ID A0A117S195_9ACTN Unreviewed; 701 AA.
AC A0A117S195;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=AQJ91_13230 {ECO:0000313|EMBL:KUO20855.1};
OS Streptomyces dysideae.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=909626 {ECO:0000313|EMBL:KUO20855.1, ECO:0000313|Proteomes:UP000053260};
RN [1] {ECO:0000313|EMBL:KUO20855.1, ECO:0000313|Proteomes:UP000053260}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RV15 {ECO:0000313|EMBL:KUO20855.1,
RC ECO:0000313|Proteomes:UP000053260};
RA Ruckert C., Abdelmohsen U.R., Winkler A., Hentschel U., Kalinowski J.,
RA Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces sp. RV15, isolated from a marine
RT sponge.";
RL Submitted (OCT-2015) 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:KUO20855.1}.
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DR EMBL; LMXB01000031; KUO20855.1; -; Genomic_DNA.
DR RefSeq; WP_067020115.1; NZ_KQ949080.1.
DR AlphaFoldDB; A0A117S195; -.
DR STRING; 909626.AQJ91_13230; -.
DR OrthoDB; 9784823at2; -.
DR Proteomes; UP000053260; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
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: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.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 4: Predicted;
KW Endonuclease {ECO:0000313|EMBL:KUO20855.1};
KW Hydrolase {ECO:0000313|EMBL:KUO20855.1};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Nuclease {ECO:0000313|EMBL:KUO20855.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053260};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 9..142
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 171..494
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 701 AA; 79291 MW; 65F83B6EA8EFE9BA CRC64;
MNSNKHTELA NHIWSVADLL RGDYKQSEYG KVILPFTVLR RLECVLEPTK NKVVEQAAAL
KDQEDIDADR WLRRASGLTF YNSSTYTLKK IASDAGHTDE HLIEYIGAFS PNAKEVLERY
EFARQITKLH DAKLLYKVMG RFADLDLRPV ERDENGELVL DDKGQPKVVV SNHQMGYVFE
ELIRRFAEQS NETAGEHFTP REVIELMVNL LIAPDEDALT IPGAVRTVLD PACGTGGMLT
ATEEHIRAFN QDATVKVYGQ ELNPESWAIC RSDLMIKGQD PDNIKYGNSF SKDGHKEDRD
DPDKVTKFDY LLANPPFGVE WKKVKDEVEH EYETLGESGR FGAGLPRIND GSLLFLQHML
SKRQPAEWVP PKGPDEPGRW KGGSRIAIVF NGSPLFTGAA ESGESKIRQW ILENDWLEGI
VALPDQLFYN TGISTYFWIL TNRKAPGHQG KVVLLDAREH FIKMRKSLGD KRKKIDDKQI
EELTRLYGEA LDVASNPEHP LYNKVKVFKN EDFGYHRITV ERPLKLRFEI TEAVLASLAV
SKPVQKLEKA EAFIEALKPV IGQRWLTKSE AWVAMKDAVV AAGLTWPTGA PFNKALRDAV
GVRDSEGEAQ TLKGGAHEPD PELRDYENVP LEEDVEAYLK REVLPHEPDA WIDHDKTKVG
YEIPFTRHFY VYEPPRPLAE IDAELKALEA QIQTLLGEVA G
//
