ID A0A2P8KK19_9BURK Unreviewed; 819 AA.
AC A0A2P8KK19;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=C7T35_16800 {ECO:0000313|EMBL:PSL83318.1}, GXN78_22300
GN {ECO:0000313|EMBL:NDZ15552.1};
OS Variovorax sp. WS11.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=1105204 {ECO:0000313|EMBL:PSL83318.1, ECO:0000313|Proteomes:UP000241151};
RN [1] {ECO:0000313|EMBL:PSL83318.1, ECO:0000313|Proteomes:UP000241151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WS11 {ECO:0000313|EMBL:PSL83318.1,
RC ECO:0000313|Proteomes:UP000241151};
RA Crombie A.T., Mejia-Florez N.L., Murrell C.;
RT "Isoprene degraders from the Poplar phyllosphere.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:NDZ15552.1, ECO:0000313|Proteomes:UP000479786}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WS11 {ECO:0000313|EMBL:NDZ15552.1,
RC ECO:0000313|Proteomes:UP000479786};
RA Dawson R.A., Larke-Mejia N.L., Crombie A.T., Ul-Haque M.F., Murrell J.C.;
RT "Isoprene oxidation by the Gram negative model bacterium Variovorax sp.
RT WS11.";
RL Submitted (FEB-2020) 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:PSL83318.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JAAGOW010000002; NDZ15552.1; -; Genomic_DNA.
DR EMBL; PXZZ01000021; PSL83318.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P8KK19; -.
DR OrthoDB; 9784823at2; -.
DR Proteomes; UP000241151; Unassembled WGS sequence.
DR Proteomes; UP000479786; 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; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Endonuclease {ECO:0000313|EMBL:PSL83318.1};
KW Hydrolase {ECO:0000313|EMBL:PSL83318.1};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:NDZ15552.1}; Nuclease {ECO:0000313|EMBL:PSL83318.1};
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:NDZ15552.1}.
FT DOMAIN 8..147
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 161..481
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
FT REGION 688..708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 709..778
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 819 AA; 91880 MW; 1BE3EC0C1BBEB5B5 CRC64;
MPLTLPQLER HLFKAADILR GKMDASEFKE YIFGMLFLKR CSDVFDQRRE EVMQRELTAC
KTDAEARESA ELKRWYGQSF YVPPKSRWKY LVNEAHVDVG GFLNRALGGL ESNNSSLAEV
LEHIDFSRKV GQSKIPDIKL RQLISHFSTY RLRNEDFEFP DLLGAAYEYL IGEFADSAGK
KGGEFYTPRS VVRMMVRLVK PEQHHSVYDP CVGSGGMLIL AKEYIDEHGQ DGNRAELFGQ
EANGTVWSIA KMNMLLHGIS TADLRNEDTL AEPQHAEGGE LMRFDRVLSN PPFSINWGTA
DTNRGGQAVW APKFRAERFR YGEVPLGAKK ADLMFLQHMV SVLKDGGQLA TVMPHGVLFR
GGEERAIRAA MIEADLLEAV IGLPANLFYG TGIPACVLVM RQRQGNHSGK PSERQGRVLF
INADREYFEG RAQNHLLPEH IEKIANTFEN FAEVPGFSAI VSNAELRDND CNLNIRRYAD
NVPPPEPHDV RAHLVGGVPK SEVENKAALF KAHGLDALAL LVERDAYYFD FRSELTTRQA
VKNAIETYPG LVAREQEVRD AFDAWWQVHS PRIIALAGAP GLVGLRNDLL HSFSAALEPT
GVLGRFQVRG IVAGFWDDAK YEFMTLMARG ARGVVDAWRI SIRTGIDDDQ SNGNPLGHKL
VKLLMGDFVD ALAELEVRKA ELDSQIKAAT PDKVEREDGE EAEPSDDELA VDDAQLKEWK
RQLVALKKEV KAKEQGFAQR LDGAVDALDD AGAATLLLAV LRNDMQAILD RYVSAQRRQV
IETYETWWDK YRVTLNDIEQ DRKGAATELD SFLRALGYV
//
