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)

Q82081

- POLG_HRV3

UniProt

Q82081 - POLG_HRV3

Protein

Genome polyprotein

Gene
N/A
Organism
Human rhinovirus 3 (HRV-3)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 102 (01 Oct 2014)
      Sequence version 4 (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
    Sitei69 – 702Cleavage; by autolysisSequence Analysis
    Sitei331 – 3322Cleavage; by Protease 3CSequence Analysis
    Sitei855 – 8562Cleavage; by Protease 2ASequence Analysis
    Active sitei875 – 8751For Protease 2A activityBy similarity
    Active sitei893 – 8931For Protease 2A activityBy similarity
    Active sitei964 – 9641For Protease 2A activityBy similarity
    Sitei1001 – 10022Cleavage; by Protease 3CSequence Analysis
    Sitei1428 – 14292Cleavage; by Protease 3CSequence Analysis
    Sitei1513 – 15142Cleavage; by Protease 3CSequence Analysis
    Sitei1536 – 15372Cleavage; by Protease 3CSequence Analysis
    Active sitei1576 – 15761For Protease 3C activitySequence Analysis
    Active sitei1607 – 16071For Protease 3C activitySequence Analysis
    Active sitei1682 – 16821For Protease 3C activityBy similarity
    Sitei1718 – 17192Cleavage; by Protease 3CSequence Analysis
    Active sitei2045 – 20451For 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. 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

    MEROPSiC03.013.

    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 3 (HRV-3)
    Taxonomic identifieri44130 [NCBI]
    Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeEnterovirus
    Virus hostiHomo sapiens (Human) [TaxID: 9606]
    ProteomesiUP000013737: 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 – 21782177Genome polyproteinBy similarityPRO_0000426521Add
    BLAST
    Chaini2 – 855854P1By similarityPRO_0000426522Add
    BLAST
    Chaini2 – 331330Capsid protein VP0Sequence AnalysisPRO_0000426523Add
    BLAST
    Chaini2 – 6968Capsid protein VP4Sequence AnalysisPRO_0000426524Add
    BLAST
    Chaini70 – 331262Capsid protein VP2Sequence AnalysisPRO_0000426525Add
    BLAST
    Chaini332 – 563232Capsid protein VP3Sequence AnalysisPRO_0000426526Add
    BLAST
    Chaini564 – 855292Capsid protein VP1Sequence AnalysisPRO_0000426527Add
    BLAST
    Chaini856 – 1428573P2By similarityPRO_0000426528Add
    BLAST
    Chaini856 – 1001146Protease 2ASequence AnalysisPRO_0000423099Add
    BLAST
    Chaini1002 – 109897Protein 2BSequence AnalysisPRO_0000423100Add
    BLAST
    Chaini1100 – 1428329Protein 2CSequence AnalysisPRO_0000426529Add
    BLAST
    Chaini1429 – 2178750P3By similarityPRO_0000426530Add
    BLAST
    Chaini1429 – 1536108Protein 3ABSequence AnalysisPRO_0000426531Add
    BLAST
    Chaini1429 – 151385Protein 3ASequence AnalysisPRO_0000423102Add
    BLAST
    Chaini1514 – 153623Viral protein genome-linkedSequence AnalysisPRO_0000426532Add
    BLAST
    Chaini1537 – 2178642Protein 3CDSequence AnalysisPRO_0000426533Add
    BLAST
    Chaini1537 – 1717181Protease 3CSequence AnalysisPRO_0000426534Add
    BLAST
    Chaini1718 – 2178461RNA-directed RNA polymeraseBy similarityPRO_0000426535Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycine; by hostBy similarity
    Modified residuei1516 – 15161O-(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
    2178
    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
    Turni113 – 1153
    Helixi126 – 1283
    Beta strandi138 – 1403
    Beta strandi147 – 1515
    Helixi153 – 1553
    Helixi159 – 1657
    Beta strandi168 – 18013
    Beta strandi188 – 19710
    Beta strandi203 – 2053
    Helixi213 – 2164
    Helixi219 – 2213
    Turni238 – 2447
    Helixi247 – 2526
    Beta strandi253 – 2597
    Turni260 – 2623
    Beta strandi264 – 2707
    Beta strandi275 – 2795
    Beta strandi281 – 2844
    Beta strandi286 – 29813
    Beta strandi307 – 32317
    Turni339 – 3424
    Beta strandi354 – 3563
    Turni374 – 3796
    Beta strandi390 – 3923
    Helixi395 – 3984
    Beta strandi399 – 4024
    Beta strandi410 – 4156
    Helixi421 – 4233
    Helixi427 – 4326
    Beta strandi435 – 4406
    Beta strandi442 – 4487
    Beta strandi457 – 4637
    Helixi473 – 4764
    Beta strandi479 – 4857
    Beta strandi487 – 4893
    Beta strandi491 – 4966
    Beta strandi501 – 5033
    Beta strandi505 – 5084
    Helixi511 – 5133
    Beta strandi517 – 5248
    Beta strandi536 – 5449
    Beta strandi549 – 5535
    Beta strandi585 – 5873
    Helixi604 – 6063
    Helixi614 – 6163
    Helixi630 – 6323
    Helixi634 – 6374
    Beta strandi642 – 65110
    Helixi660 – 6634
    Beta strandi665 – 6695
    Beta strandi673 – 6764
    Helixi677 – 6837
    Beta strandi686 – 70217
    Beta strandi714 – 7207
    Helixi733 – 7364
    Beta strandi738 – 7403
    Beta strandi742 – 7465
    Beta strandi749 – 7557
    Beta strandi760 – 7667
    Beta strandi770 – 7745
    Beta strandi776 – 7783
    Helixi784 – 7863
    Beta strandi790 – 7956
    Beta strandi804 – 82219

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1RHIX-ray3.001568-855[»]
    270-331[»]
    3332-567[»]
    42-69[»]
    ProteinModelPortaliQ82081.
    SMRiQ82081. Positions 2-69, 77-567, 583-855, 1428-1485, 1537-2178.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ82081.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini2 – 14901489CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1507 – 2178672CytoplasmicSequence AnalysisAdd
    BLAST

    Intramembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Intramembranei1491 – 150616Sequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1204 – 1360157SF3 helicasePROSITE-ProRule annotationAdd
    BLAST
    Domaini1537 – 1701165Peptidase C3Add
    BLAST
    Domaini1946 – 2059114RdRp catalyticPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni564 – 58421Amphipatic alpha-helixSequence AnalysisAdd
    BLAST
    Regioni1429 – 145022DisorderedBy 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. 2 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.

    Q82081-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGAQVSTQKS GSHENQNILT NGSNQTFTVI NYYKDAASSS SAGQSFSMDP     50
    SKFTEPVKDL MLKGAPALNS PNVEACGYSD RVQQITLGNS TITTQEAANA 100
    IVCYAEWPEY LSDNDASDVN KTSKPDISVC RFYTLDSKTW KATSKGWCWK 150
    LPDALKDMGV FGQNMFYHSL GRTGYTIHVQ CNATKFHSGC LLVVVIPEHQ 200
    LASHEGGTVS VKYKYTHPGD RGIDLDTVEV AGGPTSDAIY NMDGTLLGNL 250
    LIFPHQFINL RTNNTATIVV PYINSVPIDS MTRHNNVSLM VVPIAPLNAP 300
    TGSSPTLPVT VTIAPMCTEF TGIRSRSIVP QGLPTTTLPG SGQFLTTDDR 350
    QSPSALPSYE PTPRIHIPGK VRNLLEIIQV GTLIPMNNTG TNDNVTNYLI 400
    PLHADRQNEQ IFGTKLYIGD GVFKTTLLGE IAQYYTHWSG SLRISLMYTG 450
    PALSSAKIIL AYTPPGTRGP EDRKEAMLGT HVVWDIGLQS TIVMTIPWTS 500
    GVQFRYTDPD TYTSAGYLSC WYQTSLILPP QTSGQVYLLS FISACPDFKL 550
    RLMKDTQTIS QTDALTEGLS DELEEVIVEK TKQTLASVSS GPKHTQSVPA 600
    LTANETGATL PTRPSDNVET RTTYMHFNGS ETDVESFLGR AACVHVTEIK 650
    NKNAAGLDNH RKEGLFNDWK INLSSLVQLR KKLELFTYVR FDSEYTILAT 700
    ASQPEASSYS SNLTVQAMYV PPGAPNPKEW DDYTWQSASN PSVFFKVGET 750
    SRFSVPFVGI ASAYNCFYDG YSHDDPDTPY GITVLNHMGS MAFRVVNEHD 800
    VHTTIVKIRV YHRAKHVEAW IPRAPRALPY VSIGRTNYPR DSKTIIKKRT 850
    NIKTYGLGPR FGGVFTSNVK IINYHLMTPD DHLNLVAPYP NRDLAVVATG 900
    AHGAETIPHC NCTSGVYYSR YYRKFYPIIC ERPTNIWIEG SSYYPSRYQA 950
    GVMKGVGPAE PGDCGGILRC IHGPIGLLTA GGGGYVCFAD IRQLDFIADE 1000
    QGLGDYITSL GRAFGTGFTD QISAKVCELQ DVAKDFLTTK VLSKVVKMIS 1050
    ALVIICRNHD DLVTVTATLA LLGCDGSPWR FLKMYISKHF QVPYIERQAN 1100
    DGWFRKFNDA CNAAKGLEWI ANKISKLIEW IKNKVLPQAR EKLEFCSKLK 1150
    QLDILERQIA SIHDSNPTQE KREQLFNNVL WLEQMSQKFS PLYASEAKRI 1200
    RDLKNKITNY MQFKSKQRTE PVCVLIHGTP GSGKSLTTSI VGRALAEHFN 1250
    SSVYSLPPDP KHFDGYQQQE VVIMDDLNQN PDGQDISMFC QMVSSVDFLP 1300
    PMASLDNKGM LFTSNFVLAS TNSNTLSPPT ILNPEALIRR FGFDLDICMH 1350
    STYTKNGKLN AAMATSLCKD CHQPSNFKKC CPLVCGKAIS LVDRVSNVRF 1400
    SIDQLVTAII NDYKNKVKIT DSLEVLFQGP VYKDLEIDIC NTPPPECISD 1450
    LLKSVDSEEV REYCKKKKWI IPQISTNIER AVNQASMIIN TILMFVSTLG 1500
    IVYVIYKLFA QTQGPYSGNP VHNKLKPPTL KPVVVQGPNT EFALSLLRKN 1550
    ILTITTEKGE FTSLGIHDRI CVLPTHAQPG DNVLVNGQKI QIKDKYKLVD 1600
    PDNTNLELTI IELDRNEKFR DIRGFISEDL EGLDATLVVH SNGFTNTILD 1650
    VGPITMAGLI NLSNTPTTRM IRYDYPTKTG QCGGVLCTTG KIFGIHVGGN 1700
    GRRGFSAQLK KQYFVEKQGL IVSKQKVRDI GLNPINTPTK TKLHPSVFYN 1750
    VFPGSKQPAV LNDNDPRLEV KLAESLFSKY KGNVQMEPTE NMLIAVDHYA 1800
    GQLMSLDIST KELTLKEALY GVDGLEPIDV TTSAGYPYVS LGIKKRDILN 1850
    KETQDVEKMK FYLDKYGIDL PLVTYIKDEL RSVDKVRLGK SRLIEASSLN 1900
    DSVNMRMKLG NLYKAFHQNP GIITESAVGC DPDVFWSVIP CLMDGHLMAF 1950
    DYSNFDASLS PVWFECLEKV LNKLGFKQPS LIQSICNTHH IFRDEIYRVE 2000
    GGMPSGCSGT SIFNSMINNI IIRTLILDAY KGIDLDSLRI LAYGDDLIVS 2050
    YPFELDSNIL AAIGKNYGLT ITPPDKSDAF TKITWENITF LKRYFRPDPQ 2100
    FPFLIHPVMP MQDIYESIRW TRDPRNTQDH VRSLCMLAWH SGEKDYNDFI 2150
    TKIRTTDIGK CLNLPEYSVL RRRWLDLF 2178
    Length:2,178
    Mass (Da):242,794
    Last modified:July 24, 2013 - v4
    Checksum:i0DFED5280AF25CCF
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti87 – 871L → M.
    Natural varianti98 – 981A → R.
    Natural varianti260 – 2601L → M.
    Natural varianti475 – 4751E → K.
    Natural varianti523 – 5231Q → L.
    Natural varianti846 – 8461I → V.
    Natural varianti1349 – 13491M → L.
    Natural varianti1389 – 13891I → V.
    Natural varianti1703 – 17031R → Q.
    Natural varianti1925 – 19251E → G.
    Natural varianti1978 – 19781Q → H.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ473485 Genomic RNA. Translation: ABF51179.1.
    EF173422 Genomic RNA. Translation: ABO69378.1.
    U60874 Genomic RNA. Translation: AAB05616.1.

    Cross-referencesi

    Web resourcesi

    Virus Particle ExploreR db

    Icosahedral capsid structure

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ473485 Genomic RNA. Translation: ABF51179.1 .
    EF173422 Genomic RNA. Translation: ABO69378.1 .
    U60874 Genomic RNA. Translation: AAB05616.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1RHI X-ray 3.00 1 568-855 [» ]
    2 70-331 [» ]
    3 332-567 [» ]
    4 2-69 [» ]
    ProteinModelPortali Q82081.
    SMRi Q82081. Positions 2-69, 77-567, 583-855, 1428-1485, 1537-2178.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi C03.013.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei Q82081.

    Family and domain databases

    Gene3Di 2.60.120.20. 3 hits.
    3.40.50.300. 2 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. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    2. "New complete genome sequences of human rhinoviruses shed light on their phylogeny and genomic features."
      Tapparel C., Junier T., Gerlach D., Cordey S., Van Belle S., Perrin L., Zdobnov E.M., Kaiser L.
      BMC Genomics 8:224-224(2007)
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-855, X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
    4. "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_HRV3
    AccessioniPrimary (citable) accession number: Q82081
    Secondary accession number(s): A5GZD4, A7KC14
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: July 24, 2013
    Last modified: October 1, 2014
    This is version 102 of the entry and version 4 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