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
//