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P12916

- POLG_HRV1B

UniProt

P12916 - POLG_HRV1B

Protein

Genome polyprotein

Gene
N/A
Organism
Human rhinovirus 1B (HRV-1B)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 152 (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 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 mmbers 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 1B (HRV-1B)
    Taxonomic identifieri12129 [NCBI]
    Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeEnterovirusRhinovirus A
    Virus hostiHomo sapiens (Human) [TaxID: 9606]
    ProteomesiUP000007681: 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_0000426491Add
    BLAST
    Chaini2 – 847846P1By similarityPRO_0000426492Add
    BLAST
    Chaini2 – 332331Capsid protein VP0Sequence AnalysisPRO_0000426493Add
    BLAST
    Chaini2 – 6968Capsid protein VP4Sequence AnalysisPRO_0000426494Add
    BLAST
    Chaini70 – 332263Capsid protein VP2Sequence AnalysisPRO_0000426495Add
    BLAST
    Chaini333 – 567235Capsid protein VP3Sequence AnalysisPRO_0000426496Add
    BLAST
    Chaini567 – 847281Capsid protein VP1Sequence AnalysisPRO_0000426497Add
    BLAST
    Chaini847 – 1416570P2By similarityPRO_0000426498Add
    BLAST
    Chaini847 – 999153Protease 2ASequence AnalysisPRO_0000426499Add
    BLAST
    Chaini1000 – 109495Protein 2BSequence AnalysisPRO_0000040004Add
    BLAST
    Chaini1095 – 1416322Protein 2CSequence AnalysisPRO_0000040005Add
    BLAST
    Chaini1417 – 2157741P3By similarityPRO_0000426500Add
    BLAST
    Chaini1417 – 151498Protein 3ABSequence AnalysisPRO_0000426501Add
    BLAST
    Chaini1417 – 149377Protein 3ASequence AnalysisPRO_0000040006Add
    BLAST
    Chaini1494 – 151421Viral protein genome-linkedSequence AnalysisPRO_0000426502Add
    BLAST
    Chaini1515 – 2157643Protein 3CDSequence AnalysisPRO_0000426503Add
    BLAST
    Chaini1515 – 1696182Protease 3CSequence AnalysisPRO_0000426504Add
    BLAST
    Chaini1697 – 2157461RNA-directed RNA polymeraseBy similarityPRO_0000426505Add
    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
    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. 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 strandi1699 – 17057
    Helixi1706 – 17094
    Turni1726 – 17305
    Helixi1751 – 17566
    Helixi1769 – 178315
    Helixi1794 – 17996
    Beta strandi1802 – 18043
    Beta strandi1809 – 18113
    Helixi1817 – 18204
    Helixi1824 – 18274
    Turni1830 – 18334
    Helixi1836 – 184510
    Beta strandi1851 – 18555
    Helixi1862 – 18665
    Beta strandi1872 – 18754
    Helixi1878 – 189720
    Turni1901 – 19044
    Helixi1911 – 192111
    Beta strandi1924 – 19296
    Beta strandi1931 – 19344
    Helixi1936 – 19383
    Helixi1941 – 195313
    Helixi1959 – 19613
    Helixi1962 – 19654
    Beta strandi1966 – 19716
    Beta strandi1974 – 19818
    Helixi1989 – 200820
    Helixi2014 – 20163
    Beta strandi2018 – 20225
    Beta strandi2025 – 20328
    Helixi2036 – 20416
    Helixi2042 – 20465
    Turni2064 – 20663
    Beta strandi2072 – 20765
    Beta strandi2078 – 20803
    Beta strandi2083 – 20875
    Helixi2090 – 20978
    Beta strandi2099 – 21013
    Helixi2103 – 21053
    Helixi2106 – 211712
    Helixi2118 – 21203
    Helixi2122 – 213211
    Helixi2136 – 21405
    Helixi2146 – 21549

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1XR6X-ray2.50A1698-2157[»]
    ProteinModelPortaliP12916.
    SMRiP12916. Positions 2-69, 80-570, 575-856, 858-996, 1515-1694, 1698-2157.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP12916.

    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.

    P12916-1 [UniParc]FASTAAdd to Basket

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    MGAQVSRQNV GTHSTQNSVS NGSSLNYFNI NYFKDAASSG ASRLDFSQDP     50
    SKFTDPVKDV LEKGIPTLQS PSVEACGYSD RIIQITRGDS TITSQDVANA 100
    VVGYGVWPHY LTPQDATAID KPTQPDTSSN RFYTLESKHW NGDSKGWWWK 150
    LPDALKEMGI FGENMYYHFL GRSGYTVHVQ CNASKFHQGT LLVAMIPEHQ 200
    LASAKNGSVT AGYNLTHPGE AGRVVGQQRD ANLRQPSDDS WLNFDGTLLG 250
    NLLIFPHQFI NLRSNNSATL IVPYVNAVPM DSMLRHNNWS LVIIPISPLR 300
    SETTSSNIRP ITVSISPMCA EFSGARAKNV RQGLPVYITP GSGQFMTTDD 350
    MQSPCALPWY HPTKEISIPG EVKNLIEMCQ VDTLIPVNNV GTNVGNISMY 400
    TVQLGNQMDM AQEVFAIKVD ITSQPLATTL IGEIASYYTH WTGSLRFSFM 450
    FCGTANTTLK LLLAYTPPGI DKPATRKDAM LGTHVVWDVG LQSTISLVVP 500
    WVSASHFRLT ANDKYSMAGY ITCWYQTNLV VPPNTPQTAD MLCFVSACKD 550
    FCLRMARDTD LHIQSGPIEQ NPVENYIDEV LNEVLVVPNI KESHHTTSNS 600
    APLLDAAETG HTSNVQPEDA IETRYVMTSQ TRDEMSIESF LGRSGCVHIS 650
    RIKVDYNDYN GVNKNFTTWK ITLQEMAQIR RKFELFTYVR FDSEVTLVPC 700
    IAGRGDDIGH VVMQYMYVPP GAPIPKTRND FSWQSGTNMS IFWQHGQPFP 750
    RFSLPFLSIA SAYYMFYDGY DGDNSSSKYG SIVTNDMGTI CSRIVTEKQE 800
    HPVVITTHIY HKAKHTKAWC PRPPRAVPYT HSRVTNYVPK TGDVTTAIVP 850
    RASMKTVGPS DLYVHVGNLI YRNLHLFNSE MHDSILVSYS SDLIIYRTNT 900
    TGDDYIPSCN CTEATYYCKH KNRYYPIKVT PHDWYEIQES EYYPKHIQYN 950
    LLIGEGPCEP GDCGGKLLCR HGVIGIITAG GEGHVAFTDL RQFQCAEEQG 1000
    ITDYIHMLGE AFGNGFVDSV KEQINAINPI NSISKKVIKW LLRIISAMVI 1050
    IIRNSSDPQT IIATLTLIGC NGSPWRFLKE KFCKWTQLTY IHKESDSWLK 1100
    KFTEMCNAAR GLEWIGNKIS KFIDWMKSML PQAQLKVKYL NEIKKLSLLE 1150
    KQIENLRAAD NATQEKIKCE IDTLHDLSCK FLPLYAHEAK RIKVLYNKCS 1200
    NIIKQRKRSE PVAVMIHGPP GTGKSITTNF LARMITNESD VYSLPPDPKY 1250
    FDGYDNQSVV IMDDIMQNPD GEDMTLFCQM VSSVTFIPPM ADLPDKGKPF 1300
    DSRFVLCSTN HSLLAPPTIS SLPAMNRRFF FDLDIVVHDN YKDAQGKLNV 1350
    SKAFQPCNVN TKIGNAKCCP FVCGKAVSFK DRSTCSTYTL AQVYNHILEE 1400
    DKRRRQVVDV MSAIFQGPIS LDAPPPPAIA DLLQSVRTPE VIKYCQDNKW 1450
    IVPAECQIER DLSIANSIIT IIANIISIAG IIFVIYKLFC TLQGPYSGEP 1500
    KPKTKMPERR VVAQGPEEEF GRSILKNNTC VITTDNGKFT GLGIYDRTLI 1550
    IPTHADPGRE VQVNGIHTKV LDSYDLYNRD GVKLEITVIQ LDRNEKFRDI 1600
    RKYIPETEDD YPECNLALSA NQVEPTIIKV GDVVSYGNIL LSGNQTARML 1650
    KYNYPTKSGY CGGVLYKIGQ ILGIHVGGNG RDGFSAMLLR SYFTDTQGQI 1700
    KISKHANECG LPTIHTPSKT KLQPSVFYDV FPGSKEPAVS RDNDPRLKVN 1750
    FKEALFSKYK GNTECSLNQH MEIAIAHYSA QLITLDIDSK PIALEDSVFG 1800
    IEGLEALDLN TSAGFPYVTM GIKKRDLINN KTKDISRLKE ALDKYGVDLP 1850
    MITFLKDELR KKEKISAGKT RVIEASSIND TILFRTTFGN LFSKFHLNPG 1900
    VVTGSAVGCD PETFWSKIPV MLDGDCIMAF DYTNYDGSIH PVWFQALKKV 1950
    LENLSFQSNL IDRLCYSKHL FKSTYYEVAG GVPSGCSGTS IFNTMINNII 2000
    IRTLVLDAYK NIDLDKLKII AYGDDVIFSY KYTLDMEAIA NEGKKYGLTI 2050
    TPADKSTEFK KLDYNNVTFL KRGFKQDEKH TFLIHPTFPV EEIYESIRWT 2100
    KKPSQMQEHV LSLCHLMWHN GRKVYEDFSS KIRSVSAGRA LYIPPYDLLK 2150
    HEWYEKF 2157
    Length:2,157
    Mass (Da):242,315
    Last modified:January 23, 2007 - v3
    Checksum:i42DB649063B677B9
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D00239 Genomic RNA. Translation: BAA00168.1.
    PIRiA28699. GNNY1B.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D00239 Genomic RNA. Translation: BAA00168.1 .
    PIRi A28699. GNNY1B.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1XR6 X-ray 2.50 A 1698-2157 [» ]
    ProteinModelPortali P12916.
    SMRi P12916. Positions 2-69, 80-570, 575-856, 858-996, 1515-1694, 1698-2157.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi C03.007.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P12916.

    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. "The nucleotide sequence of human rhinovirus 1B: molecular relationships within the rhinovirus genus."
      Hughes P.J., North C., Jellis C.H., Minor P.D., Stanway G.
      J. Gen. Virol. 69:49-58(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    2. "The crystal structure of the RNA-dependent RNA polymerase from human rhinovirus: a dual function target for common cold antiviral therapy."
      Love R.A., Maegley K.A., Yu X., Ferre R.A., Lingardo L.K., Diehl W., Parge H.E., Dragovich P.S., Fuhrman S.A.
      Structure 12:1533-1544(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1698-2157.
    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_HRV1B
    AccessioniPrimary (citable) accession number: P12916
    Secondary accession number(s): Q82106
    , Q82107, Q82108, Q82109, Q82110, Q82111, Q82112, Q82113, Q82114, Q82115, Q89704
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 152 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