| IED ID | IndEnz0002013907 |
| Enzyme Type ID | protease013907 |
| Protein Name |
Replicase polyprotein 1a pp1a ORF1a polyprotein Cleaved into: Host translation inhibitor nsp1 Leader protein Non-structural protein 1 nsp1 ; Non-structural protein 2 nsp2 p65 homolog ; Papain-like protease nsp3 EC 3.4.19.12 EC 3.4.22.- Non-structural protein 3 nsp3 PL2-PRO Papain-like proteinase PL-PRO ; Non-structural protein 4 nsp4 ; 3C-like proteinase nsp5 3CL-PRO 3CLp EC 3.4.22.69 Main protease Mpro Non-structural protein 5 nsp5 SARS coronavirus main proteinase ; 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 Growth factor-like peptide GFL ; Non-structural protein 11 nsp11 |
| Gene Name | |
| Organism | Severe acute respiratory syndrome coronavirus 2 (2019-nCoV) (SARS-CoV-2) |
| Taxonomic Lineage | Viruses Riboviria Orthornavirae Pisuviricota Pisoniviricetes Nidovirales Cornidovirineae Coronaviridae Orthocoronavirinae Betacoronavirus Sarbecovirus Severe acute respiratory syndrome coronavirus (SARS-CoV) Severe acute respiratory syndrome coronavirus 2 (2019-nCoV) (SARS-CoV-2) |
| Enzyme Sequence | MESLVPGFNEKTHVQLSLPVLQVRDVLVRGFGDSVEEVLSEARQHLKDGTCGLVEVEKGVLPQLEQPYVFIKRSDARTAPHGHVMVELVAELEGIQYGRSGETLGVLVPHVGEIPVAYRKVLLRKNGNKGAGGHSYGADLKSFDLGDELGTDPYEDFQENWNTKHSSGVTRELMRELNGGAYTRYVDNNFCGPDGYPLECIKDLLARAGKASCTLSEQLDFIDTKRGVYCCREHEHEIAWYTERSEKSYELQTPFEIKLAKKFDTFNGECPNFVFPLNSIIKTIQPRVEKKKLDGFMGRIRSVYPVASPNECNQMCLSTLMKCDHCGETSWQTGDFVKATCEFCGTENLTKEGATTCGYLPQNAVVKIYCPACHNSEVGPEHSLAEYHNESGLKTILRKGGRTIAFGGCVFSYVGCHNKCAYWVPRASANIGCNHTGVVGEGSEGLNDNLLEILQKEKVNINIVGDFKLNEEIAIILASFSASTSAFVETVKGLDYKAFKQIVESCGNFKVTKGKAKKGAWNIGEQKSILSPLYAFASEAARVVRSIFSRTLETAQNSVRVLQKAAITILDGISQYSLRLIDAMMFTSDLATNNLVVMAYITGGVVQLTSQWLTNIFGTVYEKLKPVLDWLEEKFKEGVEFLRDGWEIVKFISTCACEIVGGQIVTCAKEIKESVQTFFKLVNKFLALCADSIIIGGAKLKALNLGETFVTHSKGLYRKCVKSREETGLLMPLKAPKEIIFLEGETLPTEVLTEEVVLKTGDLQPLEQPTSEAVEAPLVGTPVCINGLMLLEIKDTEKYCALAPNMMVTNNTFTLKGGAPTKVTFGDDTVIEVQGYKSVNITFELDERIDKVLNEKCSAYTVELGTEVNEFACVVADAVIKTLQPVSELLTPLGIDLDEWSMATYYLFDESGEFKLASHMYCSFYPPDEDEEEGDCEEEEFEPSTQYEYGTEDDYQGKPLEFGATSAALQPEEEQEEDWLDDDSQQTVGQQDGSEDNQTTTIQTIVEVQPQLEMELTPVVQTIEVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGSCVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNLYDKLVSSFLEMKSEKQVEQKIAEIPKEEVKPFITESKPSVEQRKQDDKKIKACVEEVTTTLEETKFLTENLLLYIDINGNLHPDSATLVSDIDITFLKKDAPYIVGDVVQEGVLTAVVIPTKKAGGTTEMLAKALRKVPTDNYITTYPGQGLNGYTVEEAKTVLKKCKSAFYILPSIISNEKQEILGTVSWNLREMLAHAEETRKLMPVCVETKAIVSTIQRKYKGIKIQEGVVDYGARFYFYTSKTTVASLINTLNDLNETLVTMPLGYVTHGLNLEEAARYMRSLKVPATVSVSSPDAVTAYNGYLTSSSKTPEEHFIETISLAGSYKDWSYSGQSTQLGIEFLKRGDKSVYYTSNPTTFHLDGEVITFDNLKTLLSLREVRTIKVFTTVDNINLHTQVVDMSMTYGQQFGPTYLDGADVTKIKPHNSHEGKTFYVLPNDDTLRVEAFEYYHTTDPSFLGRYMSALNHTKKWKYPQVNGLTSIKWADNNCYLATALLTLQQIELKFNPPALQDAYYRARAGEAANFCALILAYCNKTVGELGDVRETMSYLFQHANLDSCKRVLNVVCKTCGQQQTTLKGVEAVMYMGTLSYEQFKKGVQIPCTCGKQATKYLVQQESPFVMMSAPPAQYELKHGTFTCASEYTGNYQCGHYKHITSKETLYCIDGALLTKSSEYKGPITDVFYKENSYTTTIKPVTYKLDGVVCTEIDPKLDNYYKKDNSYFTEQPIDLVPNQPYPNASFDNFKFVCDNIKFADDLNQLTGYKKPASRELKVTFFPDLNGDVVAIDYKHYTPSFKKGAKLLHKPIVWHVNNATNKATYKPNTWCIRCLWSTKPVETSNSFDVLKSEDAQGMDNLACEDLKPVSEEVVENPTIQKDVLECNVKTTEVVGDIILKPANNSLKITEEVGHTDLMAAYVDNSSLTIKKPNELSRVLGLKTLATHGLAAVNSVPWDTIANYAKPFLNKVVSTTTNIVTRCLNRVCTNYMPYFFTLLLQLCTFTRSTNSRIKASMPTTIAKNTVKSVGKFCLEASFNYLKSPNFSKLINIIIWFLLLSVCLGSLIYSTAALGVLMSNLGMPSYCTGYREGYLNSTNVTIATYCTGSIPCSVCLSGLDSLDTYPSLETIQITISSFKWDLTAFGLVAEWFLAYILFTRFFYVLGLAAIMQLFFSYFAVHFISNSWLMWLIINLVQMAPISAMVRMYIFFASFYYVWKSYVHVVDGCNSSTCMMCYKRNRATRVECTTIVNGVRRSFYVYANGGKGFCKLHNWNCVNCDTFCAGSTFISDEVARDLSLQFKRPINPTDQSSYIVDSVTVKNGSIHLYFDKAGQKTYERHSLSHFVNLDNLRANNTKGSLPINVIVFDGKSKCEESSAKSASVYYSQLMCQPILLLDQALVSDVGDSAEVAVKMFDAYVNTFSSTFNVPMEKLKTLVATAEAELAKNVSLDNVLSTFISAARQGFVDSDVETKDVVECLKLSHQSDIEVTGDSCNNYMLTYNKVENMTPRDLGACIDCSARHINAQVAKSHNIALIWNVKDFMSLSEQLRKQIRSAAKKNNLPFKLTCATTRQVVNVVTTKIALKGGKIVNNWLKQLIKVTLVFLFVAAIFYLITPVHVMSKHTDFSSEIIGYKAIDGGVTRDIASTDTCFANKHADFDTWFSQRGGSYTNDKACPLIAAVITREVGFVVPGLPGTILRTTNGDFLHFLPRVFSAVGNICYTPSKLIEYTDFATSACVLAAECTIFKDASGKPVPYCYDTNVLEGSVAYESLRPDTRYVLMDGSIIQFPNTYLEGSVRVVTTFDSEYCRHGTCERSEAGVCVSTSGRWVLNNDYYRSLPGVFCGVDAVNLLTNMFTPLIQPIGALDISASIVAGGIVAIVVTCLAYYFMRFRRAFGEYSHVVAFNTLLFLMSFTVLCLTPVYSFLPGVYSVIYLYLTFYLTNDVSFLAHIQWMVMFTPLVPFWITIAYIICISTKHFYWFFSNYLKRRVVFNGVSFSTFEEAALCTFLLNKEMYLKLRSDVLLPLTQYNRYLALYNKYKYFSGAMDTTSYREAACCHLAKALNDFSNSGSDVLYQPPQTSITSAVLQSGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGHSMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFCYMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYEPLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQSAVKRTIKGTHHWLLLTILTSLLVLVQSTQWSLFFFLYENAFLPFAMGIIAMSAFAMMFVKHKHAFLCLFLLPSLATVAYFNMVYMPASWVMRIMTWLDMVDTSLSGFKLKDCVMYASAVVLLILMTARTVYDDGARRVWTLMNVLTLVYKVYYGNALDQAISMWALIISVTSNYSGVVTTVMFLARGIVFMCVEYCPIFFITGNTLQCIMLVYCFLGYFCTCYFGLFCLLNRYFRLTLGVYDYLVSTQEFRYMNSQGLLPPKNSIDAFKLNIKLLGVGGKPCIKVATVQSKMSDVKCTSVVLLSVLQQLRVESSSKLWAQCVQLHNDILLAKDTTEAFEKMVSLLSVLLSMQGAVDINKLCEEMLDNRATLQAIASEFSSLPSYAAFATAQEAYEQAVANGDSEVVLKKLKKSLNVAKSEFDRDAAMQRKLEKMADQAMTQMYKQARSEDKRAKVTSAMQTMLFTMLRKLDNDALNNIINNARDGCVPLNIIPLTTAAKLMVVIPDYNTYKNTCDGTTFTYASALWEIQQVVDADSKIVQLSEISMDNSPNLAWPLIVTALRANSAVKLQNNELSPVALRQMSCAAGTTQTACTDDNALAYYNTTKGGRFVLALLSDLQDLKWARFPKSDGTGTIYTELEPPCRFVTDTPKGPKVKYLYFIKGLNNLNRGMVLGSLAATVRLQAGNATEVPANSTVLSFCAFAVDAAKAYKDYLASGGQPITNCVKMLCTHTGTGQAITVTPEANMDQESFGGASCCLYCRCHIDHPNPKGFCDLKGKYVQIPTTCANDPVGFTLKNTVCTVCGMWKGYGCSCDQLREPMLQSADAQSFLNGFAV |
| Enzyme Length | 4405 |
| Uniprot Accession Number | P0DTC1 |
| Absorption | |
| Active Site | ACT_SITE 1674; /note="For PL1-PRO activity"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00444, ECO:0000269|PubMed:32726803"; ACT_SITE 1835; /note="For PL2-PRO activity"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"; ACT_SITE 3304; /note="For 3CL-PRO activity"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00772, ECO:0000269|PubMed:32198291"; ACT_SITE 3408; /note="For 3CL-PRO activity"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00772, ECO:0000269|PubMed:32198291" |
| Activity Regulation | ACTIVITY REGULATION: [Papain-like protease nsp3]: Inhibited in vitro by GRL-0617. {ECO:0000269|PubMed:32726803}.; ACTIVITY REGULATION: [3C-like proteinase nsp5]: Inhibited by pyridone-containing alpha-ketoamides compounds 13a and 13b. In turn, alpha-ketoamide 13b (tert-butyl (1-((S)-1-(((S)-4-(benzylamino)-3,4-dioxo-1-((S)-2-oxopyrrolidin-3-yl)butan-2-yl)amino)-3-cyclopropyl-1-oxopropan-2-yl)-2-oxo-1,2-dihydropyridin-3-yl)carbamate) inhibits SARS-CoV-2 replication in human lung cells (PubMed:32198291). Inhibited ex vivo by michael acceptor inhibitor N3 (PubMed:32272481). Inhibited ex vivo by compound 11a and 11b (PubMed:32321856). {ECO:0000269|PubMed:32198291, ECO:0000269|PubMed:32272481, ECO:0000269|PubMed:32321856}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: [Papain-like protease nsp3]: 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; Evidence={ECO:0000269|PubMed:32726803}; CATALYTIC ACTIVITY: [3C-like proteinase nsp5]: Reaction=TSAVLQ-|-SGFRK-NH(2) and SGVTFQ-|-GKFKK the two peptides corresponding to the two self-cleavage sites of the SARS 3C-like proteinase are the two most reactive peptide substrates. The enzyme exhibits a strong preference for substrates containing Gln at P1 position and Leu at P2 position.; EC=3.4.22.69; Evidence={ECO:0000269|PubMed:32198291, ECO:0000269|PubMed:32272481, ECO:0000269|PubMed:32321856}; |
| DNA Binding | |
| EC Number | 3.4.19.12; 3.4.22.-; 3.4.22.69 |
| Enzyme Function | FUNCTION: [Replicase polyprotein 1a]: Multifunctional protein involved in the transcription and replication of viral RNAs. Contains the proteinases responsible for the cleavages of the polyprotein. {ECO:0000250|UniProtKB:P0C6X7}.; FUNCTION: [Host translation inhibitor nsp1]: Inhibits host translation by associating with the open head conformation of the 40S subunit (PubMed:33479166, PubMed:33080218, PubMed:32680882, PubMed:32908316). The C-terminus binds to and obstructs ribosomal mRNA entry tunnel (PubMed:33479166, PubMed:33080218, PubMed:32680882, PubMed:32908316). Thereby inhibits antiviral response triggered by innate immunity or interferons (PubMed:33080218, PubMed:32680882, PubMed:32979938). The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation (By similarity). Viral mRNAs less susceptible to nsp1-mediated inhibition of translation, because of their 5'-end leader sequence (PubMed:32908316, PubMed:33080218). {ECO:0000250|UniProtKB:P0C6X7, ECO:0000269|PubMed:32680882, ECO:0000269|PubMed:32908316, ECO:0000269|PubMed:32979938, ECO:0000269|PubMed:33080218, ECO:0000269|PubMed:33479166}.; FUNCTION: [Non-structural protein 2]: May play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2. Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses. {ECO:0000250|UniProtKB:P0C6X7}.; FUNCTION: [Papain-like protease nsp3]: Responsible for the cleavages located at the N-terminus of the replicase polyprotein. Participates together with nsp4 in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication (By similarity). Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3 (PubMed:32733001). Prevents also host NF-kappa-B signaling (By similarity). In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates (PubMed:32726803). Cleaves preferentially ISG15 from antiviral protein IFIH1 (MDA5), but not DDX58 (RIG-I) (PubMed:33727702). Can play a role in host ADP-ribosylation by ADP-ribose (PubMed:32578982). {ECO:0000250|UniProtKB:P0C6X7, ECO:0000269|PubMed:32578982, ECO:0000269|PubMed:32726803, ECO:0000269|PubMed:32733001, ECO:0000269|PubMed:33727702}.; FUNCTION: [Non-structural protein 4]: Participates in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication. {ECO:0000250|UniProtKB:P0C6X7}.; FUNCTION: [3C-like proteinase nsp5]: Cleaves the C-terminus of replicase polyprotein at 11 sites (PubMed:32321856). Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN] (PubMed:32198291, PubMed:32272481). Also able to bind an ADP-ribose-1''-phosphate (ADRP) (By similarity) (PubMed:32198291, PubMed:32272481). {ECO:0000250|UniProtKB:P0C6X7, ECO:0000269|PubMed:32198291, ECO:0000269|PubMed:32272481, ECO:0000269|PubMed:32321856}.; FUNCTION: [Non-structural protein 6]: Plays a role in the initial induction of autophagosomes from host reticulum endoplasmic (By similarity). Later, limits the expansion of these phagosomes that are no longer able to deliver viral components to lysosomes (By similarity). Binds to host TBK1 without affecting TBK1 phosphorylation; the interaction with TBK1 decreases IRF3 phosphorylation, which leads to reduced IFN-beta production (PubMed:32979938). {ECO:0000250|UniProtKB:P0C6X7, ECO:0000269|PubMed:32979938}.; FUNCTION: [Non-structural protein 7]: Plays a role in viral RNA synthesis (PubMed:32358203, PubMed:32277040, PubMed:32438371, PubMed:32526208). Forms a hexadecamer with nsp8 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers (By similarity). {ECO:0000250|UniProtKB:P0C6X7, ECO:0000269|PubMed:32277040, ECO:0000269|PubMed:32358203, ECO:0000269|PubMed:32438371, ECO:0000269|PubMed:32526208}.; FUNCTION: [Non-structural protein 8]: Plays a role in viral RNA synthesis (PubMed:32358203, PubMed:32277040, PubMed:32438371, PubMed:32526208). Forms a hexadecamer with nsp7 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers (By similarity). Interacts with ribosome signal recognition particle RNA (SRP) (PubMed:33080218). Together with NSP9, suppress protein integration into the cell membrane, thereby disrupting host immune defenses (PubMed:33080218). {ECO:0000250|UniProtKB:P0C6X7, ECO:0000269|PubMed:32277040, ECO:0000269|PubMed:32358203, ECO:0000269|PubMed:32438371, ECO:0000269|PubMed:32526208, ECO:0000269|PubMed:33080218}.; FUNCTION: [Non-structural protein 9]: May participate in viral replication by acting as a ssRNA-binding protein (By similarity). Interacts with ribosome signal recognition particle RNA (SRP) (PubMed:33080218). Together with NSP9, suppress protein integration into the cell membrane, thereby disrupting host immune defenses (PubMed:33080218). {ECO:0000250|UniProtKB:P0C6X7, ECO:0000269|PubMed:33080218}.; FUNCTION: [Non-structural protein 10]: Plays a pivotal role in viral transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16 2'-O-methyltransferase activities. Therefore plays an essential role in viral mRNAs cap methylation. {ECO:0000250|UniProtKB:P0C6X7}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (4); Beta strand (20); Chain (12); Compositional bias (2); Domain (16); Helix (18); Metal binding (8); Mutagenesis (12); Natural variant (33); Region (2); Site (10); Transmembrane (16); Turn (3); Zinc finger (1) |
| Keywords | 3D-structure;Activation of host autophagy by virus;Decay of host mRNAs by virus;Endonuclease;Eukaryotic host gene expression shutoff by virus;Eukaryotic host translation shutoff by virus;Host Golgi apparatus;Host cytoplasm;Host endoplasmic reticulum;Host endosome;Host gene expression shutoff by virus;Host mRNA suppression by virus;Host membrane;Host-virus interaction;Hydrolase;Inhibition of host IRF3 by virus;Inhibition of host ISG15 by virus;Inhibition of host RLR pathway by virus;Inhibition of host innate immune response by virus;Inhibition of host interferon signaling pathway by virus;Membrane;Metal-binding;Modulation of host ubiquitin pathway by viral deubiquitinase;Modulation of host ubiquitin pathway by virus;Nuclease;Protease;RNA-binding;Reference proteome;Repeat;Ribosomal frameshifting;Thiol protease;Transmembrane;Transmembrane helix;Ubl conjugation pathway;Viral immunoevasion;Zinc;Zinc-finger |
| Interact With | O75347 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: [Host translation inhibitor nsp1]: Host cytoplasm {ECO:0000269|PubMed:33060197}.; SUBCELLULAR LOCATION: [Non-structural protein 2]: Host cytoplasm {ECO:0000269|PubMed:33060197}. Host endosome {ECO:0000269|PubMed:33060197}.; SUBCELLULAR LOCATION: [Papain-like protease nsp3]: Host membrane {ECO:0000250|UniProtKB:P0C6X7}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P0C6X7}. Host cytoplasm {ECO:0000250|UniProtKB:P0C6X7}.; SUBCELLULAR LOCATION: [Non-structural protein 4]: Host membrane {ECO:0000250|UniProtKB:P0C6X7}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P0C6X7}. Host cytoplasm {ECO:0000250|UniProtKB:P0C6X7}. Note=Localizes in virally-induced cytoplasmic double-membrane vesicles. {ECO:0000250|UniProtKB:P0C6X7}.; SUBCELLULAR LOCATION: [3C-like proteinase nsp5]: Host cytoplasm {ECO:0000269|PubMed:33060197}. Host Golgi apparatus {ECO:0000269|PubMed:33060197}.; SUBCELLULAR LOCATION: [Non-structural protein 6]: Host membrane {ECO:0000250|UniProtKB:P0C6X7}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P0C6X7}.; SUBCELLULAR LOCATION: [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P0C6X9}. Host cytoplasm {ECO:0000269|PubMed:33060197}. Host endoplasmic reticulum {ECO:0000269|PubMed:33060197}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. {ECO:0000250|UniProtKB:P0C6X9}.; SUBCELLULAR LOCATION: [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P0C6X9}. Host cytoplasm {ECO:0000269|PubMed:33060197, ECO:0000269|PubMed:33080218}. Host endoplasmic reticulum {ECO:0000269|PubMed:33060197}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. {ECO:0000250|UniProtKB:P0C6X9}.; SUBCELLULAR LOCATION: [Non-structural protein 9]: Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P0C6X9}. Host cytoplasm {ECO:0000269|PubMed:33060197, ECO:0000269|PubMed:33080218}. Host endoplasmic reticulum {ECO:0000269|PubMed:33060197}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. {ECO:0000250|UniProtKB:P0C6X9}.; SUBCELLULAR LOCATION: [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P0C6X9}. Host cytoplasm {ECO:0000269|PubMed:33060197}. Host endoplasmic reticulum {ECO:0000269|PubMed:33060197}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. {ECO:0000250|UniProtKB:P0C6X9}. |
| 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. {ECO:0000250|UniProtKB:P0C6X7}. |
| Signal Peptide | |
| Structure 3D | Electron microscopy (3); X-ray crystallography (49) |
| Cross Reference PDB | 6Y2E; 6Y2F; 6Y2G; 6YHU; 6YYT; 7BV2; 7C33; 7CZ4; 7D3I; 7D47; 7D64; 7D6H; 7DCD; 7DJR; 7DK1; 7DPP; 7DPU; 7DPV; 7E35; 7EIN; 7EIZ; 7EXM; 7FAY; 7FAZ; 7JIR; 7JIT; 7JIV; 7JIW; 7JN2; 7JRN; 7KOJ; 7KOK; 7KOL; 7KRX; 7M1Y; 7NT1; 7NT2; 7NT3; 7NTV; 7NUK; 7NW2; 7OFS; 7OFT; 7OFU; 7P51; 7RBR; 7RBS; 7RZC; 7SDR; 7SGU; 7SGV; 7SGW; |
| Mapped Pubmed ID | 32535228; 32946224; 33531496; 33594727; 33602867; 33979649; 34097796; 34109016; 34131140; 34143953; 34174194; 34341772; 34398430; 34570415; |
| Motif | |
| Gene Encoded By | |
| Mass | 489,989 |
| Kinetics | |
| Metal Binding | METAL 4327; /note=Zinc 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU01297; METAL 4330; /note=Zinc 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU01297; METAL 4336; /note=Zinc 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU01297; METAL 4343; /note=Zinc 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU01297; METAL 4370; /note=Zinc 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU01297; METAL 4373; /note=Zinc 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU01297; METAL 4381; /note=Zinc 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU01297; METAL 4383; /note=Zinc 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU01297 |
| Rhea ID | |
| Cross Reference Brenda |