ID A0A151Z259_9BACL Unreviewed; 472 AA.
AC A0A151Z259;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, 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=AYX07_04105 {ECO:0000313|EMBL:KYQ87864.1};
OS Thermoactinomyces sp. AS95.
OC Bacteria; Bacillota; Bacilli; Bacillales; Thermoactinomycetaceae;
OC Thermoactinomyces.
OX NCBI_TaxID=1811386 {ECO:0000313|EMBL:KYQ87864.1, ECO:0000313|Proteomes:UP000076382};
RN [1] {ECO:0000313|EMBL:KYQ87864.1, ECO:0000313|Proteomes:UP000076382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AS95 {ECO:0000313|EMBL:KYQ87864.1,
RC ECO:0000313|Proteomes:UP000076382};
RA Bezuidt O.K., Makhalanyane T.P., Pierneef R., Mohamed G.A., Kharroub K.,
RA Cowan D.A.;
RT "Draft genome sequence of Thermoactinomyces sp. AS95.";
RL Submitted (FEB-2016) 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}.
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:KYQ87864.1}.
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DR EMBL; LSVF01000001; KYQ87864.1; -; Genomic_DNA.
DR RefSeq; WP_037995470.1; NZ_LSVF01000001.1.
DR AlphaFoldDB; A0A151Z259; -.
DR STRING; 1811386.AYX07_04105; -.
DR REBASE; 165581; M.TspAS95ORF4105P.
DR OrthoDB; 9814572at2; -.
DR Proteomes; UP000076382; 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; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:KYQ87864.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076382};
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:KYQ87864.1}.
FT DOMAIN 7..108
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 120..422
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
FT COILED 440..467
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 472 AA; 53700 MW; 4B1BE257C44255B0 CRC64;
MTNQEIVQKL WNLCNVLRDD GITYHQYVTE LTYLLFLKML KETGEEYLLP EGYRWDDLSS
KQGLEMHTFY RKLLIHLGEE GEGLVKKIYT NASTNIEEPR NLEKIIRSID QLDWYSAKEE
GLGNLYEGLL EKNASEKKSG AGQYFTPRPL VNVMVKLIDP QPMERCNDPA AGTFGFMIAA
AQHVEKIKDT FEMTQQEAEF FINEQFSGCE LVLDTHRLAL MNAMLHGLKS NILLGDSLSN
LGKEMMNMDV ILSNPPFGTK KGGERPTRDD LTYPTKNKQL NFLQHIYRAL KPNGKARAAV
VLPDNVLFQD GDGRKVRADL MDKCNLHTIL RLPTGIFYAQ GVKTNVLFFT RGVTDHGNTK
EVWFYDLRTN MPSFGKRNPL TEEHFADFIE AYTAEDRHQV DDPRWSCYTR EEIAAKGDTL
DLGLIADKSL SDYENLPDPI ESAEEAIAKL EQAIALLNEV VHELKVTEGG CK
//
