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Q66790

- POLG_EC16H

UniProt

Q66790 - POLG_EC16H

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Protein
Genome polyprotein
Gene
N/A
Organism
Echovirus 16 (strain Harrington)
Status
Reviewed - Annotation score: 4 out of 5 - Protein inferred from homologyi

Functioni

Protein VP1: Forms, together with VP2 and VP3, an icosahedral capsid (pseudo T=3), 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome. Protein VP1 mainly forms the vertices of the capsid. VP1 interacts with host cell receptor to provide virion attachment to target cell. After binding to its receptor, the capsid undergoes conformational changes. VP1 N-terminus (that contains an amphipathic alpha-helix) is externalized, VP4 is released and together, they shape a virion-cell connecting channel and a pore in the host membrane through which RNase-protected transfer of the viral genome takes place. After genome has been released, the channel shrinks By similarity.
Protein VP2: Forms, together with VP1 and VP3, an icosahedral capsid (pseudo T=3), 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome By similarity.
Protein VP3: Forms, together with VP1 and VP2, an icosahedral capsid (pseudo T=3), 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome By similarity.
Protein VP4: Lies on the inner surface of the capsid shell. After binding to the host receptor, the capsid undergoes conformational changes. VP4 is released, VP1 N-terminus is externalized, and together, they shape a virion-cell connecting channel and a pore in the host membrane through which RNase-protected transfer of the viral genome takes place. After genome has been released, the channel shrinks By similarity.
Protein VP0: Protein VP0: VP0 precursor is a component of immature procapsids, which gives rise to VP4 and VP2 after maturation. Allows the capsid to remain inactive before the maturation step By similarity.
Protease 2A: cysteine protease that is responsible for the cleavage between the P1 and P2 regions. It cleaves the host translation initiation factor EIF4G1, in order to shut off the capped cellular mRNA transcription By similarity.

Catalytic activityi

Selective cleavage of Tyr-|-Gly bond in the picornavirus polyprotein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei69 – 702Cleavage Reviewed prediction
Sitei331 – 3322Cleavage; by protease 3C Reviewed prediction
Sitei854 – 8552Cleavage; by protease 2A Reviewed prediction

GO - Molecular functioni

  1. cysteine-type peptidase activity Source: UniProtKB-KW
  2. structural molecule activity Source: InterPro
  3. transferase activity Source: UniProtKB-KW

GO - Biological processi

  1. pore-mediated entry of viral genome into host cell Source: UniProtKB-KW
  2. suppression by virus of host translation Source: UniProtKB-KW
  3. virion attachment to host cell Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease, Transferase

Keywords - Biological processi

Eukaryotic host gene expression shutoff by virus, Eukaryotic host translation shutoff by virus, Host gene expression shutoff by virus, Host-virus interaction, Pore-mediated penetration of viral genome into host cell, Viral attachment to host cell, Viral penetration into host cytoplasm, Virus entry into host cell

Names & Taxonomyi

Protein namesi
Recommended name:
Genome polyprotein
Cleaved into the following 6 chains:
Alternative name(s):
VP4-VP2
Alternative name(s):
P1A
Virion protein 4
Alternative name(s):
P1B
Virion protein 2
Alternative name(s):
P1C
Virion protein 3
Alternative name(s):
P1D
Virion protein 1
Protease 2A (EC:3.4.22.29)
Short name:
P2A
Alternative name(s):
Protein 2A
OrganismiEchovirus 16 (strain Harrington)
Taxonomic identifieri103910 [NCBI]
Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeEnterovirusEnterovirus B
Virus hostiHomo sapiens (Human) [TaxID: 9606]

Subcellular locationi

Chain Protein VP2 : Virion. Host cytoplasm Reviewed prediction
Chain Protein VP3 : Virion. Host cytoplasm Reviewed prediction
Chain Protein VP1 : Virion. Host cytoplasm Reviewed prediction

GO - Cellular componenti

  1. host cell cytoplasm Source: UniProtKB-SubCell
  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
Initiator methioninei1 – 11Removed; by host By similarity
Chaini2 – 331330Protein VP0 Reviewed prediction
PRO_0000311060Add
BLAST
Chaini2 – 6968Protein VP4 Reviewed prediction
PRO_0000039725Add
BLAST
Chaini70 – 331262Protein VP2 Reviewed prediction
PRO_0000039726Add
BLAST
Chaini332 – 570239Protein VP3 Reviewed prediction
PRO_0000039727Add
BLAST
Chaini571 – 854284Protein VP1 Reviewed prediction
PRO_0000039728Add
BLAST
Chaini855 – ›862›8Protease 2A Reviewed prediction
PRO_0000039729

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine; by host By similarity

Post-translational modificationi

Specific enzymatic cleavages in vivo by the viral proteases yield a variety of precursors and mature proteins. Polyprotein processing intermediates such as VP0 which is a VP4-VP2 precursor are produced. During virion maturation, non-infectious particles are rendered infectious following cleavage of VP0. This maturation cleavage is followed by a conformational change of the particle By similarity.
Myristoylation of VP4 is required during RNA encapsidation and formation of the mature virus particle By similarity.

Keywords - PTMi

Lipoprotein, Myristate

Structurei

3D structure databases

ProteinModelPortaliQ66790.
SMRiQ66790. Positions 2-69, 79-328, 332-853.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di2.60.120.20. 3 hits.
4.10.80.10. 2 hits.
InterProiIPR003138. Pico_P1A.
IPR001676. Picornavirus_capsid.
IPR029053. Viral_coat.
[Graphical view]
PfamiPF02226. Pico_P1A. 1 hit.
PF00073. Rhv. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

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

Q66790-1 [UniParc]FASTAAdd to Basket

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MGAQVSTQKT GAHETLLEAA QGATINYTNI NYYKDAASNS ANRQDFSQDP    50
SKFTEPVKDI MIKSMPALNS PSAEECGYSD RVRSITLGNS TITTQESANV 100
VVAYGRWPKY LEDDQATAED QPTQPDVATC RFYTLESVQW EANSAGWWWK 150
FPEALKDMGL FGQNMYYHYL GRAGYTIHVQ CNASKFHQGC LLVVCVPEAE 200
MGCAKPDENV DATNLTNGEN TCELTAGAAP AEKGKVQTAV CNATMGVAVG 250
NLTIFPHQWI NLRTNNCATI VMPYINSVPM DNMFRHYNFT LMVIPFVPLT 300
SMGGSTYVPI TVTIAPMCAE YNGLRLSTQH QGLPVMNVPG SNQFLTSDNF 350
QSPCAMPEYD VTPPLDIPGE VNNLMEVAEV DSVVPVNNLS DNVKTIKAYQ 400
IPVSAGDSSR PEAVFKFQLD PGSGSVLKHT LLGEIINYYA HWSGSIKLTF 450
VFCGSAMATG KLLIAYSPPG ASAPATRKDA MLGTHIIWDL GLQSSCVLCV 500
PWISQTHYRM VERDEYTTAG YISCWYQTNI IVPPDTPSQC YMLCLASACN 550
DFSVRMLKDT PFIQQEAKLQ GEPGKAIESA ISRVADTISS GPTNSEQVPA 600
LTAAETGHTS QVVPGDTIQT RHVKNYHSRS ESTIENFLCR SACVHIARYE 650
AGANASNEDR FVRWEINNKE LVQLRRKCEM FTYLRYDVEV TFVITSQQDQ 700
GTDLSQDMPV LTHQVMYVPP GGSVTKQGDS YAWQTSTNPS VFWTEGNAPP 750
RMSIPFISIG NAYSSFYDGW SHFSQKGVYG YNTLNKMGTL FVRHVNKETP 800
KPVTSTVRVY FKPKHIRAWI PRPPRLCPYK YKANVNFDVT AITDSRLTIT 850
TVPQVEHNLR TA 862
Length:862
Mass (Da):95,399
Last modified:January 23, 2007 - v3
Checksum:i59587E197126595C
GO

Non-terminal residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei862 – 8621

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X89545 Genomic RNA. Translation: CAA61723.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X89545 Genomic RNA. Translation: CAA61723.1 .

3D structure databases

ProteinModelPortali Q66790.
SMRi Q66790. Positions 2-69, 79-328, 332-853.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 2.60.120.20. 3 hits.
4.10.80.10. 2 hits.
InterProi IPR003138. Pico_P1A.
IPR001676. Picornavirus_capsid.
IPR029053. Viral_coat.
[Graphical view ]
Pfami PF02226. Pico_P1A. 1 hit.
PF00073. Rhv. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "The major echovirus group is genetically coherent and related to coxsackie B viruses."
    Huttunen P., Santti J., Pulli T., Hyypiae T.
    J. Gen. Virol. 77:715-725(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

Entry informationi

Entry nameiPOLG_EC16H
AccessioniPrimary (citable) accession number: Q66790
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 86 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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