6SWY

Structure of active GID E3 ubiquitin ligase complex minus Gid2 and delta Gid9 RING domain


Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
D [auth 4]PF09783e6swy41 A: beta barrelsX: Lipocalins/StreptavidinH: Avidin/Streptavidin (From Topology)T: Avidin/StreptavidinF: PF09783ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
E [auth 9]PF10607CTLH/CRA C-terminal to LisH motif domain (CTLH)CTLH/CRA C-terminal to LisH motif domainRanBPM is a scaffolding protein and is important in regulating cellular function in both the immune system and the nervous system. This domain is at the C-terminus of the proteins and is the binding domain for the CRA motif (for CT11-RanBPM), which ...RanBPM is a scaffolding protein and is important in regulating cellular function in both the immune system and the nervous system. This domain is at the C-terminus of the proteins and is the binding domain for the CRA motif (for CT11-RanBPM), which is comprised of approximately 100 amino acids at the C terminal of RanBPM. It was found to be important for the interaction of RanBPM with fragile X messenger ribonucleoprotein 1 (FMRP), but its functional significance has yet to be determined [5]. This region contains CTLH and CRA domains annotated by SMART; however, these may be a single domain, and it is refereed to as a C-terminal to LisH motif [6].
Domain
B [auth 8]PF10607CTLH/CRA C-terminal to LisH motif domain (CTLH)CTLH/CRA C-terminal to LisH motif domainRanBPM is a scaffolding protein and is important in regulating cellular function in both the immune system and the nervous system. This domain is at the C-terminus of the proteins and is the binding domain for the CRA motif (for CT11-RanBPM), which ...RanBPM is a scaffolding protein and is important in regulating cellular function in both the immune system and the nervous system. This domain is at the C-terminus of the proteins and is the binding domain for the CRA motif (for CT11-RanBPM), which is comprised of approximately 100 amino acids at the C terminal of RanBPM. It was found to be important for the interaction of RanBPM with fragile X messenger ribonucleoprotein 1 (FMRP), but its functional significance has yet to be determined [5]. This region contains CTLH and CRA domains annotated by SMART; however, these may be a single domain, and it is refereed to as a C-terminal to LisH motif [6].
Domain
C [auth 1]PF00622SPRY domain (SPRY)SPRY domain- Family
C [auth 1]PF10607CTLH/CRA C-terminal to LisH motif domain (CTLH)CTLH/CRA C-terminal to LisH motif domainRanBPM is a scaffolding protein and is important in regulating cellular function in both the immune system and the nervous system. This domain is at the C-terminus of the proteins and is the binding domain for the CRA motif (for CT11-RanBPM), which ...RanBPM is a scaffolding protein and is important in regulating cellular function in both the immune system and the nervous system. This domain is at the C-terminus of the proteins and is the binding domain for the CRA motif (for CT11-RanBPM), which is comprised of approximately 100 amino acids at the C terminal of RanBPM. It was found to be important for the interaction of RanBPM with fragile X messenger ribonucleoprotein 1 (FMRP), but its functional significance has yet to be determined [5]. This region contains CTLH and CRA domains annotated by SMART; however, these may be a single domain, and it is refereed to as a C-terminal to LisH motif [6].
Domain
D [auth 4]PF09783Vacuolar import and degradation protein (Vac_ImportDeg)Vacuolar import and degradation protein- Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
E [auth 9]Protein FYV10,Protein FYV10,Protein FYV10,Protein FYV10,Protein FYV10,Protein FYV10,Protein FYV10
A [auth 5]Vacuolar import and degradation protein 28-
B [auth 8]Glucose-induced degradation protein 8-
C [auth 1]Vacuolar import and degradation protein 30,Vacuolar import and degradation protein 30,Vacuolar import and degradation protein 30,Vacuolar import and degradation protein 30,Vacuolar import and degradation protein 30,Vacuolar import and degradation protein 30,Vacuolar import and degradation protein 30,Vacuolar import and degradation protein 30,Vacuolar import and degradation protein 30,Vacuolar import and degradation protein 30,Vacuolar import and degradation protein 30,Vacuolar import and degradation protein 30,Vacuolar import and degradation protein 30,Vacuolar import and degradation protein 30,Vacuolar import and degradation protein 30,Vacuolar import and degradation protein 30-
D [auth 4]Vacuolar import and degradation protein 24-