{"cross_mech":[],"family":{"alphafold_models":2758,"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 entry represents the C-terminal domain of MurT ligase from Gram-positive bacteria. MurT is part of the bi-enzymatic complex MurT-GatD involved in the amidation of the alpha-carboxyl group of the D-isoglutamate residue in Lipid II in the peptidoglycan layer to produce D-isoglutamine. This domain contains an aspartate at position 349, the third residue in the catalytic triad GatD-C94, GatD-H189, MurT-D349. This C-terminal domain is built around a central six-stranded, predominantly parallel beta-sheet that is sandwiched between four alpha-helices on one side and two alpha-helices on the other. The MurT-GatD heterodimer adopts a boomerang-shaped conformation, with GatD packing against the C-terminal domain of MurT [[cite:PUB00094480]].","domain_architectures":6,"interpro_id":"IPR013564","known_evidence_count":null,"matches":4479,"name":"MurT ligase C-terminal","partial_evidence_count":null,"pfam_id":"PF08353","proteins":4479,"proteomes":4418,"short_name":"MurT_C","source_url":"https://www.ebi.ac.uk/interpro/api/entry/pfam/PF08353","structures":6,"taxa":6081,"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/PF08353.yaml","record":{"characterization_status":"UNSCORED","counters":{"alphafold_models":2758,"domain_architectures":6,"matches":4479,"proteins":4479,"proteomes":4418,"structures":6,"taxa":6081},"curation_status":"SEEDED","description":"This entry represents the C-terminal domain of MurT ligase from Gram-positive bacteria. MurT is part of the bi-enzymatic complex MurT-GatD involved in the amidation of the alpha-carboxyl group of the D-isoglutamate residue in Lipid II in the peptidoglycan layer to produce D-isoglutamine. This domain contains an aspartate at position 349, the third residue in the catalytic triad GatD-C94, GatD-H189, MurT-D349. This C-terminal domain is built around a central six-stranded, predominantly parallel beta-sheet that is sandwiched between four alpha-helices on one side and two alpha-helices on the other. The MurT-GatD heterodimer adopts a boomerang-shaped conformation, with GatD packing against the C-terminal domain of MurT [[cite:PUB00094480]].","id":"Pfam:PF08353","interpro_id":"InterPro:IPR013564","name":"MurT ligase C-terminal","pfam_id":"PF08353","provenance":{"generated_at":"2026-10-10T07:44:21.614711Z","path":"data/worklists/interpro-pfam-duf-2026-10-10.json","sha256":"17fb625876c9326ed284263a47bcd84e0d7844a31c040dc06cd2260c36f1c383","snapshot_id":"interpro-pfam-duf-2026-10-10","source_url":"https://www.ebi.ac.uk/interpro/api/entry/pfam/"},"seed_status":"EX_DUF","short_name":"MurT_C","source_url":"https://www.ebi.ac.uk/interpro/api/entry/pfam/PF08353"},"source":{"commit":"c8155abfcf881ad8662936343deb81e604e3a194","path":"data/families/PF08353.yaml","repository":"https://github.com/CultureBotAI/DUFMech","sha256":"c845e11c0fc43d843ccd30cb08b801108e689652098ae75b4cad4a3b484e68ae"}},"protein_examples":{"candidate_count":0,"discovery_scanned":true,"example_count":0,"examples":[],"pfam_id":"PF08353","short_name":"MurT_C","status":"NO_SIBLING_CANDIDATE","unresolved":[]}}
