ID A0A1V2QKS3_9PSEU Unreviewed; 658 AA.
AC A0A1V2QKS3;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, 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=ALI22I_17900 {ECO:0000313|EMBL:ONI88840.1};
OS Saccharothrix sp. ALI-22-I.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharothrix.
OX NCBI_TaxID=1933778 {ECO:0000313|EMBL:ONI88840.1, ECO:0000313|Proteomes:UP000188617};
RN [1] {ECO:0000313|EMBL:ONI88840.1, ECO:0000313|Proteomes:UP000188617}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ALI-22-I {ECO:0000313|EMBL:ONI88840.1,
RC ECO:0000313|Proteomes:UP000188617};
RX PubMed=28087533;
RA Yeager C.M., Gallegos-Graves V., Dunbar J., Hesse C.N., Daligault H.,
RA Kuske C.R.;
RT "Polysaccharide degradation capability of Actinomycetales soil isolates
RT from a semi-arid grassland of the Colorado Plateau.";
RL Appl. Environ. Microbiol. 0:0-0(2017).
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:ONI88840.1}.
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DR EMBL; MTQP01000058; ONI88840.1; -; Genomic_DNA.
DR RefSeq; WP_077006649.1; NZ_MTQP01000058.1.
DR AlphaFoldDB; A0A1V2QKS3; -.
DR STRING; 1933778.ALI22I_17900; -.
DR OrthoDB; 9784823at2; -.
DR Proteomes; UP000188617; 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 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 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:ONI88840.1};
KW Hydrolase {ECO:0000313|EMBL:ONI88840.1};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Nuclease {ECO:0000313|EMBL:ONI88840.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000188617};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 8..126
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 153..449
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
FT REGION 563..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 564..586
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 658 AA; 73933 MW; 6ECDFFF744ED3F27 CRC64;
MSSTHTRLAG FIWSVADLLR GDYKQSEYGK VILPFTVLRR LDCVLAPTKS QVLERKAKLA
EQGVQNLDML KRATGGLSFY NTSKLDFRAA VRDQDNVASN LKSYVGAFSE NAREIFEAYD
FTAQLGRLDG AGLTYQVASK FAEIDLSPEA VDNHQMGYAF EELIRRFSEI SNETAGEHFT
PREVIKLMVN LLLAPDEQDL VTPGVVKTVL DPACGTGGML TAAEDFILQH NPQAKVVPHG
QELNAESYAI CKSDMMIKGE NAANIKLGNS FSQDKHYGKS FDYLLANPPF GVEWKKVKDD
VEVEAKIGFA GRFGAGLPRI NDGSLLFLQH MIHHMKKPEQ GGSRLAIVFN GSPLFTGAAE
SGESKIRQWI LENDWLEAVV ALPDQLFYNT GISTYFWILT NRKDEAHRGK VILLDAREHW
AKMRKSLGDK RKYLPNEDIA KLTELYGEAL TAAEDAGHPM HEKVKVFTPR DFGYRRITVE
RPLRLRFEVT GEALAELEVV KPLAKYEGRE KLIEALRGLV DEPAVFRKVD FAKTLKETLA
SLGKLPATVD KAVWGVVSVS DPEGELQTDR KGDPLPDPDL RDNENVPLDE DVDEYMAREV
LPHVPDAWVD HTKTKVGYEI PFTRHFYKYV PPRPLEEIDA ELRELEDRIQ RLLGEVAE
//
