Uniprot ID	P06229
Uniprot Name	FEN_BPT5
Taxonomy ID	10726
Sequence	M S K S W G K F I E E E E A E M A S R R N L M I V D G T N L G F R F K H N N S K K P F A S S Y V S T I Q S L A K S Y S A R T T I V L G D K G K S V F R L E H L P E Y K G N R D E K Y A Q R T E E E K A L D E Q F F E Y L K D A F E L C K T T F P T F T I R G V E A D D M A A Y I V K L I G H L Y D H V W L I S T D G D W D T L L T D K V S R F S F T T R R E Y H L R D M Y E H H N V D D V E Q F I S L K A I M G D L G D N I R G V E G I G A K R G Y N I I R E F G N V L D I I D Q L P L P G K Q K Y I Q N L N A S E E L L F R N L I L V D L P T Y C V D A I A A V G Q D V L D K F T K D I L E I A E Q
Cofactor	COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_04140, ECO:0000269|PubMed:12606565, ECO:0000269|PubMed:15077103, ECO:0000269|PubMed:27273516}; Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000255|HAMAP-Rule:MF_04140, ECO:0000269|PubMed:27273516}; Note=Binds divalent metal cations, probably Mg(2+). In vitro low metal concentrations selectively stimulate the endonuclease reaction. Endonuclease activity is suggested to require only the first cation, whereas exonuclease activity is suggested to require binding of both. High pH favors the exonuclase activity whereas low pH favors the endonuclease activity. Metal ions enhance substrate binding. {ECO:0000255|HAMAP-Rule:MF_04140, ECO:0000269|PubMed:12606565, ECO:0000269|PubMed:15077103, ECO:0000269|PubMed:27273516};
Active site	No current data
Pfam	PF01367 PF02739
InterPro	IPR020046 IPR036279 IPR002421 IPR020045 IPR038969 IPR008918 IPR029060