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Database: UniProt
Entry: A0A101CWY4_9FLAO
LinkDB: A0A101CWY4_9FLAO
Original site: A0A101CWY4_9FLAO 
ID   A0A101CWY4_9FLAO        Unreviewed;       810 AA.
AC   A0A101CWY4;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 30.
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=AR687_01410 {ECO:0000313|EMBL:KUJ63873.1};
OS   Flavobacteriaceae bacterium CRH.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae.
OX   NCBI_TaxID=1742859 {ECO:0000313|EMBL:KUJ63873.1, ECO:0000313|Proteomes:UP000053826};
RN   [1] {ECO:0000313|EMBL:KUJ63873.1, ECO:0000313|Proteomes:UP000053826}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CRH {ECO:0000313|EMBL:KUJ63873.1,
RC   ECO:0000313|Proteomes:UP000053826};
RA   Newman J.D., Miller J.R., Jacobs K.T.;
RT   "Genome Sequence of Flavobacterium sp. CHR.";
RL   Submitted (OCT-2015) 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   -!- SIMILARITY: Belongs to the type-I restriction system S methylase
CC       family. {ECO:0000256|ARBA:ARBA00010923}.
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:KUJ63873.1}.
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DR   EMBL; LMAJ01000001; KUJ63873.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A101CWY4; -.
DR   STRING; 1742859.AR687_01410; -.
DR   OrthoDB; 9814572at2; -.
DR   Proteomes; UP000053826; 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; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR000055; Restrct_endonuc_typeI_TRD.
DR   InterPro; IPR044946; Restrct_endonuc_typeI_TRD_sf.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR42933:SF1; SITE-SPECIFIC DNA-METHYLTRANSFERASE (ADENINE-SPECIFIC); 1.
DR   PANTHER; PTHR42933; SLR6095 PROTEIN; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF01420; Methylase_S; 1.
DR   Pfam; PF02384; N6_Mtase; 1.
DR   PRINTS; PR00507; N12N6MTFRASE.
DR   SMART; SM00387; HATPase_c; 1.
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   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT   DOMAIN          691..806
FT                   /note="Histidine kinase/HSP90-like ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00387"
SQ   SEQUENCE   810 AA;  93435 MW;  25FE5700795B61D2 CRC64;
     MKETDFESKE VNEIIDQTWK IFEVIRGSVR SEDLEITLFL LSAYNDGLIN NDSFIYQGDI
     RENFLEDVEK SEKYRSIIYI YAPIINAISY KKKEEILYRL KVINRFILQT HFPEIFDNLL
     YRLSDAQGKY SGQFIQPLEI SRFIINLADL PNNATIYNPF AGLASFGTFL NKSQRYYGQE
     YNPRTWALGK LRLMAHEIDD SNFILDDSIE HWNNFSEFDL IVANPPYGYK IANHSNNYPN
     ERNLTAENFL VKHGIETLNK HGQLICVLPL SFLFKGGREQ RFREELVHNN LIDTIVSLPS
     GLLKHTGIPI CIVVFKKYHS NNGFIRLINA NDFFISNGTR DKRLDDILLS NVLREDFENK
     YVKFVSTEMV SASGYNLNIQ RYFVKEYLGV SLSEIGETIK GMRVAKGGFG KLVRIRNLKD
     DKIDHLLNWE KIEEVELTIP TRKIEESCLL ITVRWKTLKP TYFEYSGEPI YISHDIVTLK
     IDETIVDPHY LINELHSESI LEQIESFRIA GTIPSIHTVD LFNIKIELPS IEEQRGKVKG
     LRELSKKIEA LQNERNAIVH GKSTAQFDEF ASLKHSLGAP RQNILSNAKS LERFFENNNS
     QAFVEVNNHY QKRYGISLIE VFQQIKEDID HISLMLEKGE AGLILNNYPN EIQSLKNINK
     TINSYKENGY NFKITKYLLE NEELNKNGVE CNIVLLKILL ENILSNASKY GFSEKSPANE
     VVIEMKIIDN FLEITLKNNG IPFPKNFDKT KFTAKFSTAN SEKGSGLGGY DINRIASHFG
     NPDWDLILDK DGLYPVMFKF NLPIIQIANE
//
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