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Q66578

- POLG_HPE1H

UniProt

Q66578 - POLG_HPE1H

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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

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.1 Publication
Protein 2B: Affects membrane integrity and cause an increase in membrane permeability By similarity.1 Publication
Protein 2C: Associates with and induces structural rearrangements of intracellular membranes. It displays RNA-binding, nucleotide binding and NTPase activities By similarity.1 Publication
Protein 3A, via its hydrophobic domain, serves as membrane anchor By similarity.1 Publication
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.1 Publication
RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals By similarity.1 Publication

Catalytic activityi

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei776 – 7772Cleavage; by protease 2A Reviewed prediction
Active sitei1550 – 15501For protease 3C activity Reviewed prediction
Active sitei1581 – 15811For protease 3C activity Reviewed prediction
Active sitei1670 – 16701For protease 3C activity Reviewed prediction

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1185 – 11928ATP Reviewed prediction

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. RNA binding Source: UniProtKB-KW
  3. RNA helicase activity Source: InterPro
  4. RNA-directed RNA polymerase activity Source: UniProtKB-KW
  5. cysteine-type endopeptidase activity Source: InterPro
  6. ion channel activity Source: UniProtKB-KW
  7. structural molecule activity Source: InterPro

GO - Biological processi

  1. RNA-protein covalent cross-linking Source: UniProtKB-KW
  2. clathrin-mediated endocytosis of virus by host cell Source: UniProtKB-KW
  3. induction by virus of host autophagy Source: UniProtKB
  4. pore formation by virus in membrane of host cell Source: UniProtKB-KW
  5. protein oligomerization 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
Complete GO annotation...

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 Reviewed prediction
Chain Protein VP1 : Virion By similarity. Host cytoplasm Reviewed prediction
Chain Protein 2B : Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Reviewed prediction
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.
Chain Protein 2C : Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Reviewed prediction
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.
Chain Protein 3A : Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Reviewed prediction
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.
Chain Protein 3B : Virion Reviewed prediction
Chain Protease 3C : Host cytoplasm Reviewed prediction
Chain RNA-directed RNA polymerase 3D-POL : Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Reviewed prediction
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.

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
Complete GO annotation...

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 VP0 Reviewed prediction
PRO_0000039730Add
BLAST
Chaini290 – 542253Protein VP3 Reviewed prediction
PRO_0000039731Add
BLAST
Chaini543 – 776234Protein VP1 Reviewed prediction
PRO_0000039732Add
BLAST
Chaini777 – 923147Protein 2A Reviewed prediction
PRO_0000039733Add
BLAST
Chaini924 – 1045122Protein 2B Reviewed prediction
PRO_0000039734Add
BLAST
Chaini1046 – 1374329Protein 2C Reviewed prediction
PRO_0000039735Add
BLAST
Chaini1375 – 1491117Protein 3A Reviewed prediction
PRO_0000039736Add
BLAST
Chaini1492 – 151120Protein 3B Reviewed prediction
PRO_0000039737Add
BLAST
Chaini1512 – 1711200Protease 3C Reviewed prediction
PRO_0000039738Add
BLAST
Chaini1712 – 2180469RNA-directed RNA polymerase 3D-POL Reviewed prediction
PRO_0000039739Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1494 – 14941O-(5'-phospho-RNA)-tyrosine By 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.
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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1160 – 1318159SF3 helicase
Add
BLAST
Domaini1945 – 2059115RdRp catalytic
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi764 – 7663Cell attachment site Reviewed prediction

Sequence similaritiesi

Contains 2 peptidase C3 domains.

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

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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: July 9, 2014
This is version 115 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

Similar proteinsi