ID I0JPR4_HALH3 Unreviewed; 330 AA.
AC I0JPR4;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 45.
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=HBHAL_3789 {ECO:0000313|EMBL:CCG46134.1};
OS Halobacillus halophilus (strain ATCC 35676 / DSM 2266 / JCM 20832 / KCTC
OS 3685 / LMG 17431 / NBRC 102448 / NCIMB 2269) (Sporosarcina halophila).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halobacillus.
OX NCBI_TaxID=866895 {ECO:0000313|EMBL:CCG46134.1, ECO:0000313|Proteomes:UP000007397};
RN [1] {ECO:0000313|EMBL:CCG46134.1, ECO:0000313|Proteomes:UP000007397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35676 / DSM 2266 / JCM 20832 / KCTC 3685 / LMG 17431 /
RC NBRC 102448 / NCIMB 2269 {ECO:0000313|Proteomes:UP000007397};
RX PubMed=22583374; DOI=10.1111/j.1462-2920.2012.02770.x;
RA Saum S.H., Pfeiffer F., Palm P., Rampp M., Schuster S.C., Muller V.,
RA Oesterhelt D.;
RT "Chloride and organic osmolytes: a hybrid strategy to cope with elevated
RT salinities by the moderately halophilic, chloride-dependent bacterium
RT Halobacillus halophilus.";
RL Environ. Microbiol. 15:1619-1633(2013).
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; HE717023; CCG46134.1; -; Genomic_DNA.
DR RefSeq; WP_014644023.1; NC_017668.1.
DR AlphaFoldDB; I0JPR4; -.
DR STRING; 866895.HBHAL_3789; -.
DR KEGG; hhd:HBHAL_3789; -.
DR PATRIC; fig|866895.3.peg.2816; -.
DR eggNOG; COG0827; Bacteria.
DR HOGENOM; CLU_073534_0_0_9; -.
DR Proteomes; UP000007397; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro.
DR GO; GO:0006306; P:DNA methylation; IEA:InterPro.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 1.10.150.470; -; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR003356; DNA_methylase_A-5.
DR InterPro; IPR016843; S-AdoMet-dep_Ade-MeTrfase_prd.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR048375; YtxK-like_N.
DR PANTHER; PTHR42933; SLR6095 PROTEIN; 1.
DR PANTHER; PTHR42933:SF3; TYPE I RESTRICTION ENZYME MJAVIII METHYLASE SUBUNIT; 1.
DR Pfam; PF02384; N6_Mtase; 1.
DR Pfam; PF21106; YtxK_like; 1.
DR PIRSF; PIRSF026567; Adenine_mtase_bact_prd; 1.
DR PRINTS; PR00507; N12N6MTFRASE.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 4: Predicted;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Reference proteome {ECO:0000313|Proteomes:UP000007397};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 7..85
FT /note="YtxK-like N-terminal helical"
FT /evidence="ECO:0000259|Pfam:PF21106"
FT DOMAIN 95..293
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 330 AA; 37563 MW; A5D497E11963FDE8 CRC64;
MKQEQVEKLF QWVDETADTI SKDMNITYLE AIAETLDILF NGQPFKDMSK ELQTKLTNEL
TKINKDNFEK EEIRKAVQLA ILKGMKGATQ QQHLITPDSV AMFMGYLASK LIDNEENLKL
FDPASGSGNL ITSVMNQLEM PLTAYASEVD PTLIQLAVTN ANLQKNNIEF FHQDSLQPFL
MEPVDFVLAD LPVGYYPDDV QASRYQLKAE EGHSYAHHLF IEQGLNYTKE GGYLMFIVPN
FLFESDQSRE LNTFLRENAH IVGMLQLSDS LFKNEKHGKS ILILQKKGPE TKPPKQALLV
KLPSFKNPNA MGDILGQMNQ WFDEYKTAQL
//
