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P13418

- POLS_CRPVC

UniProt

P13418 - POLS_CRPVC

Protein

Structural polyprotein

Gene
N/A
Organism
Cricket paralysis virus (isolate Teleogryllus commodus/Australia/CrPVVIC/1968) (CrPV)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 75 (01 Oct 2014)
      Sequence version 2 (11 Oct 2004)
      Previous versions | rss
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    Functioni

    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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei283 – 2842Cleavage
    Sitei340 – 3412Cleavage
    Sitei635 – 6362Cleavage

    GO - Molecular functioni

    1. structural molecule activity Source: InterPro

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Structural polyprotein
    Cleaved into the following 4 chains:
    Alternative name(s):
    CP1
    Alternative name(s):
    CP4
    Alternative name(s):
    CP2
    Alternative name(s):
    CP3
    OrganismiCricket paralysis virus (isolate Teleogryllus commodus/Australia/CrPVVIC/1968) (CrPV)
    Taxonomic identifieri928300 [NCBI]
    Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stagePicornaviralesDicistroviridaeCripavirus
    Virus hostiTeleogryllus oceanicus (black field cricket) [TaxID: 128161]
    ProteomesiUP000008590: Genome

    Subcellular locationi

    GO - Cellular componenti

    1. host cell cytoplasm Source: UniProtKB-SubCell
    2. viral capsid Source: UniProtKB-KW

    Keywords - Cellular componenti

    Capsid protein, Host cytoplasm, Virion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 895895Structural polyproteinPRO_0000123825Add
    BLAST
    Chaini1 – 283283Capsid protein 1PRO_0000398368Add
    BLAST
    Chaini284 – 34057Capsid protein 4PRO_0000398369Add
    BLAST
    Chaini341 – 635295Capsid protein 2PRO_0000398370Add
    BLAST
    Chaini636 – 895260Capsid protein 3PRO_0000398371Add
    BLAST

    Post-translational modificationi

    Specific enzymatic cleavages in vivo yield mature proteins.

    Structurei

    Secondary structure

    1
    895
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi15 – 173
    Beta strandi19 – 246
    Beta strandi27 – 337
    Beta strandi40 – 423
    Helixi49 – 524
    Turni53 – 564
    Helixi64 – 674
    Beta strandi72 – 809
    Beta strandi88 – 947
    Helixi96 – 994
    Helixi102 – 1087
    Beta strandi111 – 12515
    Beta strandi131 – 14010
    Helixi142 – 1443
    Helixi146 – 1538
    Helixi156 – 1605
    Beta strandi162 – 1687
    Turni169 – 1713
    Beta strandi174 – 1796
    Beta strandi184 – 1896
    Turni190 – 1934
    Beta strandi198 – 20912
    Turni211 – 2133
    Beta strandi217 – 23418
    Helixi285 – 2939
    Helixi305 – 3073
    Beta strandi320 – 3234
    Helixi331 – 3377
    Beta strandi356 – 3594
    Beta strandi363 – 3653
    Turni384 – 3874
    Helixi396 – 4005
    Beta strandi404 – 4129
    Beta strandi420 – 4256
    Beta strandi431 – 4377
    Beta strandi440 – 4445
    Helixi446 – 4516
    Beta strandi455 – 4595
    Beta strandi461 – 4688
    Beta strandi473 – 48311
    Turni488 – 4903
    Beta strandi491 – 4933
    Helixi497 – 4993
    Beta strandi500 – 50910
    Beta strandi512 – 5176
    Beta strandi522 – 5243
    Helixi534 – 5363
    Turni542 – 5454
    Helixi546 – 5483
    Beta strandi552 – 56413
    Beta strandi570 – 58011
    Beta strandi593 – 5975
    Helixi603 – 61715
    Beta strandi637 – 6393
    Helixi645 – 6484
    Turni649 – 6513
    Helixi667 – 6726
    Helixi680 – 6834
    Beta strandi688 – 6969
    Beta strandi702 – 7054
    Beta strandi716 – 7183
    Helixi725 – 7295
    Helixi730 – 7323
    Beta strandi733 – 7375
    Beta strandi740 – 75112
    Beta strandi756 – 7583
    Beta strandi763 – 7686
    Beta strandi770 – 7723
    Helixi773 – 7786
    Beta strandi785 – 7895
    Beta strandi793 – 7953
    Beta strandi801 – 8055
    Helixi807 – 8104
    Beta strandi811 – 8177
    Beta strandi822 – 8243
    Beta strandi831 – 8344
    Helixi838 – 8425
    Beta strandi850 – 8578
    Turni861 – 8633
    Beta strandi864 – 87411
    Beta strandi879 – 8835
    Beta strandi889 – 8913

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1B35X-ray2.40A636-895[»]
    B8-243[»]
    C341-622[»]
    D284-340[»]
    ProteinModelPortaliP13418.
    SMRiP13418. Positions 8-243, 284-622, 636-895.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP13418.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the picornaviruses polyprotein family.Curated

    Family and domain databases

    Gene3Di2.60.120.20. 3 hits.
    InterProiIPR014872. Dicistrovirus_capsid-polyPr_C.
    IPR001676. Picornavirus_capsid.
    IPR029053. Viral_coat.
    IPR024343. VP4_dicistrovir.
    [Graphical view]
    PfamiPF08762. CRPV_capsid. 1 hit.
    PF11492. Dicistro_VP4. 1 hit.
    PF00073. Rhv. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P13418-1 [UniParc]FASTAAdd to Basket

    « Hide

    ATFQDKQENS HIENEDKRLM SEQKEIVHFV SEGITPSTTA LPDIVNLSTN    50
    YLDMTTREDR IHSIKDFLSG PIIIATNLWS SSDPVEKQLY TANFPEVLIS 100
    NAMYQDKLKG FVGLRATLVV KVQVNSQPFQ QGRLMLQYIP YAQYMPNRVT 150
    LINETLQGRS GCPTTDLELS VGTEVEMRIP YVSPHLYYNL ITGQGSFGSI 200
    YVVVYSQLHD QVSGTGSIEY TVWAHLEDVD VQYPTGANIF TGNSPNYLSI 250
    AERIATGDFT ETEMRKLWIH KTYLKRPARI YAQAAKELKQ LETNNSPSTA 300
    LGQISEGLTT LSHIPVLGNI FSTPAWISAK AADLAKLFGF SKPTVQGKIG 350
    ECKLRGQGRM ANFDGMDMSH KMALSSTNEI ETKEGLAGTS LDEMDLSRVL 400
    SIPNYWDRFT WKTSDVTNTV LWDNYVSPFK VKPYSATITD RFRCTHMGYV 450
    ANAFTYWRGS IVYTFKFVKT QYHSGRLRIS FIPYYYNTTI STGTPDVSRT 500
    QKIVVDLRTS TEVSFTVPYI ASRPWLYCIR PESSWLSKDN KDGALMYNCV 550
    SGIVRVEVLN QLVAAQNVFS EIDVICEVSG GPDLEFAGPT CPSYVPYAGD 600
    LTLADTRKIE AERTQEYSNN EDNRITTQCS RIVAQVMGED QQIPRNEAQH 650
    GVHPISIDTH RISNNWSPQA MCIGEKIVSI RQLIKRFGIF GDANTLQADG 700
    SSFVVAPFTV TSPTKTLTST RNYTQFDYYY YLYAFWRGSM RIKMVAETQD 750
    GTGTPRKKTN FTWFVRMFNS LQDSFNSLIS TSSSAVTTTV LPSGTINMGP 800
    STQVIDPTVE GLIEVEVPYY NISHITPAVT IDDGTPSMED YLKGHSPPCL 850
    LTFSPRDSIS ATNHHITASF MRAPGDDFSF MYLLEVPPLV NVARA 895
    Length:895
    Mass (Da):100,298
    Last modified:October 11, 2004 - v2
    Checksum:i92DA9084DDA850EE
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti445 – 4473THM → HTH in AAA42889. 1 PublicationCurated
    Sequence conflicti451 – 4511A → T in AAA42889. 1 PublicationCurated
    Sequence conflicti556 – 5561V → T in AAA42889. 1 PublicationCurated
    Sequence conflicti579 – 5791S → N in AAA42889. 1 PublicationCurated
    Sequence conflicti594 – 5952YV → MY in AAA42889. 1 PublicationCurated
    Sequence conflicti601 – 6011L → D in AAA42889. 1 PublicationCurated
    Sequence conflicti641 – 6422QQ → HE in AAA42889. 1 PublicationCurated
    Sequence conflicti648 – 6481A → G in AAA42889. 1 PublicationCurated
    Sequence conflicti678 – 6836VSIRQL → IDSTT in AAA42889. 1 PublicationCurated
    Sequence conflicti746 – 7461A → V in AAA42889. 1 PublicationCurated
    Sequence conflicti854 – 8552SP → A in AAA42889. 1 PublicationCurated
    Sequence conflicti861 – 89535ATNHH…NVARA → TTHTRSYACAW in AAA42889. 1 PublicationCuratedAdd
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF218039 Genomic RNA. Translation: AAF80999.1.
    M21938 Genomic RNA. Translation: AAA42889.1.
    PIRiS28374.
    RefSeqiNP_647482.1. NC_003924.1.

    Genome annotation databases

    GeneIDi944542.

    Cross-referencesi

    Web resourcesi

    Virus Particle ExploreR db

    Icosahedral capsid structure

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF218039 Genomic RNA. Translation: AAF80999.1 .
    M21938 Genomic RNA. Translation: AAA42889.1 .
    PIRi S28374.
    RefSeqi NP_647482.1. NC_003924.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1B35 X-ray 2.40 A 636-895 [» ]
    B 8-243 [» ]
    C 341-622 [» ]
    D 284-340 [» ]
    ProteinModelPortali P13418.
    SMRi P13418. Positions 8-243, 284-622, 636-895.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 944542.

    Miscellaneous databases

    EvolutionaryTracei P13418.

    Family and domain databases

    Gene3Di 2.60.120.20. 3 hits.
    InterProi IPR014872. Dicistrovirus_capsid-polyPr_C.
    IPR001676. Picornavirus_capsid.
    IPR029053. Viral_coat.
    IPR024343. VP4_dicistrovir.
    [Graphical view ]
    Pfami PF08762. CRPV_capsid. 1 hit.
    PF11492. Dicistro_VP4. 1 hit.
    PF00073. Rhv. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.

    Entry informationi

    Entry nameiPOLS_CRPVC
    AccessioniPrimary (citable) accession number: P13418
    Secondary accession number(s): Q9IJX3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: October 11, 2004
    Last modified: October 1, 2014
    This is version 75 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Caution

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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3