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Non-structural polyprotein pORF1 [Includes: Methyltransferase (EC 2.1.1.-) (EC 2.7.7.-); Putative papain-like cysteine protease (PLP) (EC 3.4.22.-); NTPase/helicase (EC 3.6.4.-); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48)]

 POLN_HEVHY              Reviewed;        1693 AA.
Q9WC28; O39221;
20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
05-DEC-2018, entry version 83.
RecName: Full=Non-structural polyprotein pORF1;
Includes:
RecName: Full=Methyltransferase;
EC=2.1.1.-;
EC=2.7.7.-;
Includes:
RecName: Full=Putative papain-like cysteine protease;
Short=PLP;
EC=3.4.22.-;
Includes:
RecName: Full=NTPase/helicase;
EC=3.6.4.-;
Includes:
RecName: Full=RNA-directed RNA polymerase;
Short=RdRp;
EC=2.7.7.48;
ORFNames=ORF1;
Hepatitis E virus genotype 1 (isolate Human/India/Hyderabad) (HEV-1).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Hepeviridae; Orthohepevirus; Orthohepevirus A.
NCBI_TaxID=512346;
NCBI_TaxID=69079; Bandicota bengalensis (lesser bandicoot rat).
NCBI_TaxID=9481; Callithrix.
NCBI_TaxID=9536; Cercopithecus hamlyni (Owl-faced monkey) (Hamlyn's monkey).
NCBI_TaxID=9534; Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops).
NCBI_TaxID=9606; Homo sapiens (Human).
NCBI_TaxID=9539; Macaca (macaques).
NCBI_TaxID=10090; Mus musculus (Mouse).
NCBI_TaxID=9598; Pan troglodytes (Chimpanzee).
NCBI_TaxID=9520; Saimiri (squirrel monkeys).
NCBI_TaxID=9823; Sus scrofa (Pig).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=10630959;
DOI=10.1002/(SICI)1096-9071(200003)60:3<275::AID-JMV5>3.0.CO;2-9;
Ansari I.H., Nanda S.K., Durgapal H., Agrawal S., Mohanty S.K.,
Gupta D., Jameel S., Panda S.K.;
"Cloning, sequencing, and expression of the hepatitis E virus (HEV)
nonstructural open reading frame 1 (ORF1).";
J. Med. Virol. 60:275-283(2000).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Infectious clone pSGI-HEV;
PubMed=10666275; DOI=10.1128/JVI.74.5.2430-2437.2000;
Panda S.K., Ansari I.H., Durgapal H., Agrawal S., Jameel S.;
"The in vitro-synthesized RNA from a cDNA clone of hepatitis E virus
is infectious.";
J. Virol. 74:2430-2437(2000).
[3]
FUNCTION (RNA-DIRECTED RNA POLYMERASE), AND RNA-BINDING.
STRAIN=Infectious clone pSGI-HEV;
PubMed=11259193; DOI=10.1006/viro.2000.0819;
Agrawal S., Gupta D., Panda S.K.;
"The 3' end of hepatitis E virus (HEV) genome binds specifically to
the viral RNA-dependent RNA polymerase (RdRp).";
Virology 282:87-101(2001).
-!- FUNCTION: Methyltransferase: Displays a capping enzyme activity.
This function is necessary since all viral RNAs are synthesized in
the cytoplasm, and host capping enzymes are restricted to the
nucleus. The enzymatic reaction involves a covalent link between
7-methyl-GMP and the methyltransferase, whereas eukaryotic capping
enzymes form a covalent complex only with GMP. Methyltransferase
catalyzes transfer of a methyl group from S-adenosylmethionine to
GTP and GDP to yield m(7)GTP or m(7)GDP. This enzyme also displays
guanylyltransferase activity to form a covalent complex,
methyltransferase-m(7)GMP, from which 7-methyl-GMP is transferred
to the mRNA to create the cap structure.
{ECO:0000250|UniProtKB:Q81862}.
-!- FUNCTION: Papain-like cysteine protease: May participate in the
processing of polyprotein pORF1 together with cellular proteases
and the cleavage of capsid protein ORF2.
{ECO:0000250|UniProtKB:Q81862}.
-!- FUNCTION: NTPase/helicase: Multi-functional protein that exhibits
NTPase and RNA unwinding activities. Hydrolyzes all NTPs
efficiently and unwinds RNA duplexes containing 5' overhangs.
Possesses a sequence independent RNA-5'-triphosphatase (RTPase)
activity suggestive of its role in forming viral cap structure (By
similarity). Participates also in viral genome replication, RNA
translocation and genome packaging/unpackaging (By similarity).
{ECO:0000250|UniProtKB:P29324, ECO:0000250|UniProtKB:Q81862}.
-!- FUNCTION: RNA-directed RNA polymerase: Plays an essential role in
the virus replication. Binds to the 3'-end of the genomic RNA to
initiate viral replication. {ECO:0000250|UniProtKB:Q81862,
ECO:0000269|PubMed:11259193}.
-!- CATALYTIC ACTIVITY:
Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:11128, Rhea:RHEA-
COMP:11129, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557,
ChEBI:CHEBI:83400; EC=2.7.7.48;
Evidence={ECO:0000250|UniProtKB:Q81862};
-!- INTERACTION:
Self; NbExp=81; IntAct=EBI-11179420, EBI-11179420;
Q68985:ORF2; NbExp=2; IntAct=EBI-11179420, EBI-11180197;
O90299:ORF3; NbExp=41; IntAct=EBI-11179420, EBI-11179411;
-!- SUBCELLULAR LOCATION: Host cytoplasm
{ECO:0000250|UniProtKB:Q81862}.
-!- PTM: It is not yet clear whether the ORF1-encoded polyprotein
contains multiple biochemical activities, or undergoes cis or
trans- processing to release biochemically distinct peptides. No
processing has been observed in mammalian expression systems.
However, the baculovirus expressed polyprotein is processed into
smaller protein, probably by a cysteine protease.
-!- SIMILARITY: Belongs to the hepevirus non-structural polyprotein
family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF028091; AAB82002.2; -; Genomic_RNA.
EMBL; AF076239; AAC27934.2; -; Genomic_RNA.
ProteinModelPortal; Q9WC28; -.
SMR; Q9WC28; -.
IntAct; Q9WC28; 2.
PRIDE; Q9WC28; -.
Proteomes; UP000007244; Genome.
GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0008174; F:mRNA methyltransferase activity; IEA:InterPro.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0006396; P:RNA processing; IEA:InterPro.
GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
GO; GO:0019082; P:viral protein processing; IEA:InterPro.
GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
InterPro; IPR027351; (+)RNA_virus_helicase_core_dom.
InterPro; IPR002588; Alphavirus-like_MT_dom.
InterPro; IPR008748; Hepatitis-E_Cys-pept.
InterPro; IPR022202; Hepatitis-E_hinge.
InterPro; IPR002589; Macro_dom.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR007094; RNA-dir_pol_PSvirus.
InterPro; IPR001788; Tymovirus_RNA-dep_RNA_pol.
Pfam; PF12526; DUF3729; 1.
Pfam; PF01661; Macro; 1.
Pfam; PF05417; Peptidase_C41; 1.
Pfam; PF00978; RdRP_2; 1.
Pfam; PF01443; Viral_helicase1; 1.
Pfam; PF01660; Vmethyltransf; 1.
ProDom; PD694051; Peptidase_C41; 1.
SMART; SM00506; A1pp; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS51743; ALPHAVIRUS_MT; 1.
PROSITE; PS51154; MACRO; 1.
PROSITE; PS51657; PSRV_HELICASE; 1.
PROSITE; PS50507; RDRP_SSRNA_POS; 1.
1: Evidence at protein level;
ATP-binding; Complete proteome; Helicase; Host cytoplasm; Hydrolase;
Methyltransferase; Nucleotide-binding; Nucleotidyltransferase;
Protease; RNA-binding; RNA-directed RNA polymerase; Thiol protease;
Transferase; Viral RNA replication.
CHAIN 1 1693 Non-structural polyprotein pORF1.
/FTId=PRO_0000334530.
DOMAIN 56 240 Alphavirus-like MT. {ECO:0000255|PROSITE-
ProRule:PRU01079}.
DOMAIN 775 921 Macro. {ECO:0000255|PROSITE-
ProRule:PRU00490}.
DOMAIN 934 1082 (+)RNA virus helicase ATP-binding.
DOMAIN 1083 1216 (+)RNA virus helicase C-terminal.
DOMAIN 1454 1565 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
NP_BIND 975 982 ATP. {ECO:0000255}.
REGION 60 240 Methyltransferase. {ECO:0000250}.
REGION 239 439 Y-domain. {ECO:0000250}.
REGION 440 610 Putative papain-like cysteine protease.
{ECO:0000250}.
REGION 712 778 Hinge. {ECO:0000250}.
REGION 785 942 X-domain. {ECO:0000250}.
REGION 960 1204 NTPase/helicase. {ECO:0000250}.
REGION 1207 1693 RNA-directed RNA polymerase.
{ECO:0000250}.
COMPBIAS 714 759 Pro-rich.
CONFLICT 1100 1100 Y -> F (in Ref. 2; AAC27934).
{ECO:0000305}.
SEQUENCE 1693 AA; 185580 MW; FB37B87BF6BBB501 CRC64;
MEAHQFLKAP GITTAVEQAA LATANSALAN AVVVRPFLSH QQIEILINLM QPRQLVFRPE
VFWNQPIQRV IHNELELYCR ARSGRCLEIG AHPRSINDNP NVVHRCFLRP VGRDVQRWYT
APTRGPAANC RRSALRGLPA ADRTYCFDGF SGCSCPAETG IALYSLHDMS PSDVAEAMFR
HGMTRLYAAL HLPPEVLLPP GTYRTASYLL IHDGRRVVVT YEGDTSAGYN HDVSNLRSWI
RTTKVTGDHP LVIERVRAIG CHFVLLLTAA PEPSPMPYVP YPRSTEVYVR SIFGPGGTPS
LFPTSCSTKS TFHAVPAHIW DRLMLFGATL DDQAFCCSRL MTYLRGISYK VTVGTLVANE
GRNASEDALT AVITAAYLTI CHQRYLRTQA ISKGIRRLER EHDQKFITRL YSWLFEKSGR
DYIPGRQLEF YAQCRRWLSA GFHLDPRVLV FDESAPCHCR TVIRKALSKF CCFMKWLGQE
CTCFLQPAEG VVGDQGHDNE SYEGSDVDPA ESAISDISGS YVVPGTALQP LYQALDLPDE
IVARACRLTA TVKVSQVDGR IDCETLLGNK TFRTSFVDGA VLETNGPERH NLSFDASQST
MAAGPFSLTY AASAAGLEVR YVGAGLDHRA IFAPGVSPRS NPGEVTAFCS ALYRFNREAQ
RHSLTGNLWF HPEGLIGLFA PFSPGHVWES AKPFCGESTL YTRTWSEVDA VSSPTRPDLG
FMSEPPIPSR AATPTLAAPL PPLAPDPSPP SSAPALDEPA SAATSGVPAI THQTARHRRL
LFTYPDGSKV FAGSLFESTC TWLVNASNVD HCPGGGLCHA FYQRYPASFD AACFVMRDGA
AAYTLTPRPI IHRVAPDYRL EHNPKRLEAA YRETCSRLGT AAYPLLGTGI YQVPIGPSFD
AWERNHRPGD ELYLPELAAR WFEANRPTRP TLTITEDAAR TANLAIELDS ATDVGRACAG
CRVTPGVVQY QFTAGVPGSG KSRSITRADV DVVVVPTREL RNAWRRRGFA AFTPHTAARV
TDGRRVVIDE APSLPPHLLL LHMQRAATVH LLGDPNQIPA IDFEHPGLVP AIRPDLAPTS
WWHVTHRCPA DVCELIRGAY PMIQTTSRVL RSLFWGEPAV GQKLVFTQAA KPANPGSVTV
HDSQGATYTY TTIIATADAR GLIQSSRAHA IVALTRHTEK WVIIDAPGLL REVGISDAIV
NNFFLAGGEI GHQRPSVIPR GNPDANVDTL AAFPPSCQIS AFHQLAEELG HRPAPVAAVL
PPCPELEQGL LYLPQELTTC DSVVTFELTD IVHCRMAAPS QRKAVVSTLV GRYGRRTKLY
NASHSDVRDS LARFIPAIGP VQVTTCELYE LVEAMVEKGQ DGSAVLELDL CNRDVSRITF
FQKDCNKFTT GETIAHGKVG QGISAWSKTF CALFGPWFRA IEKAILALLP QGVFYGDAFD
DTVFSAAVAA AKASMVFEND FSEFDSTQNN FSLGLECAIM EECGMPQGLI RLYHLIRSAW
ILQAPKESLL GFWKKHSGEP GTLLWNTVWN MAVITHCYDF RDLQVAAFKG DDSIVLCSEY
RQSPGAAVLI AGCGLKLKVD FRPMRLYAGV VVAPGLGALP DVVRFAGRLT EKNWGPGPER
ADELRIAVSD FLRKLTNVAQ MCVDVVSRVY GVSPGLVHNL IGMLQAVADG KAHFTESVKP
VLDLTNSILC RVE


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