The domain within your query sequence starts at position 1 and ends at position 262; the E-value for the SRAP domain shown below is 4.9e-58.



PFAM accession number:PF02586
Interpro abstract (IPR003738):

The SRAP (SOS-response associated peptidase) family is characterised by the SRAP domain with a novel thiol autopeptidase activity, whose active site in human HMCES is comprised of the catalytic triad residues C2, E127, and H210 [ (PUBMED:31806351) ]. SRAP proteins are evolutionarily conserved in all domains of life. For instance, human HMCES and E. coli YedK are similar in both sequence and structure [ (PUBMED:31235915) ]. HMCES was originally identified as a possible reader of 5hmC in embryonic stem cell extracts using a double-stranded DNA molecule containing 5hmC as bait [ (PUBMED:23434322) ]. The bacterial members have operonic associations with the SOS DNA damage response, mutagenic translesion DNA polymerases, non-homologous DNA-ending-joining networks that employ Ku and an ATP-dependent ligase, and other repair systems [ (PUBMED:23945014) ].

Abasic (AP) sites are one of the most common DNA lesions that block replicative polymerases. SRAP proteins shield the AP site from endonucleases and error-prone polymerases [ (PUBMED:30554877) ]. Both HMCES and YedK have been found to preferentially bind ssDNA and efficiently form DNA-protein crosslinks (DPCs) to AP sites in ssDNA. They crosslink to AP sites via a stable thiazolidine DNA-protein linkage formed with the N-erminal cysteine and the aldehyde form of the AP deoxyribose [ (PUBMED:31235915) ].

In B Cells, HMCES has also been shown to mediate microhomology-mediated alternative-end-joining through its SRAP domain [ (PUBMED:31806351) ].

GO process:protein-DNA covalent cross-linking (GO:0018142), cellular response to DNA damage stimulus (GO:0006974)
GO function:single-stranded DNA binding (GO:0003697)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry SRAP