UniProt functional annotation for P96022



	UniProt functional annotation for P96022

UniProt code: P96022.

Organism: Saccharolobus solfataricus (Sulfolobus solfataricus).

Taxonomy: Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae; Saccharolobus.

Function: Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis.

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;

Cofactor: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Note=Binds 2 magnesium ions per subunit.;

Subunit: Monomer.

Subcellular location: Cytoplasm {ECO:0000305}.

Domain: The catalytic core consists of fingers, palm and thumb subdomains, but the fingers and thumb subdomains are much smaller than in high-fidelity polymerases; residues from five sequence motifs of the Y-family cluster around an active site cleft that can accommodate DNA and nucleotide substrates with relaxed geometric constraints, with consequently higher rates of misincorporation and low processivity. It lacks the O helices present in high-fidelity DNA polymerases in the fingers domain.

Similarity: Belongs to the DNA polymerase type-Y family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Saccharolobus solfataricus (Sulfolobus solfataricus).
Taxonomy:		Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae; Saccharolobus.



Function:		Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis.


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;
Cofactor:		Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Note=Binds 2 magnesium ions per subunit.;
Subunit:		Monomer.
Subcellular location:		Cytoplasm {ECO:0000305}.
Domain:		The catalytic core consists of fingers, palm and thumb subdomains, but the fingers and thumb subdomains are much smaller than in high-fidelity polymerases; residues from five sequence motifs of the Y-family cluster around an active site cleft that can accommodate DNA and nucleotide substrates with relaxed geometric constraints, with consequently higher rates of misincorporation and low processivity. It lacks the O helices present in high-fidelity DNA polymerases in the fingers domain.
Similarity:		Belongs to the DNA polymerase type-Y family. {ECO:0000305}.