9UB8

Structure of glycosylphosphatidylinositol transamidase,state 2

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003674	molecular_function	molecular_function
A	0005515	molecular_function	protein binding
A	0005783	cellular_component	endoplasmic reticulum
A	0005789	cellular_component	endoplasmic reticulum membrane
A	0006506	biological_process	GPI anchor biosynthetic process
A	0016255	biological_process	attachment of GPI anchor to protein
A	0031505	biological_process	fungal-type cell wall organization
A	0042765	cellular_component	GPI-anchor transamidase complex
B	0003674	molecular_function	molecular_function
B	0005783	cellular_component	endoplasmic reticulum
B	0005789	cellular_component	endoplasmic reticulum membrane
B	0006506	biological_process	GPI anchor biosynthetic process
B	0016255	biological_process	attachment of GPI anchor to protein
B	0031505	biological_process	fungal-type cell wall organization
B	0042765	cellular_component	GPI-anchor transamidase complex
D	0003674	molecular_function	molecular_function
D	0005515	molecular_function	protein binding
D	0005637	cellular_component	nuclear inner membrane
D	0005783	cellular_component	endoplasmic reticulum
D	0005789	cellular_component	endoplasmic reticulum membrane
D	0006506	biological_process	GPI anchor biosynthetic process
D	0016020	cellular_component	membrane
D	0016255	biological_process	attachment of GPI anchor to protein
D	0031505	biological_process	fungal-type cell wall organization
D	0042765	cellular_component	GPI-anchor transamidase complex
E	0003674	molecular_function	molecular_function
E	0005515	molecular_function	protein binding
E	0005783	cellular_component	endoplasmic reticulum
E	0005789	cellular_component	endoplasmic reticulum membrane
E	0006506	biological_process	GPI anchor biosynthetic process
E	0016255	biological_process	attachment of GPI anchor to protein
E	0031505	biological_process	fungal-type cell wall organization
E	0042765	cellular_component	GPI-anchor transamidase complex
F	0003674	molecular_function	molecular_function
F	0005783	cellular_component	endoplasmic reticulum
F	0005789	cellular_component	endoplasmic reticulum membrane
F	0006506	biological_process	GPI anchor biosynthetic process
F	0016255	biological_process	attachment of GPI anchor to protein
F	0031505	biological_process	fungal-type cell wall organization
F	0042765	cellular_component	GPI-anchor transamidase complex
G	0003674	molecular_function	molecular_function
G	0005515	molecular_function	protein binding
G	0005637	cellular_component	nuclear inner membrane
G	0005783	cellular_component	endoplasmic reticulum
G	0005789	cellular_component	endoplasmic reticulum membrane
G	0006506	biological_process	GPI anchor biosynthetic process
G	0016020	cellular_component	membrane
G	0016255	biological_process	attachment of GPI anchor to protein
G	0031505	biological_process	fungal-type cell wall organization
G	0042765	cellular_component	GPI-anchor transamidase complex

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	680
Details	Transmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	856
Details	Topological domain: {"description":"Lumenal","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	390
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine"}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	40
Details	Region: {"description":"May be involved in recognition of long-chain fatty acids in GPI","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	10
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"11598210","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---