UniProt functional annotation for Q97W02



	UniProt functional annotation for Q97W02

UniProt code: Q97W02.

Organism: Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) (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. It is 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.;

Biophysicochemical properties: Temperature dependence: Highly active from 35 to 95 degrees Celsius. Thermostable.;

Subunit: Monomer. Interacts with the PCNA heterotrimer via PCNA1. {ECO:0000269|PubMed:19054331}.

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.

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

Annotations taken from UniProtKB at the EBI.


Organism:		Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) (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. It is 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.;
Biophysicochemical properties:		Temperature dependence: Highly active from 35 to 95 degrees Celsius. Thermostable.;
Subunit:		Monomer. Interacts with the PCNA heterotrimer via PCNA1. {ECO:0000269\|PubMed:19054331}.
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.
Similarity:		Belongs to the DNA polymerase type-Y family. {ECO:0000305}.