The Eukaryotic Linear Motif resource for
Functional Sites in Proteins
Functional site class:
RPA32C ligand-binding site
Functional site description:
The RPA interacting motif is conserved in eukaryotes DNA repair and replication proteins UNG2, XPA, RAD14, TIPIN and SMARCAL1. It is involved in DNA replication and other DNA processing pathways by binding to RPA. This protein-mediated RPA conformation is also known as ‘hand-off’ model. The interaction between RPA interacting motif and RPA32C are weak but specific.
ELMs with same func. site: LIG_RPA_C_Fungi  LIG_RPA_C_Insects  LIG_RPA_C_Plants  LIG_RPA_C_Vert 
ELM Description:
LIG_RPA_C_Fungi is similar to the vertebrate motif LIG_RPA_C_Vert, but less conserved and shorter with thirteen amino acids. The motif is only based on one alignment and therefore very unspecific. The amino acid in the first position is variable in contrast to other RPA interacting motifs. There are hydrophobic amino acids in the second position similar to the vertebrate motif. After two variable positions positive charged, polar uncharged and hydrophobic amino acids are possible followed by a highly conserved arginine. In the ninth position alanine, valine and serine are possible. In position twelve are hydrophobic and positive charged amino acid residues possible, whereas in the last position hydrophobic, positive charged and polar uncharged residues are suitable.
Pattern: [^P][MIALVF][^P][^P][NSHRA]R[^P][^P][ASV][^P][^P][RKLIA][RQLIVA]
Pattern Probability: 0.0000564
Present in taxon: Fungi
Interaction Domain:
RPA_C (PF08784) Replication protein A C terminal (Stochiometry: 1 : 1)
o See 1 Instance for LIG_RPA_C_Fungi
o Abstract
Replication protein A (RPA) is a conserved eukaryotic single stranded DNA (ssDNA) binding protein and essential for DNA replication, recombination and repair. RPA consists of three subunits RPA70, RPA32 and RPA14, named after their molecular weight 70, 32 and 14 kDa, that form a stable complex (Fanning,2006). All three subunits consist primarily of OB fold domains that form the trimrization core and are responsible for ssDNA binding. Furthermore RPA70 N-terminal domain and RPA32 C-terminal domain can recruit a variety of DNA processing proteins in response to genomic stress and DNA damage (Xie,2014). The C terminus of subunit RPA32 contains a specific surface that interacts with a variety of DNA damage response proteins and therefore this region is required for base excision repair, nucleotide excision repair and S-phase checkpoint activation. RPA32C mediating the assembly of DNA repair complexes via a hand-off mechanism. In early steps of nucleotide excision repair and the repair of double-strand breaks by homologous recombination, RPA binds to the ssDNA opposite or adjacent to the site of DNA damage and interacts with one of the damage-recognition proteins (Mer,2000).
o 5 selected references:

o 1 Instance for LIG_RPA_C_Fungi
(click table headers for sorting; Notes column: =Number of Switches, =Number of Interactions)
Acc., Gene-, NameStartEndSubsequenceLogic#Ev.OrganismNotes
P28519 RAD14
8 20 QKAKLEANRKLAIERLRKRG TP 1 Saccharomyces cerevisiae S288c
Please cite: ELM 2016-data update and new functionality of the eukaryotic linear motif resource. (PMID:26615199)

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