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Q9YID8 (POLG_HPE23) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 108. 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 2 (strain CT86-6760) (HPeV-2) (Echovirus 23) [Complete proteome]
Taxonomic identifier122961 [NCBI]
Taxonomic lineageVirusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeParechovirus
Virus hostHomo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length2188 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

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

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

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

Protein 3A, via its hydrophobic domain, serves as membrane anchor By similarity. Ref.2

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.2

RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals By similarity. Ref.2

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.

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 processHost-virus interaction
Ion transport
Transport
Viral attachment to host cell
Viral RNA replication
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
Gene Ontology (GO)
   Biological_processRNA-protein covalent cross-linking

Inferred from electronic annotation. Source: UniProtKB-KW

induction by virus of host autophagy

Inferred from sequence or structural similarity. Source: UniProtKB

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

suppression by virus of host RIG-I activity by RIG-I proteolysis

Inferred from sequence or structural similarity. Source: UniProtKB

suppression by virus of host translation initiation factor activity

Inferred from sequence or structural similarity. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: InterPro

viral RNA genome replication

Inferred from electronic annotation. Source: InterPro

viral entry into host cell

Inferred from electronic annotation. Source: UniProtKB-KW

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 – 290290Protein VP0 Potential
PRO_0000039740
Chain291 – 549259Protein VP3 Potential
PRO_0000039741
Chain550 – 784235Protein VP1 Potential
PRO_0000039742
Chain785 – 931147Protein 2A Potential
PRO_0000039743
Chain932 – 1053122Protein 2B Potential
PRO_0000039744
Chain1054 – 1382329Protein 2C Potential
PRO_0000039745
Chain1383 – 1499117Protein 3A Potential
PRO_0000039747
Chain1500 – 151920Protein 3B By similarity
PRO_0000311174
Chain1520 – 1719200Protease 3C Potential
PRO_0000039748
Chain1720 – 2188469RNA-directed RNA polymerase 3D-POL Potential
PRO_0000039749

Regions

Domain1165 – 1326162SF3 helicase
Domain1953 – 2067115RdRp catalytic
Nucleotide binding1193 – 12008ATP Potential
Motif772 – 7743Cell attachment site Potential

Sites

Active site15581For protease 3C activity Potential
Active site15891For protease 3C activity Potential
Active site16781For protease 3C activity Potential
Site784 – 7852Cleavage; by protease 2A Potential

Amino acid modifications

Modified residue15021O-(5'-phospho-RNA)-tyrosine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9YID8 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 02CC77D0A5ED3D93

FASTA2,188246,604
        10         20         30         40         50         60 
METIKSIADM ATGFTNTIDS TVNAVTEGVS KIGNDSGGEI LTKVADDASN LLGPNCVAST 

        70         80         90        100        110        120 
SQPENKDVVQ ATTTVNTLTN LTQHPSAPTM PFTPDFSNVD VFHSMAYDIT TGDKNPSKLI 

       130        140        150        160        170        180 
RLDTTTWQHT WPRQHLINDV ELPKAFWDKN SKPAYGQSRY FAAVRCGFHF QVQINVNQGT 

       190        200        210        220        230        240 
AGCALVVYEP KPIVTHGGHL EFGSYTNLPH VLMNLAETTQ ADLCIPYVSD TNYVKTDSSD 

       250        260        270        280        290        300 
LGRLRVYVWT PLTIPSSATN DVDVTVLGSL LQLDFQNPRT YDTDVNIYDN SPLDTKTKYG 

       310        320        330        340        350        360 
KLRFSKKILS MSTKYKWTRN KIDIAEGPGS MNMANVLSTT GAQSIALVGE RAFYDPRTAG 

       370        380        390        400        410        420 
SKSRFGDMIH IAQLFSVMSD TTTPSTSSGI DDLGYLDWSA TYVPQQVIHR NVVKLNQFSN 

       430        440        450        460        470        480 
LKPFVNAYTY FRGSLVLRMS VYASTFNRGR LRMGFFPNFT TNTTSEMDNA IYTICDIGSD 

       490        500        510        520        530        540 
NSFEITIPYT FSTWMRKTNG RPIGLFQVEV LNRLTYNSSC PNKVHCIVQG RLGNDARFYC 

       550        560        570        580        590        600 
PTGSLVEFQN SWGSQMDLTD PLCVEDDEAE DCKQTISPDE LGLTSAQDDG PLGVEKPNYF 

       610        620        630        640        650        660 
LNFRAINVDI FTVSHTKVDN IFGRAWLALE HTFADDGTWR ADLNFPTQGH GTLTRLFTYY 

       670        680        690        700        710        720 
SGELNVHVLY LSDNGFLRVT HAYDHDNDRS NFLSSNGVIT VPAGEQMTLS VPFYSSKPLR 

       730        740        750        760        770        780 
TIRETGALGK LICKPLLSGT HSGKIEVYLS LRCPNLFFPS PAPKEKTSRA LRGDLANFID 

       790        800        810        820        830        840 
QSPYGQQQQT QMMKLAYLDR GFYKHYGIIV GGYVYQLDSD DIFKTALTGK ARFTKTRLTP 

       850        860        870        880        890        900 
DWIVEEECEL DYFRVKYLES SVNSEHIFSV DSNCETIAKD IFGTHTLSQH QAIGLVGAIL 

       910        920        930        940        950        960 
LTAGLMSTIK TPVNATTIKE FFNHAIDGDE QGLSLLVQKC TTFFSSAATE ILDNDLVKFI 

       970        980        990       1000       1010       1020 
VKILVRILCY MVLYCHKPNI LTTACLSTLL IMDVTSSSVL SPSCKALMQC LMDGDVKKLA 

      1030       1040       1050       1060       1070       1080 
EVVAESMSNT DDDEIKEQIC DTVKYTKTIL SNQGPFKGFN EVSTAFRHVD WWIHTLLKIK 

      1090       1100       1110       1120       1130       1140 
DMVLSVFKPS IESKAIQWLE RNKEHVCSIL DYASDIIVES KDQTKMKTQE FYQRYSDCLA 

      1150       1160       1170       1180       1190       1200 
KFKPIMAICF RSCHNSISNT VYRLFQELAR IPNRISTQND LIRVEPIGVW IQGEPGQGKS 

      1210       1220       1230       1240       1250       1260 
FLTHTLSRQL QKSCKLNGVY TNPTASEFMD GYDNQDIHLI DDLGQTRKEK DIEMLCNCIS 

      1270       1280       1290       1300       1310       1320 
SVPFIVPMAH LEEKGKFYTS KLVIATTNKS DFSSTVLQDS GALKRRFPYI MHIRAAKAYS 

      1330       1340       1350       1360       1370       1380 
KSGKLNVSQA MSTMSTGECW EVSKNGRDWE TLKLKDLVQK ITEDYQERQK NYNAWKQQLE 

      1390       1400       1410       1420       1430       1440 
NQTLDDLDDA VSYIKHNFPD AIPYIDEYLN IEMSTLIEQM EAFIEPRPSV FKCFAVKLPH 

      1450       1460       1470       1480       1490       1500 
KPGKQPRKLW AGSAGKIKSM LSFIERNKAW LTVVSAVTSA ISILLLVTKI FKKEESKDER 

      1510       1520       1530       1540       1550       1560 
AYNPTLPITK PKGTFPVSQR EFKNEAPYDG QLEHIISQMA YITGSTTGHL THCAGYQHDE 

      1570       1580       1590       1600       1610       1620 
IILHGHSIKY LEQEEDLTLH YKNKVFPIEN PSVTQVTLGG KPMDLAILKC KLPFRFKKNS 

      1630       1640       1650       1660       1670       1680 
KYYTNKIGTE SMLIWMTEQG IITKEVQRVH HSGGIKTREG TESTKTISYT VKSCKGMCGG 

      1690       1700       1710       1720       1730       1740 
LLISKVEGNF KILGMHIAGN GEMGVAIPFN FLKNDMSDQG IITEVTPIQP MYINTKSQIH 

      1750       1760       1770       1780       1790       1800 
KSPVYGAVEV KMGPAVLSKS DTRLEEPVDC LIKKSASKYR VNKFQVNNEL WQGVKACVKS 

      1810       1820       1830       1840       1850       1860 
KFREIFGVNG IVDMKTAILG TSHVNSMDLS TSAGYSLVKS GYKKKDLICL EPFSVSPMLE 

      1870       1880       1890       1900       1910       1920 
KLVQDKFHNL LKGNQITTIF NTCLKDELRK LDKIAAGKTR CIEACEVDYC IVYRMIMMEI 

      1930       1940       1950       1960       1970       1980 
YDKIYQTPCY YSGLAVGINP YKDWHFMINA LNDYNYEMDY SQYDGSLSSM LLWEAVEVLA 

      1990       2000       2010       2020       2030       2040 
YCHDSPDLVM QLHKPVIDSD HVVFNERWLI HGGMPSGSPC TTVLNSLCNL MMCIYTTNLI 

      2050       2060       2070       2080       2090       2100 
SPGVDCLPIV YGDDVILSLD REIEPERLQS IMADSFGAEV TGSRKDEPPS LKPRMEVEFL 

      2110       2120       2130       2140       2150       2160 
KRKPGYFPES TFIVGKLDTE NMIQHLMWMK NFSTFKQQLQ SYLMELCLHG KDIYQRYIKI 

      2170       2180 
LDPYLKEWNI VVDDYDVVIA KLMPMVFD 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF055846 Genomic RNA. Translation: AAC79756.1.

3D structure databases

ProteinModelPortalQ9YID8.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.60.120.20. 2 hits.
3.40.50.300. 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.
IPR029053. Viral_coat.
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. 2 hits.
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_HPE23
AccessionPrimary (citable) accession number: Q9YID8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1999
Last modified: July 9, 2014
This is version 108 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