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Database: UniProt
Entry: A0A022KVF9_9ACTN
LinkDB: A0A022KVF9_9ACTN
Original site: A0A022KVF9_9ACTN 
ID   A0A022KVF9_9ACTN        Unreviewed;       298 AA.
AC   A0A022KVF9;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE            EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
DE   Flags: Fragment;
GN   ORFNames=H483_0118525 {ECO:0000313|EMBL:EYT48642.1};
OS   Dietzia sp. UCD-THP.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Dietziaceae;
OC   Dietzia.
OX   NCBI_TaxID=1292020 {ECO:0000313|EMBL:EYT48642.1, ECO:0000313|Proteomes:UP000019757};
RN   [1] {ECO:0000313|EMBL:EYT48642.1, ECO:0000313|Proteomes:UP000019757}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCD-THP {ECO:0000313|EMBL:EYT48642.1,
RC   ECO:0000313|Proteomes:UP000019757};
RX   PubMed=23661480;
RA   Diep A.L., Lang J.M., Darling A.E., Eisen J.A., Coil D.A.;
RT   "Draft Genome Sequence of Dietzia sp. Strain UCD-THP (Phylum
RT   Actinobacteria).";
RL   Genome Announc. 1:E00197-E00113(2013).
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:EYT48642.1}.
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DR   EMBL; AOSR01000171; EYT48642.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A022KVF9; -.
DR   eggNOG; COG0286; Bacteria.
DR   HOGENOM; CLU_935393_0_0_11; -.
DR   Proteomes; UP000019757; 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:0006306; P:DNA methylation; IEA:InterPro.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR003356; DNA_methylase_A-5.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR42933:SF1; SITE-SPECIFIC DNA-METHYLTRANSFERASE (ADENINE-SPECIFIC); 1.
DR   PANTHER; PTHR42933; SLR6095 PROTEIN; 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   Endonuclease {ECO:0000313|EMBL:EYT48642.1};
KW   Hydrolase {ECO:0000313|EMBL:EYT48642.1};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Nuclease {ECO:0000313|EMBL:EYT48642.1};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          4..235
FT                   /note="DNA methylase adenine-specific"
FT                   /evidence="ECO:0000259|Pfam:PF02384"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EYT48642.1"
FT   NON_TER         298
FT                   /evidence="ECO:0000313|EMBL:EYT48642.1"
SQ   SEQUENCE   298 AA;  33153 MW;  BA540E268F0BF137 CRC64;
     NALGIVLTPH HITDLMAELI DVDADDFVID PCAGTAGFLI AAMRRMFDDV DRRYGDRAGV
     LATKQREIRE HRLHGVELQD KLFAIGTTNM ILRGDGKANF RRHSIFDLST EELRGEHGFT
     KALINPPYSQ AKTKETRHLS ELSFIERALS LLNHKGRLAA IVPQSSMVGK TKEDKARKGR
     ILAGHTLDAV ITMNPDTFYG VGTNVVIAMF TAGVPHPASK KTAFVNFKDD GYKVRQHLGL
     MGDGNEKSRR AHLLSVLNDG VADDTSFIVR SEIAATDEWQ HAFFYFTDQP PTYEDFLG
//
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