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O73556

- POLG_HPE2W

UniProt

O73556 - POLG_HPE2W

Protein

Genome polyprotein

Gene
N/A
Organism
Human parechovirus 2 (strain Williamson) (HPeV-2) (Echovirus 23)
Status
Reviewed - Annotation score: 5 out of 5- Protein inferred from homologyi
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    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 1 (01 Aug 1998)
      Previous versions | rss
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    Functioni

    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
    Sitei775 – 7762Cleavage; by protease 2ASequence Analysis
    Active sitei1549 – 15491For protease 3C activitySequence Analysis
    Active sitei1580 – 15801For protease 3C activitySequence Analysis
    Active sitei1669 – 16691For protease 3C activitySequence Analysis

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi1184 – 11918ATPPROSITE-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. induction by virus of host autophagy Source: UniProtKB
    2. pore formation by virus in membrane of host cell Source: UniProtKB-KW
    3. protein oligomerization Source: UniProtKB-KW
    4. RNA-protein covalent cross-linking Source: UniProtKB-KW
    5. suppression by virus of host RIG-I activity by RIG-I proteolysis Source: UniProtKB
    6. suppression by virus of host translation initiation factor activity Source: UniProtKB
    7. transcription, DNA-templated Source: InterPro
    8. viral entry into host cell Source: UniProtKB-KW
    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

    Host-virus interaction, Ion transport, Transport, Viral attachment to host cell, Viral RNA replication, 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 2 (strain Williamson) (HPeV-2) (Echovirus 23)
    Taxonomic identifieri122962 [NCBI]
    Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeParechovirus
    Virus hostiHomo sapiens (Human) [TaxID: 9606]
    ProteomesiUP000000670: 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_0000039750Add
    BLAST
    Chaini290 – 542253Protein VP3Sequence AnalysisPRO_0000039751Add
    BLAST
    Chaini543 – 775233Protein VP1Sequence AnalysisPRO_0000039752Add
    BLAST
    Chaini776 – 922147Protein 2ASequence AnalysisPRO_0000039753Add
    BLAST
    Chaini923 – 1044122Protein 2BSequence AnalysisPRO_0000039754Add
    BLAST
    Chaini1045 – 1373329Protein 2CSequence AnalysisPRO_0000039755Add
    BLAST
    Chaini1374 – 1490117Protein 3ASequence AnalysisPRO_0000039756Add
    BLAST
    Chaini1491 – 151020Protein 3BSequence AnalysisPRO_0000039757Add
    BLAST
    Chaini1511 – 1710200Protease 3CSequence AnalysisPRO_0000039758Add
    BLAST
    Chaini1711 – 2179469RNA-directed RNA polymerase 3D-POLSequence AnalysisPRO_0000039759Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1493 – 14931O-(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.

    Keywords - PTMi

    Covalent protein-RNA linkage, Lipoprotein, Myristate, Phosphoprotein

    Structurei

    3D structure databases

    ProteinModelPortaliO73556.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1156 – 1317162SF3 helicasePROSITE-ProRule annotationAdd
    BLAST
    Domaini1944 – 2058115RdRp catalyticPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi763 – 7653Cell 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. 2 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.

    O73556-1 [UniParc]FASTAAdd to Basket

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    METIKSIADM ATGVTKTIDA TINSVNEIIT NTDNASGGDI LTKVADDASN     50
    ILGPNCYATT SEPENKDVVQ ATTTVNTTNL TQHPSAPTLP FTPDFSNVDT 100
    FHSMAYDTTT GSKNPNKLVR LTTHAWASTL QRGHQIDHVN LPVDFWDEQR 150
    KPAYGHAKYF AAVRCGFHFQ VQVNVNQGTA GSALVVYEPK PVVDYDKDLE 200
    FGAFTNLPHV LMNLAETTQA DLCIPYVADT NYVKTDSSDL GQLKVYVWTP 250
    LSIPSGSSNQ VDVTILGSLL QLDFQNPRVY GQNVDIYDTA PSKPIPLRKT 300
    KYLTMSTKYK WTRNKVDIAE GPGSMNMANV LSTTAAQSVA LVGERAFYDP 350
    RTAGSKSRFD DLVKISQLFS VMADSTTPSA NHGIDQKGYF KWSANSDPQA 400
    IVHRNLVHLN LFPNLKVFEN SYSYFRGSLI IRLSVYASTF NRGRLNGFFP 450
    NSSTDETSEI DNAIYTICDI GSDNSFEITI PYSFSTWMRK THGKPIGLFQ 500
    IEVLNRLTYN YSSPNEVYCI VQGKMGQDAK FFCPTGSLVT FQNSWGSQMD 550
    LTDPLCIEDS VEDCKQTITP TELGLTSAQD DGPLGNDKPN YFLNFKSMNV 600
    DIFTVSHTKV DNIFGRAWFA HVHDFTNDGL WRQGLEFPKE GHGALSLLFA 650
    YFTGELNIHV LFLSDRGFLR VGHTYDTETN RTNFLSSSGI ITVPAGEQMT 700
    LSVPSYSNKP LRTVRSSNAL GYLLCKPLLT GTSSGRIEIF LSLRCPNFFF 750
    PLPAPKPATR KYRGDLATWS DQSPYGRQGK KQLMKLAYLD RGFYKHYGIV 800
    VGDDVYQLDS DDIFKTALTG KAKFTKTRLT PDWVVEEECE LDYFRIKYLE 850
    SSVNSEHIFS VDNNCETIAK DIFGSHSLSQ HQQIGLIGTI LLTAGLMSTI 900
    KTPVNPTTIK EFFNHAIEGD EQGLSLLVQK CTTFFSSAAT ELLDNDLVKF 950
    IIKILVRILC YMVLYCHKPN ILTTACLSTL LVMDVTSSSV LSPSCKALMQ 1000
    CLMDGDVKKL AEVVAESMSN TDDDEIKEQI CDTVKYTKQI LSNQGPFKGF 1050
    NEISTAFRHI DWWIQTLLKI KDMVLSVFKP SVEKRAVEWL ERNKEHVCSI 1100
    LDYASDIIVK SKDQTKMKTQ EFYQRYNDCL SKFKPIMAMC FRSCHNSISN 1150
    TVYRLFQELA RIPNRMATQN DLIRVEPIGI WIQGEPGQGK SFLTHTLSKQ 1200
    LQKTCGLQGI YTNPTASEFM DGYDNQDIHL IDDLGQTRKE RDIEMLCNCI 1250
    SSDPDIVPMA HLEEKGKFYT SKLVIATTNK PDFSSTVLLD SGALRRRFPY 1300
    IMHIRAAKHY SKSGKLNVSQ AMPHMSTGEC WEVSKNGRDW ETLKLKELID 1350
    KITVDYKERI ANYNTWKKQL EDQTLDDLDD AVSYIKHNYP DAIPYIDEYL 1400
    NIEMSTLIEQ MEAFIEPKPS VFKCFASRVG DKIKEASREV VKWFSDKLKS 1450
    MLNFVERNKA WLTVVSAVTS AIGILLLVTK IFKKEESKDE RAYNPTLPVA 1500
    KPKGTFPVSQ REFKNEAPYD GQLEHIISQM AYITGSTTGH ITHCAGYQHD 1550
    EIILHGHSIK YLEQEEELTL HYKNKVFPIE QPSVTQVTLG GKPMDLAIVK 1600
    CKLPFRFKKN SKYYTNKIGT ESMLIWMTEQ GIITKEVQRV HHSGGIKTRE 1650
    GTESTKTISY TVKSCKGMCG GLLISKVEGN FKILGMHIAG NGEMGVAIPF 1700
    NFLKNDMSDQ GIVTEVTPIQ PMYINTKSQI HKSPVYGAVE VKMGPAVLSK 1750
    SDTRLEEPVD CLVKKSASKY RVNKFQVNNE LWQGVKACVK SKFREIFGVN 1800
    GIVDMKTAIL GTSHVNSMDL STSAGYSFVK SGYKKKDLIC LEPFSVSPML 1850
    EKLVQEKFHN LLKGNQITTI FNTCLKDELR KLDKIATGKT RCIEACEIDY 1900
    CIVYRMIMME IYDKIYQTPC YYSGLAVGIN PYRDWHFMIN ALNDYNYEMD 1950
    YSQYDGSLSS MLLWEAVQVL AYCHDSPDLV MQLHKPVIDS DHVVFNERWL 2000
    IHGGMPSGSP CTTVLNSLCN LMMCIYTTNL ISPGIDCLPI VYGDDVILSL 2050
    DKEIEPERLQ SIMAESFGAE VTGSRKDEPP SLKPRMEVEF LKRKPGYFPE 2100
    STFIVGKLDT ENMIQHLMWM KNFSTFKQQL QSYLMELCLH GKDTYQHYVK 2150
    ILNPYLKEWN IPVDDYEVVI GKLVPMVFD 2179
    Length:2,179
    Mass (Da):245,874
    Last modified:August 1, 1998 - v1
    Checksum:i96803C0BB8856664
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ005695 Genomic RNA. Translation: CAA06679.1.
    RefSeqiNP_046804.1. NC_001897.1.

    Genome annotation databases

    GeneIDi1403455.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ005695 Genomic RNA. Translation: CAA06679.1 .
    RefSeqi NP_046804.1. NC_001897.1.

    3D structure databases

    ProteinModelPortali O73556.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi C03.023.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 1403455.

    Family and domain databases

    Gene3Di 2.60.120.20. 2 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. "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].

    Entry informationi

    Entry nameiPOLG_HPE2W
    AccessioniPrimary (citable) accession number: O73556
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: August 1, 1998
    Last modified: October 1, 2014
    This is version 114 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, Reference proteome

    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