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Q66578 (POLG_HPE1H) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Genome polyprotein

Cleaved into the following 10 chains:

  1. Protein VP0
    Alternative name(s):
    P1AB
    Virion protein 0
  2. Protein VP3
    Alternative name(s):
    P1C
    Virion protein 3
  3. Protein VP1
    Alternative name(s):
    P1D
    Virion protein 1
  4. Protein 2A
    Short name=P2A
  5. Protein 2B
    Short name=P2B
  6. Protein 2C
    Short name=P2C
    EC=3.6.1.15
  7. Protein 3A
    Short name=P3A
  8. Protein 3B
    Short name=P3B
    Alternative name(s):
    VPg
  9. Protease 3C
    Short name=P3C
    EC=3.4.22.28
    Alternative name(s):
    Picornain 3C
  10. RNA-directed RNA polymerase 3D-POL
    Short name=P3D-POL
    EC=2.7.7.48
OrganismHuman parechovirus 1 (strain Harris) (HPeV-1) (Echovirus 22) [Complete proteome]
Taxonomic identifier103911 [NCBI]
Taxonomic lineageVirusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeParechovirus
Virus hostHomo sapiens (Human) [TaxID: 9606]
Macaca (macaques) [TaxID: 9539]

Protein attributes

Sequence length2180 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.3

Protein 2A: Is not a protease By similarity. Ref.3

Protein 2B: Affects membrane integrity and cause an increase in membrane permeability By similarity. Ref.3

Protein 2C: Associates with and induces structural rearrangements of intracellular membranes. It displays RNA-binding, nucleotide binding and NTPase activities By similarity. Ref.3

Protein 3A, via its hydrophobic domain, serves as membrane anchor By similarity. Ref.3

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. Ref.3

RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals By similarity. Ref.3

Catalytic activity

Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).

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.

Subcellular location

Protein VP3: Virion By similarity. Host cytoplasm Potential.

Protein VP1: Virion By similarity. Host cytoplasm Potential.

Protein 2B: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Potential. 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.

Protein 2C: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Potential. 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.

Protein 3A: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Potential. 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.

Protein 3B: Virion Potential.

Protease 3C: Host cytoplasm Potential.

RNA-directed RNA polymerase 3D-POL: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Potential. 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.

Post-translational modification

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.

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

The N-terminus of VP0 is blocked.

Sequence similarities

Belongs to the picornaviruses polyprotein family.

Contains 2 peptidase C3 domains.

Contains 1 RdRp catalytic domain.

Contains 1 SF3 helicase domain.

Ontologies

Keywords
   Biological processClathrin-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
   Cellular componentCapsid protein
Host cytoplasm
Host cytoplasmic vesicle
Host membrane
Membrane
Virion
   LigandATP-binding
Nucleotide-binding
RNA-binding
   Molecular functionHelicase
Hydrolase
Ion channel
Nucleotidyltransferase
Protease
RNA-directed RNA polymerase
Thiol protease
Transferase
Viral ion channel
   PTMCovalent protein-RNA linkage
Lipoprotein
Myristate
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological_processRNA-protein covalent cross-linking

Inferred from electronic annotation. Source: UniProtKB-KW

clathrin-mediated endocytosis of virus by host cell

Inferred from electronic annotation. Source: UniProtKB-KW

pore formation by virus in membrane of host cell

Inferred from electronic annotation. Source: UniProtKB-KW

protein oligomerization

Inferred from electronic annotation. Source: UniProtKB-KW

proteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: InterPro

viral RNA genome replication

Inferred from electronic annotation. Source: InterPro

virion attachment to host cell

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componenthost cell cytoplasmic vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral to membrane of host cell

Inferred from electronic annotation. Source: UniProtKB-KW

membrane

Inferred from electronic annotation. Source: UniProtKB-KW

viral capsid

Inferred from electronic annotation. Source: UniProtKB-KW

viral genome

Inferred from electronic annotation. Source: InterPro

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA helicase activity

Inferred from electronic annotation. Source: InterPro

RNA-directed RNA polymerase activity

Inferred from electronic annotation. Source: UniProtKB-KW

cysteine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

ion channel activity

Inferred from electronic annotation. Source: UniProtKB-KW

structural molecule activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 289289Protein VP0 Potential
PRO_0000039730
Chain290 – 542253Protein VP3 Potential
PRO_0000039731
Chain543 – 776234Protein VP1 Potential
PRO_0000039732
Chain777 – 923147Protein 2A Potential
PRO_0000039733
Chain924 – 1045122Protein 2B Potential
PRO_0000039734
Chain1046 – 1374329Protein 2C Potential
PRO_0000039735
Chain1375 – 1491117Protein 3A Potential
PRO_0000039736
Chain1492 – 151120Protein 3B Potential
PRO_0000039737
Chain1512 – 1711200Protease 3C Potential
PRO_0000039738
Chain1712 – 2180469RNA-directed RNA polymerase 3D-POL Potential
PRO_0000039739

Regions

Domain1160 – 1318159SF3 helicase
Domain1945 – 2059115RdRp catalytic
Nucleotide binding1185 – 11928ATP Potential
Motif764 – 7663Cell attachment site Potential

Sites

Active site15501For protease 3C activity Potential
Active site15811For protease 3C activity Potential
Active site16701For protease 3C activity Potential
Site776 – 7772Cleavage; by protease 2A Potential

Amino acid modifications

Modified residue14941O-(5'-phospho-RNA)-tyrosine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q66578 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 3A5F1DAC43C12DEE

FASTA2,180245,844
        10         20         30         40         50         60 
METIKSIADM ATGVVSSVDS TINAVNEKVE SVGNEIGGNL LTKVADDASN ILGPNCFATT 

        70         80         90        100        110        120 
AEPENKNVVQ ATTTVNTTNL TQHPSAPTMP FSPDFSNVDN FHSMAYDITT GDKNPSKLVR 

       130        140        150        160        170        180 
LETHEWTPSW ARGYQITHVE LPKVFWDHQD KPAYGQSRYF AAVRCGFHFQ VQVNVNQGTA 

       190        200        210        220        230        240 
GSALVVYEPK PVVTYDSKLE FGAFTNLPHV LMNLAETTQA DLCIPYVADT NYVKTDSSDL 

       250        260        270        280        290        300 
GQLKVYVWTP LSIPTGSANQ VDVTILGSLL QLDFQNPRVF AQDVNIYDNA PNGKKKNWKK 

       310        320        330        340        350        360 
IMTMSTKYKW TRTKIDIAEG PGSMNMANVL CTTGAQSVAL VGERAFYDPR TAGSKSRFDD 

       370        380        390        400        410        420 
LVKIAQLFSV MADSTTPSEN HGVDAKGYFK WSATTAPQSI VHRNIVYLRL FPNLNVFVNS 

       430        440        450        460        470        480 
YSYFRGSLVL RLSVYASTFN RGRLRMGFFP NATTDSTSTL DNAIYTICDI GSDNSFEITI 

       490        500        510        520        530        540 
PYSFSTWMRK TNGHPIGLFQ IEVLNRLTYN SSSPSEVYCI VQGKMGQDAR FFCPTGSVVT 

       550        560        570        580        590        600 
FQNSWGSQMD LTDPLCIEDD TENCKQTMSP NELGLTSAQD DGPLGQEKPN YFLNFRSMNV 

       610        620        630        640        650        660 
DIFTVSHTKV DNLFGRAWFF MEHTFTNEGQ WRVPLEFPKQ GHGSLSLLFA YFTGELNIHV 

       670        680        690        700        710        720 
LFLSERGFLR VAHTYDTSND RVNFLSSNGV ITVPAGEQMT LSAPYYSNKP LRTVRDNNSL 

       730        740        750        760        770        780 
GYLMCKPFLT GTSTGKIEVY LSLRCPNFFF PLPAPKVTSS RALRGDMANL TNQSPYGQQP 

       790        800        810        820        830        840 
QNRMMKLAYL DRGFYKHYGI IVGDHVYQLD SDDIFKTALT GKAKFTKTKL TSDWVIEEEC 

       850        860        870        880        890        900 
ELDYFRIKYL ESAVDSEHIF SVDKNCETIA KDIFGTHTLS QHQAIGLVGT ILLTAGLMST 

       910        920        930        940        950        960 
IKTPVNAVTI KEFFNHAIDG DEQGLSLLVQ KCTTFFSSAA TEILDNDLVK FIVKILVRIL 

       970        980        990       1000       1010       1020 
CYMVLYCHKP NILTTACLST LLIMDVTSSS VLSPSCKALM QCLMDGDVKK LAEIVAESMS 

      1030       1040       1050       1060       1070       1080 
NTDDDEVKEQ ICDTVKYTKT ILSNQGPFKG FNEVSTAFRH IDWWIHTLLK IKDMVLSVFK 

      1090       1100       1110       1120       1130       1140 
PSIESKAIQW LERNKEHVCS ILDYASDIIV ESKDQSKMKT QDFYQRYSDC LAKFKPIMAI 

      1150       1160       1170       1180       1190       1200 
CFRSCHNSIS NTVYRLFQEL ARIPNRISTN NDLIRIEPIG IWIQGEPGQG KSFLTHTLSR 

      1210       1220       1230       1240       1250       1260 
QLQKSCKLNG VFTNPTASEF MDGYDNQDIH LIDDLGQTRK EKDIEMLCNC ISSVPFIVPM 

      1270       1280       1290       1300       1310       1320 
AHLEEKGKFY TSKLVVATTN KSDFSSTVLQ DSGALKRRFP YIMHIRAAKA YSKAGKLNVS 

      1330       1340       1350       1360       1370       1380 
QAMATMSTGE CWEVSKNGRD WETLKLKDLV DKITIDYNER VKNYNAWKQQ LENQTLDDLD 

      1390       1400       1410       1420       1430       1440 
DAVSYIKHNF PDAIPYVDEY LNIEMSTLIE QMEAFIEPKP SVFKCFANKI GSKISKASRE 

      1450       1460       1470       1480       1490       1500 
VVDWFSDKIK SMLSFVERNK AWLTVVSAVT SAISILLLVT KIFKKEESKD ERAYNPTLPV 

      1510       1520       1530       1540       1550       1560 
AKPKGTFPVS QREFKNEAPY DGQLEHIISQ MAYITGSTTG HMTHCAGYQH DEIILHGHSI 

      1570       1580       1590       1600       1610       1620 
KYLEQEDELT LHYKNKVFPI EQPSVTQVTL GGKPMDLAIL KCKLPFRFKK NSKYYTNKIG 

      1630       1640       1650       1660       1670       1680 
TESMLIWMTE QGIITKEVQR VHHSGGIKTR EGTESTKTIS YTVKSCKGMC GGLLISKVEG 

      1690       1700       1710       1720       1730       1740 
NFKILGMHIA GNGEMGVAIP FNFLKNDMSD QGIVTEITPI QPMYINTKTQ IHKSPVYGAV 

      1750       1760       1770       1780       1790       1800 
EVKMGPAVLS KSDTRLEEPV ECLIKKSASK YRVNKFQVNN ELWQGVKACV KSKFREIFGM 

      1810       1820       1830       1840       1850       1860 
NGIVDMKTAI LGTSHVNSMD LSTSAGYSFV KSGYKKKDLI CLEPFSVAPL LERLVQDKFH 

      1870       1880       1890       1900       1910       1920 
NLLKGNQITT TFNTCLKDEL RKLDKIASGK TRCIEACEVD YCIVYRMIMM EIYDKIYQTP 

      1930       1940       1950       1960       1970       1980 
CYYSGLAVGI NPYKDWHFMI NALNDYNYEM DYSQYDGSLS SMLLWEAVEV LAYCHDSPDL 

      1990       2000       2010       2020       2030       2040 
VMQLHKPVID SDHVVFNERW LIHGGMPSGS PCTTVLNSLC NLMMCIYTTN LISPGIDCLP 

      2050       2060       2070       2080       2090       2100 
IVYGDDVILS LDKEIEPEKL QSIMADSFGA EVTGSRKDEP PSLKPRMEVE FLKRKPGYFP 

      2110       2120       2130       2140       2150       2160 
ESTFIVGKLD TENMIQHLMW MKNFSTFKQQ LQSYLMELCL HGKDTYQHYI KILEPYLQEW 

      2170       2180 
NITVDDYDVV ITKLMPMVFD 

« Hide

References

[1]"A distinct picornavirus group identified by sequence analysis."
Hyypiae T., Horsnell C., Maaronen M., Khan M., Kalkkinen N., Auvinen P., Kinnunen L., Stanway G.
Proc. Natl. Acad. Sci. U.S.A. 89:8847-8851(1992) [PubMed] [Europe PMC] [Abstract]
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]"Entry of human parechovirus 1."
Joki-Korpela P., Marjomaki V., Krogerus C., Heino J., Hyypia T.
J. Virol. 75:1958-1967(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF CAPSID PROTEINS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L02971 Genomic RNA. Translation: AAA72291.1.
S45208 Genomic RNA. Translation: AAB23363.1.
PIRA46182.

3D structure databases

ProteinModelPortalQ66578.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSC03.023.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR004004. 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.
IPR009419. VPP_parechovir_P3A.
IPR009407. VPP_parechovir_P3B.
[Graphical view]
PfamPF06344. 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]
PRINTSPR00918. CALICVIRUSNS.
SUPFAMSSF50494. SSF50494. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEPS50507. RDRP_SSRNA_POS. 1 hit.
PS51218. SF3_HELICASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePOLG_HPE1H
AccessionPrimary (citable) accession number: Q66578
Secondary accession number(s): Q90062
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries