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)

Q66578

- POLG_HPE1H

UniProt

Q66578 - POLG_HPE1H

Protein

Genome polyprotein

Gene
N/A
Organism
Human parechovirus 1 (strain Harris) (HPeV-1) (Echovirus 22)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Capsid proteins VP0, VP2, VP3 form a closed capsid enclosing the viral positive strand RNA genome. Capsid proteins interact with host alpha-V/beta-3 integrin heterodimer to provide virion attachment target cell. This attachment induces virion internalization predominantly through clathrin-mediated endocytosis.1 Publication
    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
    Sitei776 – 7772Cleavage; by protease 2ASequence Analysis
    Active sitei1550 – 15501For protease 3C activitySequence Analysis
    Active sitei1581 – 15811For protease 3C activitySequence Analysis
    Active sitei1670 – 16701For protease 3C activitySequence Analysis

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi1185 – 11928ATPPROSITE-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. clathrin-mediated endocytosis of virus by host cell Source: UniProtKB-KW
    2. induction by virus of host autophagy Source: UniProtKB
    3. pore formation by virus in membrane of host cell Source: UniProtKB-KW
    4. protein oligomerization Source: UniProtKB-KW
    5. RNA-protein covalent cross-linking Source: UniProtKB-KW
    6. suppression by virus of host RIG-I activity by RIG-I proteolysis Source: UniProtKB
    7. suppression by virus of host translation initiation factor activity Source: UniProtKB
    8. transcription, DNA-templated Source: InterPro
    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

    Clathrin-mediated endocytosis of virus by host, Host-virus interaction, Ion transport, Transport, Viral attachment to host cell, 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

    MEROPSiC03.023.

    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 1 (strain Harris) (HPeV-1) (Echovirus 22)
    Taxonomic identifieri103911 [NCBI]
    Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeParechovirus
    Virus hostiHomo sapiens (Human) [TaxID: 9606]
    Macaca (macaques) [TaxID: 9539]
    ProteomesiUP000002496: 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 – 289289Protein VP0Sequence AnalysisPRO_0000039730Add
    BLAST
    Chaini290 – 542253Protein VP3Sequence AnalysisPRO_0000039731Add
    BLAST
    Chaini543 – 776234Protein VP1Sequence AnalysisPRO_0000039732Add
    BLAST
    Chaini777 – 923147Protein 2ASequence AnalysisPRO_0000039733Add
    BLAST
    Chaini924 – 1045122Protein 2BSequence AnalysisPRO_0000039734Add
    BLAST
    Chaini1046 – 1374329Protein 2CSequence AnalysisPRO_0000039735Add
    BLAST
    Chaini1375 – 1491117Protein 3ASequence AnalysisPRO_0000039736Add
    BLAST
    Chaini1492 – 151120Protein 3BSequence AnalysisPRO_0000039737Add
    BLAST
    Chaini1512 – 1711200Protease 3CSequence AnalysisPRO_0000039738Add
    BLAST
    Chaini1712 – 2180469RNA-directed RNA polymerase 3D-POLSequence AnalysisPRO_0000039739Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1494 – 14941O-(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.
    The N-terminus of VP0 is blocked.

    Keywords - PTMi

    Covalent protein-RNA linkage, Lipoprotein, Myristate, Phosphoprotein

    Structurei

    3D structure databases

    ProteinModelPortaliQ66578.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1160 – 1318159SF3 helicasePROSITE-ProRule annotationAdd
    BLAST
    Domaini1945 – 2059115RdRp catalyticPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi764 – 7663Cell 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. 3 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. 1 hit.
    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.

    Q66578-1 [UniParc]FASTAAdd to Basket

    « Hide

    METIKSIADM ATGVVSSVDS TINAVNEKVE SVGNEIGGNL LTKVADDASN     50
    ILGPNCFATT AEPENKNVVQ ATTTVNTTNL TQHPSAPTMP FSPDFSNVDN 100
    FHSMAYDITT GDKNPSKLVR LETHEWTPSW ARGYQITHVE LPKVFWDHQD 150
    KPAYGQSRYF AAVRCGFHFQ VQVNVNQGTA GSALVVYEPK PVVTYDSKLE 200
    FGAFTNLPHV LMNLAETTQA DLCIPYVADT NYVKTDSSDL GQLKVYVWTP 250
    LSIPTGSANQ VDVTILGSLL QLDFQNPRVF AQDVNIYDNA PNGKKKNWKK 300
    IMTMSTKYKW TRTKIDIAEG PGSMNMANVL CTTGAQSVAL VGERAFYDPR 350
    TAGSKSRFDD LVKIAQLFSV MADSTTPSEN HGVDAKGYFK WSATTAPQSI 400
    VHRNIVYLRL FPNLNVFVNS YSYFRGSLVL RLSVYASTFN RGRLRMGFFP 450
    NATTDSTSTL DNAIYTICDI GSDNSFEITI PYSFSTWMRK TNGHPIGLFQ 500
    IEVLNRLTYN SSSPSEVYCI VQGKMGQDAR FFCPTGSVVT FQNSWGSQMD 550
    LTDPLCIEDD TENCKQTMSP NELGLTSAQD DGPLGQEKPN YFLNFRSMNV 600
    DIFTVSHTKV DNLFGRAWFF MEHTFTNEGQ WRVPLEFPKQ GHGSLSLLFA 650
    YFTGELNIHV LFLSERGFLR VAHTYDTSND RVNFLSSNGV ITVPAGEQMT 700
    LSAPYYSNKP LRTVRDNNSL GYLMCKPFLT GTSTGKIEVY LSLRCPNFFF 750
    PLPAPKVTSS RALRGDMANL TNQSPYGQQP QNRMMKLAYL DRGFYKHYGI 800
    IVGDHVYQLD SDDIFKTALT GKAKFTKTKL TSDWVIEEEC ELDYFRIKYL 850
    ESAVDSEHIF SVDKNCETIA KDIFGTHTLS QHQAIGLVGT ILLTAGLMST 900
    IKTPVNAVTI KEFFNHAIDG DEQGLSLLVQ KCTTFFSSAA TEILDNDLVK 950
    FIVKILVRIL CYMVLYCHKP NILTTACLST LLIMDVTSSS VLSPSCKALM 1000
    QCLMDGDVKK LAEIVAESMS NTDDDEVKEQ ICDTVKYTKT ILSNQGPFKG 1050
    FNEVSTAFRH IDWWIHTLLK IKDMVLSVFK PSIESKAIQW LERNKEHVCS 1100
    ILDYASDIIV ESKDQSKMKT QDFYQRYSDC LAKFKPIMAI CFRSCHNSIS 1150
    NTVYRLFQEL ARIPNRISTN NDLIRIEPIG IWIQGEPGQG KSFLTHTLSR 1200
    QLQKSCKLNG VFTNPTASEF MDGYDNQDIH LIDDLGQTRK EKDIEMLCNC 1250
    ISSVPFIVPM AHLEEKGKFY TSKLVVATTN KSDFSSTVLQ DSGALKRRFP 1300
    YIMHIRAAKA YSKAGKLNVS QAMATMSTGE CWEVSKNGRD WETLKLKDLV 1350
    DKITIDYNER VKNYNAWKQQ LENQTLDDLD DAVSYIKHNF PDAIPYVDEY 1400
    LNIEMSTLIE QMEAFIEPKP SVFKCFANKI GSKISKASRE VVDWFSDKIK 1450
    SMLSFVERNK AWLTVVSAVT SAISILLLVT KIFKKEESKD ERAYNPTLPV 1500
    AKPKGTFPVS QREFKNEAPY DGQLEHIISQ MAYITGSTTG HMTHCAGYQH 1550
    DEIILHGHSI KYLEQEDELT LHYKNKVFPI EQPSVTQVTL GGKPMDLAIL 1600
    KCKLPFRFKK NSKYYTNKIG TESMLIWMTE QGIITKEVQR VHHSGGIKTR 1650
    EGTESTKTIS YTVKSCKGMC GGLLISKVEG NFKILGMHIA GNGEMGVAIP 1700
    FNFLKNDMSD QGIVTEITPI QPMYINTKTQ IHKSPVYGAV EVKMGPAVLS 1750
    KSDTRLEEPV ECLIKKSASK YRVNKFQVNN ELWQGVKACV KSKFREIFGM 1800
    NGIVDMKTAI LGTSHVNSMD LSTSAGYSFV KSGYKKKDLI CLEPFSVAPL 1850
    LERLVQDKFH NLLKGNQITT TFNTCLKDEL RKLDKIASGK TRCIEACEVD 1900
    YCIVYRMIMM EIYDKIYQTP CYYSGLAVGI NPYKDWHFMI NALNDYNYEM 1950
    DYSQYDGSLS SMLLWEAVEV LAYCHDSPDL VMQLHKPVID SDHVVFNERW 2000
    LIHGGMPSGS PCTTVLNSLC NLMMCIYTTN LISPGIDCLP IVYGDDVILS 2050
    LDKEIEPEKL QSIMADSFGA EVTGSRKDEP PSLKPRMEVE FLKRKPGYFP 2100
    ESTFIVGKLD TENMIQHLMW MKNFSTFKQQ LQSYLMELCL HGKDTYQHYI 2150
    KILEPYLQEW NITVDDYDVV ITKLMPMVFD 2180
    Length:2,180
    Mass (Da):245,844
    Last modified:November 1, 1996 - v1
    Checksum:i3A5F1DAC43C12DEE
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L02971 Genomic RNA. Translation: AAA72291.1.
    S45208 Genomic RNA. Translation: AAB23363.1.
    PIRiA46182.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L02971 Genomic RNA. Translation: AAA72291.1 .
    S45208 Genomic RNA. Translation: AAB23363.1 .
    PIRi A46182.

    3D structure databases

    ProteinModelPortali Q66578.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi C03.023.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 2.60.120.20. 3 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. 1 hit.
    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. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA], PROTEIN SEQUENCE OF 29-61; 67-80; 290-297 AND 543-551.
    2. "Molecular and biological characteristics of echovirus 22, a representative of a new picornavirus group."
      Stanway G., Kalkinnen N., Roivainen M., Ghazi F., Khan M., Smyth M., Meurman O., Hyppiae T.
      J. Virol. 68:8232-8238(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 6-22; 29-61; 67-80 AND 118-131.
    3. Cited for: FUNCTION OF CAPSID PROTEINS.

    Entry informationi

    Entry nameiPOLG_HPE1H
    AccessioniPrimary (citable) accession number: Q66578
    Secondary accession number(s): Q90062
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 116 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, Direct protein sequencing

    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