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Genome polyprotein

 A0A1U9X9S3_9PICO        Unreviewed;      2177 AA.
A0A1U9X9S3;
07-JUN-2017, integrated into UniProtKB/TrEMBL.
07-JUN-2017, sequence version 1.
23-MAY-2018, entry version 7.
RecName: Full=Genome polyprotein {ECO:0000256|SAAS:SAAS00958788};
Human parechovirus 3.
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Picornavirales; Picornaviridae; Parechovirus.
NCBI_TaxID=195055 {ECO:0000313|EMBL:AQY77577.1};
[1] {ECO:0000313|EMBL:AQY77577.1}
NUCLEOTIDE SEQUENCE.
STRAIN=GL-Cons-comb-SA1-2015 {ECO:0000313|EMBL:AQY77577.1};
PubMed=28290509; DOI=.1038/srep44423;
Nelson T.M., Vuillermin P., Hodge J., Druce J., Williams D.T.,
Jasrotia R., Alexandersen S.;
"An outbreak of severe infections among Australian infants caused by a
novel recombinant strain of human parechovirus type 3.";
Sci. Rep. 7:44423-44423(2017).
-!- CATALYTIC ACTIVITY: NTP + H(2)O = NDP + phosphate.
{ECO:0000256|SAAS:SAAS00711622}.
-!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
+ RNA(n+1). {ECO:0000256|SAAS:SAAS00519153}.
-!- CATALYTIC ACTIVITY: 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.
{ECO:0000256|SAAS:SAAS00711755}.
-!- SUBCELLULAR LOCATION: Host cytoplasmic vesicle membrane
{ECO:0000256|SAAS:SAAS00711512}; Peripheral membrane protein
{ECO:0000256|SAAS:SAAS00711512}; Cytoplasmic side
{ECO:0000256|SAAS:SAAS00711512}. Virion
{ECO:0000256|SAAS:SAAS01033941}.
-!- SIMILARITY: Belongs to the picornaviruses polyprotein family.
{ECO:0000256|SAAS:SAAS00727971}.
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EMBL; KY020128; AQY77577.1; -; Genomic_RNA.
GO; GO:0044162; C:host cell cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0044385; C:integral to membrane of host cell; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
GO; GO:0019015; C:viral genome; IEA:InterPro.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW.
GO; GO:0051259; P:protein complex oligomerization; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
CDD; cd00205; rhv_like; 2.
Gene3D; 2.60.120.20; -; 4.
InterPro; IPR004004; Helic/Pol/Pept_Calicivir-typ.
InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir.
InterPro; IPR014759; Helicase_SF3_ssRNA_vir.
InterPro; IPR000199; Peptidase_C3A/C3B_picornavir.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001676; Picornavirus_capsid.
InterPro; IPR033703; Rhv-like.
InterPro; IPR001205; RNA-dir_pol_C.
InterPro; IPR007094; RNA-dir_pol_PSvirus.
InterPro; IPR029053; Viral_coat.
InterPro; IPR009419; VPP_parechovir_P3A.
InterPro; IPR009407; VPP_parechovir_P3B.
Pfam; PF06344; Parecho_VpG; 1.
Pfam; PF00548; Peptidase_C3; 1.
Pfam; PF06363; Picorna_P3A; 1.
Pfam; PF00680; RdRP_1; 1.
Pfam; PF00073; Rhv; 1.
Pfam; PF00910; RNA_helicase; 1.
PRINTS; PR00918; CALICVIRUSNS.
SUPFAM; SSF50494; SSF50494; 1.
PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PROSITE; PS51218; SF3_HELICASE_2; 1.
3: Inferred from homology;
ATP-binding {ECO:0000256|SAAS:SAAS01033926};
Capsid protein {ECO:0000256|SAAS:SAAS00958801};
Helicase {ECO:0000256|SAAS:SAAS01033926};
Host cytoplasm {ECO:0000256|SAAS:SAAS00711571};
Host cytoplasmic vesicle {ECO:0000256|SAAS:SAAS00711589};
Host membrane {ECO:0000256|SAAS:SAAS00795395};
Host-virus interaction {ECO:0000256|SAAS:SAAS00711583};
Hydrolase {ECO:0000256|SAAS:SAAS01033926,
ECO:0000256|SAAS:SAAS01035925};
Ion channel {ECO:0000256|SAAS:SAAS00711569};
Ion transport {ECO:0000256|SAAS:SAAS00711569};
Membrane {ECO:0000256|SAAS:SAAS00795395};
Nucleotide-binding {ECO:0000256|SAAS:SAAS01033926};
Nucleotidyltransferase {ECO:0000256|SAAS:SAAS00519100};
Protease {ECO:0000256|SAAS:SAAS01035925};
RNA-binding {ECO:0000256|SAAS:SAAS00711776};
RNA-directed RNA polymerase {ECO:0000256|SAAS:SAAS00519100};
Thiol protease {ECO:0000256|SAAS:SAAS01035925};
Transferase {ECO:0000256|SAAS:SAAS00519100};
Transport {ECO:0000256|SAAS:SAAS00711569};
Viral attachment to host cell {ECO:0000256|SAAS:SAAS00711583};
Viral ion channel {ECO:0000256|SAAS:SAAS00711569};
Viral RNA replication {ECO:0000256|SAAS:SAAS00660848};
Virion {ECO:0000256|SAAS:SAAS00711583, ECO:0000256|SAAS:SAAS00958801};
Virus entry into host cell {ECO:0000256|SAAS:SAAS00711583}.
DOMAIN 1154 1315 SF3 helicase.
{ECO:0000259|PROSITE:PS51218}.
DOMAIN 1942 2056 RdRp catalytic.
{ECO:0000259|PROSITE:PS50507}.
SEQUENCE 2177 AA; 246045 MW; 5E45D24223BF666A CRC64;
MESIKDLVNV ATGAMDTLSL SSVETEANNI ISGNEVGGEI ITKVADDASN LLGPNSFATT
AQPENKDVVQ ATTTVNTTNL TQHPSAPTIP FTPDFRNVDN FHSMAYDITT GDKNPSKLIR
LDTASWQTSY SRQYKITTVE LPKSFWDDTR KPAYGQAKYF AAVRCGFHFQ VQVNVNQGTA
GSALVVYEPK PVIDSRQYLE FGSLTNLPHV LMNLAETTQA DLCIPYVADT NYVKTDSSDL
GQLRVYVWTP LSVPTGASNE VDVTVMGSLL QLDFQNPRPY GENVEIYDNG PNKTNIGRFN
KRKFLTASTK YKWTRTKVDI AEGPGTMNMA NVLSTTGAQS VALVGERAFY DPRTAGSKSR
FDDMIKIAQL FSVMSDNTTP SSSSGIDKYG YFDWAATVAP QNMVHRNVVT LDQFPNLNLF
MNTYSYFRGS LILRLSIYAS TFNRGRLRMG FFPNCTHDTQ LELDNAIYTI CDIGSDNSFE
LTIPYSFSTW MRKTHGHQLG LFQVEVLNRL TYNSSSPNKV HCIVQGRLGD DAKFFCPTGS
LVSFQNSWGS QMDLTDPLCI EDNMENCKQS ISPNELGLTS AQDDGPLGNE KPNYFLNFRT
MNVDIFTVSH TRVDNIFGRA WYVTSHDFNN GDTWRQKLTF PKEGHGMLSQ FFAYFTGEIN
IHILYMAEQG FLRVAHTYDT EDNRKTFLSS NGVITIPAGE QMTLSVPFYS NKPLRTVRHD
SALGFLMCRP MMHGTTRTTA EVYISLRCPN FFFPVPAPKP TGSGAAAFHD ESPYVPTDNR
KMQLAYLDRG FYKHYGIIVG DSVYQLDSDD IFKTALTGKA RFTKTILTPD WIIEEECELD
YFRVKYLESS VNSEHIFSVD HNCETIAKDI FGTHTLSQHQ AIGLIGTILL TAGLMSTIKT
PVNATTIKEF FNHAIEGDEQ GLSLLVQKCT TFFSSAATEI LDNDLVKFIV KILVRILCYM
VLYCHKPNIL TTACLSTLLI MDVTSSSVLS PSCKALMQCL MDGDVKKLAE VVAESMSNTD
DEEIKEQICD TVKYTKSILS NQGPFKGFNE VSTAFRHIDW WIHTLLKIKD MVLSVFKPSM
ESKAIQWLER NKEHVCAILD YASDIIVESK DQTKMKSQEF YQKYTDCLAK FKPIMAICFR
SCHNSISNTV YRLFQELARI PSRISTQNDL IRVEPIGVWI REKPGQGKSF LTHTLSRQLQ
KSCNLNGVYT NPTASEFMDG YDNQDIHLID DLGQTRKEKD IEMLCNCISS VPFIVPMAHL
EEKGKFYTSK LVIATTNKSD FSSTVLQDSG ALKRRFPYIM HIRAAKAYSK SGKLNVSQAM
STMATGECWE VSKNGRDWET LKLQELVKKV TEDYEERQKN YNCWKRQLEN QTLDDLDDAV
SYIKHNFPDA IPYIDEYLNI EMSTLIEQME AFIEPRPSVF KCFATKVANQ TRKAAKEVVD
WFSSKIKSML SFVERNKAWL TVVSAVTSAI SILLLVTKIF KKEDSKDERA YNPTLPIAKP
KGAFPVSQRE FKNEAPYDGQ LEHIISQMAY ITGSTTGHLT HCAGYQHDEI ILHGHSIKYL
EQEEDLTLHY KNKIFPIESP SVTQVTLGGK PMDLAILKCK LPFRFKKNSK YYTNKIGTES
MLVWMTEQGI ITKEVQRVHH SGGIKTREGT ESTKTISYTV KSCKGMCGGL LISKVEGNFK
ILGMHIAGNG EMGVAIPFNF LKNDMSDQGI VTEITPIQPM YINTKSQIHK SPVYGAVEVK
MGPAVLSKSD PRLEEPVECL IKKSAAKYRV NKFQVNNELW QGVKACVKSK FREIFGVNGI
VDMKTAILGT SHVNSMDLNT SAGYSFVKSG YKKKDLICLE PFSVSPMLEK LVQDKFHNLL
KGNQITTIFN TCLKDELRKM DKIATGKTRC IEACEVDYCI VYRMIMMEIY DKVYQTPCYY
SGLAVGINPY KDWHFMVNAL NDYNYEMDYS QYDGSLSSML LWEAVEVLAY CHDSPDLVMQ
LHKPVIDSDH VVFNERWLIH GGMPSGSPCT TVLNSLCNLM MCIYTTNLIS PGIDCLPIVY
GDDVILSLDK EIEPEKLQRI MADSFGVEVT GSRKDEPPSL KPRMEVEFLK RKPGYFPEST
FIVGKLDTEN MIQHLMWMKN FSTFKQQLQS YLMELCLHGK DTYQHYIKIL DPYLREWNIS
VDDYEVVIAK LMPMVFD


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