| IED ID | IndEnz0002001216 |
| Enzyme Type ID | protease001216 |
| Protein Name |
Replicase polyprotein 1ab pp1ab ORF1ab polyprotein Cleaved into: Non-structural protein 1 nsp1 ; Non-structural protein 2 nsp2 ; Non-structural protein 3 nsp3 EC 3.4.19.12 EC 3.4.22.- PL1-PRO/PL2-PRO PLP1/PLP2 Papain-like proteinases 1/2 p195 ; Non-structural protein 4 nsp4 Peptide HD2 ; 3C-like proteinase 3CL-PRO 3CLp EC 3.4.22.- M-PRO nsp5 ; Non-structural protein 6 nsp6 ; Non-structural protein 7 nsp7 ; Non-structural protein 8 nsp8 ; Non-structural protein 9 nsp9 ; Non-structural protein 10 nsp10 ; Non-structural protein 11 nsp11 ; RNA-directed RNA polymerase Pol RdRp EC 2.7.7.48 nsp12 ; Helicase Hel EC 3.6.4.12 EC 3.6.4.13 nsp13 ; Exoribonuclease ExoN EC 3.1.13.- nsp14 ; Uridylate-specific endoribonuclease EC 4.6.1.- NendoU nsp15 ; Putative 2'-O-methyl transferase EC 2.1.1.57 nsp16 |
| Gene Name | rep 1a-1b |
| Organism | Feline coronavirus (strain FIPV WSU-79/1146) (FCoV) |
| Taxonomic Lineage | Viruses Riboviria Orthornavirae Pisuviricota Pisoniviricetes Nidovirales Cornidovirineae Coronaviridae Orthocoronavirinae Alphacoronavirus Tegacovirus Alphacoronavirus 1 Feline coronavirus Feline infectious peritonitis virus Feline coronavirus (strain FIPV WSU-79/1146) (FCoV) |
| Enzyme Sequence | MSSKQFKILVNEDYQVNVPSLPFRDALQEIKYCYRNGFDGYVFVPEYRRDLVDCNRKDHYVIGVLGNGISDLKPVLLTEPSVMLQGFIVRANCNGVLEDFDLKFARTGNGAIYVDQYMCGADGKPVIEGEFKDYFGDEDVIIYEGEEYHCAWLTVRDEKPLWQQTLLTIREIQYNLDIPHKLPNCAIREVAPPVKKNSKVVLSEEYRKLYDIFGSPFMGNGDSLNTCFDSLHFIAATLKCPCGAESSGVGDWTGFKTACCGLHGKVKGVTLGAVKPGDAIVTSMSAGKGVKFFANSVLQYAGDVENVSVWKVIKTFTVNETVCTTDFEGELNDFIRPESTSPVSCSIKRAFITGEVDDAVHDCIIAGKLDLSTNLFGSANLLFKKMPWFVQKCGAIFADAWKVVEELLCSLKLTYKQIYDVVASLCTSAFTIMDYKPVFVVSSNSVKDLVDKCVKILVKAFDVFTQTITIAGVEAKCFVLGSKYLLFNNALVKLVSVKILGKRQKGLDSAFFATNLIGATVNVTPQRTESAYISLNKVDDVVTPGGGHIVIIGDMAFYKSEEYYFMMASPDSVLVNNVFKAARVPSYNIVYDVNDDTKSKMVVKIGTSFDFDGDLDAAIAKVNDLLIEFRQEKLCFRALKDGENILVEAYLKKYKMPVCLKNHVGLWDIIRQDSGKKGFLDTFNHLNELEDVKDIKIQTIKNIICPDLLLELDFGAIWYRCMPACSDKSILGNVKIMLGNGVKVVCDGCHSFANRLTINYNKLCDTARKDIEIGGIPFSTFKTPSSSFIDMKDAIYSVVEYGEALSFKTASVPVTNSGIITTDDWSDPILLEPADYVEPKDNGDVIVIAGYTFYKDEDDHFYPYGSGMVVQKMYNKMGGGDKSVSFSDNVNVREIEPVTRVRLEFEFDNEVVTQVLEKVIGTKYKFIGTTWEEFEDSISEKLDKIFDTLAEQGVELEGYFIYDTCGGFDINNPDGVMISQYDLNTAADDKSDSDASVEDISLISDNEDVEQIEEDNTSTDDAEDVSSVEGETVSVVDVEDFVEQVSLVEENNVLTPAVNPDEQLSSVEKKDEVSAKNDPWAAAVDEQEAEQPKPSLTPFKTTNLNGKIILKQQDNNCWINACCYQLQAFDFFNHDLWDGFKKDDVMPFVDFCYAALTLKQGDSGDAEYLLETMLNDYSTAKVTLSAKCGCGVKEIVLERTVFKLTPLRNEFKYGVCGDCKQINMCKFASVEGSGVFVHDRIEKQTPVSQFIVTPTMHAVYTGTTQSGHYMIEDCIHDYCVDGMGIKPRKHKFYTSTLFLNANVMTAKSKTMVEPPVPVEDKCVEDCQSPKDLILPFYKAGKVSFYQGDLDVLINFLEPDVLVNAANGDLRHVGGVARAIDVFTGGKLTKRSKEYLKSSKAIAPGNAVLFENVLEHLSVLNAVGPRNGDSRVEGKLCNVYKAIAKCDGKILTPLISVGIFKVKLEVSLQCLLKTVTDRDLNVFVYTDQERVTIENFFNGTIPIKVTEDTVNQKRVSVALDKTYGEQLKGTVVIKDKDVTNQLPSVSDVGEKVVKALDVDWNAYYGFPNAAAFSASSHDAYEFDVVTHNNFIVHKQTDNNCWVNAICLALQRLKPTWKFPGVKSLWDAFLTRKTAGFVHMLYHISGLTKGQPGDAELTLHKLVDLMSSDSAVTVTHTTACDKCAKVETFTGPVVAAPLLVCGTDEICVHGVHVNVKVTSIRGTVAITSLIGPVVGDVIDATGYICYTGLNSRGHYTYYDNRNGLMVDADKAYHFEKNLLQVTTAIASNFVANTPKKEIMPKTQAKESKAKESNTARVFSEVEENPKNIVRKEKLLAIESGVDYTITTLGKYADVFFMAGDKILRFLLEVFKYLLVVFMCLRKSKMPKVKVKPPHVFRNLGAKVRTLNYVRQLNKPALWRYIKLVLLLIALYHFFYLFVSIPVVHKLACSGSVQAYSNSSFVKSEVCGNSILCKACLASYDELADFDHLQVSWDYKSDPLWNRVIQLSYFIFLAVFGNNYVRCLLMYFVSQYLNLWLSYFGYVKYSWFLHVVNFESISVEFVIIVVVFKAVLALKHIFLPCNNPSCKTCSKIARQTRIPIQVVVNGSMKTVYVHANGTGKLCKKHNFYCKNCDSYGFDHTFICDEIVRDLSNSIKQTVYATDRSYQEVTKVECTDGFYRFYVGEEFTAYDYDVKHKKYSSQEVLKTMFLLDDFIVYNPSGSSLASVRNVCVYFSQLIGRPIKIVNSELLEDLSVDFKGALFNAKKNVIKNSFNVDVSECKNLEECYKLCNLDVTFSTFEMAINNAHRFGILITDRSFNNFWPSKIKPGSSGVSAMDIGKCMTFDAKIVNAKVLTQRGKSVVWLSQDFSTLSSTAQKVLVKTFVEEGVNFSLTFNAVGSDEDLPYERFTESVSAKSGSGFFDVLKQLKQLFWCLVLFITLYGLCSVYSVATQSYIDSAEGYDYMVIKNGVVQSFDDSINCVHNTYKGFAVWFKAKHGFVPTFDKSCPIVLGTVFDLGNMRPIPDVPAYVALVGRSLVFAINAAFGVTNVCYDHTGAAVSKNSYFDTCVFNSACTTLTGIGGTVVYCAKQGLVEGAKLYSELLPDYYYEHASGNMVKIPAIIRSFGLRFVKTQATTYCRVGECTESQAGFCFGGDNWFVYDKEFGDGYICGSSTLGFFKNVFALFNSNMSVVATSGAMLANIVIACLAIAVCYGVLKFKKIFGDCTLLVVMIIVTLVVNNVSYFVTQNTFFMIVYAIIYYFTTRKLAYPGVLDAGFIIAYLNMAPWYVLVLYIMVFLYDSLPSLFKLKVTTNLFEGDKFVGSFESAAMGTFVIDMRSYETLVNSTSLDRIKSYANSFNKYKYYTGSMGEADYRMACYAHLGKALMDYSVSRNDMLYTPPTVSVNSTLQSGLRKMAQPSGVVEPCIVRVAYGNNVLNGLWLGDEVICPRHVIASDTSRVINYENELSSVRLHNFSIAKNNAFLGVVSAKYKGVNLVLKVNQVNPNTPEHKFKSVRPGESFNILACYEGCPGSVYGVNMRSQGTIKGSFIAGTCGSVGYVLENGTLYFVYMHHLELGNGSHVGSNLEGEMYGGYEDQPSMQLEGTNVMSSDNVVAFLYAALINGERWFVTNTSMTLESYNAWAKTNSFTEIVSTDAFNMLAAKTGYSVEKLLECIVRLNKGFGGRTILSYGSLCDEFTPTEVIRQMYGVNLQSGKVKSIFYPMMTAIAILFAFWLEFFMYTPFTWINPTFVSVVLAITTLVSVLLVAGIKHKMLFFMSFVMPSVILATAHNVVWDMTYYESLQVLVENVNTTFLPVDMQGVMLALFCVVVFVICTIRFFTCKQSWFSLFATTIFVMFNIVKLLGMIGEPWTDDHFLLCLVNMLTMLISLTTKDWFVVFASYKVAYYIVVYVMQPAFVQDFGFVKCVSIIYMACGYLFCCYYGILYWVNRFTCMTCGVYQFTVSPAELKYMTANNLSAPKTAYDAMILSFKLMGIGGGRNIKISTVQSKLTEMKCTNVVLLGLLSKMHVESNSKEWNYCVGLHNEINLCDDPDAVLEKLLALIAFFLSKHNTCDLSDLIESYFENTTILQSVASAYAALPSWIAYEKARADLEEAKKNDVSPQLLKQLTKACNIAKSEFEREASVQKKLDKMAEQAAASMYKEARAVDRKSKIVSAMHSLLFGMLKKLDMSSVNTIIEQARNGVLPLSIIPAASATRLIVVTPNLEVLSKVRQENNVHYAGAIWSIVEVKDANGAQVHLKEVTAANELNITWPLSITCERTTKLQNNEILPGKLKEKAVKASATIDGDAYGSGKALMASEGGKSFIYAFIASDSNLKYVKWESNNDVIPIELEAPLRFYVDGVNGPEVKYLYFVKSLNTLRRGAVLGYIGATVRLQAGKPTEHPSNSGLLTLCAFAPDPAKAYVDAVKRGMQPVTNCVKMLSNGAGNGMAITNGVESNTQQDSYGGASVCIYCRCHVEHPAIDGLCRFKGKFVQVPTGTQDPIRFCIENEVCVVCGCWLTNGCMCDRTSIQGTTIDQSYLNECGVLVQLDLEPCNGTDPDHVSRAFDIYNKDVACIGKFLKTNCSRFRNLDKHDAYYVVKRCTKSVMDHEQVCYNDLKDSGVVAEHDFFLYKEGRCEFGNVARKDLTKYTMMDLCYAIRNFDEKNCEVLKEILVTLGACNESFFENKDWFDPVENEAIHEVYARLGPIVANAMLKCVAFCDAIVEKGYIGIITLDNQDLNGNFYDFGDFVKTTPGFGCACVTSYYSYMMPLMGMTSCLESENFVKSDIYGADYKQYDLLAYDFTDHKEKLFHKYFKHWDRTYHPNCSDCTSDECIIHCANFNTLFSMTIPSTAFGPLVRKVHIDGVPVVVTAGYHFKQLGIVWNLDVKLDTMKLSMTDLLRFVTDPTLLVASSPALLDQRTVCFSIAALSTGVTYQTVKPGHFNKDFYDFITERGFFEEGSELTLKHFFFAQGGEAAMTDFNYYRYNRVTVLDICQAQFVYKIVGKYFECYDGGCINAREVVVTNYDKSAGYPLNKFGKARLYYETLSYEEQDALFALTKRNVLPTMTQMNLKYAISGKARARTVGGVSLLSTMTTRQYHQKHLKSIAATRNATVVIGSTKFYGGWDNMLKNLMRDVDNGCLMGWDYPKCDRALPNMIRMASAMILGSKHVGCCTHSDRFYRLSNELAQVLTEVVHCTGGFYFKPGGTTSGDGTTAYANSAFNIFQAVSANVNKLLGVDSNACNNVTVKSIQRKIYDNCYRSSSIDEEFVVEYFSYLRKHFSMMILSDDGVVCYNKDYADLGYVADINAFKATLYYQNNVFMSTSKCWVEPDLSVGPHEFCSQHTLQIVGPDGDYYLPYPDPSRILSAGVFVDDIVKTDNVIMLERYVSLAIDAYPLTKHPKPAYQKVFYTLLDWVKHLQKNLNAGVLDSFSVTMLEEGQDKFWSEEFYASLYEKSTVLQAAGMCVVCGSQTVLRCGDCLRRPLLCTKCAYDHVMGTKHKFIMSITPYVCSFNGCNVNDVTKLFLGGLSYYCMDHKPQLSFPLCANGNVFGLYKSSAVGSEDVEDFNKLAVSDWTNVEDYKLANNVKESLKIFAAETVKAKEESVKSEYAYAILKEVIGPKEIVLQWEASKTKPPLNRNSVFTCFQISKDTKIQLGEFVFEQSEYGSDSVYYKSTSTYKLTPGMIFVLTSHNVSPLKATILVNQEKYNTISKLYPVFNIAEAYNTLVPYYQMIGKQKFTTIQGPPGSGKSHCVIGLGLYYPQARIVYTACSHAAVDALCEKAAKNFNVDRCSRIIPQRIRVDCYTGFKPNNTNAQYLFCTVNALPEASCDIVVVDEVSMCTNYDLSVINSRLSYKHIVYVGDPQQLPAPRTLINKGVLQPQDYNVVTQRVCTLGPDVFLHKCYRCPAEIVKTVSALVYENKFVPVNPESKQCFKMFVKGQVQIESNSSINNKQLEVVKAFLAHNPKWRKAVFISPYNSQNYVARRLLGLQTQTVDSAQGSEYDYVIYTQTSDTQHATNVNRFNVAITRAKVGILCIMCDRTMYENLDFYELKDSKIGLQAKPETCGLFKDCSKSEQYIPPAYATTYMSLSDNFKTSDGLAVNIGTKDVKYANVISYMGFRFEANIPGYHTLFCTRDFAMRNVRAWLGFDVEGAHVCGDNVGTNVPLQLGFSNGVDFVVQTEGCVVTEKGNSIEVVKARAPPGEQFAHLIPLMRKGQPWHIVRRRIVQMVCDYFDGLSDILIFVLWAGGLELTTMRYFVKIGRPQKCECGKSATCYSSSQCVYACFKHALGCDYLYNPYCIDIQQWGYTGSLSMNHHEVCNIHRNEHVASGDAIMTRCLAIHDCFVKRVDWSIVYPFIDNEEKINKAGRIVQSHVMKAALKIFNPAAIHDVGNPKGIRCATTPIPWFCYDRDPINNNVRCLEYDYMVHGQMNGLMLFWNCNVDMYPEFSIVCRFDTRTRSKLSLEGCNGGALYVNNHAFHTPAYDRRAFAKLKPMPFFYYDDSNCELVDGQPNYVPLKSNVCITKCNIGGAVCKKHAALYRAYVEDYNMFMQAGFTIWCPQNFDTYMLWHGFVNSKALQSLENVAFNVVKKGAFTGLKGDLPTAVIADKIMVRDGPTDKCIFTNKTSLPTNVAFELYAKRKLGLTPPLTILRNLGVVATYKFVLWDYEAECPFSNFTKQVCSYTDLDSEVVTCFDNSIAGSFERFTTTKDAVLISNNAVKGLSAIKLQYGFLNDLPVSTVGNKPVTWYIYVRKNGEYVEQIDSYYTHGRTFETFKPRSTMEEDFLSMDTTLFIQKYGLEDYGFEHVVFGDVSKTTIGGMHLLISQVRLAKMGLFSVQEFMTNSDSTLKSCCITYADDPSSKNVCTYMDILLDDFVTIIKSLDLNVVSKVVDVIVDCKAWRWMLWCENSQIKTFYPQLQSAEWNPGYSMPTLYKIQRMCLERCNLYNYGAQVRLPDGITTNVVKYTQLCQYLNTTTVCVPHKMRVLHLGAAGASGVAPGSTVLRRWLPDDAILVDNDLRDYVSDADFSVTGDCTSLYIEDKFDLLISDLYDGSTKSIDGENTSKDGFFTYINGFIKEKLSLGGSAAIKITEFSWNKDLYELIQRFEYWTVFCTSVNTSSSEGFLIGINYLGPYCDKAIVDGNIMHANYIFWRNSTIMALSHNSVLDTPKFKCRCNNALIVNLKEKELNEMVVGLLRKGKLLIRNNGKLLNFGNHLVNVP |
| Enzyme Length | 6709 |
| Uniprot Accession Number | Q98VG9 |
| Absorption | |
| Active Site | ACT_SITE 1117; /note=For PL1-PRO activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU00444; ACT_SITE 1268; /note=For PL1-PRO activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU00444; ACT_SITE 1599; /note=For PL2-PRO activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU00444; ACT_SITE 1752; /note=For PL2-PRO activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU00444; ACT_SITE 2944; /note=For 3CL-PRO activity; ACT_SITE 3047; /note=For 3CL-PRO activity; ACT_SITE 4779; /evidence=ECO:0000255|PROSITE-ProRule:PRU01293; ACT_SITE 4780; /evidence=ECO:0000255|PROSITE-ProRule:PRU01293; ACT_SITE 4781; /evidence=ECO:0000255|PROSITE-ProRule:PRU01293; ACT_SITE 5641; /evidence=ECO:0000255|PROSITE-ProRule:PRU01298; ACT_SITE 5643; /evidence=ECO:0000255|PROSITE-ProRule:PRU01298; ACT_SITE 5742; /evidence=ECO:0000255|PROSITE-ProRule:PRU01298; ACT_SITE 5818; /evidence=ECO:0000255|PROSITE-ProRule:PRU01298; ACT_SITE 5823; /evidence=ECO:0000255|PROSITE-ProRule:PRU01298; ACT_SITE 6296; /evidence=ECO:0000255|PROSITE-ProRule:PRU01303; ACT_SITE 6311; /evidence=ECO:0000255|PROSITE-ProRule:PRU01303; ACT_SITE 6352; /evidence=ECO:0000255|PROSITE-ProRule:PRU01303; ACT_SITE 6454; /evidence=ECO:0000255|PROSITE-ProRule:PRU01300; ACT_SITE 6538; /evidence=ECO:0000255|PROSITE-ProRule:PRU01300; ACT_SITE 6578; /evidence=ECO:0000255|PROSITE-ProRule:PRU01300; ACT_SITE 6611; /evidence=ECO:0000255|PROSITE-ProRule:PRU01300 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: [Non-structural protein 3]: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; CATALYTIC ACTIVITY: [RNA-directed RNA polymerase]: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; CATALYTIC ACTIVITY: [Helicase]: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; CATALYTIC ACTIVITY: [Helicase]: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; CATALYTIC ACTIVITY: [Putative 2'-O-methyl transferase]: Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyl-ribonucleoside) in mRNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:67020, Rhea:RHEA-COMP:17167, Rhea:RHEA-COMP:17168, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156461, ChEBI:CHEBI:167609; EC=2.1.1.57; Evidence={ECO:0000250|UniProtKB:P0C6X7}; CATALYTIC ACTIVITY: [Uridylate-specific endoribonuclease]: Reaction=uridylyl-uridylyl-ribonucleotide-RNA = a 3'-end uridylyl-2',3'-cyclophospho-uridine-RNA + a 5'-end dephospho-ribonucleoside-RNA; Xref=Rhea:RHEA:67732, Rhea:RHEA-COMP:13936, Rhea:RHEA-COMP:17334, Rhea:RHEA-COMP:17335, ChEBI:CHEBI:138284, ChEBI:CHEBI:173079, ChEBI:CHEBI:173080; Evidence={ECO:0000250|UniProtKB:P0C6X7}; |
| DNA Binding | |
| EC Number | 3.4.19.12; 3.4.22.-; 3.4.22.-; 2.7.7.48; 3.6.4.12; 3.6.4.13; 3.1.13.-; 4.6.1.-; 2.1.1.57 |
| Enzyme Function | FUNCTION: The replicase polyprotein of coronaviruses is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products.; FUNCTION: The papain-like proteinase 1 (PLP1) and papain-like proteinase 2 (PLP2) are responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PLP2 possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. PLP2 also antagonizes innate immune induction of type I interferon by blocking the nuclear translocation of host IRF-3 (By similarity). {ECO:0000250}.; FUNCTION: [3C-like proteinase]: Responsible for the majority of cleavages as it cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln-CMK. Also contains an ADP-ribose-1''-phosphate (ADRP)-binding function (By similarity). {ECO:0000255|PROSITE-ProRule:PRU00772}.; FUNCTION: The helicase which contains a zinc finger structure displays RNA and DNA duplex-unwinding activities with 5' to 3' polarity. ATPase activity is strongly stimulated by poly(U), poly(dT), poly(C), poly(dA), but not by poly(G) (By similarity). {ECO:0000250}.; FUNCTION: The exoribonuclease acts on both ssRNA and dsRNA in a 3' to 5' direction. {ECO:0000250}.; FUNCTION: Nsp7-nsp8 hexadecamer may possibly confer processivity to the polymerase, maybe by binding to dsRNA or by producing primers utilized by the latter. {ECO:0000250}.; FUNCTION: Nsp9 is a ssRNA-binding protein. {ECO:0000250}.; FUNCTION: [Uridylate-specific endoribonuclease]: Plays a role in viral transcription/replication and prevents the simultaneous activation of host cell dsRNA sensors, such as MDA5/IFIH1, OAS, and PKR (By similarity). Acts by degrading the 5'-polyuridines generated during replication of the poly(A) region of viral genomic and subgenomic RNAs. Catalyzes a two-step reaction in which a 2'3'-cyclic phosphate (2'3'-cP) is first generated by 2'-O transesterification, which is then hydrolyzed to a 3'-phosphate (3'-P) (By similarity). If not degraded, poly(U) RNA would hybridize with poly(A) RNA tails and activate host dsRNA sensors (By similarity). {ECO:0000250|UniProtKB:P0C6X7}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 5235..5242; /note=ATP; /evidence=ECO:0000250 |
| Features | Active site (21); Alternative sequence (1); Beta strand (32); Chain (17); Compositional bias (1); Domain (24); Frameshift (1); Helix (35); Metal binding (32); Mutagenesis (13); Natural variant (10); Nucleotide binding (1); Region (7); Sequence conflict (1); Site (15); Transmembrane (15); Turn (4); Zinc finger (4) |
| Keywords | 3D-structure;ATP-binding;Activation of host autophagy by virus;Endonuclease;Exonuclease;Helicase;Host cytoplasm;Host membrane;Host-virus interaction;Hydrolase;Inhibition of host IRF3 by virus;Inhibition of host RLR pathway by virus;Inhibition of host innate immune response by virus;Lyase;Membrane;Metal-binding;Methyltransferase;Modulation of host ubiquitin pathway by viral deubiquitinase;Modulation of host ubiquitin pathway by virus;Nuclease;Nucleotide-binding;Nucleotidyltransferase;Protease;RNA-binding;RNA-directed RNA polymerase;Reference proteome;Repeat;Ribosomal frameshifting;Thiol protease;Transferase;Transmembrane;Transmembrane helix;Ubl conjugation pathway;Viral RNA replication;Viral immunoevasion;Zinc;Zinc-finger |
| Interact With | Q98VG9 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: [Non-structural protein 3]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: [Non-structural protein 4]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: [Non-structural protein 6]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}.; SUBCELLULAR LOCATION: [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}.; SUBCELLULAR LOCATION: [Non-structural protein 9]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}.; SUBCELLULAR LOCATION: [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). {ECO:0000250}.; SUBCELLULAR LOCATION: [Helicase]: Host endoplasmic reticulum-Golgi intermediate compartment {ECO:0000305}. Note=The helicase interacts with the N protein in membranous complexes and colocalizes with sites of synthesis of new viral RNA. {ECO:0000250}.; SUBCELLULAR LOCATION: [Uridylate-specific endoribonuclease]: Host cytoplasm, host perinuclear region {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | PTM: Specific enzymatic cleavages in vivo by its own proteases yield mature proteins. 3CL-PRO and PL-PRO proteinases are autocatalytically processed (By similarity). {ECO:0000250}. |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (8) |
| Cross Reference PDB | 3ETI; 3EW5; 3GZF; 3JZT; 3UB0; 4ZRO; 5EU8; 6LP9; |
| Mapped Pubmed ID | 19622868; 19966415; 22318142; 26592814; 26656689; 32731335; |
| Motif | |
| Gene Encoded By | |
| Mass | 751,196 |
| Kinetics | |
| Metal Binding | METAL 3962; /note=Zinc 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU01297; METAL 3965; /note=Zinc 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU01297; METAL 3971; /note=Zinc 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU01297; METAL 3978; /note=Zinc 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU01297; METAL 4004; /note=Zinc 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU01297; METAL 4007; /note=Zinc 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU01297; METAL 4015; /note=Zinc 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU01297; METAL 4017; /note=Zinc 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU01297; METAL 4957; /note=Zinc 3; /evidence=ECO:0000255|PROSITE-ProRule:PRU00986; METAL 4960; /note=Zinc 3; /evidence=ECO:0000255|PROSITE-ProRule:PRU00986; METAL 4968; /note=Zinc 4; /evidence=ECO:0000255|PROSITE-ProRule:PRU00986; METAL 4971; /note=Zinc 3; /evidence=ECO:0000255|PROSITE-ProRule:PRU00986; METAL 4978; /note=Zinc 3; /evidence=ECO:0000255|PROSITE-ProRule:PRU00986; METAL 4981; /note=Zinc 4; /evidence=ECO:0000255|PROSITE-ProRule:PRU00986; METAL 4985; /note=Zinc 4; /evidence=ECO:0000255|PROSITE-ProRule:PRU00986; METAL 4991; /note=Zinc 4; /evidence=ECO:0000255|PROSITE-ProRule:PRU00986; METAL 5002; /note=Zinc 5; /evidence=ECO:0000255|PROSITE-ProRule:PRU00986; METAL 5007; /note=Zinc 5; /evidence=ECO:0000255|PROSITE-ProRule:PRU00986; METAL 5024; /note=Zinc 5; /evidence=ECO:0000255|PROSITE-ProRule:PRU00986; METAL 5027; /note=Zinc 5; /evidence=ECO:0000255|PROSITE-ProRule:PRU00986; METAL 5758; /note=Zinc 6; /evidence=ECO:0000255|PROSITE-ProRule:PRU01298; METAL 5760; /note=Zinc 6; /evidence=ECO:0000255|PROSITE-ProRule:PRU01298; METAL 5776; /note=Zinc 6; /evidence=ECO:0000255|PROSITE-ProRule:PRU01298; METAL 5779; /note=Zinc 6; /evidence=ECO:0000255|PROSITE-ProRule:PRU01298; METAL 5807; /note=Zinc 7; /evidence=ECO:0000255|PROSITE-ProRule:PRU01298; METAL 5811; /note=Zinc 7; /evidence=ECO:0000255|PROSITE-ProRule:PRU01298; METAL 5814; /note=Zinc 7; /evidence=ECO:0000255|PROSITE-ProRule:PRU01298; METAL 5829; /note=Zinc 7; /evidence=ECO:0000255|PROSITE-ProRule:PRU01298; METAL 5996; /note=Zinc 8; /evidence=ECO:0000255|PROSITE-ProRule:PRU01299; METAL 6013; /note=Zinc 8; /evidence=ECO:0000255|PROSITE-ProRule:PRU01299; METAL 6024; /note=Zinc 8; /evidence=ECO:0000255|PROSITE-ProRule:PRU01299; METAL 6027; /note=Zinc 8; /evidence=ECO:0000255|PROSITE-ProRule:PRU01299 |
| Rhea ID | RHEA:21248; RHEA:13065; RHEA:67020; RHEA:67732 |
| Cross Reference Brenda |