| IED ID | IndEnz0002013903 |
| Enzyme Type ID | protease013903 |
| 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 PL-PRO EC 3.4.19.12 EC 3.4.22.- Non-structural protein 3 nsp3 PL2-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 | 1a |
| Organism | Severe acute respiratory syndrome coronavirus (SARS-CoV) |
| Taxonomic Lineage | Viruses Riboviria Orthornavirae Pisuviricota Pisoniviricetes Nidovirales Cornidovirineae Coronaviridae Orthocoronavirinae Betacoronavirus Sarbecovirus Severe acute respiratory syndrome coronavirus (SARS-CoV) |
| Enzyme Sequence | MESLVLGVNEKTHVQLSLPVLQVRDVLVRGFGDSVEEALSEAREHLKNGTCGLVELEKGVLPQLEQPYVFIKRSDALSTNHGHKVVELVAEMDGIQYGRSGITLGVLVPHVGETPIAYRNVLLRKNGNKGAGGHSYGIDLKSYDLGDELGTDPIEDYEQNWNTKHGSGALRELTRELNGGAVTRYVDNNFCGPDGYPLDCIKDFLARAGKSMCTLSEQLDYIESKRGVYCCRDHEHEIAWFTERSDKSYEHQTPFEIKSAKKFDTFKGECPKFVFPLNSKVKVIQPRVEKKKTEGFMGRIRSVYPVASPQECNNMHLSTLMKCNHCDEVSWQTCDFLKATCEHCGTENLVIEGPTTCGYLPTNAVVKMPCPACQDPEIGPEHSVADYHNHSNIETRLRKGGRTRCFGGCVFAYVGCYNKRAYWVPRASADIGSGHTGITGDNVETLNEDLLEILSRERVNINIVGDFHLNEEVAIILASFSASTSAFIDTIKSLDYKSFKTIVESCGNYKVTKGKPVKGAWNIGQQRSVLTPLCGFPSQAAGVIRSIFARTLDAANHSIPDLQRAAVTILDGISEQSLRLVDAMVYTSDLLTNSVIIMAYVTGGLVQQTSQWLSNLLGTTVEKLRPIFEWIEAKLSAGVEFLKDAWEILKFLITGVFDIVKGQIQVASDNIKDCVKCFIDVVNKALEMCIDQVTIAGAKLRSLNLGEVFIAQSKGLYRQCIRGKEQLQLLMPLKAPKEVTFLEGDSHDTVLTSEEVVLKNGELEALETPVDSFTNGAIVGTPVCVNGLMLLEIKDKEQYCALSPGLLATNNVFRLKGGAPIKGVTFGEDTVWEVQGYKNVRITFELDERVDKVLNEKCSVYTVESGTEVTEFACVVAEAVVKTLQPVSDLLTNMGIDLDEWSVATFYLFDDAGEENFSSRMYCSFYPPDEEEEDDAECEEEEIDETCEHEYGTEDDYQGLPLEFGASAETVRVEEEEEEDWLDDTTEQSEIEPEPEPTPEEPVNQFTGYLKLTDNVAIKCVDIVKEAQSANPMVIVNAANIHLKHGGGVAGALNKATNGAMQKESDDYIKLNGPLTVGGSCLLSGHNLAKKCLHVVGPNLNAGEDIQLLKAAYENFNSQDILLAPLLSAGIFGAKPLQSLQVCVQTVRTQVYIAVNDKALYEQVVMDYLDNLKPRVEAPKQEEPPNTEDSKTEEKSVVQKPVDVKPKIKACIDEVTTTLEETKFLTNKLLLFADINGKLYHDSQNMLRGEDMSFLEKDAPYMVGDVITSGDITCVVIPSKKAGGTTEMLSRALKKVPVDEYITTYPGQGCAGYTLEEAKTALKKCKSAFYVLPSEAPNAKEEILGTVSWNLREMLAHAEETRKLMPICMDVRAIMATIQRKYKGIKIQEGIVDYGVRFFFYTSKEPVASIITKLNSLNEPLVTMPIGYVTHGFNLEEAARCMRSLKAPAVVSVSSPDAVTTYNGYLTSSSKTSEEHFVETVSLAGSYRDWSYSGQRTELGVEFLKRGDKIVYHTLESPVEFHLDGEVLSLDKLKSLLSLREVKTIKVFTTVDNTNLHTQLVDMSMTYGQQFGPTYLDGADVTKIKPHVNHEGKTFFVLPSDDTLRSEAFEYYHTLDESFLGRYMSALNHTKKWKFPQVGGLTSIKWADNNCYLSSVLLALQQLEVKFNAPALQEAYYRARAGDAANFCALILAYSNKTVGELGDVRETMTHLLQHANLESAKRVLNVVCKHCGQKTTTLTGVEAVMYMGTLSYDNLKTGVSIPCVCGRDATQYLVQQESSFVMMSAPPAEYKLQQGTFLCANEYTGNYQCGHYTHITAKETLYRIDGAHLTKMSEYKGPVTDVFYKETSYTTTIKPVSYKLDGVTYTEIEPKLDGYYKKDNAYYTEQPIDLVPTQPLPNASFDNFKLTCSNTKFADDLNQMTGFTKPASRELSVTFFPDLNGDVVAIDYRHYSASFKKGAKLLHKPIVWHINQATTKTTFKPNTWCLRCLWSTKPVDTSNSFEVLAVEDTQGMDNLACESQQPTSEEVVENPTIQKEVIECDVKTTEVVGNVILKPSDEGVKVTQELGHEDLMAAYVENTSITIKKPNELSLALGLKTIATHGIAAINSVPWSKILAYVKPFLGQAAITTSNCAKRLAQRVFNNYMPYVFTLLFQLCTFTKSTNSRIRASLPTTIAKNSVKSVAKLCLDAGINYVKSPKFSKLFTIAMWLLLLSICLGSLICVTAAFGVLLSNFGAPSYCNGVRELYLNSSNVTTMDFCEGSFPCSICLSGLDSLDSYPALETIQVTISSYKLDLTILGLAAEWVLAYMLFTKFFYLLGLSAIMQVFFGYFASHFISNSWLMWFIISIVQMAPVSAMVRMYIFFASFYYIWKSYVHIMDGCTSSTCMMCYKRNRATRVECTTIVNGMKRSFYVYANGGRGFCKTHNWNCLNCDTFCTGSTFISDEVARDLSLQFKRPINPTDQSSYIVDSVAVKNGALHLYFDKAGQKTYERHPLSHFVNLDNLRANNTKGSLPINVIVFDGKSKCDESASKSASVYYSQLMCQPILLLDQALVSDVGDSTEVSVKMFDAYVDTFSATFSVPMEKLKALVATAHSELAKGVALDGVLSTFVSAARQGVVDTDVDTKDVIECLKLSHHSDLEVTGDSCNNFMLTYNKVENMTPRDLGACIDCNARHINAQVAKSHNVSLIWNVKDYMSLSEQLRKQIRSAAKKNNIPFRLTCATTRQVVNVITTKISLKGGKIVSTCFKLMLKATLLCVLAALVCYIVMPVHTLSIHDGYTNEIIGYKAIQDGVTRDIISTDDCFANKHAGFDAWFSQRGGSYKNDKSCPVVAAIITREIGFIVPGLPGTVLRAINGDFLHFLPRVFSAVGNICYTPSKLIEYSDFATSACVLAAECTIFKDAMGKPVPYCYDTNLLEGSISYSELRPDTRYVLMDGSIIQFPNTYLEGSVRVVTTFDAEYCRHGTCERSEVGICLSTSGRWVLNNEHYRALSGVFCGVDAMNLIANIFTPLVQPVGALDVSASVVAGGIIAILVTCAAYYFMKFRRVFGEYNHVVAANALLFLMSFTILCLVPAYSFLPGVYSVFYLYLTFYFTNDVSFLAHLQWFAMFSPIVPFWITAIYVFCISLKHCHWFFNNYLRKRVMFNGVTFSTFEEAALCTFLLNKEMYLKLRSETLLPLTQYNRYLALYNKYKYFSGALDTTSYREAACCHLAKALNDFSNSGADVLYQPPQTSITSAVLQSGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDTVYCPRHVICTAEDMLNPNYEDLLIRKSNHSFLVQAGNVQLRVIGHSMQNCLLRLKVDTSNPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNHTIKGSFLNGSCGSVGFNIDYDCVSFCYMHHMELPTGVHAGTDLEGKFYGPFVDRQTAQAAGTDTTITLNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYEPLTQDHVDILGPLSAQTGIAVLDMCAALKELLQNGMNGRTILGSTILEDEFTPFDVVRQCSGVTFQGKFKKIVKGTHHWMLLTFLTSLLILVQSTQWSLFFFVYENAFLPFTLGIMAIAACAMLLVKHKHAFLCLFLLPSLATVAYFNMVYMPASWVMRIMTWLELADTSLSGYRLKDCVMYASALVLLILMTARTVYDDAARRVWTLMNVITLVYKVYYGNALDQAISMWALVISVTSNYSGVVTTIMFLARAIVFVCVEYYPLLFITGNTLQCIMLVYCFLGYCCCCYFGLFCLLNRYFRLTLGVYDYLVSTQEFRYMNSQGLLPPKSSIDAFKLNIKLLGIGGKPCIKVATVQSKMSDVKCTSVVLLSVLQQLRVESSSKLWAQCVQLHNDILLAKDTTEAFEKMVSLLSVLLSMQGAVDINRLCEEMLDNRATLQAIASEFSSLPSYAAYATAQEAYEQAVANGDSEVVLKKLKKSLNVAKSEFDRDAAMQRKLEKMADQAMTQMYKQARSEDKRAKVTSAMQTMLFTMLRKLDNDALNNIINNARDGCVPLNIIPLTTAAKLMVVVPDYGTYKNTCDGNTFTYASALWEIQQVVDADSKIVQLSEINMDNSPNLAWPLIVTALRANSAVKLQNNELSPVALRQMSCAAGTTQTACTDDNALAYYNNSKGGRFVLALLSDHQDLKWARFPKSDGTGTIYTELEPPCRFVTDTPKGPKVKYLYFIKGLNNLNRGMVLGSLAATVRLQAGNATEVPANSTVLSFCAFAVDPAKAYKDYLASGGQPITNCVKMLCTHTGTGQAITVTPEANMDQESFGGASCCLYCRCHIDHPNPKGFCDLKGKYVQIPTTCANDPVGFTLRNTVCTVCGMWKGYGCSCDQLREPLMQSADASTFLNGFAV |
| Enzyme Length | 4382 |
| Uniprot Accession Number | P0C6U8 |
| Absorption | |
| Active Site | ACT_SITE 1651; /note="For PL-PRO activity"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00444"; ACT_SITE 1812; /note="For PL-PRO activity"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00444, ECO:0000269|PubMed:16306590"; ACT_SITE 1826; /note="For PL-PRO activity"; /evidence="ECO:0000269|PubMed:16306590"; ACT_SITE 3281; /note="For 3CL-PRO activity"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00772, ECO:0000269|PubMed:16306590"; ACT_SITE 3385; /note="For 3CL-PRO activity"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00772" |
| Activity Regulation | |
| 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:12917450, ECO:0000269|PubMed:16306590, ECO:0000269|PubMed:17692280}; 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:12917450, ECO:0000269|PubMed:14561748}; |
| DNA Binding | |
| EC Number | 3.4.19.12; 3.4.22.-; 3.4.22.69 |
| Enzyme Function | FUNCTION: [Isoform 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:0000305}.; FUNCTION: [Host translation inhibitor nsp1]: Inhibits host translation by interacting with the 40S ribosomal subunit. The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation. Viral mRNAs are not susceptible to nsp1-mediated endonucleolytic RNA cleavage thanks to the presence of a 5'-end leader sequence and are therefore protected from degradation. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response (PubMed:23035226). May disrupt nuclear pore function by binding and displacing host NUP93 (PubMed:30943371). {ECO:0000269|PubMed:23035226, ECO:0000269|PubMed:30943371}.; 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 (PubMed:19640993). Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses (PubMed:19640993). {ECO:0000269|PubMed:19640993}.; FUNCTION: [Papain-like protease nsp3]: Responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates (PubMed:17692280). Plays a role in host membrane rearrangement that leads to creation of cytoplasmic double-membrane vesicles (DMV) necessary for viral replication (PubMed:23943763). Nsp3, nsp4 and nsp6 together are sufficient to form DMV (PubMed:24410069, PubMed:23943763). Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3 (PubMed:19369340, PubMed:24622840). Prevents also host NF-kappa-B signaling (PubMed:19369340, PubMed:24622840). {ECO:0000269|PubMed:16271890, ECO:0000269|PubMed:17692280, ECO:0000269|PubMed:19369340, ECO:0000269|PubMed:23943763, ECO:0000269|PubMed:24622840, ECO:0000303|PubMed:24410069}.; FUNCTION: [Non-structural protein 4]: Plays a role in host membrane rearrangement that leads to creation of cytoplasmic double-membrane vesicles (DMV) necessary for viral replication (PubMed:23943763, PubMed:24410069). Alone appears incapable to induce membrane curvature, but together with nsp3 is able to induce paired membranes (PubMed:23943763). Nsp3, nsp4 and nsp6 together are sufficient to form DMV (PubMed:23943763, PubMed:24410069). {ECO:0000269|PubMed:23943763, ECO:0000303|PubMed:24410069}.; FUNCTION: [3C-like proteinase nsp5]: Cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN]. Also able to bind an ADP-ribose-1''-phosphate (ADRP). May cleave host ATP6V1G1 thereby modifying host vacuoles intracellular pH. {ECO:0000255|PROSITE-ProRule:PRU00772, ECO:0000269|PubMed:16226257}.; FUNCTION: [Non-structural protein 6]: Plays a role in host membrane rearrangement that leads to creation of cytoplasmic double-membrane vesicles (DMV) necessary for viral replication (PubMed:23943763). Nsp3, nsp4 and nsp6 together are sufficient to form DMV (PubMed:23943763, PubMed:24410069). Plays a role in the initial induction of autophagosomes from host reticulum endoplasmic. Later, limits the expansion of these phagosomes that are no longer able to deliver viral components to lysosomes (PubMed:24991833). {ECO:0000269|PubMed:23943763, ECO:0000269|PubMed:24991833, ECO:0000303|PubMed:24410069}.; FUNCTION: [Non-structural protein 7]: 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. {ECO:0000269|PubMed:22039154}.; FUNCTION: [Non-structural protein 8]: 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. {ECO:0000269|PubMed:22039154}.; FUNCTION: [Non-structural protein 9]: Plays an essential role in viral replication by forming a homodimer that binds single-stranded RNA. {ECO:0000269|PubMed:19153232}.; 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:0000269|PubMed:22635272}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0 for 3C-like proteinase activity. {ECO:0000269|PubMed:14561748}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (5); Beta strand (70); Chain (12); Compositional bias (1); Domain (16); Helix (55); Metal binding (8); Natural variant (63); Region (5); Site (10); Topological domain (13); Transmembrane (12); Turn (12); Zinc finger (3) |
| 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;Lyase;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 | Itself; P0C6U8; P05161; Q64339; Q9GKP4; L5LC70; Q9H074-2; P62992; Itself; P0C6X7 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: [Non-structural protein 2]: Host cytoplasm {ECO:0000250|UniProtKB:P0DTD1}. Host endosome {ECO:0000250|UniProtKB:P0DTD1}.; SUBCELLULAR LOCATION: [Papain-like protease nsp3]: Host membrane {ECO:0000305}; Multi-pass membrane protein. Host cytoplasm {ECO:0000269|PubMed:23943763}.; SUBCELLULAR LOCATION: [Non-structural protein 4]: Host membrane; Multi-pass membrane protein. Host cytoplasm {ECO:0000269|PubMed:23943763}. Note=Localizes in virally-induced cytoplasmic double-membrane vesicles. {ECO:0000269|PubMed:21345958, ECO:0000269|PubMed:23943763}.; SUBCELLULAR LOCATION: [3C-like proteinase nsp5]: Host cytoplasm {ECO:0000250|UniProtKB:P0DTD1}. Host Golgi apparatus {ECO:0000250|UniProtKB:P0DTD1}.; 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}. Host cytoplasm {ECO:0000250|UniProtKB:P0DTD1}. Host endoplasmic reticulum {ECO:0000250|UniProtKB:P0DTD1}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes.; SUBCELLULAR LOCATION: [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000269|PubMed:17532020}. Host cytoplasm {ECO:0000250|UniProtKB:P0DTD1}. Host endoplasmic reticulum {ECO:0000250|UniProtKB:P0DTD1}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes.; SUBCELLULAR LOCATION: [Non-structural protein 9]: Host cytoplasm, host perinuclear region {ECO:0000250}. Host cytoplasm {ECO:0000250|UniProtKB:P0DTD1}. Host endoplasmic reticulum {ECO:0000250|UniProtKB:P0DTD1}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes.; SUBCELLULAR LOCATION: [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250}. Host cytoplasm {ECO:0000250|UniProtKB:P0DTD1}. Host endoplasmic reticulum {ECO:0000250|UniProtKB:P0DTD1}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes. |
| Modified Residue | |
| Post Translational Modification | PTM: [Isoform Replicase polyprotein 1a]: Specific enzymatic cleavages in vivo by its own proteases yield mature proteins (PubMed:32083638, PubMed:16306590, PubMed:12917450, PubMed:15331731, PubMed:15564471). 3C-like proteinase nsp5 liberates nsps 6-11 from the polyprotein (PubMed:32083638). Papain-like and 3C-like proteinases are autocatalytically processed. {ECO:0000269|PubMed:12917450, ECO:0000269|PubMed:15331731, ECO:0000269|PubMed:15564471, ECO:0000269|PubMed:16306590, ECO:0000269|PubMed:32083638}. |
| Signal Peptide | |
| Structure 3D | NMR spectroscopy (10); Electron microscopy (2); X-ray crystallography (110) |
| Cross Reference PDB | 1Q2W; 1QZ8; 1UJ1; 1UK2; 1UK3; 1UK4; 1UW7; 1WOF; 1YSY; 1Z1I; 1Z1J; 2A5A; 2A5I; 2A5K; 2ACF; 2AHM; 2ALV; 2AMD; 2AMQ; 2BX3; 2BX4; 2C3S; 2D2D; 2DUC; 2FAV; 2FE8; 2FYG; 2G9T; 2GA6; 2GDT; 2GRI; 2GT7; 2GT8; 2GTB; 2GX4; 2GZ7; 2GZ8; 2GZ9; 2H2Z; 2HOB; 2HSX; 2IDY; 2KAF; 2KQV; 2KQW; 2KYS; 2LIZ; 2OP9; 2PWX; 2W2G; 2WCT; 2Z3C; 2Z3D; 2Z3E; 2ZU4; 2ZU5; 3ATW; 3AVZ; 3AW0; 3AW1; 3E91; 3EA7; 3EA8; 3EA9; 3EAJ; 3EE7; 3F9E; 3F9F; 3F9G; 3F9H; 3FZD; 3IWM; 3M3S; 3M3T; 3M3V; 3MJ5; 3R24; 3SN8; 3SNA; 3SNB; 3SNC; 3SND; 3SNE; 3SZN; 3TIT; 3TIU; 3TNS; 3TNT; 3V3M; 3VB3; 3VB4; 3VB5; 3VB6; 3VB7; 4HI3; 4M0W; 4MDS; 4MM3; 4OVZ; 4OW0; 5F22; 5Y3E; 5Y3Q; 6LNY; 6LO0; 6NUR; 6NUS; 6W2A; 6XHL; 6XHN; 6XHO; 6Y7M; 6YXJ; 7DQZ; 7EO8; 7K0G; 7K0H; 7LMG; 7LMH; 7LMI; 7LMJ; 7RC1; |
| Mapped Pubmed ID | 14585926; 15788388; 16128623; 16188992; 16219322; 16242152; 16250632; 16511208; 16821128; 16884309; 16912299; 16913704; 17189639; 17196984; 17599357; 17605471; 17728234; 17977841; 19144641; 19409595; 19436709; 20420403; 20493876; 20527968; 20709084; 21203949; 21203988; 21854807; 22014094; 22022266; 23202846; 23231439; 23633583; 24080461; 24531491; 24568342; 24854014; 27799534; 29289665; 31138817; 32198291; 32391184; 32747425; 33054210; 33876849; 34210738; 34347470; 34528437; |
| Motif | |
| Gene Encoded By | |
| Mass | 486,373 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.15 mM for peptide TSAVLQSGFRK-NH(2) {ECO:0000269|PubMed:14561748}; KM=0.58 mM for peptide SGVTFQGKFKK {ECO:0000269|PubMed:14561748}; KM=1.44 mM for peptide ATVRLQAGNAT {ECO:0000269|PubMed:14561748}; Note=The kinetic parameters are studied for the 3C-like proteinase domain.; |
| Metal Binding | METAL 4304; /note=Zinc 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU01297; METAL 4307; /note=Zinc 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU01297; METAL 4313; /note=Zinc 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU01297; METAL 4320; /note=Zinc 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU01297; METAL 4347; /note=Zinc 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU01297; METAL 4350; /note=Zinc 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU01297; METAL 4358; /note=Zinc 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU01297; METAL 4360; /note=Zinc 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU01297 |
| Rhea ID | |
| Cross Reference Brenda |