Strain
Human_MERS_KF961221
(Region: Qatar; Strain: Middle East respiratory syndrome coronavirus isolate Qatar3, complete genome.; Date: 13-Oct-13)
Gene
orf1ab
Description
Annotated in NCBI,
orf1ab
Location
GenBank Accession
Full name
Replicase polyprotein 1ab
Alternative Name
ORF1ab polyprotein
Sequence
CDS
ATGCCCGAATAGAACCCTGTTCAAGTGGTTTGTCCACTGATGTCGTCTTTAGGGCATTTGACATCTGCAACTATAAGGCTAAGGTTGCTGGTATTGGAAAATACTACAAGACTAATACTTGTAGGTTTGTAGAATTAGATGACCAAGGGCATCATTTAGACTCCTATTTTGTCGTTAAGAGGCATACTATGGAGAATTATGAACTAGAGAAGCACTGTTACGATTTGTTACGTGACTGTGATGCTGTAGCTCCCCATGATTTCTTCATCTTTGATGTAGACAAAGTTAAAACACCTCATATTGTACGTCAGCGTTTAACTGAGTACACTATGATGGATCTTGTATATGCCCTGAGGCACTTTGATCAAAATAGCGAAGTGCTTAAGGCTATCTTAGTGAAGTATGGTTGCTGTGATGTTACCTACTTTGAAAATAAACTCTGGTTTGATTTTGTTGAAAATCCCAGTGTTATTGGTGTTTATCATAAACTTGGAGAACGTGTACGCCAAGCTATCTTAAACACTGTTAAATTTTGTGACCACATGGTCAAGGCTGGTTTAGTCGGTGTGCTCACACTAGACAACCAGGACCTTAATGGCAAGTGGTATGATTTTGGTGACTTCGTAATCACTCAACCTGGTTCAGGAGTAGCTATAGTTGATAGCTACTATTCTTATTTGATGCCTGTGCTCTCAATGACCGATTGTCTGGCCGCTGAGACACATAGGGATTGTGATTTTAATAAACCACTCATTGAGTGGCCACTTACTGAGTATGATTTTACTGATTATAAGGTACAACTCTTTGAGAAGTACTTTAAATATTGGGATCAGACGTATCACGCAAATTGCGTTAATTGTACTGATGACCGTTGTGTGTTACATTGTGCTAATTTCAATGTATTGTTTGCTATGACCATGCCTAAGACTTGTTTCGGACCCATAGTCCGAAAGATCTTTGTTGATGGCGTGCCATTTGTAGTATCTTGTGGTTATCACTACAAAGAATTAGGTTTAGTCATGAATATGGATGTTAGTCTCCATAGACATAGGCTCTCTCTTAAGGAGTTGATGATGTATGCCGCTGATCCAGCCATGCACATTGCCTCCTCTAACGCTTTTCTTGATTTGAGGACATCATGTTTTAGTGTCGCTGCACTTACAACTGGTTTGACTTTTCAAACTGTGCGGCCTGGCAATTTTAACCAAGACTTCTATGATTTCGTGGTATCTAAAGGTTTCTTTAAGGAGGGCTCTTCAGTTACGCTCAAACATTTTTTCTTTGCTCAAGATGGTAATGCTGCTATTACAGATTATAATTACTATTCTTATAATCTGCCTACTATGTGTGACATCAAACAAATGTTGTTCTGCATGGAAGTTGTAAACAAGTACTTCGAAATCTATGACGGTGGTTGTCTTAATGCTTCTGAAGTGGTTGTTAATAATTTAGACAAGAGTGCTGGCCATCCTTTTAATAAGTTTGGCAAAGCTCGTGTCTATTATGAGAGCATGTCTTACCAGGAGCAAGATGAACTCTTTGCCATGACAAAGCGTAACGTCATTCCTACCATGACTCAAATGAATCTAAAATATGCTATTAGTGCTAAGAATAGAGCTCGCACTGTTGCAGGCGTGTCCATACTTAGCACAATGACTAATCGCCAGTACCATCAGAAAATGCTTAAGTCCATGGCTGCAACTCGTGGAGCGACTTGCGTCATTGGTACTACAAAGTTCTATGGTGGCTGGGATTTCATGCTTAAAACATTGTACAAAGATGTTGATAATCCGCATCTTATGGGTTGGGATTACCCTAAGTGTGATAGAGCTATGCCTAATATGTGTAGAATCTTCGCTTCACTCATATTAGCTCGTAAACATGGCACTTGTTGTACTACAAGGGACAGATTTTATCGCTTGGCAAATGAGTGTGCTCAGGTGCTAAGCGAATATGTTCTATGTGGTGGTGGTTACTACGTCAAACCTGGAGGTACCAGTAGCGGAGATGCCACCACTGCATATGCCAATAGTGTCTTTAACATTTTGCAGGCGACAACTGCTAATGTCAGTGCACTTATGGGTGCTAATGGCAACAAGATTGTTGACAAAGAAGTTAAAGACATGCAGTTTGATTTGTATGTCAATGTTTACAGGAGCACTAGCCCAGACCCCAAATTTGTTGATAAATACTATGCTTTTCTTAATAAGCACTTTTCTATGATGATACTGTCTGATGACGGTGTCGTTTGCTATAATAGTGATTATGCAGCTAAGGGTTACATTGCTGGAATACAGAATTTTAAGGAAACGCTGTATTATCAGAACAATGTCTTTATGTCTGAAGCTAAATGCTGGGTGGAAACCGATCTGAAGAAAGGGCCACATGAATTCTGTTCACAGCATACGCTTTATATTAAGGATGGCGACGATGGTTACTTCCTTCCTTATCCAGACCCTTCAAGAATTTTGTCTGCCGGTTGCTTTGTAGATGATATCGTTAAGACTGACGGTACACTCATGGTAGAGCGGTTTGTGTCTTTGGCTATAGATGCTTACCCTCTCACAAAGCATGAAGATATAGAATACCAGAATGTATTCTGGGTCTACTTACAGTATATAGAAAAACTGTATAAAGACCTTACAGGACACATGCTTGACAGTTATTCTGTCATGCTATGTGGTGATAATTCTGCTAAGTTTTGGGAAGAGGCATTCTATAGAGATCTCTATAGTTCGCCTACCACTTTGCAGGCTGTCGGTTCATGCGTTGTATGCCATTCACAGACTTCCCTACGCTGTGGGACATGCATCCGTAGACCATTTCTCTGCTGTAAATGCTGCTATGATCATGTTATAGCAACTCCACATAAGATGGTTTTGTCTGTTTCTCCTTACGTTTGTAATGCCCCTGGTTGTGGCGTTTCAGACGTTACTAAGCTATATTTAGGTGGTATGAGCTACTTTTGTGTAGATCATAGACCTGTGTGTAGTTTTCCACTTTGCGCTAATGGTCTTGTATTCGGCTTATACAAGAATATGTGCACAGGTAGTCCTTCTATAGTTGAATTTAATAGGTTGGCTACCTGTGACTGGACTGAAAGTGGTGATTACACCCTTGCCAATACTACAACAGAACCACTCAAACTTTTTGCTGCTGAGACTTTACGTGCCACTGAAGAGGCGTCTAAGCAGTCTTATGCTATTGCCACCATCAAAGAAATTGTTGGTGAGCGCCAACTATTACTTGTGTGGGAGGCTGGCAAGTCCAAACCACCACTCAATCGTAATTATGTTTTTACTGGTTATCATATAACCAAAAATAGTAAAGTGCAGCTCGGTGAGTACATCTTCGAGCGCATTGATTATAGTGATGCTGTATCCTACAAGTCTAGTACAACGTATAAACTGACTGTAGGTGACATCTTCGTACTTACCTCTCACTCTGTGGCTACCTTGACGGCGCCCACAATTGTGAATCAAGAGAGGTATGTTAAAATTACTGGGTTGTACCCAACCATTACGGTACCTGAAGAGTTCGCAAGTCATGTTGCCAACTTCCAAAAATCAGGTTATAGTAAATATGTCACTGTTCAGGGACCACCTGGCACTGGCAAAAGTCATTTTGCTATAGGGTTAGCGATTTACTACCCTACAGCACGTGTTGTTTATACAGCATGTTCACACGCAGCTGTTGATGCTTTGTGTGAAAAAGCTTTTAAATATTTGAACATTGCTAAATGTTCCCGTATCATTCCTGCAAAGGCACGTGTTGAGTGCTATGACAGGTTTAAAGTTAATGAGACAAATTCTCAATATTTGTTTAGTACTATTAATGCTCTACCAGAAACTTCTGCTGATATTCTGGTGGTTGATGAGGTTAGTATGTGCACTAATTATGATCTTTCAATTATTAATGCACGTATTAAAGCTAAGCACATTGTCTATGTAGGAGATCCAGCACAGTTGCCAGCTCCTAGGACTTTGTTGACTAGAGGCACATTGGAACCAGAAAATTTCAATAGTGTCACTAGATTGATGTGTAACTTAGGTCCTGACATATTTTTAAGTATGTGCTACAGGTGTCCTAAGGAAATAGTAAGCACTGTGAGCGCTCTTGTCTACAATAATAAATTGTTAGCCAAGAAGGAGCTTTCAGGCCAGTGCTTTAAAATACTCTATAAGGGCAATGTGACGCATGATGCTAGCTCTGCCATTAATAGACCACAACTCACATTTGTGAAGAATTTTATTACTGCCAATCCGGCATGGAGTAAGGCAGTCTTTATTTCGCCTTATAATTCACAGAATGCTGTGGCTCGTTCAATGCTGGGCCTTACTACTCAGACTGTTGATTCCTCACAGGGTTCAGAATACCAGTACGTTATCTTCTGTCAAACAGCAGATACGGCACATGCTAACAACATTAACAGATTTAATGTTGCAATCACTCGTGCCCAAAAAGGTATTCTTTGTGTTATGACATCTCAGGCACTCTTTGAGTCCTTAGAGTTTACTGAATTGTCTTTTACTAATTACAAGCTCCAGTCTCAGATTGTAACTGGCCTTTTTAAAGATTGCTCTAGAGAAACTTCTGGCCTCTCACCTGCTTATGCACCAACATACGTTAGTGTTGATGACAAGTATAAGACGAGTGATGAGCTTTGCGTGAATCTTAATTTACCCGCAAATGTCCCATACTCTCGTGTTATTTCCAGGATGGGCTTTAAACTCGATGCAACAGTTCCTGGATATCCTAAGCTTTTCATTACTCGTGAAGAGGCTGTAAGGCAAGTTCGAAGCTGGATAGGCTTCGATGTTGAGGGTGCTCATGCTTCCCGTAATGCATGTGGCACCAATGTGCCTCTACAATTAGGATTTTCAACTGGTGTGAACTTTGTTGTTCAGCCAGTTGGTGTTGTAGACACTGAGTGGGGTAACATGTTAACGGGCATTGCTGCCCGTCCTCCACCAGGTGAACAGTTTAAGCACCTCGTGCCTCTTATGCATAAGGGGGCTGCATGGCCTATTGTTAGACGACGTATAGTGCAAATGTTGTCAGACACTTTAGACAAATTGTCTGATTACTGTACGTTTGTTTGTTGGGCTCATGGCTTTGAATTAACGTCTGCATCATACTTTTGCAAGATAGGTAAGGAACAGAAGTGTTGCATGTGCAATAGACGCGCTGCAGCGTACTCTTCACCTCTGCAATCTTATGCCTGCTGGACTCATTCCTGCGGTTATGATTATGTCTACAACCCTTTCTTTGTCGATGTTCAACAGTGGGGTTATGTAGGCAATCTTGCTACTAATCACGATCGTTATTGCTCTGTCCATCAAGGAGCTCATGTGGCTTCTAATGATGCAATAATGACTCGTTGTTTAGCTATTCATTCTTGTTTTATAGAACGTGTGGATTGGGATATAGAGTATCCTTATATCTCACATGAAAAGAAATTGAATTCCTGTTGTAGAATCGTTGAGCGCAACGTCGTACGTGCTGCTCTTCTTGCCGGTTCATTTGACAAAGTCTATGATATTGGCAATCCTAAAGGAATTCCTATTGTTGATGACCCTGTGGTTGATTGGCATTATTTTGATGCACAGCCCTTGACCAGGAAGGTACAACAGCTTTTCTATACAGAGGACATGGCCTCAAGATTTGCTGATGGGCTCTGCYTATTTTGGAACTGTAATGTACCAAAATATCCTAATAATGCAATTGTATGCAGRTTTGACACACGTGTGCATTCTGAGTTCAATTTGCCAGGTTGTGATGGCGGTAGTTTGTATGTYAACAAGCACGCTTTTCATACACCAGCATATGATGTGAGTGCATTCCGTGATCTGAAACCTTTACCATTCTTTTATTATTCTACTACACCATGTGAAGTGCATGGTAATGGTAGTATGATAGAGGATATTGATTATGTACCCCTAAAATCTGCAGTCTGTATTACAACTTGTAATTTAGGGGGCGCTGTTTGTAGGAAGCATGCTACAGAGTACAGAGAGTATATGGAAGCATATAATCTTGTCTCTGCATCAGGTTTCCGCCTTTGGTGTTATAAGACCTTTGATATTTATAATCTCTGGTCTACTTTTACAAAAGTTCAAGGTTTGGAAAACATTGCTTTTAATGTTGTTAAACAAGGCCATTTTATTGGTGTTGAGGGTGAACTACCTGTAGCTGTAGTCAATGATAAGATCTTCACCAAGAGTGGCGTTAATGACATTTGTATGTTTGAGAATAAAACCACTTTGCCTACTAATATAGCTTTTGAACTCTATGCTAAGCGTGCTGTACGCTCGCATCCCGATTTCAAATTGCTACACAATTTACAAGCAGACATTTGCTACAAGTTCGTCCTTTGGGATTATGAACGTAGCAATATTTATGGTACTGCTACTATTGGTGTATGTAAGTACACTGATATTGATGTTAATTCAGCTTTGAATATATGTTTTGACATACGCGATAATGGTTCATTGGAGAAGTTCATGTCTACTCCCAATGCCATCTTTATTTCTGATAGAAAAATCAAGAAATACCCTTGTATGGTAGGTCCTGATTATGCTTACTTCAATGGTGCTATCATCCGTGATAGTGATGTTGTTAAACAACCAGTGAAGTTCTACTTGTATAAGAAAGTCAATAATGAGTTTATTGATCCTACTGAGTGTATTTACACTCAGAGTCGCTCTTGTAGTGACTTCCTACCCCTGTCTGACATGGAGAAAGACTTTCTATCTTTTGATAGTGATGTTTTCATTAAGAAGTATGGCTTGGAAAACTATGCTTTTGAGCACGTAGTCTATGGAGACTTCTCTCATACTACGTTAGGCGGTCTTCACTTGCTTATTGGTTTATACAAGAAGCAACAGGAAGGTCATATTATTATGGAAGAAATGCTAAAAGGTAGCTCAACTATTCATAACTATTTTATTACTGAGACTAACACAGCGGCTTTTAAGGCGGTGTGTTCTGTTATAGATTTAAAGCTTGACGACTTTGTTATGATTTTAAAGAGTCAAGACCTTGGCGTAGTATCCAAGGTTGTCAAGGTTCCTATTGACTTAACAATGATTGAGTTTATGTTATGGTGTAAGGATGGACAGGTTCAAACCTTCTACCCTCGACTCCAGGCTTCTGCAGATTGGAAACCTGGTCATGCAATGCCATCCCTCTTTAAAGTTCAAAATGTAAACCTTGAACGTTGTGAGCTTGCTAATTACAAGCAATCTATTCCTATGCCTCGCGGTGTGCACATGAACATCGCTAAATATATGCAATTGTGCCAGTATTTAAATACTTGCACATTAGCCGTGCCTGCCAATATGCGTGTTATACATTTTGGCGCTGGTTCTGATAAAGGTATCGCTCCTGGTACATCAGTTTTACGACAGTGGCTTCCTATAGATGCCATTATTATAGATAATGATTTAAATGAGTTCGTGTCAGATGCTGACATAACTTTATTTGGAGATTGTGTAACTGTACGTGTCGGCCAACAAGTGGATCTTGTTATTTCCGACATGTATGATCCTACTACTAAGAATGTAACAGGTAGTAATGAGTCAAAGGCTTTATTCTTTACTTACCTGTGTAACCTCATTAATAATAATCTTGCTCTTGGTGGGTCTGTTGCTATTAAAATAACAGAACACTCTTGGAGCGTTGAACTTTATGAACTTATGGGAAAATTTGCTTGGTGGACTGTTTTCTGCACMAATGCAAATGCATCCTCATCTGAAGGATTCCTTTTAGGTATTAATTACTTGGGTACTATTAAAGAAAATATAGATGGTGGTGCTATGCACGCCAACTATATATTTTGGAGAAATTCCACTCCTATGAATCTGAGTACTTACTCACTTTTTGATTTATCCAAGTTTCAATTAAAATTAAAAGGAACACCAGTTCTTCAATTAAAGGAGAGTCAAATTAACGAACTCGTAATATCTCTCCTGTCGCAGGGTAAGTTACTTATCCGTGACAATGATACACTCAGTGTTTCTACTGATGTTCTTGTTAACACCTACAGAAAGTTACGTTGA
Protein
ARIEPCSSGLSTDVVFRAFDICNYKAKVAGIGKYYKTNTCRFVELDDQGHHLDSYFVVKRHTMENYELEKHCYDLLRDCDAVAPHDFFIFDVDKVKTPHIVRQRLTEYTMMDLVYALRHFDQNSEVLKAILVKYGCCDVTYFENKLWFDFVENPSVIGVYHKLGERVRQAILNTVKFCDHMVKAGLVGVLTLDNQDLNGKWYDFGDFVITQPGSGVAIVDSYYSYLMPVLSMTDCLAAETHRDCDFNKPLIEWPLTEYDFTDYKVQLFEKYFKYWDQTYHANCVNCTDDRCVLHCANFNVLFAMTMPKTCFGPIVRKIFVDGVPFVVSCGYHYKELGLVMNMDVSLHRHRLSLKELMMYAADPAMHIASSNAFLDLRTSCFSVAALTTGLTFQTVRPGNFNQDFYDFVVSKGFFKEGSSVTLKHFFFAQDGNAAITDYNYYSYNLPTMCDIKQMLFCMEVVNKYFEIYDGGCLNASEVVVNNLDKSAGHPFNKFGKARVYYESMSYQEQDELFAMTKRNVIPTMTQMNLKYAISAKNRARTVAGVSILSTMTNRQYHQKMLKSMAATRGATCVIGTTKFYGGWDFMLKTLYKDVDNPHLMGWDYPKCDRAMPNMCRIFASLILARKHGTCCTTRDRFYRLANECAQVLSEYVLCGGGYYVKPGGTSSGDATTAYANSVFNILQATTANVSALMGANGNKIVDKEVKDMQFDLYVNVYRSTSPDPKFVDKYYAFLNKHFSMMILSDDGVVCYNSDYAAKGYIAGIQNFKETLYYQNNVFMSEAKCWVETDLKKGPHEFCSQHTLYIKDGDDGYFLPYPDPSRILSAGCFVDDIVKTDGTLMVERFVSLAIDAYPLTKHEDIEYQNVFWVYLQYIEKLYKDLTGHMLDSYSVMLCGDNSAKFWEEAFYRDLYSSPTTLQAVGSCVVCHSQTSLRCGTCIRRPFLCCKCCYDHVIATPHKMVLSVSPYVCNAPGCGVSDVTKLYLGGMSYFCVDHRPVCSFPLCANGLVFGLYKNMCTGSPSIVEFNRLATCDWTESGDYTLANTTTEPLKLFAAETLRATEEASKQSYAIATIKEIVGERQLLLVWEAGKSKPPLNRNYVFTGYHITKNSKVQLGEYIFERIDYSDAVSYKSSTTYKLTVGDIFVLTSHSVATLTAPTIVNQERYVKITGLYPTITVPEEFASHVANFQKSGYSKYVTVQGPPGTGKSHFAIGLAIYYPTARVVYTACSHAAVDALCEKAFKYLNIAKCSRIIPAKARVECYDRFKVNETNSQYLFSTINALPETSADILVVDEVSMCTNYDLSIINARIKAKHIVYVGDPAQLPAPRTLLTRGTLEPENFNSVTRLMCNLGPDIFLSMCYRCPKEIVSTVSALVYNNKLLAKKELSGQCFKILYKGNVTHDASSAINRPQLTFVKNFITANPAWSKAVFISPYNSQNAVARSMLGLTTQTVDSSQGSEYQYVIFCQTADTAHANNINRFNVAITRAQKGILCVMTSQALFESLEFTELSFTNYKLQSQIVTGLFKDCSRETSGLSPAYAPTYVSVDDKYKTSDELCVNLNLPANVPYSRVISRMGFKLDATVPGYPKLFITREEAVRQVRSWIGFDVEGAHASRNACGTNVPLQLGFSTGVNFVVQPVGVVDTEWGNMLTGIAARPPPGEQFKHLVPLMHKGAAWPIVRRRIVQMLSDTLDKLSDYCTFVCWAHGFELTSASYFCKIGKEQKCCMCNRRAAAYSSPLQSYACWTHSCGYDYVYNPFFVDVQQWGYVGNLATNHDRYCSVHQGAHVASNDAIMTRCLAIHSCFIERVDWDIEYPYISHEKKLNSCCRIVERNVVRAALLAGSFDKVYDIGNPKGIPIVDDPVVDWHYFDAQPLTRKVQQLFYTEDMASRFADGLCLFWNCNVPKYPNNAIVCRFDTRVHSEFNLPGCDGGSLYVNKHAFHTPAYDVSAFRDLKPLPFFYYSTTPCEVHGNGSMIEDIDYVPLKSAVCITTCNLGGAVCRKHATEYREYMEAYNLVSASGFRLWCYKTFDIYNLWSTFTKVQGLENIAFNVVKQGHFIGVEGELPVAVVNDKIFTKSGVNDICMFENKTTLPTNIAFELYAKRAVRSHPDFKLLHNLQADICYKFVLWDYERSNIYGTATIGVCKYTDIDVNSALNICFDIRDNGSLEKFMSTPNAIFISDRKIKKYPCMVGPDYAYFNGAIIRDSDVVKQPVKFYLYKKVNNEFIDPTECIYTQSRSCSDFLPLSDMEKDFLSFDSDVFIKKYGLENYAFEHVVYGDFSHTTLGGLHLLIGLYKKQQEGHIIMEEMLKGSSTIHNYFITETNTAAFKAVCSVIDLKLDDFVMILKSQDLGVVSKVVKVPIDLTMIEFMLWCKDGQVQTFYPRLQASADWKPGHAMPSLFKVQNVNLERCELANYKQSIPMPRGVHMNIAKYMQLCQYLNTCTLAVPANMRVIHFGAGSDKGIAPGTSVLRQWLPIDAIIIDNDLNEFVSDADITLFGDCVTVRVGQQVDLVISDMYDPTTKNVTGSNESKALFFTYLCNLINNNLALGGSVAIKITEHSWSVELYELMGKFAWWTVFCTNANASSSEGFLLGINYLGTIKENIDGGAMHANYIFWRNSTPMNLSTYSLFDLSKFQLKLKGTPVLQLKESQINELVISLLSQGKLLIRDNDTLSVSTDVLVNTYRKLR
Summary
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.
Promotes the degradation of host mRNAs by inducing an endonucleolytic RNA cleavage in template mRNAs, and inhibits of host mRNA translation, a function that is separable from its RNA cleavage activity. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response.
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.
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. Participates together with nsp4 in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3. Prevents also host NF-kappa-B signaling.
Participates in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication.
Proteinase 3CL-PRO: 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).
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.
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.
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.
May participate in viral replication by acting as a ssRNA-binding protein.
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.
Responsible for replication and transcription of the viral RNA genome.
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.
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.
Mn(2+)-dependent, uridylate-specific enzyme, which leaves 2'-3'-cyclic phosphates 5' to the cleaved bond.
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.
Promotes the degradation of host mRNAs by inducing an endonucleolytic RNA cleavage in template mRNAs, and inhibits of host mRNA translation, a function that is separable from its RNA cleavage activity. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response.
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.
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. Participates together with nsp4 in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3. Prevents also host NF-kappa-B signaling.
Participates in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication.
Proteinase 3CL-PRO: 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).
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.
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.
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.
May participate in viral replication by acting as a ssRNA-binding protein.
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.
Responsible for replication and transcription of the viral RNA genome.
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.
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.
Mn(2+)-dependent, uridylate-specific enzyme, which leaves 2'-3'-cyclic phosphates 5' to the cleaved bond.
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.
Catalytic Activity
a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
ATP + H2O = ADP + H(+) + phosphate
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.
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).
ATP + H2O = ADP + H(+) + phosphate
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.
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).
Subunit
Nsp2 interacts with host PHB and PHB2. 3CL-PRO exists as monomer and homodimer. Nsp4 interacts with PL-PRO and nsp6. Only the homodimer shows catalytic activity. Eight copies of nsp7 and eight copies of nsp8 assemble to form a heterohexadecamer dsRNA-encircling ring structure. Nsp9 is a dimer. Nsp10 forms a dodecamer and interacts with nsp14 and nsp16; these interactions enhance nsp14 and nsp16 enzymatic activities. Nsp14 interacts (via N-terminus) with DDX1.
Miscellaneous
Produced by -1 ribosomal frameshifting at the 1a-1b genes boundary.
Similarity
Belongs to the coronaviruses polyprotein 1ab family.
Keywords
3D-structure
Activation of host autophagy by virus
ATP-binding
Decay of host mRNAs by virus
Endonuclease
Eukaryotic host gene expression shutoff by virus
Eukaryotic host translation shutoff by virus
Exonuclease
Helicase
Host cytoplasm
Host gene expression shutoff by virus
Host membrane
Host mRNA suppression by virus
Host-virus interaction
Hydrolase
Inhibition of host innate immune response by virus
Inhibition of host interferon signaling pathway by virus
Inhibition of host ISG15 by virus
Inhibition of host NF-kappa-B by virus
Membrane
Metal-binding
Methyltransferase
Modulation of host ubiquitin pathway by viral deubiquitinase
Modulation of host ubiquitin pathway by virus
Nuclease
Nucleotide-binding
Nucleotidyltransferase
Protease
Reference proteome
Repeat
Ribosomal frameshifting
RNA-binding
RNA-directed RNA polymerase
Thiol protease
Transferase
Transmembrane
Transmembrane helix
Ubl conjugation pathway
Viral immunoevasion
Viral RNA replication
Zinc
Zinc-finger
Feature
chain Host translation inhibitor nsp1
Uniprot
EMBL
Proteomes
PRIDE
Pfam
Interpro
IPR009469
RNA_pol_N_coronovir
IPR032505 Corona_NSP4_C
IPR037204 NSP7_sf
IPR008740 Peptidase_C30
IPR001205 RNA-dir_pol_C
IPR014828 NSP7
IPR032592 NAR_dom
IPR027352 CV_ZBD
IPR036333 NSP10_sf
IPR009003 Peptidase_S1_PA
IPR014822 NSP9
IPR037227 EndoU-like
IPR037230 NSP8_sf
IPR038123 NSP4_C_sf
IPR027417 P-loop_NTPase
IPR013016 Peptidase_C30/C16
IPR018995 RNA_synth_NSP10_coronavirus
IPR029063 SAM-dependent_MTases
IPR041679 DNA2/NAM7-like_AAA
IPR038083 R1a/1ab
IPR038400 Nsp3_coronavir_sf
IPR009466 NSP11
IPR042570 NAR_sf
IPR024375 Nsp3_coronavir
IPR014829 NSP8
IPR002589 Macro_dom
IPR009461 Coronavirus_NSP16
IPR042515 Nsp15_N
IPR014827 Viral_protease
IPR007094 RNA-dir_pol_PSvirus
IPR027351 (+)RNA_virus_helicase_core_dom
IPR036499 NSP9_sf
IPR032505 Corona_NSP4_C
IPR037204 NSP7_sf
IPR008740 Peptidase_C30
IPR001205 RNA-dir_pol_C
IPR014828 NSP7
IPR032592 NAR_dom
IPR027352 CV_ZBD
IPR036333 NSP10_sf
IPR009003 Peptidase_S1_PA
IPR014822 NSP9
IPR037227 EndoU-like
IPR037230 NSP8_sf
IPR038123 NSP4_C_sf
IPR027417 P-loop_NTPase
IPR013016 Peptidase_C30/C16
IPR018995 RNA_synth_NSP10_coronavirus
IPR029063 SAM-dependent_MTases
IPR041679 DNA2/NAM7-like_AAA
IPR038083 R1a/1ab
IPR038400 Nsp3_coronavir_sf
IPR009466 NSP11
IPR042570 NAR_sf
IPR024375 Nsp3_coronavir
IPR014829 NSP8
IPR002589 Macro_dom
IPR009461 Coronavirus_NSP16
IPR042515 Nsp15_N
IPR014827 Viral_protease
IPR007094 RNA-dir_pol_PSvirus
IPR027351 (+)RNA_virus_helicase_core_dom
IPR036499 NSP9_sf
SUPFAM
Gene 3D
ProteinModelPortal
PDB
6NUS
E-value=0.0 Score=1404 Identity=72.19%
Cov(Q)=34.15% Cov(P)=96.02%
3D Structure
Ontologies
GO
GO:0044172 C:host cell endoplasmic reticulum-Golgi intermediate compartment
GO:0004197 F:cysteine-type endopeptidase activity
GO:0039648 P:modulation by virus of host protein ubiquitination
GO:0039520 P:induction by virus of host autophagy
GO:0003724 F:RNA helicase activity
GO:0039595 P:induction by virus of catabolism of host mRNA
GO:0039644 P:suppression by virus of host NF-kappaB transcription factor activity
GO:0071108 P:protein K48-linked deubiquitination
GO:0004519 F:endonuclease activity
GO:0008168 F:methyltransferase activity
GO:0003968 F:RNA-directed 5'-3' RNA polymerase activity
GO:0032259 P:methylation
GO:0003678 F:DNA helicase activity
GO:0070536 P:protein K63-linked deubiquitination
GO:0039502 P:suppression by virus of host type I interferon-mediated signaling pathway
GO:0006351 P:transcription, DNA-templated
GO:0044220 C:host cell perinuclear region of cytoplasm
GO:0003723 F:RNA binding
GO:0039579 P:suppression by virus of host ISG15 activity
GO:0008242 F:omega peptidase activity
GO:0039503 P:suppression by virus of host innate immune response
GO:0039694 P:viral RNA genome replication
GO:0033644 C:host cell membrane
GO:0039604 P:suppression by virus of host translation
GO:0036459 F:thiol-dependent ubiquitinyl hydrolase activity
GO:0005524 F:ATP binding
GO:0019082 P:viral protein processing
GO:0008270 F:zinc ion binding
GO:0016896 F:exoribonuclease activity, producing 5'-phosphomonoesters
GO:0016021 C:integral component of membrane
GO:0039653 P:suppression by virus of host transcription
GO:0004197 F:cysteine-type endopeptidase activity
GO:0039648 P:modulation by virus of host protein ubiquitination
GO:0039520 P:induction by virus of host autophagy
GO:0003724 F:RNA helicase activity
GO:0039595 P:induction by virus of catabolism of host mRNA
GO:0039644 P:suppression by virus of host NF-kappaB transcription factor activity
GO:0071108 P:protein K48-linked deubiquitination
GO:0004519 F:endonuclease activity
GO:0008168 F:methyltransferase activity
GO:0003968 F:RNA-directed 5'-3' RNA polymerase activity
GO:0032259 P:methylation
GO:0003678 F:DNA helicase activity
GO:0070536 P:protein K63-linked deubiquitination
GO:0039502 P:suppression by virus of host type I interferon-mediated signaling pathway
GO:0006351 P:transcription, DNA-templated
GO:0044220 C:host cell perinuclear region of cytoplasm
GO:0003723 F:RNA binding
GO:0039579 P:suppression by virus of host ISG15 activity
GO:0008242 F:omega peptidase activity
GO:0039503 P:suppression by virus of host innate immune response
GO:0039694 P:viral RNA genome replication
GO:0033644 C:host cell membrane
GO:0039604 P:suppression by virus of host translation
GO:0036459 F:thiol-dependent ubiquitinyl hydrolase activity
GO:0005524 F:ATP binding
GO:0019082 P:viral protein processing
GO:0008270 F:zinc ion binding
GO:0016896 F:exoribonuclease activity, producing 5'-phosphomonoesters
GO:0016021 C:integral component of membrane
GO:0039653 P:suppression by virus of host transcription
Subcellular Location
From MSLVP
Capsid
From Uniprot
Host membrane
Host cytoplasm
nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). With evidence from 4 publications.
Host endoplasmic reticulum-Golgi intermediate compartment The helicase interacts with the N protein in membranous complexes and colocalizes with sites of synthesis of new viral RNA. With evidence from 4 publications.
Host cytoplasm
nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity). With evidence from 4 publications.
Host endoplasmic reticulum-Golgi intermediate compartment The helicase interacts with the N protein in membranous complexes and colocalizes with sites of synthesis of new viral RNA. With evidence from 4 publications.
Topology
Length:
2685
Number of predicted TMHs:
0
Exp number of AAs in TMHs:
0.20498
Exp number, first 60 AAs:
0.00019
Total prob of N-in:
0.00044
outside
1 - 2685
