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P13418

- POLS_CRPVC

UniProt

P13418 - POLS_CRPVC

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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

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
Complete GO annotation...

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-KW
  2. viral capsid Source: UniProtKB-KW
Complete GO annotation...

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
ATFQDKQENS HIENEDKRLM SEQKEIVHFV SEGITPSTTA LPDIVNLSTN
60 70 80 90 100
YLDMTTREDR IHSIKDFLSG PIIIATNLWS SSDPVEKQLY TANFPEVLIS
110 120 130 140 150
NAMYQDKLKG FVGLRATLVV KVQVNSQPFQ QGRLMLQYIP YAQYMPNRVT
160 170 180 190 200
LINETLQGRS GCPTTDLELS VGTEVEMRIP YVSPHLYYNL ITGQGSFGSI
210 220 230 240 250
YVVVYSQLHD QVSGTGSIEY TVWAHLEDVD VQYPTGANIF TGNSPNYLSI
260 270 280 290 300
AERIATGDFT ETEMRKLWIH KTYLKRPARI YAQAAKELKQ LETNNSPSTA
310 320 330 340 350
LGQISEGLTT LSHIPVLGNI FSTPAWISAK AADLAKLFGF SKPTVQGKIG
360 370 380 390 400
ECKLRGQGRM ANFDGMDMSH KMALSSTNEI ETKEGLAGTS LDEMDLSRVL
410 420 430 440 450
SIPNYWDRFT WKTSDVTNTV LWDNYVSPFK VKPYSATITD RFRCTHMGYV
460 470 480 490 500
ANAFTYWRGS IVYTFKFVKT QYHSGRLRIS FIPYYYNTTI STGTPDVSRT
510 520 530 540 550
QKIVVDLRTS TEVSFTVPYI ASRPWLYCIR PESSWLSKDN KDGALMYNCV
560 570 580 590 600
SGIVRVEVLN QLVAAQNVFS EIDVICEVSG GPDLEFAGPT CPSYVPYAGD
610 620 630 640 650
LTLADTRKIE AERTQEYSNN EDNRITTQCS RIVAQVMGED QQIPRNEAQH
660 670 680 690 700
GVHPISIDTH RISNNWSPQA MCIGEKIVSI RQLIKRFGIF GDANTLQADG
710 720 730 740 750
SSFVVAPFTV TSPTKTLTST RNYTQFDYYY YLYAFWRGSM RIKMVAETQD
760 770 780 790 800
GTGTPRKKTN FTWFVRMFNS LQDSFNSLIS TSSSAVTTTV LPSGTINMGP
810 820 830 840 850
STQVIDPTVE GLIEVEVPYY NISHITPAVT IDDGTPSMED YLKGHSPPCL
860 870 880 890
LTFSPRDSIS ATNHHITASF MRAPGDDFSF MYLLEVPPLV NVARA
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 77 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