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Database: UniProt
Entry: B1R9L2_CLOPF
LinkDB: B1R9L2_CLOPF
Original site: B1R9L2_CLOPF 
ID   B1R9L2_CLOPF            Unreviewed;       514 AA.
AC   B1R9L2;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   27-MAR-2024, entry version 49.
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:EDT23056.1};
GN   ORFNames=AC1_1182 {ECO:0000313|EMBL:EDT23056.1};
OS   Clostridium perfringens B str. ATCC 3626.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=451754 {ECO:0000313|EMBL:EDT23056.1, ECO:0000313|Proteomes:UP000004342};
RN   [1] {ECO:0000313|EMBL:EDT23056.1, ECO:0000313|Proteomes:UP000004342}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B str. ATCC 3626 {ECO:0000313|Proteomes:UP000004342};
RA   Paulsen I., Sebastian Y.;
RT   "Annotation of Clostridium perfringens B str. ATCC 3626.";
RL   Submitted (JUL-2007) 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:EDT23056.1}.
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DR   EMBL; ABDV01000023; EDT23056.1; -; Genomic_DNA.
DR   RefSeq; WP_003459199.1; NZ_ABDV01000023.1.
DR   AlphaFoldDB; B1R9L2; -.
DR   Proteomes; UP000004342; 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:UniProtKB-KW.
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; 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.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:EDT23056.1};
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:EDT23056.1}.
FT   DOMAIN          14..166
FT                   /note="N6 adenine-specific DNA methyltransferase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12161"
FT   DOMAIN          177..480
FT                   /note="DNA methylase adenine-specific"
FT                   /evidence="ECO:0000259|Pfam:PF02384"
FT   COILED          477..511
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   514 AA;  58981 MW;  E082D492B1E8E4C5 CRC64;
     MSTSEIQKEQ QSNLQSNLWN IANDLRGNMD ASEFKNYILG LIFYRYLSEN VESRANKLLE
     EDGVSYEEAW EDEELREALK EELVNDIGYF IEPKFLFDKL LAKIETGDFD IEILEEAINN
     ITESTLGQES EEEFDHLFDD MDLKSTKLGK DVKSRSELIA KVMGKIAQID FRFDNSEIDI
     LGDAYEYLIG QFAANAGKKA GEFYTPQQVS KILAKIVTMG KTDLKNVYDP TCGSGSLLLR
     VSREAKVRMF YGQEKTSTTY NLARMNMLLH GVKYSDFNIK NDDTLENPQH GDLKFEAIVA
     NPPYSAKWSR DDKFLDDERF SAYGKLAPKS KADFAFIQHM IHHLEDNGTM AVVLPHGVLF
     RGAAEGVIRK HLIEQRNVLD AVIGLPANIF FGTSIPTVIL VFKKNRKNAD NIMFIDASNE
     FEKGKNQNVL RDRDVEKIVE TYKKRENVDK YAYVATMEEV KENDYNLNIP RYVDTFEEEE
     EIDIIEVQKN IKELDKEIEE LKKSLEADLK ELGL
//
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