{"cross_mech":[],"family":{"alphafold_models":301,"candidate_reasons":["pfam_previous_unknown_name"],"characterization_status":"","context_evidence_count":null,"cross_mech":{"example_proteins":0,"protein_traits_record":false,"records_by_mech":{},"scanned":false},"curation_status":"SEEDED","demotion_reasons":[],"description":"This domain is found in the human Protein shortage in chiasmata 1 ortholog (SHOC1) and related proteins from chordate. SHOC1 is an integral to the formation of crossover recombination intermediates during mammalian meiosis [[cite:PUB00090399]]. SHOC1 preferentially binds branched DNA molecules but apparently lacks in vitro endonuclease activity [[cite:PUB00090399]]. The core of SHOC1 resembles the DNA repair endonuclease XPF. This domain has significant similarity to P-loop AAA ATPase domains. This aligns with the SHOC1 ATPase activity, which is stimulated by the presence of single-stranded DNA [[cite:PUB00090399]].","domain_architectures":29,"interpro_id":"IPR063559","known_evidence_count":null,"matches":818,"name":"SHOC1 ATPase domain","partial_evidence_count":null,"pfam_id":"PF17825","proteins":793,"proteomes":575,"short_name":"SHOC1_ATPase","source_url":"https://www.ebi.ac.uk/interpro/api/entry/pfam/PF17825","structures":0,"taxa":2030,"unknown_status":"EX_DUF"},"inputs":{"cross_mech":"cross-mech-duf-examples-2026-10-10","members":"pfam-uniprot-uniref90-2026-10-07","protein_examples":"duf-protein-examples-2026-10-13","worklist":"interpro-pfam-duf-2026-10-10"},"members":[],"metadata":{"curation_status":"SEEDED","local_source":"source/data/families/PF17825.yaml","record":{"characterization_status":"UNSCORED","counters":{"alphafold_models":301,"domain_architectures":29,"matches":818,"proteins":793,"proteomes":575,"structures":0,"taxa":2030},"curation_status":"SEEDED","description":"This domain is found in the human Protein shortage in chiasmata 1 ortholog (SHOC1) and related proteins from chordate. SHOC1 is an integral to the formation of crossover recombination intermediates during mammalian meiosis [[cite:PUB00090399]]. SHOC1 preferentially binds branched DNA molecules but apparently lacks in vitro endonuclease activity [[cite:PUB00090399]]. The core of SHOC1 resembles the DNA repair endonuclease XPF. This domain has significant similarity to P-loop AAA ATPase domains. This aligns with the SHOC1 ATPase activity, which is stimulated by the presence of single-stranded DNA [[cite:PUB00090399]].","id":"Pfam:PF17825","interpro_id":"InterPro:IPR063559","name":"SHOC1 ATPase 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