RPOA_PRRSB
ID RPOA_PRRSB Reviewed; 3961 AA.
AC Q8B912; Q8B911;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 3.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Replicase polyprotein 1ab;
DE AltName: Full=ORF1ab polyprotein;
DE Contains:
DE RecName: Full=Nsp1;
DE EC=3.4.22.-;
DE Contains:
DE RecName: Full=Nsp1-alpha papain-like cysteine proteinase;
DE EC=3.4.22.-;
DE AltName: Full=PCP1-alpha;
DE Contains:
DE RecName: Full=Nsp1-beta papain-like cysteine proteinase;
DE EC=3.4.22.-;
DE AltName: Full=PCP1-beta;
DE Contains:
DE RecName: Full=Nsp2 cysteine proteinase;
DE EC=3.4.19.12;
DE EC=3.4.22.-;
DE AltName: Full=CP2;
DE Short=CP;
DE Contains:
DE RecName: Full=Non-structural protein 3;
DE Short=Nsp3;
DE Contains:
DE RecName: Full=3C-like serine proteinase;
DE Short=3CLSP;
DE EC=3.4.21.-;
DE AltName: Full=Nsp4;
DE Contains:
DE RecName: Full=Non-structural protein 5-6-7;
DE Short=Nsp5-6-7;
DE Contains:
DE RecName: Full=Non-structural protein 5;
DE Short=Nsp5;
DE Contains:
DE RecName: Full=Non-structural protein 6;
DE Short=Nsp6;
DE Contains:
DE RecName: Full=Non-structural protein 7-alpha;
DE Short=Nsp7-alpha;
DE Contains:
DE RecName: Full=Non-structural protein 7-beta;
DE Short=Nsp7-beta;
DE Contains:
DE RecName: Full=Non-structural protein 8;
DE Short=Nsp8;
DE Contains:
DE RecName: Full=RNA-directed RNA polymerase;
DE Short=Pol;
DE Short=RdRp;
DE EC=2.7.7.48;
DE AltName: Full=Nsp9;
DE Contains:
DE RecName: Full=Helicase;
DE Short=Hel;
DE EC=3.6.4.12;
DE EC=3.6.4.13;
DE AltName: Full=Nsp10;
DE Contains:
DE RecName: Full=Uridylate-specific endoribonuclease nsp11;
DE EC=4.6.1.-;
DE AltName: Full=Non-structural protein 11;
DE Short=Nsp11;
DE Contains:
DE RecName: Full=Non-structural protein 12;
DE Short=Nsp12;
GN Name=rep; ORFNames=1a-1b;
OS Porcine reproductive and respiratory syndrome virus (strain HB-1) (PRRSV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Arnidovirineae; Arteriviridae; unclassified Arteriviridae.
OX NCBI_TaxID=300563;
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=15221535; DOI=10.1007/s00705-004-0292-0;
RA Gao Z.Q., Guo X., Yang H.C.;
RT "Genomic characterization of two Chinese isolates of porcine respiratory
RT and reproductive syndrome virus.";
RL Arch. Virol. 149:1341-1351(2004).
CC -!- FUNCTION: The replicase polyprotein 1ab is a multifunctional protein:
CC it contains the activities necessary for the transcription of negative
CC stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as
CC well as proteinases responsible for the cleavage of the polyprotein
CC into functional products.
CC -!- FUNCTION: Nsp1 is essential for viral subgenomic mRNA synthesis.
CC {ECO:0000250}.
CC -!- FUNCTION: Nsp1-alpha inhibits IFN-beta production. Counteracts the
CC action of NF-kappaB by decreasing the phosphorylation of IkappaB-alpha,
CC such that the degradation of IkappaB-alpha is suppressed. This leads to
CC the blockage of NF-kappaB nuclear translocation and thus interference
CC of NF-kappaB activation. Also seems to inhibit IRF3-dependent pathways
CC (By similarity). {ECO:0000250}.
CC -!- FUNCTION: Nsp2 cysteine proteinase which cleaves the nsp2/nsp3 site in
CC the polyprotein. Also displays deubiquitinating and deISGylase
CC activities. The deubiquitinating activity cleaves both ubiquitinated
CC and ISGylated products and may therefore regulate ubiquitin and ISG15
CC dependent host innate immunity. Deubiquitinates host NFKBIA, thereby
CC interfering with NFKBIA degradation and impairing subsequent NF-kappa-B
CC activation (By similarity). {ECO:0000250}.
CC -!- FUNCTION: The 3C-like serine proteinase chain is responsible for the
CC majority of cleavages as it cleaves the C-terminus of the polyprotein.
CC {ECO:0000250}.
CC -!- FUNCTION: The helicase chain, which contains a zinc finger structure,
CC displays RNA and DNA duplex-unwinding activities with 5' to 3'
CC polarity. {ECO:0000250}.
CC -!- FUNCTION: [Uridylate-specific endoribonuclease nsp11]: Plays a role in
CC viral transcription/replication and prevents the simultaneous
CC activation of host cell dsRNA sensors, such as MDA5/IFIH1, OAS, and PKR
CC (By similarity). Acts by degrading the 5'-polyuridines generated during
CC replication of the poly(A) region of viral genomic and subgenomic RNAs.
CC Catalyzes a two-step reaction in which a 2'3'-cyclic phosphate (2'3'-
CC cP) is first generated by 2'-O transesterification, which is then
CC hydrolyzed to a 3'-phosphate (3'-P) (By similarity). If not degraded,
CC poly(U) RNA would hybridize with poly(A) RNA tails and activate host
CC dsRNA sensors (By similarity). {ECO:0000250|UniProtKB:P0C6X7,
CC ECO:0000250|UniProtKB:P19811}.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC residue protein attached to proteins as an intracellular targeting
CC signal).; EC=3.4.19.12;
CC -!- CATALYTIC ACTIVITY: [Uridylate-specific endoribonuclease nsp11]:
CC Reaction=uridylyl-uridylyl-ribonucleotide-RNA = a 3'-end uridylyl-
CC 2',3'-cyclophospho-uridine-RNA + a 5'-end dephospho-ribonucleoside-
CC RNA; Xref=Rhea:RHEA:67732, Rhea:RHEA-COMP:13936, Rhea:RHEA-
CC COMP:17334, Rhea:RHEA-COMP:17335, ChEBI:CHEBI:138284,
CC ChEBI:CHEBI:173079, ChEBI:CHEBI:173080;
CC Evidence={ECO:0000250|UniProtKB:P19811};
CC -!- SUBCELLULAR LOCATION: [Nsp1]: Host nucleus {ECO:0000250}. Host
CC cytoplasm {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Nsp1-alpha papain-like cysteine proteinase]:
CC Host nucleus {ECO:0000250}. Host cytoplasm {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Nsp1-beta papain-like cysteine proteinase]: Host
CC cytoplasm {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Nsp2 cysteine proteinase]: Host membrane
CC {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 3]: Host membrane
CC {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 5-6-7]: Host membrane
CC {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [3C-like serine proteinase]: Host cytoplasm
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [RNA-directed RNA polymerase]: Host cytoplasm,
CC host perinuclear region {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Helicase]: Host cytoplasm, host perinuclear
CC region {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=2;
CC Name=Replicase polyprotein 1ab; Synonyms=pp1ab;
CC IsoId=Q8B912-1; Sequence=Displayed;
CC Name=Replicase polyprotein 1a; Synonyms=pp1a, ORF1a polyprotein;
CC IsoId=Q8B912-2; Sequence=VSP_032891;
CC -!- DOMAIN: The hydrophobic domains (HD) could mediate the membrane
CC association of the replication complex and thereby alter the
CC architecture of the host cell membrane. {ECO:0000250}.
CC -!- DOMAIN: The OTU-like region is responsible for the deubiquitinating and
CC deISGylation activities of Nsp2. {ECO:0000250}.
CC -!- PTM: Specific enzymatic cleavages in vivo by its own proteases yield
CC mature proteins. Nsp1 is autocleaved into two subunits, Nsp1-alpha and
CC Nsp1-beta. There are two alternative pathways for processing. Either
CC nsp4-5 is cleaved, which represents the major pathway or the nsp5-6 and
CC nsp6-7 are processed, which represents the minor pathway. The major
CC pathway occurs when nsp2 acts as cofactor for nsp4 (By similarity).
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform Replicase polyprotein 1ab]: Produced by -1
CC ribosomal frameshifting at the 1a-1b genes boundary.
CC -!- MISCELLANEOUS: [Isoform Replicase polyprotein 1a]: Produced by
CC conventional translation. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the arteriviridae polyprotein family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN73221.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY150312; AAN73220.1; -; mRNA.
DR EMBL; AY150312; AAN73221.1; ALT_INIT; mRNA.
DR SMR; Q8B912; -.
DR MEROPS; S32.002; -.
DR PRIDE; Q8B912; -.
DR ABCD; Q8B912; 8 sequenced antibodies.
DR Proteomes; UP000124990; Genome.
DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0044220; C:host cell perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0039648; P:modulation by virus of host protein ubiquitination; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0039579; P:suppression by virus of host ISG15-protein conjugation; IEA:UniProtKB-KW.
DR GO; GO:0039563; P:suppression by virus of host JAK-STAT cascade via inhibition of STAT1 activity; IEA:UniProtKB-KW.
DR GO; GO:0039644; P:suppression by virus of host NF-kappaB cascade; IEA:UniProtKB-KW.
DR GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
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; cd21410; 1B_av_Nsp10-like; 1.
DR CDD; cd21160; NendoU_av_Nsp11-like; 1.
DR CDD; cd21166; NTD_av_Nsp11-like; 1.
DR CDD; cd21405; ZBD_av_Nsp10-like; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR Gene3D; 3.30.1330.220; -; 1.
DR Gene3D; 3.30.40.20; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR Gene3D; 3.90.70.60; -; 1.
DR Gene3D; 3.90.70.70; -; 1.
DR InterPro; IPR027351; (+)RNA_virus_helicase_core_dom.
DR InterPro; IPR031932; Arteri_nsp7a.
DR InterPro; IPR038451; Arteri_nsp7a_sf.
DR InterPro; IPR008743; Arterivirus_Nsp2_C33.
DR InterPro; IPR023338; Arterivirus_NSP4_peptidase.
DR InterPro; IPR008741; AV_PCPalpha.
DR InterPro; IPR038155; AV_PCPalpha_sf.
DR InterPro; IPR025773; AV_PCPbeta.
DR InterPro; IPR038154; AV_PCPbeta_sf.
DR InterPro; IPR023183; Chymotrypsin-like_C.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR008760; EAV_peptidase_S32.
DR InterPro; IPR037227; EndoU-like.
DR InterPro; IPR043609; NendoU_nidovirus.
DR InterPro; IPR044863; NIRAN.
DR InterPro; IPR044348; NSP10_1B_Av.
DR InterPro; IPR027355; NSP10_Av_ZBD.
DR InterPro; IPR044320; NSP11_Av_N.
DR InterPro; IPR044314; NSP11_NendoU_Av.
DR InterPro; IPR032855; NSP2-B_epitope.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR032785; Pdase_C33_assoc.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001205; RNA-dir_pol_C.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR Pfam; PF16749; Arteri_nsp7a; 1.
DR Pfam; PF19215; CoV_NSP15_C; 1.
DR Pfam; PF14757; NSP2-B_epitope; 1.
DR Pfam; PF14756; Pdase_C33_assoc; 1.
DR Pfam; PF05410; Peptidase_C31; 1.
DR Pfam; PF05411; Peptidase_C32; 1.
DR Pfam; PF05412; Peptidase_C33; 1.
DR Pfam; PF05579; Peptidase_S32; 1.
DR Pfam; PF00680; RdRP_1; 1.
DR Pfam; PF01443; Viral_helicase1; 1.
DR SUPFAM; SSF142877; SSF142877; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS51538; AV_CP; 1.
DR PROSITE; PS51961; AV_NSP11N_COV_NSP15M; 1.
DR PROSITE; PS51493; AV_NSP4_PRO; 1.
DR PROSITE; PS51539; AV_PCP_ALPHA; 1.
DR PROSITE; PS51540; AV_PCP_BETA; 1.
DR PROSITE; PS51652; AV_ZBD; 1.
DR PROSITE; PS51958; NENDOU; 1.
DR PROSITE; PS51947; NIRAN; 1.
DR PROSITE; PS51657; PSRV_HELICASE; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Endonuclease; Helicase; Host cytoplasm; Host membrane;
KW Host nucleus; Host-virus interaction; Hydrolase;
KW Inhibition of host innate immune response by virus;
KW Inhibition of host interferon signaling pathway by virus;
KW Inhibition of host ISG15 by virus; Inhibition of host NF-kappa-B by virus;
KW Inhibition of host STAT1 by virus; Lyase; Membrane; Metal-binding;
KW Modulation of host ubiquitin pathway by viral deubiquitinase;
KW Modulation of host ubiquitin pathway by virus; Multifunctional enzyme;
KW Nuclease; Nucleotide-binding; Nucleotidyltransferase; Protease;
KW Reference proteome; Ribosomal frameshifting; RNA-directed RNA polymerase;
KW Serine protease; Thiol protease; Transferase; Transmembrane;
KW Transmembrane helix; Viral immunoevasion; Viral RNA replication; Zinc;
KW Zinc-finger.
FT CHAIN 1..3961
FT /note="Replicase polyprotein 1ab"
FT /id="PRO_0000036670"
FT CHAIN 1..382
FT /note="Nsp1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000410827"
FT CHAIN 1..180
FT /note="Nsp1-alpha papain-like cysteine proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000036672"
FT CHAIN 181..383
FT /note="Nsp1-beta papain-like cysteine proteinase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036673"
FT CHAIN 384..1579
FT /note="Nsp2 cysteine proteinase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036674"
FT CHAIN 1580..1809
FT /note="Non-structural protein 3"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036675"
FT CHAIN 1810..2013
FT /note="3C-like serine proteinase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036676"
FT CHAIN 2014..2458
FT /note="Non-structural protein 5-6-7"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036677"
FT CHAIN 2014..2183
FT /note="Non-structural protein 5"
FT /evidence="ECO:0000250"
FT /id="PRO_0000423122"
FT CHAIN 2184..2199
FT /note="Non-structural protein 6"
FT /evidence="ECO:0000250"
FT /id="PRO_0000423123"
FT CHAIN 2200..2348
FT /note="Non-structural protein 7-alpha"
FT /evidence="ECO:0000250"
FT /id="PRO_0000423124"
FT CHAIN 2349..2458
FT /note="Non-structural protein 7-beta"
FT /evidence="ECO:0000250"
FT /id="PRO_0000423125"
FT CHAIN 2459..3144
FT /note="RNA-directed RNA polymerase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036678"
FT CHAIN 2459..2503
FT /note="Non-structural protein 8"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036679"
FT CHAIN 3145..3585
FT /note="Helicase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036680"
FT CHAIN 3586..3808
FT /note="Uridylate-specific endoribonuclease nsp11"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036681"
FT CHAIN 3809..3961
FT /note="Non-structural protein 12"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036682"
FT TRANSMEM 1266..1286
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1296..1316
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1368..1388
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1583..1603
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1648..1668
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1685..1705
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1719..1739
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2036..2056
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2060..2080
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2092..2112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2137..2157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2162..2182
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 69..180
FT /note="Peptidase C31"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00872"
FT DOMAIN 263..383
FT /note="Peptidase C32"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00873"
FT DOMAIN 428..535
FT /note="Peptidase C33"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00871"
FT DOMAIN 1810..2013
FT /note="Peptidase S32"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00826"
FT DOMAIN 2488..2651
FT /note="NiRAN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01292"
FT DOMAIN 2890..3024
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT DOMAIN 3145..3208
FT /note="AV ZBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985"
FT DOMAIN 3265..3417
FT /note="(+)RNA virus helicase ATP-binding"
FT DOMAIN 3418..3546
FT /note="(+)RNA virus helicase C-terminal"
FT DOMAIN 3585..3681
FT /note="AV-Nsp11N/CoV-Nsp15M"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01306"
FT DOMAIN 3683..3805
FT /note="NendoU"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT ZN_FING 8..28
FT /note="C4-type; atypical"
FT REGION 69..182
FT /note="PCP1-alpha"
FT REGION 263..382
FT /note="PCP1-beta"
FT REGION 426..513
FT /note="OTU-like"
FT REGION 810..875
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 899..918
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1148..1191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1266..1388
FT /note="HD1"
FT REGION 1583..1745
FT /note="HD2"
FT REGION 2036..2157
FT /note="HD3"
FT COMPBIAS 825..840
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 76
FT /note="For Nsp1-alpha papain-like cysteine proteinase
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00872"
FT ACT_SITE 146
FT /note="For Nsp1-alpha papain-like cysteine proteinase
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00872"
FT ACT_SITE 270
FT /note="For Nsp1-beta papain-like cysteine proteinase
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00873"
FT ACT_SITE 339
FT /note="For Nsp1-beta papain-like cysteine proteinase
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00873"
FT ACT_SITE 437
FT /note="For Nsp2 cysteine proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00871"
FT ACT_SITE 506
FT /note="For Nsp2 cysteine proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00871"
FT ACT_SITE 1848
FT /note="Charge relay system; for 3C-like serine proteinase
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00826"
FT ACT_SITE 1873
FT /note="Charge relay system; for 3C-like serine proteinase
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00826"
FT ACT_SITE 1927
FT /note="Charge relay system; for 3C-like serine proteinase
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00826"
FT ACT_SITE 3714
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT ACT_SITE 3729
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT ACT_SITE 3758
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT BINDING 3151
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985"
FT BINDING 3154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985"
FT BINDING 3164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985"
FT BINDING 3169
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985"
FT BINDING 3172
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985"
FT BINDING 3174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985"
FT BINDING 3176
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985"
FT BINDING 3178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985"
FT BINDING 3185
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985"
FT BINDING 3187
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985"
FT BINDING 3194
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985"
FT BINDING 3197
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985"
FT BINDING 3293..3300
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT SITE 180..181
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250"
FT SITE 383..384
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250"
FT SITE 1579..1580
FT /note="Cleavage; by CP2"
FT /evidence="ECO:0000255"
FT SITE 1809..1810
FT /note="Cleavage; by 3CLSP"
FT /evidence="ECO:0000250"
FT SITE 2013..2014
FT /note="Cleavage; by 3CLSP"
FT /evidence="ECO:0000250"
FT SITE 2183..2184
FT /note="Cleavage; by 3CLSP"
FT /evidence="ECO:0000250"
FT SITE 2199..2200
FT /note="Cleavage; by 3CLSP"
FT /evidence="ECO:0000250"
FT SITE 2348..2349
FT /note="Cleavage; by 3CLSP"
FT /evidence="ECO:0000250"
FT SITE 2458..2459
FT /note="Cleavage; by 3CLSP"
FT /evidence="ECO:0000250"
FT SITE 3144..3145
FT /note="Cleavage; by 3CLSP"
FT /evidence="ECO:0000250"
FT SITE 3585..3586
FT /note="Cleavage; by 3CLSP"
FT /evidence="ECO:0000250"
FT SITE 3808..3809
FT /note="Cleavage; by 3CLSP"
FT /evidence="ECO:0000250"
FT VAR_SEQ 2504..3961
FT /note="Missing (in isoform Replicase polyprotein 1a)"
FT /evidence="ECO:0000305"
FT /id="VSP_032891"
SQ SEQUENCE 3961 AA; 433077 MW; 45D39828CC48EA77 CRC64;
MSGILDRCTC TPNARVFVAE GQVYCTRCLS ARSLLPLNLQ VPELGVLGLF YRPEEPLRWT
LPRAFPTVEC SPTGACWLSA IFPIARMTSG NLNFQQRMVR VAGEIYRAGQ LTPTVLKTIQ
VYERGCRWYP IVGPVPGVGV YANSLHVSDK PFPGATHVLT NLPLPQRPKP EDFCPFECAM
ADVYDIGRGA VMYVAGGKVS WAPRGGDEVK FEPVPKELKL VANRLHTSFP PHHVVDMSKF
TFMTPGSGVS MRVEYQYGCL PADTVPEGNC WWRLFDLLPP EVQNKEIRHA NQFGYQTKHG
VPGKYLQRRL QVNGLRAVTD THGPIVIQYF SVKESWIRHL KPVEEPSLPG FEDLLRIRVE
PNTSPLAGKN EKIFRFGSHK WYGAGKRARK ARSGATTMVA HRASSAHETR QATKHEGAGA
NKAEHLKLYS PPAEGNCGWH CISAIVNRMV NSNFETTLPE RVRPPDDWAT DEDLVNTIQI
LRLPAALDRN GACGGAKYVL KLEGEHWTVS VNPGMSPSLL PLECVQGCCE HKGGLGSPDA
VEVSGFDPAC LDRLLQVMHL PSSTIPAALA ELSDDSNRPV SPAAATWTVS QSYARHRGGN
HHDQVCLGKI ISLCQVIEDC CCHQNKTNRA TPEEVAAKID QYLRGATSLE ECLAKLERVS
PPGAADTSFD WNVVLPGVEA AHQTTEQLHV NPCRTLVPPV TQEPLGKDSV PLTAFSLSNC
YYPAQGNEVR HRERLNSVLS KLEEVVLEEY GLMSTGLGPR PVLPSGLDEL KDQMEEDLLK
LANTQATSEM MAWAAEQVDL KAWVKSYPRW TPPPPPPRVQ PRKTKSVKSL PEDKPVPAPR
RKVRSGCGSP VLMGDNVPNG SEDLTVGGPL NFPTPSEPMT PMSEPVLTPA LQRVPKLMTP
LDGSAPVPAP RRTVSRPMTP LSEPIFLSAP RHKFQQVEEA NPATTTLTHQ NEPLDLSASS
QTEYEASPLA SSQNMSILEA GGQEAEEVLS EISDILNDTS PAPVSSSSSL SSVKITRPKY
SAQAIIDSGG PCSGHLQKEK EACLSIMREA CDASKLSDPA TQEWLSRMWD RVDMLTWRNT
SAYQAFRTLN GRFEFLPKMI LETPPPHPCG FVMLPHTPAP SVSAESDLTI GSVATEDVPR
ILGKIGDTGE LLNQGPSAPF KGGPVCDQPA KNSRMSPRES DESIIAPPAD TGGAGSFTDL
PSSDSVDANG GGPLRTVKTK AGRLLDQLSC QVFSLVSHLP VFFSHLFKSD SGYSPGDWGF
AAFTLFCLFL CYSYPFFGFA PLLGVFSGSS RRVRMGVFGC WLAFAVGLFK PVSDPVGTAC
EFDSPECRNV LHSFELLKPW DPVRSLVVGP VGLGLAILGR LLGGARYVWH FLLRFGIVAD
CILAGAYVLS QGRCKKCWGS CVRTAPNEIA FNVFPFTRAT RSSLIDLCDR FCAPKGMDPI
FLATVWRGCW TGRSPIEQPS EKPIAFAQLD EKRITARTVV AQPYDPNQAV KCLRVLQAGG
AMVAEAVPKV VKVSAIPFRA PFFPAGVKVD PECRIVVDPD TFTTALRSGY STTNLVLGMG
DFAQLNGLKI RQISKPSGGG SHLVAALHVA CSMALHMLAG VYVTAVGSCG TGTNDPWCTN
PFAAPGYGPG SLCTSRLCIS QHGLTLPLTA LVAGFGLQEI ALVVLIFVSM GGMAHRLSCK
ADMLCILLAI ASYVWVPLTW LLCVFPCWLR WFSLHPLTIL WLVFFLISVN IPSGILAVVL
LVSLWLLGRY TNIAGLVTPY DIHHYTSGPR GVAALATAPD GTYLAAVRRA ALTGRTMLFT
PSQLGSLLEG AFRTQKPSLN TVNVVGSSMG SGGVFTIDGK IKCVTAAHVL TGNSARVSGV
GFNQMLDFDV KGDFAIADCP NWQGAAPKAQ FCEDGWTGRA YWLTSSGVEP GVIGNGFAFC
FTACGDSGSP VITEAGELVG VHTGSNKQGG GIVTRPSGQF CNVTPIKLSE LSEFFAGPKV
PLGDVKIGSH IIKDTCEVPS DLCALLAAKP ELEGGLSTVQ LLCVFFLLWR MMGHAWTPLV
AVGFFILNEI LPAVLVRSVF SFGMFVLSWL TPWSAQVLMI RLLTAALNRN RLSLGFYSLG
AVTSFVADLA VTQGHPLQVV MNLSTYAFLP RMMVVTSPVP VIACGVVHLL AIILYLFKYR
CLHYVLVGDG VFSSAFFLRY FAEGKLREGV SQSCGMSHES LTGALAMRLT DEDLDFLTKW
TDFKCFVSAS NMRNAAGQFI EAAYAKALRI ELAQLVQVDK VRGTLAKLEA FADTVAPQLS
PGDIVVALGH TPVGSIFDLK VGSTKHTLQA IETRVLAGSK MTVARVVDPT PAPPPVPVPI
PLPPKVLENG PNAWGDEDRL NKKKRRRMEA VGIFVMDGKK YQKFWDKNSG DVFYEEVHNS
TDEWECLRAG DPADFDPETG VQCGHITIED RVYNVFTSPS GRKFLVPANP ENRRAQWEAA
KLSVEQALGM MNVDGELTAK ELEKLKGIID KLQGLTKEQC LNCLLAASGL TRCGRGGLVV
TETAVKIVKF HNRTFTLGPV NLKVASEVEL KDAVEHNQHP VARPVDGGVV LLRSAVPSLI
DVLISGADAS PKLLARHGPG NTGIDGTLWD FEAEATKEEV ALSAQIIQAC DIRRGDAPEI
GLPYKLYPVR GNPERVKGVL QNTRFGDIPY KTPSDTGSPV HAAACLTPNA TPVTDGRSVL
ATTMPSGFEL YVPTIPASVL DYLDSRPDCP KQLTEHGCED AALRDLSKYD LVTQGFVLPG
VLRLVRKYLF AHVGKCPPVH RPSTYPAKNS MAGINGNRFP TKDIQSVPEI DVLCAQAVRE
NWQTVTPCTL KKQYCGKKKT RTILGTNNFI ALAHRAALSG VTQGFMKKAF NSPIALGKNK
FKELQTPVLG RCLEADLASC DRSTPAIVRW FAANLLYELA CAEEHLPSYV LNCCHDLLVT
QSGAVTKRGG LSSGDPITSV SNTIYSLVIY AQHMVLSYFK SGHPHGLLFL QDQLKFEDML
KVQPLIVYSD DLVLYAESPS MPNYHWWVEH LNLMLGFQTD PKKTAITDSP TFLGCRIING
RQLVPNRDRI LAALAYHMKA SNVSEYYASA AAILMDSCAC LEYDPEWFEE LVVGIAQCAR
KDGYSFPGPP FFLSMWEKLR SNHEGKKSRM CGYCMAPAPY ATACGLDVCV YHTHFHQHCP
VIIWCGHPAG SGSCGECEPP LGKGTSPLDE VLEQVPYKPP RTVIMHVEQG LTPLDPGRYQ
TRRGLVSVRR GIRGNEVDLP DGDYASTALL PTCKEINMVA VAPNVLRSRF IIGPPGAGKT
HWLLQQVQDG DVIYTPTHQT MLDMIRALGT CRFNVPAGTT LQFPAPSRTG PWVRILAGGW
CPGKNSFLDE AAYCNHLDVL RLLSKTTLTC LGDFKQLHPV GFDSHCYVFD IMPQTQLKTI
WRFGQNICDA IQPDYRDKLV SMVNTTRVTY VEKPVRYGQV LTPYHRDRED GAITIDSSQG
ATFDVVTLHL PTKDSLNRQR ALVAITRARH AIFVYDPHRQ LQSMFDLPAK GTPVNLAVHR
DEQLIVLDRN NKEITVAQAL GNGDKFRATD KRVVDSLRAI CADLEGSSSP LPKVAHNLGF
YFSPDLTQFA KLPAELAPHW PVVTTQNNER WPDRLVASLR PIHKYSRACI GAGYMVGPSV
FLGTPGVVSY YLTKFVRGEA QVLPETVFST GRIEVDCREY LDDREREVAE SLPHAFIGDV
KGTTVGGCHH VTSKYLPRFL PKESVAVVGV SSPGEAAKAF CTLTDVYLPD LEAYLHPETQ
SKCWKVMLDF KEVRLMVWKG KTAYFQLEGR HFTWYQLASY TSYIRVPVNS TVYLDPCMGP
ALCNRRVVGS THWGADLAVT PYDYGAKIIL SSAYHGEMPP GYKILACAEF SLDDPVRYKH
TWGFESDTAY LYEFTGNGED WEDYNGAFRA RQKGKIYKAT ATSMKFHFPP GPVIEPTLGL
N
