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Protein

Genome polyprotein

Gene
N/A
Organism
Human rhinovirus 14 (HRV-14)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Capsid protein VP1: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome. Capsid protein VP1 mainly forms the vertices of the capsid. Capsid protein VP1 interacts with host ICAM1 to provide virion attachment to target host cells. This attachment induces virion internalization. Tyrosine kinases are probably involved in the entry process. After binding to its receptor, the capsid undergoes conformational changes. Capsid protein VP1 N-terminus (that contains an amphipathic alpha-helix) and capsid protein VP4 are externalized. Together, they shape a pore in the host membrane through which viral genome is translocated to host cell cytoplasm. After genome has been released, the channel shrinks (By similarity).By similarity
Capsid protein VP2: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity).By similarity
Capsid protein VP3: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity).By similarity
Capsid protein VP4: Lies on the inner surface of the capsid shell. After binding to the host receptor, the capsid undergoes conformational changes. Capsid protein VP4 is released, Capsid protein VP1 N-terminus is externalized, and together, they shape a pore in the host membrane through which the viral genome is translocated into the host cell cytoplasm. After genome has been released, the channel shrinks (By similarity).By similarity
Capsid protein VP0: Component of immature procapsids, which is cleaved into capsid proteins VP4 and VP2 after maturation. Allows the capsid to remain inactive before the maturation step (By similarity).By similarity
Protein 2A: Cysteine protease that cleaves viral polyprotein and specific host proteins. It is responsible for the cleavage between the P1 and P2 regions, first cleavage occurring in the polyprotein. Cleaves also the host translation initiation factor EIF4G1, in order to shut down the capped cellular mRNA translation. Inhibits the host nucleus-cytoplasm protein and RNA trafficking by cleaving host members of the nuclear pores (By similarity).By similarity
Protein 2B: Plays an essential role in the virus replication cycle by acting as a viroporin. Creates a pore in the host reticulum endoplasmic and as a consequence releases Ca2+ in the cytoplasm of infected cell. In turn, high levels of cyctoplasmic calcium may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication (By similarity).By similarity
Protein 2C: Induces and associates with structural rearrangements of intracellular membranes. Displays RNA-binding, nucleotide binding and NTPase activities. May play a role in virion morphogenesis and viral RNA encapsidation by interacting with the capsid protein VP3 (By similarity).By similarity
Protein 3AB: Localizes the viral replication complex to the surface of membranous vesicles. Together with protein 3CD binds the Cis-Active RNA Element (CRE) which is involved in RNA synthesis initiation. Acts as a cofactor to stimulate the activity of 3D polymerase, maybe through a nucleid acid chaperone activity (By similarity).By similarity
Protein 3A: Localizes the viral replication complex to the surface of membranous vesicles. It inhibits host cell endoplasmic reticulum-to-Golgi apparatus transport and causes the dissassembly of the Golgi complex, possibly through GBF1 interaction. This would result in depletion of MHC, trail receptors and IFN receptors at the host cell surface (By similarity).By similarity
Viral protein genome-linked: acts as a primer for viral RNA replication and remains covalently bound to viral genomic RNA. VPg is uridylylated prior to priming replication into VPg-pUpU. The oriI viral genomic sequence may act as a template for this. The VPg-pUpU is then used as primer on the genomic RNA poly(A) by the RNA-dependent RNA polymerase to replicate the viral genome. VPg may be removed in the cytoplasm by an unknown enzyme termed "unlinkase". VPg is not cleaved off virion genomes because replicated genomic RNA are encapsidated at the site of replication (By similarity).By similarity
Protein 3CD: Is involved in the viral replication complex and viral polypeptide maturation. It exhibits protease activity with a specificity and catalytic efficiency that is different from protease 3C. Protein 3CD lacks polymerase activity. The 3C domain in the context of protein 3CD may have an RNA binding activity (By similarity).By similarity
Protease 3C: cleaves host DDX58/RIG-I and thus contributes to the inhibition of type I interferon production. Cleaves also host PABPC1 (By similarity).By similarity
RNA-directed RNA polymerase: Replicates the viral genomic RNA on the surface of intracellular membranes. May form linear arrays of subunits that propagate along a strong head-to-tail interaction called interface-I. Covalently attaches UMP to a tyrosine of VPg, which is used to prime RNA synthesis. The positive stranded RNA genome is first replicated at virus induced membranous vesicles, creating a dsRNA genomic replication form. This dsRNA is then used as template to synthesize positive stranded RNA genomes. ss+RNA genomes are either translated, replicated or encapsidated (By similarity).PROSITE-ProRule annotation

Catalytic activityi

Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).PROSITE-ProRule annotation
Selective cleavage of Tyr-|-Gly bond in the picornavirus polyprotein.
Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.
NTP + H2O = NDP + phosphate.

Enzyme regulationi

RNA-directed RNA polymerase: replication or transcription is subject to high level of random mutations by the nucleotide analog ribavirin.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei876For Protease 2A activityBy similarity1
Active sitei894For Protease 2A activityBy similarity1
Active sitei965For Protease 2A activityBy similarity1
Active sitei1577For Protease 3C activitySequence analysis1
Active sitei1608For Protease 3C activitySequence analysis1
Active sitei1683For Protease 3C activityBy similarity1
Active sitei2046For RdRp activityBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase, Ion channel, Nucleotidyltransferase, Protease, RNA-directed RNA polymerase, Thiol protease, Transferase, Viral ion channel

Keywords - Biological processi

Activation of host autophagy by virus, DNA replication, Eukaryotic host gene expression shutoff by virus, Eukaryotic host translation shutoff by virus, Host gene expression shutoff by virus, Host mRNA suppression by virus, Host-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host mRNA nuclear export by virus, Inhibition of host RIG-I by virus, Inhibition of host RLR pathway by virus, Ion transport, Pore-mediated penetration of viral genome into host cell, Transport, Viral attachment to host cell, Viral immunoevasion, Viral penetration into host cytoplasm, Viral penetration via lysis of host organellar membrane, Viral RNA replication, Virus endocytosis by host, Virus entry into host cell

Keywords - Ligandi

ATP-binding, Nucleotide-binding, RNA-binding

Protein family/group databases

MEROPSiN08.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Genome polyprotein
Cleaved into the following 17 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):
Picornain 2A
Protein 2A
Protein 2B
Short name:
P2B
Protein 2C (EC:3.6.1.15)
Short name:
P2C
Protein 3A
Short name:
P3A
Alternative name(s):
Protein 3B
Short name:
P3B
Protease 3C (EC:3.4.22.28)
Short name:
P3C
Alternative name(s):
3D polymerase
Short name:
3Dpol
Protein 3D
Short name:
3D
OrganismiHuman rhinovirus 14 (HRV-14)
Taxonomic identifieri12131 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeEnterovirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000007679 Componenti: Genome

Subcellular locationi

Capsid protein VP0 :
Capsid protein VP4 :
Capsid protein VP2 :
Capsid protein VP3 :
Capsid protein VP1 :
Protein 2B :
Protein 2C :
Protein 3A :
Protein 3AB :
Protease 3C :
Protein 3CD :
RNA-directed RNA polymerase :

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini2 – 1491CytoplasmicSequence analysisAdd BLAST1490
Intramembranei1492 – 1507Sequence analysisAdd BLAST16
Topological domaini1508 – 2179CytoplasmicSequence analysisAdd BLAST672

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Capsid protein, Host cytoplasm, Host cytoplasmic vesicle, Host membrane, Membrane, T=pseudo3 icosahedral capsid protein, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved; by hostBy similarity
ChainiPRO_00004265362 – 2179Genome polyproteinBy similarityAdd BLAST2178
ChainiPRO_00004265372 – 856P1By similarityAdd BLAST855
ChainiPRO_00004265382 – 331Capsid protein VP0Sequence analysisAdd BLAST330
ChainiPRO_00004265392 – 69Capsid protein VP4Sequence analysisAdd BLAST68
ChainiPRO_000042654070 – 331Capsid protein VP2Sequence analysisAdd BLAST262
ChainiPRO_0000426541332 – 563Capsid protein VP3Sequence analysisAdd BLAST232
ChainiPRO_0000426542564 – 858Capsid protein VP1Sequence analysisAdd BLAST295
ChainiPRO_0000426543859 – 1429P2By similarityAdd BLAST571
ChainiPRO_0000040029859 – 1002Protease 2ASequence analysisAdd BLAST144
ChainiPRO_00000400301003 – 1099Protein 2BSequence analysisAdd BLAST97
ChainiPRO_00004265441101 – 1429Protein 2CSequence analysisAdd BLAST329
ChainiPRO_00004265451430 – 2179P3By similarityAdd BLAST750
ChainiPRO_00004265461430 – 1537Protein 3ABSequence analysisAdd BLAST108
ChainiPRO_00000400321430 – 1514Protein 3ASequence analysisAdd BLAST85
ChainiPRO_00004265471515 – 1537Viral protein genome-linkedSequence analysisAdd BLAST23
ChainiPRO_00004265481538 – 2179Protein 3CDSequence analysisAdd BLAST642
ChainiPRO_00004265491538 – 1718Protease 3CSequence analysisAdd BLAST181
ChainiPRO_00004265501719 – 2179RNA-directed RNA polymeraseBy similarityAdd BLAST461

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi2N-myristoyl glycine; by hostBy similarity1
Modified residuei1517O-(5'-phospho-RNA)-tyrosineBy similarity1

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).By similarity
VPg is uridylylated by the polymerase and is covalently linked to the 5'-end of genomic RNA. This uridylylated form acts as a nucleotide-peptide primer for the polymerase (By similarity).By similarity
Myristoylation of VP4 is required during RNA encapsidation and formation of the mature virus particle.By similarity
Capsid protein VP0: Myristoylation is required for the formation of pentamers during virus assembly. Further assembly of 12 pentamers and a molecule of genomic RNA generates the provirion (By similarity).By similarity
Genome polyprotein: Specific enzymatic cleavages in vivo by the viral proteases yield processing intermediates and the mature proteins.By similarity
Capsid protein VP0: During virion maturation, immature virions are rendered infectious following cleavage of VP0 into VP4 and VP2. This maturation seems to be an autocatalytic event triggered by the presence of RNA in the capsid and it is followed by a conformational change infectious virion (By similarity).By similarity
Viral protein genome-linked: VPg is uridylylated by the polymerase into VPg-pUpU. This acts as a nucleotide-peptide primer for the genomic RNA replication (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei69 – 70Cleavage; by autolysisSequence analysis2
Sitei331 – 332Cleavage; by Protease 3CSequence analysis2
Sitei858 – 859Cleavage; by Protease 2ASequence analysis2
Sitei1002 – 1003Cleavage; by Protease 3CSequence analysis2
Sitei1429 – 1430Cleavage; by Protease 3CSequence analysis2
Sitei1514 – 1515Cleavage; by Protease 3CSequence analysis2
Sitei1537 – 1538Cleavage; by Protease 3CSequence analysis2
Sitei1719 – 1720Cleavage; by Protease 3CSequence analysis2

Keywords - PTMi

Covalent protein-RNA linkage, Lipoprotein, Myristate, Phosphoprotein

Interactioni

Subunit structurei

Capsid protein VP1: Interacts with capsid protein VP0, and capsid protein VP3 to form heterotrimeric protomers. Five protomers subsequently associate to form pentamers which serve as building blocks for the capsid. Interacts with capsid protein VP4 in the mature capsid (By similarity). Interacts with host ICAM1. Capsid protein VP0: interacts with capsid protein VP1 and capsid protein VP3 to form heterotrimeric protomers. Five protomers subsequently associate to form pentamers which serve as building blocks for the capsid. Capsid protein VP2: Interacts with capsid protein VP1 and capsid protein VP3 in the mature capsid (By similarity). Capsid protein VP3: interacts with capsid protein VP0 and capsid protein VP1 to form heterotrimeric protomers. Five protomers subsequently associate to form pentamers which serve as building blocks for the capsid. Interacts with capsid protein VP4 in the mature capsid (By similarity). Capsid protein VP4: Interacts with capsid protein VP1 and capsid protein VP3 (By similarity). Protein 2C: interacts with capsid protein VP3; this interaction may be important for virion morphogenesis (By similarity). Protein 3AB: interacts with protein 3CD (By similarity). Viral protein genome-linked: interacts with RNA-directed RNA polymerase (By similarity). Protein 3CD: interacts with protein 3AB and with RNA-directed RNA polymerase. RNA-directed RNA polymerase: interacts with viral protein genome-linked and with protein 3CD (By similarity).By similarity

Structurei

Secondary structure

12179
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi33 – 35Combined sources3
Helixi36 – 38Combined sources3
Helixi51 – 54Combined sources4
Beta strandi57 – 59Combined sources3
Beta strandi83 – 87Combined sources5
Beta strandi90 – 96Combined sources7
Helixi103 – 105Combined sources3
Helixi113 – 115Combined sources3
Helixi126 – 128Combined sources3
Beta strandi138 – 141Combined sources4
Beta strandi147 – 151Combined sources5
Helixi153 – 155Combined sources3
Helixi159 – 167Combined sources9
Beta strandi168 – 180Combined sources13
Beta strandi188 – 197Combined sources10
Helixi213 – 216Combined sources4
Helixi219 – 221Combined sources3
Helixi225 – 227Combined sources3
Helixi238 – 240Combined sources3
Turni241 – 243Combined sources3
Helixi247 – 252Combined sources6
Beta strandi253 – 259Combined sources7
Turni260 – 262Combined sources3
Beta strandi264 – 270Combined sources7
Beta strandi275 – 279Combined sources5
Beta strandi281 – 284Combined sources4
Beta strandi287 – 298Combined sources12
Beta strandi305 – 323Combined sources19
Turni339 – 342Combined sources4
Beta strandi354 – 356Combined sources3
Helixi374 – 377Combined sources4
Turni386 – 389Combined sources4
Beta strandi390 – 392Combined sources3
Helixi395 – 398Combined sources4
Beta strandi399 – 402Combined sources4
Beta strandi410 – 415Combined sources6
Helixi421 – 425Combined sources5
Helixi427 – 432Combined sources6
Beta strandi435 – 440Combined sources6
Beta strandi442 – 448Combined sources7
Beta strandi457 – 463Combined sources7
Helixi473 – 477Combined sources5
Beta strandi479 – 485Combined sources7
Beta strandi487 – 489Combined sources3
Beta strandi491 – 496Combined sources6
Beta strandi501 – 503Combined sources3
Beta strandi505 – 508Combined sources4
Beta strandi509 – 512Combined sources4
Beta strandi517 – 524Combined sources8
Beta strandi536 – 544Combined sources9
Beta strandi549 – 553Combined sources5
Helixi580 – 582Combined sources3
Beta strandi585 – 587Combined sources3
Helixi604 – 606Combined sources3
Helixi614 – 616Combined sources3
Helixi630 – 632Combined sources3
Helixi634 – 637Combined sources4
Beta strandi642 – 651Combined sources10
Turni660 – 664Combined sources5
Beta strandi665 – 670Combined sources6
Beta strandi673 – 676Combined sources4
Helixi677 – 683Combined sources7
Beta strandi686 – 702Combined sources17
Beta strandi714 – 720Combined sources7
Beta strandi722 – 724Combined sources3
Beta strandi729 – 731Combined sources3
Helixi733 – 736Combined sources4
Beta strandi738 – 740Combined sources3
Beta strandi742 – 746Combined sources5
Beta strandi749 – 755Combined sources7
Beta strandi760 – 766Combined sources7
Beta strandi772 – 774Combined sources3
Beta strandi776 – 778Combined sources3
Helixi782 – 784Combined sources3
Beta strandi790 – 795Combined sources6
Beta strandi804 – 822Combined sources19
Beta strandi832 – 834Combined sources3
Helixi1539 – 1551Combined sources13
Beta strandi1552 – 1557Combined sources6
Beta strandi1560 – 1569Combined sources10
Beta strandi1571 – 1576Combined sources6
Beta strandi1582 – 1586Combined sources5
Beta strandi1589 – 1592Combined sources4
Beta strandi1594 – 1601Combined sources8
Turni1602 – 1604Combined sources3
Beta strandi1605 – 1613Combined sources9
Helixi1623 – 1625Combined sources3
Beta strandi1634 – 1644Combined sources11
Beta strandi1646 – 1663Combined sources18
Beta strandi1666 – 1676Combined sources11
Beta strandi1686 – 1689Combined sources4
Beta strandi1692 – 1701Combined sources10
Beta strandi1704 – 1709Combined sources6
Helixi1712 – 1716Combined sources5
Beta strandi1721 – 1726Combined sources6
Helixi1728 – 1731Combined sources4
Helixi1748 – 1750Combined sources3
Helixi1773 – 1778Combined sources6
Helixi1791 – 1805Combined sources15
Helixi1816 – 1821Combined sources6
Beta strandi1824 – 1826Combined sources3
Helixi1839 – 1842Combined sources4
Helixi1846 – 1849Combined sources4
Turni1852 – 1855Combined sources4
Helixi1858 – 1867Combined sources10
Beta strandi1873 – 1877Combined sources5
Helixi1884 – 1888Combined sources5
Beta strandi1894 – 1897Combined sources4
Helixi1900 – 1906Combined sources7
Turni1907 – 1909Combined sources3
Helixi1911 – 1919Combined sources9
Turni1923 – 1926Combined sources4
Helixi1933 – 1936Combined sources4
Helixi1937 – 1939Combined sources3
Helixi1940 – 1943Combined sources4
Beta strandi1949 – 1955Combined sources7
Helixi1957 – 1959Combined sources3
Helixi1962 – 1975Combined sources14
Turni1978 – 1981Combined sources4
Helixi1982 – 1987Combined sources6
Beta strandi1988 – 1992Combined sources5
Beta strandi1994 – 2002Combined sources9
Beta strandi2008 – 2010Combined sources3
Helixi2011 – 2030Combined sources20
Helixi2036 – 2038Combined sources3
Beta strandi2040 – 2044Combined sources5
Beta strandi2047 – 2051Combined sources5
Helixi2058 – 2065Combined sources8
Turni2066 – 2069Combined sources4
Turni2086 – 2088Combined sources3
Beta strandi2094 – 2098Combined sources5
Beta strandi2100 – 2102Combined sources3
Beta strandi2105 – 2109Combined sources5
Helixi2112 – 2119Combined sources8
Beta strandi2121 – 2124Combined sources4
Turni2125 – 2127Combined sources3
Helixi2128 – 2139Combined sources12
Helixi2140 – 2142Combined sources3
Helixi2144 – 2154Combined sources11
Helixi2158 – 2162Combined sources5
Helixi2168 – 2177Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1D3Ielectron microscopy26.001568-856[»]
270-331[»]
3332-567[»]
42-69[»]
1HRIX-ray3.001568-856[»]
270-331[»]
3332-567[»]
42-69[»]
1HRVX-ray3.001568-856[»]
270-331[»]
3332-567[»]
42-69[»]
1K5MX-ray2.70A568-856[»]
B70-331[»]
C332-567[»]
D2-69[»]
1NA1X-ray3.30A568-856[»]
B70-331[»]
C332-567[»]
D2-69[»]
1NCQX-ray2.50A568-856[»]
B70-331[»]
C332-567[»]
D2-69[»]
1R08X-ray3.001568-856[»]
270-331[»]
3332-567[»]
42-69[»]
1R09X-ray2.901568-856[»]
270-331[»]
3332-567[»]
42-69[»]
1RMUX-ray3.001568-856[»]
270-331[»]
3332-567[»]
42-69[»]
1RUCX-ray3.101568-856[»]
270-331[»]
3332-567[»]
42-69[»]
1RUDX-ray2.901568-856[»]
270-331[»]
3332-567[»]
42-69[»]
1RUEX-ray2.901568-856[»]
270-331[»]
3332-567[»]
42-69[»]
1RUFX-ray2.901568-856[»]
270-331[»]
3332-567[»]
42-69[»]
1RUGX-ray3.001568-856[»]
270-331[»]
3332-567[»]
42-69[»]
1RUHX-ray3.001568-856[»]
270-331[»]
3332-567[»]
42-69[»]
1RUIX-ray3.001568-856[»]
270-331[»]
3332-567[»]
42-69[»]
1RUJX-ray3.001568-856[»]
270-331[»]
3332-567[»]
42-69[»]
1RVFX-ray4.001568-856[»]
270-331[»]
3332-567[»]
42-69[»]
1VRHX-ray3.001568-856[»]
270-331[»]
3332-567[»]
42-69[»]
1XR5X-ray2.80A1720-2179[»]
2B0FNMR-A1538-1719[»]
2HWBX-ray3.001568-856[»]
270-331[»]
3332-567[»]
42-69[»]
2HWCX-ray3.001568-856[»]
270-331[»]
3332-567[»]
42-69[»]
2IN2NMR-A1538-1719[»]
2R04X-ray3.001568-856[»]
270-331[»]
3332-567[»]
42-69[»]
2R06X-ray3.001568-856[»]
270-331[»]
3332-567[»]
42-69[»]
2R07X-ray3.001568-856[»]
270-331[»]
3332-567[»]
42-69[»]
2RM2X-ray3.001568-856[»]
270-331[»]
3332-567[»]
42-69[»]
2RMUX-ray3.001568-856[»]
270-331[»]
3332-567[»]
42-69[»]
2RR1X-ray3.001568-856[»]
270-331[»]
3332-567[»]
42-69[»]
2RS1X-ray3.001568-856[»]
270-331[»]
3332-567[»]
42-69[»]
2RS3X-ray3.001568-856[»]
270-331[»]
3332-567[»]
42-69[»]
2RS5X-ray3.001568-856[»]
270-331[»]
3332-567[»]
42-69[»]
4PDWX-ray3.00A568-856[»]
B70-331[»]
C332-567[»]
4RHVX-ray3.001568-856[»]
270-331[»]
3332-567[»]
42-69[»]
ProteinModelPortaliP03303.
SMRiP03303.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03303.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1205 – 1361SF3 helicasePROSITE-ProRule annotationAdd BLAST157
Domaini1538 – 1702Peptidase C3Add BLAST165
Domaini1946 – 2060RdRp catalyticPROSITE-ProRule annotationAdd BLAST115

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni564 – 584Amphipatic alpha-helixSequence analysisAdd BLAST21
Regioni1430 – 1451DisorderedBy similarityAdd BLAST22

Sequence similaritiesi

Belongs to the picornaviruses polyprotein family.Curated
Contains 1 peptidase C3 domain.Curated
Contains 1 RdRp catalytic domain.PROSITE-ProRule annotation
Contains 1 SF3 helicase domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Family and domain databases

CDDicd00205. rhv_like. 3 hits.
Gene3Di2.60.120.20. 3 hits.
3.40.50.300. 1 hit.
4.10.80.10. 2 hits.
InterProiIPR003593. AAA+_ATPase.
IPR000605. Helicase_SF3_ssDNA/RNA_vir.
IPR014759. Helicase_SF3_ssRNA_vir.
IPR027417. P-loop_NTPase.
IPR014838. P3A.
IPR000081. Peptidase_C3.
IPR000199. Peptidase_C3A/C3B_picornavir.
IPR009003. Peptidase_S1_PA.
IPR003138. Pico_P1A.
IPR002527. Pico_P2B.
IPR001676. Picornavirus_capsid.
IPR033703. Rhv-like.
IPR001205. RNA-dir_pol_C.
IPR007094. RNA-dir_pol_PSvirus.
IPR029053. Viral_coat.
[Graphical view]
PfamiPF08727. P3A. 1 hit.
PF00548. Peptidase_C3. 1 hit.
PF02226. Pico_P1A. 1 hit.
PF00947. Pico_P2A. 1 hit.
PF01552. Pico_P2B. 1 hit.
PF00680. RdRP_1. 1 hit.
PF00073. Rhv. 3 hits.
PF00910. RNA_helicase. 1 hit.
[Graphical view]
ProDomiPD001306. Peptidase_C3. 1 hit.
PD649346. Pico_P2B. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 2 hits.
SSF52540. SSF52540. 1 hit.
SSF89043. SSF89043. 1 hit.
PROSITEiPS50507. RDRP_SSRNA_POS. 1 hit.
PS51218. SF3_HELICASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P03303-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGAQVSTQKS GSHENQNILT NGSNQTFTVI NYYKDAASTS SAGQSLSMDP
60 70 80 90 100
SKFTEPVKDL MLKGAPALNS PNVEACGYSD RVQQITLGNS TITTQEAANA
110 120 130 140 150
VVCYAEWPEY LPDVDASDVN KTSKPDTSVC RFYTLDSKTW TTGSKGWCWK
160 170 180 190 200
LPDALKDMGV FGQNMFFHSL GRSGYTVHVQ CNATKFHSGC LLVVVIPEHQ
210 220 230 240 250
LASHEGGNVS VKYTFTHPGE RGIDLSSANE VGGPVKDVIY NMNGTLLGNL
260 270 280 290 300
LIFPHQFINL RTNNTATIVI PYINSVPIDS MTRHNNVSLM VIPIAPLTVP
310 320 330 340 350
TGATPSLPIT VTIAPMCTEF SGIRSKSIVP QGLPTTTLPG SGQFLTTDDR
360 370 380 390 400
QSPSALPNYE PTPRIHIPGK VHNLLEIIQV DTLIPMNNTH TKDEVNSYLI
410 420 430 440 450
PLNANRQNEQ VFGTNLFIGD GVFKTTLLGE IVQYYTHWSG SLRFSLMYTG
460 470 480 490 500
PALSSAKLIL AYTPPGARGP QDRREAMLGT HVVWDIGLQS TIVMTIPWTS
510 520 530 540 550
GVQFRYTDPD TYTSAGFLSC WYQTSLILPP ETTGQVYLLS FISACPDFKL
560 570 580 590 600
RLMKDTQTIS QTVALTEGLG DELEEVIVEK TKQTVASISS GPKHTQKVPI
610 620 630 640 650
LTANETGATM PVLPSDSIET RTTYMHFNGS ETDVECFLGR AACVHVTEIQ
660 670 680 690 700
NKDATGIDNH REAKLFNDWK INLSSLVQLR KKLELFTYVR FDSEYTILAT
710 720 730 740 750
ASQPDSANYS SNLVVQAMYV PPGAPNPKEW DDYTWQSASN PSVFFKVGDT
760 770 780 790 800
SRFSVPYVGL ASAYNCFYDG YSHDDAETQY GITVLNHMGS MAFRIVNEHD
810 820 830 840 850
EHKTLVKIRV YHRAKHVEAW IPRAPRALPY TSIGRTNYPK NTEPVIKKRK
860 870 880 890 900
GDIKSYGLGP RYGGIYTSNV KIMNYHLMTP EDHHNLIAPY PNRDLAIVST
910 920 930 940 950
GGHGAETIPH CNCTSGVYYS TYYRKYYPII CEKPTNIWIE GNPYYPSRFQ
960 970 980 990 1000
AGVMKGVGPA EPGDCGGILR CIHGPIGLLT AGGSGYVCFA DIRQLECIAE
1010 1020 1030 1040 1050
EQGLSDYITG LGRAFGVGFT DQISTKVTEL QEVAKDFLTT KVLSKVVKMV
1060 1070 1080 1090 1100
SALVIICRNH DDLVTVTATL ALLGCDGSPW RFLKMYISKH FQVPYIERQA
1110 1120 1130 1140 1150
NDGWFRKFND ACNAAKGLEW IANKISKLIE WIKNKVLPQA KEKLEFCSKL
1160 1170 1180 1190 1200
KQLDILERQI TTMHISNPTQ EKREQLFNNV LWLEQMSQKF APLYAVESKR
1210 1220 1230 1240 1250
IRELKNKMVN YMQFKSKQRI EPVCVLIHGT PGSGKSLTTS IVGRAIAEHF
1260 1270 1280 1290 1300
NSAVYSLPPD PKHFDGYQQQ EVVIMDDLNQ NPDGQDISMF CQMVSSVDFL
1310 1320 1330 1340 1350
PPMASLDNKG MLFTSNFVLA STNSNTLSPP TILNPEALVR RFGFDLDICL
1360 1370 1380 1390 1400
HTTYTKNGKL NAGMSTKTCK DCHQPSNFKK CCPLVCGKAI SLVDRTTNIR
1410 1420 1430 1440 1450
YSVDQLVTAI ISDFKSKMQI TDSLETLFQG PVYKDLEIDV CNTPPPECIN
1460 1470 1480 1490 1500
DLLKSVDSEE IREYCKKKKW IIPEIPTNIE RAMNQASMII NTILMFVSTL
1510 1520 1530 1540 1550
GIVYVIYKLF AQTQGPYSGN PPHNKLKAPT LRPVVVQGPN TEFALSLLRK
1560 1570 1580 1590 1600
NIMTITTSKG EFTGLGIHDR VCVIPTHAQP GDDVLVNGQK IRVKDKYKLV
1610 1620 1630 1640 1650
DPENINLELT VLTLDRNEKF RDIRGFISED LEGVDATLVV HSNNFTNTIL
1660 1670 1680 1690 1700
EVGPVTMAGL INLSSTPTNR MIRYDYATKT GQCGGVLCAT GKIFGIHVGG
1710 1720 1730 1740 1750
NGRQGFSAQL KKQYFVEKQG QVIARHKVRE FNINPVNTPT KSKLHPSVFY
1760 1770 1780 1790 1800
DVFPGDKEPA VLSDNDPRLE VKLTESLFSK YKGNVNTEPT ENMLVAVDHY
1810 1820 1830 1840 1850
AGQLLSLDIP TSELTLKEAL YGVDGLEPID ITTSAGFPYV SLGIKKRDIL
1860 1870 1880 1890 1900
NKETQDTEKM KFYLDKYGID LPLVTYIKDE LRSVDKVRLG KSRLIEASSL
1910 1920 1930 1940 1950
NDSVNMRMKL GNLYKAFHQN PGVLTGSAVG CDPDVFWSVI PCLMDGHLMA
1960 1970 1980 1990 2000
FDYSNFDASL SPVWFVCLEK VLTKLGFAGS SLIQSICNTH HIFRDEIYVV
2010 2020 2030 2040 2050
EGGMPSGCSG TSIFNSMINN IIIRTLILDA YKGIDLDKLK ILAYGDDLIV
2060 2070 2080 2090 2100
SYPYELDPQV LATLGKNYGL TITPPDKSET FTKMTWENLT FLKRYFKPDQ
2110 2120 2130 2140 2150
QFPFLVHPVM PMKDIHESIR WTKDPKNTQD HVRSLCMLAW HSGEKEYNEF
2160 2170
IQKIRTTDIG KCLILPEYSV LRRRWLDLF
Length:2,179
Mass (Da):242,991
Last modified:January 23, 2007 - v3
Checksum:i827201A3032F0285
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti368P → L in AAA45756 (PubMed:2983312).Curated1
Sequence conflicti459I → T in AAA45756 (PubMed:2983312).Curated1
Sequence conflicti722P → H in AAA45756 (PubMed:2983312).Curated1
Sequence conflicti726 – 727NP → KS (PubMed:2983312).Curated2
Sequence conflicti729 – 731EWD → RVG (PubMed:2983312).Curated3
Sequence conflicti913C → R in AAA45756 (PubMed:2983312).Curated1
Sequence conflicti942N → S in AAA45756 (PubMed:2983312).Curated1
Sequence conflicti962P → L in AAA45756 (PubMed:2983312).Curated1
Sequence conflicti982G → E in AAA45756 (PubMed:2983312).Curated1
Sequence conflicti1193L → F in AAA45756 (PubMed:2983312).Curated1
Sequence conflicti1193L → H in AAA45758 (PubMed:8383233).Curated1
Sequence conflicti1220I → T (PubMed:8383233).Curated1
Sequence conflicti1220I → T (PubMed:2983312).Curated1
Sequence conflicti1399I → V (PubMed:8383233).Curated1
Sequence conflicti1399I → V (PubMed:2983312).Curated1
Sequence conflicti1446P → S in AAA45756 (PubMed:2983312).Curated1
Sequence conflicti1739P → A in AAA45756 (PubMed:2983312).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01087 Genomic RNA. Translation: CAA25565.1.
L05355 Genomic RNA. Translation: AAA45758.1.
K02121 Genomic RNA. Translation: AAA45756.1.
PIRiA03901. GNNYH4.
RefSeqiNP_041009.1. NC_001490.1.

Genome annotation databases

GeneIDi1461213.
KEGGivg:1461213.

Cross-referencesi

Web resourcesi

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure complexed with antiviral compound SCH 38057

Virus Particle ExploreR db

Icosahedral capsid structure complexed with antiviral compound SDZ 35-682

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01087 Genomic RNA. Translation: CAA25565.1.
L05355 Genomic RNA. Translation: AAA45758.1.
K02121 Genomic RNA. Translation: AAA45756.1.
PIRiA03901. GNNYH4.
RefSeqiNP_041009.1. NC_001490.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1D3Ielectron microscopy26.001568-856[»]
270-331[»]
3332-567[»]
42-69[»]
1HRIX-ray3.001568-856[»]
270-331[»]
3332-567[»]
42-69[»]
1HRVX-ray3.001568-856[»]
270-331[»]
3332-567[»]
42-69[»]
1K5MX-ray2.70A568-856[»]
B70-331[»]
C332-567[»]
D2-69[»]
1NA1X-ray3.30A568-856[»]
B70-331[»]
C332-567[»]
D2-69[»]
1NCQX-ray2.50A568-856[»]
B70-331[»]
C332-567[»]
D2-69[»]
1R08X-ray3.001568-856[»]
270-331[»]
3332-567[»]
42-69[»]
1R09X-ray2.901568-856[»]
270-331[»]
3332-567[»]
42-69[»]
1RMUX-ray3.001568-856[»]
270-331[»]
3332-567[»]
42-69[»]
1RUCX-ray3.101568-856[»]
270-331[»]
3332-567[»]
42-69[»]
1RUDX-ray2.901568-856[»]
270-331[»]
3332-567[»]
42-69[»]
1RUEX-ray2.901568-856[»]
270-331[»]
3332-567[»]
42-69[»]
1RUFX-ray2.901568-856[»]
270-331[»]
3332-567[»]
42-69[»]
1RUGX-ray3.001568-856[»]
270-331[»]
3332-567[»]
42-69[»]
1RUHX-ray3.001568-856[»]
270-331[»]
3332-567[»]
42-69[»]
1RUIX-ray3.001568-856[»]
270-331[»]
3332-567[»]
42-69[»]
1RUJX-ray3.001568-856[»]
270-331[»]
3332-567[»]
42-69[»]
1RVFX-ray4.001568-856[»]
270-331[»]
3332-567[»]
42-69[»]
1VRHX-ray3.001568-856[»]
270-331[»]
3332-567[»]
42-69[»]
1XR5X-ray2.80A1720-2179[»]
2B0FNMR-A1538-1719[»]
2HWBX-ray3.001568-856[»]
270-331[»]
3332-567[»]
42-69[»]
2HWCX-ray3.001568-856[»]
270-331[»]
3332-567[»]
42-69[»]
2IN2NMR-A1538-1719[»]
2R04X-ray3.001568-856[»]
270-331[»]
3332-567[»]
42-69[»]
2R06X-ray3.001568-856[»]
270-331[»]
3332-567[»]
42-69[»]
2R07X-ray3.001568-856[»]
270-331[»]
3332-567[»]
42-69[»]
2RM2X-ray3.001568-856[»]
270-331[»]
3332-567[»]
42-69[»]
2RMUX-ray3.001568-856[»]
270-331[»]
3332-567[»]
42-69[»]
2RR1X-ray3.001568-856[»]
270-331[»]
3332-567[»]
42-69[»]
2RS1X-ray3.001568-856[»]
270-331[»]
3332-567[»]
42-69[»]
2RS3X-ray3.001568-856[»]
270-331[»]
3332-567[»]
42-69[»]
2RS5X-ray3.001568-856[»]
270-331[»]
3332-567[»]
42-69[»]
4PDWX-ray3.00A568-856[»]
B70-331[»]
C332-567[»]
4RHVX-ray3.001568-856[»]
270-331[»]
3332-567[»]
42-69[»]
ProteinModelPortaliP03303.
SMRiP03303.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiN08.001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi1461213.
KEGGivg:1461213.

Miscellaneous databases

EvolutionaryTraceiP03303.

Family and domain databases

CDDicd00205. rhv_like. 3 hits.
Gene3Di2.60.120.20. 3 hits.
3.40.50.300. 1 hit.
4.10.80.10. 2 hits.
InterProiIPR003593. AAA+_ATPase.
IPR000605. Helicase_SF3_ssDNA/RNA_vir.
IPR014759. Helicase_SF3_ssRNA_vir.
IPR027417. P-loop_NTPase.
IPR014838. P3A.
IPR000081. Peptidase_C3.
IPR000199. Peptidase_C3A/C3B_picornavir.
IPR009003. Peptidase_S1_PA.
IPR003138. Pico_P1A.
IPR002527. Pico_P2B.
IPR001676. Picornavirus_capsid.
IPR033703. Rhv-like.
IPR001205. RNA-dir_pol_C.
IPR007094. RNA-dir_pol_PSvirus.
IPR029053. Viral_coat.
[Graphical view]
PfamiPF08727. P3A. 1 hit.
PF00548. Peptidase_C3. 1 hit.
PF02226. Pico_P1A. 1 hit.
PF00947. Pico_P2A. 1 hit.
PF01552. Pico_P2B. 1 hit.
PF00680. RdRP_1. 1 hit.
PF00073. Rhv. 3 hits.
PF00910. RNA_helicase. 1 hit.
[Graphical view]
ProDomiPD001306. Peptidase_C3. 1 hit.
PD649346. Pico_P2B. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 2 hits.
SSF52540. SSF52540. 1 hit.
SSF89043. SSF89043. 1 hit.
PROSITEiPS50507. RDRP_SSRNA_POS. 1 hit.
PS51218. SF3_HELICASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPOLG_HRV14
AccessioniPrimary (citable) accession number: P03303
Secondary accession number(s): Q82083
, Q82123, Q84736, Q84737, Q84738, Q84739, Q84740, Q84741, Q84774, Q84775, Q84776, Q84777, Q84778, Q84779, Q89441, Q89649, Q89763, Q89883
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 185 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Caution

The PDB data bank contains the 3D-structure coordinates of proteins VP1, VP2, VP3 and VP4.Curated

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. 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.