ID D3AEW1_9CLOT Unreviewed; 300 AA.
AC D3AEW1;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
GN ORFNames=CLOSTHATH_02145 {ECO:0000313|EMBL:EFC99619.1};
OS Hungatella hathewayi DSM 13479.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; Hungatella.
OX NCBI_TaxID=566550 {ECO:0000313|EMBL:EFC99619.1, ECO:0000313|Proteomes:UP000004968};
RN [1] {ECO:0000313|EMBL:EFC99619.1, ECO:0000313|Proteomes:UP000004968}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13479 {ECO:0000313|EMBL:EFC99619.1,
RC ECO:0000313|Proteomes:UP000004968};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (JAN-2010) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFC99619.1}.
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DR EMBL; ACIO01000160; EFC99619.1; -; Genomic_DNA.
DR RefSeq; WP_006772667.1; NZ_GG667635.1.
DR AlphaFoldDB; D3AEW1; -.
DR HOGENOM; CLU_072010_0_0_9; -.
DR Proteomes; UP000004968; Unassembled WGS sequence.
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 Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR003356; DNA_methylase_A-5.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
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 PRINTS; PR00507; N12N6MTFRASE.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 4: Predicted;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 153..285
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..51
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 300 AA; 34868 MW; 0AC3502965702077 CRC64;
MFWNKKKPKS KPQIKTTVPK TFKAKEPPPK WQPTFGETKK KGEKPPEVTT KSEPKIDWED
KFLKSFQKLT YRRRAWDVWR DYILLHACSI SNVLDKDNYD QREKLYLKII HQYSKEEQAI
FPELAAYTTM ALDRNQEQDF LGKMFMRLDL GNRSAGQFFT PYHVCELMAE VVATNALEKI
EQYGYISIND PCCGAGATLI AGVHVIRKQL EHCEPPRNYQ NHILVVAQDV DEIVGLMCYI
QISLLGLAGF IKIGNSITDP ISTDDSSEKY WYTPMYFSDV WSTRRMLRQI NKLFGKGDDE
//
