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O73556 (POLG_HPE2W) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 113. 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 Williamson) (HPeV-2) (Echovirus 23) [Reference proteome]
Taxonomic identifier122962 [NCBI]
Taxonomic lineageVirusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeParechovirus
Virus hostHomo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length2179 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.

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.

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.

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

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
Reference 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 – 289289Protein VP0 Potential
PRO_0000039750
Chain290 – 542253Protein VP3 Potential
PRO_0000039751
Chain543 – 775233Protein VP1 Potential
PRO_0000039752
Chain776 – 922147Protein 2A Potential
PRO_0000039753
Chain923 – 1044122Protein 2B Potential
PRO_0000039754
Chain1045 – 1373329Protein 2C Potential
PRO_0000039755
Chain1374 – 1490117Protein 3A Potential
PRO_0000039756
Chain1491 – 151020Protein 3B Potential
PRO_0000039757
Chain1511 – 1710200Protease 3C Potential
PRO_0000039758
Chain1711 – 2179469RNA-directed RNA polymerase 3D-POL Potential
PRO_0000039759

Regions

Domain1156 – 1317162SF3 helicase
Domain1944 – 2058115RdRp catalytic
Nucleotide binding1184 – 11918ATP Potential
Motif763 – 7653Cell attachment site Potential

Sites

Active site15491For protease 3C activity Potential
Active site15801For protease 3C activity Potential
Active site16691For protease 3C activity Potential
Site775 – 7762Cleavage; by protease 2A Potential

Amino acid modifications

Modified residue14931O-(5'-phospho-RNA)-tyrosine By similarity

Sequences

Sequence LengthMass (Da)Tools
O73556 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 96803C0BB8856664

FASTA2,179245,874
        10         20         30         40         50         60 
METIKSIADM ATGVTKTIDA TINSVNEIIT NTDNASGGDI LTKVADDASN ILGPNCYATT 

        70         80         90        100        110        120 
SEPENKDVVQ ATTTVNTTNL TQHPSAPTLP FTPDFSNVDT FHSMAYDTTT GSKNPNKLVR 

       130        140        150        160        170        180 
LTTHAWASTL QRGHQIDHVN LPVDFWDEQR KPAYGHAKYF AAVRCGFHFQ VQVNVNQGTA 

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

       250        260        270        280        290        300 
GQLKVYVWTP LSIPSGSSNQ VDVTILGSLL QLDFQNPRVY GQNVDIYDTA PSKPIPLRKT 

       310        320        330        340        350        360 
KYLTMSTKYK WTRNKVDIAE GPGSMNMANV LSTTAAQSVA LVGERAFYDP RTAGSKSRFD 

       370        380        390        400        410        420 
DLVKISQLFS VMADSTTPSA NHGIDQKGYF KWSANSDPQA IVHRNLVHLN LFPNLKVFEN 

       430        440        450        460        470        480 
SYSYFRGSLI IRLSVYASTF NRGRLNGFFP NSSTDETSEI DNAIYTICDI GSDNSFEITI 

       490        500        510        520        530        540 
PYSFSTWMRK THGKPIGLFQ IEVLNRLTYN YSSPNEVYCI VQGKMGQDAK FFCPTGSLVT 

       550        560        570        580        590        600 
FQNSWGSQMD LTDPLCIEDS VEDCKQTITP TELGLTSAQD DGPLGNDKPN YFLNFKSMNV 

       610        620        630        640        650        660 
DIFTVSHTKV DNIFGRAWFA HVHDFTNDGL WRQGLEFPKE GHGALSLLFA YFTGELNIHV 

       670        680        690        700        710        720 
LFLSDRGFLR VGHTYDTETN RTNFLSSSGI ITVPAGEQMT LSVPSYSNKP LRTVRSSNAL 

       730        740        750        760        770        780 
GYLLCKPLLT GTSSGRIEIF LSLRCPNFFF PLPAPKPATR KYRGDLATWS DQSPYGRQGK 

       790        800        810        820        830        840 
KQLMKLAYLD RGFYKHYGIV VGDDVYQLDS DDIFKTALTG KAKFTKTRLT PDWVVEEECE 

       850        860        870        880        890        900 
LDYFRIKYLE SSVNSEHIFS VDNNCETIAK DIFGSHSLSQ HQQIGLIGTI LLTAGLMSTI 

       910        920        930        940        950        960 
KTPVNPTTIK EFFNHAIEGD EQGLSLLVQK CTTFFSSAAT ELLDNDLVKF IIKILVRILC 

       970        980        990       1000       1010       1020 
YMVLYCHKPN ILTTACLSTL LVMDVTSSSV LSPSCKALMQ CLMDGDVKKL AEVVAESMSN 

      1030       1040       1050       1060       1070       1080 
TDDDEIKEQI CDTVKYTKQI LSNQGPFKGF NEISTAFRHI DWWIQTLLKI KDMVLSVFKP 

      1090       1100       1110       1120       1130       1140 
SVEKRAVEWL ERNKEHVCSI LDYASDIIVK SKDQTKMKTQ EFYQRYNDCL SKFKPIMAMC 

      1150       1160       1170       1180       1190       1200 
FRSCHNSISN TVYRLFQELA RIPNRMATQN DLIRVEPIGI WIQGEPGQGK SFLTHTLSKQ 

      1210       1220       1230       1240       1250       1260 
LQKTCGLQGI YTNPTASEFM DGYDNQDIHL IDDLGQTRKE RDIEMLCNCI SSDPDIVPMA 

      1270       1280       1290       1300       1310       1320 
HLEEKGKFYT SKLVIATTNK PDFSSTVLLD SGALRRRFPY IMHIRAAKHY SKSGKLNVSQ 

      1330       1340       1350       1360       1370       1380 
AMPHMSTGEC WEVSKNGRDW ETLKLKELID KITVDYKERI ANYNTWKKQL EDQTLDDLDD 

      1390       1400       1410       1420       1430       1440 
AVSYIKHNYP DAIPYIDEYL NIEMSTLIEQ MEAFIEPKPS VFKCFASRVG DKIKEASREV 

      1450       1460       1470       1480       1490       1500 
VKWFSDKLKS MLNFVERNKA WLTVVSAVTS AIGILLLVTK IFKKEESKDE RAYNPTLPVA 

      1510       1520       1530       1540       1550       1560 
KPKGTFPVSQ REFKNEAPYD GQLEHIISQM AYITGSTTGH ITHCAGYQHD EIILHGHSIK 

      1570       1580       1590       1600       1610       1620 
YLEQEEELTL HYKNKVFPIE QPSVTQVTLG GKPMDLAIVK CKLPFRFKKN SKYYTNKIGT 

      1630       1640       1650       1660       1670       1680 
ESMLIWMTEQ GIITKEVQRV HHSGGIKTRE GTESTKTISY TVKSCKGMCG GLLISKVEGN 

      1690       1700       1710       1720       1730       1740 
FKILGMHIAG NGEMGVAIPF NFLKNDMSDQ GIVTEVTPIQ PMYINTKSQI HKSPVYGAVE 

      1750       1760       1770       1780       1790       1800 
VKMGPAVLSK SDTRLEEPVD CLVKKSASKY RVNKFQVNNE LWQGVKACVK SKFREIFGVN 

      1810       1820       1830       1840       1850       1860 
GIVDMKTAIL GTSHVNSMDL STSAGYSFVK SGYKKKDLIC LEPFSVSPML EKLVQEKFHN 

      1870       1880       1890       1900       1910       1920 
LLKGNQITTI FNTCLKDELR KLDKIATGKT RCIEACEIDY CIVYRMIMME IYDKIYQTPC 

      1930       1940       1950       1960       1970       1980 
YYSGLAVGIN PYRDWHFMIN ALNDYNYEMD YSQYDGSLSS MLLWEAVQVL AYCHDSPDLV 

      1990       2000       2010       2020       2030       2040 
MQLHKPVIDS DHVVFNERWL IHGGMPSGSP CTTVLNSLCN LMMCIYTTNL ISPGIDCLPI 

      2050       2060       2070       2080       2090       2100 
VYGDDVILSL DKEIEPERLQ SIMAESFGAE VTGSRKDEPP SLKPRMEVEF LKRKPGYFPE 

      2110       2120       2130       2140       2150       2160 
STFIVGKLDT ENMIQHLMWM KNFSTFKQQL QSYLMELCLH GKDTYQHYVK ILNPYLKEWN 

      2170 
IPVDDYEVVI GKLVPMVFD 

« Hide

References

[1]"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: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ005695 Genomic RNA. Translation: CAA06679.1.
RefSeqNP_046804.1. NC_001897.1.

3D structure databases

ProteinModelPortalO73556.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSC03.023.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1403455.

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. 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_HPE2W
AccessionPrimary (citable) accession number: O73556
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: August 1, 1998
Last modified: July 9, 2014
This is version 113 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