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POLN_HEVBU
ID   POLN_HEVBU              Reviewed;        1693 AA.
AC   P29324; Q81873;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   03-AUG-2022, entry version 112.
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 1 (isolate Human/Burma) (HEV-1).
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC   Hepelivirales; Hepeviridae; Orthohepevirus; Hepatitis E virus.
OX   NCBI_TaxID=31767;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=1926770; DOI=10.1016/0042-6822(91)90760-9;
RA   Tam A.W., Smith M.M., Guerra M.E., Huang C.-C., Bradley D.W., Fry K.E.,
RA   Reyes G.R.;
RT   "Hepatitis E virus (HEV): molecular cloning and sequencing of the full-
RT   length viral genome.";
RL   Virology 185:120-131(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 967-1693.
RX   PubMed=2107574; DOI=10.1126/science.2107574;
RA   Reyes G.R., Purdy M.A., Kim J.P., Luk K.-C., Young L.M., Fry K.E.,
RA   Bradley D.W.;
RT   "Isolation of a cDNA from the virus responsible for enterically transmitted
RT   non-A, non-B hepatitis.";
RL   Science 247:1335-1339(1990).
RN   [3]
RP   IDENTIFICATION.
RX   PubMed=1589964; DOI=10.1007/bf01703066;
RA   Fry K.E., Tam A.W., Smith M.M., Kim J.P., Luk K.-C., Young L.M., Piatak M.,
RA   Feldman R.A., Yun K.Y., Purdy M.A., McCaustland K.A., Bradley D.W.,
RA   Reyes G.R.;
RT   "Hepatitis E virus (HEV): strain variation in the nonstructural gene region
RT   encoding consensus motifs for an RNA-dependent RNA polymerase and an
RT   ATP/GTP binding site.";
RL   Virus Genes 6:173-185(1992).
RN   [4]
RP   POSSIBLE PROTEOLYTIC PROCESSING OF POLYPROTEIN.
RX   PubMed=16725054; DOI=10.1186/1743-422x-3-38;
RA   Sehgal D., Thomas S., Chakraborty M., Jameel S.;
RT   "Expression and processing of the Hepatitis E virus ORF1 nonstructural
RT   polyprotein.";
RL   Virol. J. 3:38-38(2006).
RN   [5]
RP   FUNCTION (NTPASE/HELICASE), AND MUTAGENESIS OF LYS-981 AND
RP   1029-ASP-GLU-1030.
RC   STRAIN=Isolate Human/India/Lole/2000;
RX   PubMed=20071563; DOI=10.1128/jvi.02130-09;
RA   Karpe Y.A., Lole K.S.;
RT   "NTPase and 5' to 3' RNA duplex-unwinding activities of the hepatitis E
RT   virus helicase domain.";
RL   J. Virol. 84:3595-3602(2010).
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 (PubMed:20071563) (By similarity).
CC       Participates also in viral genome replication, RNA translocation and
CC       genome packaging/unpackaging (By similarity).
CC       {ECO:0000250|UniProtKB:Q81862, ECO:0000269|PubMed:20071563}.
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; M73218; AAA45734.1; -; Genomic_RNA.
DR   EMBL; M32400; AAA03206.1; -; mRNA.
DR   PIR; A40778; MNWWHE.
DR   SMR; P29324; -.
DR   Proteomes; UP000007243; 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; PF01661; Macro; 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; 1.
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   1: Evidence at protein level;
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..1693
FT                   /note="Non-structural polyprotein pORF1"
FT                   /id="PRO_0000100132"
FT   DOMAIN          56..240
FT                   /note="Alphavirus-like MT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01079"
FT   DOMAIN          775..921
FT                   /note="Macro"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT   DOMAIN          934..1082
FT                   /note="(+)RNA virus helicase ATP-binding"
FT   DOMAIN          1083..1216
FT                   /note="(+)RNA virus helicase C-terminal"
FT   DOMAIN          1454..1565
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   REGION          60..240
FT                   /note="Methyltransferase"
FT   REGION          239..439
FT                   /note="Y-domain"
FT   REGION          440..610
FT                   /note="Putative papain-like cysteine protease"
FT   REGION          712..778
FT                   /note="Hinge"
FT   REGION          732..768
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          785..942
FT                   /note="X-domain"
FT   REGION          960..1204
FT                   /note="NTPase/helicase"
FT   REGION          1207..1693
FT                   /note="RNA-directed RNA polymerase"
FT   COMPBIAS        735..756
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         975..982
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         981
FT                   /note="K->A: 70% loss of ATPase activity; complete lost of
FT                   unwinding ability."
FT                   /evidence="ECO:0000269|PubMed:20071563"
FT   MUTAGEN         1029..1030
FT                   /note="DE->AA: 50% loss of ATPase activity; complete loss
FT                   of unwinding ability."
FT                   /evidence="ECO:0000269|PubMed:20071563"
SQ   SEQUENCE   1693 AA;  185192 MW;  2F355E46E9ED219B CRC64;
     MEAHQFIKAP GITTAIEQAA LAAANSALAN AVVVRPFLSH QQIEILINLM QPRQLVFRPE
     VFWNHPIQRV IHNELELYCR ARSGRCLEIG AHPRSINDNP NVVHRCFLRP VGRDVQRWYT
     APTRGPAANC RRSALRGLPA ADRTYCLDGF SGCNFPAETG IALYSLHDMS PSDVAEAMFR
     HGMTRLYAAL HLPPEVLLPP GTYRTASYLL IHDGRRVVVT YEGDTSAGYN HDVSNLRSWI
     RTTKVTGDHP LVIERVRAIG CHFVLLLTAA PEPSPMPYVP YPRSTEVYVR SIFGPGGTPS
     LFPTSCSTKS TFHAVPAHIW DRLMLFGATL DDQAFCCSRL MTYLRGISYK VTVGTLVANE
     GWNASEDALT AVITAAYLTI CHQRYLRTQA ISKGMRRLER EHAQKFITRL YSWLFEKSGR
     DYIPGRQLEF YAQCRRWLSA GFHLDPRVLV FDESAPCHCR TAIRKALSKF CCFMKWLGQE
     CTCFLQPAEG AVGDQGHDNE AYEGSDVDPA ESAISDISGS YVVPGTALQP LYQALDLPAE
     IVARAGRLTA TVKVSQVDGR IDCETLLGNK TFRTSFVDGA VLETNGPERH NLSFDASQST
     MAAGPFSLTY AASAAGLEVR YVAAGLDHRA VFAPGVSPRS APGEVTAFCS ALYRFNREAQ
     RHSLIGNLWF HPEGLIGLFA PFSPGHVWES ANPFCGESTL YTRTWSEVDA VSSPARPDLG
     FMSEPSIPSR AATPTLAAPL PPPAPDPSPP PSAPALAEPA SGATAGAPAI THQTARHRRL
     LFTYPDGSKV FAGSLFESTC TWLVNASNVD HRPGGGLCHA FYQRYPASFD AASFVMRDGA
     AAYTLTPRPI IHAVAPDYRL EHNPKRLEAA YRETCSRLGT AAYPLLGTGI YQVPIGPSFD
     AWERNHRPGD ELYLPELAAR WFEANRPTRP TLTITEDVAR TANLAIELDS ATDVGRACAG
     CRVTPGVVQY QFTAGVPGSG KSRSITQADV DVVVVPTREL RNAWRRRGFA AFTPHTAARV
     TQGRRVVIDE APSLPPHLLL LHMQRAATVH LLGDPNQIPA IDFEHAGLVP AIRPDLGPTS
     WWHVTHRWPA DVCELIRGAY PMIQTTSRVL RSLFWGEPAV GQKLVFTQAA KPANPGSVTV
     HEAQGATYTE TTIIATADAR GLIQSSRAHA IVALTRHTEK CVIIDAPGLL REVGISDAIV
     NNFFLAGGEI GHQRPSVIPR GNPDANVDTL AAFPPSCQIS AFHQLAEELG HRPVPVAAVL
     PPCPELEQGL LYLPQELTTC DSVVTFELTD IVHCRMAAPS QRKAVLSTLV GRYGGRTKLY
     NASHSDVRDS LARFIPAIGP VQVTTCELYE LVEAMVEKGQ DGSAVLELDL CNRDVSRITF
     FQKDCNKFTT GETIAHGKVG QGISAWSKTF CALFGPWFRA IEKAILALLP QGVFYGDAFD
     DTVFSAAVAA AKASMVFEND FSEFDSTQNN FSLGLECAIM EECGMPQWLI RLYHLIRSAW
     ILQAPKESLR GFWKKHSGEP GTLLWNTVWN MAVITHCYDF RDFQVAAFKG DDSIVLCSEY
     RQSPGAAVLI AGCGLKLKVD FRPIGLYAGV VVAPGLGALP DVVRFAGRLT EKNWGPGPER
     AEQLRLAVSD FLRKLTNVAQ MCVDVVSRVY GVSPGLVHNL IGMLQAVADG KAHFTESVKP
     VLDLTNSILC RVE
 
 
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