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P13418 (POLS_CRPVC) Reviewed, UniProtKB/Swiss-Prot

Last modified July 24, 2013. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Structural polyprotein

Cleaved into the following 4 chains:

  1. Capsid protein 1
    Alternative name(s):
    CP1
  2. Capsid protein 4
    Alternative name(s):
    CP4
  3. Capsid protein 2
    Alternative name(s):
    CP2
  4. Capsid protein 3
    Alternative name(s):
    CP3
OrganismCricket paralysis virus (isolate Teleogryllus commodus/Australia/CrPVVIC/1968) (CrPV) [Reference proteome]
Taxonomic identifier928300 [NCBI]
Taxonomic lineageVirusesssRNA positive-strand viruses, no DNA stagePicornaviralesDicistroviridaeCripavirus
Virus hostTeleogryllus oceanicus (black field cricket) [TaxID: 128161]

Protein attributes

Sequence length895 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Structural polyprotein: precursor of all the viral capsid proteins.

Capsid protein 1, together with capsid proteins 2 and 3, form an icosahedral capsid protecting the viral RNA genome. The icosahedral capsid has a pseudo-T=3 symmetry with a diameter of approximately 300 Angstroms, and is composed of 60 copies of each CP1, CP2, and CP3. CP1 is situated at the 12 fivefold axes, whereas CP2 and CP3 are located at the quasi-sixfold axes. All these proteins contain a beta-sheet structure called beta-barrel jelly roll.

Capsid protein 4 is a tstructural component of the icosahedral capsid protecting the genomic RNA. It may play an important role in capsid assembly.

Capsid protein 2, together with capsid proteins 1 and 3, form an icosahedral capsid protecting the viral RNA genome. The icosahedral capsid has a pseudo-T=3 symmetry with a diameter of approximately 300 Angstroms, and is composed of 60 copies of each CP1, CP2, and CP3. CP1 is situated at the 12 fivefold axes, whereas CP2 and CP3 are located at the quasi-sixfold axes. All these proteins contain a beta-sheet structure called beta-barrel jelly roll.

Capsid protein 3, together with capsid proteins 1 and 2, form an icosahedral capsid protecting the viral RNA genome. The icosahedral capsid has a pseudo-T=3 symmetry with a diameter of approximately 300 Angstroms, and is composed of 60 copies of each CP1, CP2, and CP3. CP1 is situated at the 12 fivefold axes, whereas CP2 and CP3 are located at the quasi-sixfold axes. All these proteins contain a beta-sheet structure called beta-barrel jelly roll.

Subcellular location

Capsid protein 1: Virion. Host cytoplasm Potential.

Capsid protein 4: Virion. Host cytoplasm Potential.

Capsid protein 2: Virion. Host cytoplasm Potential.

Capsid protein 3: Virion. Host cytoplasm Potential.

Post-translational modification

Specific enzymatic cleavages in vivo yield mature proteins.

Sequence similarities

Belongs to the picornaviruses polyprotein family.

Caution

Translation initiates on an Ala codon through an unusual Internal Ribosome Entry Site (IRES).

Ontologies

Keywords
   Cellular componentCapsid protein
Host cytoplasm
Virion
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componenthost cell cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

viral capsid

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionstructural molecule activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 895895Structural polyprotein
PRO_0000123825
Chain1 – 283283Capsid protein 1
PRO_0000398368
Chain284 – 34057Capsid protein 4
PRO_0000398369
Chain341 – 635295Capsid protein 2
PRO_0000398370
Chain636 – 895260Capsid protein 3
PRO_0000398371

Sites

Site283 – 2842Cleavage
Site340 – 3412Cleavage
Site635 – 6362Cleavage

Experimental info

Sequence conflict445 – 4473THM → HTH in AAA42889. Ref.2
Sequence conflict4511A → T in AAA42889. Ref.2
Sequence conflict5561V → T in AAA42889. Ref.2
Sequence conflict5791S → N in AAA42889. Ref.2
Sequence conflict594 – 5952YV → MY in AAA42889. Ref.2
Sequence conflict6011L → D in AAA42889. Ref.2
Sequence conflict641 – 6422QQ → HE in AAA42889. Ref.2
Sequence conflict6481A → G in AAA42889. Ref.2
Sequence conflict678 – 6836VSIRQL → IDSTT in AAA42889. Ref.2
Sequence conflict7461A → V in AAA42889. Ref.2
Sequence conflict854 – 8552SP → A in AAA42889. Ref.2
Sequence conflict861 – 89535ATNHH…NVARA → TTHTRSYACAW in AAA42889. Ref.2

Secondary structure

......................................................................................................................................................... 895
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P13418 [UniParc].

Last modified October 11, 2004. Version 2.
Checksum: 92DA9084DDA850EE

FASTA895100,298
        10         20         30         40         50         60 
ATFQDKQENS HIENEDKRLM SEQKEIVHFV SEGITPSTTA LPDIVNLSTN YLDMTTREDR 

        70         80         90        100        110        120 
IHSIKDFLSG PIIIATNLWS SSDPVEKQLY TANFPEVLIS NAMYQDKLKG FVGLRATLVV 

       130        140        150        160        170        180 
KVQVNSQPFQ QGRLMLQYIP YAQYMPNRVT LINETLQGRS GCPTTDLELS VGTEVEMRIP 

       190        200        210        220        230        240 
YVSPHLYYNL ITGQGSFGSI YVVVYSQLHD QVSGTGSIEY TVWAHLEDVD VQYPTGANIF 

       250        260        270        280        290        300 
TGNSPNYLSI AERIATGDFT ETEMRKLWIH KTYLKRPARI YAQAAKELKQ LETNNSPSTA 

       310        320        330        340        350        360 
LGQISEGLTT LSHIPVLGNI FSTPAWISAK AADLAKLFGF SKPTVQGKIG ECKLRGQGRM 

       370        380        390        400        410        420 
ANFDGMDMSH KMALSSTNEI ETKEGLAGTS LDEMDLSRVL SIPNYWDRFT WKTSDVTNTV 

       430        440        450        460        470        480 
LWDNYVSPFK VKPYSATITD RFRCTHMGYV ANAFTYWRGS IVYTFKFVKT QYHSGRLRIS 

       490        500        510        520        530        540 
FIPYYYNTTI STGTPDVSRT QKIVVDLRTS TEVSFTVPYI ASRPWLYCIR PESSWLSKDN 

       550        560        570        580        590        600 
KDGALMYNCV SGIVRVEVLN QLVAAQNVFS EIDVICEVSG GPDLEFAGPT CPSYVPYAGD 

       610        620        630        640        650        660 
LTLADTRKIE AERTQEYSNN EDNRITTQCS RIVAQVMGED QQIPRNEAQH GVHPISIDTH 

       670        680        690        700        710        720 
RISNNWSPQA MCIGEKIVSI RQLIKRFGIF GDANTLQADG SSFVVAPFTV TSPTKTLTST 

       730        740        750        760        770        780 
RNYTQFDYYY YLYAFWRGSM RIKMVAETQD GTGTPRKKTN FTWFVRMFNS LQDSFNSLIS 

       790        800        810        820        830        840 
TSSSAVTTTV LPSGTINMGP STQVIDPTVE GLIEVEVPYY NISHITPAVT IDDGTPSMED 

       850        860        870        880        890 
YLKGHSPPCL LTFSPRDSIS ATNHHITASF MRAPGDDFSF MYLLEVPPLV NVARA 

« Hide

References

[1]"Naturally occurring dicistronic cricket paralysis virus RNA is regulated by two internal ribosome entry sites."
Wilson J.E., Powell M.J., Hoover S.E., Sarnow P.
Mol. Cell. Biol. 20:4990-4999(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]"Cloning of the genome of cricket paralysis virus: sequence of the 3' end."
King L.A., Pullin J.S.K., Stanway G., Almond J.W., Moore N.F.
Virus Res. 6:331-344(1987)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 444-895.
[3]"Translation initiation by factor-independent binding of eukaryotic ribosomes to internal ribosomal entry sites."
Pisarev A.V., Shirokikh N.E., Hellen C.U.
C. R. Biol. 328:589-605(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NON-METHIONINE TRANSLATION INITIATION.
[4]"Translation initiation factors are not required for Dicistroviridae IRES function in vivo."
Deniz N., Lenarcic E.M., Landry D.M., Thompson S.R.
RNA 15:932-946(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NON-METHIONINE TRANSLATION INITIATION.
[5]"The crystal structure of cricket paralysis virus: the first view of a new virus family."
Tate J., Liljas L., Scotti P., Christian P., Lin T., Johnson J.E.
Nat. Struct. Biol. 6:765-774(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 8-895, POLYPROTEIN PROTEOLYTIC CLEAVAGES.

Web resources

Virus Particle ExploreR db

Icosahedral capsid structure

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF218039 Genomic RNA. Translation: AAF80999.1.
M21938 Genomic RNA. Translation: AAA42889.1.
PIRS28374.
RefSeqNP_647482.1. NC_003924.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1B35X-ray2.40A636-895[»]
B8-243[»]
C341-622[»]
D284-340[»]
ProteinModelPortalP13418.
SMRP13418. Positions 8-243, 284-622, 636-895.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID944542.

Family and domain databases

InterProIPR014872. Dicistrovirus_capsid-polyPr_C.
IPR001676. Picornavirus_capsid.
IPR024343. VP4_dicistrovir.
[Graphical view]
PfamPF08762. CRPV_capsid. 1 hit.
PF11492. Dicistro_VP4. 1 hit.
PF00073. Rhv. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP13418.

Entry information

Entry namePOLS_CRPVC
AccessionPrimary (citable) accession number: P13418
Secondary accession number(s): Q9IJX3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: October 11, 2004
Last modified: July 24, 2013
This is version 72 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references