ID A0A2K9ETM1_9FIRM Unreviewed; 476 AA.
AC A0A2K9ETM1;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=HVS_15155 {ECO:0000313|EMBL:AUG58880.1};
OS Acetivibrio saccincola.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Acetivibrio.
OX NCBI_TaxID=1677857 {ECO:0000313|EMBL:AUG58880.1, ECO:0000313|Proteomes:UP000233534};
RN [1] {ECO:0000313|EMBL:AUG58880.1, ECO:0000313|Proteomes:UP000233534}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SR1 {ECO:0000313|Proteomes:UP000233534};
RA Pechtl A., Ruckert C., Koeck D.E., Maus I., Winkler A., Kalinowski J.,
RA Puhler A., Schwarz W.W., Zverlov V.V., Schluter A., Liebl W.;
RT "Complete genome sequence of Herbivorax saccincola GGR1, a novel
RT Cellulosome-producing hydrolytic bacterium in a thermophilic biogas plant,
RT established by Illumina and Nanopore MinION sequencing.";
RL Submitted (DEC-2017) 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 -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC {ECO:0000256|ARBA:ARBA00006594}.
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DR EMBL; CP025197; AUG58880.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K9ETM1; -.
DR REBASE; 227340; M.HsaGGR1ORF15155P.
DR KEGG; hsc:HVS_15155; -.
DR Proteomes; UP000233534; Chromosome.
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 CDD; cd02440; AdoMet_MTases; 1.
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; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR038333; T1MK-like_N_sf.
DR PANTHER; PTHR42933; SLR6095 PROTEIN; 1.
DR PANTHER; PTHR42933:SF4; TYPE I RESTRICTION ENZYME ECOKI METHYLASE SUBUNIT; 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 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:AUG58880.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000233534};
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:AUG58880.1}.
FT DOMAIN 4..130
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 140..442
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 476 AA; 55179 MW; 78461F8EB28B7FD1 CRC64;
MSISATIKAV QDIMRQDAGV DGDAQRISQL VWMIFLKVFD AKEEEWELMD DDYTPIIPEG
LRWRDWAADD EGITGDELLD FVNNKLFKEL KEMKLDENSN PKAFIVKAVF EDSYNYMKSG
TLMRQVINKL NEIDFTTQKD RHLFNDIYES ILRDLQSAGN AGEYYTPRPV TQFMVDMVNP
QLGEKVLDFA CGTGGFLVCA LEHLKKQVKN IEDEKTLQET ILGIEKKPLP YMLAVTNLIL
HDIDVPKIRH DNSLARNVRD YKPVDKVDII VTNPPFGGIE EDGILVNFPQ QFQTKETADL
FMVLLMYLLK DNGRAAIVLP DGFLFGEGVK TTIKEKLLEE FNLHTIVRLP NGVFAPYTDI
NTNLLFLEKG KPTKEIWFFE HPLPEGYKKY TKTKPIRHEE FELEKQWWNN REENQYAWKV
SIEEIKSRNY NLDIKNPDKQ TEEFVLSTDE LIDRIDKNLE KSKNLLHELK GVLNNG
//
