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Replicase polyprotein 1TF (ORF1ab polyprotein) [Cleaved into: Nsp1 (EC 3.4.22.-); Nsp1-alpha papain-like cysteine proteinase (EC 3.4.22.-) (PCP1-alpha); Nsp1-beta papain-like cysteine proteinase (EC 3.4.22.-) (PCP1-beta); Nsp2TF]

 RPOTF_PRRSL             Reviewed;        1285 AA.
P0DJZ9;
09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
09-DEC-2015, sequence version 1.
28-MAR-2018, entry version 7.
RecName: Full=Replicase polyprotein 1TF;
AltName: Full=ORF1ab polyprotein;
Contains:
RecName: Full=Nsp1;
EC=3.4.22.-;
Contains:
RecName: Full=Nsp1-alpha papain-like cysteine proteinase;
EC=3.4.22.-;
AltName: Full=PCP1-alpha;
Contains:
RecName: Full=Nsp1-beta papain-like cysteine proteinase;
EC=3.4.22.-;
AltName: Full=PCP1-beta;
Contains:
RecName: Full=Nsp2TF;
Porcine reproductive and respiratory syndrome virus (strain Lelystad)
(PRRSV).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Nidovirales; Arteriviridae; unclassified Arteriviridae.
NCBI_TaxID=11049;
NCBI_TaxID=9823; Sus scrofa (Pig).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=8517032; DOI=10.1006/viro.1993.1008;
Meulenberg J.J.M., Hulst M.M., de Meijer E.J., Moonen P.L.J.M.,
den Besten A., de Kluyver E.P., Wensvoort G., Moormann R.J.M.;
"Lelystad virus, the causative agent of porcine epidemic abortion and
respiratory syndrome (PEARS), is related to LDV and EAV.";
Virology 192:62-72(1993).
[2]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=23043113; DOI=10.1073/pnas.1211145109;
Fang Y., Treffers E.E., Li Y., Tas A., Sun Z., van der Meer Y.,
de Ru A.H., van Veelen P.A., Atkins J.F., Snijder E.J., Firth A.E.;
"Efficient -2 frameshifting by mammalian ribosomes to synthesize an
additional arterivirus protein.";
Proc. Natl. Acad. Sci. U.S.A. 109:E2920-E2928(2012).
[3]
FUNCTION (NSP1-ALPHA PAPAIN-LIKE CYSTEINE PROTEINASE), AND SUBCELLULAR
LOCATION (NSP1-ALPHA PAPAIN-LIKE CYSTEINE PROTEINASE).
STRAIN=PA8;
PubMed=23287061; DOI=10.1016/j.virusres.2012.12.012;
Han M., Du Y., Song C., Yoo D.;
"Degradation of CREB-binding protein and modulation of type I
interferon induction by the zinc finger motif of the porcine
reproductive and respiratory syndrome virus nsp1alpha subunit.";
Virus Res. 172:54-65(2013).
-!- FUNCTION: Nsp1-alpha papain-like cysteine proteinase: Inhibits
host IFN-beta production. Plays a role in the degradation of the
host transcriptional activator CREBBP protein. The degradation of
host CREBBP which is a key component of the IFN enhanceosome is
likely responsible for the inhibition of interferon mediated by
Nsp1-alpha. Participates also in the inhibition of host NF-kappa-B
activation. {ECO:0000250|UniProtKB:Q9WJB2,
ECO:0000269|PubMed:23287061}.
-!- FUNCTION: Nsp1-beta papain-like cysteine proteinase: Plays a role
in the inhibition of the interferon-activated JAK/STAT signal
transduction by mediating the ubiquitination and subsequent
proteasomal degradation of host KPNA1.
{ECO:0000250|UniProtKB:Q9WJB2}.
-!- FUNCTION: Nsp2TF: Plays a role in viral replication.
{ECO:0000269|PubMed:23043113}.
-!- SUBCELLULAR LOCATION: Nsp1: Host nucleus
{ECO:0000269|PubMed:23287061}. Host cytoplasm
{ECO:0000269|PubMed:23287061}.
-!- SUBCELLULAR LOCATION: Nsp1-alpha papain-like cysteine proteinase:
Host nucleus {ECO:0000269|PubMed:23287061}. Host cytoplasm
{ECO:0000269|PubMed:23287061}.
-!- SUBCELLULAR LOCATION: Nsp1-beta papain-like cysteine proteinase:
Host nucleus {ECO:0000269|PubMed:23287061}.
-!- SUBCELLULAR LOCATION: Nsp2TF: Host cytoplasm
{ECO:0000269|PubMed:23043113}. Host membrane {ECO:0000255}; Multi-
pass membrane protein {ECO:0000255}. Note=Nsp2 and nsp2TF localize
to different intracellular compartments.
-!- ALTERNATIVE PRODUCTS:
Event=Ribosomal frameshifting; Named isoforms=3;
Name=Replicase polyprotein 1TF;
IsoId=P0DJZ9-1; Sequence=Displayed;
Note=Produced by a -2 ribosomal frameshift.;
Name=Replicase polyprotein 1ab; Synonyms=pp1ab;
IsoId=Q04561-1; Sequence=External;
Note=Produced by -1 ribosomal frameshifting at the 1a-1b genes
boundary.;
Name=Replicase polyprotein 1a; Synonyms=pp1a, ORF1a polyprotein;
IsoId=Q04561-2; Sequence=External;
Note=Produced by conventional translation.;
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EMBL; M96262; -; NOT_ANNOTATED_CDS; Genomic_RNA.
SMR; P0DJZ9; -.
OrthoDB; VOG09000000; -.
Proteomes; UP000006687; Genome.
GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0019082; P:viral protein processing; IEA:InterPro.
Gene3D; 3.90.70.60; -; 1.
Gene3D; 3.90.70.70; -; 1.
InterPro; IPR008743; Arterivirus_Nsp2_C33.
InterPro; IPR008741; AV_PCPalpha.
InterPro; IPR038155; AV_PCPalpha_sf.
InterPro; IPR025773; AV_PCPbeta.
InterPro; IPR038154; AV_PCPbeta_sf.
InterPro; IPR032855; NSP2-B_epitope.
InterPro; IPR032841; NSP2_assoc.
Pfam; PF14757; NSP2-B_epitope; 1.
Pfam; PF14758; NSP2_assoc; 1.
Pfam; PF05410; Peptidase_C31; 1.
Pfam; PF05411; Peptidase_C32; 1.
Pfam; PF05412; Peptidase_C33; 1.
PROSITE; PS51538; AV_CP; 1.
PROSITE; PS51539; AV_PCP_ALPHA; 1.
PROSITE; PS51540; AV_PCP_BETA; 1.
3: Inferred from homology;
Complete proteome; Host cytoplasm; Host membrane; Host nucleus;
Hydrolase; Membrane; Metal-binding; Protease; Reference proteome;
Ribosomal frameshifting; Thiol protease; Transmembrane;
Transmembrane helix; Zinc; Zinc-finger.
CHAIN 1 1285 Replicase polyprotein 1TF.
/FTId=PRO_0000434874.
CHAIN 1 384 Nsp1. {ECO:0000250}.
/FTId=PRO_0000434875.
CHAIN 1 180 Nsp1-alpha papain-like cysteine
proteinase. {ECO:0000255}.
/FTId=PRO_0000434876.
CHAIN 181 385 Nsp1-beta papain-like cysteine
proteinase. {ECO:0000255}.
/FTId=PRO_0000434877.
CHAIN 386 1285 Nsp2TF.
/FTId=PRO_0000434878.
TRANSMEM 1136 1156 Helical. {ECO:0000255}.
TRANSMEM 1170 1190 Helical. {ECO:0000255}.
TRANSMEM 1211 1231 Helical. {ECO:0000255}.
TRANSMEM 1250 1270 Helical. {ECO:0000255}.
DOMAIN 69 180 Peptidase C31. {ECO:0000255|PROSITE-
ProRule:PRU00872}.
DOMAIN 269 385 Peptidase C32. {ECO:0000255|PROSITE-
ProRule:PRU00873}.
ZN_FING 8 28 C4-type; atypical.
{ECO:0000250|UniProtKB:Q04561}.
REGION 69 182 PCP1-alpha.
{ECO:0000250|UniProtKB:Q04561}.
REGION 269 384 PCP1-beta.
{ECO:0000250|UniProtKB:Q04561}.
ACT_SITE 76 76 For Nsp1-alpha papain-like cysteine
proteinase activity.
{ECO:0000250|UniProtKB:Q04561,
ECO:0000255|PROSITE-ProRule:PRU00872}.
ACT_SITE 146 146 For Nsp1-alpha papain-like cysteine
proteinase activity.
{ECO:0000250|UniProtKB:Q04561,
ECO:0000255|PROSITE-ProRule:PRU00872}.
ACT_SITE 276 276 For Nsp1-beta papain-like cysteine
proteinase activity.
{ECO:0000250|UniProtKB:Q04561,
ECO:0000255|PROSITE-ProRule:PRU00873}.
ACT_SITE 345 345 For Nsp1-beta papain-like cysteine
proteinase activity.
{ECO:0000250|UniProtKB:Q04561,
ECO:0000255|PROSITE-ProRule:PRU00873}.
SITE 180 181 Cleavage; by autolysis. {ECO:0000255}.
SITE 385 386 Cleavage; by autolysis. {ECO:0000250}.
SEQUENCE 1285 AA; 141133 MW; 548F4A21A77E6BE1 CRC64;
MSGTFSRCMC TPAARVFWNA GQVFCTRCLS ARSLLSPELQ DTDLGAVGLF YKPRDKLHWK
VPIGIPQVEC TPSGCCWLSA VFPLARMTSG NHNFLQRLVK VADVLYRDGC LAPRHLRELQ
VYERGCNWYP ITGPVPGMGL FANSMHVSDQ PFPGATHVLT NSPLPQQACR QPFCPFEEAH
SSVYRWKKFV VFTDSSLNGR SRMMWTPESD DSAALEVLPP ELERQVEILI RSFPAHHPVD
LADWELTESP ENGFSFNTSH SCGHLVQNPD VFDGKCWLSC FLGQSVEVRC HEEHLADAFG
YQTKWGVHGK YLQRRLQVRG IRAVVDPDGP IHVEALSCPQ SWIRHLTLDD DVTPGFVRLT
SLRIVPNTEP TTSRIFRFGA HKWYGAAGKR ARAKRAAKSE KDSAPTPKVA LPVPTCGITT
YSPPTDGSCG WHVLAAIMNR MINGDFTSPL TQYNRPEDDW ASDYDLVQAI QCLRLPATVV
RNRACPNAKY LIKLNGVHWE VEVRSGMAPR SLSRECVVGV CSEGCVAPPY PADGLPKRAL
EALASAYRLP SDCVSSGIAD FLANPPPQEF WTLDKMLTSP SPERSGFSSL YKLLLEVVPQ
KCGATEGAFI YAVERMLKDC PSSKQAMALL AKIKVPSSKA PSVSLDECFP TDVLADFEPA
SQERPQSSGA AVVLCSPDAK EFEEAAPEEV QESGHKAVHS ALLAEGPNNE QVQVVAGEQL
KLGGCGLAVG NAHEGALVSA GLINLVGGNL SPSDPMKENM LNSREDEPLD LSQPAPASTT
TLVREQTPDN PGSDAGALPV TVREFVPTGP ILCHVEHCGT ESGDSSSPLD LSDAQTLDQP
LNLSLAAWPV RATASDPGWV HGRREPVFVK PRNAFSDGDS ALQFGELSES SSVIEFDRTK
DAPVVDAPVD LTTSNEALSV VDPFEFAELK RPRFSAQALI DRGGPLADVH AKIKNRVYEQ
CLQACEPGSR ATPATREWLD KMWDRVDMKT WRCTSQFQAG RILASLKFLP DMIQDTPPPV
PRKNRASDNA GLKQLVAQWD RKLSVTPPPK PVGPVLDQIV PPPTDIQQED VTPSDGPPHA
PDFPSRVSTG GSWKGLMLSG TRLAGSISQR LMTWVFLKFS PTSQLLCSHF SRRGALWLQV
IGCLQVSFYL LSCSVVLTRY SDAFPYWVSF LVLCGVFVWV FLVLGWLLLY FYSRLHPTQS
VLLVTTIRRS VMLSFWLLSS ANFGNLCAAL WSAPQASYVS FLASYSVGHV ISGMFSYVYA
CLQIWPFLLF MWCPRGVVTS VGESV


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