8YVY

Semliki Forest virus virion

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004252	molecular_function	serine-type endopeptidase activity
A	0019028	cellular_component	viral capsid
A	0055036	cellular_component	virion membrane
B	0005198	molecular_function	structural molecule activity
B	0019028	cellular_component	viral capsid
C	0004252	molecular_function	serine-type endopeptidase activity
C	0019028	cellular_component	viral capsid
C	0055036	cellular_component	virion membrane
D	0004252	molecular_function	serine-type endopeptidase activity
D	0006508	biological_process	proteolysis
F	0004252	molecular_function	serine-type endopeptidase activity
F	0019028	cellular_component	viral capsid
F	0055036	cellular_component	virion membrane
G	0004252	molecular_function	serine-type endopeptidase activity
G	0019028	cellular_component	viral capsid
G	0055036	cellular_component	virion membrane
H	0004252	molecular_function	serine-type endopeptidase activity
H	0019028	cellular_component	viral capsid
H	0055036	cellular_component	virion membrane
I	0005198	molecular_function	structural molecule activity
I	0019028	cellular_component	viral capsid
J	0005198	molecular_function	structural molecule activity
J	0019028	cellular_component	viral capsid
K	0005198	molecular_function	structural molecule activity
K	0019028	cellular_component	viral capsid
L	0004252	molecular_function	serine-type endopeptidase activity
L	0019028	cellular_component	viral capsid
L	0055036	cellular_component	virion membrane
M	0004252	molecular_function	serine-type endopeptidase activity
M	0019028	cellular_component	viral capsid
M	0055036	cellular_component	virion membrane
N	0004252	molecular_function	serine-type endopeptidase activity
N	0019028	cellular_component	viral capsid
N	0055036	cellular_component	virion membrane
O	0004252	molecular_function	serine-type endopeptidase activity
O	0006508	biological_process	proteolysis
P	0004252	molecular_function	serine-type endopeptidase activity
P	0006508	biological_process	proteolysis
Q	0004252	molecular_function	serine-type endopeptidase activity
Q	0006508	biological_process	proteolysis

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	ACT_SITE: Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01027

Chain	Residue	Details
D	HIS145
D	ASP167
O	HIS145
O	ASP167
P	HIS145
P	ASP167
Q	HIS145
Q	ASP167

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site_id	SWS_FT_FI2
Number of Residues	4
Details	ACT_SITE: Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01027, ECO:0000269|PubMed:3553612

Chain	Residue	Details
D	SER219
O	SER219
P	SER219
Q	SER219

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site_id	SWS_FT_FI3
Number of Residues	8
Details	SITE: Involved in dimerization of the capsid protein => ECO:0000250|UniProtKB:Q86925

Chain	Residue	Details
D	TYR193
D	ASN226
O	TYR193
O	ASN226
P	TYR193
P	ASN226
Q	TYR193
Q	ASN226

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site_id	SWS_FT_FI4
Number of Residues	4
Details	SITE: Cleavage; by autolysis => ECO:0000269|PubMed:3553612

Chain	Residue	Details
D	TRP267
O	TRP267
P	TRP267
Q	TRP267

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site_id	SWS_FT_FI5
Number of Residues	12
Details	LIPID: S-palmitoyl cysteine; by host => ECO:0000250

Chain	Residue	Details
B	CYS395
K	CYS395
K	CYS415
K	CYS416
B	CYS415
B	CYS416
I	CYS395
I	CYS415
I	CYS416
J	CYS395
J	CYS415
J	CYS416

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site_id	SWS_FT_FI6
Number of Residues	8
Details	CARBOHYD: N-linked (GlcNAc...) asparagine; by host => ECO:0000255

Chain	Residue	Details
B	ASN200
B	ASN262
I	ASN200
I	ASN262
J	ASN200
J	ASN262
K	ASN200
K	ASN262

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