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Database: UniProt
Entry: A0A433RXK8_9BACL
LinkDB: A0A433RXK8_9BACL
Original site: A0A433RXK8_9BACL 
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
//
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