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Zinc is chelated by the four conserved cysteines in the alignment.","domain_architectures":44,"interpro_id":"IPR022002","known_evidence_count":null,"matches":12166,"name":"ChsH2, rubredoxin-like zinc ribbon domain","partial_evidence_count":null,"pfam_id":"PF12172","proteins":12165,"proteomes":4066,"short_name":"zf-ChsH2","source_url":"https://www.ebi.ac.uk/interpro/api/entry/pfam/PF12172","structures":15,"taxa":5926,"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/PF12172.yaml","record":{"characterization_status":"UNSCORED","counters":{"alphafold_models":7456,"domain_architectures":44,"matches":12166,"proteins":12165,"proteomes":4066,"structures":15,"taxa":5926},"curation_status":"SEEDED","description":"This domain is found at the C-terminal end of the probable enoyl -CoA hydratase alpha subunit from Thermomonospora curvata (ChsH2) and similar archaeal and bacterial proteins. ChsH2 is likely to be involved in bile acid degradation. The C-terminal region of this protein is organised into two domains: an N-terminal zinc finger domain with a three-stranded antiparallel beta-sheet and an N-terminal alpha-helix (this entry) and a OB-fold domain ([pfam:PF01796]) [[cite:PUB00155451]]. The domain is duplicated in some members like [swissprot:O53566] from M.tuberculosis. The structure of [swissprot:Q97WQ4] from Saccharolobus solfataricus reveals two long N-terminal helices followed by a rubredoxin -like zinc ribbon domain represented in this family and a C-terminal OB fold domain [[cite:PUB00097287]]. Zinc is chelated by the four conserved cysteines in the alignment.","id":"Pfam:PF12172","interpro_id":"InterPro:IPR022002","name":"ChsH2, rubredoxin-like zinc ribbon 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