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
//