ID B2BLI5_PRRSV Unreviewed; 1457 AA.
AC B2BLI5;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 80.
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:ABU43301.1, ECO:0000313|Proteomes:UP000151219};
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1] {ECO:0000313|EMBL:ABU43301.1, ECO:0000313|Proteomes:UP000151219}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISU-P {ECO:0000313|EMBL:ABU43301.1};
RA Murtaugh M.P., Abrahante J.E.;
RT "Mechanisms of Failed Protection Against PRRS in Sow Herds.";
RL Submitted (APR-2007) 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; EF532816; ABU43301.1; -; Genomic_RNA.
DR Proteomes; UP000151219; 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; 3.30.70.270; -; 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; IPR043128; Rev_trsase/Diguanyl_cyclase.
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:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Ribosomal frameshifting {ECO:0000256|ARBA:ARBA00022758};
KW RNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022484,
KW ECO:0000313|EMBL:ABU43301.1}; 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..147
FT /note="NiRAN"
FT /evidence="ECO:0000259|PROSITE:PS51947"
FT DOMAIN 386..520
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50507"
FT DOMAIN 641..704
FT /note="AV ZBD"
FT /evidence="ECO:0000259|PROSITE:PS51652"
FT DOMAIN 761..1042
FT /note="(+)RNA virus helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51657"
FT DOMAIN 1081..1177
FT /note="AV-Nsp11N/CoV-Nsp15M"
FT /evidence="ECO:0000259|PROSITE:PS51961"
FT DOMAIN 1179..1301
FT /note="NendoU"
FT /evidence="ECO:0000259|PROSITE:PS51958"
FT ACT_SITE 1210
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01303"
FT ACT_SITE 1225
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01303"
FT ACT_SITE 1254
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01303"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABU43301.1"
SQ SEQUENCE 1457 AA; 161105 MW; 70B4B8002B640CAE CRC64;
LAASGLTRCG RGGLVVTETA VKIVKFHNRT FTLGPVNLKV ASEVELKDAV EHNQHPVARP
VDGGVVLLRS AVPSLIDVLI SGADASPKLL AHHGPGNTGI DGTLWDFESE ATKEEVALSA
QIIQACDIRR GDAPEIGLPY KLYPVRGNPE RVKGVLQNTR FGDIPYKTPS DTGSPVHAAA
CLTPNATPVT DGRSVLATTM PSGFELYVPT IPASVLDYLD SRPDCPKQLT EHGCEDAALR
DLSKYDLSTQ GFVLPGVLRL VRKYLFAHVG KCPPVHRPST YPARNSMAGI NGNRFPTKDI
QSVPEIDVLC AQAVRENWQT VTPCTLKKQY CGKRKTRTIL GTNNFIALAH RAALSGVTLG
FMKKAFNSPI ALGKNKFKEL QTPVLGRCLE ADLASCDRST PAIVRWFAAN LLYELACAEE
HLPSYVLNCC HDLLVTQSGA VTKRGGLSSG DPITSVSNTI YSLVIYAQHM VLSYFKSGHP
HGLLFLQDQL KFEDMLKVQP LIVYSDDLVL YAESPTMPNY HWWVEHLNLM LGFQTDPKKT
AITDSPSFLG CRIINGRQLV PNRDRILAAL AYHMKASNVS EYYASAAAIL MDSCACLEYD
PEWFEELVVG VAQCARKDGY SFPGTPFFMS MWEKLRTNYE GKKSRVCGYC GAPAPYATAC
GLDVCIYHAH FHQHCPVTIW CGHPAGSGSC SECKSPVGKG TSPLDEVLEQ VPYKPPRTVI
MHVEQGLTPL DPGRYQTRRG LVSVRRGIRG NEVELPDGDY ASTALLPTCK EINMVAVASN
VLRSRFIIGP PGAGKTYWLL QQVQDGDVIY TPTHQTMLDM IRALGTCRFN VPAGTTLQFP
VPSRTGPWVR ILAGGWCPGK NSFLDEAAYC NHLDVLRLLS KTTLTCLGDF KQLHPVGFDS
HCYVFDIMPQ TQLKTIWRFG QNVCDAIQPD YRDKLMSMVN TTRVTYVEKP VRYGQVLTPY
HRDREDDAIT IDSSQGATFD VVTLHLPTKD SLNRQRALVA ITRARHAIFV YDPHRQLQSL
FDLPAKGTPV NLAVHRDGQL IVLDRNNKEC TVAQALGNGD KFRATDKRVV DSLRAICADL
EGSSSPLPKV AHNLGFYFSP DLTQFAKLPV ELAPHWPVVT TQNNEKWPDR LVASLRPIHK
YSRACIGAGY MVGPSVFLGT PGVVSYYLTK FVKGEAQVLP ETVFSTGRIE VDCREYLDDR
EREVAASLPH AFIGDVKGTT VGGCHHVTSR YLPRFLPKES VAVVGVSSPG KAAKALCTLT
DVYLPDLEAY LHPETQSKCW KMMLDFKEVR LMVWKDKTAY FQLEGRYFTW YQLASYASYI
RVPVNSTVYL DPCMGPALCN RRVVGSAHWG ADLAVTPYDY GAKIILSSAY HGEMPPGYKI
LACAEFSLDD PVKYKHTWGF ESDTAYLYEL TGNGEDWEDY NDAFRARQEG KIYKATATSM
KFYFPPGPVI EPTLGLN
//
