ID A1BH53_CHLPD Unreviewed; 662 AA.
AC A1BH53;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 88.
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=Cpha266_1712 {ECO:0000313|EMBL:ABL65730.1};
OS Chlorobium phaeobacteroides (strain DSM 266 / SMG 266 / 2430).
OC Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Chlorobium.
OX NCBI_TaxID=290317 {ECO:0000313|EMBL:ABL65730.1, ECO:0000313|Proteomes:UP000008701};
RN [1] {ECO:0000313|EMBL:ABL65730.1, ECO:0000313|Proteomes:UP000008701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 266 {ECO:0000313|EMBL:ABL65730.1,
RC ECO:0000313|Proteomes:UP000008701};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.,
RA Schmutz J., Larimer F., Land M., Hauser L., Mikhailova N., Li T.,
RA Overmann J., Bryant D.A., Richardson P.;
RT "Complete sequence of Chlorobium phaeobacteroides DSM 266.";
RL Submitted (DEC-2006) 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; CP000492; ABL65730.1; -; Genomic_DNA.
DR AlphaFoldDB; A1BH53; -.
DR STRING; 290317.Cpha266_1712; -.
DR REBASE; 14103; M.Cph266ORF1712P.
DR KEGG; cph:Cpha266_1712; -.
DR eggNOG; COG0286; Bacteria.
DR HOGENOM; CLU_013049_4_1_10; -.
DR OrthoDB; 9814572at2; -.
DR Proteomes; UP000008701; 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; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR038333; T1MK-like_N_sf.
DR PANTHER; PTHR42998:SF1; TYPE I RESTRICTION ENZYME HINDI METHYLASE SUBUNIT; 1.
DR PANTHER; PTHR42998; TYPE I RESTRICTION ENZYME HINDVIIP M PROTEIN-RELATED; 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.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Methyltransferase {ECO:0000313|EMBL:ABL65730.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008701};
KW Transferase {ECO:0000313|EMBL:ABL65730.1}.
FT DOMAIN 16..147
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 156..473
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
FT REGION 517..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 624..651
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 531..575
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 662 AA; 72694 MW; 3816321E3C0A00D5 CRC64;
MHWIAPSEKD TATAALEKRL WDAADQLRAN SGLKAQEYSA PVLGLIFLLF ADVRFAARRA
ELESAKSSTR RGSRVDDPAA YHAEGVLYLS PEARFVYLLN RPEAENIGVM VNEAMRAIEK
HNPQLAGVLP KTYYLFDSPL LKQLLKKVSE IPSSMDYDAF GRIYEYFLGE FAMSEGQGGG
EFYTPVSIVR LLTEVIEPYH GRILDPACGS GGMFVSSARF VAQHKQNPSA ELSIHGIEKT
DETGRLCRLN LAVHGLEGRI MHGGNVNSYY DDPHDATGNF DFVLANPPFN VNAVDKERLK
DSVGPGRRFP FGLPRTDNAN YLWIQLFYSA LNERGRAGFV MANSASDARS SEQEIRRQLI
ESRTVDVMVA VGPNMFYTVT LPCTLWFFDK AKARLSPPSS PALLPKVEGG EEDLPLSRRI
LTERDGEGNV PNRADTVLFI DARHIYRQVD RAHRDWTPAQ IGFMANLVRL WRGEALDYTL
GGDEAREKIE EVFAAKSSDP AGLNGQEGHS AHALAAESPA PYGSSDEIEK LPSTFGRRAG
DEGAVKHEGA GNVAYRDEAK EHPSPSGRRA GDEGAVKHEG AGNVAYSDIP GLCKAATLKE
IEAQGWSLNP GRYVGVAPGE AISDEDFKVQ LETLNEELEL LNAQARELEA TIAGNVAQIL
ET
//
