| IED ID | IndEnz0002001211 |
| Enzyme Type ID | protease001211 |
| Protein Name |
Replicase polyprotein 1ab pp1ab ORF1ab polyprotein Cleaved into: Non-structural protein 1 nsp1 p9 ; Non-structural protein 2 nsp2 p87 ; 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 p34 ; Non-structural protein 6 nsp6 ; Non-structural protein 7 nsp7 p5 ; Non-structural protein 8 nsp8 p23 ; Non-structural protein 9 nsp9 p12 ; Non-structural protein 10 nsp10 Growth factor-like peptide GFL p14 ; RNA-directed RNA polymerase Pol RdRp EC 2.7.7.48 nsp12 p100 ; Helicase Hel EC 3.6.4.12 EC 3.6.4.13 nsp13 p66 p66-HEL ; Exoribonuclease ExoN EC 3.1.13.- nsp14 ; Uridylate-specific endoribonuclease EC 4.6.1.- NendoU nsp15 p41 ; Putative 2'-O-methyl transferase EC 2.1.1.57 nsp16 |
| Gene Name | rep 1a-1b |
| Organism | Porcine transmissible gastroenteritis coronavirus (strain Purdue) (TGEV) |
| Taxonomic Lineage | Viruses Riboviria Orthornavirae Pisuviricota Pisoniviricetes Nidovirales Cornidovirineae Coronaviridae Orthocoronavirinae Alphacoronavirus Tegacovirus Alphacoronavirus 1 Transmissible gastroenteritis virus Porcine transmissible gastroenteritis coronavirus (strain Purdue) (TGEV) |
| Enzyme Sequence | MSSKQFKILVNEDYQVNVPSLPIRDVLQEIKYCYRNGFEGYVFVPEYCRDLVDCDRKDHYVIGVLGNGVSDLKPVLLTEPSVMLQGFIVRANCNGVLEDFDLKIARTGRGAIYVDQYMCGADGKPVIEGDFKDYFGDEDIIEFEGEEYHCAWTTVRDEKPLNQQTLFTIQEIQYNLDIPHKLPNCATRHVAPPVKKNSKIVLSEDYKKLYDIFGSPFMGNGDCLSKCFDTLHFIAATLRCPCGSESSGVGDWTGFKTACCGLSGKVKGVTLGDIKPGDAVVTSMSAGKGVKFFANCVLQYAGDVEGVSIWKVIKTFTVDETVCTPGFEGELNDFIKPESKSLVACSVKRAFITGDIDDAVHDCIITGKLDLSTNLFGNVGLLFKKTPWFVQKCGALFVDAWKVVEELCGSLTLTYKQIYEVVASLCTSAFTIVNYKPTFVVPDNRVKDLVDKCVKVLVKAFDVFTQIITIAGIEAKCFVLGAKYLLFNNALVKLVSVKILGKKQKGLECAFFATSLVGATVNVTPKRTETATISLNKVDDVVAPGEGYIVIVGDMAFYKSGEYYFMMSSPNFVLTNNVFKAVKVPSYDIVYDVDNDTKSKMIAKLGSSFEYDGDIDAAIVKVNELLIEFRQQSLCFRAFKDDKSIFVEAYFKKYKMPACLAKHIGLWNIIKKDSCKRGFLNLFNHLNELEDIKETNIQAIKNILCPDPLLDLDYGAIWYNCMPGCSDPSVLGSVQLLIGNGVKVVCDGCKGFANQLSKGYNKLCNAARNDIEIGGIPFSTFKTPTNTFIEMTDAIYSVIEQGKALSFRDADVPVVDNGTISTADWSEPILLEPAEYVKPKNNGNVIVIAGYTFYKDEDEHFYPYGFGKIVQRMYNKMGGGDKTVSFSEEVDVQEIAPVTRVKLEFEFDNEIVTGVLERAIGTRYKFTGTTWEEFEESISEELDAIFDTLANQGVELEGYFIYDTCGGFDIKNPDGIMISQYDINITADEKSEVSASSEEEEVESVEEDPENEIVEASEGAEGTSSQEEVETVEVADITSTEEDVDIVEVSAKDDPWAAAVDVQEAEQFNPSLPPFKTTNLNGKIILKQGDNNCWINACCYQLQAFDFFNNEAWEKFKKGDVMDFVNLCYAATTLARGHSGDAEYLLELMLNDYSTAKIVLAAKCGCGEKEIVLERAVFKLTPLKESFNYGVCGDCMQVNTCRFLSVEGSGVFVHDILSKQTPEAMFVVKPVMHAVYTGTTQNGHYMVDDIEHGYCVDGMGIKPLKKRCYTSTLFINANVMTRAEKPKQEFKVEKVEQQPIVEENKSSIEKEEIQSPKNDDLILPFYKAGKLSFYQGALDVLINFLEPDVIVNAANGDLKHMGGVARAIDVFTGGKLTERSKDYLKKNKSIAPGNAVFFENVIEHLSVLNAVGPRNGDSRVEAKLCNVYKAIAKCEGKILTPLISVGIFNVRLETSLQCLLKTVNDRGLNVFVYTDQERQTIENFFSCSIPVNVTEDNVNHERVSVSFDKTYGEQLKGTVVIKDKDVTNQLPSAFDVGQKVIKAIDIDWQAHYGFRDAAAFSASSHDAYKFEVVTHSNFIVHKQTDNNCWINAICLALQRLKPQWKFPGVRGLWNEFLERKTQGFVHMLYHISGVKKGEPGDAELMLHKLGDLMDNDCEIIVTHTTACDKCAKVEKFVGPVVAAPLAIHGTDETCVHGVSVNVKVTQIKGTVAITSLIGPIIGEVLEATGYICYSGSNRNGHYTYYDNRNGLVVDAEKAYHFNRDLLQVTTAIASNFVVKKPQAEERPKNCAFNKVAASPKIVQEQKLLAIESGANYALTEFGRYADMFFMAGDKILRLLLEVFKYLLVLFMCLRSTKMPKVKVKPPLAFKDFGAKVRTLNYMRQLNKPSVWRYAKLVLLLIAIYNFFYLFVSIPVVHKLTCNGAVQAYKNSSFIKSAVCGNSILCKACLASYDELADFQHLQVTWDFKSDPLWNRLVQLSYFAFLAVFGNNYVRCFLMYFVSQYLNLWLSYFGYVEYSWFLHVVNFESISAEFVIVVIVVKAVLALKHIVFACSNPSCKTCSRTARQTRIPIQVVVNGSMKTVYVHANGTGKFCKKHNFYCKNCDSYGFENTFICDEIVRDLSNSVKQTVYATDRSHQEVTKVECSDGFYRFYVGDEFTSYDYDVKHKKYSSQEVLKSMLLLDDFIVYSPSGSALANVRNACVYFSQLIGKPIKIVNSDLLEDLSVDFKGALFNAKKNVIKNSFNVDVSECKNLDECYRACNLNVSFSTFEMAVNNAHRFGILITDRSFNNFWPSKVKPGSSGVSAMDIGKCMTSDAKIVNAKVLTQRGKSVVWLSQDFAALSSTAQKVLVKTFVEEGVNFSLTFNAVGSDDDLPYERFTESVSPKSGSGFFDVITQLKQIVILVFVFIFICGLCSVYSVATQSYIESAEGYDYMVIKNGIVQPFDDTISCVHNTYKGFGDWFKAKYGFIPTFGKSCPIVVGTVFDLENMRPIPDVPAYVSIVGRSLVFAINAAFGVTNMCYDHTGNAVSKDSYFDTCVFNTACTTLTGLGGTIVYCAKQGLVEGAKLYSDLMPDYYYEHASGNMVKLPAIIRGLGLRFVKTQATTYCRVGECIDSKAGFCFGGDNWFVYDNEFGNGYICGNSVLGFFKNVFKLFNSNMSVVATSGAMLVNIIIACLAIAMCYGVLKFKKIFGDCTFLIVMIIVTLVVNNVSYFVTQNTFFMIIYAIVYYFITRKLAYPGILDAGFIIAYINMAPWYVITAYILVFLYDSLPSLFKLKVSTNLFEGDKFVGNFESAAMGTFVIDMRSYETIVNSTSIARIKSYANSFNKYKYYTGSMGEADYRMACYAHLGKALMDYSVNRTDMLYTPPTVSVNSTLQSGLRKMAQPSGLVEPCIVRVSYGNNVLNGLWLGDEVICPRHVIASDTTRVINYENEMSSVRLHNFSVSKNNVFLGVVSARYKGVNLVLKVNQVNPNTPEHKFKSIKAGESFNILACYEGCPGSVYGVNMRSQGTIKGSFIAGTCGSVGYVLENGILYFVYMHHLELGNGSHVGSNFEGEMYGGYEDQPSMQLEGTNVMSSDNVVAFLYAALINGERWFVTNTSMSLESYNTWAKTNSFTELSSTDAFSMLAAKTGQSVEKLLDSIVRLNKGFGGRTILSYGSLCDEFTPTEVIRQMYGVNLQAGKVKSFFYPIMTAMTILFAFWLEFFMYTPFTWINPTFVSIVLAVTTLISTVFVSGIKHKMLFFMSFVLPSVILVTAHNLFWDFSYYESLQSIVENTNTMFLPVDMQGVMLTVFCFIVFVTYSVRFFTCKQSWFSLAVTTILVIFNMVKIFGTSDEPWTENQIAFCFVNMLTMIVSLTTKDWMVVIASYRIAYYIVVCVMPSAFVSDFGFMKCISIVYMACGYLFCCYYGILYWVNRFTCMTCGVYQFTVSAAELKYMTANNLSAPKNAYDAMILSAKLIGVGGKRNIKISTVQSKLTEMKCTNVVLLGLLSKMHVESNSKEWNYCVGLHNEINLCDDPEIVLEKLLALIAFFLSKHNTCDLSELIESYFENTTILQSVASAYAALPSWIALEKARADLEEAKKNDVSPQILKQLTKAFNIAKSDFEREASVQKKLDKMAEQAAASMYKEARAVDRKSKIVSAMHSLLFGMLKKLDMSSVNTIIDQARNGVLPLSIIPAASATRLVVITPSLEVFSKIRQENNVHYAGAIWTIVEVKDANGSHVHLKEVTAANELNLTWPLSITCERTTKLQNNEIMPGKLKERAVRASATLDGEAFGSGKALMASESGKSFMYAFIASDNNLKYVKWESNNDIIPIELEAPLRFYVDGANGPEVKYLYFVKNLNTLRRGAVLGYIGATVRLQAGKPTEHPSNSSLLTLCAFSPDPAKAYVDAVKRGMQPVNNCVKMLSNGAGNGMAVTNGVEANTQQDSYGGASVCIYCRCHVEHPAIDGLCRYKGKFVQIPTGTQDPIRFCIENEVCVVCGCWLNNGCMCDRTSMQSFTVDQSYLNRVRGSSAARLEPCNGTDPDHVSRAFDIYNKDVACIGKFLKTNCSRFRNLDKHDAYYIVKRCTKTVMDHEQVCYNDLKDSGAVAEHDFFTYKEGRCEFGNVARRNLTKYTMMDLCYAIRNFDEKNCEVLKEILVTVGACTEEFFENKDWFDPVENEAIHEVYAKLGPIVANAMLKCVAFCDAIVEKGYIGVITLDNQDLNGNFYDFGDFVKTAPGFGCACVTSYYSYMMPLMGMTSCLESENFVKSDIYGSDYKQYDLLAYDFTEHKEYLFQKYFKYWDRTYHPNCSDCTSDECIIHCANFNTLFSMTIPMTAFGPLVRKVHIDGVPVVVTAGYHFKQLGIVWNLDVKLDTMKLSMTDLLRFVTDPTLLVASSPALLDQRTVCFSIAALSTGITYQTVKPGHFNKDFYDFITERGFFEEGSELTLKHFFFAQGGEAAMTDFNYYRYNRVTVLDICQAQFVYKIVGKYFECYDGGCINAREVVVTNYDKSAGYPLNKFGKARLYYETLSYEEQDALFALTKRNVLPTMTQMNLKYAISGKARARTVGGVSLLSTMTTRQYHQKHLKSIAATRNATVVIGSTKFYGGWDNMLKNLMRDVDNGCLMGWDYPKCDRALPNMIRMASAMILGSKHVGCCTHNDRFYRLSNELAQVLTEVVHCTGGFYFKPGGTTSGDGTTAYANSAFNIFQAVSANVNKLLGVDSNACNNVTVKSIQRKIYDNCYRSSSIDEEFVVEYFSYLRKHFSMMILSDDGVVCYNKDYADLGYVADINAFKATLYYQNNVFMSTSKCWVEPDLSVGPHEFCSQHTLQIVGPDGDYYLPYPDPSRILSAGVFVDDIVKTDNVIMLERYVSLAIDAYPLTKHPKPAYQKVFYTLLDWVKHLQKNLNAGVLDSFSVTMLEEGQDKFWSEEFYASLYEKSTVLQAAGMCVVCGSQTVLRCGDCLRRPLLCTKCAYDHVMGTKHKFIMSITPYVCSFNGCNVNDVTKLFLGGLSYYCMNHKPQLSFPLCANGNVFGLYKSSAVGSEAVEDFNKLAVSDWTNVEDYKLANNVKESLKIFAAETVKAKEESVKSEYAYAVLKEVIGPKEIVLQWEASKTKPPLNRNSVFTCFQISKDTKIQLGEFVFEQSEYGSDSVYYKSTSTYKLTPGMIFVLTSHNVSPLKAPILVNQEKYNTISKLYPVFNIAEAYNTLVPYYQMIGKQKFTTIQGPPGSGKSHCVIGLGLYYPQARIVYTACSHAAVDALCEKAAKNFNVDRCSRIIPQRIRVDCYTGFKPNNTNAQYLFCTVNALPEASCDIVVVDEVSMCTNYDLSVINSRLSYKHIVYVGDPQQLPAPRTLINKGVLQPQDYNVVTKRMCTLGPDVFLHKCYRCPAEIVKTVSALVYENKFVPVNPESKQCFKMFVKGQVQIESNSSINNKQLEVVKAFLAHNPKWRKAVFISPYNSQNYVARRLLGLQTQTVDSAQGSEYDYVIYTQTSDTQHATNVNRFNVAITRAKVGILCIMCDRTMYENLDFYELKDSKIGLQAKPETCGLFKDCSKSEQYIPPAYATTYMSLSDNFKTSDGLAVNIGTKDVKYANVISYMGFRFEANIPGYHTLFCTRDFAMRNVRAWLGFDVEGAHVCGDNVGTNVPLQLGFSNGVDFVVQTEGCVITEKGNSIEVVKARAPPGEQFAHLIPLMRKGQPWHIVRRRIVQMVCDYFDGLSDILIFVLWAGGLELTTMRYFVKIGRPQKCECGKSATCYSSSQSVYACFKHALGCDYLYNPYCIDIQQWGYTGSLSMNHHEVCNIHRNEHVASGDAIMTRCLAIHDCFVKRVDWSIVYPFIDNEEKINKAGRIVQSHVMKAALKIFNPAAIHDVGNPKGIRCATTPIPWFCYDRDPINNNVRCLDYDYMVHGQMNGLMLFWNCNVDMYPEFSIVCRFDTRTRSKLSLEGCNGGALYVNNHAFHTPAYDRRAFAKLKPMPFFYYDDSNCELVDGQPNYVPLKSNVCITKCNIGGAVCKKHAALYRAYVEDYNIFMQAGFTIWCPQNFDTYMLWHGFVNSKALQSLENVAFNVVKKGAFTGLKGDLPTAVIADKIMVRDGPTDKCIFTNKTSLPTNVAFELYAKRKLGLTPPLTILRNLGVVATYKFVLWDYEAERPFSNFTKQVCSYTDLDSEVVTCFDNSIAGSFERFTTTRDAVLISNNAVKGLSAIKLQYGLLNDLPVSTVGNKPVTWYIYVRKNGEYVEQIDSYYTQGRTFETFKPRSTMEEDFLSMDTTLFIQKYGLEDYGFEHVVFGDVSKTTIGGMHLLISQVRLAKMGLFSVQEFMNNSDSTLKSCCITYADDPSSKNVCTYMDILLDDFVTIIKSLDLNVVSKVVDVIVDCKAWRWMLWCENSHIKTFYPQLQSAEWNPGYSMPTLYKIQRMCLERCNLYNYGAQVKLPDGITTNVVKYTQLCQYLNTTTLCVPHKMRVLHLGAAGASGVAPGSTVLRRWLPDDAILVDNDLRDYVSDADFSVTGDCTSLYIEDKFDLLVSDLYDGSTKSIDGENTSKDGFFTYINGFIKEKLSLGGSVAIKITEFSWNKDLYELIQRFEYWTVFCTSVNTSSSEGFLIGINYLGPYCDKAIVDGNIMHANYIFWRNSTIMALSHNSVLDTPKFKCRCNNALIVNLKEKELNEMVIGLLRKGKLLIRNNGKLLNFGNHFVNTP |
| Enzyme Length | 6684 |
| Uniprot Accession Number | P0C6Y5 |
| Absorption | |
| Active Site | ACT_SITE 1093; /note=For PL1-PRO activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU00444; ACT_SITE 1244; /note=For PL1-PRO activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU00444; ACT_SITE 1588; /note=For PL2-PRO activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU00444; ACT_SITE 1741; /note=For PL2-PRO activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU00444; ACT_SITE 2919; /note=For 3CL-PRO activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU00772; ACT_SITE 3022; /note=For 3CL-PRO activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU00772; ACT_SITE 4754; /evidence=ECO:0000255|PROSITE-ProRule:PRU01293; ACT_SITE 4755; /evidence=ECO:0000255|PROSITE-ProRule:PRU01293; ACT_SITE 4756; /evidence=ECO:0000255|PROSITE-ProRule:PRU01293; ACT_SITE 5616; /evidence=ECO:0000255|PROSITE-ProRule:PRU01298; ACT_SITE 5618; /evidence=ECO:0000255|PROSITE-ProRule:PRU01298; ACT_SITE 5717; /evidence=ECO:0000255|PROSITE-ProRule:PRU01298; ACT_SITE 5793; /evidence=ECO:0000255|PROSITE-ProRule:PRU01298; ACT_SITE 5798; /evidence=ECO:0000255|PROSITE-ProRule:PRU01298; ACT_SITE 6271; /evidence=ECO:0000255|PROSITE-ProRule:PRU01303; ACT_SITE 6286; /evidence=ECO:0000255|PROSITE-ProRule:PRU01303; ACT_SITE 6327; /evidence=ECO:0000255|PROSITE-ProRule:PRU01303; ACT_SITE 6429; /evidence=ECO:0000255|PROSITE-ProRule:PRU01300; ACT_SITE 6513; /evidence=ECO:0000255|PROSITE-ProRule:PRU01300; ACT_SITE 6553; /evidence=ECO:0000255|PROSITE-ProRule:PRU01300; ACT_SITE 6586; /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. {ECO:0000269|PubMed:21047955}.; FUNCTION: Non-structural protein 1 inhibits host translation. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response. {ECO:0000269|PubMed:21047955}.; 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-|-[SAGC]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln-CMK. {ECO:0000269|PubMed:21047955}.; 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). {ECO:0000269|PubMed:21047955}.; 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 5210..5217; /note=ATP; /evidence=ECO:0000250 |
| Features | Active site (21); Beta strand (20); Chain (15); Compositional bias (2); Domain (24); Helix (13); Metal binding (32); Natural variant (8); Nucleotide binding (1); Region (6); Site (14); Transmembrane (19); Turn (2); Zinc finger (3) |
| 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 | P0C6Y5 |
| 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 is autocatalytically processed. {ECO:0000269|PubMed:11842254}. |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (4) |
| Cross Reference PDB | 1LVO; 1P9U; 2AMP; 6IVC; |
| Mapped Pubmed ID | 16128623; 31350335; |
| Motif | |
| Gene Encoded By | |
| Mass | 748,912 |
| Kinetics | |
| Metal Binding | METAL 3937; /note=Zinc 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU01297; METAL 3940; /note=Zinc 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU01297; METAL 3946; /note=Zinc 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU01297; METAL 3953; /note=Zinc 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU01297; METAL 3979; /note=Zinc 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU01297; METAL 3982; /note=Zinc 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU01297; METAL 3990; /note=Zinc 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU01297; METAL 3992; /note=Zinc 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU01297; METAL 4932; /note=Zinc 3; /evidence=ECO:0000255|PROSITE-ProRule:PRU00986; METAL 4935; /note=Zinc 3; /evidence=ECO:0000255|PROSITE-ProRule:PRU00986; METAL 4943; /note=Zinc 4; /evidence=ECO:0000255|PROSITE-ProRule:PRU00986; METAL 4946; /note=Zinc 3; /evidence=ECO:0000255|PROSITE-ProRule:PRU00986; METAL 4953; /note=Zinc 3; /evidence=ECO:0000255|PROSITE-ProRule:PRU00986; METAL 4956; /note=Zinc 4; /evidence=ECO:0000255|PROSITE-ProRule:PRU00986; METAL 4960; /note=Zinc 4; /evidence=ECO:0000255|PROSITE-ProRule:PRU00986; METAL 4966; /note=Zinc 4; /evidence=ECO:0000255|PROSITE-ProRule:PRU00986; METAL 4977; /note=Zinc 5; /evidence=ECO:0000255|PROSITE-ProRule:PRU00986; METAL 4982; /note=Zinc 5; /evidence=ECO:0000255|PROSITE-ProRule:PRU00986; METAL 4999; /note=Zinc 5; /evidence=ECO:0000255|PROSITE-ProRule:PRU00986; METAL 5002; /note=Zinc 5; /evidence=ECO:0000255|PROSITE-ProRule:PRU00986; METAL 5733; /note=Zinc 6; /evidence=ECO:0000255|PROSITE-ProRule:PRU01298; METAL 5735; /note=Zinc 6; /evidence=ECO:0000255|PROSITE-ProRule:PRU01298; METAL 5751; /note=Zinc 6; /evidence=ECO:0000255|PROSITE-ProRule:PRU01298; METAL 5754; /note=Zinc 6; /evidence=ECO:0000255|PROSITE-ProRule:PRU01298; METAL 5782; /note=Zinc 7; /evidence=ECO:0000255|PROSITE-ProRule:PRU01298; METAL 5786; /note=Zinc 7; /evidence=ECO:0000255|PROSITE-ProRule:PRU01298; METAL 5789; /note=Zinc 7; /evidence=ECO:0000255|PROSITE-ProRule:PRU01298; METAL 5804; /note=Zinc 7; /evidence=ECO:0000255|PROSITE-ProRule:PRU01298; METAL 5971; /note=Zinc 8; /evidence=ECO:0000255|PROSITE-ProRule:PRU01299; METAL 5988; /note=Zinc 8; /evidence=ECO:0000255|PROSITE-ProRule:PRU01299; METAL 5999; /note=Zinc 8; /evidence=ECO:0000255|PROSITE-ProRule:PRU01299; METAL 6002; /note=Zinc 8; /evidence=ECO:0000255|PROSITE-ProRule:PRU01299 |
| Rhea ID | RHEA:21248; RHEA:13065; RHEA:67020; RHEA:67732 |
| Cross Reference Brenda |