Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6ND1

CryoEM structure of the Sec Complex from yeast

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003723	molecular_function	RNA binding
A	0005515	molecular_function	protein binding
A	0005637	cellular_component	nuclear inner membrane
A	0005739	cellular_component	mitochondrion
A	0005783	cellular_component	endoplasmic reticulum
A	0005789	cellular_component	endoplasmic reticulum membrane
A	0006614	biological_process	SRP-dependent cotranslational protein targeting to membrane
A	0006620	biological_process	post-translational protein targeting to endoplasmic reticulum membrane
A	0008320	molecular_function	protein transmembrane transporter activity
A	0015031	biological_process	protein transport
A	0030867	cellular_component	rough endoplasmic reticulum membrane
A	0031204	biological_process	post-translational protein targeting to membrane, translocation
A	0031207	cellular_component	Sec62/Sec63 complex
A	0031965	cellular_component	nuclear membrane
A	0046967	biological_process	cytosol to endoplasmic reticulum transport
B	0005048	molecular_function	signal sequence binding
B	0005515	molecular_function	protein binding
B	0005783	cellular_component	endoplasmic reticulum
B	0005784	cellular_component	Sec61 translocon complex
B	0005789	cellular_component	endoplasmic reticulum membrane
B	0006616	biological_process	SRP-dependent cotranslational protein targeting to membrane, translocation
B	0008320	molecular_function	protein transmembrane transporter activity
B	0015031	biological_process	protein transport
B	0015450	molecular_function	protein-transporting ATPase activity
B	0016020	cellular_component	membrane
B	0030867	cellular_component	rough endoplasmic reticulum membrane
B	0030970	biological_process	retrograde protein transport, ER to cytosol
B	0031204	biological_process	post-translational protein targeting to membrane, translocation
B	0036503	biological_process	ERAD pathway
B	0043022	molecular_function	ribosome binding
B	0045184	biological_process	establishment of protein localization
B	0070843	biological_process	misfolded protein transport
B	1904680	molecular_function	peptide transmembrane transporter activity
C	0005198	molecular_function	structural molecule activity
C	0005515	molecular_function	protein binding
C	0005637	cellular_component	nuclear inner membrane
C	0005783	cellular_component	endoplasmic reticulum
C	0005784	cellular_component	Sec61 translocon complex
C	0005789	cellular_component	endoplasmic reticulum membrane
C	0006605	biological_process	protein targeting
C	0006614	biological_process	SRP-dependent cotranslational protein targeting to membrane
C	0006616	biological_process	SRP-dependent cotranslational protein targeting to membrane, translocation
C	0006886	biological_process	intracellular protein transport
C	0008320	molecular_function	protein transmembrane transporter activity
C	0015031	biological_process	protein transport
C	0015450	molecular_function	protein-transporting ATPase activity
C	0016020	cellular_component	membrane
C	0030867	cellular_component	rough endoplasmic reticulum membrane
C	0031204	biological_process	post-translational protein targeting to membrane, translocation
C	0071261	cellular_component	Ssh1 translocon complex
D	0005085	molecular_function	guanyl-nucleotide exchange factor activity
D	0005515	molecular_function	protein binding
D	0005783	cellular_component	endoplasmic reticulum
D	0005784	cellular_component	Sec61 translocon complex
D	0005789	cellular_component	endoplasmic reticulum membrane
D	0005829	cellular_component	cytosol
D	0006616	biological_process	SRP-dependent cotranslational protein targeting to membrane, translocation
D	0006886	biological_process	intracellular protein transport
D	0008320	molecular_function	protein transmembrane transporter activity
D	0015031	biological_process	protein transport
D	0015450	molecular_function	protein-transporting ATPase activity
D	0016020	cellular_component	membrane
D	0030867	cellular_component	rough endoplasmic reticulum membrane
D	0031204	biological_process	post-translational protein targeting to membrane, translocation
E	0005515	molecular_function	protein binding
E	0005783	cellular_component	endoplasmic reticulum
E	0005789	cellular_component	endoplasmic reticulum membrane
E	0008320	molecular_function	protein transmembrane transporter activity
E	0015031	biological_process	protein transport
E	0030447	biological_process	filamentous growth
E	0030867	cellular_component	rough endoplasmic reticulum membrane
E	0031204	biological_process	post-translational protein targeting to membrane, translocation
E	0031207	cellular_component	Sec62/Sec63 complex
E	0071944	cellular_component	cell periphery
F	0005515	molecular_function	protein binding
F	0005737	cellular_component	cytoplasm
F	0005783	cellular_component	endoplasmic reticulum
F	0008320	molecular_function	protein transmembrane transporter activity
F	0015031	biological_process	protein transport
F	0030867	cellular_component	rough endoplasmic reticulum membrane
F	0031204	biological_process	post-translational protein targeting to membrane, translocation
F	0031207	cellular_component	Sec62/Sec63 complex

Functional Information from PROSITE/UniProt

site_id	PS00636
Number of Residues	20
Details	DNAJ_1 Nt-dnaJ domain signature. YVqITkaYEsLtDelvRQNY

Chain	Residue	Details
A	TYR173-TYR192

site_id	PS00755
Number of Residues	20
Details	SECY_1 Protein secY signature 1. TLLeLGVsPIItSSMIFQFL

Chain	Residue	Details
B	THR76-LEU95

site_id	PS00756
Number of Residues	19
Details	SECY_2 Protein secY signature 2. LLdElLSkgyGLGSGiSLF

Chain	Residue	Details
B	LEU166-PHE184

site_id	PS01067
Number of Residues	29
Details	SECE_SEC61G Protein secE/sec61-gamma signature. FvREgTqfLaKckKPdlkEytkivKAVGI

Chain	Residue	Details
C	PHE28-ILE56

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	20
Details	Transmembrane: {"description":"Helical; Name=4","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	107
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	11
Details	Transmembrane: {"description":"Helical; Name=5","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	19
Details	Transmembrane: {"description":"Helical; Name=6","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	20
Details	Transmembrane: {"description":"Helical; Name=7","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	19
Details	Transmembrane: {"description":"Helical; Name=8","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	17
Details	Transmembrane: {"description":"Helical; Name=9","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	2
Details	Topological domain: {"description":"Lumenal","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	21
Details	Transmembrane: {"description":"Helical; Name=10","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	81
Details	Transmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	304
Details	Domain: {"description":"SEC63"}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	10
Details	Repeat: {"description":"1"}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	10
Details	Repeat: {"description":"2"}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	42
Details	Region: {"description":"2 X 11 AA repeats"}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17287358","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"17330950","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	4
Details	Topological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)