POLN_HEVCT
ID POLN_HEVCT Reviewed; 1707 AA.
AC Q9IVZ9;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Non-structural polyprotein pORF1;
DE Includes:
DE RecName: Full=Methyltransferase;
DE EC=2.1.1.-;
DE EC=2.7.7.-;
DE Includes:
DE RecName: Full=Putative papain-like cysteine protease;
DE Short=PLP;
DE EC=3.4.22.-;
DE Includes:
DE RecName: Full=NTPase/helicase;
DE EC=3.6.4.-;
DE Includes:
DE RecName: Full=RNA-directed RNA polymerase;
DE Short=RdRp;
DE EC=2.7.7.48;
GN ORFNames=ORF1;
OS Hepatitis E virus genotype 4 (isolate Human/China/T1) (HEV-4) (Hepatitis E
OS virus genotype 4 (isolate Human/China/Ct1)).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC Hepelivirales; Hepeviridae; Orthohepevirus; Hepatitis E virus.
OX NCBI_TaxID=509627;
OH NCBI_TaxID=69079; Bandicota bengalensis (lesser bandicoot rat).
OH NCBI_TaxID=9481; Callithrix.
OH NCBI_TaxID=9536; Cercopithecus hamlyni (Owl-faced monkey) (Hamlyn's monkey).
OH NCBI_TaxID=9534; Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops).
OH NCBI_TaxID=9031; Gallus gallus (Chicken).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9539; Macaca (macaques).
OH NCBI_TaxID=10090; Mus musculus (Mouse).
OH NCBI_TaxID=9598; Pan troglodytes (Chimpanzee).
OH NCBI_TaxID=9520; Saimiri (squirrel monkeys).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=10859372; DOI=10.1099/0022-1317-81-7-1675;
RA Wang Y., Zhang H., Ling R., Li H., Harrison T.J.;
RT "The complete sequence of hepatitis E virus genotype 4 reveals an
RT alternative strategy for translation of open reading frames 2 and 3.";
RL J. Gen. Virol. 81:1675-1686(2000).
CC -!- FUNCTION: Methyltransferase: Displays a capping enzyme activity. This
CC function is necessary since all viral RNAs are synthesized in the
CC cytoplasm, and host capping enzymes are restricted to the nucleus. The
CC enzymatic reaction involves a covalent link between 7-methyl-GMP and
CC the methyltransferase, whereas eukaryotic capping enzymes form a
CC covalent complex only with GMP. Methyltransferase catalyzes transfer of
CC a methyl group from S-adenosylmethionine to GTP and GDP to yield
CC m(7)GTP or m(7)GDP. This enzyme also displays guanylyltransferase
CC activity to form a covalent complex, methyltransferase-m(7)GMP, from
CC which 7-methyl-GMP is transferred to the mRNA to create the cap
CC structure. {ECO:0000250|UniProtKB:Q81862}.
CC -!- FUNCTION: Papain-like cysteine protease: May participate in the
CC processing of polyprotein pORF1 together with cellular proteases and
CC the cleavage of capsid protein ORF2. {ECO:0000250|UniProtKB:Q81862}.
CC -!- FUNCTION: NTPase/helicase: Multi-functional protein that exhibits
CC NTPase and RNA unwinding activities. Hydrolyzes all NTPs efficiently
CC and unwinds RNA duplexes containing 5' overhangs. Possesses a sequence
CC independent RNA-5'-triphosphatase (RTPase) activity suggestive of its
CC role in forming viral cap structure (By similarity). Participates also
CC in viral genome replication, RNA translocation and genome
CC packaging/unpackaging (By similarity). {ECO:0000250|UniProtKB:P29324,
CC ECO:0000250|UniProtKB:Q81862}.
CC -!- FUNCTION: RNA-directed RNA polymerase: Plays an essential role in the
CC virus replication. Binds to the 3'-end of the genomic RNA to initiate
CC viral replication. {ECO:0000250|UniProtKB:Q81862}.
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:0000250|UniProtKB:Q81862};
CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000250|UniProtKB:Q81862}.
CC -!- PTM: It is not yet clear whether the ORF1-encoded polyprotein contains
CC multiple biochemical activities, or undergoes cis or trans- processing
CC to release biochemically distinct peptides. No processing has been
CC observed in mammalian expression systems. However, the baculovirus
CC expressed polyprotein is processed into smaller protein, probably by a
CC cysteine protease.
CC -!- SIMILARITY: Belongs to the hepevirus non-structural polyprotein family.
CC {ECO:0000305}.
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DR EMBL; AJ272108; CAB83209.1; -; Genomic_RNA.
DR SMR; Q9IVZ9; -.
DR PRIDE; Q9IVZ9; -.
DR Proteomes; UP000007242; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0008174; F:mRNA methyltransferase activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0019082; P:viral protein processing; IEA:InterPro.
DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR CDD; cd21557; Macro_X_Nsp3-like; 1.
DR Gene3D; 3.40.220.10; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR027351; (+)RNA_virus_helicase_core_dom.
DR InterPro; IPR002588; Alphavirus-like_MT_dom.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR008748; Hepatitis-E_Cys-pept.
DR InterPro; IPR022202; Hepatitis-E_hinge.
DR InterPro; IPR002589; Macro_dom.
DR InterPro; IPR043472; Macro_dom-like.
DR InterPro; IPR044371; Macro_X_NSP3-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR InterPro; IPR001788; Tymovirus_RNA-dep_RNA_pol.
DR Pfam; PF12526; DUF3729; 1.
DR Pfam; PF05417; Peptidase_C41; 1.
DR Pfam; PF00978; RdRP_2; 1.
DR Pfam; PF01443; Viral_helicase1; 1.
DR Pfam; PF01660; Vmethyltransf; 1.
DR SMART; SM00506; A1pp; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF52949; SSF52949; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS51743; ALPHAVIRUS_MT; 1.
DR PROSITE; PS51154; MACRO; 1.
DR PROSITE; PS51657; PSRV_HELICASE; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE 3: Inferred from homology;
KW ATP-binding; Helicase; Host cytoplasm; Hydrolase; Methyltransferase;
KW Nucleotide-binding; Nucleotidyltransferase; Protease; RNA-binding;
KW RNA-directed RNA polymerase; Thiol protease; Transferase;
KW Viral RNA replication.
FT CHAIN 1..1707
FT /note="Non-structural polyprotein pORF1"
FT /id="PRO_0000334532"
FT DOMAIN 56..240
FT /note="Alphavirus-like MT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01079"
FT DOMAIN 789..937
FT /note="Macro"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT DOMAIN 948..1096
FT /note="(+)RNA virus helicase ATP-binding"
FT DOMAIN 1097..1230
FT /note="(+)RNA virus helicase C-terminal"
FT DOMAIN 1468..1579
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 60..240
FT /note="Methyltransferase"
FT /evidence="ECO:0000250"
FT REGION 239..439
FT /note="Y-domain"
FT /evidence="ECO:0000250"
FT REGION 440..610
FT /note="Putative papain-like cysteine protease"
FT /evidence="ECO:0000250"
FT REGION 714..792
FT /note="Hinge"
FT /evidence="ECO:0000250"
FT REGION 745..783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 799..956
FT /note="X-domain"
FT /evidence="ECO:0000250"
FT REGION 974..1218
FT /note="NTPase/helicase"
FT /evidence="ECO:0000250"
FT REGION 1221..1707
FT /note="RNA-directed RNA polymerase"
FT /evidence="ECO:0000250"
FT COMPBIAS 758..772
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 989..996
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1707 AA; 187298 MW; 2A80F303AB98C4EC CRC64;
MEAHQFIKAP GVTTAIEQAA LAAANSALAN AVVVRPFLSR LQTEILINLM QPWQLVFRPE
VLWNHPIQRV IHNELEQYCR ARAGRCLEEG AHPRSINDDP NVLHRCFLKP VGRDVQRWYT
APTRGPAANC RRSALRGLPP VDRTYCFDGF SGCTFAAETG VALYSLHDLW PADVAEAMAR
HGMTRLYAAL HLPPEVLLPP GTYHTTSYLL IHDGDRAVIT YEGDSSAGYN HDVSILRAWI
RTTKVTGDHP LVIERVRAVG CHFVLLLTAA PEPSPMPYVP YPRSTEVYVR SIFGPGGSPS
LFPSACSTKS TFHAVPVHIW DRLMLFGATL DDQAFCCSRL MTYLRGISYK VTVGALVANE
GWNASEDALT AVITAAYLTI CHQRYLRTQA ISKGMKRLEL EHAQKFITRL YSWLFEKSGR
DYIPGRQLQF YAQCRRWLSA GFHLDPRVLV FDEAAPCRCR SFLRKAATKF CCFMRWLGQD
CTCFLQPIEG RVGEQGYDNE AFEGSDIDPA EEATVSIAGS YIVTGSQLQP LYQALGIPSD
LAARASRLTA TVEVSDADGR LTCKTTMGNK TFSTVFTDGT QLEANGPEQY VLSFDPAKQT
MAAGPHSLSY TLTSAGLEVH VVSAGLDCKV VFQSGVAAPS AAGEVTAFCS ALYRFNRCVQ
RHSLIGGLWY HPEGLVGLFP PFSPGHSWES ANPFCGESTL YTRTWSVSGF SSCFSPLEPC
VPSMPPPAEV NTPVVLDALP SEIMEPAQPP ASEPAAPPSD SVDNSFSPTS SGAPIAPPAP
ALPVTHLSGP RRRLLHTYPD GSKVYAGSLF ESECTWLVNA SNPGHRPGGG LCHAFYQRFP
ESFDPAEFIM SDGFAAYTLT PRPIIHAVAP DYRVEHNPKR LEAAYRETCS RRGTAAYPLL
GVGIYRVPVG LSFDAWERNH RPGDELYLTE PAIAWFEANR PTLPALTITE DTARTANLAL
ELDAATEVGR ACVGCRVEPG VIHYQFTAGV PGSGKSRSVQ QGDVDVIVVP TRELRNSWRR
RGFAAYTPHT AVRVTRGRRV VIDEAPSLPP HLLLLHMQRA SSVHLLGDPN QIPAIDFEHA
GLVPAIRPEL VPTKWWHLTY RCPADVCELI RGAYPKIQTA SRVLRSLFWE EPPVGQNLVF
TQAAKAANPG AITVHEAQGA TFTETTIIAT ADARGLIQSS RAHAIVALTR HTEKCVVVDA
PGLLREVGIS DAIVNNFFLS GGQIGQHRPS VIRRGTIDNN VDTLDAFPPS CQFSAYHQLA
EELGHRPAPI AAVLPPCPEL EQGLLYMPQE LTTSDSVLTF ELTDIVHCRM AAPSQRRAVL
STLVGRYGRR TKLYEAAHTD VRGSLNHFIP ELGPINVTTC ELYELVEAMV EKGQDGSAVL
ELDLCSRDVS RITFFQKDCN KFTTGETIAH GKVGQGISAW SKTFCALFGP WFRAIEKEIL
AALAPNVFYG DAYEDTVLAA AVAGAPGCKV FENDFSEFDS TQNNFSLGLE CIIMEECGMP
QWMIRLYHLV RSAWILQAPK ESLRGFWKKH SGEPGTLLWN TVWNMAVIAH CYEFRDLKVA
AFKGDDSVVL CSDYRQSRDA AVLIAGCGLK LKVDFRPIGL YAGVVVAPGL GTLPDVVRFA
GRLSEKNWGP GPERAEQLRL AVCDFLRKLT NVAQVCVDVV SQVYGVSPGL VHNLIGMLQT
IADGKAHFTE TIKPVLDLTS SIIYRVE
