Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
C2A060601e5f1bC1 A: a+b two layersX: Alpha-beta plaitsH: Ferredoxin domains in multidrug efflux transporterT: Multidrug efflux transporter AcrB pore domainF: 2A060601ECOD (1.6)
AFilo_glycope5f1bA1 A: a+b complex topologyX: Envelope glycoprotein GP1 (From Topology)H: Envelope glycoprotein GP1 (From Topology)T: Envelope glycoprotein GP1F: Filo_glycopECOD (1.6)
BEbola-like_HR1-HR2e5f1bB1 A: a+b duplicates or obligate multimersX: Envelope glycoprotein GP2-related (From Topology)H: Envelope glycoprotein GP2-related (From Topology)T: Envelope glycoprotein GP2-relatedF: Ebola-like_HR1-HR2ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
PF22314NPC1, middle luminal domain (NPC1_MLD)NPC1, middle luminal domainNPC intracellular cholesterol transporter 1 (NPC1) is a endosomal/lysosomal membrane protein that facilitates the trafficking of cholesterol and other cargo from lysosomes and is involved in cholesterol homeostasis. Mutations in the NPC1 gene cause t ...NPC intracellular cholesterol transporter 1 (NPC1) is a endosomal/lysosomal membrane protein that facilitates the trafficking of cholesterol and other cargo from lysosomes and is involved in cholesterol homeostasis. Mutations in the NPC1 gene cause the rare neurodegenerative disease Niemann-Pick Type C (NPC). This entry represents the middle luminal domain (MLD) of NPC1, which contains the Ebola glycoprotein interacting site [5].
Domain
PF01611Filovirus glycoprotein (Filo_glycop)Filovirus glycoprotein- Family
PF22307Envelope glycoprotein GP2-like, HR1-HR2 (Ebola-like_HR1-HR2)Envelope glycoprotein GP2-like, HR1-HR2This entry spans heptad repeats 1 and 2 of the glycoprotein (GP) from Ebola and Marburg viruses [1-5]. Viral infection involves the formation of a trimer-of-hairpins structure (three HR1s helices, buttressed by three HR2 helices lying in antiparallel ...This entry spans heptad repeats 1 and 2 of the glycoprotein (GP) from Ebola and Marburg viruses [1-5]. Viral infection involves the formation of a trimer-of-hairpins structure (three HR1s helices, buttressed by three HR2 helices lying in antiparallel orientation). This domain may have been acquired via horizontal transfer from retroviruses.
Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
Niemann-Pick C1 protein
GP1
GP2

Membrane Protein Annotation: OPM OPM Database Homepage