ID I3QIS2_PRRSV Unreviewed; 2473 AA. AC I3QIS2; DT 05-SEP-2012, integrated into UniProtKB/TrEMBL. DT 05-SEP-2012, sequence version 1. DT 29-MAY-2024, entry version 49. DE SubName: Full=Non-structural protein {ECO:0000313|EMBL:AFK09059.1}; 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:AFK09059.1, ECO:0000313|Proteomes:UP000152673}; OH NCBI_TaxID=9823; Sus scrofa (Pig). RN [1] {ECO:0000313|EMBL:AFK09059.1, ECO:0000313|Proteomes:UP000152673} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=10-10FUJ-4 {ECO:0000313|EMBL:AFK09059.1}; 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 -!- CATALYTIC ACTIVITY: CC Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide CC and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76- CC residue protein attached to proteins as an intracellular targeting CC signal).; EC=3.4.19.12; Evidence={ECO:0000256|ARBA:ARBA00000707}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Host CC cytoplasm {ECO:0000256|ARBA:ARBA00004192}. Host nucleus CC {ECO:0000256|ARBA:ARBA00004147}. Membrane CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004141}. Nucleus CC {ECO:0000256|ARBA:ARBA00004123}. 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; JQ663549; AFK09059.1; -; Genomic_RNA. DR Proteomes; UP000152673; Genome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0044165; C:host cell endoplasmic reticulum; IEA:UniProtKB-KW. DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-KW. DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR GO; GO:0039579; P:symbiont-mediated suppression of host ISG15-protein conjugation; IEA:UniProtKB-KW. DR GO; GO:0039563; P:symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT1 activity; IEA:UniProtKB-KW. DR GO; GO:0039502; P:symbiont-mediated suppression of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW. DR GO; GO:0019082; P:viral protein processing; IEA:InterPro. DR GO; GO:0019049; P:virus-mediated perturbation of host defense response; IEA:UniProtKB-KW. DR CDD; cd22528; av_Nsp3_ER-remodelling; 1. DR Gene3D; 3.90.70.160; -; 1. DR Gene3D; 4.10.80.390; -; 1. DR Gene3D; 3.30.1330.220; Arterivirus nonstructural protein 7 alpha; 1. DR Gene3D; 2.30.31.30; Arterivirus nps1beta, nuclease domain; 1. DR Gene3D; 3.90.70.70; Arterivirus papain-like cysteine protease beta domain; 1. DR Gene3D; 3.90.70.60; Porcine arterivirus-type cysteine proteinase alpha domain; 1. DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2. DR InterPro; IPR031932; Arteri_nsp7a. DR InterPro; IPR038451; Arteri_nsp7a_sf. DR InterPro; IPR008743; Arterivirus_Nsp2_C33. DR InterPro; IPR023338; Arterivirus_NSP4_peptidase. DR InterPro; IPR008741; AV_PCPalpha. DR InterPro; IPR038155; AV_PCPalpha_sf. DR InterPro; IPR025773; AV_PCPbeta. DR InterPro; IPR038154; AV_PCPbeta_sf. DR InterPro; IPR023183; Chymotrypsin-like_C. DR InterPro; IPR008760; EAV_peptidase_S32. DR InterPro; IPR032855; NSP2-B_epitope. DR InterPro; IPR032785; Pdase_C33_assoc. DR InterPro; IPR009003; Peptidase_S1_PA. DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin. DR Pfam; PF16749; Arteri_nsp7a; 1. DR Pfam; PF14757; NSP2-B_epitope; 2. DR Pfam; PF14756; Pdase_C33_assoc; 1. DR Pfam; PF05410; Peptidase_C31; 1. DR Pfam; PF05411; Peptidase_C32; 1. DR Pfam; PF05412; Peptidase_C33; 1. DR Pfam; PF05579; Peptidase_S32; 1. DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1. DR PROSITE; PS51538; AV_CP; 1. DR PROSITE; PS51493; AV_NSP4_PRO; 1. DR PROSITE; PS51539; AV_PCP_ALPHA; 1. DR PROSITE; PS51540; AV_PCP_BETA; 1. PE 4: Predicted; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840}; KW Helicase {ECO:0000256|ARBA:ARBA00022806}; KW Host cytoplasm {ECO:0000256|ARBA:ARBA00023200}; KW Host endoplasmic reticulum {ECO:0000256|ARBA:ARBA00023184}; KW Host membrane {ECO:0000256|ARBA:ARBA00022870}; KW Host nucleus {ECO:0000256|ARBA:ARBA00022562}; KW Host-virus interaction {ECO:0000256|ARBA:ARBA00022581}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Inhibition of host innate immune response by virus KW {ECO:0000256|ARBA:ARBA00022632}; KW Inhibition of host interferon signaling pathway by virus KW {ECO:0000256|ARBA:ARBA00022830}; KW Inhibition of host ISG15 by virus {ECO:0000256|ARBA:ARBA00023208}; KW Inhibition of host NF-kappa-B by virus {ECO:0000256|ARBA:ARBA00022863}; KW Inhibition of host STAT1 by virus {ECO:0000256|ARBA:ARBA00022961}; KW Interferon antiviral system evasion {ECO:0000256|ARBA:ARBA00023258}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW Protease {ECO:0000256|ARBA:ARBA00022670}; KW Ribosomal frameshifting {ECO:0000256|ARBA:ARBA00022758}; KW Thiol protease {ECO:0000256|ARBA:ARBA00022807}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}; KW Viral immunoevasion {ECO:0000256|ARBA:ARBA00023280}; KW Zinc {ECO:0000256|ARBA:ARBA00022833}; KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}. FT TRANSMEM 1228..1256 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1263..1279 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1341..1359 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1618..1642 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1654..1682 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1688..1717 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1992..2017 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 2029..2050 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 2062..2082 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 2102..2127 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 2134..2152 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 69..180 FT /note="Peptidase C31" FT /evidence="ECO:0000259|PROSITE:PS51539" FT DOMAIN 263..383 FT /note="Peptidase C32" FT /evidence="ECO:0000259|PROSITE:PS51540" FT DOMAIN 428..535 FT /note="Peptidase C33" FT /evidence="ECO:0000259|PROSITE:PS51538" FT DOMAIN 1780..1983 FT /note="Peptidase S32" FT /evidence="ECO:0000259|PROSITE:PS51493" FT REGION 401..422 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 809..865 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1122..1149 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 401..417 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 825..841 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 2473 AA; 268852 MW; B1AFA0CE8A651A86 CRC64; MSGILDRCTC TPNARVFVAE GQVYCTRCLS ARSLLPLNLQ VPELGVLGLF YRPEEPLRWT LPRAFPTVEC SPAGACWLSA IFPIARMTSG NLNFQQRMVR VAAEIYRAGQ LTPTVLKTLQ VYERGCRWYP IVGPVPGVGV YANSLHVSDK PFPGATHVLT NLPLPQRPKP EDFCPFECAM ADVYDIGRGA VMYVAGGKVS WAPRGGNEVK FEPVPKELRL VASRLHTSFP PHHVVDMSRF TFMTPGSGVS MRVEYQCGCL PADTVPEGNC WWRLFDSLPP EVQYKEIRHA NQFGYQTKHG VPGKYLQRRL QVNGLRAVTD THGPIVIQYF SVKESWIRHL KLVEEPSLPG FEDLLRIRVE PNTSPLVGKD EKIFRFGSHK WYGAGKRARK TRSGATTVVA HHASSAHETQ QATKHEGTGA NKAEHLKRYS PPAEGNCGWH CISAIANRMV NSNFETTLPE RARPSDDWAT DEDLVNTIQI LRLPAALDRN GACGSAKYVL KLEGEHWTVS VIPGMSPTLL PLECVQGCCE HKGGLVSSDA VEISEFDPAC LDRLAKVMHL PSSAIPAALA ELSDDSNRPV SPAATTWTVS QFYARHGGGD HHDQVCLGKI ISLCQVIEDC CCHQNKTNRA TPEEVAAKID QYLRGATSLE ECLAKLERVS PPGAADTSFD WNVVLPGVEA ASQTTEQPHV NSCCTLVPPV TQEPLGKDSV PLTAFSLSNC YYPAQGDEVH HRERLNSVLS RLEEVVMEEY GLMPTGLGPR PVLPSGLDEL KDQMEEDLLK LANTQATSEM MARAAEQVDL KAWVKSYPRW APPPPPPRVQ PRRTKSVKSL PEDKPVPAPR RKVRSDCGGP VLMGDNVPNG SEETVGGPLN FPTPSELMTP MSEPVLVPAS QFVPKLMTPL IGSAPVPAPR RTVTTTLTHL DEPLDLSASS QTEYKASPLA PSQNMGILVA GGQEAEEVLS EISDILNDTN PAPVSSSSSL SSVKITRPKY SAQAIIDSGG PCSGHLQKEK EACLSIMREA CDASKLSDPA TQEWLSRMWD RVDMLTWRNT SAYQAFRILN GRFGFLPKMI LETPPPYPCG FVMLPHTPAP SVSAESDLTI GSVATEDVPR ILGKIGDTNE LLDRGPLAPS KGEPVCDQPA KDPLMSPRES DESIIAPPAD TGGVGSFTDL PSSDGVDVDG GGLLRTVKTK AGRLLDQLSC QVFSLVSHLP IFFSHLFKSD SGYSPGDWGF AAFTLFCLFL CYSYPFFGFA PLLGVFSGSS RRVRMGVFGC WLAFAVGLFK PVSDPVGNAC EFDSPECRNV LHSFELLKPW DPVRSLVVGP VGLGLAILGR LLGGARYVWH FLLRLGIVAD CILAGAYVLS QGRCKKCWGS CVRTAPNEIA FNVFPFTRAT RSSLIDLCDR FCAPKGMDPI FLATGWRGCW TGRSPIEQPS EKPIAFAQLD EKRITARTVV AQPYDPNQAV KCLRVLQAGG AMVAETVPKV VKVSAIPFRA PFFPAGVKVD PECRIVVDPD TFTTALRSGY STANLVLGTG DFAQLNGLKI RQISKPSGGG PHLIAALHVA CSMALHMLAG VYVTAVGSCG TGTNDPWCTN PFAVPGYGPG SLCTSRLCIS QHGLTLPLTA LVVGFGLQEI ALVVLIFVSV GGMAHRLSCK ADMLCILLAI ASYVWVPLTW LLCVFPCWLR WFSLHPLTIL WLVFFLISVN IPSGILAVVL LVSLWLLGRY TNIAGLVTPY DIHHYTSGPR GVAALATAPD GTYLAAVRRA ALTGRTMLFT PSQLGSLLEG AFRTQKPSLN TVNVVGSSMG SGGVFTIDGK IKCVTAAHVL TGNSARVSGV GFNQMLDFDV KGDFAIADCP NWQGVAPKAQ FCEDGWTGRA YWLTSSGVEP GVIGNGFAFC FTACGDSGSP VITEAGELVG VHTGSNKQGG GIVTRPSGQF RNVEPIKLSE LSEFFAGPKV PLGDVKIGSH IIKDTCEVPS DLCALLAAKP ELEGGLSTVQ RLCVFFLLWR MMGHAWTPLV AVGFFILNEI LPAVLVRSVF SFGMFVLSWL TPWSAQVLMI RLLTAALNRN RWSLGFYSLG AVTSFVADLA VTQGHPLQVV MNLSTYAFLP RMMVMTSPVP VIACGVVHLL AIILYLFKYR CLHNVLVGDG VFSSAFFLRY FAEGKLREGV SQSCGMSHES LTGALAMRLT DEDLDFLTKW TDFKCFVSAS NMRNAAGQFI EAAYAKALRI ELAQLVQVDK VRGTMAKLEA FADTVAPQLS PGDIVVALGH TPVGSIFDLK VGSTKHTLQA IETRVLAGSK MTVARVVDPT PAPPPVPVPI PLPPKVLENG PNAWGDEDRL NKKKRRRMEA VGIFVMDGKK YQKFWDKNSG DVFYEEVHIS TDEWECLRTG DPVDFDPETG IQCGHITIED KVYNVFTSPS GRRFLVPANP ENRRAQWEAA KLSVEQALGM MNVDGELTAK ELEKLKRIID KLQGLTKEQC LNC //