ID Q2RHW5_MOOTA Unreviewed; 516 AA.
AC Q2RHW5;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
GN OrderedLocusNames=Moth_1672 {ECO:0000313|EMBL:ABC19974.1};
OS Moorella thermoacetica (strain ATCC 39073 / JCM 9320).
OC Bacteria; Bacillota; Clostridia; Moorellales; Moorellaceae; Moorella.
OX NCBI_TaxID=264732 {ECO:0000313|EMBL:ABC19974.1};
RN [1] {ECO:0000313|EMBL:ABC19974.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 39073 {ECO:0000313|EMBL:ABC19974.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chertkov O., Saunders E.H., Brettin T.,
RA Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Anderson I., Richardson P., Ragsdale S.;
RT "Complete sequence of Moorella thermoacetica ATCC 39073.";
RL Submitted (DEC-2005) 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};
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DR EMBL; CP000232; ABC19974.1; -; Genomic_DNA.
DR RefSeq; YP_430517.1; NC_007644.1.
DR AlphaFoldDB; Q2RHW5; -.
DR STRING; 264732.Moth_1672; -.
DR REBASE; 11709; M.Mte39073ORF1672P.
DR EnsemblBacteria; ABC19974; ABC19974; Moth_1672.
DR KEGG; mta:Moth_1672; -.
DR PATRIC; fig|264732.11.peg.1812; -.
DR eggNOG; COG0286; Bacteria.
DR HOGENOM; CLU_013049_4_2_9; -.
DR OrthoDB; 9814572at2; -.
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 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; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR038333; T1MK-like_N_sf.
DR PANTHER; PTHR42933; SLR6095 PROTEIN; 1.
DR PANTHER; PTHR42933:SF3; TYPE I RESTRICTION ENZYME MJAVIII 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.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:ABC19974.1};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 12..146
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 159..475
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
FT COILED 480..507
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 516 AA; 58693 MW; 7FE7CB3CD71B3BE6 CRC64;
MTENTNMDLS TLENWLWEAA CVIRGAVDAP KYKDYILPLI FLKRLSDVFE DEIARLAEEI
FDSIEEALKQ VEEDHALVRF YIPPQARWDA ISRQTTNIGE YLTSAVRAVA RENPKLHGIF
ENIDFNAQMA GQPVIDNDRL YNLIQVLSRH RLGLKDVEVD ILGRAYEYLL RKFAEGQGQS
AGEFYTPREV TWLMAYLLEP RPGDEIYDPA CGSGGLLIKS VLALKETYGD DPRIAPVKIY
GQEILYTTFA MAKMNAFIHD LEADIRLGDT MARPAFTNPD GSLRTFDKVT ANPMWNQKFP
LPLYEEDPFD RFKFGGIPPA SSADWGWIQH MFASLKEGGK MAVVLDTGSV SRGSGNQGSN
RERDIRKVFV ENDLVECVIL LPENMFYNTT APGIIMVINK AKKHPAEILL INASKLFTKG
RPKNYMEDEH IKQVYSIYRE WREEEGLSKI IPVEEAARND YNLSPSRYVS INGKEEYRPI
EEILVELAEV EEERQAVDKE LNDILGKLGF GGWLNG
//
