7T92

Structure of the peroxisomal retro-translocon formed by a heterotrimeric ubiquitin ligase complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005778	cellular_component	peroxisomal membrane
A	0007031	biological_process	peroxisome organization
A	0008270	molecular_function	zinc ion binding
A	0016558	biological_process	protein import into peroxisome matrix
B	0005777	cellular_component	peroxisome
B	0005778	cellular_component	peroxisomal membrane
B	0008270	molecular_function	zinc ion binding
B	0015031	biological_process	protein transport
B	0016020	cellular_component	membrane
B	0016558	biological_process	protein import into peroxisome matrix
B	0016562	biological_process	protein import into peroxisome matrix, receptor recycling
B	0016567	biological_process	protein ubiquitination
B	0046872	molecular_function	metal ion binding
C	0005777	cellular_component	peroxisome
C	0005778	cellular_component	peroxisomal membrane
C	0007031	biological_process	peroxisome organization
C	0008270	molecular_function	zinc ion binding
C	0015031	biological_process	protein transport
C	0016020	cellular_component	membrane
C	0016558	biological_process	protein import into peroxisome matrix
C	0016562	biological_process	protein import into peroxisome matrix, receptor recycling
C	0016567	biological_process	protein ubiquitination
C	0016740	molecular_function	transferase activity
C	0046872	molecular_function	metal ion binding

Functional Information from PROSITE/UniProt

site_id	PS00518
Number of Residues	10
Details	ZF_RING_1 Zinc finger RING-type signature. CgHvFCwaCI

Chain	Residue	Details
C	CYS417-ILE426

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site_id	PS01012
Number of Residues	16
Details	FOLYLPOLYGLU_SYNT_2 Folylpolyglutamate synthase signature 2. IYEnGLGGggDgGpLL

Chain	Residue	Details
C	ILE115-LEU130

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	123
Details	TOPO_DOM: Peroxisomal matrix => ECO:0000305|PubMed:35768507

Chain	Residue	Details
C	MET1-ALA23
C	THR77-SER132
C	GLY230-GLY276

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site_id	SWS_FT_FI2
Number of Residues	29
Details	TRANSMEM: Helical; Name=TM1 => ECO:0000269|PubMed:35768507, ECO:0007744|PDB:7T92

Chain	Residue	Details
C	ALA24-ARG53
A	GLU136-SER145

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site_id	SWS_FT_FI3
Number of Residues	193
Details	TOPO_DOM: Cytoplasmic => ECO:0000305|PubMed:35768507

Chain	Residue	Details
C	GLY54
C	GLN166-VAL201
C	ARG297-ALA454

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site_id	SWS_FT_FI4
Number of Residues	21
Details	TRANSMEM: Helical; Name=TM2 => ECO:0000269|PubMed:35768507, ECO:0007744|PDB:7T92

Chain	Residue	Details
C	ALA55-LEU76
A	GLY177-SER203

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site_id	SWS_FT_FI5
Number of Residues	32
Details	TRANSMEM: Helical; Name=TM3 => ECO:0000269|PubMed:35768507, ECO:0007744|PDB:7T92

Chain	Residue	Details
C	LEU133-LEU165

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site_id	SWS_FT_FI6
Number of Residues	27
Details	TRANSMEM: Helical; Name=TM4 => ECO:0000269|PubMed:35768507, ECO:0007744|PDB:7T92

Chain	Residue	Details
C	LEU202-THR229

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site_id	SWS_FT_FI7
Number of Residues	19
Details	TRANSMEM: Helical; Name=TM5 => ECO:0000269|PubMed:35768507, ECO:0007744|PDB:7T92

Chain	Residue	Details
C	TYR277-VAL296

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site_id	SWS_FT_FI8
Number of Residues	38
Details	ZN_FING: RING-type => ECO:0000255|PROSITE-ProRule:PRU00175

Chain	Residue	Details
C	CYS402-ARG440

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site_id	SWS_FT_FI9
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269|PubMed:35768507, ECO:0007744|PDB:7T92

Chain	Residue	Details
C	CYS402
C	CYS405
C	CYS417
C	HIS419
C	CYS422
C	CYS425
C	CYS436
C	CYS439

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