9E61

Cryo-EM structure of Saccharomyces cerevisiae Pmt4 apo form

This is a non-PDB format compatible entry.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000030	molecular_function	mannosyltransferase activity
A	0004169	molecular_function	dolichyl-phosphate-mannose-protein mannosyltransferase activity
A	0005783	cellular_component	endoplasmic reticulum
A	0005789	cellular_component	endoplasmic reticulum membrane
A	0006486	biological_process	obsolete protein glycosylation
A	0006493	biological_process	protein O-linked glycosylation
A	0016020	cellular_component	membrane
A	0016740	molecular_function	transferase activity
A	0016757	molecular_function	glycosyltransferase activity
A	0035269	biological_process	protein O-linked glycosylation via mannose
A	0042802	molecular_function	identical protein binding
A	0097586	cellular_component	dolichyl-phosphate-mannose-protein mannosyltransferase Pmt4p homodimer complex
A	1900101	biological_process	regulation of endoplasmic reticulum unfolded protein response
B	0000030	molecular_function	mannosyltransferase activity
B	0004169	molecular_function	dolichyl-phosphate-mannose-protein mannosyltransferase activity
B	0005783	cellular_component	endoplasmic reticulum
B	0005789	cellular_component	endoplasmic reticulum membrane
B	0006486	biological_process	obsolete protein glycosylation
B	0006493	biological_process	protein O-linked glycosylation
B	0016020	cellular_component	membrane
B	0016740	molecular_function	transferase activity
B	0016757	molecular_function	glycosyltransferase activity
B	0035269	biological_process	protein O-linked glycosylation via mannose
B	0042802	molecular_function	identical protein binding
B	0097586	cellular_component	dolichyl-phosphate-mannose-protein mannosyltransferase Pmt4p homodimer complex
B	1900101	biological_process	regulation of endoplasmic reticulum unfolded protein response

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	400
Details	Transmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	824
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	154
Details	Topological domain: {"description":"Lumenal","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	120
Details	Domain: {"description":"MIR 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00131","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	118
Details	Domain: {"description":"MIR 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00131","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	114
Details	Domain: {"description":"MIR 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00131","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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