{"cross_mech":[],"family":{"alphafold_models":3568,"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":"Members of this entry are serine/threonine-protein kinases and includes ATG1 from yeasts, Unc-51 from C. elegans and ULK1-2 from humans. ATG1 is required for vesicle formation in autophagy and the cytoplasm-to-vacuole targeting (Cvt) pathway [[cite:PUB00101056],[cite:PUB00066530]]. Unc-51 is important for axonal elongation and axonal guidance [[cite:PUB00042769]] and ULK1-2 are involved in autophagy in response to starvation [[cite:PUB00098424]]. They consist of a kinase domain at the N-terminal ([pfam:PF00069]) and two tandem microtubule interacting and transport (MIT) domains (tMIT) at the C-terminal. MIT domains are known to mediate protein-protein interactions. In ATG1, MIT domains mediate the interaction with ATG13 [[cite:PUB00101056]]. In ULK1-2, MIT domains control the regulatory function and localization of the proteins and also mediate interactions with additional autophagy proteins [[cite:PUB00098424]]. This is the C-terminal MIT domain (MIT2).","domain_architectures":55,"interpro_id":"IPR022708","known_evidence_count":null,"matches":4135,"name":"Atg1-like, MIT domain 1","partial_evidence_count":null,"pfam_id":"PF12063","proteins":4128,"proteomes":2270,"short_name":"ATG1-like_MIT1","source_url":"https://www.ebi.ac.uk/interpro/api/entry/pfam/PF12063","structures":4,"taxa":5730,"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/PF12063.yaml","record":{"characterization_status":"UNSCORED","counters":{"alphafold_models":3568,"domain_architectures":55,"matches":4135,"proteins":4128,"proteomes":2270,"structures":4,"taxa":5730},"curation_status":"SEEDED","description":"Members of this entry are serine/threonine-protein kinases and includes ATG1 from yeasts, Unc-51 from C. elegans and ULK1-2 from humans. ATG1 is required for vesicle formation in autophagy and the cytoplasm-to-vacuole targeting (Cvt) pathway [[cite:PUB00101056],[cite:PUB00066530]]. Unc-51 is important for axonal elongation and axonal guidance [[cite:PUB00042769]] and ULK1-2 are involved in autophagy in response to starvation [[cite:PUB00098424]]. They consist of a kinase domain at the N-terminal ([pfam:PF00069]) and two tandem microtubule interacting and transport (MIT) domains (tMIT) at the C-terminal. MIT domains are known to mediate protein-protein interactions. In ATG1, MIT domains mediate the interaction with ATG13 [[cite:PUB00101056]]. In ULK1-2, MIT domains control the regulatory function and localization of the proteins and also mediate interactions with additional autophagy proteins [[cite:PUB00098424]]. This is the C-terminal MIT domain (MIT2).","id":"Pfam:PF12063","interpro_id":"InterPro:IPR022708","name":"Atg1-like, MIT domain 1","pfam_id":"PF12063","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":"ATG1-like_MIT1","source_url":"https://www.ebi.ac.uk/interpro/api/entry/pfam/PF12063"},"source":{"commit":"c8155abfcf881ad8662936343deb81e604e3a194","path":"data/families/PF12063.yaml","repository":"https://github.com/CultureBotAI/DUFMech","sha256":"035a24c70edcbcfb63c1bb5b7081fccbdcadb427609149b399b38c82e3b35742"}},"protein_examples":{"candidate_count":4,"discovery_scanned":true,"example_count":4,"examples":[{"evidence_scope":"FAMILY_MEMBERSHIP_NOT_FUNCTION","organism":"Mus 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