ID C4P6W8_PRRSV Unreviewed; 1460 AA.
AC C4P6W8;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 77.
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:ACQ71961.1, ECO:0000313|Proteomes:UP000107910};
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1] {ECO:0000313|EMBL:ACQ71961.1, ECO:0000313|Proteomes:UP000107910}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBB-1-F3 {ECO:0000313|EMBL:ACQ71961.1};
RA Gao J.;
RT "Porcine reproductive and respiratory syndrome virus Chongqing isolates.";
RL Submitted (APR-2009) 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=3.6.4.13;
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; FJ889129; ACQ71961.1; -; Genomic_RNA.
DR Proteomes; UP000107910; 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; 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 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..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:ACQ71961.1"
SQ SEQUENCE 1460 AA; 161600 MW; C6A371B1A5F63119 CRC64;
FKLLAASGLT RCGRGGLVVT ETAVKIVKFH NRTFTLGPVN LKVASEVELK DAIEHNQHPV
ARPVDGGVVL LRSAVPSLID VLISGADASP KLLARHGPGN TGIDGTLWDF EAEATKEEVA
LSAQIIQACD IRRGDAPEIG LPYKLYPVRG 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 IRGNEVDLPD 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 VVTTQNNERW PDRLVASLRP
IHKYSRACIG AGYMVGPSVF LGTPGVVSYY LTKFVRGEAQ VLPETVFSTG RIEVDCREYL
DDREREVAES LPHAFIGDVK GTTVGGCHHV TSKYLPRFLP KESVAVVGVS SPGKAAKAVC
TLTDVYLPDL EAYLHPETQS RCWKVMLDFK EVRLMVWKDK TAYFQLEGRH FTWYQLASYA
SYIRVPANST VYLDPCMGPA LCNRRVVGST HWGADLAVTP YDYGAKIILS SAYHGEMPPG
YKILACAEFS LDDPVRYKHT WGFESDTAYL YEFTGNGEDW EDYNDAFRAR QKGKIYKANA
TSMRFHFPPG PVIEPTLGLN
//
