Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P23008

- POLG_HRV1A

UniProt

P23008 - POLG_HRV1A

Protein

Genome polyprotein

Gene
N/A
Organism
Human rhinovirus 1A (HRV-1A)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 3 (24 Jul 2013)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 cell receptor 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
    Sitei332 – 3332Cleavage; by Protease 3CSequence Analysis
    Active sitei875 – 8751For Protease 2A activityBy similarity
    Active sitei892 – 8921For Protease 2A activityBy similarity
    Active sitei963 – 9631For Protease 2A activityBy similarity
    Sitei999 – 10002Cleavage; by Protease 3CSequence Analysis
    Sitei1416 – 14172Cleavage; by Protease 3CSequence Analysis
    Sitei1493 – 14942Cleavage; by Protease 3CSequence Analysis
    Sitei1514 – 15152Cleavage; by Protease 3CSequence Analysis
    Active sitei1554 – 15541For Protease 3C activitySequence Analysis
    Active sitei1585 – 15851For Protease 3C activitySequence Analysis
    Active sitei1661 – 16611For Protease 3C activityBy similarity
    Sitei1697 – 16982Cleavage; by Protease 3CSequence Analysis
    Active sitei2024 – 20241For 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-KW
    4. pore formation by virus in membrane of host cell Source: UniProtKB-KW
    5. pore-mediated entry of viral genome into host cell Source: UniProtKB-KW
    6. protein oligomerization Source: UniProtKB-KW
    7. RNA-protein covalent cross-linking Source: UniProtKB-KW
    8. suppression by virus of host gene expression Source: UniProtKB-KW
    9. suppression by virus of host mRNA export from nucleus Source: UniProtKB-KW
    10. suppression by virus of host RIG-I activity by RIG-I proteolysis Source: UniProtKB
    11. suppression by virus of host translation initiation factor activity Source: UniProtKB
    12. transcription, DNA-templated Source: InterPro
    13. viral RNA genome replication Source: InterPro
    14. 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 RNA replication, Virus endocytosis by host, Virus entry into host cell

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding, RNA-binding

    Protein family/group databases

    MEROPSiC03.007.

    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 1A (HRV-1A)
    Taxonomic identifieri12134 [NCBI]
    Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeEnterovirusRhinovirus A
    Virus hostiHomo sapiens (Human) [TaxID: 9606]
    ProteomesiUP000013736: 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 – 21572156Genome polyproteinBy similarityPRO_0000426476Add
    BLAST
    Chaini2 – 857856P1By similarityPRO_0000426477Add
    BLAST
    Chaini2 – 332331Capsid protein VP0Sequence AnalysisPRO_0000426478Add
    BLAST
    Chaini2 – 6968Capsid protein VP4Sequence AnalysisPRO_0000426479Add
    BLAST
    Chaini70 – 332263Capsid protein VP2Sequence AnalysisPRO_0000426480Add
    BLAST
    Chaini333 – 567235Capsid protein VP3Sequence AnalysisPRO_0000426481Add
    BLAST
    Chaini567 – 857291Capsid protein VP1Sequence AnalysisPRO_0000426482Add
    BLAST
    Chaini857 – 1416560P2By similarityPRO_0000426483Add
    BLAST
    Chaini857 – 999143Protease 2ASequence AnalysisPRO_0000426484Add
    BLAST
    Chaini1000 – 109495Protein 2BSequence AnalysisPRO_5000438367Add
    BLAST
    Chaini1095 – 1416322Protein 2CSequence AnalysisPRO_5000438368Add
    BLAST
    Chaini1417 – 2157741P3By similarityPRO_0000426485Add
    BLAST
    Chaini1417 – 151498Protein 3ABSequence AnalysisPRO_0000426486Add
    BLAST
    Chaini1417 – 149377Protein 3ASequence AnalysisPRO_5000438369Add
    BLAST
    Chaini1494 – 151421Viral protein genome-linkedSequence AnalysisPRO_0000426487Add
    BLAST
    Chaini1515 – 2157643Protein 3CDSequence AnalysisPRO_0000426488Add
    BLAST
    Chaini1515 – 1696182Protease 3CSequence AnalysisPRO_0000426489Add
    BLAST
    Chaini1697 – 2157461RNA-directed RNA polymeraseBy similarityPRO_0000426490Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycine; by hostBy similarity
    Modified residuei1496 – 14961O-(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
    Myristoylation of VP4 is required during RNA encapsidation and formation of the mature virus particle.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
    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. 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
    2157
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 64
    Beta strandi27 – 304
    Beta strandi33 – 353
    Helixi36 – 383
    Beta strandi83 – 864
    Beta strandi91 – 966
    Helixi103 – 1053
    Turni113 – 1153
    Beta strandi127 – 1315
    Beta strandi146 – 1505
    Helixi151 – 1544
    Beta strandi156 – 1583
    Helixi161 – 1644
    Beta strandi167 – 18014
    Beta strandi190 – 1989
    Beta strandi203 – 2086
    Turni214 – 2163
    Beta strandi223 – 2264
    Beta strandi231 – 2333
    Turni240 – 2467
    Helixi252 – 2543
    Beta strandi255 – 2617
    Turni262 – 2643
    Beta strandi266 – 2727
    Beta strandi276 – 2827
    Turni283 – 2853
    Beta strandi289 – 2979
    Beta strandi310 – 32516
    Turni340 – 3434
    Beta strandi355 – 3573
    Helixi375 – 3795
    Helixi391 – 3933
    Helixi398 – 4003
    Beta strandi401 – 4044
    Beta strandi408 – 4114
    Beta strandi413 – 4186
    Beta strandi421 – 4233
    Helixi432 – 4354
    Beta strandi438 – 4436
    Beta strandi445 – 4517
    Beta strandi458 – 4669
    Helixi476 – 4805
    Beta strandi482 – 4887
    Beta strandi490 – 4923
    Beta strandi494 – 4996
    Beta strandi504 – 5118
    Beta strandi520 – 53011
    Beta strandi533 – 5353
    Beta strandi539 – 5479
    Beta strandi552 – 5565
    Helixi576 – 5805
    Beta strandi584 – 5863
    Helixi607 – 6093
    Helixi617 – 6204
    Beta strandi633 – 6364
    Helixi637 – 6415
    Beta strandi645 – 6539
    Beta strandi656 – 6605
    Beta strandi667 – 6704
    Helixi679 – 6835
    Beta strandi686 – 70318
    Beta strandi713 – 7186
    Beta strandi720 – 7223
    Beta strandi726 – 7294
    Helixi732 – 7343
    Beta strandi738 – 7436
    Beta strandi751 – 7544
    Beta strandi759 – 7657
    Beta strandi789 – 7935
    Beta strandi803 – 82119
    Beta strandi831 – 8344
    Beta strandi840 – 8423

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AYMX-ray2.1542-69[»]
    1AYNX-ray2.9042-69[»]
    1R1AX-ray3.201571-857[»]
    270-332[»]
    3333-570[»]
    42-45[»]
    2HWDX-ray3.801571-857[»]
    270-332[»]
    3333-570[»]
    42-45[»]
    2HWEX-ray3.801571-857[»]
    270-332[»]
    3333-570[»]
    42-45[»]
    2HWFX-ray3.801571-857[»]
    270-332[»]
    3333-570[»]
    42-45[»]
    ProteinModelPortaliP23008.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP23008.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini2 – 14701469CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1487 – 2157671CytoplasmicSequence AnalysisAdd
    BLAST

    Intramembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Intramembranei1471 – 148616Sequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1188 – 1350163SF3 helicasePROSITE-ProRule annotationAdd
    BLAST
    Domaini1515 – 1680166Peptidase C3Add
    BLAST
    Domaini1925 – 2038114RdRp catalyticPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni567 – 58418Amphipatic alpha-helixSequence AnalysisAdd
    BLAST
    Regioni1417 – 143115DisorderedBy 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.
    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.
    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.

    P23008-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGAQVSRQNV GTHSTQNSVS NGSSLNYFNI NYFKDAASSG ASRLDFSQDP     50
    SKFTDPVKDV LEKGIPTLQS PSVEACGYSD RIMQITRGDS TITSQDVANA 100
    VVGYGVWPHY LTPQDATAID KPTQPDTSSN RFYTLESKHW NGSSKGWWWK 150
    LPDALKDMGI FGENMYYHFL GRSGYTVHVQ CNASKFHQGT LLVAMIPEHQ 200
    LASAKHGSVT AGYKLTHPGE AGRDVSQERD ASLRQPSDDS WLNFDGTLLG 250
    NLLIFPHQFI NLRSNNSATL IVPYVNAVPM DSMLRHNNWS LVIIPISPLR 300
    SETTSSNIVP ITVSISPMCA EFSGARAKNI KQGLPVYITP GSGQFMTTDD 350
    MQSPCALPWY HPTKEISIPG EVKNLIEMCQ VDTLIPVNNV GNNVGNVSMY 400
    TVQLGNQTGM AQKVFSIKVD ITSQPLATTL IGEIASYYTH WTGSLRFSFM 450
    FCGTANTTLK LLLAYTPPGI DEPTTRKDAM LGTHVVWDVG LQSTISLVVP 500
    WVSASHFRLT ADNKYSMAGY ITCWYQTNLV VPPSTPQTAD MLCFVSACKD 550
    FCLRMARDTD LHIQSGPIEQ NPVENYIDEV LNEVLVVPNI KESHHTTSNS 600
    APLLDAAETG HTSNVQPEDA IETRYVITSQ TRDEMSIESF LGRSGCVHIS 650
    RIKVDYTDYN GQDINFTKWK ITLQEMAQIR RKFELFTYVR FDSEITLVPC 700
    IAGRGDDIGH IVMQYMYVPP GAPIPSKRND FSWQSGTNMS IFWQHGQPFP 750
    RFSLPFLSIA SAYYMFYDGY DGDNTSSKYG SVVTNDMGTI CSRIVTEKQK 800
    HSVVITTHIY HKAKHTKAWC PRPPRAVPYT HSHVTNYMPE TGDVTTAIVR 850
    RNTITTAGPS DLYVHVGNLI YRNLHLFNSE MHDSILISYS SDLIIYRTNT 900
    IGDDYIPNCN CTEATYYCRH KNRYYPIKVT PHDWYEIQES EYYPKHIQYN 950
    LLIGEGPCEP GDCGGKLLCR HGVIGIITAG GEGHVAFIDL RQFHCAEEQG 1000
    ITDYIHMLGE AFGNGFVDSV KEQINAINPI NNISKKVIKW LLRIISAMVI 1050
    IIRNSSDPQT IIATLTLIGC NGSPWRFLKE KFCKWTQLTY IHKESDSWLK 1100
    KFTEMCNAAR GLEWIGNKIS KFIDWMKSML PQAQLKVKYL NEIKKLSLLE 1150
    KQIENLRAAD SATQEKIKCE IDTLHDLSCK FLPLYAHEAK RIKVLYNKCS 1200
    NIIKQRKRSE PVAVMIHGPP GTGKSITTNF LARMITNESD VYSLPPDPKY 1250
    FDGYDNQSVV IMDDIMQNPD GEDMTLFCQM VSSVTFIPPM ADLPDKGKPF 1300
    DSRFILCSTN HSLLAPPTIS SLPAMNRRFF FDLDIVVHDN YKDTQGKLDV 1350
    SKAFRPCNVN TKIGNAKCCP FVCGKAVXFK DRSTCSTYTL AQVYNHILEE 1400
    DKRRRQVVDV MSAIFQGPIS LDXPPPPAIX DLLQSVRTPE VIKYCQDNKW 1450
    VIPAECQVER DLNIANSIIA IIANIISIAG IIFVIYKLFC SLQGPYSGEP 1500
    KPKTKVPERR VVAQGPEEEF GRSILKNNTC VITTGNGKFT GLGIHDRILI 1550
    IPTHADPGRE VQVNGVHTKV LDSYDLYNRD GVKLEITVIQ LDRNEKFRDI 1600
    RKYIPETEDD YPECNLALSA NQDEPTIIKV GDVVSYGNIL LSGNQTARML 1650
    KYNYPTKSGY CGGVLYKIGQ ILGIHVGGNG RDGFSAMLLR SYFTDTQGQI 1700
    KVNKHATECG LPTIHTPSKT KLQPSVFYDV FPGSKEPAVL TDNDPRLEVN 1750
    FKEALFSKYK GNVECNLNEH MEIAIAHYSA QLMTLDIDSR PIALEDSVFG 1800
    IEGLEALDLN TSAGFPYVTM GIKKRDLINN KTKDISRLKE ALDKYGVDLP 1850
    MITFLKDELR KKEKISTGKT RVIEASSIND TILFRTTFGN LFSKFHLNPG 1900
    VVTGSAVGCD PETFWSKIPV MLDGDCIMAF DYTNYDGSIH PVWFQALKKV 1950
    LENLSFQSNL IDRLCYSKHL FKSTYYEVAG GVPSGCSGTS IFNTMINNII 2000
    IRTLVLDAYK NIDLDKLKII AYGDDVIFSY KYTLDMEAIA NEGKKYGLTI 2050
    TPADKSNEFK KLDYSNVTFL KRGFKQDERH TFLIHPTFPV EEIHESIRWT 2100
    KKPSQMQEHV LSLCHLMWHN GRKVYEDFSS KIRSVSAGRA LYIPPYDLLK 2150
    HEWYEKF 2157
    Length:2,157
    Mass (Da):242,487
    Last modified:July 24, 2013 - v3
    Checksum:i8B7807D279FC0A84
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti4 – 41Q → G.
    Natural varianti93 – 953TSQ → SSD.
    Natural varianti120 – 1201D → N.
    Natural varianti290 – 2901S → C.
    Natural varianti424 – 4241Q → T.
    Natural varianti754 – 7541L → I.
    Natural varianti801 – 8011H → L.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    FJ445111 Genomic RNA. Translation: ACK37367.1.

    Cross-referencesi

    Web resourcesi

    Virus Particle ExploreR db

    Icosahedral capsid structure in complex with antiviral compound Win56291

    Virus Particle ExploreR db

    Icosahedral capsid structure in complex with antiviral compound Win54954

    Virus Particle ExploreR db

    Icosahedral capsid structure in complex with antiviral compound R61837

    Virus Particle ExploreR db

    Icosahedral capsid structure

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    FJ445111 Genomic RNA. Translation: ACK37367.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AYM X-ray 2.15 4 2-69 [» ]
    1AYN X-ray 2.90 4 2-69 [» ]
    1R1A X-ray 3.20 1 571-857 [» ]
    2 70-332 [» ]
    3 333-570 [» ]
    4 2-45 [» ]
    2HWD X-ray 3.80 1 571-857 [» ]
    2 70-332 [» ]
    3 333-570 [» ]
    4 2-45 [» ]
    2HWE X-ray 3.80 1 571-857 [» ]
    2 70-332 [» ]
    3 333-570 [» ]
    4 2-45 [» ]
    2HWF X-ray 3.80 1 571-857 [» ]
    2 70-332 [» ]
    3 333-570 [» ]
    4 2-45 [» ]
    ProteinModelPortali P23008.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi C03.007.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P23008.

    Family and domain databases

    Gene3Di 2.60.120.20. 3 hits.
    3.40.50.300. 1 hit.
    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. "Sequencing and analyses of all known human rhinovirus genomes reveal structure and evolution."
      Palmenberg A.C., Spiro D., Kuzmickas R., Wang S., Djikeng A., Rathe J.A., Fraser-Liggett C.M., Liggett S.B.
      Science 324:55-59(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
      Strain: ATCC VR-1559.
    2. Cited for: NUCLEOTIDE SEQUENCE OF 1-45 AND 70-857, X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS).
    3. "Productive entry pathways of human rhinoviruses."
      Fuchs R., Blaas D.
      Adv. Virol. 2012:826301-826301(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.

    Entry informationi

    Entry nameiPOLG_HRV1A
    AccessioniPrimary (citable) accession number: P23008
    Secondary accession number(s): B9V432
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1991
    Last sequence update: July 24, 2013
    Last modified: October 1, 2014
    This is version 107 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    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