POLG_HPEV5
ID POLG_HPEV5 Reviewed; 2188 AA.
AC Q9YID8;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Genome polyprotein;
DE Contains:
DE RecName: Full=Capsid protein VP0;
DE AltName: Full=P1AB;
DE AltName: Full=Virion protein 0;
DE Contains:
DE RecName: Full=Capsid protein VP3;
DE AltName: Full=P1C;
DE AltName: Full=Virion protein 3;
DE Contains:
DE RecName: Full=Capsid protein VP1;
DE AltName: Full=P1D;
DE AltName: Full=Virion protein 1;
DE Contains:
DE RecName: Full=Protein 2A;
DE Short=P2A;
DE Contains:
DE RecName: Full=Protein 2B;
DE Short=P2B;
DE Contains:
DE RecName: Full=Protein 2C;
DE Short=P2C;
DE EC=3.6.1.15;
DE Contains:
DE RecName: Full=Protein 3A;
DE Short=P3A;
DE Contains:
DE RecName: Full=Protein 3B;
DE Short=P3B;
DE AltName: Full=VPg;
DE Contains:
DE RecName: Full=Protease 3C;
DE Short=P3C;
DE EC=3.4.22.28;
DE EC=3.4.22.29;
DE AltName: Full=Picornain 3C;
DE Contains:
DE RecName: Full=RNA-directed RNA polymerase 3D-POL;
DE Short=P3D-POL;
DE EC=2.7.7.48;
OS Human parechovirus 5 (strain CT86-6760) (HPeV-5) (Echovirus 23).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Picornaviridae; Parechovirus.
OX NCBI_TaxID=122961;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=9783471; DOI=10.1016/s0168-1702(98)00080-x;
RA Oberste M.S., Maher K., Pallansch M.A.;
RT "Complete sequence of echovirus 23 and its relationship to echovirus 22 and
RT other human enteroviruses.";
RL Virus Res. 56:217-223(1998).
RN [2]
RP FUNCTION OF PROTEIN 2A.
RX PubMed=9820139; DOI=10.1099/0022-1317-79-11-2641;
RA Ghazi F., Hughes P.J., Hyypiae T., Stanway G.;
RT "Molecular analysis of human parechovirus type 2 (formerly echovirus 23).";
RL J. Gen. Virol. 79:2641-2650(1998).
CC -!- FUNCTION: [Protein 2A]: Is not a protease. {ECO:0000250}.
CC -!- FUNCTION: [Protein 2B]: Affects membrane integrity and cause an
CC increase in membrane permeability. {ECO:0000250}.
CC -!- FUNCTION: [Protein 2C]: Associates with and induces structural
CC rearrangements of intracellular membranes. It displays RNA-binding,
CC nucleotide binding and NTPase activities (By similarity).
CC {ECO:0000250}.
CC -!- FUNCTION: Protein 3A, via its hydrophobic domain, serves as membrane
CC anchor. {ECO:0000250}.
CC -!- FUNCTION: [Protease 3C]: Cysteine protease that generates mature viral
CC proteins from the precursor polyprotein. In addition to its proteolytic
CC activity, it binds to viral RNA, and thus influences viral genome
CC replication. RNA and substrate bind cooperatively to the protease (By
CC similarity). {ECO:0000250}.
CC -!- FUNCTION: RNA-directed RNA polymerase 3D-POL replicates genomic and
CC antigenomic RNA by recognizing replications specific signals.
CC {ECO:0000255|PROSITE-ProRule:PRU00539}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Selective cleavage of Tyr-|-Gly bond in the picornavirus
CC polyprotein.; EC=3.4.22.29;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
CC diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Selective cleavage of Gln-|-Gly bond in the poliovirus
CC polyprotein. In other picornavirus reactions Glu may be substituted
CC for Gln, and Ser or Thr for Gly.; EC=3.4.22.28;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU01222};
CC -!- SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion {ECO:0000250}. Host
CC cytoplasm {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein VP1]: Virion {ECO:0000250}. Host
CC cytoplasm {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Protein 2B]: Host cytoplasmic vesicle membrane
CC {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic
CC side {ECO:0000305}. Note=Probably localizes to the surface of
CC intracellular membrane vesicles that are induced after virus infection
CC as the site for viral RNA replication. These vesicles are derived from
CC the endoplasmic reticulum (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Protein 2C]: Host cytoplasmic vesicle membrane
CC {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic
CC side {ECO:0000305}. Note=Probably localizes to the surface of
CC intracellular membrane vesicles that are induced after virus infection
CC as the site for viral RNA replication. These vesicles are derived from
CC the endoplasmic reticulum (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Protein 3A]: Host cytoplasmic vesicle membrane
CC {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic
CC side {ECO:0000305}. Note=Probably localizes to the surface of
CC intracellular membrane vesicles that are induced after virus infection
CC as the site for viral RNA replication. These vesicles are derived from
CC the endoplasmic reticulum (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Protein 3B]: Virion {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Protease 3C]: Host cytoplasm {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [RNA-directed RNA polymerase 3D-POL]: Host
CC cytoplasmic vesicle membrane {ECO:0000305}; Peripheral membrane protein
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Probably localizes
CC to the surface of intracellular membrane vesicles that are induced
CC after virus infection as the site for viral RNA replication. These
CC vesicles are derived from the endoplasmic reticulum (By similarity).
CC {ECO:0000250}.
CC -!- PTM: VPg is uridylylated by the polymerase and is covalently linked to
CC the 5'-end of genomic RNA. This uridylylated form acts as a nucleotide-
CC peptide primer for the polymerase (By similarity). {ECO:0000250}.
CC -!- PTM: Specific enzymatic cleavages yield mature proteins. All cleavages
CC are catalyzed by P3C.
CC -!- SIMILARITY: Belongs to the picornaviruses polyprotein family.
CC {ECO:0000305}.
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DR EMBL; AF055846; AAC79756.1; -; Genomic_RNA.
DR SMR; Q9YID8; -.
DR PRIDE; Q9YID8; -.
DR Proteomes; UP000008274; Genome.
DR GO; GO:0044162; C:host cell cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044385; C:integral to membrane of host cell; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0039618; C:T=pseudo3 icosahedral viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0017111; F:nucleoside-triphosphatase activity; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0039520; P:induction by virus of host autophagy; ISS:UniProtKB.
DR GO; GO:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW.
DR GO; GO:0051259; P:protein complex oligomerization; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0018144; P:RNA-protein covalent cross-linking; IEA:UniProtKB-KW.
DR GO; GO:0039611; P:suppression by virus of host translation initiation factor activity; ISS:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR CDD; cd00205; rhv_like; 2.
DR Gene3D; 2.40.10.10; -; 1.
DR Gene3D; 2.60.120.20; -; 2.
DR Gene3D; 3.30.70.270; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR004004; Helic/Pol/Pept_Calicivir-typ.
DR InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir.
DR InterPro; IPR014759; Helicase_SF3_ssRNA_vir.
DR InterPro; IPR007053; LRAT_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR044067; PCV_3C_PRO.
DR InterPro; IPR000199; Peptidase_C3A/C3B_picornavir.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001676; Picornavirus_capsid.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR033703; Rhv-like.
DR InterPro; IPR001205; RNA-dir_pol_C.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR InterPro; IPR029053; Viral_coat.
DR InterPro; IPR009419; VPP_parechovir_P3A.
DR InterPro; IPR009407; VPP_parechovir_P3B.
DR Pfam; PF06344; Parecho_VpG; 1.
DR Pfam; PF00548; Peptidase_C3; 1.
DR Pfam; PF06363; Picorna_P3A; 1.
DR Pfam; PF00680; RdRP_1; 1.
DR Pfam; PF00073; Rhv; 1.
DR Pfam; PF00910; RNA_helicase; 1.
DR PRINTS; PR00918; CALICVIRUSNS.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS51934; LRAT; 1.
DR PROSITE; PS51874; PCV_3C_PRO; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
DR PROSITE; PS51218; SF3_HELICASE_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Capsid protein; Covalent protein-RNA linkage; Helicase;
KW Host cytoplasm; Host cytoplasmic vesicle; Host membrane;
KW Host-virus interaction; Hydrolase; Ion channel; Ion transport; Lipoprotein;
KW Membrane; Myristate; Nucleotide-binding; Nucleotidyltransferase;
KW Phosphoprotein; Protease; RNA-binding; RNA-directed RNA polymerase;
KW T=pseudo3 icosahedral capsid protein; Thiol protease; Transferase;
KW Transport; Viral attachment to host cell; Viral ion channel;
KW Viral RNA replication; Virion; Virus entry into host cell.
FT CHAIN 1..290
FT /note="Capsid protein VP0"
FT /evidence="ECO:0000255"
FT /id="PRO_0000039740"
FT CHAIN 291..549
FT /note="Capsid protein VP3"
FT /evidence="ECO:0000255"
FT /id="PRO_0000039741"
FT CHAIN 550..784
FT /note="Capsid protein VP1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000039742"
FT CHAIN 785..931
FT /note="Protein 2A"
FT /evidence="ECO:0000255"
FT /id="PRO_0000039743"
FT CHAIN 932..1053
FT /note="Protein 2B"
FT /evidence="ECO:0000255"
FT /id="PRO_0000039744"
FT CHAIN 1054..1382
FT /note="Protein 2C"
FT /evidence="ECO:0000255"
FT /id="PRO_0000039745"
FT CHAIN 1383..1499
FT /note="Protein 3A"
FT /evidence="ECO:0000255"
FT /id="PRO_0000039747"
FT CHAIN 1500..1519
FT /note="Protein 3B"
FT /evidence="ECO:0000250"
FT /id="PRO_0000311174"
FT CHAIN 1520..1719
FT /note="Protease 3C"
FT /evidence="ECO:0000255"
FT /id="PRO_0000039748"
FT CHAIN 1720..2188
FT /note="RNA-directed RNA polymerase 3D-POL"
FT /evidence="ECO:0000255"
FT /id="PRO_0000039749"
FT DOMAIN 795..889
FT /note="LRAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01283"
FT DOMAIN 1165..1326
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT DOMAIN 1526..1716
FT /note="Peptidase C3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT DOMAIN 1953..2067
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT MOTIF 772..774
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT ACT_SITE 1566
FT /note="For protease 3C activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 1604
FT /note="For protease 3C activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 1678
FT /note="For protease 3C activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 2053
FT /note="For RdRp activity"
FT /evidence="ECO:0000250|UniProtKB:P12296"
FT BINDING 1193..1200
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT SITE 784..785
FT /note="Cleavage; by protease 2A"
FT /evidence="ECO:0000255"
FT MOD_RES 1502
FT /note="O-(5'-phospho-RNA)-tyrosine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 2188 AA; 246604 MW; 02CC77D0A5ED3D93 CRC64;
METIKSIADM ATGFTNTIDS TVNAVTEGVS KIGNDSGGEI LTKVADDASN LLGPNCVAST
SQPENKDVVQ ATTTVNTLTN LTQHPSAPTM PFTPDFSNVD VFHSMAYDIT TGDKNPSKLI
RLDTTTWQHT WPRQHLINDV ELPKAFWDKN SKPAYGQSRY FAAVRCGFHF QVQINVNQGT
AGCALVVYEP KPIVTHGGHL EFGSYTNLPH VLMNLAETTQ ADLCIPYVSD TNYVKTDSSD
LGRLRVYVWT PLTIPSSATN DVDVTVLGSL LQLDFQNPRT YDTDVNIYDN SPLDTKTKYG
KLRFSKKILS MSTKYKWTRN KIDIAEGPGS MNMANVLSTT GAQSIALVGE RAFYDPRTAG
SKSRFGDMIH IAQLFSVMSD TTTPSTSSGI DDLGYLDWSA TYVPQQVIHR NVVKLNQFSN
LKPFVNAYTY FRGSLVLRMS VYASTFNRGR LRMGFFPNFT TNTTSEMDNA IYTICDIGSD
NSFEITIPYT FSTWMRKTNG RPIGLFQVEV LNRLTYNSSC PNKVHCIVQG RLGNDARFYC
PTGSLVEFQN SWGSQMDLTD PLCVEDDEAE DCKQTISPDE LGLTSAQDDG PLGVEKPNYF
LNFRAINVDI FTVSHTKVDN IFGRAWLALE HTFADDGTWR ADLNFPTQGH GTLTRLFTYY
SGELNVHVLY LSDNGFLRVT HAYDHDNDRS NFLSSNGVIT VPAGEQMTLS VPFYSSKPLR
TIRETGALGK LICKPLLSGT HSGKIEVYLS LRCPNLFFPS PAPKEKTSRA LRGDLANFID
QSPYGQQQQT QMMKLAYLDR GFYKHYGIIV GGYVYQLDSD DIFKTALTGK ARFTKTRLTP
DWIVEEECEL DYFRVKYLES SVNSEHIFSV DSNCETIAKD IFGTHTLSQH QAIGLVGAIL
LTAGLMSTIK TPVNATTIKE FFNHAIDGDE QGLSLLVQKC TTFFSSAATE ILDNDLVKFI
VKILVRILCY MVLYCHKPNI LTTACLSTLL IMDVTSSSVL SPSCKALMQC LMDGDVKKLA
EVVAESMSNT DDDEIKEQIC DTVKYTKTIL SNQGPFKGFN EVSTAFRHVD WWIHTLLKIK
DMVLSVFKPS IESKAIQWLE RNKEHVCSIL DYASDIIVES KDQTKMKTQE FYQRYSDCLA
KFKPIMAICF RSCHNSISNT VYRLFQELAR IPNRISTQND LIRVEPIGVW IQGEPGQGKS
FLTHTLSRQL QKSCKLNGVY TNPTASEFMD GYDNQDIHLI DDLGQTRKEK DIEMLCNCIS
SVPFIVPMAH LEEKGKFYTS KLVIATTNKS DFSSTVLQDS GALKRRFPYI MHIRAAKAYS
KSGKLNVSQA MSTMSTGECW EVSKNGRDWE TLKLKDLVQK ITEDYQERQK NYNAWKQQLE
NQTLDDLDDA VSYIKHNFPD AIPYIDEYLN IEMSTLIEQM EAFIEPRPSV FKCFAVKLPH
KPGKQPRKLW AGSAGKIKSM LSFIERNKAW LTVVSAVTSA ISILLLVTKI FKKEESKDER
AYNPTLPITK PKGTFPVSQR EFKNEAPYDG QLEHIISQMA YITGSTTGHL THCAGYQHDE
IILHGHSIKY LEQEEDLTLH YKNKVFPIEN PSVTQVTLGG KPMDLAILKC KLPFRFKKNS
KYYTNKIGTE SMLIWMTEQG IITKEVQRVH HSGGIKTREG TESTKTISYT VKSCKGMCGG
LLISKVEGNF KILGMHIAGN GEMGVAIPFN FLKNDMSDQG IITEVTPIQP MYINTKSQIH
KSPVYGAVEV KMGPAVLSKS DTRLEEPVDC LIKKSASKYR VNKFQVNNEL WQGVKACVKS
KFREIFGVNG IVDMKTAILG TSHVNSMDLS TSAGYSLVKS GYKKKDLICL EPFSVSPMLE
KLVQDKFHNL LKGNQITTIF NTCLKDELRK LDKIAAGKTR CIEACEVDYC IVYRMIMMEI
YDKIYQTPCY YSGLAVGINP YKDWHFMINA LNDYNYEMDY SQYDGSLSSM LLWEAVEVLA
YCHDSPDLVM QLHKPVIDSD HVVFNERWLI HGGMPSGSPC TTVLNSLCNL MMCIYTTNLI
SPGVDCLPIV YGDDVILSLD REIEPERLQS IMADSFGAEV TGSRKDEPPS LKPRMEVEFL
KRKPGYFPES TFIVGKLDTE NMIQHLMWMK NFSTFKQQLQ SYLMELCLHG KDIYQRYIKI
LDPYLKEWNI VVDDYDVVIA KLMPMVFD
