ID A0A433RXK8_9BACL Unreviewed; 670 AA.
AC A0A433RXK8;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
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=QI30_02335 {ECO:0000313|EMBL:RUS58011.1};
OS Kurthia sp. 3B1D.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Kurthia.
OX NCBI_TaxID=1562256 {ECO:0000313|EMBL:RUS58011.1, ECO:0000313|Proteomes:UP000288623};
RN [1] {ECO:0000313|EMBL:RUS58011.1, ECO:0000313|Proteomes:UP000288623}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3B1D {ECO:0000313|EMBL:RUS58011.1,
RC ECO:0000313|Proteomes:UP000288623};
RA Lawson J.N., Gonzalez J.E., Rinauldi L., Xuan Z., Firman A., Shaddox L.,
RA Trudeau A., Shah S., Reiman D.;
RT "Genome sequence and analysis of novel Kurthia sp.";
RL Submitted (NOV-2014) 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:RUS58011.1}.
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DR EMBL; JTFC01000008; RUS58011.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A433RXK8; -.
DR OrthoDB; 9814572at2; -.
DR Proteomes; UP000288623; 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; 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:RUS58011.1};
KW Hydrolase {ECO:0000313|EMBL:RUS58011.1};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Nuclease {ECO:0000313|EMBL:RUS58011.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000288623};
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..140
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 155..452
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 670 AA; 76538 MW; 8DCFBBF65DA17400 CRC64;
MINFQDKVSF IWSIAEILRG PYKPEDYGKI VLPLAVLRRF DCVLESTKEE VLAKAEQFAT
MSEEAREPIL NRVSKQNFHN ISKYDFKKLL TDSDNIADNL RDYINGFSKV ARDIMEHFDF
DRQIDKLDQN NLLYLTIKRF SELDLHPETV SNVEMGYVFE ELIRRFSEHA EAGDHYTPRE
VIRLMTHLLF LHDDANILTK PGLTQTLYDA AAGTGGMGSV AQEYLLNLNP TAHLEFFGQE
INPESYAICK ADLLIKGEDA TNIRLGNTLS NDKFPTDKFD YLISNPPYGV DWKSYEKPIK
AEHEQQGFDG RFGPGTPRTS DGQLLFLLHL LSKMKDVTPE NPQGSRLAII MNGSPLFTGD
AGSGESEIRK YVLENDLVEG IVALPNDLFY NTGIATYIWI LTNNKAPLSK GKVRLINAVD
FYKKMKKSMG SKRNEIREDQ LNEIVRLYGD AQPNEYVKIF DNEDFGYAKI TVERPLRLNF
QVSEERLARV VEEKGFANLA TSKKKGDAAH FEMEEGKKLQ AQILHVLRTL ESDEVYKNRE
TFTKILKDAL AEATIKLGAP VLKAILNGLS EKDETADVCM KNKKDIEPDT DLRDTESVPL
KENIEEYFAR EVLPHVPDAW IDQSKTKIGY EIPFTRQFYK YTALRSSAEI MDEIRTLEVE
IAEQLKKVME
//