ID D4CBV1_9CLOT Unreviewed; 522 AA.
AC D4CBV1;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, 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 Name=hsdM {ECO:0000313|EMBL:EFE12697.1};
GN ORFNames=CLOM621_06883 {ECO:0000313|EMBL:EFE12697.1};
OS Clostridium sp. M62/1.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=411486 {ECO:0000313|EMBL:EFE12697.1, ECO:0000313|Proteomes:UP000004936};
RN [1] {ECO:0000313|EMBL:EFE12697.1, ECO:0000313|Proteomes:UP000004936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M62/1 {ECO:0000313|EMBL:EFE12697.1,
RC ECO:0000313|Proteomes:UP000004936};
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., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (FEB-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:EFE12697.1}.
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DR EMBL; ACFX02000016; EFE12697.1; -; Genomic_DNA.
DR RefSeq; WP_008396812.1; NZ_GG730311.1.
DR AlphaFoldDB; D4CBV1; -.
DR HOGENOM; CLU_013049_0_2_9; -.
DR OrthoDB; 9814572at2; -.
DR Proteomes; UP000004936; 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:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC.
DR GO; GO:0009307; P:DNA restriction-modification system; IEA:InterPro.
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; IPR004546; Restrct_endonuc_T1M.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR038333; T1MK-like_N_sf.
DR NCBIfam; TIGR00497; hsdM; 1.
DR PANTHER; PTHR42933:SF1; SITE-SPECIFIC DNA-METHYLTRANSFERASE (ADENINE-SPECIFIC); 1.
DR PANTHER; PTHR42933; SLR6095 PROTEIN; 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 4: Predicted;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:EFE12697.1};
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:EFE12697.1}.
FT DOMAIN 14..162
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 175..476
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 522 AA; 59404 MW; FEAE38D86BF0B348 CRC64;
MDNSIQAHQK ELCNKLWAMA NALRGNMEAY EFKNYILGMI FYYYLSDRTE KYMANLLKDD
GIGYEEAWAD EEYKTAVIEE ALRDLGYVIE PQYLFRKMVK MVENRSFDIE FLQSAINALM
ESTIGNDSQE DFDGLFSDMQ LDSSKLGHTV KDRSAVMAKI IASLDEINFG VDDTKIDVLG
NAYEYLIGQF AATAGKKAGE FYTPSGPAEL LCRLACLGLT DVKDAADPTC GSGSLLLRLK
NYANVRNYYG QELTSTTYNL ARMNMILRGV PYRNFNIYNG DTLEHDYFGD MKFRVQVANP
PYSANWSADM HFMEDERFNE YGKLAPKSKA DFAFVQHMVY HMDEDGRAVV LLPHGVLFRG
AAEEVIRKHL IQKLNVLDAV IGLPANLFFG TGIPVCVLVL KRERNGNSDN ILFIDASSDF
EAGKNQNILR ECDIDKIVET YERRQDVDKY AHVATMQEIE ENGFNLNIPR YVDTFEPEPE
IDLNEVAAEI RKLQSEIKDI DAELKPFFDE LGLDFPFDVE GK
//
