ELM - Detail for LIG_RPA_C

Accession:	ELME000380
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_Plants is similar to the vertebrate motif LIG_RPA_C_Vert, but shorter. The 12-amino acid long motif contains a highly conserved lysine residue in the first position, followed by mostly charged amino acids in the second position. After two variable positions, an asparagine or a glutamine is possible in the fifth position, followed by a positive charged amino acid, leucine is also possible, in the sixth position. The highly conserved alanine residue is found in all RPA interacting motifs. In the last position is arginine or lysine possible.
Pattern:	`R[MIVAS][^P][^P][NQ][KRL][^P][^P]A[^P][^P][RK]`
Pattern Probability:	`0.0000016`
Present in taxon:	Viridiplantae
Interaction Domain:	RPA_C (PF08784) Replication protein A C terminal (Stochiometry: 1 : 1)

RPA32C ligand-binding site

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_Plants is similar to the vertebrate motif LIG_RPA_C_Vert, but shorter. The 12-amino acid long motif contains a highly conserved lysine residue in the first position, followed by mostly charged amino acids in the second position. After two variable positions, an asparagine or a glutamine is possible in the fifth position, followed by a positive charged amino acid, leucine is also possible, in the sixth position. The highly conserved alanine residue is found in all RPA interacting motifs. In the last position is arginine or lysine possible.

Pattern:

R[MIVAS][^P][^P][NQ][KRL][^P][^P]A[^P][^P][RK]

Pattern Probability:

0.0000016

Present in taxon:

Viridiplantae

Interaction Domain:

RPA_C (PF08784) Replication protein A C terminal (Stochiometry: 1 : 1)

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).