ID RPOA_LDVP Reviewed; 3616 AA.
AC Q83017; Q83018; Q83024; Q83025; Q86716;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 2.
DT 27-MAR-2024, entry version 135.
DE RecName: Full=Replicase polyprotein 1ab;
DE AltName: Full=ORF1ab polyprotein;
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=3.4.22.-;
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 Lactate dehydrogenase elevating virus (strain Plagemann) (LDV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Arnidovirineae; Arteriviridae; Variarterivirinae;
OC Gammaarterivirus; Gammaarterivirus lacdeh.
OX NCBI_TaxID=300016;
OH NCBI_TaxID=10092; Mus musculus domesticus (western European house mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=7778295; DOI=10.1006/viro.1995.1296;
RA Palmer G.A., Kuo L.L., Chen Z., Faaberg K.S., Plagemann P.G.W.;
RT "Sequence of the genome of lactate dehydrogenase-elevating virus:
RT heterogenicity between strains P and C.";
RL Virology 209:637-642(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-57.
RX PubMed=7512122; DOI=10.1099/0022-1317-75-4-925;
RA Chen Z., Faaberg K.S., Plagemann P.G.W.;
RT "Determination of the 5' end of the lactate dehydrogenase-elevating virus
RT genome by two independent approaches.";
RL J. Gen. Virol. 75:925-930(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 769-1187 AND 2307-2846.
RX PubMed=1870216; DOI=10.1128/jvi.65.9.5118-5123.1991;
RA Kuo L.L., Harty J.T., Erickson L., Palmer G.A., Plagemann P.G.W.;
RT "A nested set of eight RNAs is formed in macrophages infected with lactate
RT dehydrogenase-elevating virus.";
RL J. Virol. 65:5118-5123(1991).
RN [4]
RP ACTIVE SITES OF PCP1-ALPHA AND PCP1-BETA, AND MUTAGENESIS OF CYS-76 AND
RP CYS-269.
RX PubMed=7769711; DOI=10.1128/jvi.69.7.4500-4505.1995;
RA den Boon J.A., Faaberg K.S., Meulenberg J.J.M., Wassenaar A.L.M.,
RA Plagemann P.G.W., Gorbalenya A.E., Snijder E.J.;
RT "Processing and evolution of the N-terminal region of the arterivirus
RT replicase ORF1a protein: identification of two papainlike cysteine
RT proteases.";
RL J. Virol. 69:4500-4505(1995).
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: The Nsp1 chain is essential for viral subgenomic mRNA
CC synthesis. {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: [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: [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=Q83017-1; Sequence=Displayed;
CC Name=Replicase polyprotein 1a; Synonyms=pp1a, ORF1a polyprotein;
CC IsoId=Q83017-2; Sequence=VSP_032889;
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 -!- PTM: Specific enzymatic cleavages in vivo by its own proteases yield
CC mature proteins. There are two alternative pathways for processing.
CC Either nsp4-5 is cleaved, which represents the major pathway or the
CC nsp5-6 and nsp6-7 are processed, which represents the minor pathway.
CC The major pathway occurs when nsp2 acts as a cofactor for nsp4 (By
CC similarity). {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=AAA85664.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U15146; AAA85663.1; -; Genomic_RNA.
DR EMBL; U15146; AAA85664.1; ALT_INIT; Genomic_RNA.
DR EMBL; S69379; AAB30448.1; -; Genomic_RNA.
DR EMBL; S50064; AAB19478.1; -; mRNA.
DR EMBL; S50068; AAB19479.1; -; mRNA.
DR PIR; B40901; B40901.
DR PIR; C40901; C40901.
DR PIR; JQ1998; JQ1998.
DR PIR; PQ0618; PQ0618.
DR SMR; Q83017; -.
DR MEROPS; C31.001; -.
DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044220; C:host cell perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C: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:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
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:0004540; F:RNA nuclease activity; IEA:UniProt.
DR GO; GO:0003968; F:RNA-dependent RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0070008; F:serine-type exopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; cd23189; Arteriviridae_RdRp; 1.
DR CDD; cd22528; av_Nsp3_ER-remodelling; 1.
DR CDD; cd17937; DEXXYc_viral_SF1-N; 1.
DR CDD; cd21160; NendoU_av_Nsp11-like; 1.
DR CDD; cd21166; NTD_av_Nsp11-like; 1.
DR CDD; cd18786; SF1_C; 1.
DR CDD; cd21405; ZBD_av_Nsp10-like; 1.
DR Gene3D; 3.90.70.160; -; 1.
DR Gene3D; 4.10.80.390; -; 1.
DR Gene3D; 3.30.1330.220; Arterivirus nonstructural protein 7 alpha; 1.
DR Gene3D; 3.90.70.70; Arterivirus papain-like cysteine protease beta domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.90.70.60; Porcine arterivirus-type cysteine proteinase alpha domain; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
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; IPR046440; AV_NSP11N_COV_NSP15M.
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; IPR022230; DUF3756.
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; IPR027417; P-loop_NTPase.
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; PF12581; DUF3756; 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; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF142877; EndoU-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 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 1: Evidence at protein level;
KW ATP-binding; Helicase; Host cytoplasm; Host membrane; Hydrolase; Lyase;
KW Membrane; Metal-binding; Nucleotide-binding; Nucleotidyltransferase;
KW Protease; Ribosomal frameshifting; RNA-directed RNA polymerase;
KW Serine protease; Thiol protease; Transferase; Transmembrane;
KW Transmembrane helix; Viral RNA replication; Zinc; Zinc-finger.
FT CHAIN 1..3616
FT /note="Replicase polyprotein 1ab"
FT /id="PRO_0000036644"
FT CHAIN 1..?
FT /note="Nsp1-alpha papain-like cysteine proteinase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036646"
FT CHAIN ?..380
FT /note="Nsp1-beta papain-like cysteine proteinase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036647"
FT CHAIN 381..1286
FT /note="Nsp2 cysteine proteinase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036648"
FT CHAIN 1287..1512
FT /note="Non-structural protein 3"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036649"
FT CHAIN 1513..1714
FT /note="3C-like serine proteinase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036650"
FT CHAIN 1715..2161
FT /note="Non-structural protein 5-6-7"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036651"
FT CHAIN 1715..1878
FT /note="Non-structural protein 5"
FT /evidence="ECO:0000250"
FT /id="PRO_0000423114"
FT CHAIN 1879..1894
FT /note="Non-structural protein 6"
FT /evidence="ECO:0000250"
FT /id="PRO_0000423115"
FT CHAIN 1895..2026
FT /note="Non-structural protein 7-alpha"
FT /evidence="ECO:0000250"
FT /id="PRO_0000423116"
FT CHAIN 2027..2161
FT /note="Non-structural protein 7-beta"
FT /evidence="ECO:0000250"
FT /id="PRO_0000423117"
FT CHAIN 2162..2843
FT /note="RNA-directed RNA polymerase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036652"
FT CHAIN 2162..2206
FT /note="Non-structural protein 8"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036653"
FT CHAIN 2844..3272
FT /note="Helicase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036654"
FT CHAIN 3273..3494
FT /note="Uridylate-specific endoribonuclease nsp11"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036655"
FT CHAIN 3495..3616
FT /note="Non-structural protein 12"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036656"
FT TRANSMEM 942..962
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 977..997
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1010..1030
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1060..1080
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1085..1105
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1289..1309
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1364..1384
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1386..1406
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1425..1445
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1715..1735
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1737..1757
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1761..1781
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1832..1852
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 69..181
FT /note="Peptidase C31"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00872"
FT DOMAIN 262..381
FT /note="Peptidase C32"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00873"
FT DOMAIN 381..486
FT /note="Peptidase C33"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00871"
FT DOMAIN 1513..1714
FT /note="Peptidase S32"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00826"
FT DOMAIN 2194..2352
FT /note="NiRAN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01292"
FT DOMAIN 2590..2724
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT DOMAIN 2844..2907
FT /note="AV ZBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985"
FT DOMAIN 2964..3116
FT /note="(+)RNA virus helicase ATP-binding"
FT DOMAIN 3117..3248
FT /note="(+)RNA virus helicase C-terminal"
FT DOMAIN 3272..3368
FT /note="AV-Nsp11N/CoV-Nsp15M"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01306"
FT DOMAIN 3370..3492
FT /note="NendoU"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT ZN_FING 8..28
FT /note="C4-type; atypical"
FT REGION 672..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 883..912
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 981..1105
FT /note="HD1"
FT REGION 1289..1448
FT /note="HD2"
FT REGION 1737..1852
FT /note="HD3"
FT ACT_SITE 76
FT /note="For Nsp1-alpha papain-like cysteine proteinase
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00872,
FT ECO:0000269|PubMed:7769711"
FT ACT_SITE 147
FT /note="For Nsp1-alpha papain-like cysteine proteinase
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00872,
FT ECO:0000269|PubMed:7769711"
FT ACT_SITE 269
FT /note="For Nsp1-beta papain-like cysteine proteinase
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00873,
FT ECO:0000269|PubMed:7769711"
FT ACT_SITE 340
FT /note="For Nsp1-beta papain-like cysteine proteinase
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00873,
FT ECO:0000269|PubMed:7769711"
FT ACT_SITE 390
FT /note="For Nsp2 cysteine proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00871"
FT ACT_SITE 456
FT /note="For Nsp2 cysteine proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00871"
FT ACT_SITE 1551
FT /note="Charge relay system; for 3C-like serine proteinase
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00826"
FT ACT_SITE 1576
FT /note="Charge relay system; for 3C-like serine proteinase
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00826"
FT ACT_SITE 1628
FT /note="Charge relay system; for 3C-like serine proteinase
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00826"
FT BINDING 2850
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985"
FT BINDING 2853
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985"
FT BINDING 2863
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985"
FT BINDING 2868
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985"
FT BINDING 2871
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985"
FT BINDING 2873
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985"
FT BINDING 2875
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985"
FT BINDING 2877
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985"
FT BINDING 2884
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985"
FT BINDING 2886
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985"
FT BINDING 2893
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985"
FT BINDING 2896
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985"
FT BINDING 2992..2999
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT SITE 181..182
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000255"
FT SITE 381..382
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000255"
FT SITE 1286..1287
FT /note="Cleavage; by CP2"
FT /evidence="ECO:0000250"
FT SITE 1512..1513
FT /note="Cleavage; by 3CLSP"
FT /evidence="ECO:0000250"
FT SITE 1714..1715
FT /note="Cleavage; by 3CLSP"
FT /evidence="ECO:0000250"
FT SITE 1878..1879
FT /note="Cleavage; by 3CLSP"
FT /evidence="ECO:0000250"
FT SITE 1894..1895
FT /note="Cleavage; by 3CLSP"
FT /evidence="ECO:0000250"
FT SITE 2026..2027
FT /note="Cleavage; by 3CLSP"
FT /evidence="ECO:0000250"
FT SITE 2161..2162
FT /note="Cleavage; by 3CLSP"
FT /evidence="ECO:0000250"
FT SITE 2843..2844
FT /note="Cleavage; by 3CLSP"
FT /evidence="ECO:0000250"
FT SITE 3272..3273
FT /note="Cleavage; by 3CLSP"
FT /evidence="ECO:0000250"
FT SITE 3494..3495
FT /note="Cleavage; by 3CLSP"
FT /evidence="ECO:0000250"
FT VAR_SEQ 2207..3616
FT /note="Missing (in isoform Replicase polyprotein 1a)"
FT /evidence="ECO:0000305"
FT /id="VSP_032889"
FT MUTAGEN 76
FT /note="C->S: Complete loss of cleavage between nsp1-alpha
FT and nsp1-beta."
FT /evidence="ECO:0000269|PubMed:7769711"
FT MUTAGEN 269
FT /note="C->A: Complete loss of cleavage between nsp1-beta
FT and nsp2."
FT /evidence="ECO:0000269|PubMed:7769711"
FT CONFLICT 1185
FT /note="E -> K (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 2748..2753
FT /note="SEPKLP -> QNPNFL (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 2771..2777
FT /note="VAALAYQ -> RRGASVS (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 2820..2823
FT /note="GSPW -> RKEG (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 2843
FT /note="E -> K (in Ref. 3)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3616 AA; 396434 MW; 6167A231CDE7B611 CRC64;
MQSGFDRCLC TPNARVFWEH GQVYCTRCLA ARPLLPLSQQ NPRLGALGLF YRPATPLTWE
APITYPTKEC RPGGLCWLSG IYPIARMTSG NHNFQARLNF VASVVYRDGK LTSKHLEEEF
EVYSRGCRWY PITGPVPGIA LYANAVHVSD EPFPGCTHVL SNLPLPQQPL RKGLCPFSDA
RAEVWRYKGN TIFVSEQGYL WTTGSNDSVP EPWGEARRLC EKIIASLPAD HLVKIEFSNY
PFDYSFTGGD GAGYVLFPCK KNDTKFSKCW EKVFEDHSSW KVACEEADLA DRMGYRTPAG
VAGPYLARRL QYRGLRAVVK PEQNDYVVWA LGVPESYIRH ISRAGEPVEN FFVRVGEFSI
VSNCVATPYP KFRFQTRKYY GYSPPGDGAC GLHCISAIIN DIFGDALCTK LTNCSRDSSE
WLSDQDMYQL VMTARLPATL GHCPSATYKL DCVNQHWTVT KRKGDRALGG LSPECVRGVC
GGECKFVPTY PREINLELAA KSPISALAFS LGVEPYCDCW NFTNSVLVND SLAVETARAG
EAYRSAMGIP KDDWVLLAEL MTENCLTRRE VLDKLQRGLR LHATSKPGSP ASVSPASSID
FSAAGLLLDG TESDKEAVVA VNNDCYTVLG FDKNSATKSE QELATGLFSE LVEPMETSTS
KHESRKILEA ASRALKSAKP KRKRNKKKKT SSPTPTPPET PTREVPGAIE VVSGDEEAGA
CESATIVPDK AQARPPPRPK RQALKKAEQG FILKDIIWNP TESGVKCLTI VEDVRAFLKS
ITPPGGALGT RARITAHIVE QFHVIRESTP ELVLAHAEHQ AKNMHELLLS EKAKLILGIG
EDTLKKLVSS QRSLPRSIGF GAWLSDQQKT ADSCGEREFV EVPLKSGAEP TPSKRDLGVS
LGDQLSQDGA PRLSSSTACE IKERVPPIKD SGGGLGQKFM AWLNHQVFLL SSHLLAMWSV
VLGSRQKLNW ADYVYTLFCL CCVLLCFHFP AIGFIPLAGC VFGSPWRVRL SVFSVWLCVA
VVVFQEVLPE PGSVCSSASA ECAAALERYS GNGVHRPVNH IGVGLVGTVA GFVARVVGGP
RHYWFYFLRL MVVLDLGLVF LAVALRGRCK KCFCKCVRVA PHEVHLRVFP LTKVARPTLE
AVCDMYSAPR VDPILVATGI KGCWQGKVSP HQVTDKPVSY SNLEEKKISN KTVVPPPTDP
QQAVKCLKVL QCGGSIQDVG VPEVKKVSKV PYKAPFFPNV SIDPECYIVV DPVTYSAAMR
GGYGVSHLIV GTGDFAEVNG LRFVSGGHVA DFVCLGLYVM LNFLISAWLS SPVSCGRGTN
DPWCKNPFSY PVVGQGVMCN SHLCISEDGL TSPMVLSYSL IDWALMIAVI ATVAIFIAKV
SLLVDVICVF LCLLMYVFPP LSVIAFAFPF ALCKVHLHPV TLVWVQFFLL AVNFWAGVAV
AVILISSWFL ARATSSTGLV TPYDVHLVTS TPRGASSLAS APEGTYLAAV RRSALTGRCC
MFVPTNFGSV LEGSLRTRGC AKNVVSVFGS ASGSGGVFTI HGNPVVVTAT HLLSDGKARV
SCVGFSQCLT FKSVGDYAFA RVAEWKGDAP KVELSDRRGR AYCSPQVEWS LVLLGPNTAF
CFTKCGDSGS PVVDEDGNLI GVHTGSNKRG SGMITTHNGK TLGMSNVKLS EMCQHYGGSG
VPVSTVRLPK HLIVDVEAVA SDLVAVVESL PTPEGALSSV QLLCVFFFLW RLIHVPFVPV
IAVAFFFLNE ILPVVLARLM FSFALSLFSV FTGFSVQVLL LRLVIAALNR SAVSFGSFLL
GQLFHCCLMP SHLETLGPVP GYFYPSTTEV ASKEIFVTLL AIHVLALLLS LFKRPMLADV
LVGNGSFDAA FFLKYFAEGN LRDGVSDSCN MTPEGLTAAL AITLSDDDLE FLQRHSEFKC
FVSASNMRNG AKEFIESAYA RALRAQLAAT DKIKASKSIL AKLESFAGGV VTKVEPGDVV
VVLGKKIVGD LVEITINDVK HVIRVIETRV MAGTQFSVGT ICGDLENACE DPSGLVKTSK
KQRRRQKRTG LGTEVVGTVE IDGVSYNKVW HKATGDVTYE GFLVSENSRL RTLGTSAIGR
FQEFIRKHGS KVKTSVEKYP VGKNKHIEFA VTTYNLDGEE FDVPDHEPLE WTITIGDSDL
EAERLTVDQA LRHMGHDSLL TPKEKEKLAR IIESLNGLQQ SSALNCLTTS GLERCSRGGV
TVSKDAVKIV KYHSRTFSIG DVNLKVMSFD EYRRTMGKPG HLLVAKLTDG VVVMRKHEPS
LVDVILTGED AEFFPRTHGP GNTGIHRFVW DFESPPVDLE LELSEQIITA CSMRRGDAPA
LDLPYKLHPV RGDPYRHRGV LFNTRFGDIT YLIPEKTKEP LHAAACYNKG VPVSDSETLV
ATTLPHGFEL YVPTLPPSVL EYLDSRPDTP RMLTKHGCAS AAEKDLQKFD LSRQGFVLPG
VLYMVRRYLS RLIGVRRRLF MPSTYPAKNS MAGINGGRFP LTWLQSHPDI DALCKRACEE
HWQTVTPCTL KKQYCSKSKT RTILGTNNFV ALGLRSALSG VTQGFMRKGI GTPICLGKNK
FTPLPVRIGG RCLEADLASC DRSTPAIIRW FTTNLLFELA GAEEWIPSYV LNCCHDVVST
MSGCFDKRGG LSSGDPVTSI SNTVYSLIIY AQHMVLSAFR CGHKIGGLFL QDSLEMEQLF
ELQPLLVYSD DVVFYNESDE LPNYHFFVDH LDLMLGFKTD RSKTVITSEP KLPGCRISGG
RVLVPQRDRI VAALAYQMKA SCVGEYFASA AAILMDACAC CDHDESWYFD LVCGIAECAG
SPWFRFPGPS FFLDMWNRLS AEEKKKCRTC AHCGAPATLV SSCGLNLCDY HGHGHPHCPV
VLPCGHAVGS GVCEQCSSSA MNLNTELDIL LMCVPYHPPK VELLSVNDKV SSLPPGAYQA
RGGVVSVRRD ILGNVVDLPD GDYQVMKVAQ TCADISMVSV NSNILRSQFV TGAPGTGKTT
YLLSVVRDDD VIYTPTHRTM LDVVKALKVC RFDPPKDTPL EFPVPGRTGP TVRLIGAGFV
PGRVSYLDEA AYCNPLDVLK VLSKTPLVCV GDLNQLPPVG FNGPCFAFSL MPGRQLIEVF
RFGPAVVNSI KKFYKEELVP RGPDTGVKFL KQYQPYGQVL TPYHRDRVDG AITIDSSQGC
TYDVVTVYLP TPKSLNSARA LVALTRARHY VFIYDPYDQL QQYLQVFEHE PADAWAFWCG
DQPKMIVGGV VKQLAGHSRT TDLKLQQLMG LEGTASPLPQ VGHNLGFYYS PDLIQFAKIP
PELCKHWPVV TAQNRTEWPD RLVCGMNKMD KNSRAVFCAG YYVGPSIFLG VPGVVSYYLT
KYLKGESVPL PDSIMSTGRI RLNVREYLDE NEIEFAKKCP QPFIGEVKGS NVGGCHHVTS
RFLPPVLVPG SVVKVGVSCP GKAAKGLCTV TDVYLPELDS YLHPPSKSMD YKLLVDFQPV
KLMVWKDATA YFHEGIRPME AMSRFLKVPE GEGVFFDLDE FVTNAKVSKL PCKYSVSAHQ
FLTEVVLSMT PTSEAPPDYE LLFARAYCVP GLDVGTLNAY IYKRGPSTYT TSNFARLVKD
TAVPVGCKGS GYMFPK
//
