ID D4J8W2_9FIRM Unreviewed; 412 AA.
AC D4J8W2;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 48.
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=CC1_20650 {ECO:0000313|EMBL:CBK80783.1};
OS Coprococcus catus GD/7.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Coprococcus.
OX NCBI_TaxID=717962 {ECO:0000313|EMBL:CBK80783.1, ECO:0000313|Proteomes:UP000008798};
RN [1] {ECO:0000313|EMBL:CBK80783.1, ECO:0000313|Proteomes:UP000008798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GD/7 {ECO:0000313|EMBL:CBK80783.1,
RC ECO:0000313|Proteomes:UP000008798};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT "The genome sequence of Coprococcus catus GD/7.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBK80783.1, ECO:0000313|Proteomes:UP000008798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GD/7 {ECO:0000313|EMBL:CBK80783.1,
RC ECO:0000313|Proteomes:UP000008798};
RA Pajon A.;
RL Submitted (MAR-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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FP929038; CBK80783.1; -; Genomic_DNA.
DR AlphaFoldDB; D4J8W2; -.
DR STRING; 717962.CC1_20650; -.
DR REBASE; 28911; CcaGD7ORF20640P.
DR KEGG; cct:CC1_20650; -.
DR PATRIC; fig|717962.3.peg.1964; -.
DR HOGENOM; CLU_015410_2_0_9; -.
DR Proteomes; UP000008798; Chromosome.
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 CDD; cd02440; AdoMet_MTases; 1.
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:SF1; SITE-SPECIFIC DNA-METHYLTRANSFERASE (ADENINE-SPECIFIC); 1.
DR PANTHER; PTHR42933; SLR6095 PROTEIN; 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:CBK80783.1};
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:CBK80783.1}.
FT DOMAIN 114..238
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 412 AA; 47212 MW; 4878F3E080626DE3 CRC64;
MEELEIRQNV IALHNDLRTV NMPDQYKSLF VSILMLDEVE MLAKNDTEQL MADISYVIAR
RFSGEQAERI SEKFTKSCTV SLIRERKSCE EYSLWWFLQQ LQKIKSQLKE TNMDAISLFY
HVFLSYSSGG RNSLGIVLTP EHIADFMAKV INVQPGDSIL DICCGTGALL NAASHYNGGG
MLYGCERDEG VYDMASISQG VRYENMRLFH SDCYKLRSSN PRLMADKGLL NPPYAMKDHD
ELEFLLEELK MIRPHGLAAA IVPSKTAYVM SEPYITRRRQ LLEEHTLKAV FSMPDDIFNG
NGATAVTCIM VFEAHVPHDP SEKTFFGFFK DDGYKKKGKI GRIDEYGKWG EIRQRWLDLY
HGNIIMDGVS TLASVGAEDE WLCEAYLRND YSKLTEDVFR RTIRDYMAYI IS
//
