RPOA_EAVBU
ID RPOA_EAVBU Reviewed; 3175 AA.
AC P19811; Q88625; Q8QZQ5; Q91DM2;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 3.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Replicase polyprotein 1ab;
DE AltName: Full=ORF1ab polyprotein;
DE Contains:
DE RecName: Full=Nsp1 papain-like cysteine proteinase;
DE Short=PCP;
DE EC=3.4.22.- {ECO:0000269|PubMed:1331507, ECO:0000269|PubMed:8617757};
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 {ECO:0000303|PubMed:11000230, ECO:0000303|PubMed:24369429};
DE Short=Hel;
DE EC=3.6.4.12 {ECO:0000269|PubMed:24369429};
DE EC=3.6.4.13 {ECO:0000269|PubMed:24369429};
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 Equine arteritis virus (strain Bucyrus) (EAV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Arnidovirineae; Arteriviridae; Equarterivirinae;
OC Alphaarterivirus; Alphaarterivirus equid.
OX NCBI_TaxID=299386;
OH NCBI_TaxID=9788; Equidae (horses).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=1851863; DOI=10.1128/jvi.65.6.2910-2920.1991;
RA den Boon J.A., Snijder E.J., Chirnside E.D., de Vries A.A.F.,
RA Horzinek M.C., Spaan W.J.M.;
RT "Equine arteritis virus is not a togavirus but belongs to the
RT coronaviruslike superfamily.";
RL J. Virol. 65:2910-2920(1991).
RN [2]
RP SEQUENCE REVISION.
RA Snijder E.J.;
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-17.
RX PubMed=2162519; DOI=10.1093/nar/18.11.3241;
RA de Vries A.A.F., Chirnside E.D., Bredenbeek P.J., Gravestein L.A.,
RA Horzinek M.C., Spaan W.J.M.;
RT "All subgenomic mRNAs of equine arteritis virus contain a common leader
RT sequence.";
RL Nucleic Acids Res. 18:3241-3247(1990).
RN [4]
RP PROTEOLYTIC PROCESSING OF POLYPROTEIN 1A, CHARACTERIZATION OF PCP,
RP MUTAGENESIS OF CYS-164; HIS-219; HIS-230 AND GLY-260, CATALYTIC ACTIVITY,
RP AND ACTIVE SITE.
RX PubMed=1331507; DOI=10.1128/jvi.66.12.7040-7048.1992;
RA Snijder E.J., Wassenaar A.L.M., Spaan W.J.M.;
RT "The 5' end of the equine arteritis virus replicase gene encodes a
RT papainlike cysteine protease.";
RL J. Virol. 66:7040-7048(1992).
RN [5]
RP CHARACTERIZATION OF NSP2, ACTIVE SITE, AND MUTAGENESIS OF CYS-270; GLY-271;
RP ASP-291; ASP-295; ASP-296; GLU-297; CYS-319; HIS-332; CYS-344; CYS-349;
RP CYS-354 AND CYS-356.
RX PubMed=7622476; DOI=10.1074/jbc.270.28.16671;
RA Snijder E.J., Wassenaar A.L.M., Spaan W.J.M., Gorbalenya A.E.;
RT "The arterivirus Nsp2 protease. An unusual cysteine protease with primary
RT structure similarities to both papain-like and chymotrypsin-like
RT proteases.";
RL J. Biol. Chem. 270:16671-16676(1995).
RN [6]
RP PROTEOLYTIC PROCESSING OF POLYPROTEIN 1A, CHARACTERIZATION OF 3CLSP,
RP CATALYTIC ACTIVITY, ACTIVE SITE, AND MUTAGENESIS OF CYS-164; GLY-831;
RP GLU-1064; HIS-1103; ASP-1117; ASP-1129; THR-1179; SER-1184; HIS-1198;
RP GLU-1268; GLU-1430 AND GLU-1677.
RX PubMed=8617757; DOI=10.1074/jbc.271.9.4864;
RA Snijder E.J., Wassenaar A.L.M., van Dinten L.C., Spaan W.J.M.,
RA Gorbalenya A.E.;
RT "The arterivirus nsp4 protease is the prototype of a novel group of
RT chymotrypsin-like enzymes, the 3C-like serine proteases.";
RL J. Biol. Chem. 271:4864-4871(1996).
RN [7]
RP MUTAGENESIS OF SER-2429.
RX PubMed=9023370; DOI=10.1073/pnas.94.3.991;
RA van Dinten L.C., den Boon J.A., Wassenaar A.L.M., Spaan W.J.M.,
RA Snijder E.J.;
RT "An infectious arterivirus cDNA clone: identification of a replicase point
RT mutation that abolishes discontinuous mRNA transcription.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:991-996(1997).
RN [8]
RP PROTEOLYTIC PROCESSING OF POLYPROTEIN 1A, AND MUTAGENESIS OF GLU-1268.
RX PubMed=9371590; DOI=10.1128/jvi.71.12.9313-9322.1997;
RA Wassenaar A.L.M., Spaan W.J.M., Gorbalenya A.E., Snijder E.J.;
RT "Alternative proteolytic processing of the arterivirus replicase ORF1a
RT polyprotein: evidence that NSP2 acts as a cofactor for the NSP4 serine
RT protease.";
RL J. Virol. 71:9313-9322(1997).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=9658116; DOI=10.1128/jvi.72.8.6689-6698.1998;
RA van der Meer Y., van Tol H., Locker J.K., Snijder E.J.;
RT "ORF1a-encoded replicase subunits are involved in the membrane association
RT of the arterivirus replication complex.";
RL J. Virol. 72:6689-6698(1998).
RN [10]
RP PROTEOLYTIC PROCESSING OF POLYPROTEIN 1B, AND MUTAGENESIS OF ASP-2351;
RP GLU-2370; GLU-2800; ASP-2819; GLU-2835; GLN-2837 AND GLU-3056.
RX PubMed=9971783; DOI=10.1128/jvi.73.3.2027-2037.1999;
RA van Dinten L.C., Rensen S., Gorbalenya A.E., Snijder E.J.;
RT "Proteolytic processing of the open reading frame 1b-encoded part of
RT arterivirus replicase is mediated by nsp4 serine protease and is essential
RT for virus replication.";
RL J. Virol. 73:2027-2037(1999).
RN [11]
RP CHARACTERIZATION OF HELICASE.
RX PubMed=11000230; DOI=10.1128/jvi.74.20.9586-9593.2000;
RA Seybert A., van Dinten L.C., Snijder E.J., Ziebuhr J.;
RT "Biochemical characterization of the equine arteritis virus helicase
RT suggests a close functional relationship between arterivirus and
RT coronavirus helicases.";
RL J. Virol. 74:9586-9593(2000).
RN [12]
RP C4-TYPE ZINC-FINGER OF NSP1, AND MUTAGENESIS OF CYS-25 AND CYS-44.
RX PubMed=11172046; DOI=10.1073/pnas.98.4.1889;
RA Tijms M.A., van Dinten L.C., Gorbalenya A.E., Snijder E.J.;
RT "A zinc finger-containing papain-like protease couples subgenomic mRNA
RT synthesis to genome translation in a positive-stranded RNA virus.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:1889-1894(2001).
RN [13]
RP SUBCELLULAR LOCATION OF NSP1 PAPAIN-LIKE CYSTEINE PROTEINASE.
RX PubMed=11907328; DOI=10.1099/0022-1317-83-4-795;
RA Tijms M.A., van der Meer Y., Snijder E.J.;
RT "Nuclear localization of non-structural protein 1 and nucleocapsid protein
RT of equine arteritis virus.";
RL J. Gen. Virol. 83:795-800(2002).
RN [14]
RP INTERACTION WITH HUMAN SND1/P100.
RX PubMed=12917451; DOI=10.1099/vir.0.19297-0;
RA Tijms M.A., Snijder E.J.;
RT "Equine arteritis virus non-structural protein 1, an essential factor for
RT viral subgenomic mRNA synthesis, interacts with the cellular transcription
RT co-factor p100.";
RL J. Gen. Virol. 84:2317-2322(2003).
RN [15]
RP FUNCTION OF NSP2.
RX PubMed=18078692; DOI=10.1016/j.chom.2007.09.014;
RA Frias-Staheli N., Giannakopoulos N.V., Kikkert M., Taylor S.L., Bridgen A.,
RA Paragas J., Richt J.A., Rowland R.R., Schmaljohn C.S., Lenschow D.J.,
RA Snijder E.J., Garcia-Sastre A., Virgin H.W.;
RT "Ovarian tumor domain-containing viral proteases evade ubiquitin- and
RT ISG15-dependent innate immune responses.";
RL Cell Host Microbe 2:404-416(2007).
RN [16]
RP CATALYTIC ACTIVITY (URIDYLATE-SPECIFIC ENDORIBONUCLEASE NSP11), AND
RP FUNCTION (URIDYLATE-SPECIFIC ENDORIBONUCLEASE NSP11).
RX PubMed=19297500; DOI=10.1128/jvi.00261-09;
RA Nedialkova D.D., Ulferts R., van den Born E., Lauber C., Gorbalenya A.E.,
RA Ziebuhr J., Snijder E.J.;
RT "Biochemical characterization of arterivirus nonstructural protein 11
RT reveals the nidovirus-wide conservation of a replicative
RT endoribonuclease.";
RL J. Virol. 83:5671-5682(2009).
RN [17]
RP PROTEOLYTIC PROCESSING OF POLYPROTEIN 1A, AND PROTEOLYTIC PROCESSING OF
RP POLYPROTEIN 1B.
RX PubMed=22258855; DOI=10.1099/vir.0.039289-0;
RA Li Y., Tas A., Snijder E.J., Fang Y.;
RT "Identification of porcine reproductive and respiratory syndrome virus
RT ORF1a-encoded non-structural proteins in virus-infected cells.";
RL J. Gen. Virol. 93:829-839(2012).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1071-1268 (NSP4).
RX PubMed=12163505; DOI=10.1074/jbc.m206978200;
RA Barrette-Ng I.H., Ng K.K.-S., Mark B.L., Van Aken D., Cherney M.M.,
RA Garen C., Kolodenko Y., Gorbalenya A.E., Snijder E.J., James M.N.G.;
RT "Structure of arterivirus nsp4. The smallest chymotrypsin-like proteinase
RT with an alpha/beta C-terminal extension and alternate conformations of the
RT oxyanion hole.";
RL J. Biol. Chem. 277:39960-39966(2002).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 2371-2772 IN COMPLEX WITH ZINC
RP IONS, FUNCTION, AND MUTAGENESIS OF LYS-2534.
RX PubMed=24369429; DOI=10.1093/nar/gkt1310;
RA Deng Z., Lehmann K.C., Li X., Feng C., Wang G., Zhang Q., Qi X., Yu L.,
RA Zhang X., Feng W., Wu W., Gong P., Tao Y., Posthuma C.C., Snijder E.J.,
RA Gorbalenya A.E., Chen Z.;
RT "Structural basis for the regulatory function of a complex zinc-binding
RT domain in a replicative arterivirus helicase resembling a nonsense-mediated
RT mRNA decay helicase.";
RL Nucleic Acids Res. 42:3464-3477(2014).
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. {ECO:0000269|PubMed:18078692}.
CC -!- FUNCTION: Nsp1 is essential for viral subgenomic mRNA synthesis.
CC {ECO:0000269|PubMed:11172046}.
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. {ECO:0000269|PubMed:18078692}.
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:0000269|PubMed:18078692}.
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:0000269|PubMed:11000230, ECO:0000269|PubMed:24369429}.
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) (PubMed:19297500). 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:0000269|PubMed:19297500}.
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 Evidence={ECO:0000269|PubMed:24369429};
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 Evidence={ECO:0000269|PubMed:24369429};
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:0000269|PubMed:19297500};
CC -!- SUBUNIT: Nsp1 interacts with cellular transcription cofactor SND1/p100.
CC {ECO:0000269|PubMed:12917451}.
CC -!- INTERACTION:
CC P19811; PRO_0000036626 [P19811]: rep; NbExp=4; IntAct=EBI-27070211, EBI-27070280;
CC -!- SUBCELLULAR LOCATION: [Nsp1 papain-like cysteine proteinase]: Host
CC nucleus. Host cytoplasm.
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=P19811-1; Sequence=Displayed;
CC Name=Replicase polyprotein 1a; Synonyms=pp1a, ORF1a polyprotein;
CC IsoId=P19811-2; Sequence=VSP_032887;
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.
CC -!- DOMAIN: The OTU-like region is responsible for the deubiquitinating and
CC deISGylation activities of Nsp2. {ECO:0000305}.
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 cofactor for nsp4.
CC {ECO:0000269|PubMed:1331507, ECO:0000269|PubMed:22258855,
CC ECO:0000269|PubMed:8617757, ECO:0000269|PubMed:9371590,
CC ECO:0000269|PubMed:9971783}.
CC -!- MISCELLANEOUS: Nsp1 contains an inactivated papain-like cysteine
CC proteinase domain due to a Lys instead of a Cys in position 73.
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}.
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DR EMBL; X53459; CAC42774.2; -; Genomic_RNA.
DR EMBL; X53459; CAC42775.2; -; Genomic_RNA.
DR EMBL; X52277; CAA36520.1; -; Genomic_RNA.
DR PIR; A39925; RRWVEV.
DR RefSeq; NP_127506.1; NC_002532.2.
DR RefSeq; NP_127507.1; NC_002532.2.
DR PDB; 1MBM; X-ray; 2.00 A; A/B/C/D=1071-1268.
DR PDB; 2L8K; NMR; -; A=1454-1575.
DR PDB; 4IUM; X-ray; 1.45 A; A=261-392.
DR PDB; 4N0N; X-ray; 2.00 A; A=2371-2772.
DR PDB; 4N0O; X-ray; 2.65 A; A/C/E/G=2371-2772.
DR PDB; 5F17; X-ray; 3.20 A; A/B/C/D/E/F=2838-3056.
DR PDB; 5HBZ; X-ray; 3.10 A; A/B/C/D/E/F=2838-3056.
DR PDB; 5HC1; X-ray; 3.10 A; A/B/C/D=2838-3056.
DR PDBsum; 1MBM; -.
DR PDBsum; 2L8K; -.
DR PDBsum; 4IUM; -.
DR PDBsum; 4N0N; -.
DR PDBsum; 4N0O; -.
DR PDBsum; 5F17; -.
DR PDBsum; 5HBZ; -.
DR PDBsum; 5HC1; -.
DR BMRB; P19811; -.
DR SMR; P19811; -.
DR MEROPS; C33.001; -.
DR MEROPS; S32.001; -.
DR PRIDE; P19811; -.
DR GeneID; 921339; -.
DR KEGG; vg:921339; -.
DR BioCyc; MetaCyc:MON-20069; -.
DR BRENDA; 3.4.21.114; 6985.
DR BRENDA; 3.4.22.B50; 6985.
DR EvolutionaryTrace; P19811; -.
DR Proteomes; UP000000353; 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:0070008; F:serine-type exopeptidase 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: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; 3.30.70.270; -; 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; IPR025773; AV_PCPbeta.
DR InterPro; IPR023183; Chymotrypsin-like_C.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR022230; DUF3756.
DR InterPro; IPR029323; EAV_nsp1.
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; IPR032786; NSP2_TM_arteriviridae.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR041053; Rep_1B.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR001205; RNA-dir_pol_C.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR InterPro; IPR041361; Znf-RING_13.
DR Pfam; PF16749; Arteri_nsp7a; 1.
DR Pfam; PF19215; CoV_NSP15_C; 1.
DR Pfam; PF12581; DUF3756; 1.
DR Pfam; PF14754; IFR3_antag; 1.
DR Pfam; PF14755; Nsp2_AV; 1.
DR Pfam; PF05412; Peptidase_C33; 1.
DR Pfam; PF05579; Peptidase_S32; 1.
DR Pfam; PF00680; RdRP_1; 1.
DR Pfam; PF17873; Rep_1B; 1.
DR Pfam; PF01443; Viral_helicase1; 1.
DR Pfam; PF17977; zf-RING_13; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Endonuclease; Glycoprotein; Helicase;
KW Host cytoplasm; Host membrane; Host nucleus; Host-virus interaction;
KW Hydrolase; Inhibition of host innate immune response by virus;
KW Inhibition of host interferon signaling pathway by virus;
KW Inhibition of host ISG15 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..3175
FT /note="Replicase polyprotein 1ab"
FT /id="PRO_0000036619"
FT CHAIN 1..260
FT /note="Nsp1 papain-like cysteine proteinase"
FT /id="PRO_0000036621"
FT CHAIN 261..831
FT /note="Nsp2 cysteine proteinase"
FT /id="PRO_0000036622"
FT CHAIN 832..1064
FT /note="Non-structural protein 3"
FT /id="PRO_0000036623"
FT CHAIN 1065..1268
FT /note="3C-like serine proteinase"
FT /id="PRO_0000036624"
FT CHAIN 1269..1677
FT /note="Non-structural protein 5-6-7"
FT /id="PRO_0000036625"
FT CHAIN 1269..1430
FT /note="Non-structural protein 5"
FT /id="PRO_0000423106"
FT CHAIN 1431..1452
FT /note="Non-structural protein 6"
FT /id="PRO_0000423107"
FT CHAIN 1453..1575
FT /note="Non-structural protein 7-alpha"
FT /id="PRO_0000423108"
FT CHAIN 1576..1677
FT /note="Non-structural protein 7-beta"
FT /id="PRO_0000423109"
FT CHAIN 1678..2370
FT /note="RNA-directed RNA polymerase"
FT /id="PRO_0000036626"
FT CHAIN 1678..1727
FT /note="Non-structural protein 8"
FT /id="PRO_0000036627"
FT CHAIN 2371..2837
FT /note="Helicase"
FT /id="PRO_0000036628"
FT CHAIN 2838..3056
FT /note="Uridylate-specific endoribonuclease nsp11"
FT /id="PRO_0000036629"
FT CHAIN 3057..3175
FT /note="Non-structural protein 12"
FT /id="PRO_0000036630"
FT TRANSMEM 530..550
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 551..571
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 625..645
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 829..849
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 903..923
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 935..955
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 977..997
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1291..1311
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1333..1353
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1355..1375
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1385..1405
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 66..156
FT /note="Peptidase C31"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00872"
FT DOMAIN 157..260
FT /note="Peptidase C32"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00873"
FT DOMAIN 261..360
FT /note="Peptidase C33"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00871"
FT DOMAIN 1065..1268
FT /note="Peptidase S32"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00826"
FT DOMAIN 1716..1883
FT /note="NiRAN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01292"
FT DOMAIN 2116..2251
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT DOMAIN 2371..2438
FT /note="AV ZBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985"
FT DOMAIN 2496..2661
FT /note="(+)RNA virus helicase ATP-binding"
FT DOMAIN 2662..2793
FT /note="(+)RNA virus helicase C-terminal"
FT DOMAIN 2840..2930
FT /note="AV-Nsp11N/CoV-Nsp15M"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01306"
FT DOMAIN 2932..3054
FT /note="NendoU"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT ZN_FING 25..44
FT /note="C4-type; atypical"
FT REGION 261..339
FT /note="OTU-like"
FT REGION 386..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..645
FT /note="HD1"
FT REGION 829..997
FT /note="HD2"
FT REGION 1291..1405
FT /note="HD3"
FT REGION 1577..1614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1593..1614
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 164
FT /note="For Nsp1 papain-like cysteine proteinase activity"
FT /evidence="ECO:0000269|PubMed:1331507,
FT ECO:0000269|PubMed:8617757"
FT ACT_SITE 230
FT /note="For Nsp1 papain-like cysteine proteinase activity"
FT /evidence="ECO:0000269|PubMed:1331507"
FT ACT_SITE 270
FT /note="For Nsp2 cysteine proteinase activity"
FT /evidence="ECO:0000269|PubMed:7622476"
FT ACT_SITE 332
FT /note="For Nsp2 cysteine proteinase activity"
FT /evidence="ECO:0000269|PubMed:7622476"
FT ACT_SITE 1103
FT /note="Charge relay system; for 3C-like serine proteinase
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00826"
FT ACT_SITE 1129
FT /note="Charge relay system; for 3C-like serine proteinase
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00826"
FT ACT_SITE 1184
FT /note="Charge relay system; for 3C-like serine proteinase
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00826"
FT ACT_SITE 2963
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT ACT_SITE 2978
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT ACT_SITE 3007
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT BINDING 319
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0007744|PDB:4IUM"
FT BINDING 349
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0007744|PDB:4IUM"
FT BINDING 354
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0007744|PDB:4IUM"
FT BINDING 356
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0007744|PDB:4IUM"
FT BINDING 2374
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985,
FT ECO:0007744|PDB:4N0N, ECO:0007744|PDB:4N0O"
FT BINDING 2377
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985,
FT ECO:0007744|PDB:4N0N, ECO:0007744|PDB:4N0O"
FT BINDING 2387
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985,
FT ECO:0007744|PDB:4N0N, ECO:0007744|PDB:4N0O"
FT BINDING 2392
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985,
FT ECO:0007744|PDB:4N0N, ECO:0007744|PDB:4N0O"
FT BINDING 2395
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985,
FT ECO:0007744|PDB:4N0N, ECO:0007744|PDB:4N0O"
FT BINDING 2399
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985,
FT ECO:0007744|PDB:4N0N, ECO:0007744|PDB:4N0O"
FT BINDING 2402
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985,
FT ECO:0007744|PDB:4N0N, ECO:0007744|PDB:4N0O"
FT BINDING 2403
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985,
FT ECO:0007744|PDB:4N0N, ECO:0007744|PDB:4N0O"
FT BINDING 2412
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985,
FT ECO:0007744|PDB:4N0N, ECO:0007744|PDB:4N0O"
FT BINDING 2414
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985,
FT ECO:0007744|PDB:4N0N, ECO:0007744|PDB:4N0O"
FT BINDING 2423
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985,
FT ECO:0007744|PDB:4N0N, ECO:0007744|PDB:4N0O"
FT BINDING 2426
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985,
FT ECO:0007744|PDB:4N0N, ECO:0007744|PDB:4N0O"
FT BINDING 2528..2535
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT SITE 260..261
FT /note="Cleavage; by PCP"
FT SITE 831..832
FT /note="Cleavage; by Nsp2 cysteine proteinase"
FT SITE 1064..1065
FT /note="Cleavage; by 3CLSP"
FT SITE 1268..1269
FT /note="Cleavage; by 3CLSP; in major pathway"
FT SITE 1430..1431
FT /note="Cleavage; by 3CLSP; in minor pathway"
FT SITE 1452..1453
FT /note="Cleavage; by 3CLSP; in minor pathway"
FT SITE 1575..1576
FT /note="Cleavage; by 3CLSP"
FT SITE 1677..1678
FT /note="Cleavage; by 3CLSP"
FT SITE 2370..2371
FT /note="Cleavage; by 3CLSP"
FT SITE 2429
FT /note="Involved in mRNA transcription process"
FT SITE 2837..2838
FT /note="Cleavage; by 3CLSP"
FT SITE 3056..3057
FT /note="Cleavage; by 3CLSP"
FT CARBOHYD 1501
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000305"
FT VAR_SEQ 1728..3175
FT /note="Missing (in isoform Replicase polyprotein 1a)"
FT /evidence="ECO:0000305"
FT /id="VSP_032887"
FT MUTAGEN 25
FT /note="C->A: Complete loss of transcription."
FT /evidence="ECO:0000269|PubMed:11172046"
FT MUTAGEN 44
FT /note="C->A: Complete loss of transcription."
FT /evidence="ECO:0000269|PubMed:11172046"
FT MUTAGEN 164
FT /note="C->G,S: Complete loss of PCP proteinase activity."
FT /evidence="ECO:0000269|PubMed:1331507,
FT ECO:0000269|PubMed:8617757"
FT MUTAGEN 219
FT /note="H->A,G,V: No effect."
FT /evidence="ECO:0000269|PubMed:1331507"
FT MUTAGEN 230
FT /note="H->A,G,V: Complete loss of PCP proteinase activity."
FT /evidence="ECO:0000269|PubMed:1331507"
FT MUTAGEN 260
FT /note="G->V: Complete loss of nsp1-nsp2 cleavage."
FT /evidence="ECO:0000269|PubMed:1331507"
FT MUTAGEN 270
FT /note="C->A,H,R,S: Complete loss of CP2 activity."
FT /evidence="ECO:0000269|PubMed:7622476"
FT MUTAGEN 271
FT /note="G->W: Complete loss of CP2 activity."
FT /evidence="ECO:0000269|PubMed:7622476"
FT MUTAGEN 291
FT /note="D->E,N: No effect."
FT /evidence="ECO:0000269|PubMed:7622476"
FT MUTAGEN 295
FT /note="D->E,N: No effect."
FT /evidence="ECO:0000269|PubMed:7622476"
FT MUTAGEN 296
FT /note="D->E,N: No effect."
FT /evidence="ECO:0000269|PubMed:7622476"
FT MUTAGEN 297
FT /note="E->D,Q: No effect."
FT /evidence="ECO:0000269|PubMed:7622476"
FT MUTAGEN 319
FT /note="C->A,H,P: Complete loss of CP2 activity."
FT /evidence="ECO:0000269|PubMed:7622476"
FT MUTAGEN 332
FT /note="H->C,I,N,Y: Complete loss of CP2 activity."
FT /evidence="ECO:0000269|PubMed:7622476"
FT MUTAGEN 344
FT /note="C->A: No effect."
FT /evidence="ECO:0000269|PubMed:7622476"
FT MUTAGEN 344
FT /note="C->H: Almost complete loss of CP2 activity."
FT /evidence="ECO:0000269|PubMed:7622476"
FT MUTAGEN 349
FT /note="C->A,H,S: Complete loss of CP2 activity."
FT /evidence="ECO:0000269|PubMed:7622476"
FT MUTAGEN 354
FT /note="C->A,H,P: Complete loss of CP2 activity."
FT /evidence="ECO:0000269|PubMed:7622476"
FT MUTAGEN 356
FT /note="C->A: Complete loss of CP2 activity."
FT /evidence="ECO:0000269|PubMed:7622476"
FT MUTAGEN 356
FT /note="C->H: No effect."
FT /evidence="ECO:0000269|PubMed:7622476"
FT MUTAGEN 831
FT /note="G->P: Complete loss of nsp2-nsp3 cleavage."
FT /evidence="ECO:0000269|PubMed:8617757"
FT MUTAGEN 1064
FT /note="E->P: Complete loss of nsp3-nsp4 cleavage."
FT /evidence="ECO:0000269|PubMed:8617757"
FT MUTAGEN 1103
FT /note="H->G,R: Complete loss of nsp3-nsp4, nsp4-nsp5 and
FT nsp5-nsp6 cleavages."
FT /evidence="ECO:0000269|PubMed:8617757"
FT MUTAGEN 1117
FT /note="D->N,T: No effect."
FT /evidence="ECO:0000269|PubMed:8617757"
FT MUTAGEN 1129
FT /note="D->E: Complete loss of nsp3-nsp4 and nsp5-nsp6
FT cleavages."
FT /evidence="ECO:0000269|PubMed:8617757"
FT MUTAGEN 1129
FT /note="D->K,V: Complete loss of nsp3-nsp4, nsp4-nsp5 and
FT nsp5-nsp6 cleavages."
FT /evidence="ECO:0000269|PubMed:8617757"
FT MUTAGEN 1179
FT /note="T->G,S: Partial loss of nsp4-nsp5 cleavage."
FT /evidence="ECO:0000269|PubMed:8617757"
FT MUTAGEN 1179
FT /note="T->N: Increased nsp5-nsp6 cleavage."
FT /evidence="ECO:0000269|PubMed:8617757"
FT MUTAGEN 1184
FT /note="S->C,F,I,T: Complete loss of nsp3-nsp4, nsp4-nsp5
FT and nsp5-nsp6 cleavages."
FT /evidence="ECO:0000269|PubMed:8617757"
FT MUTAGEN 1198
FT /note="H->L,R,Y: Complete loss of nsp4-nsp5 and nsp5-nsp6
FT cleavages."
FT /evidence="ECO:0000269|PubMed:8617757"
FT MUTAGEN 1268
FT /note="E->P: Complete loss of nsp3-nsp4 and nsp4-nsp5
FT cleavages."
FT /evidence="ECO:0000269|PubMed:8617757,
FT ECO:0000269|PubMed:9371590"
FT MUTAGEN 1430
FT /note="E->P: No effect."
FT /evidence="ECO:0000269|PubMed:8617757"
FT MUTAGEN 1677
FT /note="E->P: Complete loss of nsp5-nsp6 cleavage."
FT /evidence="ECO:0000269|PubMed:8617757"
FT MUTAGEN 2351
FT /note="D->P: No effect."
FT /evidence="ECO:0000269|PubMed:9971783"
FT MUTAGEN 2370
FT /note="E->P: Complete loss of nsp9-nsp10 cleavage."
FT /evidence="ECO:0000269|PubMed:9971783"
FT MUTAGEN 2429
FT /note="S->P: RNA can replicate efficiently but does not
FT produce the subgenomic mRNAs required for structural
FT protein expression."
FT /evidence="ECO:0000269|PubMed:9023370"
FT MUTAGEN 2534
FT /note="K->Q: Abolishes ATPase and helicase activity."
FT /evidence="ECO:0000269|PubMed:24369429"
FT MUTAGEN 2800
FT /note="E->P: No effect."
FT /evidence="ECO:0000269|PubMed:9971783"
FT MUTAGEN 2819
FT /note="D->P: No effect."
FT /evidence="ECO:0000269|PubMed:9971783"
FT MUTAGEN 2835
FT /note="E->D,P,Q: Almost complete loss of nsp9-nsp10
FT cleavage."
FT /evidence="ECO:0000269|PubMed:9971783"
FT MUTAGEN 2837
FT /note="Q->D,N: No effect."
FT /evidence="ECO:0000269|PubMed:9971783"
FT MUTAGEN 2837
FT /note="Q->E: Increased nsp9-nsp10 cleavage."
FT /evidence="ECO:0000269|PubMed:9971783"
FT MUTAGEN 2837
FT /note="Q->P: Almost complete loss of nsp9-nsp10 cleavage."
FT /evidence="ECO:0000269|PubMed:9971783"
FT MUTAGEN 3056
FT /note="E->P: Complete loss of nsp10-nsp11 cleavage."
FT /evidence="ECO:0000269|PubMed:9971783"
FT HELIX 270..277
FT /evidence="ECO:0007829|PDB:4IUM"
FT TURN 278..280
FT /evidence="ECO:0007829|PDB:4IUM"
FT STRAND 283..286
FT /evidence="ECO:0007829|PDB:4IUM"
FT HELIX 290..292
FT /evidence="ECO:0007829|PDB:4IUM"
FT HELIX 296..305
FT /evidence="ECO:0007829|PDB:4IUM"
FT STRAND 309..312
FT /evidence="ECO:0007829|PDB:4IUM"
FT STRAND 323..329
FT /evidence="ECO:0007829|PDB:4IUM"
FT STRAND 332..337
FT /evidence="ECO:0007829|PDB:4IUM"
FT HELIX 347..351
FT /evidence="ECO:0007829|PDB:4IUM"
FT HELIX 369..379
FT /evidence="ECO:0007829|PDB:4IUM"
FT TURN 380..382
FT /evidence="ECO:0007829|PDB:4IUM"
FT STRAND 383..386
FT /evidence="ECO:0007829|PDB:4IUM"
FT STRAND 1076..1092
FT /evidence="ECO:0007829|PDB:1MBM"
FT STRAND 1095..1101
FT /evidence="ECO:0007829|PDB:1MBM"
FT HELIX 1102..1105
FT /evidence="ECO:0007829|PDB:1MBM"
FT STRAND 1110..1115
FT /evidence="ECO:0007829|PDB:1MBM"
FT STRAND 1118..1123
FT /evidence="ECO:0007829|PDB:1MBM"
FT STRAND 1125..1127
FT /evidence="ECO:0007829|PDB:1MBM"
FT STRAND 1130..1135
FT /evidence="ECO:0007829|PDB:1MBM"
FT TURN 1137..1139
FT /evidence="ECO:0007829|PDB:1MBM"
FT STRAND 1154..1161
FT /evidence="ECO:0007829|PDB:1MBM"
FT STRAND 1164..1170
FT /evidence="ECO:0007829|PDB:1MBM"
FT HELIX 1181..1183
FT /evidence="ECO:0007829|PDB:1MBM"
FT STRAND 1187..1190
FT /evidence="ECO:0007829|PDB:1MBM"
FT STRAND 1193..1202
FT /evidence="ECO:0007829|PDB:1MBM"
FT HELIX 1203..1205
FT /evidence="ECO:0007829|PDB:1MBM"
FT STRAND 1206..1210
FT /evidence="ECO:0007829|PDB:1MBM"
FT STRAND 1216..1220
FT /evidence="ECO:0007829|PDB:1MBM"
FT HELIX 1224..1228
FT /evidence="ECO:0007829|PDB:1MBM"
FT STRAND 1233..1237
FT /evidence="ECO:0007829|PDB:1MBM"
FT STRAND 1250..1254
FT /evidence="ECO:0007829|PDB:1MBM"
FT HELIX 1255..1262
FT /evidence="ECO:0007829|PDB:1MBM"
FT TURN 1454..1459
FT /evidence="ECO:0007829|PDB:2L8K"
FT HELIX 1463..1474
FT /evidence="ECO:0007829|PDB:2L8K"
FT STRAND 1476..1480
FT /evidence="ECO:0007829|PDB:2L8K"
FT STRAND 1483..1486
FT /evidence="ECO:0007829|PDB:2L8K"
FT HELIX 1490..1506
FT /evidence="ECO:0007829|PDB:2L8K"
FT HELIX 1510..1520
FT /evidence="ECO:0007829|PDB:2L8K"
FT TURN 1521..1524
FT /evidence="ECO:0007829|PDB:2L8K"
FT STRAND 1533..1539
FT /evidence="ECO:0007829|PDB:2L8K"
FT STRAND 1545..1548
FT /evidence="ECO:0007829|PDB:2L8K"
FT STRAND 1551..1560
FT /evidence="ECO:0007829|PDB:2L8K"
FT STRAND 1565..1573
FT /evidence="ECO:0007829|PDB:2L8K"
FT TURN 2375..2377
FT /evidence="ECO:0007829|PDB:4N0N"
FT STRAND 2382..2385
FT /evidence="ECO:0007829|PDB:4N0N"
FT TURN 2393..2395
FT /evidence="ECO:0007829|PDB:4N0N"
FT HELIX 2396..2399
FT /evidence="ECO:0007829|PDB:4N0N"
FT STRAND 2400..2403
FT /evidence="ECO:0007829|PDB:4N0O"
FT STRAND 2405..2409
FT /evidence="ECO:0007829|PDB:4N0N"
FT HELIX 2416..2418
FT /evidence="ECO:0007829|PDB:4N0N"
FT STRAND 2419..2423
FT /evidence="ECO:0007829|PDB:4N0N"
FT TURN 2424..2428
FT /evidence="ECO:0007829|PDB:4N0N"
FT HELIX 2440..2451
FT /evidence="ECO:0007829|PDB:4N0N"
FT STRAND 2457..2462
FT /evidence="ECO:0007829|PDB:4N0N"
FT STRAND 2465..2468
FT /evidence="ECO:0007829|PDB:4N0N"
FT STRAND 2470..2475
FT /evidence="ECO:0007829|PDB:4N0N"
FT STRAND 2478..2483
FT /evidence="ECO:0007829|PDB:4N0N"
FT STRAND 2488..2494
FT /evidence="ECO:0007829|PDB:4N0N"
FT STRAND 2496..2503
FT /evidence="ECO:0007829|PDB:4N0N"
FT HELIX 2513..2521
FT /evidence="ECO:0007829|PDB:4N0N"
FT STRAND 2524..2527
FT /evidence="ECO:0007829|PDB:4N0N"
FT HELIX 2534..2544
FT /evidence="ECO:0007829|PDB:4N0N"
FT STRAND 2549..2552
FT /evidence="ECO:0007829|PDB:4N0N"
FT HELIX 2556..2568
FT /evidence="ECO:0007829|PDB:4N0N"
FT STRAND 2591..2596
FT /evidence="ECO:0007829|PDB:4N0N"
FT STRAND 2605..2609
FT /evidence="ECO:0007829|PDB:4N0N"
FT TURN 2610..2614
FT /evidence="ECO:0007829|PDB:4N0N"
FT HELIX 2617..2626
FT /evidence="ECO:0007829|PDB:4N0N"
FT STRAND 2630..2633
FT /evidence="ECO:0007829|PDB:4N0N"
FT TURN 2648..2651
FT /evidence="ECO:0007829|PDB:4N0N"
FT HELIX 2652..2654
FT /evidence="ECO:0007829|PDB:4N0N"
FT STRAND 2655..2657
FT /evidence="ECO:0007829|PDB:4N0N"
FT STRAND 2665..2667
FT /evidence="ECO:0007829|PDB:4N0O"
FT HELIX 2669..2674
FT /evidence="ECO:0007829|PDB:4N0N"
FT TURN 2675..2678
FT /evidence="ECO:0007829|PDB:4N0N"
FT STRAND 2690..2693
FT /evidence="ECO:0007829|PDB:4N0N"
FT STRAND 2702..2708
FT /evidence="ECO:0007829|PDB:4N0N"
FT HELIX 2709..2711
FT /evidence="ECO:0007829|PDB:4N0N"
FT STRAND 2717..2719
FT /evidence="ECO:0007829|PDB:4N0O"
FT HELIX 2720..2722
FT /evidence="ECO:0007829|PDB:4N0N"
FT STRAND 2727..2733
FT /evidence="ECO:0007829|PDB:4N0N"
FT STRAND 2736..2738
FT /evidence="ECO:0007829|PDB:4N0O"
FT HELIX 2742..2748
FT /evidence="ECO:0007829|PDB:4N0N"
FT STRAND 2750..2759
FT /evidence="ECO:0007829|PDB:4N0N"
FT HELIX 2765..2768
FT /evidence="ECO:0007829|PDB:4N0N"
FT STRAND 2841..2843
FT /evidence="ECO:0007829|PDB:5HBZ"
FT HELIX 2845..2851
FT /evidence="ECO:0007829|PDB:5HBZ"
FT STRAND 2855..2858
FT /evidence="ECO:0007829|PDB:5HBZ"
FT STRAND 2862..2864
FT /evidence="ECO:0007829|PDB:5HBZ"
FT HELIX 2867..2870
FT /evidence="ECO:0007829|PDB:5HBZ"
FT STRAND 2875..2879
FT /evidence="ECO:0007829|PDB:5HBZ"
FT STRAND 2882..2890
FT /evidence="ECO:0007829|PDB:5HBZ"
FT STRAND 2897..2899
FT /evidence="ECO:0007829|PDB:5HBZ"
FT STRAND 2903..2905
FT /evidence="ECO:0007829|PDB:5HBZ"
FT STRAND 2908..2910
FT /evidence="ECO:0007829|PDB:5HBZ"
FT STRAND 2919..2927
FT /evidence="ECO:0007829|PDB:5HBZ"
FT STRAND 2928..2930
FT /evidence="ECO:0007829|PDB:5HC1"
FT HELIX 2941..2944
FT /evidence="ECO:0007829|PDB:5HBZ"
FT HELIX 2952..2960
FT /evidence="ECO:0007829|PDB:5HBZ"
FT HELIX 2962..2965
FT /evidence="ECO:0007829|PDB:5HBZ"
FT STRAND 2968..2970
FT /evidence="ECO:0007829|PDB:5HBZ"
FT STRAND 2973..2975
FT /evidence="ECO:0007829|PDB:5HBZ"
FT STRAND 2992..3001
FT /evidence="ECO:0007829|PDB:5HBZ"
FT TURN 3002..3004
FT /evidence="ECO:0007829|PDB:5HBZ"
FT STRAND 3005..3013
FT /evidence="ECO:0007829|PDB:5HBZ"
FT HELIX 3017..3023
FT /evidence="ECO:0007829|PDB:5HBZ"
FT STRAND 3027..3037
FT /evidence="ECO:0007829|PDB:5HBZ"
FT STRAND 3040..3047
FT /evidence="ECO:0007829|PDB:5HBZ"
FT TURN 3048..3050
FT /evidence="ECO:0007829|PDB:5HBZ"
FT STRAND 3051..3055
FT /evidence="ECO:0007829|PDB:5HBZ"
SQ SEQUENCE 3175 AA; 345384 MW; CB536C1F5091045C CRC64;
MATFSATGFG GSFVRDWSLD LPDACEHGAG LCCEVDGSTL CAECFRGCEG MEQCPGLFMG
LLKLASPVPV GHKFLIGWYR AAKVTGRYNF LELLQHPAFA QLRVVDARLA IEEASVFIST
DHASAKRFPG ARFALTPVYA NAWVVSPAAN SLIVTTDQEQ DGFCWLKLLP PDRREAGLRL
YYNHYREQRT GWLSKTGLRL WLGDLGLGIN ASSGGLKFHI MRGSPQRAWH ITTRSCKLKS
YYVCDISEAD WSCLPAGNYG GYNPPGDGAC GYRCLAFMNG ATVVSAGCSS DLWCDDELAY
RVFQLSPTFT VTIPGGRVCP NAKYAMICDK QHWRVKRAKG VGLCLDESCF RGICNCQRMS
GPPPAPVSAA VLDHILEAAT FGNVRVVTPE GQPRPVPAPR VRPSANSSGD VKDPAPVPPV
PKPRTKLATP NPTQAPIPAP RTRLQGASTQ EPLASAGVAS DSAPKWRVAK TVYSSAERFR
TELVQRARSV GDVLVQALPL KTPAVQRYTM TLKMMRSRFS WHCDVWYPLA VIACLLPIWP
SLALLLSFAI GLIPSVGNNV VLTALLVSSA NYVASMDHQC EGAACLALLE EEHYYRAVRW
RPITGALSLV LNLLGQVGYV ARSTFDAAYV PCTVFDLCSF AILYLCRNRC WRCFGRCVRV
GPATHVLGST GQRVSKLALI DLCDHFSKPT IDVVGMATGW SGCYTGTAAM ERQCASTVDP
HSFDQKKAGA TVYLTPPVNS GSALQCLNVM WKRPIGSTVL GEQTGAVVTA VKSISFSPPC
CVSTTLPTRP GVTVVDHALY NRLTASGVDP ALLRVGQGDF LKLNPGFRLI GGWIYGICYF
VLVVVSTFTC LPIKCGIGTR DPFCRRVFSV PVTKTQEHCH AGMCASAEGI SLDSLGLTQL
QSYWIAAVTS GLVILLVCHR LAISALDLLT LASPLVLLVF PWASVGLLLA CSLAGAAVKI
QLLATLFVNL FFPQATLVTM GYWACVAALA VYSLMGLRVK VNVPMCVTPA HFLLLARSAG
QSREQMLRVS AAAPTNSLLG VARDCYVTGT TRLYIPKEGG MVFEGLFRSP KARGNVGFVA
GSSYGTGSVW TRNNEVVVLT ASHVVGRANM ATLKIGDAML TLTFKKNGDF AEAVTTQSEL
PGNWPQLHFA QPTTGPASWC TATGDEEGLL SGEVCLAWTT SGDSGSAVVQ GDAVVGVHTG
SNTSGVAYVT TPSGKLLGAD TVTLSSLSKH FTGPLTSIPK DIPDNIIADV DAVPRSLAML
IDGLSNRESS LSGPQLLLIA CFMWSYLNQP AYLPYVLGFF AANFFLPKSV GRPVVTGLLW
LCCLFTPLSM RLCLFHLVCA TVTGNVISLW FYITAAGTSY LSEMWFGGYP TMLFVPRFLV
YQFPGWAIGT VLAVCSITML AAALGHTLLL DVFSASGRFD RTFMMKYFLE GGVKESVTAS
VTRAYGKPIT QESLTATLAA LTDDDFQFLS DVLDCRAVRS AMNLRAALTS FQVAQYRNIL
NASLQVDRDA ARSRRLMAKL ADFAVEQEVT AGDRVVVIDG LDRMAHFKDD LVLVPLTTKV
VGGSRCTICD VVKEEANDTP VKPMPSRRRR KGLPKGAQLE WDRHQEEKRN AGDDDFAVSN
DYVKRVPKYW DPSDTRGTTV KIAGTTYQKV VDYSGNVHYV EHQEDLLDYV LGKGSYEGLD
QDKVLDLTNM LKVDPTELSS KDKAKARQLA HLLLDLANPV EAVNQLNLRA PHIFPGDVGR
RTFADSKDKG FVALHSRTMF LAARDFLFNI KFVCDEEFTK TPKDTLLGYV RACPGYWFIF
RRTHRSLIDA YWDSMECVYA LPTISDFDVS PGDVAVTGER WDFESPGGGR AKRLTADLVH
AFQGFHGASY SYDDKVAAAV SGDPYRSDGV LYNTRWGNIP YSVPTNALEA TACYRAGCEA
VTDGTNVIAT IGPFPEQQPI PDIPKSVLDN CADISCDAFI APAAETALCG DLEKYNLSTQ
GFVLPSVFSM VRAYLKEEIG DAPPLYLPST VPSKNSQAGI NGAEFPTKSL QSYCLIDDMV
SQSMKSNLQT ATMATCKRQY CSKYKIRSIL GTNNYIGLGL RACLSGVTAA FQKAGKDGSP
IYLGKSKFDP IPAPDKYCLE TDLESCDRST PALVRWFATN LIFELAGQPE LVHSYVLNCC
HDLVVAGSVA FTKRGGLSSG DPITSISNTI YSLVLYTQHM LLCGLEGYFP EIAEKYLDGS
LELRDMFKYV RVYIYSDDVV LTTPNQHYAA SFDRWVPHLQ ALLGFKVDPK KTVNTSSPSF
LGCRFKQVDG KCYLASLQDR VTRSLLYHIG AKNPSEYYEA AVSIFKDSII CCDEDWWTDL
HRRISGAART DGVEFPTIEM LTSFRTKQYE SAVCTVCGAA PVAKSACGGW FCGNCVPYHA
GHCHTTSLFA NCGHDIMYRS TYCTMCEGSP KQMVPKVPHP ILDHLLCHID YGSKEELTLV
VADGRTTSPP GRYKVGHKVV AVVADVGGNI VFGCGPGSHI AVPLQDTLKG VVVNKALKNA
AASEYVEGPP GSGKTFHLVK DVLAVVGSAT LVVPTHASML DCINKLKQAG ADPYFVVPKY
TVLDFPRPGS GNITVRLPQV GTSEGETFVD EVAYFSPVDL ARILTQGRVK GYGDLNQLGC
VGPASVPRNL WLRHFVSLEP LRVCHRFGAA VCDLIKGIYP YYEPAPHTTK VVFVPNPDFE
KGVVITAYHK DRGLGHRTID SIQGCTFPVV TLRLPTPQSL TRPRAVVAVT RASQELYIYD
PFDQLSGLLK FTKEAEAQDL IHGPPTACHL GQEIDLWSNE GLEYYKEVNL LYTHVPIKDG
VIHSYPNCGP ACGWEKQSNK ISCLPRVAQN LGYHYSPDLP GFCPIPKELA EHWPVVSNDR
YPNCLQITLQ QVCELSKPCS AGYMVGQSVF VQTPGVTSYW LTEWVDGKAR ALPDSLFSSG
RFETNSRAFL DEAEEKFAAA HPHACLGEIN KSTVGGSHFI FSQYLPPLLP ADAVALVGAS
LAGKAAKAAC SVVDVYAPSF EPYLHPETLS RVYKIMIDFK PCRLMVWRNA TFYVQEGVDA
VTSALAAVSK LIKVPANEPV SFHVASGYRT NALVAPQAKI SIGAYAAEWA LSTEPPPAGY
AIVRRYIVKR LLSSTEVFLC RRGVVSSTSV QTICALEGCK PLFNFLQIGS VIGPV
