ID A8DJT4_9BACT Unreviewed; 412 AA.
AC A8DJT4;
DT 13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2007, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=DNA methyltransferase {ECO:0000313|EMBL:ABV27284.1};
GN ORFNames=YS_M60-F11.177 {ECO:0000313|EMBL:ABV27284.1};
OS Chloracidobacterium thermophilum.
OC Bacteria; Acidobacteriota; Blastocatellia; Chloracidobacterium.
OX NCBI_TaxID=458033 {ECO:0000313|EMBL:ABV27284.1};
RN [1] {ECO:0000313|EMBL:ABV27284.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=17656724; DOI=10.1126/science.1143236;
RA Bryant D.A., Costas A.M., Maresca J.A., Chew A.G., Klatt C.G.,
RA Bateson M.M., Tallon L.J., Hostetler J., Nelson W.C., Heidelberg J.F.,
RA Ward D.M.;
RT "Candidatus Chloracidobacterium thermophilum: an aerobic phototrophic
RT Acidobacterium.";
RL Science 317:523-526(2007).
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 -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = an N(4)-
CC methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:16857, Rhea:RHEA-COMP:11369, Rhea:RHEA-COMP:13674,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:85452, ChEBI:CHEBI:137933; EC=2.1.1.113;
CC Evidence={ECO:0000256|ARBA:ARBA00001893};
CC -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family. N(4)
CC subfamily. {ECO:0000256|ARBA:ARBA00010203}.
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DR EMBL; EF531339; ABV27284.1; -; Genomic_DNA.
DR AlphaFoldDB; A8DJT4; -.
DR REBASE; 23223; M.CthEORF177P.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:InterPro.
DR GO; GO:0015667; F:site-specific DNA-methyltransferase (cytosine-N4-specific) activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 2.
DR InterPro; IPR017985; MeTrfase_CN4_CS.
DR InterPro; IPR012327; MeTrfase_D12.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF02086; MethyltransfD12; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 2.
DR PROSITE; PS00093; N4_MTASE; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:ABV27284.1};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABV27284.1}.
SQ SEQUENCE 412 AA; 46442 MW; D3AEB5E4FD826519 CRC64;
MVSLPLREQL RRRAEYTHKF NARVGRYGWL RLTPAYSLKI VEELIANHPN AQRILDPFCG
TGTTALCAAC YGRESTTADI NPFLVWLTQT KIARYPAETI EAVQSACQEV LDLVARRAVK
PVSTPPIFNV ERWWSLETLT FLRLLRAAIE KATEPDTPSR NLLLVAFCRT LIELSQAAFN
HQSLSFGNDD GFALPFPVDR GSVFAASVQF VLEGVLENPS GTASVVLADA RTLKDKISGT
FDLVITSPPY VNRMSYIREL RPYMYWLGFL QNGRDAGELD WKAIGGTWGI ATSRLTDWKR
PEGHFRSTRL TNVLQAIACA ENKHGRLLAK YVAKYFDDMW THFCELPKLL AAGAEVHYIV
GNSTFYGTLV PTEQLYAEML SALGFSHIEC RPLRKRNSNK ALVEFDVVAR WK
//
