The domain within your query sequence starts at position 24 and ends at position 221; the E-value for the AP_endonuc_2 domain shown below is 4.2e-28.

LHAAGRAGFEAAEVAWPYTESPQALASAAQTAGLRLVLINTPRGDHEKGEMGLGEGLEQA
VLYAKALGCPRIHLMAGRVPQGADRAAVKGEMETVFVENLKHAAGVLAQENLVGLLEPIN
TRITDPQYFLDTPRQAAAILQKVGRPNLQLQMDIFHWQIMDGNLTGNIREFLPTVGHVQV
AQVPDRGEPGSSGELDFT

AP_endonuc_2

AP_endonuc_2
PFAM accession number:PF01261
Interpro abstract (IPR013022):

This entry represents a structural motif with a beta/alpha TIM barrel found in several proteins families:

  • Endonuclease IV (EC 3.1.21.2), an AP (apurinic/apyrimidinic) endonuclease that primes DNA repair synthesis by cleaving the DNA backbone 5' of AP sites [(PUBMED:10458614)].
  • L-rhamnose isomerase (EC 5.3.1.14), a tetramer of four TIM barrels that catalyses the isomerisation between aldoses and ketoses, such as between L-rhamnose and L-rhamnulose [(PUBMED:17141803)].
  • Xylose isomerase (EC 5.3.1.5), which catalyses the first reaction in the catabolism of D-xylose by converting D-xylose to D-xylulose [(PUBMED:16673077)].
  • Mannonate dehydratase UxuA, which along with mannonate oxidoreductase converts D-fructuronate to 2-keto-3-deoxy-D-gluconate [(PUBMED:7007313)].

These proteins share similar, but not identical, metal-binding sites. In addition, xylose isomerase and L-rhamnose isomerase each have additional alpha-helical domains involved in tetramer formation.

This is a PFAM domain. For full annotation and more information, please see the PFAM entry AP_endonuc_2