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Database: UniProt
Entry: A3XIU5_LEEBM
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Original site: A3XIU5_LEEBM 
ID   A3XIU5_LEEBM            Unreviewed;       816 AA.
AC   A3XIU5;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   24-JAN-2024, entry version 65.
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=MED217_05837 {ECO:0000313|EMBL:EAQ50529.1};
OS   Leeuwenhoekiella blandensis (strain CECT 7118 / CCUG 51940 / KCTC 22103 /
OS   MED217) (Flavobacterium sp. (strain MED217)).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Leeuwenhoekiella.
OX   NCBI_TaxID=398720 {ECO:0000313|EMBL:EAQ50529.1, ECO:0000313|Proteomes:UP000001601};
RN   [1] {ECO:0000313|EMBL:EAQ50529.1, ECO:0000313|Proteomes:UP000001601}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MED217 {ECO:0000313|EMBL:EAQ50529.1,
RC   ECO:0000313|Proteomes:UP000001601};
RX   PubMed=17215843; DOI=10.1038/nature05381;
RA   Gomez-Consarnau L., Gonzalez J.M., Coll-Llado M., Gourdon P., Pascher T.,
RA   Neutze R., Pedros-Alio C., Pinhassi J.;
RT   "Light stimulates growth of proteorhodopsin-containing marine
RT   Flavobacteria.";
RL   Nature 445:210-213(2007).
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:EAQ50529.1}.
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DR   EMBL; AANC01000002; EAQ50529.1; -; Genomic_DNA.
DR   RefSeq; WP_009779551.1; NZ_CH672395.1.
DR   AlphaFoldDB; A3XIU5; -.
DR   STRING; 398720.MED217_05837; -.
DR   eggNOG; COG0286; Bacteria.
DR   eggNOG; COG0732; Bacteria.
DR   HOGENOM; CLU_340608_0_0_10; -.
DR   OMA; NENDIAH; -.
DR   OrthoDB; 9814572at2; -.
DR   Proteomes; UP000001601; Unassembled WGS sequence.
DR   GO; GO:0003677; F:DNA binding; 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; 3.90.220.20; DNA methylase specificity domains; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR003356; DNA_methylase_A-5.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR044946; Restrct_endonuc_typeI_TRD_sf.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR42933:SF3; 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; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF116734; DNA methylase specificity domain; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   4: Predicted;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Methyltransferase {ECO:0000313|EMBL:EAQ50529.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001601};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW   Transferase {ECO:0000313|EMBL:EAQ50529.1}.
FT   DOMAIN          113..385
FT                   /note="DNA methylase adenine-specific"
FT                   /evidence="ECO:0000259|Pfam:PF02384"
SQ   SEQUENCE   816 AA;  93925 MW;  0DCEA3808AC35429 CRC64;
     MKEDNYRDSA EVKMITNQVW KSMSLLRGIL PVEHHHVYLF LLSAYYDGII KNVHIDFSNS
     LCNYIFSSLE SEQKYSEILN VYIPILKSIP EERLNEVLHQ LTMFNNEILD RYFDEIFDDL
     LFRLADNQGK YSGEFLLPNE ISKFVVEIAD MPNWASVFNP FAGLASFATH LNKNQNYYGQ
     EIVSSTWALG MLRLMRLHKH TQINYRVEDS IHNWPGTNNF DLIISNPPFN YKIDPYIAHY
     FGRKKMTAET YVICKGLESI NFDGKVACIV SQGMLFRGSD DQRLRESLVE QGLIETIVSL
     PSGMLKHTGI PICIMILTRK KNINRTIKMI DASSFVESKG KREKRLETNR LLEHLYKFSR
     SKAVVEVPIE QIRKNNYNLN VQRYFVEDFR GVPLIKVVKR ISGKRVGKEK TLIGKFIRTS
     NLKDNDVSYQ LDLNEIKERE LPSHSIKIEN DCILISTRWK SLKPTLFEYK GEPIYIGIDL
     LAIRVYSENF EVNPHYLISE LRSPNVLKQV SAFQNPGAIT SLNRADFFAI KIALPSIEEQ
     KAKVQGILEL SEKFKILQQE RNALAHGKQV KSFDEFASLK HSLGAPRQNI LSNTKSLIRF
     FENNNSEAFL EVKKNYRSMY GNNLTEDIGQ IKNDINHISS ILEKGEQGLV LSNFELNVIS
     LKEINSLLMN LNKSSQNFTL HYDKASPEET KGKAIKANLT LFEILLNNIL TNASKYAFED
     GNVMNLLVIE LKVTEDLMIL EIRNNGKPFP RNYDKGKFSA KYTTANPSKG TGLGGYDINR
     IASYFDNEEW ELILNSEEVF PVIFKFSFPI IPMINE
//
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