7KTX

Cryo-EM structure of Saccharomyces cerevisiae ER membrane protein complex bound to a Fab in DDM detergent

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0072546	cellular_component	EMC complex
B	0003674	molecular_function	molecular_function
B	0005515	molecular_function	protein binding
B	0005634	cellular_component	nucleus
B	0005783	cellular_component	endoplasmic reticulum
B	0005789	cellular_component	endoplasmic reticulum membrane
B	0006644	biological_process	phospholipid metabolic process
B	0015914	biological_process	phospholipid transport
B	0032977	molecular_function	membrane insertase activity
B	0034975	biological_process	protein folding in endoplasmic reticulum
B	0045050	biological_process	protein insertion into ER membrane by stop-transfer membrane-anchor sequence
B	0071816	biological_process	tail-anchored membrane protein insertion into ER membrane
B	0072546	cellular_component	EMC complex
C	0003674	molecular_function	molecular_function
C	0005789	cellular_component	endoplasmic reticulum membrane
C	0006644	biological_process	phospholipid metabolic process
C	0015914	biological_process	phospholipid transport
C	0016020	cellular_component	membrane
C	0032977	molecular_function	membrane insertase activity
C	0034975	biological_process	protein folding in endoplasmic reticulum
C	0045050	biological_process	protein insertion into ER membrane by stop-transfer membrane-anchor sequence
C	0051087	molecular_function	protein-folding chaperone binding
C	0071816	biological_process	tail-anchored membrane protein insertion into ER membrane
C	0072546	cellular_component	EMC complex
D	0003674	molecular_function	molecular_function
D	0005783	cellular_component	endoplasmic reticulum
D	0005789	cellular_component	endoplasmic reticulum membrane
D	0006644	biological_process	phospholipid metabolic process
D	0015914	biological_process	phospholipid transport
D	0032977	molecular_function	membrane insertase activity
D	0034975	biological_process	protein folding in endoplasmic reticulum
D	0045050	biological_process	protein insertion into ER membrane by stop-transfer membrane-anchor sequence
D	0072546	cellular_component	EMC 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	0006644	biological_process	phospholipid metabolic process
E	0015914	biological_process	phospholipid transport
E	0032977	molecular_function	membrane insertase activity
E	0034975	biological_process	protein folding in endoplasmic reticulum
E	0045050	biological_process	protein insertion into ER membrane by stop-transfer membrane-anchor sequence
E	0072546	cellular_component	EMC complex
F	0000045	biological_process	autophagosome assembly
F	0003674	molecular_function	molecular_function
F	0005515	molecular_function	protein binding
F	0005783	cellular_component	endoplasmic reticulum
F	0005789	cellular_component	endoplasmic reticulum membrane
F	0006644	biological_process	phospholipid metabolic process
F	0015914	biological_process	phospholipid transport
F	0016020	cellular_component	membrane
F	0032977	molecular_function	membrane insertase activity
F	0034975	biological_process	protein folding in endoplasmic reticulum
F	0045050	biological_process	protein insertion into ER membrane by stop-transfer membrane-anchor sequence
F	0072546	cellular_component	EMC complex

Functional Information from PROSITE/UniProt

site_id	PS00290
Number of Residues	7
Details	IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YACEVTH

Chain	Residue	Details
J	TYR212-HIS218
I	TYR206-HIS212

---

site_id	PS00923
Number of Residues	10
Details	ASP_GLU_RACEMASE_1 Aspartate and glutamate racemases signature 1. AMvCvNSSSN

Chain	Residue	Details
A	ALA101-ASN110

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	178
Details	Transmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	12
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	33
Details	Repeat: {"description":"TPR","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	3
Details	Topological domain: {"description":"Lumenal","evidences":[{"source":"UniProtKB","id":"Q9BV81","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	17
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---