位置:首页 > 蛋白库 > POLN_HEVMG
POLN_HEVMG
ID   POLN_HEVMG              Reviewed;        1708 AA.
AC   Q6J8G2; Q9YK10;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 80.
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 3 (isolate Swine/United States/swUS1) (HEV-3)
OS   (Hepatitis E virus genotype 3 (isolate Swine/United States/Meng)).
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC   Hepelivirales; Hepeviridae; Orthohepevirus; Hepatitis E virus.
OX   NCBI_TaxID=512345;
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=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=9811705; DOI=10.1128/jvi.72.12.9714-9721.1998;
RA   Meng X.J., Halbur P.G., Shapiro M.S., Govindarajan S., Bruna J.D.,
RA   Mushahwar I.K., Purcell R.H., Emerson S.U.;
RT   "Genetic and experimental evidence for cross-species infection by swine
RT   hepatitis E virus.";
RL   J. Virol. 72:9714-9721(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate pSHEV-1, Isolate pSHEV-2, and Isolate pSHEV-3;
RX   PubMed=15650181; DOI=10.1128/jvi.79.3.1552-1558.2005;
RA   Huang Y.W., Haqshenas G., Kasorndorkbua C., Halbur P.G., Emerson S.U.,
RA   Meng X.J.;
RT   "Capped RNA transcripts of full-length cDNA clones of swine hepatitis E
RT   virus are replication competent when transfected into Huh7 cells and
RT   infectious when intrahepatically inoculated into pigs.";
RL   J. Virol. 79:1552-1558(2005).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF082843; AAC97208.1; -; Genomic_RNA.
DR   EMBL; AY575857; AAT40994.1; -; Genomic_RNA.
DR   EMBL; AY575858; AAT40997.1; -; Genomic_RNA.
DR   EMBL; AY575859; AAT41000.1; -; Genomic_RNA.
DR   SMR; Q6J8G2; -.
DR   Proteomes; UP000001028; Genome.
DR   Proteomes; UP000008858; Genome.
DR   Proteomes; UP000008859; Genome.
DR   Proteomes; UP000008989; 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..1708
FT                   /note="Non-structural polyprotein pORF1"
FT                   /id="PRO_5000055029"
FT   DOMAIN          56..240
FT                   /note="Alphavirus-like MT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01079"
FT   DOMAIN          790..936
FT                   /note="Macro"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT   DOMAIN          949..1097
FT                   /note="(+)RNA virus helicase ATP-binding"
FT   DOMAIN          1098..1231
FT                   /note="(+)RNA virus helicase C-terminal"
FT   DOMAIN          1469..1580
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..793
FT                   /note="Hinge"
FT                   /evidence="ECO:0000250"
FT   REGION          800..957
FT                   /note="X-domain"
FT                   /evidence="ECO:0000250"
FT   REGION          975..1219
FT                   /note="NTPase/helicase"
FT                   /evidence="ECO:0000250"
FT   REGION          1222..1708
FT                   /note="RNA-directed RNA polymerase"
FT                   /evidence="ECO:0000250"
FT   BINDING         990..997
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        4
FT                   /note="Q -> H (in Ref. 1; AAC97208)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        70
FT                   /note="V -> A (in Ref. 1; AAC97208)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        85
FT                   /note="R -> C (in Ref. 1; AAC97208)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        95
FT                   /note="S -> F (in Ref. 1; AAC97208)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        193
FT                   /note="P -> L (in Ref. 1; AAC97208)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        690
FT                   /note="S -> P (in Ref. 1; AAC97208)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        748
FT                   /note="E -> K (in Ref. 1; AAC97208)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1708 AA;  187395 MW;  CB1C6A04193571BC CRC64;
     MEAQQFIKAP GITTAIEQAA LAAANSALAN AVVVRPFLSR VQTEILINLM QPRQLVFRPE
     VLWNHPIQRV IHNELEQYCR ARAGRCLEVG AHPRSINDNP NVLHRCFLRP VGRDVQRWYS
     APTRGPAANC RRSALRGLPP VDRTYCFDGF SRCAFAAETG VALYSLHDLW PADVAEAMAR
     HGMTRLYAAL HLPPEVLLPP GTYHTTSYLL IHDGDRAVVT YEGDTSAGYN HDVSILRAWI
     RTTKIVGDHP LVIERVRAIG CHFVLLLTAA PEPSPMPYVP YPRSTEVYVR SIFGPGGSPS
     LFPSACSTKS TFHAVPVHIW DRLMLFGATL DDQAFCCSRL MTYLRGISYK VTVGALVANE
     GWNASEDALT AVITAAYLTI CHQRYLRTQA ISKGMRRLEV EHAQKFITRL YSWLFEKSGR
     DYIPGRQLQF YAQCRRWLSA GFHLDPRVLV FDESVPCRCR TFLKKVAGKF CCFMRWLGQE
     CTCFLEPAEG LVGDYGHDNE AYEGSEVDPA EPAHLDVSGT YAVHGRQLEA LYRALNVPHD
     IAARASRLTA TVELTASPDR LECRTVLGNK TFRTTVVDGA HLEANGPEQY VLSFDASRQS
     MGAGSHSLTY ELTPAGLQVR ISSNGLDCTA TFPPGGAPSA APGEVAAFCS ALYRYNRFTQ
     RHSLTGGLWL HPEGLLGIFP PFSPGHIWES ANPFCGEGTL YTRTWSTSGF SSDFSPPEAA
     APVLAAAPGL PHPTPPVSDI WVLPPPSEES QVDAASVPPA PEPAGLPSSI VLTLPPPLPP
     VRKPPTPPPS RTRRLLYTYP DGAKVYAGSL FESDCNWLVN ASNPGHRPGG GLCHAFYQRF
     PEAFYPTEFI MREGLAAYTL TPRPIIHAVA PDYRVEQNPK RLEAAYRETC SRRGTAAYPL
     LGSGIYQVPV SLSFDAWERN HRPGDELYLT EPAAAWFEAN KPAQPALTIT EDTARTANLA
     LEIDAATDVG RACAGCTISP GIVHYQFTAG VPGSGKSRSI QQGDVDVVVV PTRELRNSWR
     RRGFAAFTPH TAARVTIGRR VVIDEAPSLP PHLLLLHMQR ASSVHLLGDP NQIPAIDFEH
     AGLVPAIRPE LAPTSWWHVT HRCPADVCEL IRGAYPKIQT TSRVLRSLFW NEPAIGQKLV
     FTQAAKAANP GAITVHEAQG ATFTETTIIA TADARGLIQS SRAHAIVALT RHTEKCVILD
     APGLLREVGI SDVIVNNFFL AGGEVGHHRP SVIPRGNPDQ NLGTLQAFPP SCQISAYHQL
     AEELGHRPAP VAAVLPPCPE LEQGLLYMPQ ELTVSDSVLV FELTDIVHCR MAAPSQRKAV
     LSTLVGRYGR RTKLYEAAHS DVRESLARFI PTIGPVQATT CELYELVEAM VEKGQDGSAV
     LELDLCNRDV SRITFFQKDC NKFTTGETIA HGKVGQGISA WSKTFCALFG PWFRAIEKEI
     LALLPPNIFY GDAYEESVFA AAVSGAGSCM VFENDFSEFD STQNNFSLGL ECVVMEECGM
     PQWLIRLYHL VRSAWILQAP KESLKGFWKK HSGEPGTLLW NTVWNMAIIA HCYEFRDFRV
     AAFKGDDSVV LCSDYRQSRN AAALIAGCGL KLKVDYRPIG LYAGVVVAPG LGTLPDVVRF
     AGRLSEKNWG PGPERAEQLR LAVCDFLRGL TNVAQVCVDV VSRVYGVSPG LVHNLIGMLQ
     TIADGKAHFT ETIKPVLDLT NSIIQRVE
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024