RPOA_PRRSS
ID RPOA_PRRSS Reviewed; 3838 AA.
AC A0MD28; A0MD29; Q6U9W7; Q6U9W8;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 2.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Replicase polyprotein 1ab;
DE AltName: Full=ORF1ab polyprotein;
DE Contains:
DE RecName: Full=Nsp1;
DE EC=3.4.22.-;
DE Contains:
DE RecName: Full=Nsp1-alpha papain-like cysteine proteinase;
DE EC=3.4.22.-;
DE AltName: Full=PCP1-alpha;
DE Contains:
DE RecName: Full=Nsp1-beta papain-like cysteine proteinase;
DE EC=3.4.22.-;
DE AltName: Full=PCP1-beta;
DE Contains:
DE RecName: Full=Nsp2 cysteine proteinase;
DE EC=3.4.19.12;
DE EC=3.4.22.-;
DE AltName: Full=CP2;
DE Short=CP;
DE Contains:
DE RecName: Full=Non-structural protein 3;
DE Short=Nsp3;
DE Contains:
DE RecName: Full=Serine protease nsp4;
DE Short=3CLSP;
DE EC=3.4.21.-;
DE AltName: Full=3C-like serine proteinase;
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 nsp10;
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;
OS Porcine reproductive and respiratory syndrome virus (isolate Pig/United
OS States/SD 01-08/2001) (PRRSV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Arnidovirineae; Arteriviridae; unclassified Arteriviridae.
OX NCBI_TaxID=857306;
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=15019241; DOI=10.1016/j.virusres.2003.12.026;
RA Fang Y., Kim D.Y., Ropp S., Steen P., Christopher-Hennings J., Nelson E.A.,
RA Rowland R.R.;
RT "Heterogeneity in Nsp2 of European-like porcine reproductive and
RT respiratory syndrome viruses isolated in the United States.";
RL Virus Res. 100:229-235(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Infectious clone SD 01-08;
RX PubMed=16971421; DOI=10.1128/jvi.01032-06;
RA Fang Y., Rowland R.R., Roof M., Lunney J.K., Christopher-Hennings J.,
RA Nelson E.A.;
RT "A full-length cDNA infectious clone of North American type 1 porcine
RT reproductive and respiratory syndrome virus: expression of green
RT fluorescent protein in the Nsp2 region.";
RL J. Virol. 80:11447-11455(2006).
RN [3]
RP FUNCTION (NSP2 CYSTEINE PROTEINASE), AND MUTAGENESIS OF CYS-429; ASP-458;
RP SER-462; ASP-463; ASP-465 AND HIS-498.
RX PubMed=20504922; DOI=10.1128/jvi.00217-10;
RA Sun Z., Chen Z., Lawson S.R., Fang Y.;
RT "The cysteine protease domain of porcine reproductive and respiratory
RT syndrome virus nonstructural protein 2 possesses deubiquitinating and
RT interferon antagonism functions.";
RL J. Virol. 84:7832-7846(2010).
RN [4]
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 [5]
RP SUBCELLULAR LOCATION (NSP2 CYSTEINE PROTEINASE).
RX PubMed=23043113; DOI=10.1073/pnas.1211145109;
RA Fang Y., Treffers E.E., Li Y., Tas A., Sun Z., van der Meer Y., de Ru A.H.,
RA van Veelen P.A., Atkins J.F., Snijder E.J., Firth A.E.;
RT "Efficient -2 frameshifting by mammalian ribosomes to synthesize an
RT additional arterivirus protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:E2920-E2928(2012).
RN [6]
RP FUNCTION (NSP2 CYSTEINE PROTEINASE).
RX PubMed=22258253; DOI=10.1128/jvi.06466-11;
RA Sun Z., Li Y., Ransburgh R., Snijder E.J., Fang Y.;
RT "Nonstructural protein 2 of porcine reproductive and respiratory syndrome
RT virus inhibits the antiviral function of interferon-stimulated gene 15.";
RL J. Virol. 86:3839-3850(2012).
CC -!- FUNCTION: [Replicase polyprotein 1ab]: Contains the activities
CC necessary for the transcription of negative stranded RNA, leader RNA,
CC subgenomic mRNAs and progeny virion RNA as well as proteinases
CC responsible for the cleavage of the polyprotein into functional
CC products. {ECO:0000250|UniProtKB:Q04561}.
CC -!- FUNCTION: [Nsp1-alpha papain-like cysteine proteinase]: Inhibits host
CC IFN-beta production. Plays a role in the degradation of the host
CC transcriptional activator CREBBP protein. The degradation of host
CC CREBBP which is a key component of the IFN enhanceosome is likely
CC responsible for the inhibition of interferon mediated by Nsp1-alpha.
CC Participates also in the inhibition of host NF-kappa-B activation by
CC counteracting LUBAC-dependent induction of NF-kappa-B. Reduces host
CC NEMO ubiquitination by blocking the interaction between the two LUBAC
CC complex components RNF31 and SHARPIN. {ECO:0000250|UniProtKB:Q04561}.
CC -!- FUNCTION: [Nsp1-beta papain-like cysteine proteinase]: Plays a role in
CC blocking host mRNA nuclear export to the cytoplasm and subversion of
CC host protein synthesis. Additionally, inhibits the interferon-activated
CC JAK/STAT signal transduction by mediating the ubiquitination and
CC subsequent proteasomal degradation of host KPNA1.
CC {ECO:0000250|UniProtKB:Q04561}.
CC -!- FUNCTION: [Nsp2 cysteine proteinase]: Multifunctional protein that acts
CC as a viral protease and as a viral antagonist of host immune response.
CC Cleaves the nsp2/nsp3 site in the viral polyprotein. Displays
CC deubiquitinating activity that cleaves both ubiquitinated and ISGylated
CC products and therefore inhibits ubiquitin and ISG15-dependent host
CC innate immunity. Deubiquitinates also host NFKBIA, thereby interfering
CC with NFKBIA degradation and impairing subsequent NF-kappa-B activation.
CC {ECO:0000269|PubMed:20504922, ECO:0000269|PubMed:22258253}.
CC -!- FUNCTION: [Non-structural protein 3]: Plays a role in the inhibition of
CC the immune response by interacting with host IFITM1. This interaction
CC leads to the proteasomal degradation of the IFN-induced antiviral
CC protein IFITM1. {ECO:0000250|UniProtKB:Q04561}.
CC -!- FUNCTION: [Serine protease nsp4]: Cleaves the majority of cleavage
CC sites present in the C-terminus of the polyprotein. Triggers host
CC apoptosis through caspase-3, -8, and -9 activations. Subverts host
CC innate immune responses through its protease activity. Targets the NF-
CC kappa-B essential modulator NEMO and mediates its cleavage. Blocks host
CC interferon beta induction and downstream signaling by cleaving
CC mitochondrial MAVS, dislodging it from the mitochondria. Impairs host
CC defense by cleaving host mRNA-decapping enzyme DCP1A to attenuate its
CC antiviral activity. {ECO:0000250|UniProtKB:Q04561}.
CC -!- FUNCTION: [Non-structural protein 5-6-7]: Plays a role in the initial
CC induction of autophagosomes from host reticulum endoplasmic.
CC {ECO:0000250|UniProtKB:Q04561}.
CC -!- FUNCTION: [Non-structural protein 5]: Plays a role in the inhibition of
CC host STAT3 signaling pathway by inducing the degradation of STAT3.
CC {ECO:0000250|UniProtKB:Q04561}.
CC -!- FUNCTION: [RNA-directed RNA polymerase]: Responsible for replication
CC and transcription of the viral RNA genome.
CC {ECO:0000250|UniProtKB:Q04561}.
CC -!- FUNCTION: [Helicase nsp10]: Displays RNA and DNA duplex-unwinding
CC activities with 5' to 3' polarity. {ECO:0000250|UniProtKB:Q04561}.
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:0000250|UniProtKB:Q04561};
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:0000250|UniProtKB:Q04561};
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:0000250|UniProtKB:Q04561};
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; Evidence={ECO:0000250|UniProtKB:Q04561};
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 -!- SUBUNIT: Nsp1-alpha papain-like: Interacts with host RNF31.
CC {ECO:0000250|UniProtKB:Q04561}.
CC -!- SUBUNIT: [Nsp2 cysteine proteinase]: Interacts with host DDX18; this
CC interaction redistributes host DDX18 to the cytoplasm.
CC {ECO:0000250|UniProtKB:Q04561}.
CC -!- SUBUNIT: [Non-structural protein 3]: Interacts with host IFITM1.
CC {ECO:0000250|UniProtKB:Q04561}.
CC -!- SUBUNIT: [RNA-directed RNA polymerase]: Interacts with host DDX5.
CC {ECO:0000250|UniProtKB:Q04561}.
CC -!- SUBUNIT: [Helicase nsp10]: Interacts with host DDX18; this interaction
CC redistributes host DDX18 to the cytoplasm.
CC {ECO:0000250|UniProtKB:Q04561}.
CC -!- SUBUNIT: [Uridylate-specific endoribonuclease nsp11]: Interacts with
CC host OTULIN. {ECO:0000250|UniProtKB:Q04561}.
CC -!- SUBUNIT: [Non-structural protein 12]: Interacts with host LGALS3.
CC {ECO:0000250|UniProtKB:Q04561}.
CC -!- SUBCELLULAR LOCATION: [Nsp1]: Host nucleus
CC {ECO:0000250|UniProtKB:Q04561}. Host cytoplasm
CC {ECO:0000250|UniProtKB:Q04561}.
CC -!- SUBCELLULAR LOCATION: [Nsp1-alpha papain-like cysteine proteinase]:
CC Host nucleus {ECO:0000250|UniProtKB:Q04561}. Host cytoplasm
CC {ECO:0000250|UniProtKB:Q04561}.
CC -!- SUBCELLULAR LOCATION: [Nsp1-beta papain-like cysteine proteinase]: Host
CC nucleus {ECO:0000250|UniProtKB:Q04561}.
CC -!- SUBCELLULAR LOCATION: [Nsp2 cysteine proteinase]: Host cytoplasm
CC {ECO:0000269|PubMed:23043113}. Host membrane
CC {ECO:0000250|UniProtKB:Q04561}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q04561}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 3]: Host membrane
CC {ECO:0000250|UniProtKB:Q04561}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q04561}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 5-6-7]: Host endoplasmic
CC reticulum {ECO:0000250|UniProtKB:Q04561}. Host membrane
CC {ECO:0000250|UniProtKB:Q04561}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q04561}.
CC -!- SUBCELLULAR LOCATION: [Serine protease nsp4]: Host cytoplasm
CC {ECO:0000250|UniProtKB:Q04561}.
CC -!- SUBCELLULAR LOCATION: [RNA-directed RNA polymerase]: Host cytoplasm
CC {ECO:0000250|UniProtKB:Q04561}. Host cytoplasm, host perinuclear region
CC {ECO:0000250|UniProtKB:Q04561}.
CC -!- SUBCELLULAR LOCATION: [Helicase nsp10]: Host cytoplasm
CC {ECO:0000250|UniProtKB:Q04561}. Host cytoplasm, host perinuclear region
CC {ECO:0000250|UniProtKB:Q04561}.
CC -!- SUBCELLULAR LOCATION: [Uridylate-specific endoribonuclease nsp11]: Host
CC cytoplasm {ECO:0000250|UniProtKB:Q04561}. Host nucleus
CC {ECO:0000250|UniProtKB:Q04561}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 12]: Host cytoplasm
CC {ECO:0000250|UniProtKB:Q04561}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=3;
CC Name=Replicase polyprotein 1ab; Synonyms=pp1ab;
CC IsoId=A0MD28-1; Sequence=Displayed;
CC Name=Replicase polyprotein 1a; Synonyms=pp1a, ORF1a polyprotein;
CC IsoId=A0MD28-2; Sequence=VSP_039634;
CC Name=Truncated polyprotein 1aTF;
CC IsoId=P0DJY0-1; Sequence=External;
CC -!- DOMAIN: The hydrophobic domains (HD) could mediate the membrane
CC association of the replication complex and thereby alter the
CC architecture of the host cell membrane. {ECO:0000250}.
CC -!- DOMAIN: The OTU-like region is responsible for the deubiquitinating and
CC deISGylation activities of Nsp2. {ECO:0000250}.
CC -!- PTM: Specific enzymatic cleavages in vivo by its own proteases yield
CC mature proteins. Nsp1 is autocleaved into two subunits, Nsp1-alpha and
CC Nsp1-beta. There are two alternative pathways for processing. Either
CC nsp4-5 is cleaved, which represents the major pathway or the nsp5-6 and
CC nsp6-7 are processed, which represents the minor pathway. The major
CC pathway occurs when nsp2 acts as cofactor for nsp4. {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=AAR37017.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY375474; AAR37016.1; -; Genomic_RNA.
DR EMBL; AY375474; AAR37017.1; ALT_INIT; Genomic_RNA.
DR EMBL; DQ489311; ABF66340.1; -; Genomic_RNA.
DR EMBL; DQ489311; ABF66341.1; -; Genomic_RNA.
DR SMR; A0MD28; -.
DR MEROPS; S32.002; -.
DR Proteomes; UP000000937; Genome.
DR GO; GO:0044165; C:host cell endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0044220; C:host cell perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0039648; P:modulation by virus of host protein ubiquitination; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0039579; P:suppression by virus of host ISG15-protein conjugation; IEA:UniProtKB-KW.
DR GO; GO:0039563; P:suppression by virus of host JAK-STAT cascade via inhibition of STAT1 activity; IEA:UniProtKB-KW.
DR GO; GO:0039644; P:suppression by virus of host NF-kappaB cascade; IEA:UniProtKB-KW.
DR GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0019082; P:viral protein processing; IEA:InterPro.
DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR GO; GO:0075523; P:viral translational frameshifting; IDA:UniProtKB.
DR CDD; cd21410; 1B_av_Nsp10-like; 1.
DR CDD; cd21160; NendoU_av_Nsp11-like; 1.
DR CDD; cd21166; NTD_av_Nsp11-like; 1.
DR CDD; cd21405; ZBD_av_Nsp10-like; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR Gene3D; 3.30.1330.220; -; 1.
DR Gene3D; 3.30.40.20; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR Gene3D; 3.90.70.60; -; 1.
DR Gene3D; 3.90.70.70; -; 1.
DR InterPro; IPR027351; (+)RNA_virus_helicase_core_dom.
DR InterPro; IPR031932; Arteri_nsp7a.
DR InterPro; IPR038451; Arteri_nsp7a_sf.
DR InterPro; IPR008743; Arterivirus_Nsp2_C33.
DR InterPro; IPR023338; Arterivirus_NSP4_peptidase.
DR InterPro; IPR008741; AV_PCPalpha.
DR InterPro; IPR038155; AV_PCPalpha_sf.
DR InterPro; IPR025773; AV_PCPbeta.
DR InterPro; IPR038154; AV_PCPbeta_sf.
DR InterPro; IPR023183; Chymotrypsin-like_C.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR008760; EAV_peptidase_S32.
DR InterPro; IPR037227; EndoU-like.
DR InterPro; IPR044863; NIRAN.
DR InterPro; IPR044348; NSP10_1B_Av.
DR InterPro; IPR027355; NSP10_Av_ZBD.
DR InterPro; IPR044320; NSP11_Av_N.
DR InterPro; IPR044314; NSP11_NendoU_Av.
DR InterPro; IPR032855; NSP2-B_epitope.
DR InterPro; IPR032841; NSP2_assoc.
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; PF14757; NSP2-B_epitope; 1.
DR Pfam; PF14758; NSP2_assoc; 1.
DR Pfam; PF05410; Peptidase_C31; 1.
DR Pfam; PF05411; Peptidase_C32; 1.
DR Pfam; PF05412; Peptidase_C33; 1.
DR Pfam; PF05579; Peptidase_S32; 1.
DR Pfam; PF00680; RdRP_1; 1.
DR Pfam; PF01443; Viral_helicase1; 1.
DR SUPFAM; SSF142877; SSF142877; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS51538; AV_CP; 1.
DR PROSITE; PS51961; AV_NSP11N_COV_NSP15M; 1.
DR PROSITE; PS51493; AV_NSP4_PRO; 1.
DR PROSITE; PS51539; AV_PCP_ALPHA; 1.
DR PROSITE; PS51540; AV_PCP_BETA; 1.
DR PROSITE; PS51652; AV_ZBD; 1.
DR PROSITE; PS51958; NENDOU; 1.
DR PROSITE; PS51947; NIRAN; 1.
DR PROSITE; PS51657; PSRV_HELICASE; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Endonuclease; Helicase; Host cytoplasm;
KW Host endoplasmic reticulum; Host membrane; Host nucleus;
KW Host-virus interaction; Hydrolase;
KW Inhibition of host innate immune response by virus;
KW Inhibition of host interferon signaling pathway by virus;
KW Inhibition of host ISG15 by virus; Inhibition of host NF-kappa-B by virus;
KW Inhibition of host STAT1 by virus; Lyase; Membrane; Metal-binding;
KW Modulation of host ubiquitin pathway by viral deubiquitinase;
KW Modulation of host ubiquitin pathway by virus; Multifunctional enzyme;
KW Nuclease; Nucleotide-binding; Nucleotidyltransferase; Protease;
KW Ribosomal frameshifting; RNA-directed RNA polymerase; Serine protease;
KW Thiol protease; Transferase; Transmembrane; Transmembrane helix;
KW Viral immunoevasion; Viral RNA replication; Zinc; Zinc-finger.
FT CHAIN 1..3838
FT /note="Replicase polyprotein 1ab"
FT /evidence="ECO:0000250"
FT /id="PRO_0000397084"
FT CHAIN 1..385
FT /note="Nsp1"
FT /id="PRO_0000410830"
FT CHAIN 1..180
FT /note="Nsp1-alpha papain-like cysteine proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000397085"
FT CHAIN 181..385
FT /note="Nsp1-beta papain-like cysteine proteinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000397086"
FT CHAIN 386..1446
FT /note="Nsp2 cysteine proteinase"
FT /id="PRO_0000397087"
FT CHAIN 1447..1676
FT /note="Non-structural protein 3"
FT /id="PRO_0000397088"
FT CHAIN 1677..1879
FT /note="Serine protease nsp4"
FT /id="PRO_0000397089"
FT CHAIN 1880..2334
FT /note="Non-structural protein 5-6-7"
FT /evidence="ECO:0000250"
FT /id="PRO_0000397090"
FT CHAIN 1880..2049
FT /note="Non-structural protein 5"
FT /id="PRO_0000423134"
FT CHAIN 2050..2065
FT /note="Non-structural protein 6"
FT /id="PRO_0000423135"
FT CHAIN 2066..2214
FT /note="Non-structural protein 7-alpha"
FT /id="PRO_0000423136"
FT CHAIN 2215..2334
FT /note="Non-structural protein 7-beta"
FT /id="PRO_0000423137"
FT CHAIN 2335..3020
FT /note="RNA-directed RNA polymerase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000397091"
FT CHAIN 2335..2379
FT /note="Non-structural protein 8"
FT /evidence="ECO:0000250"
FT /id="PRO_0000397092"
FT CHAIN 3021..3462
FT /note="Helicase nsp10"
FT /evidence="ECO:0000250"
FT /id="PRO_0000397093"
FT CHAIN 3463..3686
FT /note="Uridylate-specific endoribonuclease nsp11"
FT /evidence="ECO:0000250"
FT /id="PRO_0000397094"
FT CHAIN 3687..3838
FT /note="Non-structural protein 12"
FT /evidence="ECO:0000250"
FT /id="PRO_0000397095"
FT TRANSMEM 1094..1114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1117..1137
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1162..1182
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1211..1231
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1235..1255
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1450..1470
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1526..1546
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1556..1576
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1592..1612
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1875..1895
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1916..1936
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1960..1980
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2003..2023
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2029..2048
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 69..180
FT /note="Peptidase C31"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00872"
FT DOMAIN 269..385
FT /note="Peptidase C32"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00873"
FT DOMAIN 420..527
FT /note="Peptidase C33"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00871"
FT DOMAIN 1677..1879
FT /note="Peptidase S32"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00826"
FT DOMAIN 2364..2527
FT /note="NiRAN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01292"
FT DOMAIN 2765..2899
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT DOMAIN 3021..3084
FT /note="AV ZBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985"
FT DOMAIN 3134..3293
FT /note="(+)RNA virus helicase ATP-binding"
FT DOMAIN 3294..3423
FT /note="(+)RNA virus helicase C-terminal"
FT DOMAIN 3462..3559
FT /note="AV-Nsp11N/CoV-Nsp15M"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01306"
FT DOMAIN 3561..3683
FT /note="NendoU"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT ZN_FING 8..28
FT /note="C4-type; atypical"
FT REGION 69..182
FT /note="PCP1-alpha"
FT /evidence="ECO:0000250"
FT REGION 269..384
FT /note="PCP1-beta"
FT /evidence="ECO:0000250"
FT REGION 418..505
FT /note="OTU-like"
FT REGION 728..758
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1027..1064
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1132..1255
FT /note="HD1"
FT /evidence="ECO:0000250"
FT REGION 1310..1334
FT /note="WCCH"
FT /evidence="ECO:0000250"
FT REGION 1451..1612
FT /note="HD2"
FT /evidence="ECO:0000250"
FT REGION 1902..2023
FT /note="HD3"
FT /evidence="ECO:0000250"
FT COMPBIAS 740..754
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1044..1064
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 76
FT /note="For Nsp1-alpha papain-like cysteine proteinase
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00872"
FT ACT_SITE 146
FT /note="For Nsp1-alpha papain-like cysteine proteinase
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00872"
FT ACT_SITE 276
FT /note="For Nsp1-beta papain-like cysteine proteinase
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00873"
FT ACT_SITE 345
FT /note="For Nsp1-beta papain-like cysteine proteinase
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00873"
FT ACT_SITE 429
FT /note="For Nsp2 cysteine proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00871"
FT ACT_SITE 498
FT /note="For Nsp2 cysteine proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00871"
FT ACT_SITE 1715
FT /note="Charge relay system; for 3C-like serine proteinase
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00826"
FT ACT_SITE 1740
FT /note="Charge relay system; for 3C-like serine proteinase
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00826"
FT ACT_SITE 1793
FT /note="Charge relay system; for 3C-like serine proteinase
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00826"
FT ACT_SITE 3592
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT ACT_SITE 3607
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT ACT_SITE 3636
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT BINDING 3027
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985"
FT BINDING 3030
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985"
FT BINDING 3040
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985"
FT BINDING 3045
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985"
FT BINDING 3048
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985"
FT BINDING 3050
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985"
FT BINDING 3052
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985"
FT BINDING 3054
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985"
FT BINDING 3061
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985"
FT BINDING 3063
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985"
FT BINDING 3070
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985"
FT BINDING 3073
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985"
FT BINDING 3168..3175
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT SITE 180..181
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000255"
FT SITE 385..386
FT /note="Cleavage; by autolysis"
FT SITE 1446..1447
FT /note="Cleavage; by CP2"
FT /evidence="ECO:0000255"
FT SITE 1676..1677
FT /note="Cleavage; by 3CLSP"
FT SITE 1879..1880
FT /note="Cleavage; by 3CLSP"
FT SITE 2049..2050
FT /note="Cleavage; by 3CLSP"
FT SITE 2065..2066
FT /note="Cleavage; by 3CLSP"
FT SITE 2214..2215
FT /note="Cleavage; by 3CLSP"
FT SITE 2334..2335
FT /note="Cleavage; by 3CLSP"
FT SITE 3020..3021
FT /note="Cleavage; by 3CLSP"
FT SITE 3071
FT /note="Involved in mRNA transcription process"
FT /evidence="ECO:0000250"
FT SITE 3462..3463
FT /note="Cleavage; by 3CLSP"
FT /evidence="ECO:0000250"
FT SITE 3686..3687
FT /note="Cleavage; by 3CLSP"
FT /evidence="ECO:0000250"
FT VAR_SEQ 2380..3838
FT /note="Missing (in isoform Replicase polyprotein 1a)"
FT /evidence="ECO:0000305"
FT /id="VSP_039634"
FT VARIANT 666
FT /note="R -> Q (in strain: Infectious clone SD 01-08)"
FT VARIANT 1005
FT /note="R -> K (in strain: Infectious clone SD 01-08)"
FT VARIANT 1012
FT /note="N -> S (in strain: Infectious clone SD 01-08)"
FT VARIANT 3092
FT /note="P -> L (in strain: Infectious clone SD 01-08)"
FT VARIANT 3682
FT /note="Y -> H (in strain: Infectious clone SD 01-08)"
FT MUTAGEN 429
FT /note="C->A: Lethal."
FT /evidence="ECO:0000269|PubMed:20504922"
FT MUTAGEN 458
FT /note="D->A: Slight reduction in the ability of Nsp2 to
FT impair NF-kappaB activation."
FT /evidence="ECO:0000269|PubMed:20504922"
FT MUTAGEN 462
FT /note="S->A: Reduction in the ability of Nsp2 to impair NF-
FT kappaB activation."
FT /evidence="ECO:0000269|PubMed:20504922"
FT MUTAGEN 463
FT /note="D->A: Lethal."
FT /evidence="ECO:0000269|PubMed:20504922"
FT MUTAGEN 465
FT /note="D->A: Reduction in the ability of Nsp2 to impair NF-
FT kappaB activation."
FT /evidence="ECO:0000269|PubMed:20504922"
FT MUTAGEN 498
FT /note="H->A: Lethal."
FT /evidence="ECO:0000269|PubMed:20504922"
SQ SEQUENCE 3838 AA; 418948 MW; 07ADB34E6578FFC9 CRC64;
MSGTFSRCMC TPAARVFWNA GQVFCTRCLS ARPLLSPELQ DTDLGVVGLF YKPKDKIHWK
VPIGIPQVEC TPSGCCWLSA VFPLARMTSG NHNFLQRLVK VADVLYRDGC LAPRHLRELQ
VYERGCSWYP ITGPVPGMGL FANSMHVSDQ PFPGATHVLT NSPLPQRACR QPFCPFEEAH
SDVYRWKKFV IFTDSSPNGR FRMMWTPESD DSAALEVLPP ELERQVEILT RSFPAHHPIN
LADWELTESP ENGFSFGTSH SCGHIVQNPN VFDGKCWLTC FLGQSAEVCY HEEHLANALG
YQTKWGVHGK YLQRRLQVRG MRAVVDPDGP IHVEALSCSQ SWVRHLTLNN DVTPGFVRLT
SIRIVSNTEP TAFRIFRFGA HKWYGAAGKR ARAKRATKSG KDSALAPKIA PPVPTCGITT
YSPPTDGSCG WHVLAAIVNR MINGDFTSPL PQYNRPEDDW ASDYDLAQAI QCLQLPATVV
RNRACPNAKY LIKLNGVHWE VEVRSGMAPR SLSRECVVGV CSEGCVAPPY PADGLPKRAL
EALASAYRLP SDCVSSGIAD FLADPPPQEF WTLDKMLTSP SPERSGFSSL YKLLLEVVPQ
KCGATEGAFV YAVERMLKDC PSPEQAMALL AKIKVPSSKA PSVSLDECFP AGVPADFEPA
FQERPRSPGA AVALCSPDAK GFEGTASEEA QESGHKAVHA VPLAEGPNNE QVQVVAGEQL
ELGGCGLAIG SAQSSSDSKR ENMHNSREDE PLDLSHPAPA ATTTLVGEQT PDNPGSDASA
LPIAVRGFVP TGPILRHVEH CGTESGDSSS PLDLSFAQTL DQPLDLSLAA WPVKATASDP
GWVRGRCEPV FLKPRKAFSD GDSALQFGEL SESSSVIEFD QTKDTLVADA PVDLTTSNEA
LSAVDPSEFV ELRRPRHSAQ ALIDRGGPLA DVHAKIKNRV YEQCLQACEP GSRATPATRE
WLDKMWDRVD MKTWRCTSQF QAGRILASLK FLPDMIQDTP PPVPRKNRAS DNAGLKQLVA
RWDKKLSVTP PPKSAGLVLD QTVPPPTDIQ QEDATPSDGL SHASDFSSRV STSWSWKGLM
LSGTRLAGSA GQRLMTWVFE VYSHLPAFIL TLFSPRGSMA PGDWLFAGVV LLALLLCRSY
PILGCLPLLG VFSGSLRRVR LGVFGSWMAF AVFLFSTPSN PVGSSCDHDS PECHAELLAL
EQRQLWEPVR GLVVGPSGLL CVILGKLLGG SRHLWHVILR LCMLTDLALS LVYVVSQGRC
HKCWGKCIRT APAEVALNVF PFSRATRNSL TSLCDRFQTP KGVDPVHLAT GWRGCWRGES
PIHQPHQKPI AYANLDEKKI SAQTVVAVPY DPSQAIKCLK VLQAGGAIVD QPTPEVVRVS
EIPFSAPFFP KVPVNPDCRI VVDSDTFVAA VRCGYSTAQL VLGRGNFAKL NQTPLRDSAS
TKTTGGASYT LAVAQVSVWT LVHFILGLWF TSPQVCGRGT ADPWCSNPFS YPAYGPGVVC
SSRLCVSADG VTLPLFSAVA QLSGREVGIF ILVLVSLTAL AHRLALKADM LVVFSAFCAY
AWPMSSWLIC FFPILLKWVT LHPLTMLWVH SFLVFCMPAA GILSLGITGL LWAVGRFTQV
AGIITPYDIH QYTSGPRGAA AVATAPEGTY MAAVRRAALT GRTLIFTPSA VGSLLEGAFR
THKPCLNTVN VVGSSLGSGG VFTIDGRKTV VTAAHVLNGD TARVTGDSYN RMHTFKTSGD
YAWSHADDWQ GVAPVVKVAK GYRGRAYWQT STGVEPGVIG EGFAFCFTNC GDSGSPVISE
SGDLIGIHTG SNKLGSGLVT TPEGETCAIK ETKLSDLSRH FAGPSVPLGD IKLSPAIVPD
VTSIPSDLAS LLASVPVMEG GLSTVQLLCV FFLLWRMMGH AWTPIVAVGF FLLNEILPAV
LVRAVFSFAL FILAWATPWS AQVLMIRLLT ASLNRNKLSL AFYALGGVVG LAAEIGAFAG
RLPELSQALS TYCFLPRVLA MASYVPIIII GGLHALGVIL WLFKYRCLHN MLVGDGSFSS
AFFLRYFAEG NLRKGVSQSC GMSNESLTAA LACKLSQADL DFLSSLTNFK CFVSASNMKN
AAGQYIEAAY AKALRQELAS LVQVDKMKGI LSKLEAFAET ATPSLDAGDV VVLLGQHPHG
SILDINVGTE RKTVSVQETR SLGGSKFSVC TVVSNTPVDA LTGIPLQTPT PLFENGPRHR
GEEDDLRVER MKKHCVSLGF HNINGKVYCK IWDKSTGDTF YTDDSRYTQD LAFQDRSADY
RDRDYEGVQT APQQGFDPKS ETPIGTVVIG GITYNRYLIK GKEVLVPKPD NCLEAAKLSL
EQALAGMGQT CDLTAAEVEK LRRIISQLQG LTTEQALNCL LAASGLTRCG RGGLVVTETA
VKIVKYHSRT FTLGPLDLKV TSEAEVKKST EQGHAVVANL CSGVILMRPH PPSLVDVLLK
PGLDTKPGIQ PGHGAGNMGV DGSTWDFETA PTKAELELSK QIIQACEVRR GDAPNLQLPY
KLYPVRGDPE RHGGRLINTR FGDLSYKTPQ DTKSAIHAAC CLHPNGAPVS DGKSTLGTTL
QHGFELYVPT VPYSVMEYLD SRPDTPFMCT KHGTSKAAAE DLQKYDLSTQ GFVLPGVLRL
VRRFIFGHIG KAPPLFLPST YPAKNSMAGI NGQRFPTKDV QSIPEIDEMC ARAVKENWQT
VTPCTLKKQY CSKPKTRTIL GTNNFIALAH RSALSGVTQA FMKKAWKSPI ALGKNKFKEL
HCTVAGRCLE ADLASCDRST PAIVRWFVAN LLYELAGCEE YLPSYVLNCC HDLVATQDGA
FTKRGGLSSG DPVTSVSNTV YSLIIYAQHM VLSALKMGHE IGLKFLEEQL KFEDLLEIQP
MLVYSDDLVL YAERPTFPNY HWWVEHLDLM LGFRTDPKKT VITDKPSFLG CRIEAGRQLV
PNRDRILAAL AYHMKAQNAS EYYASAAAIL MDSCACIDHD PEWYEDLICG IARCARQDGY
SFPGPAFFMS MWEKLRSHNE GKKFRHCGIC DAKADHASAC GLDLCLFHSH FHQHCPVTLS
CGHHAGSREC SQCQSPVGAG RSPLDAVLKQ IPYKPPRTVI MKVGNKTTAL DPGRYQSRRG
LVAVKRGIAG NEVDLPDGDY QVVPLLPTCK DINMVKVACN VLLSKFIVGP PGSGKTTWLL
SQVQDDDVIY TPTHQTMFDI VSALKVCRYS IPGASGLPFP PPARSGPWVR LVASGHVPGR
TSYLDEAGYC NHLDILRLLS KTPLVCLGDL QQLHPVGFDS YCYVFDQMPQ KQLTTIYRFG
PNICAAIQPC YREKLESKAR NTRVVFTTWP VAFGQVLTPY HKDRIGSAIT IDSSQGATFD
IVTLHLPSPK SLNKSRALVA ITRARHGLFI YDPHNQLQEF FNLIPERTDC NLVFSRGDDL
VVLSADNAVT TVAKALGTGP SRFRVSDPRC KSLLAACSAS LEGSCMPLPQ VAHNLGFYFS
PDSPAFAPLP KELAPHWPVV THQNNRAWPD RLVASMRPID ARYSKPMVGA GYVVGPSTFL
GTPGVVSYYL TLYIRGEPQA LPETLVSTGR IATDCREYLD AAEEEAAKEL PHAFIGDVKG
TTVGGCHHIT SKYLPRTLPK DSVAVVGVSS PGRAAKAMCT LTDVYLPELR PYLQPETASK
CWKLKLDFRD VRLMVWKGAT AYFQLEGLTW SALPDYARFI QLPKDAVVYI DPCIGPATAN
RKVVRTTDWR ADLAVTPYDY GAQNILTTAW FEDLGPQWKI LGLQPFRRAF GFENTEDWAI
LARRMSDGKD YTDYNWDCVR ERPHAIYGRA RDHTYHFAPG TELQVELGKP RLPPGREP
