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Protein Domain : IPR014646

Name  Replication protein A, subunit RPA32 Short Name  RPA32
Type  Family Description  Replication protein A (RPA) is a single-stranded DNA-binding protein that is required for multiple processes in eukaryotic DNA metabolism, including DNA replication, DNA repair, and recombination. RPA homologues have been identified in all eukaryotic organisms examined and are all abundant heterotrimeric proteins composed of subunits of approximately 70 kDa (RPA70, ), 30 kDa (RPA32, this group), and 14 kDa (RPA14, ). RPA was initially identified as a nuclear component of HeLa cell extracts that is absolutely necessary to support simian virus 40 DNA replication [].RPA binds non-specifically to single-stranded DNA (ssDNA) and interacts with and/or modifies the activities of multiple proteins, but it does not possess any intrinsic enzymatic activity. The four ssDNA-binding domains of RPA have a characteristic OB (oligonucleotide/oligosaccharide-binding) fold and contact DNA with specific polarity via a hierarchy-driven dynamic pathway [].RPA is required for both the initiation and elongation phases of chromosomal DNA replication []. RPA associates with origins of replication after loading and activation of the initiation complex by CDC45[]. RPA promotes the initial opening of the DNA and is required for loading of DNA polymerase alpha and additional replication fork proteins. Once replication forks are established, RPA remains associated with the forks during elongation [, ]. In human cells, RPA is localized at replication foci during S-phase []. Cellular DNA damage causes the N terminus of human RPA32 to become hyper-phosphorylated. Current data indicates that hyper-phosphorylation causes a change in RPA conformation that down-regulates activity in DNA replication but does not affect DNA repair processes. This suggests that the role of RPA phosphorylation in the cellular response to DNA damage is to help regulate DNA metabolism and promote DNA repair [].The OB-fold consists of five beta-strands in a Greek-key beta-barrel []. RPA70 consists of four OB-fold domains, all except the N-terminal, are involved in ssDNA binding. RPA32 and RPA14 have a single OB-fold domain. In RPA32 this domain is involved in DNA binding, whereas in RPA14 this domain is necessary for the assembly of the subunits.

Publication Counts Displayer

0 Child Features

4 Contains

DB identifier Name Short Name Type
IPR012340 Nucleic acid-binding, OB-fold NA-bd_OB-fold Domain
IPR011991 Winged helix-turn-helix DNA-binding domain WHTH_DNA-bd_dom Domain
IPR004365 OB-fold nucleic acid binding domain, AA-tRNA synthetase-type NA-bd_OB_tRNA Domain
IPR014892 Replication protein A, C-terminal RPA_C Domain

1 Cross References

Identifier
Source . Name

Subject . Primary Identifier
PIRSF036949 PIRSF IPR014646

2 Data Sets

Name URL
TrEMBL data set http://www.ebi.ac.uk/trembl/
InterPro data set  

0 Found In

0 GO Annotation

0 Ontology Annotations

0 Parent Features

12 Proteins

DB identifier Primary Accession
Organism . Name
FBpp0080967 Q9VIH1 Drosophila melanogaster
FBpp0280713 Q29LY7 Drosophila pseudoobscura
FBpp0167419 B4KIC1 Drosophila mojavensis
FBpp0229127 B4LQB3 Drosophila virilis
FBpp0258024 B4P713 Drosophila yakuba
A8WVU6_CAEBR A8WVU6 Caenorhabditis briggsae
Q95Y97_CAEEL Q95Y97 Caenorhabditis elegans
Q8SXG3_DROME Q8SXG3 Drosophila melanogaster
A0ANL2_DROME A0ANL2 Drosophila melanogaster
C0MJ04_DROME C0MJ04 Drosophila melanogaster
A0ANL8_DROME A0ANL8 Drosophila melanogaster
E3N7I0_CAERE E3N7I0 Caenorhabditis remanei