POLN_AHEV
ID POLN_AHEV Reviewed; 1531 AA.
AC Q6QLN1; Q913Y9;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 82.
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 Avian hepatitis E virus (isolate Chicken/California/Meng) (AHEV).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC Hepelivirales; Hepeviridae; Orthohepevirus.
OX NCBI_TaxID=516993;
OH NCBI_TaxID=9031; Gallus gallus (Chicken).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=15166445; DOI=10.1099/vir.0.79841-0;
RA Huang F.F., Sun Z.F., Emerson S.U., Purcell R.H., Shivaprasad H.L.,
RA Pierson F.W., Toth T.E., Meng X.J.;
RT "Determination and analysis of the complete genomic sequence of avian
RT hepatitis E virus (avian HEV) and attempts to infect rhesus monkeys with
RT avian HEV.";
RL J. Gen. Virol. 85:1609-1618(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 901-1531.
RX PubMed=11562538; DOI=10.1099/0022-1317-82-10-2449;
RA Haqshenas G., Shivaprasad H.L., Woolcock P.R., Read D.H., Meng X.J.;
RT "Genetic identification and characterization of a novel virus related to
RT human hepatitis E virus from chickens with hepatitis-splenomegaly syndrome
RT in the United States.";
RL J. Gen. Virol. 82:2449-2462(2001).
CC -!- FUNCTION: Methyltransferase displays a cytoplasmic capping enzyme
CC activity. This function is necessary since all viral RNAs are
CC synthesized in the cytoplasm, and host capping enzymes are restricted
CC to the nucleus. The enzymatic reaction involves a covalent link between
CC 7-methyl-GMP and the methyltransferase, whereas eukaryotic capping
CC enzymes form a covalent complex only with GMP. Methyltransferase
CC catalyzes transfer of a methyl group from S-adenosylmethionine to GTP
CC and GDP to yield m(7)GTP or m(7)GDP. GMP, GpppG, and GpppA were poor
CC substrates for the methyltransferase. This enzyme also displays
CC guanylyltransferase activity to form a covalent complex,
CC methyltransferase-m(7)GMP, from which 7-methyl-GMP is transferred to
CC the mRNA to create the cap structure. Cap analogs such as m(7)GTP,
CC m(7)GDP, et(2)m(7)GMP, and m(2)et(7)GMP inhibit the methyltransferase
CC reaction (By similarity). {ECO:0000250}.
CC -!- FUNCTION: RNA-directed RNA polymerase plays an essential role in the
CC virus replication. Binds to the 3'-end of the genomic RNA, probably to
CC initiate replication (By similarity). {ECO:0000255|PROSITE-
CC ProRule:PRU00539}.
CC -!- FUNCTION: Helicase region exhibits NTPase and RNA unwinding activities.
CC {ECO:0000250}.
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 -!- 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.
CC -!- SIMILARITY: Belongs to the hepevirus non-structural polyprotein family.
CC {ECO:0000305}.
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DR EMBL; AY535004; AAS45830.1; -; Genomic_RNA.
DR EMBL; AY043166; AAL13366.1; -; Genomic_RNA.
DR RefSeq; YP_009001465.1; NC_023425.1.
DR SMR; Q6QLN1; -.
DR PRIDE; Q6QLN1; -.
DR GeneID; 18263429; -.
DR KEGG; vg:18263429; -.
DR Proteomes; UP000007439; Genome.
DR Proteomes; UP000139094; Genome.
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: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; 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; 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; Hydrolase; Methyltransferase; Nucleotide-binding;
KW Nucleotidyltransferase; Protease; RNA-binding; RNA-directed RNA polymerase;
KW Thiol protease; Transferase; Viral RNA replication.
FT CHAIN 1..1531
FT /note="Non-structural polyprotein pORF1"
FT /id="PRO_0000334529"
FT DOMAIN 56..239
FT /note="Alphavirus-like MT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01079"
FT DOMAIN 612..761
FT /note="Macro"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT DOMAIN 786..924
FT /note="(+)RNA virus helicase ATP-binding"
FT DOMAIN 925..1058
FT /note="(+)RNA virus helicase C-terminal"
FT DOMAIN 1295..1406
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 60..239
FT /note="Methyltransferase"
FT /evidence="ECO:0000250"
FT REGION 238..434
FT /note="Y-domain"
FT /evidence="ECO:0000250"
FT REGION 435..621
FT /note="Putative papain-like cysteine protease"
FT /evidence="ECO:0000250"
FT REGION 561..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 622..786
FT /note="X-domain"
FT /evidence="ECO:0000250"
FT REGION 803..1046
FT /note="NTPase/helicase"
FT /evidence="ECO:0000250"
FT REGION 1049..1531
FT /note="RNA-directed RNA polymerase"
FT /evidence="ECO:0000250"
FT BINDING 818..825
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1531 AA; 168040 MW; 730F80BA135CEA95 CRC64;
MDVSQFAESK GVKTALEAAA LAAANTALRN ARVVTPYLTQ QQTKNLLELF RGAQLRFEPR
DNWAHPVQRV VHDALEQYVR RAAGPNCLEV GAHPRSINRH QASHRCFLPP VGRDEQRWQV
APRRGLCNLI RRALLNGVKV AREFCQLGFG ACSHQCEVGI ALYSLHDMRP ADVACAMARH
NMRTMYVVLH LPEEAMLPPG SYSNKFYNTV NTADKCIITY ADDSCAGYVH KREVLQDWIT
TTGVSGRHPM LIERVRAIGC HFVLLCTATQ PCPMPYTPYP SSNTVYVRNV YGPALGAGLF
TPKCCVDATF YPVPRRVWQR LMMFGTTLDD DAFCCSRLLT YLRGISTKVT VGNIVANEGW
QPEEQQLTAV AIAAYLTVCH QRWVRTQGIA RGVRRLQAEH AQQFWFKVWE LFTNTGTVPG
YSAGFYRQLA TWISGGLTID FERRVFDKRV KCGCCCVCER RPADPGCLCI DDFPDGANGL
VKLKKWPIRA GTKSAVSKWA QVRVRADSTE DLIDLSVPKL LTLKELAAAA IRKQPSAPPS
LHILDRRPVG DPRRPVNCAP PAVSAGPVPA PPGNPVIESV QGSGAGGPEV SESQPGLTPT
REVTNMPLPP QRGQEEVLAV LPSGARVIVG NLLDVAADWL VNPANRDHQP GGGLCGMFHR
RWPHLWPVCG EVQDLPTGPV IFQQGPPKVI HAPGPDYRIK PDPDGLRRVY AVVHQAHGTV
ASPLISAGIY RAPARESFEA WAATARDGDL LVVQRSMAQH IRDFVLNEGR HRPRELHVDR
AMADMVNYGL ATEPEPYNEL VKGVEVAPMT VKYALIAGVP GSGKSSSVDH RGAVVITPTK
TLAREWSARG ATAVTPHVAA SAAPEGRVIV DEAYAIPPHL LVASLRRARD VVMLGDPHQI
PALDFDGRCL TSAVDLGLQP TSWRTVSHRC PWDVCIFLRT DYPTITTTSR VLRSVVFTGE
TIGQKIVFTQ VAKQSNPGSI TVHEAQGSTF DQTTIIATLD ARGLIASSRA HAIVALTRHR
ERCSVIDVGG VLVEIGVTDA MFNNIEMQLV RPDAAAPAGV LRAPDDTVDG LLDIPPAHTD
VAAVLTAEAI GHAPLELAAI NPPGPVLEQG LLYMPARLDG RDEVVKLQLS DTVHCRLAAP
TSRLAVINTL VGRYGKATKL PEVEYDLMDT IAQFWHHIGP INPSTLEYAE MCEAMLSKGQ
DGSLIVHLDL QDADCSRITF FQKDCAKFTL DDPVAHGKVG QGISAWPKTL CALFGPWFRA
IEKHLVAGLP PGYYYGDLYT EADLHRSVLC APAGHLVFEN DFSEFDSTQN NVSLDLECEL
MRRFGMPDWM VALYHLVRSY WLLVAPKEAL RGCWKKHSGE PGTLLWNTVW NMTVLHHVYE
FDRPSVLCFK GDDSVVVCES VRARPEGVSL VADCGLKMKD KTGPCGAFSN LLIFPGAGVV
CDLLRQWGRL TDKNWGPDIQ RMQDLEQACK DFVARVVTQG KEMLTIQLVA GYYGVEVGMV
EVVWGALKAC AAARETLVTN RLPVLNLSKE D
