ID I6YQR1_PRRSV Unreviewed; 643 AA.
AC I6YQR1;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Replicase polyprotein 1ab {ECO:0000256|ARBA:ARBA00022087};
DE AltName: Full=ORF1ab polyprotein {ECO:0000256|ARBA:ARBA00029611};
DE Flags: Fragment;
OS Porcine reproductive and respiratory syndrome virus (PRRSV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Arnidovirineae; Arteriviridae; Variarterivirinae;
OC Betaarterivirus; Ampobartevirus; Betaarterivirus suid 2.
OX NCBI_TaxID=28344 {ECO:0000313|EMBL:AFN55161.1};
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1] {ECO:0000313|EMBL:AFN55161.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=25617-00 {ECO:0000313|EMBL:AFN55161.1};
RX PubMed=22771938; DOI=10.1016/j.virusres.2012.06.024;
RA Parida R., Choi I.S., Peterson D.A., Pattnaik A.K., Laegreid W.,
RA Zuckermann F.A., Osorio F.A.;
RT "Location of T-cell epitopes in nonstructural proteins 9 and 10 of type-II
RT porcine reproductive and respiratory syndrome virus.";
RL Virus Res. 169:13-21(2012).
CC -!- FUNCTION: Cleaves the majority of cleavage sites present in the C-
CC terminus of the polyprotein. Triggers host apoptosis through caspase-3,
CC -8, and -9 activations. Subverts host innate immune responses through
CC its protease activity. Targets the NF-kappa-B essential modulator NEMO
CC and mediates its cleavage. Blocks host interferon beta induction and
CC downstream signaling by cleaving mitochondrial MAVS, dislodging it from
CC the mitochondria. Impairs host defense by cleaving host mRNA-decapping
CC enzyme DCP1A to attenuate its antiviral activity.
CC {ECO:0000256|ARBA:ARBA00043848}.
CC -!- FUNCTION: Plays a role in the inhibition of the immune response by
CC interacting with host IFITM1. This interaction leads to the proteasomal
CC degradation of the IFN-induced antiviral protein IFITM1.
CC {ECO:0000256|ARBA:ARBA00043938}.
CC -!- FUNCTION: Plays a role in viral transcription/replication and prevents
CC the simultaneous activation of host cell dsRNA sensors, such as
CC MDA5/IFIH1, OAS, PKR (By similarity) and NLRP3 inflammasome (By
CC 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). Also plays a role in the inhibition of
CC host type I interferon production by recruiting host OTULIN to promote
CC removal of linear ubiquitination targeting host NEMO.
CC {ECO:0000256|ARBA:ARBA00043885}.
CC -!- SUBUNIT: Interacts with host DDX18; this interaction redistributes host
CC DDX18 to the cytoplasm. {ECO:0000256|ARBA:ARBA00044015}.
CC -!- SUBUNIT: Interacts with host DDX5. {ECO:0000256|ARBA:ARBA00044025}.
CC -!- SUBUNIT: Interacts with host IFITM1. {ECO:0000256|ARBA:ARBA00044033}.
CC -!- SUBUNIT: Interacts with host LGALS3. {ECO:0000256|ARBA:ARBA00044014}.
CC -!- SUBUNIT: Interacts with host OTULIN. {ECO:0000256|ARBA:ARBA00044017}.
CC -!- SUBUNIT: Nsp1-alpha papain-like: Interacts with host RNF31.
CC {ECO:0000256|ARBA:ARBA00044019}.
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DR EMBL; JX294620; AFN55161.1; -; Genomic_RNA.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003968; F:RNA-dependent RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR CDD; cd23189; Arteriviridae_RdRp; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR044863; NIRAN.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR001205; RNA-dir_pol_C.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR Pfam; PF00680; RdRP_1; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR PROSITE; PS51947; NIRAN; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE 4: Predicted;
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW RNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022484,
KW ECO:0000313|EMBL:AFN55161.1}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Viral RNA replication {ECO:0000256|ARBA:ARBA00022953}.
FT DOMAIN 1..150
FT /note="NiRAN"
FT /evidence="ECO:0000259|PROSITE:PS51947"
FT DOMAIN 389..523
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50507"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AFN55161.1"
FT NON_TER 643
FT /evidence="ECO:0000313|EMBL:AFN55161.1"
SQ SEQUENCE 643 AA; 70447 MW; 7747ACD8B5A2F44F CRC64;
FKLLAASGLT RCGRGGLVIT ETAVKIVKFH NRTFTLGPVN LKVASEVELK DAVEHNQYPV
ARPVDGGVVL LRSAVPSLID VLISGADASP KLLACHGPGN TGIDGSLWDF EAEATKEEIA
LSAQIIQACG IRRGDAPEIG LPYKLHPVRG NPERVKGVLQ NTRFGDIPYK TPSDTGSPVH
AAACLTPNAA PVTDGRSVLA TTMPSGFELY VPTIPASVLD YLDSRPDCPK QLTEHGCEDA
ALRDLSKYDL STQGFVLPGV LRLVRKYLFA HVGKCPPIHR PSTYPAKNSM AGINGNRFPT
KDIQSVPEID VLCAQAVREN WQTVTPCTLK KQYCGKKKTR TILGTNNFIA LAHRAALSGV
TQGFMKKAFN SPIALGKNKF KELQTPVLGR CLEADLASCD RSTPAIVRWF AANLLYELAC
AEEHLPSYVL NCCHDLLVTQ SGAVTKRGGL SSGDPITSVS NTIYSLVIYA QHMVLSYFKS
GHPHGLLFLQ DQLKFEDMLK VQPLIVYSDD LVLYAESPTM PNYHWWVEHL NLMLGFQTDP
KKTAITDSPS FLGCRIINGR QLVPNRDRIL AALAYHMKAN NVSEYYASAA AILMDSCACL
EYDPEWFEEL VVGMAQCARK DGYSFPGPPF FLSMWEKLRS NHE
//
