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P03303

- POLG_HRV14

UniProt

P03303 - POLG_HRV14

Protein

Genome polyprotein

Gene
N/A
Organism
Human rhinovirus 14 (HRV-14)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 171 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    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)LengthDescriptionGraphical viewFeature identifierActions
    Sitei69 – 702Cleavage; by autolysisSequence Analysis
    Sitei331 – 3322Cleavage; by Protease 3CSequence Analysis
    Sitei856 – 8572Cleavage; by Protease 2ASequence Analysis
    Active sitei876 – 8761For Protease 2A activityBy similarity
    Active sitei894 – 8941For Protease 2A activityBy similarity
    Active sitei965 – 9651For Protease 2A activityBy similarity
    Sitei1002 – 10032Cleavage; by Protease 3CSequence Analysis
    Sitei1429 – 14302Cleavage; by Protease 3CSequence Analysis
    Sitei1514 – 15152Cleavage; by Protease 3CSequence Analysis
    Sitei1537 – 15382Cleavage; by Protease 3CSequence Analysis
    Active sitei1577 – 15771For Protease 3C activitySequence Analysis
    Active sitei1608 – 16081For Protease 3C activitySequence Analysis
    Active sitei1683 – 16831For Protease 3C activityBy similarity
    Sitei1719 – 17202Cleavage; by Protease 3CSequence Analysis
    Active sitei2046 – 20461For RdRp activityBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. cysteine-type endopeptidase activity Source: InterPro
    3. ion channel activity Source: UniProtKB-KW
    4. RNA binding Source: UniProtKB-KW
    5. RNA-directed RNA polymerase activity Source: UniProtKB-KW
    6. RNA helicase activity Source: InterPro
    7. structural molecule activity Source: InterPro

    GO - Biological processi

    1. DNA replication Source: UniProtKB-KW
    2. endocytosis involved in viral entry into host cell Source: UniProtKB-KW
    3. induction by virus of host autophagy Source: UniProtKB
    4. lysis of host organelle involved in viral entry into host cell Source: UniProtKB-KW
    5. pore formation by virus in membrane of host cell Source: UniProtKB-KW
    6. pore-mediated entry of viral genome into host cell Source: UniProtKB-KW
    7. protein oligomerization Source: UniProtKB-KW
    8. RNA-protein covalent cross-linking Source: UniProtKB-KW
    9. suppression by virus of host gene expression Source: UniProtKB-KW
    10. suppression by virus of host mRNA export from nucleus Source: UniProtKB-KW
    11. suppression by virus of host RIG-I activity by RIG-I proteolysis Source: UniProtKB
    12. suppression by virus of host translation initiation factor activity Source: UniProtKB
    13. transcription, DNA-templated Source: InterPro
    14. viral RNA genome replication Source: InterPro
    15. virion attachment to host cell Source: UniProtKB-KW

    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

    MEROPSiC03.013.

    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 positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeEnterovirus
    Virus hostiHomo sapiens (Human) [TaxID: 9606]
    ProteomesiUP000007679: Genome

    Subcellular locationi

    Chain Capsid protein VP0 : Virion By similarity. Host cytoplasm By similarity
    Chain Capsid protein VP2 : Virion By similarity. Host cytoplasm By similarity
    Chain Capsid protein VP3 : Virion By similarity. Host cytoplasm By similarity
    Chain Capsid protein VP1 : Virion By similarity. Host cytoplasm By similarity
    Chain Protein 2B : Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated
    Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum.
    Chain Protein 2C : Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated
    Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum.
    Chain Protein 3A : Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated
    Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum.
    Chain Protein 3AB : Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated
    Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum.
    Chain Protein 3CD : Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated
    Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum.
    Chain RNA-directed RNA polymerase : Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated
    Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum.

    GO - Cellular componenti

    1. host cell cytoplasmic vesicle membrane Source: UniProtKB-SubCell
    2. integral to membrane of host cell Source: UniProtKB-KW
    3. membrane Source: UniProtKB-KW
    4. T=pseudo3 icosahedral viral capsid Source: UniProtKB-KW

    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)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed; by hostBy similarity
    Chaini2 – 21792178Genome polyproteinBy similarityPRO_0000426536Add
    BLAST
    Chaini2 – 856855P1By similarityPRO_0000426537Add
    BLAST
    Chaini2 – 331330Capsid protein VP0Sequence AnalysisPRO_0000426538Add
    BLAST
    Chaini2 – 6968Capsid protein VP4Sequence AnalysisPRO_0000426539Add
    BLAST
    Chaini70 – 331262Capsid protein VP2Sequence AnalysisPRO_0000426540Add
    BLAST
    Chaini332 – 563232Capsid protein VP3Sequence AnalysisPRO_0000426541Add
    BLAST
    Chaini564 – 856293Capsid protein VP1Sequence AnalysisPRO_0000426542Add
    BLAST
    Chaini857 – 1429573P2By similarityPRO_0000426543Add
    BLAST
    Chaini857 – 1002146Protease 2ASequence AnalysisPRO_0000040029Add
    BLAST
    Chaini1003 – 109997Protein 2BSequence AnalysisPRO_0000040030Add
    BLAST
    Chaini1101 – 1429329Protein 2CSequence AnalysisPRO_0000426544Add
    BLAST
    Chaini1430 – 2179750P3By similarityPRO_0000426545Add
    BLAST
    Chaini1430 – 1537108Protein 3ABSequence AnalysisPRO_0000426546Add
    BLAST
    Chaini1430 – 151485Protein 3ASequence AnalysisPRO_0000040032Add
    BLAST
    Chaini1515 – 153723Viral protein genome-linkedSequence AnalysisPRO_0000426547Add
    BLAST
    Chaini1538 – 2179642Protein 3CDSequence AnalysisPRO_0000426548Add
    BLAST
    Chaini1538 – 1718181Protease 3CSequence AnalysisPRO_0000426549Add
    BLAST
    Chaini1719 – 2179461RNA-directed RNA polymeraseBy similarityPRO_0000426550Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycine; by hostBy similarity
    Modified residuei1517 – 15171O-(5'-phospho-RNA)-tyrosineBy 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.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

    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. Interact 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

    1
    2179
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi33 – 353
    Helixi36 – 383
    Helixi51 – 544
    Beta strandi57 – 593
    Beta strandi83 – 875
    Beta strandi90 – 967
    Helixi103 – 1053
    Helixi113 – 1153
    Helixi126 – 1283
    Beta strandi138 – 1414
    Beta strandi147 – 1515
    Helixi153 – 1553
    Helixi159 – 1679
    Beta strandi168 – 18013
    Beta strandi188 – 19710
    Helixi213 – 2164
    Helixi219 – 2213
    Helixi225 – 2273
    Helixi238 – 2403
    Turni241 – 2433
    Helixi247 – 2526
    Beta strandi253 – 2597
    Turni260 – 2623
    Beta strandi264 – 2707
    Beta strandi275 – 2795
    Beta strandi281 – 2844
    Beta strandi287 – 29812
    Beta strandi305 – 32319
    Turni339 – 3424
    Beta strandi354 – 3563
    Helixi374 – 3774
    Turni386 – 3894
    Beta strandi390 – 3923
    Helixi395 – 3984
    Beta strandi399 – 4024
    Beta strandi410 – 4156
    Helixi421 – 4255
    Helixi427 – 4326
    Beta strandi435 – 4406
    Beta strandi442 – 4487
    Beta strandi457 – 4637
    Helixi473 – 4775
    Beta strandi479 – 4857
    Beta strandi487 – 4893
    Beta strandi491 – 4966
    Beta strandi501 – 5033
    Beta strandi505 – 5084
    Beta strandi509 – 5124
    Beta strandi517 – 5248
    Beta strandi536 – 5449
    Beta strandi549 – 5535
    Helixi580 – 5823
    Beta strandi585 – 5873
    Helixi604 – 6063
    Helixi614 – 6163
    Helixi630 – 6323
    Helixi634 – 6374
    Beta strandi642 – 65110
    Turni660 – 6645
    Beta strandi665 – 6706
    Beta strandi673 – 6764
    Helixi677 – 6837
    Beta strandi686 – 70217
    Beta strandi714 – 7207
    Beta strandi722 – 7243
    Beta strandi729 – 7313
    Helixi733 – 7364
    Beta strandi738 – 7403
    Beta strandi742 – 7465
    Beta strandi749 – 7557
    Beta strandi760 – 7667
    Beta strandi772 – 7743
    Beta strandi776 – 7783
    Helixi782 – 7843
    Beta strandi790 – 7956
    Beta strandi804 – 82219
    Beta strandi832 – 8343
    Helixi1539 – 155113
    Beta strandi1552 – 15576
    Beta strandi1560 – 156910
    Beta strandi1571 – 15766
    Beta strandi1582 – 15865
    Beta strandi1589 – 15924
    Beta strandi1594 – 16018
    Turni1602 – 16043
    Beta strandi1605 – 16139
    Helixi1623 – 16253
    Beta strandi1634 – 164411
    Beta strandi1646 – 166318
    Beta strandi1666 – 167611
    Beta strandi1686 – 16894
    Beta strandi1692 – 170110
    Beta strandi1704 – 17096
    Helixi1712 – 17165
    Beta strandi1721 – 17266
    Helixi1728 – 17314
    Helixi1748 – 17503
    Helixi1773 – 17786
    Helixi1791 – 180515
    Helixi1816 – 18216
    Beta strandi1824 – 18263
    Helixi1839 – 18424
    Helixi1846 – 18494
    Turni1852 – 18554
    Helixi1858 – 186710
    Beta strandi1873 – 18775
    Helixi1884 – 18885
    Beta strandi1894 – 18974
    Helixi1900 – 19067
    Turni1907 – 19093
    Helixi1911 – 19199
    Turni1923 – 19264
    Helixi1933 – 19364
    Helixi1937 – 19393
    Helixi1940 – 19434
    Beta strandi1949 – 19557
    Helixi1957 – 19593
    Helixi1962 – 197514
    Turni1978 – 19814
    Helixi1982 – 19876
    Beta strandi1988 – 19925
    Beta strandi1994 – 20029
    Beta strandi2008 – 20103
    Helixi2011 – 203020
    Helixi2036 – 20383
    Beta strandi2040 – 20445
    Beta strandi2047 – 20515
    Helixi2058 – 20658
    Turni2066 – 20694
    Turni2086 – 20883
    Beta strandi2094 – 20985
    Beta strandi2100 – 21023
    Beta strandi2105 – 21095
    Helixi2112 – 21198
    Beta strandi2121 – 21244
    Turni2125 – 21273
    Helixi2128 – 213912
    Helixi2140 – 21423
    Helixi2144 – 215411
    Helixi2158 – 21625
    Helixi2168 – 217710

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    4RHVX-ray3.001568-856[»]
    270-331[»]
    3332-567[»]
    42-69[»]
    ProteinModelPortaliP03303.
    SMRiP03303. Positions 2-69, 77-567, 574-856, 1429-1486, 1538-2179.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP03303.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini2 – 14911490CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1508 – 2179672CytoplasmicSequence AnalysisAdd
    BLAST

    Intramembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Intramembranei1492 – 150716Sequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1205 – 1361157SF3 helicasePROSITE-ProRule annotationAdd
    BLAST
    Domaini1538 – 1702165Peptidase C3Add
    BLAST
    Domaini1946 – 2060115RdRp catalyticPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni564 – 58421Amphipatic alpha-helixSequence AnalysisAdd
    BLAST
    Regioni1430 – 145122DisorderedBy similarityAdd
    BLAST

    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

    Gene3Di2.60.120.20. 3 hits.
    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.
    IPR003138. Pico_P1A.
    IPR002527. Pico_P2B.
    IPR001676. Picornavirus_capsid.
    IPR001205. RNA-dir_pol_C.
    IPR007094. RNA-dir_pol_PSvirus.
    IPR009003. Trypsin-like_Pept_dom.
    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

    MGAQVSTQKS GSHENQNILT NGSNQTFTVI NYYKDAASTS SAGQSLSMDP     50
    SKFTEPVKDL MLKGAPALNS PNVEACGYSD RVQQITLGNS TITTQEAANA 100
    VVCYAEWPEY LPDVDASDVN KTSKPDTSVC RFYTLDSKTW TTGSKGWCWK 150
    LPDALKDMGV FGQNMFFHSL GRSGYTVHVQ CNATKFHSGC LLVVVIPEHQ 200
    LASHEGGNVS VKYTFTHPGE RGIDLSSANE VGGPVKDVIY NMNGTLLGNL 250
    LIFPHQFINL RTNNTATIVI PYINSVPIDS MTRHNNVSLM VIPIAPLTVP 300
    TGATPSLPIT VTIAPMCTEF SGIRSKSIVP QGLPTTTLPG SGQFLTTDDR 350
    QSPSALPNYE PTPRIHIPGK VHNLLEIIQV DTLIPMNNTH TKDEVNSYLI 400
    PLNANRQNEQ VFGTNLFIGD GVFKTTLLGE IVQYYTHWSG SLRFSLMYTG 450
    PALSSAKLIL AYTPPGARGP QDRREAMLGT HVVWDIGLQS TIVMTIPWTS 500
    GVQFRYTDPD TYTSAGFLSC WYQTSLILPP ETTGQVYLLS FISACPDFKL 550
    RLMKDTQTIS QTVALTEGLG DELEEVIVEK TKQTVASISS GPKHTQKVPI 600
    LTANETGATM PVLPSDSIET RTTYMHFNGS ETDVECFLGR AACVHVTEIQ 650
    NKDATGIDNH REAKLFNDWK INLSSLVQLR KKLELFTYVR FDSEYTILAT 700
    ASQPDSANYS SNLVVQAMYV PPGAPNPKEW DDYTWQSASN PSVFFKVGDT 750
    SRFSVPYVGL ASAYNCFYDG YSHDDAETQY GITVLNHMGS MAFRIVNEHD 800
    EHKTLVKIRV YHRAKHVEAW IPRAPRALPY TSIGRTNYPK NTEPVIKKRK 850
    GDIKSYGLGP RYGGIYTSNV KIMNYHLMTP EDHHNLIAPY PNRDLAIVST 900
    GGHGAETIPH CNCTSGVYYS TYYRKYYPII CEKPTNIWIE GNPYYPSRFQ 950
    AGVMKGVGPA EPGDCGGILR CIHGPIGLLT AGGSGYVCFA DIRQLECIAE 1000
    EQGLSDYITG LGRAFGVGFT DQISTKVTEL QEVAKDFLTT KVLSKVVKMV 1050
    SALVIICRNH DDLVTVTATL ALLGCDGSPW RFLKMYISKH FQVPYIERQA 1100
    NDGWFRKFND ACNAAKGLEW IANKISKLIE WIKNKVLPQA KEKLEFCSKL 1150
    KQLDILERQI TTMHISNPTQ EKREQLFNNV LWLEQMSQKF APLYAVESKR 1200
    IRELKNKMVN YMQFKSKQRI EPVCVLIHGT PGSGKSLTTS IVGRAIAEHF 1250
    NSAVYSLPPD PKHFDGYQQQ EVVIMDDLNQ NPDGQDISMF CQMVSSVDFL 1300
    PPMASLDNKG MLFTSNFVLA STNSNTLSPP TILNPEALVR RFGFDLDICL 1350
    HTTYTKNGKL NAGMSTKTCK DCHQPSNFKK CCPLVCGKAI SLVDRTTNIR 1400
    YSVDQLVTAI ISDFKSKMQI TDSLETLFQG PVYKDLEIDV CNTPPPECIN 1450
    DLLKSVDSEE IREYCKKKKW IIPEIPTNIE RAMNQASMII NTILMFVSTL 1500
    GIVYVIYKLF AQTQGPYSGN PPHNKLKAPT LRPVVVQGPN TEFALSLLRK 1550
    NIMTITTSKG EFTGLGIHDR VCVIPTHAQP GDDVLVNGQK IRVKDKYKLV 1600
    DPENINLELT VLTLDRNEKF RDIRGFISED LEGVDATLVV HSNNFTNTIL 1650
    EVGPVTMAGL INLSSTPTNR MIRYDYATKT GQCGGVLCAT GKIFGIHVGG 1700
    NGRQGFSAQL KKQYFVEKQG QVIARHKVRE FNINPVNTPT KSKLHPSVFY 1750
    DVFPGDKEPA VLSDNDPRLE VKLTESLFSK YKGNVNTEPT ENMLVAVDHY 1800
    AGQLLSLDIP TSELTLKEAL YGVDGLEPID ITTSAGFPYV SLGIKKRDIL 1850
    NKETQDTEKM KFYLDKYGID LPLVTYIKDE LRSVDKVRLG KSRLIEASSL 1900
    NDSVNMRMKL GNLYKAFHQN PGVLTGSAVG CDPDVFWSVI PCLMDGHLMA 1950
    FDYSNFDASL SPVWFVCLEK VLTKLGFAGS SLIQSICNTH HIFRDEIYVV 2000
    EGGMPSGCSG TSIFNSMINN IIIRTLILDA YKGIDLDKLK ILAYGDDLIV 2050
    SYPYELDPQV LATLGKNYGL TITPPDKSET FTKMTWENLT FLKRYFKPDQ 2100
    QFPFLVHPVM PMKDIHESIR WTKDPKNTQD HVRSLCMLAW HSGEKEYNEF 2150
    IQKIRTTDIG KCLILPEYSV LRRRWLDLF 2179
    Length:2,179
    Mass (Da):242,991
    Last modified:January 23, 2007 - v3
    Checksum:i827201A3032F0285
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti368 – 3681P → L in AAA45756. (PubMed:2983312)Curated
    Sequence conflicti459 – 4591I → T in AAA45756. (PubMed:2983312)Curated
    Sequence conflicti722 – 7221P → H in AAA45756. (PubMed:2983312)Curated
    Sequence conflicti726 – 7272NP → KS(PubMed:2983312)Curated
    Sequence conflicti729 – 7313EWD → RVG(PubMed:2983312)Curated
    Sequence conflicti913 – 9131C → R in AAA45756. (PubMed:2983312)Curated
    Sequence conflicti942 – 9421N → S in AAA45756. (PubMed:2983312)Curated
    Sequence conflicti962 – 9621P → L in AAA45756. (PubMed:2983312)Curated
    Sequence conflicti982 – 9821G → E in AAA45756. (PubMed:2983312)Curated
    Sequence conflicti1193 – 11931L → F in AAA45756. (PubMed:2983312)Curated
    Sequence conflicti1193 – 11931L → H in AAA45758. (PubMed:8383233)Curated
    Sequence conflicti1220 – 12201I → T(PubMed:8383233)Curated
    Sequence conflicti1220 – 12201I → T(PubMed:2983312)Curated
    Sequence conflicti1399 – 13991I → V(PubMed:8383233)Curated
    Sequence conflicti1399 – 13991I → V(PubMed:2983312)Curated
    Sequence conflicti1446 – 14461P → S in AAA45756. (PubMed:2983312)Curated
    Sequence conflicti1739 – 17391P → A in AAA45756. (PubMed:2983312)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.

    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X01087 Genomic RNA. Translation: CAA25565.1 .
    L05355 Genomic RNA. Translation: AAA45758.1 .
    K02121 Genomic RNA. Translation: AAA45756.1 .
    PIRi A03901. GNNYH4.
    RefSeqi NP_041009.1. NC_001490.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1D3I electron microscopy 26.00 1 568-856 [» ]
    2 70-331 [» ]
    3 332-567 [» ]
    4 2-69 [» ]
    1HRI X-ray 3.00 1 568-856 [» ]
    2 70-331 [» ]
    3 332-567 [» ]
    4 2-69 [» ]
    1HRV X-ray 3.00 1 568-856 [» ]
    2 70-331 [» ]
    3 332-567 [» ]
    4 2-69 [» ]
    1K5M X-ray 2.70 A 568-856 [» ]
    B 70-331 [» ]
    C 332-567 [» ]
    D 2-69 [» ]
    1NA1 X-ray 3.30 A 568-856 [» ]
    B 70-331 [» ]
    C 332-567 [» ]
    D 2-69 [» ]
    1NCQ X-ray 2.50 A 568-856 [» ]
    B 70-331 [» ]
    C 332-567 [» ]
    D 2-69 [» ]
    1R08 X-ray 3.00 1 568-856 [» ]
    2 70-331 [» ]
    3 332-567 [» ]
    4 2-69 [» ]
    1R09 X-ray 2.90 1 568-856 [» ]
    2 70-331 [» ]
    3 332-567 [» ]
    4 2-69 [» ]
    1RMU X-ray 3.00 1 568-856 [» ]
    2 70-331 [» ]
    3 332-567 [» ]
    4 2-69 [» ]
    1RUC X-ray 3.10 1 568-856 [» ]
    2 70-331 [» ]
    3 332-567 [» ]
    4 2-69 [» ]
    1RUD X-ray 2.90 1 568-856 [» ]
    2 70-331 [» ]
    3 332-567 [» ]
    4 2-69 [» ]
    1RUE X-ray 2.90 1 568-856 [» ]
    2 70-331 [» ]
    3 332-567 [» ]
    4 2-69 [» ]
    1RUF X-ray 2.90 1 568-856 [» ]
    2 70-331 [» ]
    3 332-567 [» ]
    4 2-69 [» ]
    1RUG X-ray 3.00 1 568-856 [» ]
    2 70-331 [» ]
    3 332-567 [» ]
    4 2-69 [» ]
    1RUH X-ray 3.00 1 568-856 [» ]
    2 70-331 [» ]
    3 332-567 [» ]
    4 2-69 [» ]
    1RUI X-ray 3.00 1 568-856 [» ]
    2 70-331 [» ]
    3 332-567 [» ]
    4 2-69 [» ]
    1RUJ X-ray 3.00 1 568-856 [» ]
    2 70-331 [» ]
    3 332-567 [» ]
    4 2-69 [» ]
    1RVF X-ray 4.00 1 568-856 [» ]
    2 70-331 [» ]
    3 332-567 [» ]
    4 2-69 [» ]
    1VRH X-ray 3.00 1 568-856 [» ]
    2 70-331 [» ]
    3 332-567 [» ]
    4 2-69 [» ]
    1XR5 X-ray 2.80 A 1720-2179 [» ]
    2B0F NMR - A 1538-1719 [» ]
    2HWB X-ray 3.00 1 568-856 [» ]
    2 70-331 [» ]
    3 332-567 [» ]
    4 2-69 [» ]
    2HWC X-ray 3.00 1 568-856 [» ]
    2 70-331 [» ]
    3 332-567 [» ]
    4 2-69 [» ]
    2IN2 NMR - A 1538-1719 [» ]
    2R04 X-ray 3.00 1 568-856 [» ]
    2 70-331 [» ]
    3 332-567 [» ]
    4 2-69 [» ]
    2R06 X-ray 3.00 1 568-856 [» ]
    2 70-331 [» ]
    3 332-567 [» ]
    4 2-69 [» ]
    2R07 X-ray 3.00 1 568-856 [» ]
    2 70-331 [» ]
    3 332-567 [» ]
    4 2-69 [» ]
    2RM2 X-ray 3.00 1 568-856 [» ]
    2 70-331 [» ]
    3 332-567 [» ]
    4 2-69 [» ]
    2RMU X-ray 3.00 1 568-856 [» ]
    2 70-331 [» ]
    3 332-567 [» ]
    4 2-69 [» ]
    2RR1 X-ray 3.00 1 568-856 [» ]
    2 70-331 [» ]
    3 332-567 [» ]
    4 2-69 [» ]
    2RS1 X-ray 3.00 1 568-856 [» ]
    2 70-331 [» ]
    3 332-567 [» ]
    4 2-69 [» ]
    2RS3 X-ray 3.00 1 568-856 [» ]
    2 70-331 [» ]
    3 332-567 [» ]
    4 2-69 [» ]
    2RS5 X-ray 3.00 1 568-856 [» ]
    2 70-331 [» ]
    3 332-567 [» ]
    4 2-69 [» ]
    4RHV X-ray 3.00 1 568-856 [» ]
    2 70-331 [» ]
    3 332-567 [» ]
    4 2-69 [» ]
    ProteinModelPortali P03303.
    SMRi P03303. Positions 2-69, 77-567, 574-856, 1429-1486, 1538-2179.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi C03.013.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 1461213.

    Miscellaneous databases

    EvolutionaryTracei P03303.

    Family and domain databases

    Gene3Di 2.60.120.20. 3 hits.
    4.10.80.10. 2 hits.
    InterProi IPR003593. 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.
    IPR003138. Pico_P1A.
    IPR002527. Pico_P2B.
    IPR001676. Picornavirus_capsid.
    IPR001205. RNA-dir_pol_C.
    IPR007094. RNA-dir_pol_PSvirus.
    IPR009003. Trypsin-like_Pept_dom.
    IPR029053. Viral_coat.
    [Graphical view ]
    Pfami PF08727. 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 ]
    ProDomi PD001306. Peptidase_C3. 1 hit.
    PD649346. Pico_P2B. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SMARTi SM00382. AAA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50494. SSF50494. 2 hits.
    SSF52540. SSF52540. 1 hit.
    SSF89043. SSF89043. 1 hit.
    PROSITEi PS50507. RDRP_SSRNA_POS. 1 hit.
    PS51218. SF3_HELICASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The complete nucleotide sequence of a common cold virus: human rhinovirus 14."
      Stanway G., Hughes P.J., Mountford R.C., Minor P.D., Almond J.W.
      Nucleic Acids Res. 12:7859-7875(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    2. "Role of maturation cleavage in infectivity of picornaviruses: activation of an infectosome."
      Lee W.M., Monroe S., Rueckert R.R.
      J. Virol. 67:2110-2122(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    3. "Molecular cloning and complete sequence determination of RNA genome of human rhinovirus type 14."
      Callahan P.L., Mizutani S., Colonno R.J.
      Proc. Natl. Acad. Sci. U.S.A. 82:732-736(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    4. "Inhibition of nuclear import and alteration of nuclear pore complex composition by rhinovirus."
      Gustin K.E., Sarnow P.
      J. Virol. 76:8787-8796(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF PROTEASE 2A.
    5. Cited for: REVIEW.
    6. "Productive entry pathways of human rhinoviruses."
      Fuchs R., Blaas D.
      Adv. Virol. 2012:826301-826301(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    7. Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
    8. "The use of molecular-replacement phases for the refinement of the human rhinovirus 14 structure."
      Arnold E., Rossman M.G.
      Acta Crystallogr. A 44:270-282(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
    9. "Structural studies of two rhinovirus serotypes complexed with fragments of their cellular receptor."
      Kolatkar P.R., Bella J., Olson N.H., Bator C.M., Baker T.S., Rossmann M.G.
      EMBO J. 18:6249-6259(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY ELECTRON MICROSCOPY (6.0 ANGSTROMS) OF 70-856 IN COMPLEX WITH ICAM1.
    10. "Analysis of the structure of a common cold virus, human rhinovirus 14, refined at a resolution of 3.0 A."
      Arnold E., Rossman M.G.
      J. Mol. Biol. 211:763-801(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).

    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: October 1, 2014
    This is version 171 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

    External Data

    Dasty 3