ID A0A513WY84_PRRSV Unreviewed; 1460 AA. AC A0A513WY84; DT 16-OCT-2019, integrated into UniProtKB/TrEMBL. DT 16-OCT-2019, sequence version 1. DT 02-OCT-2024, entry version 26. 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:QDH06638.1}; OH NCBI_TaxID=9823; Sus scrofa (Pig). RN [1] {ECO:0000313|EMBL:QDH06638.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=180900-5 {ECO:0000313|EMBL:QDH06638.1}; RA Chang Y., Li T., Wang J., Jin C., Tan F., Li X., Tian K.; RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases. 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 -!- 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:0000256|ARBA:ARBA00001665}; 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:0000256|ARBA:ARBA00001556}; 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}. CC -!- SUBCELLULAR LOCATION: Host cytoplasm, host perinuclear region CC {ECO:0000256|ARBA:ARBA00004407}. Host membrane CC {ECO:0000256|ARBA:ARBA00004301}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004301}. Membrane CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004141}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; MK303390; QDH06638.1; -; Genomic_RNA. DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell. DR GO; GO:0044220; C:host cell perinuclear region of cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-UniRule. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC. DR GO; GO:0004540; F:RNA nuclease activity; IEA:UniProt. DR GO; GO:0003968; F:RNA-dependent RNA polymerase activity; IEA:UniProtKB-KW. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro. DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro. DR GO; GO:0075523; P:viral translational frameshifting; IEA:UniProtKB-KW. DR CDD; cd21410; 1B_av_Nsp10-like; 1. DR CDD; cd23189; Arteriviridae_RdRp; 1. DR CDD; cd17937; DEXXYc_viral_SF1-N; 1. DR CDD; cd21160; NendoU_av_Nsp11-like; 1. DR CDD; cd21166; NTD_av_Nsp11-like; 1. DR CDD; cd18786; SF1_C; 1. DR CDD; cd21405; ZBD_av_Nsp10-like; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2. DR InterPro; IPR027351; (+)RNA_virus_helicase_core_dom. DR InterPro; IPR046440; AV_NSP11N_COV_NSP15M. DR InterPro; IPR043502; DNA/RNA_pol_sf. 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; IPR027417; P-loop_NTPase. DR InterPro; IPR001205; RNA-dir_pol_C. DR InterPro; IPR007094; RNA-dir_pol_PSvirus. DR Pfam; PF19215; CoV_NSP15_C; 1. DR Pfam; PF22049; PRRSV-NSP11_N; 1. DR Pfam; PF00680; RdRP_1; 1. DR Pfam; PF01443; Viral_helicase1; 1. DR SUPFAM; SSF56672; DNA/RNA polymerases; 1. DR SUPFAM; SSF142877; EndoU-like; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2. DR PROSITE; PS51961; AV_NSP11N_COV_NSP15M; 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 4: Predicted; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840}; KW Endonuclease {ECO:0000256|PROSITE-ProRule:PRU01303}; KW Host cytoplasm {ECO:0000256|ARBA:ARBA00023200}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE- KW ProRule:PRU01303}; Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Nuclease {ECO:0000256|PROSITE-ProRule:PRU01303}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840}; KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695}; KW Ribosomal frameshifting {ECO:0000256|ARBA:ARBA00022758}; KW RNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022484}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}; KW Viral RNA replication {ECO:0000256|ARBA:ARBA00022953}; KW Zinc {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-ProRule:PRU00985}; KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE- KW ProRule:PRU00985}. FT DOMAIN 1..152 FT /note="NiRAN" FT /evidence="ECO:0000259|PROSITE:PS51947" FT DOMAIN 391..525 FT /note="RdRp catalytic" FT /evidence="ECO:0000259|PROSITE:PS50507" FT DOMAIN 646..709 FT /note="AV ZBD" FT /evidence="ECO:0000259|PROSITE:PS51652" FT DOMAIN 759..1048 FT /note="(+)RNA virus helicase C-terminal" FT /evidence="ECO:0000259|PROSITE:PS51657" FT DOMAIN 1087..1184 FT /note="AV-Nsp11N/CoV-Nsp15M" FT /evidence="ECO:0000259|PROSITE:PS51961" FT DOMAIN 1186..1308 FT /note="NendoU" FT /evidence="ECO:0000259|PROSITE:PS51958" FT ACT_SITE 1217 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01303" FT ACT_SITE 1232 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01303" FT ACT_SITE 1261 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01303" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:QDH06638.1" SQ SEQUENCE 1460 AA; 161201 MW; ECD39982308CE534 CRC64; TGFKLLAASG LTRCGRGGLV VTETAVKIVK YHSRTFTLGP LDLKVTSETE VKKSTEQGHA VVANLCSGVV LMRPHPPSLV DVLLVPGLDT IPGIQPGHGA GNMGVNGAIW DFETAPTKAE LELSKQIIQA CEIRRGDAPN LQLPYKLYPV RGDPERRNGR LSNTRFGDLP YKTPQDTKSA IHAACCLHPN GAPVSDGKST LGTTLQRGFE LYVPTVPYSV LEYLDSRPDT PVMCTKHGTS EAAAEDLQKY NLSTQGFVLP GVLRLVRKFV FGHIGKAPPL YLPSTYPAKN SMAGINGQRF PTKDVQSIPE IDEMCARAVK ENWQTVTPCT LKKQYCSKLK TRTILGTNNF IALAHRSALS GVTQAFMKKA WKSPIALGKN KFKELHCTVA GRCLEADLAS CDRSTPAIVR WFTANLLYEL AGCEEYLPSY VLNCCHDLVA TQDGAFTKRG GLSSGDPVTS VSNTVYSLVI YAQHMVLSAL KMGHEIGLKF LEEQLKFEDL IEIQPMLVYS DDLVLYAEKP TFPNYHWWVE HLDLMLGFKT DPKKTVITDK PSFLGCRIEA GRQLVPNRDR ILAALAYHMK AQNASEYYAS AAAILMDSCA CIDYDPEWYE DLICGIAQCA RQDGYSFPGP AFFMSMWEKL KGHNEGKKFR HCGICDAKAD HASACGLDLC LFHSHFHQHC PVTLSCGHHA GSKECPQCQS PVGAGKSPLD TVLQQVPYKP PRTVIMKVNN KTTALDPGRY QSRRGLVAVK RGIAGNEVDL ADGDYQVVPL LPTCKDINMV KVACNVLLSK FIVGPPGSGK TTWLLSQVQN DDVIYTPTHQ TMFDIVSALK VCRYSIPVAS GLPFPPPSRS GPWVRLVASG HTPGRVSYLD EAGYCNHLDI LRLLSKTPLV CLGDLQQLHP VGFDSCCYVF NQMPHKQLTT IYRFGPNICA AIQPCYREKL ESKARNTRVV FTTRPVAYGQ VLTPFHKDRD GSAITIDSSQ GATFDVVTLH LPSPKSLNKP RALVAITRAR HGLFIYDPHN QLQEFFNLTP EHTDCNLVFH RGDELVVLDP DNVTTTVAKA LEAGPSQFRV TDPRCKSLLA ACSVSLEGSC MPLPQVAHNL GFYFSPDSPA FAPLPKELAP HWPVVTHQNN HAWPDRLVAS MRPIDARYSK PMVGAGYVVG PSTFLGTPGV VSYYLTLYIR GEPQALPETL VSTGRIATDC REYLDTAEEE TAKELPHAFI GDVKGTTVGG CHHITSKYLP RFLPKDSVAV VGVSSPGKAA KAVCTLTDVY LPDLRPYLQP ETASKCWKLK LDFRDVRLMV WKGATAYFQL EGLTWSALPD YARFIQLPKD AVVYIDPCIG PAAANRKVVR TTDWRADLAV TPYDYGAQTI LTTAWFEDLG PQWKILGLQP FKRALGLENT EDWAILARRM NDGKDYTDYN WTCVRERPHA IYGRARDHTY HFALGTELQV ELGKPRPLSE //