ID W0P0Q8_PRRSV Unreviewed; 1463 AA.
AC W0P0Q8;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 54.
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:AHG56683.1, ECO:0000313|Proteomes:UP000122800};
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1] {ECO:0000313|EMBL:AHG56683.1, ECO:0000313|Proteomes:UP000122800}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MLV-DV {ECO:0000313|EMBL:AHG56683.1};
RX PubMed=24371078; DOI=10.1128/JVI.02858-13;
RA Martin-Valls G.E., Kvisgaard L.K., Tello M., Darwich L., Cortey M.,
RA Burgara-Estrella A.J., Hernandez J., Larsen L.E., Mateu E.;
RT "Analysis of ORF5 and full-length genome sequences of porcine reproductive
RT and respiratory syndrome virus isolates of genotypes 1 and 2 retrieved
RT worldwide provides evidence that recombination is a common phenomenon and
RT may produce mosaic isolates.";
RL J. Virol. 88:3170-3181(2014).
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}.
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DR EMBL; KJ127878; AHG56683.1; -; Genomic_RNA.
DR Proteomes; UP000122800; 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:0008236; F:serine-type peptidase 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; 1.
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 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: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:AHG56683.1"
SQ SEQUENCE 1463 AA; 161616 MW; 005E02E1E820DDBD CRC64;
TGFKLLAASG LTRCGRGGLV VTETAVKIIK YHSRTFTLGP LDLKVTSEVE VKKSTEQGHA
VVANLCSGVI LMRPHPPSLV DVLLKPGLDT TPGIQPGHGA GNMGVDGSIW DFETAPTKAE
LELSKQIIQA CEVRRGDAPN LQLPYKLYPV RGDPERHKGR LINTRFGDLP YKTPQDTKSA
IHAACCLHPN GAPVSDGKST LGTTLQHGFE LYVPTVPYSV MEYLDSRPDT PFMCTKHGTS
KAAAEDLQKY DLSTQGFVLP GVLRLVRRFI FGHIGKAPPL FLPSTYPAKN SMAGINGQRF
PTKDVQSIPE IDEMCARAVK ENWQTVTPCT LKKQYCSKPK TRTILGTNNF IALAHRSALS
GVTQAFMKKA WKSPIALGKN KFKELHCTVA GRCLEADLAS CDRSTPAIVR WFVANLLYEL
AGCEEYLPSY VLNCCHDLVA TQDGAFTKRG GLSSGDPVTS VSNTVYSLVI YAQHMVLSAL
KMGHEIGLKF LEEQLKFEDL LEIQPMLVYS DDLVLYAERP TFPNYHWWVD HLDLMLGFRT
DPKKTVITDK PSFLGCRIEA GRQLVPNRDR ILAALAYHMK AQNASEYYAS AAAILMDSCA
CIDHDPEWYE DLICGIARCA RQDGYSFPGP AFFMSMWEKL RSHNEGKKFR HCGICDAKAD
YASACGLDLC LFHSHFHQHC PVTLSCGHHA GSKECSQCQS PVGAGRSPLD AVLKQIPYKP
PRTVIMKVGN KTTALDPGRY QSRRGLVAVK RGIAGNEVDL SDGDYQVVPL LPTCKDINMV
KVACNVLLSK FIVGPPGSGK TTWLLSQVQD DDVIYTPTHQ TMFDIVSALK VCRYSVPGAS
GLPFPPPARS GPWVRLIASG HVPGRVSYLD EAGYCNHLDI LRLLSKTPLV CLGDLQQLHP
VGFDSYCYVF DQMPQKQLTT IYRFGPNICA AIQPCYREKL ESKARNTRVV FTTRPVAFGQ
VLTPYHKDRI GSAITIDSSQ GATFDIVTLH LPSPKSLNKS RALVAITRAR HGLFIYDPHN
QLQEFFNLTP ERTDCNLVFS CGDELVVLNA DNAVTTVAKA LETGPSRFRV SDPRCKSLLA
ACSASLEGSC MPLPQVAHNL GFYFSPDSPV FAPLPKELAP HWPVVTHQNN RAWPDRLVAS
MRPIDARYSK PMVGAGYVVG SSTFLGTPGV VSYYLTLYIR GEPQALPETL VSTGRIATDC
REYLDAAEEE AAKELPHAFI GDVKGTTVGG CHHITSKYLP RSLPKDSVAV VGVSSPGRAA
KAVCTLTDVY LPELRPYLQP ETASKCWKLK LDFRDVRLMV WKGATAYFQL EGLTWSALPD
YARFIQLPKD AVVYIDPCIG PATANRKVVR TTDWRADLAV TPYDYGAQNI LTTAWFEDLG
PQWKILGLQP FRRAFGFENT EDWAILARRM NDGKDYTDYN WNCVRERPHA IYGRARDLTY
HFAPGTELQV ELGKPRLPPG QVP
//
