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Q9YID8

- POLG_HPE23

UniProt

Q9YID8 - POLG_HPE23

Protein

Genome polyprotein

Gene
N/A
Organism
Human parechovirus 2 (strain CT86-6760) (HPeV-2) (Echovirus 23)
Status
Reviewed - Annotation score: 5 out of 5- Protein inferred from homologyi
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      Previous versions | rss
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    Functioni

    Protein 2A: Is not a protease.By similarity
    Protein 2B: Affects membrane integrity and cause an increase in membrane permeability.By similarity
    Protein 2C: Associates with and induces structural rearrangements of intracellular membranes. It displays RNA-binding, nucleotide binding and NTPase activities By similarity.By similarity
    Protein 3A, via its hydrophobic domain, serves as membrane anchor.By similarity
    Protease 3C: cysteine protease that generates mature viral proteins from the precursor polyprotein. In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate bind cooperatively to the protease By similarity.By similarity
    RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals.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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei784 – 7852Cleavage; by protease 2ASequence Analysis
    Active sitei1558 – 15581For protease 3C activitySequence Analysis
    Active sitei1589 – 15891For protease 3C activitySequence Analysis
    Active sitei1678 – 16781For protease 3C activitySequence Analysis

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi1193 – 12008ATPPROSITE-ProRule annotation

    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. induction by virus of host autophagy Source: UniProtKB
    2. pore formation by virus in membrane of host cell Source: UniProtKB-KW
    3. protein oligomerization Source: UniProtKB-KW
    4. RNA-protein covalent cross-linking Source: UniProtKB-KW
    5. suppression by virus of host RIG-I activity by RIG-I proteolysis Source: UniProtKB
    6. suppression by virus of host translation initiation factor activity Source: UniProtKB
    7. transcription, DNA-templated Source: InterPro
    8. viral entry into host cell Source: UniProtKB-KW
    9. viral RNA genome replication Source: InterPro
    10. 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

    Host-virus interaction, Ion transport, Transport, Viral attachment to host cell, Viral RNA replication, Virus entry into host cell

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding, RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Genome polyprotein
    Cleaved into the following 10 chains:
    Alternative name(s):
    P1AB
    Virion protein 0
    Alternative name(s):
    P1C
    Virion protein 3
    Alternative name(s):
    P1D
    Virion protein 1
    Protein 2A
    Short name:
    P2A
    Protein 2B
    Short name:
    P2B
    Protein 2C (EC:3.6.1.15)
    Short name:
    P2C
    Protein 3A
    Short name:
    P3A
    Protein 3B
    Short name:
    P3B
    Alternative name(s):
    VPg
    Protease 3C (EC:3.4.22.28)
    Short name:
    P3C
    Alternative name(s):
    Picornain 3C
    OrganismiHuman parechovirus 2 (strain CT86-6760) (HPeV-2) (Echovirus 23)
    Taxonomic identifieri122961 [NCBI]
    Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeParechovirus
    Virus hostiHomo sapiens (Human) [TaxID: 9606]
    ProteomesiUP000008274: Genome

    Subcellular locationi

    Chain Protein VP3 : Virion By similarity. Host cytoplasm Curated
    Chain Protein VP1 : Virion By similarity. Host cytoplasm Curated
    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 By similarity.By similarity
    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 By similarity.By similarity
    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 By similarity.By similarity
    Chain RNA-directed RNA polymerase 3D-POL : 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 By similarity.By similarity

    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. viral capsid Source: UniProtKB-KW
    5. viral genome Source: InterPro

    Keywords - Cellular componenti

    Capsid protein, Host cytoplasm, Host cytoplasmic vesicle, Host membrane, Membrane, Virion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 290290Protein VP0Sequence AnalysisPRO_0000039740Add
    BLAST
    Chaini291 – 549259Protein VP3Sequence AnalysisPRO_0000039741Add
    BLAST
    Chaini550 – 784235Protein VP1Sequence AnalysisPRO_0000039742Add
    BLAST
    Chaini785 – 931147Protein 2ASequence AnalysisPRO_0000039743Add
    BLAST
    Chaini932 – 1053122Protein 2BSequence AnalysisPRO_0000039744Add
    BLAST
    Chaini1054 – 1382329Protein 2CSequence AnalysisPRO_0000039745Add
    BLAST
    Chaini1383 – 1499117Protein 3ASequence AnalysisPRO_0000039747Add
    BLAST
    Chaini1500 – 151920Protein 3BBy similarityPRO_0000311174Add
    BLAST
    Chaini1520 – 1719200Protease 3CSequence AnalysisPRO_0000039748Add
    BLAST
    Chaini1720 – 2188469RNA-directed RNA polymerase 3D-POLSequence AnalysisPRO_0000039749Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1502 – 15021O-(5'-phospho-RNA)-tyrosineBy similarity

    Post-translational modificationi

    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
    Specific enzymatic cleavages yield mature proteins. All cleavages are catalyzed by P3C.

    Keywords - PTMi

    Covalent protein-RNA linkage, Lipoprotein, Myristate, Phosphoprotein

    Structurei

    3D structure databases

    ProteinModelPortaliQ9YID8.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1165 – 1326162SF3 helicasePROSITE-ProRule annotationAdd
    BLAST
    Domaini1953 – 2067115RdRp catalyticPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi772 – 7743Cell attachment siteSequence Analysis

    Sequence similaritiesi

    Belongs to the picornaviruses polyprotein family.Curated
    Contains 2 peptidase C3 domains.Curated
    Contains 1 RdRp catalytic domain.PROSITE-ProRule annotation
    Contains 1 SF3 helicase domain.PROSITE-ProRule annotation

    Family and domain databases

    Gene3Di2.60.120.20. 2 hits.
    3.40.50.300. 1 hit.
    InterProiIPR004004. Helic/Pol/Pept_Calicivir-typ.
    IPR000605. Helicase_SF3_ssDNA/RNA_vir.
    IPR014759. Helicase_SF3_ssRNA_vir.
    IPR027417. P-loop_NTPase.
    IPR000199. Peptidase_C3A/C3B_picornavir.
    IPR001676. Picornavirus_capsid.
    IPR001205. RNA-dir_pol_C.
    IPR007094. RNA-dir_pol_PSvirus.
    IPR009003. Trypsin-like_Pept_dom.
    IPR029053. Viral_coat.
    IPR009419. VPP_parechovir_P3A.
    IPR009407. VPP_parechovir_P3B.
    [Graphical view]
    PfamiPF06344. Parecho_VpG. 1 hit.
    PF00548. Peptidase_C3. 1 hit.
    PF06363. Picorna_P3A. 1 hit.
    PF00680. RdRP_1. 1 hit.
    PF00073. Rhv. 2 hits.
    PF00910. RNA_helicase. 1 hit.
    [Graphical view]
    PRINTSiPR00918. CALICVIRUSNS.
    SUPFAMiSSF50494. SSF50494. 1 hit.
    SSF52540. SSF52540. 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.

    Q9YID8-1 [UniParc]FASTAAdd to Basket

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    METIKSIADM ATGFTNTIDS TVNAVTEGVS KIGNDSGGEI LTKVADDASN     50
    LLGPNCVAST SQPENKDVVQ ATTTVNTLTN LTQHPSAPTM PFTPDFSNVD 100
    VFHSMAYDIT TGDKNPSKLI RLDTTTWQHT WPRQHLINDV ELPKAFWDKN 150
    SKPAYGQSRY FAAVRCGFHF QVQINVNQGT AGCALVVYEP KPIVTHGGHL 200
    EFGSYTNLPH VLMNLAETTQ ADLCIPYVSD TNYVKTDSSD LGRLRVYVWT 250
    PLTIPSSATN DVDVTVLGSL LQLDFQNPRT YDTDVNIYDN SPLDTKTKYG 300
    KLRFSKKILS MSTKYKWTRN KIDIAEGPGS MNMANVLSTT GAQSIALVGE 350
    RAFYDPRTAG SKSRFGDMIH IAQLFSVMSD TTTPSTSSGI DDLGYLDWSA 400
    TYVPQQVIHR NVVKLNQFSN LKPFVNAYTY FRGSLVLRMS VYASTFNRGR 450
    LRMGFFPNFT TNTTSEMDNA IYTICDIGSD NSFEITIPYT FSTWMRKTNG 500
    RPIGLFQVEV LNRLTYNSSC PNKVHCIVQG RLGNDARFYC PTGSLVEFQN 550
    SWGSQMDLTD PLCVEDDEAE DCKQTISPDE LGLTSAQDDG PLGVEKPNYF 600
    LNFRAINVDI FTVSHTKVDN IFGRAWLALE HTFADDGTWR ADLNFPTQGH 650
    GTLTRLFTYY SGELNVHVLY LSDNGFLRVT HAYDHDNDRS NFLSSNGVIT 700
    VPAGEQMTLS VPFYSSKPLR TIRETGALGK LICKPLLSGT HSGKIEVYLS 750
    LRCPNLFFPS PAPKEKTSRA LRGDLANFID QSPYGQQQQT QMMKLAYLDR 800
    GFYKHYGIIV GGYVYQLDSD DIFKTALTGK ARFTKTRLTP DWIVEEECEL 850
    DYFRVKYLES SVNSEHIFSV DSNCETIAKD IFGTHTLSQH QAIGLVGAIL 900
    LTAGLMSTIK TPVNATTIKE FFNHAIDGDE QGLSLLVQKC TTFFSSAATE 950
    ILDNDLVKFI VKILVRILCY MVLYCHKPNI LTTACLSTLL IMDVTSSSVL 1000
    SPSCKALMQC LMDGDVKKLA EVVAESMSNT DDDEIKEQIC DTVKYTKTIL 1050
    SNQGPFKGFN EVSTAFRHVD WWIHTLLKIK DMVLSVFKPS IESKAIQWLE 1100
    RNKEHVCSIL DYASDIIVES KDQTKMKTQE FYQRYSDCLA KFKPIMAICF 1150
    RSCHNSISNT VYRLFQELAR IPNRISTQND LIRVEPIGVW IQGEPGQGKS 1200
    FLTHTLSRQL QKSCKLNGVY TNPTASEFMD GYDNQDIHLI DDLGQTRKEK 1250
    DIEMLCNCIS SVPFIVPMAH LEEKGKFYTS KLVIATTNKS DFSSTVLQDS 1300
    GALKRRFPYI MHIRAAKAYS KSGKLNVSQA MSTMSTGECW EVSKNGRDWE 1350
    TLKLKDLVQK ITEDYQERQK NYNAWKQQLE NQTLDDLDDA VSYIKHNFPD 1400
    AIPYIDEYLN IEMSTLIEQM EAFIEPRPSV FKCFAVKLPH KPGKQPRKLW 1450
    AGSAGKIKSM LSFIERNKAW LTVVSAVTSA ISILLLVTKI FKKEESKDER 1500
    AYNPTLPITK PKGTFPVSQR EFKNEAPYDG QLEHIISQMA YITGSTTGHL 1550
    THCAGYQHDE IILHGHSIKY LEQEEDLTLH YKNKVFPIEN PSVTQVTLGG 1600
    KPMDLAILKC KLPFRFKKNS KYYTNKIGTE SMLIWMTEQG IITKEVQRVH 1650
    HSGGIKTREG TESTKTISYT VKSCKGMCGG LLISKVEGNF KILGMHIAGN 1700
    GEMGVAIPFN FLKNDMSDQG IITEVTPIQP MYINTKSQIH KSPVYGAVEV 1750
    KMGPAVLSKS DTRLEEPVDC LIKKSASKYR VNKFQVNNEL WQGVKACVKS 1800
    KFREIFGVNG IVDMKTAILG TSHVNSMDLS TSAGYSLVKS GYKKKDLICL 1850
    EPFSVSPMLE KLVQDKFHNL LKGNQITTIF NTCLKDELRK LDKIAAGKTR 1900
    CIEACEVDYC IVYRMIMMEI YDKIYQTPCY YSGLAVGINP YKDWHFMINA 1950
    LNDYNYEMDY SQYDGSLSSM LLWEAVEVLA YCHDSPDLVM QLHKPVIDSD 2000
    HVVFNERWLI HGGMPSGSPC TTVLNSLCNL MMCIYTTNLI SPGVDCLPIV 2050
    YGDDVILSLD REIEPERLQS IMADSFGAEV TGSRKDEPPS LKPRMEVEFL 2100
    KRKPGYFPES TFIVGKLDTE NMIQHLMWMK NFSTFKQQLQ SYLMELCLHG 2150
    KDIYQRYIKI LDPYLKEWNI VVDDYDVVIA KLMPMVFD 2188
    Length:2,188
    Mass (Da):246,604
    Last modified:May 1, 1999 - v1
    Checksum:i02CC77D0A5ED3D93
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF055846 Genomic RNA. Translation: AAC79756.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF055846 Genomic RNA. Translation: AAC79756.1 .

    3D structure databases

    ProteinModelPortali Q9YID8.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 2.60.120.20. 2 hits.
    3.40.50.300. 1 hit.
    InterProi IPR004004. Helic/Pol/Pept_Calicivir-typ.
    IPR000605. Helicase_SF3_ssDNA/RNA_vir.
    IPR014759. Helicase_SF3_ssRNA_vir.
    IPR027417. P-loop_NTPase.
    IPR000199. Peptidase_C3A/C3B_picornavir.
    IPR001676. Picornavirus_capsid.
    IPR001205. RNA-dir_pol_C.
    IPR007094. RNA-dir_pol_PSvirus.
    IPR009003. Trypsin-like_Pept_dom.
    IPR029053. Viral_coat.
    IPR009419. VPP_parechovir_P3A.
    IPR009407. VPP_parechovir_P3B.
    [Graphical view ]
    Pfami PF06344. Parecho_VpG. 1 hit.
    PF00548. Peptidase_C3. 1 hit.
    PF06363. Picorna_P3A. 1 hit.
    PF00680. RdRP_1. 1 hit.
    PF00073. Rhv. 2 hits.
    PF00910. RNA_helicase. 1 hit.
    [Graphical view ]
    PRINTSi PR00918. CALICVIRUSNS.
    SUPFAMi SSF50494. SSF50494. 1 hit.
    SSF52540. SSF52540. 1 hit.
    PROSITEi PS50507. RDRP_SSRNA_POS. 1 hit.
    PS51218. SF3_HELICASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Complete sequence of echovirus 23 and its relationship to echovirus 22 and other human enteroviruses."
      Oberste M.S., Maher K., Pallansch M.A.
      Virus Res. 56:217-223(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    2. "Molecular analysis of human parechovirus type 2 (formerly echovirus 23)."
      Ghazi F., Hughes P.J., Hyypiae T., Stanway G.
      J. Gen. Virol. 79:2641-2650(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF PROTEIN 2A.

    Entry informationi

    Entry nameiPOLG_HPE23
    AccessioniPrimary (citable) accession number: Q9YID8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 109 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome

    Documents

    1. Peptidase families
      Classification of peptidase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3