ID A0A0N8PT21_9CHLR Unreviewed; 992 AA.
AC A0A0N8PT21;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Site-specific DNA-methyltransferase (adenine-specific) {ECO:0008006|Google:ProtNLM};
GN ORFNames=SE17_04535 {ECO:0000313|EMBL:KPV54309.1};
OS Kouleothrix aurantiaca.
OC Bacteria; Chloroflexota; Chloroflexia; Chloroflexales; Roseiflexineae;
OC Roseiflexaceae; Kouleothrix.
OX NCBI_TaxID=186479 {ECO:0000313|EMBL:KPV54309.1, ECO:0000313|Proteomes:UP000050509};
RN [1] {ECO:0000313|EMBL:KPV54309.1, ECO:0000313|Proteomes:UP000050509}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COM-B {ECO:0000313|EMBL:KPV54309.1,
RC ECO:0000313|Proteomes:UP000050509};
RA Hemp J.;
RT "Draft genome sequence of Kouleothrix aurantiaca JCM 19913.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage of DNA to give random double-stranded
CC fragments with terminal 5'-phosphates, ATP is simultaneously
CC hydrolyzed.; EC=3.1.21.3; Evidence={ECO:0000256|ARBA:ARBA00000851};
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 HsdR family.
CC {ECO:0000256|ARBA:ARBA00008598}.
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:KPV54309.1}.
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DR EMBL; LJCR01000076; KPV54309.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N8PT21; -.
DR PATRIC; fig|186479.3.peg.10065; -.
DR Proteomes; UP000050509; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC.
DR GO; GO:0009035; F:type I site-specific deoxyribonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR Gene3D; 3.90.1570.30; -; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR046816; MmeI_Mtase.
DR InterPro; IPR007409; Restrct_endonuc_type1_HsdR_N.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR025931; TaqI_C.
DR PANTHER; PTHR33841:SF1; ADENINE-SPECIFIC METHYLTRANSFERASE PGLX; 1.
DR PANTHER; PTHR33841; DNA METHYLTRANSFERASE YEEA-RELATED; 1.
DR Pfam; PF04313; HSDR_N; 1.
DR Pfam; PF20473; MmeI_Mtase; 1.
DR Pfam; PF12950; TaqI_C; 1.
DR PRINTS; PR00507; N12N6MTFRASE.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000050509};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 25..137
FT /note="Restriction endonuclease type I HsdR N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04313"
FT DOMAIN 393..563
FT /note="MmeI-like DNA-methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF20473"
FT DOMAIN 772..918
FT /note="TaqI-like C-terminal specificity"
FT /evidence="ECO:0000259|Pfam:PF12950"
SQ SEQUENCE 992 AA; 115030 MW; 2A25D1921647CE53 CRC64;
MAIPSRVINL IEHFGRDIKA FRSGQYNETQ VRREFIDPFF KALGWDVENE QGVPETYKDV
IHEDQIKIGG QTKAPDYCFR VGGSRKFFLE AKKPVVNLDS DTKPAFQLRR YAWSANLPVS
ILTDFEEFVV YDCRIKPDKD DKATTARTLY IDYTQYYDRW DEIETLFHRD AVLAGSLDQY
TVSLKDKKGV ATVDDAFLGE IETWRRILAE NIAERNPQLS KRDINYAVQM TIDRIIFLRI
CEDRGIEPYE RLKGVLTNGS IYTKLCKIFQ DADDRYNSGL FHFRKEKERP ELPDDLTLDL
VIDDEPFQRI IPNFYYPDSP YEFSVLPIEI LGQVYEQFLG KVINLTTDHR ATIDDKPEVR
KAGGVYYTPT YVVDYIVKNT VGKLLDGKTP RQTTKLKILD PACGSGSFLI GAYQFLLDWH
RDWYVNDGPE KHKKDLYQAI SGEWRLTADT RKRVLLNNIY GVDIDPQAVE VTKLSLLLKV
LEGESSQTLA TQLRMFHERA LPDLAQNIKC GNSLIASDFY DNQQLGFFDA EEQYRINVFD
WEDEFSNILQ DGGFDIVIGN PPWGAEFTEP ELEYLRTHNK EVIVRMIDSF MYFVYQNSKR
LKENGYFGMI LPDVLLYQID NAKLRKFILD GYEIDTTLNM GDVFNKVVRP SSVIIYKNHH
SRNTNIKIGD FASVNKVMKA VALLDESHYD SIPQKEIYNI PSLLFVTANP SHYLIWTKVK
SAAHDLLENI IDTDGIQRGV SPDLKQAFLV NTEVANTWAL EKEKLRKSLT GGRQVKRYYI
ERPDLWLIYT SRADDFRRLP NICKYVEQHK NEITCKEVQQ GKHPLYALHR PREEHIFTKP
QKIVGVITED EIIVALDSEQ TFVTDGLYLF GLREPYDPRY VMGILNSRLF VFIYRLLAIE
KGRVLAQVKP TTLSQLPIRT INPNNTQEKL LHDKICVSVD EISTLYINQT KAKTAQDKTL
YNRQIIAATR RIDRLIYSLY NLNEQEIQLI EA
//
