UniProt functional annotation for F2Z289



	UniProt functional annotation for F2Z289

UniProt code: F2Z289.

Organism: Desulfurococcus amylolyticus.

Taxonomy: Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales; Desulfurococcaceae; Desulfurococcus.

Function: Structure-specific nuclease with 5'-flap endonuclease and 5'- 3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. Binds the unpaired 3'-DNA end and kinks the DNA to facilitate 5' cleavage specificity. Cleaves one nucleotide into the double-stranded DNA from the junction in flap DNA, leaving a nick for ligation. Also involved in the base excision repair (BER) pathway. Acts as a genome stabilization factor that prevents flaps from equilibrating into structurs that lead to duplications and deletions. Also possesses 5'-3' exonuclease activity on nicked or gapped double-stranded DNA. {ECO:0000256|HAMAP- Rule:MF_00614}.

Cofactor: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|ARBA:ARBA00001946};

Cofactor: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-Rule:MF_00614}; Note=Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding. {ECO:0000256|HAMAP- Rule:MF_00614};

Subunit: Interacts with PCNA. PCNA stimulates the nuclease activity without altering cleavage specificity. {ECO:0000256|HAMAP- Rule:MF_00614}.

Similarity: Belongs to the XPG/RAD2 endonuclease family. FEN1 subfamily. {ECO:0000256|HAMAP-Rule:MF_00614}.

Annotations taken from UniProtKB at the EBI.


Organism:		Desulfurococcus amylolyticus.
Taxonomy:		Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales; Desulfurococcaceae; Desulfurococcus.



Function:		Structure-specific nuclease with 5'-flap endonuclease and 5'- 3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. Binds the unpaired 3'-DNA end and kinks the DNA to facilitate 5' cleavage specificity. Cleaves one nucleotide into the double-stranded DNA from the junction in flap DNA, leaving a nick for ligation. Also involved in the base excision repair (BER) pathway. Acts as a genome stabilization factor that prevents flaps from equilibrating into structurs that lead to duplications and deletions. Also possesses 5'-3' exonuclease activity on nicked or gapped double-stranded DNA. {ECO:0000256\|HAMAP- Rule:MF_00614}.


Cofactor:		Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256\|ARBA:ARBA00001946};
Cofactor:		Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256\|HAMAP-Rule:MF_00614}; Note=Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding. {ECO:0000256\|HAMAP- Rule:MF_00614};
Subunit:		Interacts with PCNA. PCNA stimulates the nuclease activity without altering cleavage specificity. {ECO:0000256\|HAMAP- Rule:MF_00614}.
Similarity:		Belongs to the XPG/RAD2 endonuclease family. FEN1 subfamily. {ECO:0000256\|HAMAP-Rule:MF_00614}.