ID I3QIT9_PRRSV Unreviewed; 1460 AA. AC I3QIT9; DT 05-SEP-2012, integrated into UniProtKB/TrEMBL. DT 05-SEP-2012, sequence version 1. DT 29-MAY-2024, entry version 62. 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:AFK09076.1, ECO:0000313|Proteomes:UP000107649}; OH NCBI_TaxID=9823; Sus scrofa (Pig). RN [1] {ECO:0000313|EMBL:AFK09076.1, ECO:0000313|Proteomes:UP000107649} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=10-10HEB-1 {ECO:0000313|EMBL:AFK09076.1}; RX PubMed=22525010; DOI=10.1016/j.vetmic.2012.02.036; RA Yu X., Chen N., Wang L., Wu J., Zhou Z., Ni J., Li X., Zhai X., Shi J., RA Tian K.; RT "New genomic characteristics of highly pathogenic porcine reproductive and RT respiratory syndrome viruses do not lead to significant changes in RT pathogenicity."; RL Vet. Microbiol. 158:291-299(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 -!- 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; JQ663551; AFK09076.1; -; Genomic_RNA. DR Proteomes; UP000107649; Genome. 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 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; 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 Host membrane {ECO:0000256|ARBA:ARBA00022870}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE- KW ProRule:PRU01303}; Membrane {ECO:0000256|ARBA:ARBA00023136}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE- KW ProRule:PRU00985}; 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..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 DOMAIN 644..707 FT /note="AV ZBD" FT /evidence="ECO:0000259|PROSITE:PS51652" FT DOMAIN 764..1045 FT /note="(+)RNA virus helicase C-terminal" FT /evidence="ECO:0000259|PROSITE:PS51657" FT DOMAIN 1084..1180 FT /note="AV-Nsp11N/CoV-Nsp15M" FT /evidence="ECO:0000259|PROSITE:PS51961" FT DOMAIN 1182..1304 FT /note="NendoU" FT /evidence="ECO:0000259|PROSITE:PS51958" FT ACT_SITE 1213 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01303" FT ACT_SITE 1228 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01303" FT ACT_SITE 1257 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01303" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AFK09076.1" SQ SEQUENCE 1460 AA; 161442 MW; A8D03135FE54E505 CRC64; FKLLAASGLT RCGRGGLVVT ETAVKIVKFH NRTFTLGPVN LKVASEVELK DAVEHNQHPV ARPVDGGVVL LRSAVPSLID VLISGADASP KLLARHGPGN TGIDGTLWDF EAEATKEEVA LSAQIIQACD IRRGDAPEIG LPYKLHPVRG NPERVKGVLQ NTRFGDIPYK TPSDTGSPVH AAACLTPNAT PVTDGRSVLA TTMPSGFELY VPTIPASVLD YLDSRPDCPK QLTEHGCEDA ALRDLSKYDL STQGFVLPGV LRLVRKYLFA HVGKCPPVHR PSTYPAKNSM AGINGNRFPT KDIQSVPEID VLCAQAVREN WQTVTPCTLK KQYCGKKKTR TILGTNNFIA LAHRAALSGV TQGFMKKAFN SPIALGKNKF KELQAPVLGR CLEADLASCD RSTPAIVRWF AANLLYELAC AEEHLPSYVL NCCHDLLVTQ SGAVTKRGGL SSGDPITSVS NTIYSLVIYA QHMVLSYFKS GHPHGLLFLQ DQLKFEDMLK VQPLIVYSDD LVLYAESPSM PNYHWWVEHL NLMLGFQTDP KKTTITDSPS FLGCRIINGR QLVPNRDRIL AALAYHMKAS NVSEYYASAA AILMDSCACL EYDPEWFEEL VVGIAQCARK DGYSFPGPPF FLSMWEKLRS NHEGKKSRMC GYCGAPAPYA TACGLDVCVY HTHFHQHCPV IIWCGHPAGS GSCSECEPPL GKGTSPLDEV LEQVPYKPPR TVIMHVEQGL TPLDPGRYQT RRGLVSVRRG IKGNEVDLPD GDYASTALLP TCKEINMVAV ASNVLRSRFI IGPPGAGKTH WLLQQVQDGD VIYTPTHQTM LDMIRALGTC RFNVPAGTTL QFPAPSRTGP WVRILAGGWC PGKNSFLDEA AYCNHLDVLR LLSKTTLTCL GDFKQLHPVG FDSHCYVFDI MPQTQLKTIW RFGQNICDAI QPDYRDKLMS MVNTTRVTYV EKPVRYGQVL TPYHRDREDG AITIDSSQGA TFDVVTLHLP TKDSLNRQRA LVAITRARHA IFVYDPHRQL QSMFDLPAKG TPVNLAVHRD EQLIVLDRNN REITVAQALG NGDKFRATDK RVVDSLRAIC ADLEGSSSPL PKVAHNLGFY FSPDLTQFAK LPAELAPHWP VVTAQNNERW PDRLVASLRP IHKYSRACIG AGYMVGPSVF LGTPGVVSYY LTKFVRGEAQ VLPETVFSTG RIEVDCREYL DDREREVAES LPHAFIGDVK GTTVGGCHHV TSKYLPRFLP KESVAVVGVS SPGKAAKAVC TLTDVYLPDL EAYLHPETQS RCWKVMLDFK EVRLMVWKDK TAYFQLEGRH FTWYQLASYA SYIRVPVNST VYLDPCMGPA LCNRKVVGST HWGADLAVTP YDYGAKIILS SAYHGEMPPG CKILACAEFS LDDPVRYKHT WGFESDTAYL YEFTGNGEDW EDYNDAFRAR QKGKIYKANA TSMRFHFPPG PVIEPTLGLN //