| IED ID | IndEnz0002001219 |
| Enzyme Type ID | protease001219 |
| Protein Name |
Replicase polyprotein 1ab pp1ab ORF1ab polyprotein Cleaved into: Non-structural protein 2 nsp2 p87 ; Papain-like protease PL-PRO EC 3.4.19.12 EC 3.4.22.- Non-structural protein 3 nsp3 p195 ; Non-structural protein 4 nsp4 Peptide HD2 p41 ; 3C-like proteinase 3CL-PRO 3CLp EC 3.4.22.- Main protease Mpro Non-structural protein 5 nsp5 p33 ; Non-structural protein 6 nsp6 p34 ; Non-structural protein 7 nsp7 p9 ; Non-structural protein 8 nsp8 p24 ; Non-structural protein 9 nsp9 p10 ; Non-structural protein 10 nsp10 Growth factor-like peptide GFL p16 ; 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 p68 ; Proofreading exoribonuclease ExoN EC 2.1.1.- EC 3.1.13.- Guanine-N7 methyltransferase Non-structural protein 14 nsp14 p58 ; Uridylate-specific endoribonuclease EC 4.6.1.- NendoU Non-structural protein 15 nsp15 p39 ; 2'-O-methyl transferase EC 2.1.1.57 Non-structural protein 16 nsp16 p35 |
| Gene Name | rep 1a-1b |
| Organism | Avian infectious bronchitis virus (strain Beaudette CK) (IBV) |
| Taxonomic Lineage | Viruses Riboviria Orthornavirae Pisuviricota Pisoniviricetes Nidovirales Cornidovirineae Coronaviridae Orthocoronavirinae Gammacoronavirus Igacovirus Avian coronavirus Infectious bronchitis virus Avian infectious bronchitis virus (strain Beaudette CK) (IBV) |
| Enzyme Sequence | MASSLKQGVSPKPRDVILVSKDIPEQLCDALFFYTSHNPKDYADAFAVRQKFDRSLQTGKQFKFETVCGLFLLKGVDKITPGVPAKVLKATSKLADLEDIFGVSPLARKYRELLKTACQWSLTVEALDVRAQTLDEIFDPTEILWLQVAAKIHVSSMAMRRLVGEVTAKVMDALGSNLSALFQIVKQQIARIFQKALAIFENVNELPQRIAALKMAFAKCARSITVVVVERTLVVKEFAGTCLASINGAVAKFFEELPNGFMGSKIFTTLAFFKEAAVRVVENIPNAPRGTKGFEVVGNAKGTQVVVRGMRNDLTLLDQKADIPVEPEGWSAILDGHLCYVFRSGDRFYAAPLSGNFALSDVHCCERVVCLSDGVTPEINDGLILAAIYSSFSVSELVTALKKGEPFKFLGHKFVYAKDAAVSFTLAKAATIADVLRLFQSARVIAEDVWSSFTEKSFEFWKLAYGKVRNLEEFVKTYVCKAQMSIVILAAVLGEDIWHLVSQVIYKLGVLFTKVVDFCDKHWKGFCVQLKRAKLIVTETFCVLKGVAQHCFQLLLDAIHSLYKSFKKCALGRIHGDLLFWKGGVHKIVQDGDEIWFDAIDSVDVEDLGVVQEKSIDFEVCDDVTLPENQPGHMVQIEDDGKNYMFFRFKKDENIYYTPMSQLGAINVVCKAGGKTVTFGETTVQEIPPPDVVPIKVSIECCGEPWNTIFKKAYKEPIEVDTDLTVEQLLSVIYEKMCDDLKLFPEAPEPPPFENVALVDKNGKDLDCIKSCHLIYRDYESDDDIEEEDAEECDTDSGEAEECDTNSECEEEDEDTKVLALIQDPASIKYPLPLDEDYSVYNGCIVHKDALDVVNLPSGEETFVVNNCFEGAVKPLPQKVVDVLGDWGEAVDAQEQLCQQEPLQHTFEEPVENSTGSSKTMTEQVVVEDQELPVVEQDQDVVVYTPTDLEVAKETAEEVDEFILIFAVPKEEVVSQKDGAQIKQEPIQVVKPQREKKAKKFKVKPATCEKPKFLEYKTCVGDLTVVIAKALDEFKEFCIVNAANEHMTHGSGVAKAIADFCGLDFVEYCEDYVKKHGPQQRLVTPSFVKGIQCVNNVVGPRHGDNNLHEKLVAAYKNVLVDGVVNYVVPVLSLGIFGVDFKMSIDAMREAFEGCTIRVLLFSLSQEHIDYFDVTCKQKTIYLTEDGVKYRSIVLKPGDSLGQFGQVYAKNKIVFTADDVEDKEILYVPTTDKSILEYYGLDAQKYVIYLQTLAQKWNVQYRDNFLILEWRDGNCWISSAIVLLQAAKIRFKGFLTEAWAKLLGGDPTDFVAWCYASCTAKVGDFSDANWLLANLAEHFDADYTNAFLKKRVSCNCGIKSYELRGLEACIQPVRATNLLHFKTQYSNCPTCGANNTDEVIEASLPYLLLFATDGPATVDCDEDAVGTVVFVGSTNSGHCYTQAAGQAFDNLAKDRKFGKKSPYITAMYTRFAFKNETSLPVAKQSKGKSKSVKEDVSNLATSSKASFDNLTDFEQWYDSNIYESLKVQESPDNFDKYVSFTTKEDSKLPLTLKVRGIKSVVDFRSKDGFIYKLTPDTDENSKAPVYYPVLDAISLKAIWVEGNANFVVGHPNYYSKSLHIPTFWENAENFVKMGDKIGGVTMGLWRAEHLNKPNLERIFNIAKKAIVGSSVVTTQCGKLIGKAATFIADKVGGGVVRNITDSIKGLCGITRGHFERKMSPQFLKTLMFFLFYFLKASVKSVVASYKTVLCKVVLATLLIVWFVYTSNPVMFTGIRVLDFLFEGSLCGPYKDYGKDSFDVLRYCADDFICRVCLHDKDSLHLYKHAYSVEQVYKDAASGFIFNWNWLYLVFLILFVKPVAGFVIICYCVKYLVLNSTVLQTGVCFLDWFVQTVFSHFNFMGAGFYFWLFYKIYIQVHHILYCKDVTCEVCKRVARSNRQEVSVVVGGRKQIVHVYTNSGYNFCKRHNWYCRNCDDYGHQNTFMSPEVAGELSEKLKRHVKPTAYAYHVVDEACLVDDFVNLKYKAATPGKDSASSAVKCFSVTDFLKKAVFLKEALKCEQISNDGFIVCNTQSAHALEEAKNAAIYYAQYLCKPILILDQALYEQLVVEPVSKSVIDKVCSILSSIISVDTAALNYKAGTLRDALLSITKDEEAVDMAIFCHNHDVDYTGDGFTNVIPSYGIDTGKLTPRDRGFLINADASIANLRVKNAPPVVWKFSELIKLSDSCLKYLISATVKSGVRFFITKSGAKQVIACHTQKLLVEKKAGGIVSGTFKCFKSYFKWLLIFYILFTACCSGYYYMEVSKSFVHPMYDVNSTLHVEGFKVIDKGVLREIVPEDTCFSNKFVNFDAFWGRPYDNSRNCPIVTAVIDGDGTVATGVPGFVSWVMDGVMFIHMTQTERKPWYIPTWFNREIVGYTQDSIITEGSFYTSIALFSARCLYLTASNTPQLYCFNGDNDAPGALPFGSIIPHRVYFQPNGVRLIVPQQILHTPYVVKFVSDSYCRGSVCEYTRPGYCVSLNPQWVLFNDEYTSKPGVFCGSTVRELMFSMVSTFFTGVNPNIYMQLATMFLILVVVVLIFAMVIKFQGVFKAYATTVFITMLVWVINAFILCVHSYNSVLAVILLVLYCYASLVTSRNTVIIMHCWLVFTFGLIVPTWLACCYLGFIIYMYTPLFLWCYGTTKNTRKLYDGNEFVGNYDLAAKSTFVIRGSEFVKLTNEIGDKFEAYLSAYARLKYYSGTGSEQDYLQACRAWLAYALDQYRNSGVEIVYTPPRYSIGVSRLQSGFKKLVSPSSAVEKCIVSVSYRGNNLNGLWLGDTIYCPRHVLGKFSGDQWNDVLNLANNHEFEVTTQHGVTLNVVSRRLKGAVLILQTAVANAETPKYKFIKANCGDSFTIACAYGGTVVGLYPVTMRSNGTIRASFLAGACGSVGFNIEKGVVNFFYMHHLELPNALHTGTDLMGEFYGGYVDEEVAQRVPPDNLVTNNIVAWLYAAIISVKESSFSLPKWLESTTVSVDDYNKWAGDNGFTPFSTSTAITKLSAITGVDVCKLLRTIMVKNSQWGGDPILGQYNFEDELTPESVFNQIGGVRLQSSFVRKATSWFWSRCVLACFLFVLCAIVLFTAVPLKFYVYAAVILLMAVLFISFTVKHVMAYMDTFLLPTLITVIIGVCAEVPFIYNTLISQVVIFLSQWYDPVVFDTMVPWMFLPLVLYTAFKCVQGCYMNSFNTSLLMLYQFVKLGFVIYTSSNTLTAYTEGNWELFFELVHTTVLANVSSNSLIGLFVFKCAKWMLYYCNATYLNNYVLMAVMVNCIGWLCTCYFGLYWWVNKVFGLTLGKYNFKVSVDQYRYMCLHKINPPKTVWEVFSTNILIQGIGGDRVLPIATVQAKLSDVKCTTVVLMQLLTKLNVEANSKMHVYLVELHNKILASDDVGECMDNLLGMLITLFCIDSTIDLSEYCDDILKRSTVLQSVTQEFSHIPSYAEYERAKNLYEKVLVDSKNGGVTQQELAAYRKAANIAKSVFDRDLAVQKKLDSMAERAMTTMYKEARVTDRRAKLVSSLHALLFSMLKKIDSEKLNVLFDQASSGVVPLATVPIVCSNKLTLVIPDPETWVKCVEGVHVTYSTVVWNIDTVIDADGTELHPTSTGSGLTYCISGANIAWPLKVNLTRNGHNKVDVVLQNNELMPHGVKTKACVAGVDQAHCSVESKCYYTNISGNSVVAAITSSNPNLKVASFLNEAGNQIYVDLDPPCKFGMKVGVKVEVVYLYFIKNTRSIVRGMVLGAISNVVVLQSKGHETEEVDAVGILSLCSFAVDPADTYCKYVAAGNQPLGNCVKMLTVHNGSGFAITSKPSPTPDQDSYGGASVCLYCRAHIAHPGSVGNLDGRCQFKGSFVQIPTTEKDPVGFCLRNKVCTVCQCWIGYGCQCDSLRQPKSSVQSVAGASDFDKNYLNRVRGSSEARLIPLASGCDPDVVKRAFDVCNKESAGMFQNLKRNCARFQELRDTEDGNLEYLDSYFVVKQTTPSNYEHEKSCYEDLKSEVTADHDFFVFNKNIYNISRQRLTKYTMMDFCYALRHFDPKDCEVLKEILVTYGCIEDYHPKWFEENKDWYDPIENSKYYVMLAKMGPIVRRALLNAIEFGNLMVEKGYVGVITLDNQDLNGKFYDFGDFQKTAPGAGVPVFDTYYSYMMPIIAMTDALAPERYFEYDVHKGYKSYDLLKYDYTEEKQELFQKYFKYWDQEYHPNCRDCSDDRCLIHCANFNILFSTLIPQTSFGNLCRKVFVDGVPFIATCGYHSKELGVIMNQDNTMSFSKMGLSQLMQFVGDPALLVGTSNNLVDLRTSCFSVCALTSGITHQTVKPGHFNKDFYDFAEKAGMFKEGSSIPLKHFFYPQTGNAAINDYDYYRYNRPTMFDICQLLFCLEVTSKYFECYEGGCIPASQVVVNNLDKSAGYPFNKFGKARLYYEMSLEEQDQLFEITKKNVLPTITQMNLKYAISAKNRARTVAGVSILSTMTNRQFHQKILKSIVNTRNASVVIGTTKFYGGWDNMLRNLIQGVEDPILMGWDYPKCDRAMPNLLRIAASLVLARKHTNCCSWSERIYRLYNECAQVLSETVLATGGIYVKPGGTSSGDATTAYANSVFNIIQATSANVARLLSVITRDIVYDNIKSLQYELYQQVYRRVNFDPAFVEKFYSYLCKNFSLMILSDDGVVCYNNTLAKQGLVADISGFREVLYYQNNVFMADSKCWVEPDLEKGPHEFCSQHTMLVEVDGEPKYLPYPDPSRILGACVFVDDVDKTEPVAVMERYIALAIDAYPLVHHENEEYKKVFFVLLAYIRKLYQELSQNMLMDYSFVMDIDKGSKFWEQEFYENMYRAPTTLQSCGVCVVCNSQTILRCGNCIRKPFLCCKCCYDHVMHTDHKNVLSINPYICSQLGCGEADVTKLYLGGMSYFCGNHKPKLSIPLVSNGTVFGIYRANCAGSENVDDFNQLATTNWSIVEPYILANRCSDSLRRFAAETVKATEELHKQQFASAEVREVFSDRELILSWEPGKTRPPLNRNYVFTGYHFTRTSKVQLGDFTFEKGEGKDVVYYKATSTAKLSVGDIFVLTSHNVVSLVAPTLCPQQTFSRFVNLRPNVMVPECFVNNIPLYHLVGKQKRTTVQGPPGSGKSHFAIGLAVYFSSARVVFTACSHAAVDALCEKAFKFLKVDDCTRIVPQRTTVDCFSKFKANDTGKKYIFSTINALPEVSCDILLVDEVSMLTNYELSFINGKINYQYVVYVGDPAQLPAPRTLLNGSLSPKDYNVVTNLMVCVKPDIFLAKCYRCPKEIVDTVSTLVYDGKFIANNPESRECFKVIVNNGNSDVGHESGSAYNTTQLEFVKDFVCRNKQWREAIFISPYNAMNQRAYRMLGLNVQTVDSSQGSEYDYVIFCVTADSQHALNINRFNVALTRAKRGILVVMRQRDELYSALKFTELDSETSLQGTGLFKICNKEFSGVHPAYAVTTKALAATYKVNDELAALVNVEAGSEITYKHLISLLGFKMSVNVEGCHNMFITRDEAIRNVRGWVGFDVEATHACGTNIGTNLPFQVGFSTGADFVVTPEGLVDTSIGNNFEPVNSKAPPGEQFNHLRVLFKSAKPWHVIRPRIVQMLADNLCNVSDCVVFVTWCHGLELTTLRYFVKIGKEQVCSCGSRATTFNSHTQAYACWKHCLGFDFVYNPLLVDIQQWGYSGNLQFNHDLHCNVHGHAHVASVDAIMTRCLAINNAFCQDVNWDLTYPHIANEDEVNSSCRYLQRMYLNACVDALKVNVVYDIGNPKGIKCVRRGDVNFRFYDKNPIVRNVKQFEYDYNQHKDKFADGLCMFWNCNVDCYPDNSLVCRYDTRNLSVFNLPGCNGGSLYVNKHAFYTPKFDRISFRNLKAMPFFFYDSSPCETIQVDGVAQDLVSLATKDCITKCNIGGAVCKKHAQMYAEFVTSYNAAVTAGFTFWVTNKLNPYNLWKSFSALQSIDNIAYNMYKGGHYDAIAGEMPTVITGDKVFVIDQGVEKAVFVNQTTLPTSVAFELYAKRNIRTLPNNRILKGLGVDVTNGFVIWDYANQTPLYRNTVKVCAYTDIEPNGLVVLYDDRYGDYQSFLAADNAVLVSTQCYKRYSYVEIPSNLLVQNGMPLKDGANLYVYKRVNGAFVTLPNTINTQGRSYETFEPRSDIERDFLAMSEESFVERYGKDLGLQHILYGEVDKPQLGGLHTVIGMYRLLRANKLNAKSVTNSDSDVMQNYFVLSDNGSYKQVCTVVDLLLDDFLELLRNILKEYGTNKSKVVTVSIDYHSINFMTWFEDGSIKTCYPQLQSAWTCGYNMPELYKVQNCVMEPCNIPNYGVGITLPSGILMNVAKYTQLCQYLLKTTICVPHNMRVMHFGAGSDKGVAPGSTVLKQWLPEGTLLVDNDIVDYVSDAHVSVLSDCNKYNTEHKFDLVISDMYTDNDSKRKHEGVIANNGNDDVFIYLSSFLRNNLALGGSFAVKVTETSWHEVLYDIAQDCAWWTMFCTAVNASSSEAFLIGVNYLGASEKVKVSGKTLHANYIFWRNCNYLQTSAYSIFDVAKFDLRLKATPVVNLKTEQKTDLVFNLIKCGKLLVRDVGNTSFTSDSFVCTM |
| Enzyme Length | 6629 |
| Uniprot Accession Number | P0C6Y2 |
| Absorption | |
| Active Site | ACT_SITE 1274; /note=For PL-PRO activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU00444; ACT_SITE 1437; /note=For PL-PRO activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU00444; ACT_SITE 1448; /note=For PL-PRO activity; /evidence=ECO:0000250|UniProtKB:P0C6Y1; ACT_SITE 2820; /note=For 3CL-PRO activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU00772; ACT_SITE 2922; /note=For 3CL-PRO activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU00772; ACT_SITE 4695; /evidence=ECO:0000255|PROSITE-ProRule:PRU01293; ACT_SITE 4696; /evidence=ECO:0000255|PROSITE-ProRule:PRU01293; ACT_SITE 4697; /evidence=ECO:0000255|PROSITE-ProRule:PRU01293; ACT_SITE 5557; /evidence=ECO:0000255|PROSITE-ProRule:PRU01298; ACT_SITE 5559; /evidence=ECO:0000255|PROSITE-ProRule:PRU01298; ACT_SITE 5658; /evidence=ECO:0000255|PROSITE-ProRule:PRU01298; ACT_SITE 5734; /evidence=ECO:0000255|PROSITE-ProRule:PRU01298; ACT_SITE 5739; /evidence=ECO:0000255|PROSITE-ProRule:PRU01298; ACT_SITE 6212; /evidence=ECO:0000255|PROSITE-ProRule:PRU01303; ACT_SITE 6227; /evidence=ECO:0000255|PROSITE-ProRule:PRU01303; ACT_SITE 6267; /evidence=ECO:0000255|PROSITE-ProRule:PRU01303; ACT_SITE 6371; /evidence=ECO:0000255|PROSITE-ProRule:PRU01300; ACT_SITE 6455; /evidence=ECO:0000255|PROSITE-ProRule:PRU01300; ACT_SITE 6499; /evidence=ECO:0000255|PROSITE-ProRule:PRU01300; ACT_SITE 6532; /evidence=ECO:0000255|PROSITE-ProRule:PRU01300 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | 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; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539}; 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; Evidence={ECO:0000250|UniProtKB:P0C6X7}; 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; Evidence={ECO:0000250|UniProtKB:P0C6X7}; CATALYTIC ACTIVITY: [Papain-like protease]: 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:0000250|UniProtKB:P0C6Y1}; 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}; CATALYTIC ACTIVITY: [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}; |
| 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; 2.1.1.-; 3.1.13.-; 4.6.1.-; 2.1.1.57 |
| Enzyme Function | FUNCTION: [Isoform Replicase polyprotein 1ab]: Multifunctional protein involved in the transcription and replication of viral RNAs. Contains the proteinases responsible for the cleavages of the polyprotein. {ECO:0000305}.; 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 (By similarity). Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses (By similarity). {ECO:0000250|UniProtKB:P0C6X7}.; FUNCTION: [Papain-like protease]: Responsible for the cleavages located at the N-terminus of the replicase polyprotein (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 (By similarity). {ECO:0000250|UniProtKB:P0C6X7}.; 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 (By similarity). Alone is able to induce paired membranes (By similarity). Coexpression of nsp3 and nsp4 does not result in the formation of DMVs (By similarity). {ECO:0000250|UniProtKB:P0C6Y3}.; 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. {ECO:0000255|PROSITE-ProRule:PRU00772}.; 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:0000250|UniProtKB:P0C6X7}.; 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:0000250|UniProtKB:P0C6X7}.; FUNCTION: [Non-structural protein 9]: Plays an essential role in viral replication by forming a homodimer that binds single-stranded RNA. {ECO:0000250|UniProtKB:P0C6Y3}.; 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 (By similarity). Therefore plays an essential role in viral mRNAs cap methylation (By similarity). {ECO:0000250|UniProtKB:P0C6X7}.; FUNCTION: [RNA-directed RNA polymerase]: Responsible for replication and transcription of the viral RNA genome. {ECO:0000250|UniProtKB:P0C6X7}.; FUNCTION: [Helicase]: Multi-functional protein with a zinc-binding domain in N-terminus displaying RNA and DNA duplex-unwinding activities with 5' to 3' polarity. Activity of helicase is dependent on magnesium. {ECO:0000250|UniProtKB:P0C6X7}.; FUNCTION: [Proofreading exoribonuclease]: Enzyme possessing two different activities: an exoribonuclease activity acting on both ssRNA and dsRNA in a 3' to 5' direction and a N7-guanine methyltransferase activity (By similarity). Acts as a proofreading exoribonuclease for RNA replication, thereby lowering The sensitivity of the virus to RNA mutagens (By similarity). {ECO:0000250|UniProtKB:P0C6X7}.; 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 (By similarity). 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}.; FUNCTION: [2'-O-methyl transferase]: Methyltransferase that mediates mRNA cap 2'-O-ribose methylation to the 5'-cap structure of viral mRNAs. N7-methyl guanosine cap is a prerequisite for binding of nsp16. Therefore plays an essential role in viral mRNAs cap methylation which is essential to evade immune system. {ECO:0000250|UniProtKB:P0C6X7}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 5150..5157; /note=ATP; /evidence=ECO:0000250 |
| Features | Active site (20); Chain (14); Domain (22); Erroneous gene model prediction (1); Metal binding (32); Nucleotide binding (1); Region (6); Site (13); Topological domain (13); Transmembrane (12); Zinc finger (3) |
| Keywords | ATP-binding;Activation of host autophagy by virus;Endonuclease;Exonuclease;Helicase;Host cytoplasm;Host endoplasmic reticulum;Host membrane;Host-virus interaction;Hydrolase;Lyase;Membrane;Metal-binding;Methyltransferase;Nuclease;Nucleotide-binding;Nucleotidyltransferase;Protease;RNA-binding;RNA-directed RNA polymerase;Repeat;Ribosomal frameshifting;Thiol protease;Transferase;Transmembrane;Transmembrane helix;Viral RNA replication;Zinc;Zinc-finger |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: [Papain-like protease]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P0C6Y3}; Multi-pass membrane protein {ECO:0000305}. Host cytoplasm {ECO:0000250|UniProtKB:P0C6X7}. Note=Gammacoronaviruses induce membrane zippering to form zippered endoplasmic reticulum (zER). {ECO:0000250|UniProtKB:P0C6Y3}.; SUBCELLULAR LOCATION: [Non-structural protein 4]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P0C6Y3}; Multi-pass membrane protein {ECO:0000305}. Host cytoplasm {ECO:0000250|UniProtKB:P0C6X7}. Note=Localizes in virally-induced cytoplasmic double-membrane vesicles (By similarity). Gammacoronaviruses induce membrane zippering to form zippered endoplasmic reticulum (zER) (By similarity). {ECO:0000250|UniProtKB:P0C6X7, ECO:0000250|UniProtKB:P0C6Y3}.; SUBCELLULAR LOCATION: [Non-structural protein 6]: Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P0C6Y3}; Multi-pass membrane protein {ECO:0000305}. Note=Gammacoronaviruses induce membrane zippering to form zippered endoplasmic reticulum (zER). {ECO:0000250|UniProtKB:P0C6Y3}.; 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:0000250|UniProtKB:P0C6X7}. 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.; 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.; SUBCELLULAR LOCATION: [Proofreading exoribonuclease]: Host cytoplasm {ECO:0000250|UniProtKB:P0DTD1}. Host endoplasmic reticulum {ECO:0000250|UniProtKB:P0DTD1}.; SUBCELLULAR LOCATION: [Uridylate-specific endoribonuclease]: Host cytoplasm {ECO:0000250|UniProtKB:P0DTD1}. Host endoplasmic reticulum {ECO:0000250|UniProtKB:P0DTD1}. |
| Modified Residue | |
| Post Translational Modification | PTM: [Isoform Replicase polyprotein 1ab]: Specific enzymatic cleavages in vivo by its own proteases yield mature proteins (By similarity). 3C-like proteinase nsp5 liberates nsps 6-16 from the polyprotein (By similarity). Papain-like and 3C-like proteinases are autocatalytically processed. {ECO:0000250|UniProtKB:P0C6X7}.; PTM: [Non-structural protein 4]: N-glycosylated. {ECO:0000250|UniProtKB:P0C6Y1}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 744,566 |
| Kinetics | |
| Metal Binding | METAL 3858; /note=Zinc 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU01297; METAL 3861; /note=Zinc 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU01297; METAL 3867; /note=Zinc 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU01297; METAL 3878; /note=Zinc 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU01297; METAL 3904; /note=Zinc 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU01297; METAL 3907; /note=Zinc 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU01297; METAL 3915; /note=Zinc 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU01297; METAL 3917; /note=Zinc 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU01297; METAL 4873; /note=Zinc 3; /evidence=ECO:0000255|PROSITE-ProRule:PRU00986; METAL 4876; /note=Zinc 3; /evidence=ECO:0000255|PROSITE-ProRule:PRU00986; METAL 4884; /note=Zinc 4; /evidence=ECO:0000255|PROSITE-ProRule:PRU00986; METAL 4887; /note=Zinc 3; /evidence=ECO:0000255|PROSITE-ProRule:PRU00986; METAL 4894; /note=Zinc 3; /evidence=ECO:0000255|PROSITE-ProRule:PRU00986; METAL 4897; /note=Zinc 4; /evidence=ECO:0000255|PROSITE-ProRule:PRU00986; METAL 4901; /note=Zinc 4; /evidence=ECO:0000255|PROSITE-ProRule:PRU00986; METAL 4907; /note=Zinc 4; /evidence=ECO:0000255|PROSITE-ProRule:PRU00986; METAL 4918; /note=Zinc 5; /evidence=ECO:0000255|PROSITE-ProRule:PRU00986; METAL 4923; /note=Zinc 5; /evidence=ECO:0000255|PROSITE-ProRule:PRU00986; METAL 4940; /note=Zinc 5; /evidence=ECO:0000255|PROSITE-ProRule:PRU00986; METAL 4943; /note=Zinc 5; /evidence=ECO:0000255|PROSITE-ProRule:PRU00986; METAL 5674; /note=Zinc 6; /evidence=ECO:0000255|PROSITE-ProRule:PRU01298; METAL 5676; /note=Zinc 6; /evidence=ECO:0000255|PROSITE-ProRule:PRU01298; METAL 5692; /note=Zinc 6; /evidence=ECO:0000255|PROSITE-ProRule:PRU01298; METAL 5695; /note=Zinc 6; /evidence=ECO:0000255|PROSITE-ProRule:PRU01298; METAL 5723; /note=Zinc 7; /evidence=ECO:0000255|PROSITE-ProRule:PRU01298; METAL 5727; /note=Zinc 7; /evidence=ECO:0000255|PROSITE-ProRule:PRU01298; METAL 5730; /note=Zinc 7; /evidence=ECO:0000255|PROSITE-ProRule:PRU01298; METAL 5745; /note=Zinc 7; /evidence=ECO:0000255|PROSITE-ProRule:PRU01298; METAL 5915; /note=Zinc 8; /evidence=ECO:0000255|PROSITE-ProRule:PRU01299; METAL 5935; /note=Zinc 8; /evidence=ECO:0000255|PROSITE-ProRule:PRU01299; METAL 5946; /note=Zinc 8; /evidence=ECO:0000255|PROSITE-ProRule:PRU01299; METAL 5949; /note=Zinc 8; /evidence=ECO:0000255|PROSITE-ProRule:PRU01299 |
| Rhea ID | RHEA:21248; RHEA:13065; RHEA:67732; RHEA:67020 |
| Cross Reference Brenda |