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Database: UniProt
Entry: A0A1G9QLP7_9BURK
LinkDB: A0A1G9QLP7_9BURK
Original site: A0A1G9QLP7_9BURK 
ID   A0A1G9QLP7_9BURK        Unreviewed;       493 AA.
AC   A0A1G9QLP7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, 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=SAMN05428957_102414 {ECO:0000313|EMBL:SDM11896.1};
OS   Oryzisolibacter propanilivorax.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Oryzisolibacter.
OX   NCBI_TaxID=1527607 {ECO:0000313|EMBL:SDM11896.1, ECO:0000313|Proteomes:UP000198552};
RN   [1] {ECO:0000313|Proteomes:UP000198552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EPL6 {ECO:0000313|Proteomes:UP000198552};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-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}.
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DR   EMBL; FNHP01000002; SDM11896.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G9QLP7; -.
DR   STRING; 1527607.SAMN05428957_102414; -.
DR   OrthoDB; 9784823at2; -.
DR   Proteomes; UP000198552; 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   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198552};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          6..131
FT                   /note="N6 adenine-specific DNA methyltransferase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12161"
FT   DOMAIN          141..454
FT                   /note="DNA methylase adenine-specific"
FT                   /evidence="ECO:0000259|Pfam:PF02384"
SQ   SEQUENCE   493 AA;  55367 MW;  735562DA8B00AAB3 CRC64;
     MSNLTPVIKS IQDVMRQDSG VDGDAQRIGQ LTWLLFLKVF DALEEELELT RDHYASPLPE
     ALRWRAWAAD AEGMTGDALL DFVDQQLFPA LKNLPADPQR NPRGYVLRSV FEDAYNYMKS
     GHLLRQVVNK LNAIDFNRQA ERHQFNDLYE KILRDLQSAG NAGEFYTPRA VTQFMVDMTN
     PQLGESVMDP ATGTGGFLVC AIEHLRKQVH NAEQEAVLQN SIRGVEKKQL PHMLCVTNLL
     LHGIEVPSQI AHDNTLARPL RDYSNADRVD VILTNPPFGG IEEPGIEQGF PADVRTKETA
     DLFLVLIQHL LKPGGRAAVV LPDGFLFGEG VKARIKEQLL QHCNLHTIVR LPNGVFAPYT
     GIKTNLLFFT KGQPTQHIWY YEHPYPQGVK TYNKTKPIRI DEFDAEKAWW GNEADGFAAR
     VENERAWKVG IDAIRAANWN LDQKNPHVGE QQSHDPEVLL ADYARLQAEA QALRDELKGI
     LAECLNAKTA AGA
//
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