[Papain-like protease]: Host endoplasmic reticulum membrane {Curator InferencePubMed:30200673}; Multi-pass membrane protein {Curator Inference}. Host cytoplasm {By
SimilarityUniProtKB:P0C6X7}. Note=Gammacoronaviruses induce membrane zippering to form zippered endoplasmic reticulum (zER). {Curator InferencePubMed:30200673}. [Non-structural protein 4]: Host endoplasmic reticulum membrane {Curator InferencePubMed:30200673}; Multi-pass membrane protein {Curator Inference}. Host cytoplasm {By
SimilarityUniProtKB:P0C6X7}. Note=Gammacoronaviruses induce membrane zippering to form zippered endoplasmic reticulum (zER). {Curator InferencePubMed:30200673}. [Non-structural protein 6]: Host endoplasmic reticulum membrane {Curator InferencePubMed:30200673}; Multi-pass membrane protein {Curator Inference}. Note=Gammacoronaviruses induce membrane zippering to form zippered endoplasmic reticulum (zER). {Curator InferencePubMed:30200673}. [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. [Non-structural protein 8]: Host cytoplasm, host perinuclear region {By
SimilarityUniProtKB: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. [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. [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. [Helicase]: Host endoplasmic reticulum-Golgi intermediate compartment {Curator Inference}. Note=The helicase interacts with the N protein in membranous complexes and colocalizes with sites of synthesis of new viral RNA. [Proofreading exoribonuclease]: Host cytoplasm {ECO:0000250|UniProtKB:P0DTD1}. Host endoplasmic reticulum {ECO:0000250|UniProtKB:P0DTD1}. [Uridylate-specific endoribonuclease]: Host cytoplasm {ECO:0000250|UniProtKB:P0DTD1}. Host endoplasmic reticulum {ECO:0000250|UniProtKB:P0DTD1}.
The host perinuclear region is the host cytoplasmic region just around the host nucleus. Note: This location is defined for viral proteins that appear in the perinuclear region of infected host cells
[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. {Curator Inference}. [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). {By
SimilarityUniProtKB:P0C6X7}. [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). {By
SimilarityUniProtKB:P0C6X7}. [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:30200673). Alone is able to induce paired membranes (PubMed:30200673). Coexpression of nsp3 and nsp4 does not result in the formation of DMVs (PubMed:30200673). {Experimental EvidencePubMed:30200673}. [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. {Sequence AnalysisPROSITE-ProRule:PRU00772}. [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. {By
SimilarityUniProtKB:P0C6X7}. [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. {By
SimilarityUniProtKB:P0C6X7}. [Non-structural protein 9]: Plays an essential role in viral replication by forming a homodimer that binds single-stranded RNA. {ECO:0000269|PubMed:28257598}. [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). {By
SimilarityUniProtKB:P0C6X7}. [RNA-directed RNA polymerase]: Responsible for replication and transcription of the viral RNA genome. {By
SimilarityUniProtKB:P0C6X7}. [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. {By
SimilarityUniProtKB:P0C6X7}. [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). {By
SimilarityUniProtKB:P0C6X7}. [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). {By
SimilarityUniProtKB:P0C6X7}. [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. {By
SimilarityUniProtKB:P0C6X7}.
National and Kapodistrian University of Athens
Department of Biology
Biophysics & Bioinformatics Laboratory