0000313|Proteomes:UP000006050};
RN   [1] {ECO:0000313|Proteomes:UP000006050}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15883 / CIP 108006 / LMG 21964 / BA134
RC   {ECO:0000313|Proteomes:UP000006050};
RA   Lucas S., Copeland A., Lapidus A., Goodwin L., Pitluck S., Peters L.,
RA   Mikhailova N., Davenport K., Kyrpides N., Mavromatis K., Pagani I.,
RA   Ivanova N., Ovchinnikova G., Zeytun A., Detter J.C., Han C., Land M.,
RA   Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA   Tindall B., Pomrenke H., Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Belliella baltica DSM 15883.";
RL   Submitted (JUN-2012) 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}.
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DR   EMBL; CP003281; AFL83663.1; -; Genomic_DNA.
DR   RefSeq; WP_014771670.1; NC_018010.1.
DR   AlphaFoldDB; I3Z345; -.
DR   STRING; 866536.Belba_1022; -.
DR   REBASE; 49032; M.Bba15883ORF1022P.
DR   KEGG; bbd:Belba_1022; -.
DR   PATRIC; fig|866536.3.peg.1054; -.
DR   eggNOG; COG0286; Bacteria.
DR   HOGENOM; CLU_018284_4_0_10; -.
DR   OrthoDB; 9814572at2; -.
DR   Proteomes; UP000006050; Chromosome.
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   CDD; cd02440; AdoMet_MTases; 1.
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; 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.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:AFL83663.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006050};
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:AFL83663.1}.
FT   DOMAIN          8..133
FT                   /note="N6 adenine-specific DNA methyltransferase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12161"
FT   DOMAIN          144..447
FT                   /note="DNA methylase adenine-specific"
FT                   /evidence="ECO:0000259|Pfam:PF02384"
SQ   SEQUENCE   478 AA;  54669 MW;  7970217F1B99EDC4 CRC64;
     MANIKGIVDG IRKIMWQDTG LNGDAQRIEQ LGWMLFLKIF SDKDKELETL KDDYVSPIPA
     ELHWDAWAGD DEGMTGDKLQ EFVDRELFPK LRNLKVGVTN DLPNKRALIV REVFQGNNNY
     MKSGINIRKV LNKLNEIDFN IAKDRHAFGE IYETILKELQ SAGKSGEFYT PRAITEFITE
     MINPQLGEKI LDPSCGTGGY LTAAIEHLKK QANSVEELES ISNNIIGWEY KPLPYLLATT
     NLILHDVEVP NITFRDSLEQ PLSAYTEKNR VNVILANPPF GGIVANNNEK NFPQNYRTKE
     SADLFLVLMV HLLKKVGRAG IVLPDGSLTG GGIKERVRQK LLEECNLHTI IRLPNSVFQP
     YATVATNLLF FTKGEKTKEV WYYEHRLPED QKAYSKTKPL QLDELDPIKT WWNDRKESEI
     SWKVDIKTII ERNYDLDIKN PTKVEESVEH SSEDLIKMLE ASFQKSNELF NQLKAAVK
//
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