1LD4

Placement of the Structural Proteins in Sindbis Virus

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004252	molecular_function	serine-type endopeptidase activity
A	0006508	biological_process	proteolysis
B	0004252	molecular_function	serine-type endopeptidase activity
B	0006508	biological_process	proteolysis
C	0004252	molecular_function	serine-type endopeptidase activity
C	0006508	biological_process	proteolysis
D	0004252	molecular_function	serine-type endopeptidase activity
D	0006508	biological_process	proteolysis
E	0003700	molecular_function	DNA-binding transcription factor activity
E	0006355	biological_process	regulation of DNA-templated transcription
F	0003700	molecular_function	DNA-binding transcription factor activity
F	0006355	biological_process	regulation of DNA-templated transcription
G	0003700	molecular_function	DNA-binding transcription factor activity
G	0006355	biological_process	regulation of DNA-templated transcription
H	0003700	molecular_function	DNA-binding transcription factor activity
H	0006355	biological_process	regulation of DNA-templated transcription
I	0003700	molecular_function	DNA-binding transcription factor activity
I	0006355	biological_process	regulation of DNA-templated transcription
J	0003700	molecular_function	DNA-binding transcription factor activity
J	0006355	biological_process	regulation of DNA-templated transcription
K	0003700	molecular_function	DNA-binding transcription factor activity
K	0006355	biological_process	regulation of DNA-templated transcription
L	0003700	molecular_function	DNA-binding transcription factor activity
L	0006355	biological_process	regulation of DNA-templated transcription
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	0019028	cellular_component	viral capsid
O	0055036	cellular_component	virion membrane
P	0004252	molecular_function	serine-type endopeptidase activity
P	0019028	cellular_component	viral capsid
P	0055036	cellular_component	virion membrane

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE LYS M1196

Chain	Residue
M	MET1195
M	PRO1197
M	GLY1198
M	ALA1199

---

site_id	AC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE UNX N4440

Chain	Residue
N	ARG4324
N	GLU4325

---

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE LYS N4196

Chain	Residue
N	ALA4199
N	MET4195
N	PRO4197
N	GLY4198

---

site_id	AC4
Number of Residues	1
Details	BINDING SITE FOR RESIDUE UNX O5440

Chain	Residue
O	GLU5325

---

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE LYS O5196

Chain	Residue
O	MET5195
O	PRO5197
O	GLY5198
O	ALA5199

---

site_id	AC6
Number of Residues	1
Details	BINDING SITE FOR RESIDUE UNX P6440

Chain	Residue
P	GLU6325

---

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE LYS P6196

Chain	Residue
P	MET6195
P	PRO6197
P	GLY6198
P	ALA6199

---

Functional Information from PROSITE/UniProt

site_id	PS00036
Number of Residues	15
Details	BZIP_BASIC Basic-leucine zipper (bZIP) domain signature. Kra.RNTeAARRsRAR

Chain	Residue	Details
E	LYS1131-ARG1145

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	600
Details	Domain: {"description":"Peptidase S3","evidences":[{"source":"PROSITE-ProRule","id":"PRU01027","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	36
Details	Region: {"description":"Interaction with spike glycoprotein E2","evidences":[{"source":"PubMed","id":"22001018","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	56
Details	Region: {"description":"Dimerization of the capsid protein","evidences":[{"source":"UniProtKB","id":"P0DOK1","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	40
Details	Motif: {"description":"Nuclear export signal","evidences":[{"source":"UniProtKB","id":"P09592","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	12
Details	Active site: {"description":"Charge relay system","evidences":[{"source":"PROSITE-ProRule","id":"PRU01027","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1944569","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8450538","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	8
Details	Site: {"description":"Involved in dimerization of the capsid protein","evidences":[{"source":"UniProtKB","id":"Q86925","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	168
Details	Region: {"description":"Leucine-zipper","evidences":[{"source":"PROSITE-ProRule","id":"PRU00978","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1473154","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	68
Details	Region: {"description":"E1 fusion peptide loop","evidences":[{"source":"UniProtKB","id":"Q8JUX5","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	8
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"source":"PubMed","id":"12388725","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---