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Protein

Outer capsid protein sigma-3

Gene

S4

Organism
Reovirus type 3 (strain Dearing) (T3D) (Mammalian orthoreovirus 3)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Stimulates translation by blocking the activation of the dsRNA-dependent protein kinase EIF2AK2/PKR, thereby inhibiting the host interferon response. Sigma3 prevents the activation of EIF2AK2 by competing with the kinase for dsRNA-binding.1 Publication
The viral outer shell polypeptides, of which sigma-3 is one, impose structural constraints that prevent elongation of nascent transcripts by the RNA-dependent RNA polymerase lambda-3.By similarity

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri51 – 73CCHC-typeAdd BLAST23

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Host-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host interferon signaling pathway by virus, Inhibition of host PKR by virus, Interferon antiviral system evasion, Transcription, Transcription regulation, Translation regulation, Viral immunoevasion

Keywords - Ligandi

Metal-binding, RNA-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Outer capsid protein sigma-3
Short name:
Sigma3
Gene namesi
Name:S4
OrganismiReovirus type 3 (strain Dearing) (T3D) (Mammalian orthoreovirus 3)
Taxonomic identifieri10886 [NCBI]
Taxonomic lineageiVirusesdsRNA virusesReoviridaeSpinareovirinaeOrthoreovirus
Virus hostiMammalia [TaxID: 40674]
Proteomesi
  • UP000006373 Componenti: Genome

Subcellular locationi

  • Virion

  • Note: Found in the outer capsid. Each subunit is positioned with the small lobe anchoring it to the protein mu1 on the surface of the virion, and the large lobe, the site of initial cleavages during entry-related proteolytic disassembly, protruding outwards.

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Capsid protein, Outer capsid protein, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002227521 – 365Outer capsid protein sigma-3Add BLAST365

Post-translational modificationi

Cleaved during virus the endosomal proteolytic disassembly of the outer capsid.

Interactioni

Subunit structurei

Heterohexamer of three sigma-3 and three Mu-1 proteins (By similarity). The RNA-binding form is probably a homodimer.By similarity

Structurei

Secondary structure

1365
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi8 – 18Combined sources11
Turni19 – 21Combined sources3
Beta strandi25 – 27Combined sources3
Turni28 – 30Combined sources3
Beta strandi41 – 45Combined sources5
Beta strandi48 – 51Combined sources4
Turni52 – 54Combined sources3
Beta strandi57 – 60Combined sources4
Helixi61 – 63Combined sources3
Helixi79 – 111Combined sources33
Helixi115 – 124Combined sources10
Beta strandi126 – 130Combined sources5
Helixi133 – 135Combined sources3
Turni141 – 143Combined sources3
Helixi159 – 176Combined sources18
Beta strandi180 – 186Combined sources7
Helixi189 – 192Combined sources4
Helixi199 – 203Combined sources5
Beta strandi221 – 223Combined sources3
Helixi226 – 230Combined sources5
Helixi232 – 234Combined sources3
Helixi236 – 242Combined sources7
Helixi246 – 249Combined sources4
Helixi252 – 254Combined sources3
Beta strandi259 – 261Combined sources3
Beta strandi270 – 272Combined sources3
Helixi275 – 277Combined sources3
Beta strandi282 – 284Combined sources3
Helixi288 – 292Combined sources5
Helixi293 – 295Combined sources3
Helixi296 – 305Combined sources10
Helixi308 – 315Combined sources8
Helixi319 – 334Combined sources16
Helixi338 – 341Combined sources4
Beta strandi351 – 354Combined sources4
Beta strandi356 – 358Combined sources3
Beta strandi362 – 365Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FN9X-ray1.80A/B1-365[»]
ProteinModelPortaliP03527.
SMRiP03527.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03527.

Family & Domainsi

Sequence similaritiesi

Contains 1 CCHC-type zinc finger.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri51 – 73CCHC-typeAdd BLAST23

Keywords - Domaini

Zinc-finger

Family and domain databases

InterProiIPR000153. Reo_capsid_sigma3.
IPR023634. Reovirus_capsid_sigma-3_dom.
[Graphical view]
PfamiPF00979. Reovirus_cap. 1 hit.
[Graphical view]
SUPFAMiSSF64465. SSF64465. 1 hit.

Sequencei

Sequence statusi: Complete.

P03527-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEVCLPNGHQ VVDLINNAFE GRVSIYSAQE GWDKTISAQP DMMVCGGAVV
60 70 80 90 100
CMHCLGVVGS LQRKLKHLPH HRCNQQIRHQ DYVDVQFADR VTAHWKRGML
110 120 130 140 150
SFVAQMHEMM NDVSPDDLDR VRTEGGSLVE LNWLQVDPNS MFRSIHSSWT
160 170 180 190 200
DPLQVVDDLD TKLDQYWTAL NLMIDSSDLI PNFMMRDPSH AFNGVKLGGD
210 220 230 240 250
ARQTQFSRTF DSRSSLEWGV MVYDYSELEH DPSKGRAYRK ELVTPARDFG
260 270 280 290 300
HFGLSHYSRA TTPILGKMPA VFSGMLTGNC KMYPFIKGTA KLKTVRKLVE
310 320 330 340 350
AVNHAWGVEK IRYALGPGGM TGWYNRTMQQ APIVLTPAAL TMFPDTIKFG
360
DLNYPVMIGD PMILG
Length:365
Mass (Da):41,118
Last modified:July 22, 2008 - v2
Checksum:iCF50174AA43244EB
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti133W → R in AAA47283 (PubMed:6492267).Curated1
Sequence conflicti198G → E in AAA47283 (PubMed:6492267).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti354Y → H in strain: Isolate D-EA1 and Isolate D-EA3; altered susceptibility to proteolysis during virus disassembly. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K02739 Genomic RNA. Translation: AAA47283.1.
AF332137 Genomic RNA. Translation: AAK07648.1.
EF494444 Genomic RNA. Translation: ABP48922.1.
PIRiA04127. MNXRS3.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K02739 Genomic RNA. Translation: AAA47283.1.
AF332137 Genomic RNA. Translation: AAK07648.1.
EF494444 Genomic RNA. Translation: ABP48922.1.
PIRiA04127. MNXRS3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FN9X-ray1.80A/B1-365[»]
ProteinModelPortaliP03527.
SMRiP03527.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP03527.

Family and domain databases

InterProiIPR000153. Reo_capsid_sigma3.
IPR023634. Reovirus_capsid_sigma-3_dom.
[Graphical view]
PfamiPF00979. Reovirus_cap. 1 hit.
[Graphical view]
SUPFAMiSSF64465. SSF64465. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiSIGM3_REOVD
AccessioniPrimary (citable) accession number: P03527
Secondary accession number(s): A4ZY29, Q99AV2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 22, 2008
Last modified: November 2, 2016
This is version 84 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.