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 RPOA_EAVBU              Reviewed;        3175 AA.
P19811; Q88625; Q8QZQ5; Q91DM2;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
13-APR-2004, sequence version 3.
05-JUL-2017, entry version 154.
RecName: Full=Replicase polyprotein 1ab;
AltName: Full=ORF1ab polyprotein;
Contains:
RecName: Full=Nsp1 papain-like cysteine proteinase;
Short=PCP;
EC=3.4.22.- {ECO:0000269|PubMed:1331507, ECO:0000269|PubMed:8617757};
Contains:
RecName: Full=Nsp2 cysteine proteinase;
EC=3.4.19.12;
EC=3.4.22.-;
AltName: Full=CP2;
Short=CP;
Contains:
RecName: Full=Non-structural protein 3;
Short=Nsp3;
Contains:
RecName: Full=3C-like serine proteinase;
Short=3CLSP;
EC=3.4.21.-;
AltName: Full=Nsp4;
Contains:
RecName: Full=Non-structural protein 5-6-7;
Short=Nsp5-6-7;
Contains:
RecName: Full=Non-structural protein 5;
Short=Nsp5;
Contains:
RecName: Full=Non-structural protein 6;
Short=Nsp6;
Contains:
RecName: Full=Non-structural protein 7-alpha;
Short=Nsp7-alpha;
Contains:
RecName: Full=Non-structural protein 7-beta;
Short=Nsp7-beta;
Contains:
RecName: Full=Non-structural protein 8;
Short=Nsp8;
Contains:
RecName: Full=RNA-directed RNA polymerase;
Short=Pol;
Short=RdRp;
EC=2.7.7.48;
AltName: Full=Nsp9;
Contains:
RecName: Full=Helicase {ECO:0000303|PubMed:11000230, ECO:0000303|PubMed:24369429};
Short=Hel;
EC=3.6.4.12 {ECO:0000269|PubMed:24369429};
EC=3.6.4.13 {ECO:0000269|PubMed:24369429};
AltName: Full=Nsp10;
Contains:
RecName: Full=Non-structural protein 11;
Short=Nsp11;
Contains:
RecName: Full=Non-structural protein 12;
Short=Nsp12;
Name=rep; ORFNames=1a-1b;
Equine arteritis virus (strain Bucyrus) (EAV).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Nidovirales; Arteriviridae.
NCBI_TaxID=299386;
NCBI_TaxID=9788; Equidae (horses).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=1851863;
den Boon J.A., Snijder E.J., Chirnside E.D., de Vries A.A.F.,
Horzinek M.C., Spaan W.J.M.;
"Equine arteritis virus is not a togavirus but belongs to the
coronaviruslike superfamily.";
J. Virol. 65:2910-2920(1991).
[2]
SEQUENCE REVISION.
Snijder E.J.;
Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-17.
PubMed=2162519; DOI=10.1093/nar/18.11.3241;
de Vries A.A.F., Chirnside E.D., Bredenbeek P.J., Gravestein L.A.,
Horzinek M.C., Spaan W.J.M.;
"All subgenomic mRNAs of equine arteritis virus contain a common
leader sequence.";
Nucleic Acids Res. 18:3241-3247(1990).
[4]
PROTEOLYTIC PROCESSING OF POLYPROTEIN 1A, CHARACTERIZATION OF PCP,
MUTAGENESIS OF CYS-164; HIS-219; HIS-230 AND GLY-260, CATALYTIC
ACTIVITY, AND ACTIVE SITE.
PubMed=1331507;
Snijder E.J., Wassenaar A.L.M., Spaan W.J.M.;
"The 5' end of the equine arteritis virus replicase gene encodes a
papainlike cysteine protease.";
J. Virol. 66:7040-7048(1992).
[5]
CHARACTERIZATION OF NSP2, ACTIVE SITE, AND MUTAGENESIS OF CYS-270;
GLY-271; ASP-291; ASP-295; ASP-296; GLU-297; CYS-319; HIS-332;
CYS-344; CYS-349; CYS-354 AND CYS-356.
PubMed=7622476; DOI=10.1074/jbc.270.28.16671;
Snijder E.J., Wassenaar A.L.M., Spaan W.J.M., Gorbalenya A.E.;
"The arterivirus Nsp2 protease. An unusual cysteine protease with
primary structure similarities to both papain-like and chymotrypsin-
like proteases.";
J. Biol. Chem. 270:16671-16676(1995).
[6]
PROTEOLYTIC PROCESSING OF POLYPROTEIN 1A, CHARACTERIZATION OF 3CLSP,
CATALYTIC ACTIVITY, ACTIVE SITE, AND MUTAGENESIS OF CYS-164; GLY-831;
GLU-1064; HIS-1103; ASP-1117; ASP-1129; THR-1179; SER-1184; HIS-1198;
GLU-1268; GLU-1430 AND GLU-1677.
PubMed=8617757; DOI=10.1074/jbc.271.9.4864;
Snijder E.J., Wassenaar A.L.M., van Dinten L.C., Spaan W.J.M.,
Gorbalenya A.E.;
"The arterivirus nsp4 protease is the prototype of a novel group of
chymotrypsin-like enzymes, the 3C-like serine proteases.";
J. Biol. Chem. 271:4864-4871(1996).
[7]
MUTAGENESIS OF SER-2429.
PubMed=9023370; DOI=10.1073/pnas.94.3.991;
van Dinten L.C., den Boon J.A., Wassenaar A.L.M., Spaan W.J.M.,
Snijder E.J.;
"An infectious arterivirus cDNA clone: identification of a replicase
point mutation that abolishes discontinuous mRNA transcription.";
Proc. Natl. Acad. Sci. U.S.A. 94:991-996(1997).
[8]
PROTEOLYTIC PROCESSING OF POLYPROTEIN 1A, AND MUTAGENESIS OF GLU-1268.
PubMed=9371590;
Wassenaar A.L.M., Spaan W.J.M., Gorbalenya A.E., Snijder E.J.;
"Alternative proteolytic processing of the arterivirus replicase ORF1a
polyprotein: evidence that NSP2 acts as a cofactor for the NSP4 serine
protease.";
J. Virol. 71:9313-9322(1997).
[9]
SUBCELLULAR LOCATION.
PubMed=9658116;
van der Meer Y., van Tol H., Locker J.K., Snijder E.J.;
"ORF1a-encoded replicase subunits are involved in the membrane
association of the arterivirus replication complex.";
J. Virol. 72:6689-6698(1998).
[10]
PROTEOLYTIC PROCESSING OF POLYPROTEIN 1B, AND MUTAGENESIS OF ASP-2351;
GLU-2370; GLU-2800; ASP-2819; GLU-2835; GLN-2837 AND GLU-3056.
PubMed=9971783;
van Dinten L.C., Rensen S., Gorbalenya A.E., Snijder E.J.;
"Proteolytic processing of the open reading frame 1b-encoded part of
arterivirus replicase is mediated by nsp4 serine protease and is
essential for virus replication.";
J. Virol. 73:2027-2037(1999).
[11]
CHARACTERIZATION OF HELICASE.
PubMed=11000230; DOI=10.1128/JVI.74.20.9586-9593.2000;
Seybert A., van Dinten L.C., Snijder E.J., Ziebuhr J.;
"Biochemical characterization of the equine arteritis virus helicase
suggests a close functional relationship between arterivirus and
coronavirus helicases.";
J. Virol. 74:9586-9593(2000).
[12]
C4-TYPE ZINC-FINGER OF NSP1, AND MUTAGENESIS OF CYS-25 AND CYS-44.
PubMed=11172046; DOI=10.1073/pnas.98.4.1889;
Tijms M.A., van Dinten L.C., Gorbalenya A.E., Snijder E.J.;
"A zinc finger-containing papain-like protease couples subgenomic mRNA
synthesis to genome translation in a positive-stranded RNA virus.";
Proc. Natl. Acad. Sci. U.S.A. 98:1889-1894(2001).
[13]
SUBCELLULAR LOCATION OF NSP1 PAPAIN-LIKE CYSTEINE PROTEINASE.
PubMed=11907328;
Tijms M.A., van der Meer Y., Snijder E.J.;
"Nuclear localization of non-structural protein 1 and nucleocapsid
protein of equine arteritis virus.";
J. Gen. Virol. 83:795-800(2002).
[14]
INTERACTION WITH HUMAN SND1/P100.
PubMed=12917451; DOI=10.1099/vir.0.19297-0;
Tijms M.A., Snijder E.J.;
"Equine arteritis virus non-structural protein 1, an essential factor
for viral subgenomic mRNA synthesis, interacts with the cellular
transcription co-factor p100.";
J. Gen. Virol. 84:2317-2322(2003).
[15]
FUNCTION OF NSP2.
PubMed=18078692; DOI=10.1016/j.chom.2007.09.014;
Frias-Staheli N., Giannakopoulos N.V., Kikkert M., Taylor S.L.,
Bridgen A., Paragas J., Richt J.A., Rowland R.R., Schmaljohn C.S.,
Lenschow D.J., Snijder E.J., Garcia-Sastre A., Virgin H.W.;
"Ovarian tumor domain-containing viral proteases evade ubiquitin- and
ISG15-dependent innate immune responses.";
Cell Host Microbe 2:404-416(2007).
[16]
PROTEOLYTIC PROCESSING OF POLYPROTEIN 1A, AND PROTEOLYTIC PROCESSING
OF POLYPROTEIN 1B.
PubMed=22258855; DOI=10.1099/vir.0.039289-0;
Li Y., Tas A., Snijder E.J., Fang Y.;
"Identification of porcine reproductive and respiratory syndrome virus
ORF1a-encoded non-structural proteins in virus-infected cells.";
J. Gen. Virol. 93:829-839(2012).
[17]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1071-1268 (NSP4).
PubMed=12163505; DOI=10.1074/jbc.M206978200;
Barrette-Ng I.H., Ng K.K.-S., Mark B.L., Van Aken D., Cherney M.M.,
Garen C., Kolodenko Y., Gorbalenya A.E., Snijder E.J., James M.N.G.;
"Structure of arterivirus nsp4. The smallest chymotrypsin-like
proteinase with an alpha/beta C-terminal extension and alternate
conformations of the oxyanion hole.";
J. Biol. Chem. 277:39960-39966(2002).
[18]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 2371-2772 IN COMPLEX WITH
ZINC IONS, FUNCTION, AND MUTAGENESIS OF LYS-2534.
PubMed=24369429; DOI=10.1093/nar/gkt1310;
Deng Z., Lehmann K.C., Li X., Feng C., Wang G., Zhang Q., Qi X.,
Yu L., Zhang X., Feng W., Wu W., Gong P., Tao Y., Posthuma C.C.,
Snijder E.J., Gorbalenya A.E., Chen Z.;
"Structural basis for the regulatory function of a complex zinc-
binding domain in a replicative arterivirus helicase resembling a
nonsense-mediated mRNA decay helicase.";
Nucleic Acids Res. 42:3464-3477(2014).
-!- FUNCTION: The replicase polyprotein 1ab is a multifunctional
protein: it contains the activities necessary for the
transcription of negative stranded RNA, leader RNA, subgenomic
mRNAs and progeny virion RNA as well as proteinases responsible
for the cleavage of the polyprotein into functional products.
{ECO:0000269|PubMed:18078692}.
-!- FUNCTION: Nsp1 is essential for viral subgenomic mRNA synthesis.
{ECO:0000269|PubMed:11172046}.
-!- FUNCTION: Nsp2 cysteine proteinase which cleaves the nsp2/nsp3
site in the polyprotein. Also displays deubiquitinating and
deISGylase activities. The deubiquitinating activity cleaves both
ubiquitinated and ISGylated products and may therefore regulate
ubiquitin and ISG15 dependent host innate immunity.
{ECO:0000269|PubMed:18078692}.
-!- FUNCTION: The 3C-like serine proteinase chain is responsible for
the majority of cleavages as it cleaves the C-terminus of the
polyprotein. {ECO:0000269|PubMed:18078692}.
-!- FUNCTION: The helicase chain, which contains a zinc finger
structure, displays RNA and DNA duplex-unwinding activities with
5' to 3' polarity. {ECO:0000269|PubMed:11000230,
ECO:0000269|PubMed:24369429}.
-!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
+ RNA(n+1). {ECO:0000255|PROSITE-ProRule:PRU00539}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
{ECO:0000269|PubMed:24369429}.
-!- CATALYTIC ACTIVITY: Thiol-dependent hydrolysis of ester,
thioester, amide, peptide and isopeptide bonds formed by the C-
terminal Gly of ubiquitin (a 76-residue protein attached to
proteins as an intracellular targeting signal).
-!- SUBUNIT: Nsp1 interacts with cellular transcription cofactor
SND1/p100. {ECO:0000269|PubMed:12917451}.
-!- SUBCELLULAR LOCATION: Nsp1 papain-like cysteine proteinase: Host
nucleus. Host cytoplasm.
-!- SUBCELLULAR LOCATION: Nsp2 cysteine proteinase: Host membrane
{ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Non-structural protein 3: Host membrane
{ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Non-structural protein 5-6-7: Host membrane
{ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
-!- SUBCELLULAR LOCATION: 3C-like serine proteinase: Host cytoplasm
{ECO:0000305}.
-!- SUBCELLULAR LOCATION: RNA-directed RNA polymerase: Host cytoplasm,
host perinuclear region {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Helicase: Host cytoplasm, host perinuclear
region {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Ribosomal frameshifting; Named isoforms=2;
Name=Replicase polyprotein 1ab; Synonyms=pp1ab;
IsoId=P19811-1; Sequence=Displayed;
Note=Produced by -1 ribosomal frameshifting at the 1a-1b genes
boundary.;
Name=Replicase polyprotein 1a; Synonyms=pp1a, ORF1a polyprotein;
IsoId=P19811-2; Sequence=VSP_032887;
Note=Produced by conventional translation.;
-!- DOMAIN: The hydrophobic domains (HD) could mediate the membrane
association of the replication complex and thereby alter the
architecture of the host cell membrane.
-!- DOMAIN: The OTU-like region is responsible for the
deubiquitinating and deISGylation activities of Nsp2.
{ECO:0000305}.
-!- PTM: Specific enzymatic cleavages in vivo by its own proteases
yield mature proteins. There are two alternative pathways for
processing. Either nsp4-5 is cleaved, which represents the major
pathway or the nsp5-6 and nsp6-7 are processed, which represents
the minor pathway. The major pathway occurs when nsp2 acts as
cofactor for nsp4. {ECO:0000269|PubMed:1331507,
ECO:0000269|PubMed:22258855, ECO:0000269|PubMed:8617757,
ECO:0000269|PubMed:9371590, ECO:0000269|PubMed:9971783}.
-!- MISCELLANEOUS: Nsp1 contains an inactivated papain-like cysteine
proteinase domain due to a Lys instead of a Cys in position 73.
-!- SIMILARITY: Belongs to the arteriviridae polyprotein family.
{ECO:0000305}.
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EMBL; X53459; CAC42774.2; -; Genomic_RNA.
EMBL; X53459; CAC42775.2; -; Genomic_RNA.
EMBL; X52277; CAA36520.1; -; Genomic_RNA.
PIR; A39925; RRWVEV.
RefSeq; NP_127506.1; NC_002532.2.
RefSeq; NP_127507.1; NC_002532.2.
PDB; 1MBM; X-ray; 2.00 A; A/B/C/D=1071-1268.
PDB; 2L8K; NMR; -; A=1454-1575.
PDB; 4IUM; X-ray; 1.45 A; A=261-392.
PDB; 4N0N; X-ray; 2.00 A; A=2371-2772.
PDB; 4N0O; X-ray; 2.65 A; A/C/E/G=2371-2772.
PDB; 5F17; X-ray; 3.20 A; A/B/C/D/E/F=2838-3056.
PDB; 5HBZ; X-ray; 3.10 A; A/B/C/D/E/F=2838-3056.
PDB; 5HC1; X-ray; 3.10 A; A/B/C/D=2838-3056.
PDBsum; 1MBM; -.
PDBsum; 2L8K; -.
PDBsum; 4IUM; -.
PDBsum; 4N0N; -.
PDBsum; 4N0O; -.
PDBsum; 5F17; -.
PDBsum; 5HBZ; -.
PDBsum; 5HC1; -.
ProteinModelPortal; P19811; -.
SMR; P19811; -.
MEROPS; C33.001; -.
GeneID; 921339; -.
KEGG; vg:921339; -.
OrthoDB; VOG090000J7; -.
BRENDA; 3.4.21.114; 6985.
EvolutionaryTrace; P19811; -.
Proteomes; UP000000353; Genome.
GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
GO; GO:0044220; C:host cell perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; IEA:InterPro.
GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
GO; GO:0070008; F:serine-type exopeptidase activity; IEA:InterPro.
GO; GO:0036459; F:thiol-dependent ubiquitinyl hydrolase activity; IEA:UniProtKB-EC.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0039648; P:modulation by virus of host protein ubiquitination; IEA:UniProtKB-KW.
GO; GO:0039579; P:suppression by virus of host ISG15 activity; IEA:UniProtKB-KW.
GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
GO; GO:0019082; P:viral protein processing; IEA:InterPro.
GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
Gene3D; 3.30.40.20; -; 1.
InterPro; IPR027351; (+)RNA_virus_helicase_core_dom.
InterPro; IPR031932; Arteri_nsp7a.
InterPro; IPR008743; Arterivirus_Nsp2_C33.
InterPro; IPR023338; Arterivirus_NSP4_peptidase.
InterPro; IPR008741; AV_PCPalpha.
InterPro; IPR025773; AV_PCPbeta.
InterPro; IPR027355; AV_ZBD.
InterPro; IPR023183; Chymotrypsin-like_domain3.
InterPro; IPR022230; DUF3756.
InterPro; IPR029323; EAV_nsp1.
InterPro; IPR008760; EAV_peptidase_S32.
InterPro; IPR032786; Nsp3.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001205; RNA-dir_pol_C.
InterPro; IPR007094; RNA-dir_pol_PSvirus.
Pfam; PF16749; Arteri_nsp7a; 1.
Pfam; PF12581; DUF3756; 1.
Pfam; PF14755; ER-remodelling; 1.
Pfam; PF14754; IFR3_antag; 1.
Pfam; PF05412; Peptidase_C33; 1.
Pfam; PF05579; Peptidase_S32; 1.
Pfam; PF00680; RdRP_1; 1.
Pfam; PF01443; Viral_helicase1; 1.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS51538; AV_CP; 1.
PROSITE; PS51493; AV_NSP4_PRO; 1.
PROSITE; PS51539; AV_PCP_ALPHA; 1.
PROSITE; PS51540; AV_PCP_BETA; 1.
PROSITE; PS51652; AV_ZBD; 1.
PROSITE; PS51657; PSRV_HELICASE; 1.
PROSITE; PS50507; RDRP_SSRNA_POS; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Complete proteome; Glycoprotein; Helicase;
Host cytoplasm; Host membrane; Host nucleus; Host-virus interaction;
Hydrolase; Inhibition of host innate immune response by virus;
Inhibition of host interferon signaling pathway by virus;
Inhibition of host ISG15 by virus; Membrane; Metal-binding;
Modulation of host ubiquitin pathway by viral deubiquitinase;
Modulation of host ubiquitin pathway by virus; Multifunctional enzyme;
Nucleotide-binding; Nucleotidyltransferase; Protease;
Reference proteome; Ribosomal frameshifting;
RNA-directed RNA polymerase; Serine protease; Thiol protease;
Transferase; Transmembrane; Transmembrane helix; Viral immunoevasion;
Viral RNA replication; Zinc; Zinc-finger.
CHAIN 1 3175 Replicase polyprotein 1ab.
/FTId=PRO_0000036619.
CHAIN 1 260 Nsp1 papain-like cysteine proteinase.
/FTId=PRO_0000036621.
CHAIN 261 831 Nsp2 cysteine proteinase.
/FTId=PRO_0000036622.
CHAIN 832 1064 Non-structural protein 3.
/FTId=PRO_0000036623.
CHAIN 1065 1268 3C-like serine proteinase.
/FTId=PRO_0000036624.
CHAIN 1269 1677 Non-structural protein 5-6-7.
/FTId=PRO_0000036625.
CHAIN 1269 1430 Non-structural protein 5.
/FTId=PRO_0000423106.
CHAIN 1431 1452 Non-structural protein 6.
/FTId=PRO_0000423107.
CHAIN 1453 1575 Non-structural protein 7-alpha.
/FTId=PRO_0000423108.
CHAIN 1576 1677 Non-structural protein 7-beta.
/FTId=PRO_0000423109.
CHAIN 1678 2370 RNA-directed RNA polymerase.
/FTId=PRO_0000036626.
CHAIN 1678 1727 Non-structural protein 8.
/FTId=PRO_0000036627.
CHAIN 2371 2837 Helicase.
/FTId=PRO_0000036628.
CHAIN 2838 3056 Non-structural protein 11.
/FTId=PRO_0000036629.
CHAIN 3057 3175 Non-structural protein 12.
/FTId=PRO_0000036630.
TRANSMEM 530 550 Helical. {ECO:0000255}.
TRANSMEM 551 571 Helical. {ECO:0000255}.
TRANSMEM 625 645 Helical. {ECO:0000255}.
TRANSMEM 829 849 Helical. {ECO:0000255}.
TRANSMEM 903 923 Helical. {ECO:0000255}.
TRANSMEM 935 955 Helical. {ECO:0000255}.
TRANSMEM 977 997 Helical. {ECO:0000255}.
TRANSMEM 1291 1311 Helical. {ECO:0000255}.
TRANSMEM 1333 1353 Helical. {ECO:0000255}.
TRANSMEM 1355 1375 Helical. {ECO:0000255}.
TRANSMEM 1385 1405 Helical. {ECO:0000255}.
DOMAIN 66 156 Peptidase C31. {ECO:0000255|PROSITE-
ProRule:PRU00872}.
DOMAIN 157 260 Peptidase C32. {ECO:0000255|PROSITE-
ProRule:PRU00873}.
DOMAIN 261 360 Peptidase C33. {ECO:0000255|PROSITE-
ProRule:PRU00871}.
DOMAIN 1065 1268 Peptidase S32. {ECO:0000255|PROSITE-
ProRule:PRU00826}.
DOMAIN 2116 2251 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
DOMAIN 2371 2438 AV ZBD. {ECO:0000255|PROSITE-
ProRule:PRU00985}.
DOMAIN 2496 2661 (+)RNA virus helicase ATP-binding.
DOMAIN 2662 2793 (+)RNA virus helicase C-terminal.
ZN_FING 25 44 C4-type; atypical.
NP_BIND 2528 2535 ATP. {ECO:0000250}.
REGION 261 339 OTU-like.
REGION 530 645 HD1.
REGION 829 997 HD2.
REGION 1291 1405 HD3.
COMPBIAS 389 440 Pro-rich.
ACT_SITE 164 164 For Nsp1 papain-like cysteine proteinase
activity. {ECO:0000269|PubMed:1331507,
ECO:0000269|PubMed:8617757}.
ACT_SITE 230 230 For Nsp1 papain-like cysteine proteinase
activity. {ECO:0000269|PubMed:1331507}.
ACT_SITE 270 270 For Nsp2 cysteine proteinase activity.
{ECO:0000269|PubMed:7622476}.
ACT_SITE 332 332 For Nsp2 cysteine proteinase activity.
{ECO:0000269|PubMed:7622476}.
ACT_SITE 1103 1103 Charge relay system; for 3C-like serine
proteinase activity.
{ECO:0000255|PROSITE-ProRule:PRU00826}.
ACT_SITE 1129 1129 Charge relay system; for 3C-like serine
proteinase activity.
{ECO:0000255|PROSITE-ProRule:PRU00826}.
ACT_SITE 1184 1184 Charge relay system; for 3C-like serine
proteinase activity.
{ECO:0000255|PROSITE-ProRule:PRU00826}.
METAL 319 319 Zinc 1. {ECO:0000244|PDB:4IUM}.
METAL 349 349 Zinc 1. {ECO:0000244|PDB:4IUM}.
METAL 354 354 Zinc 1. {ECO:0000244|PDB:4IUM}.
METAL 356 356 Zinc 1. {ECO:0000244|PDB:4IUM}.
METAL 2374 2374 Zinc 2. {ECO:0000244|PDB:4N0N,
ECO:0000244|PDB:4N0O,
ECO:0000255|PROSITE-ProRule:PRU00985}.
METAL 2377 2377 Zinc 2. {ECO:0000244|PDB:4N0N,
ECO:0000244|PDB:4N0O,
ECO:0000255|PROSITE-ProRule:PRU00985}.
METAL 2387 2387 Zinc 3. {ECO:0000244|PDB:4N0N,
ECO:0000244|PDB:4N0O,
ECO:0000255|PROSITE-ProRule:PRU00985}.
METAL 2392 2392 Zinc 2. {ECO:0000244|PDB:4N0N,
ECO:0000244|PDB:4N0O,
ECO:0000255|PROSITE-ProRule:PRU00985}.
METAL 2395 2395 Zinc 2. {ECO:0000244|PDB:4N0N,
ECO:0000244|PDB:4N0O,
ECO:0000255|PROSITE-ProRule:PRU00985}.
METAL 2399 2399 Zinc 3; via tele nitrogen.
{ECO:0000244|PDB:4N0N,
ECO:0000244|PDB:4N0O,
ECO:0000255|PROSITE-ProRule:PRU00985}.
METAL 2402 2402 Zinc 3; via pros nitrogen.
{ECO:0000244|PDB:4N0N,
ECO:0000244|PDB:4N0O,
ECO:0000255|PROSITE-ProRule:PRU00985}.
METAL 2403 2403 Zinc 3. {ECO:0000244|PDB:4N0N,
ECO:0000244|PDB:4N0O,
ECO:0000255|PROSITE-ProRule:PRU00985}.
METAL 2412 2412 Zinc 4. {ECO:0000244|PDB:4N0N,
ECO:0000244|PDB:4N0O,
ECO:0000255|PROSITE-ProRule:PRU00985}.
METAL 2414 2414 Zinc 4; via pros nitrogen.
{ECO:0000244|PDB:4N0N,
ECO:0000244|PDB:4N0O,
ECO:0000255|PROSITE-ProRule:PRU00985}.
METAL 2423 2423 Zinc 4. {ECO:0000244|PDB:4N0N,
ECO:0000244|PDB:4N0O,
ECO:0000255|PROSITE-ProRule:PRU00985}.
METAL 2426 2426 Zinc 4. {ECO:0000244|PDB:4N0N,
ECO:0000244|PDB:4N0O,
ECO:0000255|PROSITE-ProRule:PRU00985}.
SITE 260 261 Cleavage; by PCP.
SITE 831 832 Cleavage; by Nsp2 cysteine proteinase.
SITE 1064 1065 Cleavage; by 3CLSP.
SITE 1268 1269 Cleavage; by 3CLSP; in major pathway.
SITE 1430 1431 Cleavage; by 3CLSP; in minor pathway.
SITE 1452 1453 Cleavage; by 3CLSP; in minor pathway.
SITE 1575 1576 Cleavage; by 3CLSP.
SITE 1677 1678 Cleavage; by 3CLSP.
SITE 2370 2371 Cleavage; by 3CLSP.
SITE 2429 2429 Involved in mRNA transcription process.
SITE 2837 2838 Cleavage; by 3CLSP.
SITE 3056 3057 Cleavage; by 3CLSP.
CARBOHYD 1501 1501 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000305}.
VAR_SEQ 1728 3175 Missing (in isoform Replicase polyprotein
1a). {ECO:0000305}.
/FTId=VSP_032887.
MUTAGEN 25 25 C->A: Complete loss of transcription.
{ECO:0000269|PubMed:11172046}.
MUTAGEN 44 44 C->A: Complete loss of transcription.
{ECO:0000269|PubMed:11172046}.
MUTAGEN 164 164 C->G,S: Complete loss of PCP proteinase
activity. {ECO:0000269|PubMed:1331507,
ECO:0000269|PubMed:8617757}.
MUTAGEN 219 219 H->A,G,V: No effect.
{ECO:0000269|PubMed:1331507}.
MUTAGEN 230 230 H->A,G,V: Complete loss of PCP proteinase
activity. {ECO:0000269|PubMed:1331507}.
MUTAGEN 260 260 G->V: Complete loss of nsp1-nsp2
cleavage. {ECO:0000269|PubMed:1331507}.
MUTAGEN 270 270 C->A,H,R,S: Complete loss of CP2
activity. {ECO:0000269|PubMed:7622476}.
MUTAGEN 271 271 G->W: Complete loss of CP2 activity.
{ECO:0000269|PubMed:7622476}.
MUTAGEN 291 291 D->E,N: No effect.
{ECO:0000269|PubMed:7622476}.
MUTAGEN 295 295 D->E,N: No effect.
{ECO:0000269|PubMed:7622476}.
MUTAGEN 296 296 D->E,N: No effect.
{ECO:0000269|PubMed:7622476}.
MUTAGEN 297 297 E->D,Q: No effect.
{ECO:0000269|PubMed:7622476}.
MUTAGEN 319 319 C->A,H,P: Complete loss of CP2 activity.
{ECO:0000269|PubMed:7622476}.
MUTAGEN 332 332 H->C,I,N,Y: Complete loss of CP2
activity. {ECO:0000269|PubMed:7622476}.
MUTAGEN 344 344 C->A: No effect.
{ECO:0000269|PubMed:7622476}.
MUTAGEN 344 344 C->H: Almost complete loss of CP2
activity. {ECO:0000269|PubMed:7622476}.
MUTAGEN 349 349 C->A,H,S: Complete loss of CP2 activity.
{ECO:0000269|PubMed:7622476}.
MUTAGEN 354 354 C->A,H,P: Complete loss of CP2 activity.
{ECO:0000269|PubMed:7622476}.
MUTAGEN 356 356 C->A: Complete loss of CP2 activity.
{ECO:0000269|PubMed:7622476}.
MUTAGEN 356 356 C->H: No effect.
{ECO:0000269|PubMed:7622476}.
MUTAGEN 831 831 G->P: Complete loss of nsp2-nsp3
cleavage. {ECO:0000269|PubMed:8617757}.
MUTAGEN 1064 1064 E->P: Complete loss of nsp3-nsp4
cleavage. {ECO:0000269|PubMed:8617757}.
MUTAGEN 1103 1103 H->G,R: Complete loss of nsp3-nsp4, nsp4-
nsp5 and nsp5-nsp6 cleavages.
{ECO:0000269|PubMed:8617757}.
MUTAGEN 1117 1117 D->N,T: No effect.
{ECO:0000269|PubMed:8617757}.
MUTAGEN 1129 1129 D->E: Complete loss of nsp3-nsp4 and
nsp5-nsp6 cleavages.
{ECO:0000269|PubMed:8617757}.
MUTAGEN 1129 1129 D->K,V: Complete loss of nsp3-nsp4, nsp4-
nsp5 and nsp5-nsp6 cleavages.
{ECO:0000269|PubMed:8617757}.
MUTAGEN 1179 1179 T->G,S: Partial loss of nsp4-nsp5
cleavage. {ECO:0000269|PubMed:8617757}.
MUTAGEN 1179 1179 T->N: Increased nsp5-nsp6 cleavage.
{ECO:0000269|PubMed:8617757}.
MUTAGEN 1184 1184 S->C,F,I,T: Complete loss of nsp3-nsp4,
nsp4-nsp5 and nsp5-nsp6 cleavages.
{ECO:0000269|PubMed:8617757}.
MUTAGEN 1198 1198 H->L,R,Y: Complete loss of nsp4-nsp5 and
nsp5-nsp6 cleavages.
{ECO:0000269|PubMed:8617757}.
MUTAGEN 1268 1268 E->P: Complete loss of nsp3-nsp4 and
nsp4-nsp5 cleavages.
{ECO:0000269|PubMed:8617757,
ECO:0000269|PubMed:9371590}.
MUTAGEN 1430 1430 E->P: No effect.
{ECO:0000269|PubMed:8617757}.
MUTAGEN 1677 1677 E->P: Complete loss of nsp5-nsp6
cleavage. {ECO:0000269|PubMed:8617757}.
MUTAGEN 2351 2351 D->P: No effect.
{ECO:0000269|PubMed:9971783}.
MUTAGEN 2370 2370 E->P: Complete loss of nsp9-nsp10
cleavage. {ECO:0000269|PubMed:9971783}.
MUTAGEN 2429 2429 S->P: RNA can replicate efficiently but
does not produce the subgenomic mRNAs
required for structural protein
expression. {ECO:0000269|PubMed:9023370}.
MUTAGEN 2534 2534 K->Q: Abolishes ATPase and helicase
activity. {ECO:0000269|PubMed:24369429}.
MUTAGEN 2800 2800 E->P: No effect.
{ECO:0000269|PubMed:9971783}.
MUTAGEN 2819 2819 D->P: No effect.
{ECO:0000269|PubMed:9971783}.
MUTAGEN 2835 2835 E->D,P,Q: Almost complete loss of nsp9-
nsp10 cleavage.
{ECO:0000269|PubMed:9971783}.
MUTAGEN 2837 2837 Q->D,N: No effect.
{ECO:0000269|PubMed:9971783}.
MUTAGEN 2837 2837 Q->E: Increased nsp9-nsp10 cleavage.
{ECO:0000269|PubMed:9971783}.
MUTAGEN 2837 2837 Q->P: Almost complete loss of nsp9-nsp10
cleavage. {ECO:0000269|PubMed:9971783}.
MUTAGEN 3056 3056 E->P: Complete loss of nsp10-nsp11
cleavage. {ECO:0000269|PubMed:9971783}.
HELIX 270 277 {ECO:0000244|PDB:4IUM}.
TURN 278 280 {ECO:0000244|PDB:4IUM}.
STRAND 283 286 {ECO:0000244|PDB:4IUM}.
HELIX 290 292 {ECO:0000244|PDB:4IUM}.
HELIX 296 305 {ECO:0000244|PDB:4IUM}.
STRAND 309 312 {ECO:0000244|PDB:4IUM}.
STRAND 323 329 {ECO:0000244|PDB:4IUM}.
STRAND 332 337 {ECO:0000244|PDB:4IUM}.
HELIX 347 351 {ECO:0000244|PDB:4IUM}.
HELIX 369 379 {ECO:0000244|PDB:4IUM}.
TURN 380 382 {ECO:0000244|PDB:4IUM}.
STRAND 383 386 {ECO:0000244|PDB:4IUM}.
STRAND 1076 1092 {ECO:0000244|PDB:1MBM}.
STRAND 1095 1101 {ECO:0000244|PDB:1MBM}.
HELIX 1102 1105 {ECO:0000244|PDB:1MBM}.
STRAND 1110 1115 {ECO:0000244|PDB:1MBM}.
STRAND 1118 1123 {ECO:0000244|PDB:1MBM}.
STRAND 1125 1127 {ECO:0000244|PDB:1MBM}.
STRAND 1130 1135 {ECO:0000244|PDB:1MBM}.
TURN 1137 1139 {ECO:0000244|PDB:1MBM}.
STRAND 1154 1161 {ECO:0000244|PDB:1MBM}.
STRAND 1164 1170 {ECO:0000244|PDB:1MBM}.
HELIX 1181 1183 {ECO:0000244|PDB:1MBM}.
STRAND 1187 1190 {ECO:0000244|PDB:1MBM}.
STRAND 1193 1202 {ECO:0000244|PDB:1MBM}.
HELIX 1203 1205 {ECO:0000244|PDB:1MBM}.
STRAND 1206 1210 {ECO:0000244|PDB:1MBM}.
STRAND 1216 1220 {ECO:0000244|PDB:1MBM}.
HELIX 1224 1228 {ECO:0000244|PDB:1MBM}.
STRAND 1233 1237 {ECO:0000244|PDB:1MBM}.
STRAND 1250 1254 {ECO:0000244|PDB:1MBM}.
HELIX 1255 1262 {ECO:0000244|PDB:1MBM}.
TURN 1454 1459 {ECO:0000244|PDB:2L8K}.
HELIX 1463 1474 {ECO:0000244|PDB:2L8K}.
STRAND 1476 1480 {ECO:0000244|PDB:2L8K}.
STRAND 1483 1486 {ECO:0000244|PDB:2L8K}.
HELIX 1490 1506 {ECO:0000244|PDB:2L8K}.
HELIX 1510 1520 {ECO:0000244|PDB:2L8K}.
TURN 1521 1524 {ECO:0000244|PDB:2L8K}.
STRAND 1533 1539 {ECO:0000244|PDB:2L8K}.
STRAND 1545 1548 {ECO:0000244|PDB:2L8K}.
STRAND 1551 1560 {ECO:0000244|PDB:2L8K}.
STRAND 1565 1573 {ECO:0000244|PDB:2L8K}.
TURN 2375 2377 {ECO:0000244|PDB:4N0N}.
STRAND 2382 2385 {ECO:0000244|PDB:4N0N}.
TURN 2393 2395 {ECO:0000244|PDB:4N0N}.
HELIX 2396 2399 {ECO:0000244|PDB:4N0N}.
STRAND 2400 2403 {ECO:0000244|PDB:4N0O}.
STRAND 2405 2409 {ECO:0000244|PDB:4N0N}.
HELIX 2416 2418 {ECO:0000244|PDB:4N0N}.
STRAND 2419 2423 {ECO:0000244|PDB:4N0N}.
TURN 2424 2428 {ECO:0000244|PDB:4N0N}.
HELIX 2440 2451 {ECO:0000244|PDB:4N0N}.
STRAND 2457 2462 {ECO:0000244|PDB:4N0N}.
STRAND 2465 2468 {ECO:0000244|PDB:4N0N}.
STRAND 2470 2475 {ECO:0000244|PDB:4N0N}.
STRAND 2478 2483 {ECO:0000244|PDB:4N0N}.
STRAND 2488 2494 {ECO:0000244|PDB:4N0N}.
STRAND 2496 2503 {ECO:0000244|PDB:4N0N}.
HELIX 2513 2521 {ECO:0000244|PDB:4N0N}.
STRAND 2524 2527 {ECO:0000244|PDB:4N0N}.
HELIX 2534 2544 {ECO:0000244|PDB:4N0N}.
STRAND 2549 2552 {ECO:0000244|PDB:4N0N}.
HELIX 2556 2568 {ECO:0000244|PDB:4N0N}.
STRAND 2591 2596 {ECO:0000244|PDB:4N0N}.
STRAND 2605 2609 {ECO:0000244|PDB:4N0N}.
TURN 2610 2614 {ECO:0000244|PDB:4N0N}.
HELIX 2617 2626 {ECO:0000244|PDB:4N0N}.
STRAND 2630 2633 {ECO:0000244|PDB:4N0N}.
TURN 2648 2651 {ECO:0000244|PDB:4N0N}.
HELIX 2652 2654 {ECO:0000244|PDB:4N0N}.
STRAND 2655 2657 {ECO:0000244|PDB:4N0N}.
STRAND 2665 2667 {ECO:0000244|PDB:4N0O}.
HELIX 2669 2674 {ECO:0000244|PDB:4N0N}.
TURN 2675 2678 {ECO:0000244|PDB:4N0N}.
STRAND 2690 2693 {ECO:0000244|PDB:4N0N}.
STRAND 2702 2708 {ECO:0000244|PDB:4N0N}.
HELIX 2709 2711 {ECO:0000244|PDB:4N0N}.
STRAND 2717 2719 {ECO:0000244|PDB:4N0O}.
HELIX 2720 2722 {ECO:0000244|PDB:4N0N}.
STRAND 2727 2733 {ECO:0000244|PDB:4N0N}.
STRAND 2736 2738 {ECO:0000244|PDB:4N0O}.
HELIX 2742 2748 {ECO:0000244|PDB:4N0N}.
STRAND 2750 2759 {ECO:0000244|PDB:4N0N}.
HELIX 2765 2768 {ECO:0000244|PDB:4N0N}.
STRAND 2841 2843 {ECO:0000244|PDB:5HBZ}.
HELIX 2845 2851 {ECO:0000244|PDB:5HBZ}.
STRAND 2855 2858 {ECO:0000244|PDB:5HBZ}.
STRAND 2862 2864 {ECO:0000244|PDB:5HBZ}.
HELIX 2867 2870 {ECO:0000244|PDB:5HBZ}.
STRAND 2875 2879 {ECO:0000244|PDB:5HBZ}.
STRAND 2882 2890 {ECO:0000244|PDB:5HBZ}.
STRAND 2897 2899 {ECO:0000244|PDB:5HBZ}.
STRAND 2903 2905 {ECO:0000244|PDB:5HBZ}.
STRAND 2908 2910 {ECO:0000244|PDB:5HBZ}.
STRAND 2919 2927 {ECO:0000244|PDB:5HBZ}.
STRAND 2928 2930 {ECO:0000244|PDB:5HC1}.
HELIX 2941 2944 {ECO:0000244|PDB:5HBZ}.
HELIX 2952 2960 {ECO:0000244|PDB:5HBZ}.
HELIX 2962 2965 {ECO:0000244|PDB:5HBZ}.
STRAND 2968 2970 {ECO:0000244|PDB:5HBZ}.
STRAND 2973 2975 {ECO:0000244|PDB:5HBZ}.
STRAND 2992 3001 {ECO:0000244|PDB:5HBZ}.
TURN 3002 3004 {ECO:0000244|PDB:5HBZ}.
STRAND 3005 3013 {ECO:0000244|PDB:5HBZ}.
HELIX 3017 3023 {ECO:0000244|PDB:5HBZ}.
STRAND 3027 3037 {ECO:0000244|PDB:5HBZ}.
STRAND 3040 3047 {ECO:0000244|PDB:5HBZ}.
TURN 3048 3050 {ECO:0000244|PDB:5HBZ}.
STRAND 3051 3055 {ECO:0000244|PDB:5HBZ}.
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


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