UniProt functional annotation for Q38087



	UniProt functional annotation for Q38087

UniProt code: Q38087.

Organism: Escherichia phage RB69 (Bacteriophage RB69).

Taxonomy: Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes; Caudovirales; Myoviridae; Tevenvirinae; Mosigvirus.

Function: Replicates the viral genomic DNA. This polymerase possesses two enzymatic activities: DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3'- to 5'-direction for proofreading purpose. {ECO:0000255|HAMAP- Rule:MF_04100, ECO:0000269|PubMed:17098747, ECO:0000269|PubMed:18503083, ECO:0000269|PubMed:22571765, ECO:0000269|PubMed:22616982}.

Catalytic activity: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:11130, Rhea:RHEA-COMP:11131, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:83828; EC=2.7.7.7; Evidence={ECO:0000255|HAMAP- Rule:MF_04100, ECO:0000269|PubMed:17098747, ECO:0000269|PubMed:18503083, ECO:0000269|PubMed:20795733, ECO:0000269|PubMed:22616982, ECO:0000269|PubMed:24116139};

Cofactor: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_04100, ECO:0000269|PubMed:20166752, ECO:0000269|PubMed:22026756, ECO:0000305|PubMed:11389835, ECO:0000305|PubMed:15057282, ECO:0000305|PubMed:15057283, ECO:0000305|PubMed:17718515, ECO:0000305|PubMed:18503083, ECO:0000305|PubMed:20166748, ECO:0000305|PubMed:21158418, ECO:0000305|PubMed:21566148, ECO:0000305|PubMed:21923197, ECO:0000305|PubMed:22571765, ECO:0000305|PubMed:23214497, ECO:0000305|PubMed:23921641, ECO:0000305|PubMed:24116139};

Subunit: Part of the replicase complex that includes the DNA polymerase, the polymerase clamp, the clamp loader complex, the single- stranded DNA binding protein, and the primase/helicase (By similarity). Interacts with the polymerase clamp; this interaction constitutes the polymerase holoenzyme (PubMed:10535734). {ECO:0000255|HAMAP- Rule:MF_04100, ECO:0000269|PubMed:10535734}.

Domain: The N-terminus contains the 3'-5' exonuclease activity (PubMed:9215631). The C-terminus contains the polymerase activity and is involved in binding to the polymerase clamp protein (PubMed:9215631). A beta hairpin structure is necessary for the proofreading function of the polymerase (By similarity). {ECO:0000255|HAMAP-Rule:MF_04100, ECO:0000269|PubMed:9215631}.

Similarity: Belongs to the DNA polymerase type-B family. {ECO:0000255|HAMAP-Rule:MF_04100}.

Annotations taken from UniProtKB at the EBI.


Organism:		Escherichia phage RB69 (Bacteriophage RB69).
Taxonomy:		Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes; Caudovirales; Myoviridae; Tevenvirinae; Mosigvirus.



Function:		Replicates the viral genomic DNA. This polymerase possesses two enzymatic activities: DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3'- to 5'-direction for proofreading purpose. {ECO:0000255\|HAMAP- Rule:MF_04100, ECO:0000269\|PubMed:17098747, ECO:0000269\|PubMed:18503083, ECO:0000269\|PubMed:22571765, ECO:0000269\|PubMed:22616982}.


Catalytic activity:		Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:11130, Rhea:RHEA-COMP:11131, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:83828; EC=2.7.7.7; Evidence={ECO:0000255\|HAMAP- Rule:MF_04100, ECO:0000269\|PubMed:17098747, ECO:0000269\|PubMed:18503083, ECO:0000269\|PubMed:20795733, ECO:0000269\|PubMed:22616982, ECO:0000269\|PubMed:24116139};
Cofactor:		Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255\|HAMAP-Rule:MF_04100, ECO:0000269\|PubMed:20166752, ECO:0000269\|PubMed:22026756, ECO:0000305\|PubMed:11389835, ECO:0000305\|PubMed:15057282, ECO:0000305\|PubMed:15057283, ECO:0000305\|PubMed:17718515, ECO:0000305\|PubMed:18503083, ECO:0000305\|PubMed:20166748, ECO:0000305\|PubMed:21158418, ECO:0000305\|PubMed:21566148, ECO:0000305\|PubMed:21923197, ECO:0000305\|PubMed:22571765, ECO:0000305\|PubMed:23214497, ECO:0000305\|PubMed:23921641, ECO:0000305\|PubMed:24116139};
Subunit:		Part of the replicase complex that includes the DNA polymerase, the polymerase clamp, the clamp loader complex, the single- stranded DNA binding protein, and the primase/helicase (By similarity). Interacts with the polymerase clamp; this interaction constitutes the polymerase holoenzyme (PubMed:10535734). {ECO:0000255\|HAMAP- Rule:MF_04100, ECO:0000269\|PubMed:10535734}.
Domain:		The N-terminus contains the 3'-5' exonuclease activity (PubMed:9215631). The C-terminus contains the polymerase activity and is involved in binding to the polymerase clamp protein (PubMed:9215631). A beta hairpin structure is necessary for the proofreading function of the polymerase (By similarity). {ECO:0000255\|HAMAP-Rule:MF_04100, ECO:0000269\|PubMed:9215631}.
Similarity:		Belongs to the DNA polymerase type-B family. {ECO:0000255\|HAMAP-Rule:MF_04100}.