P0C6T5 (R1A_BCHK5) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 34.
History...
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Replicase polyprotein 1a Short name=pp1a Alternative name(s): ORF1a polyprotein Cleaved into the following 11 chains:
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| Gene names |
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| Organism | Bat coronavirus HKU5 (BtCoV) (BtCoV/HKU5/2004) [Complete proteome] | ||
| Taxonomic identifier | 694008 [NCBI] | ||
| Taxonomic lineage | Viruses › ssRNA positive-strand viruses, no DNA stage › Nidovirales › Coronaviridae › Coronavirinae › Betacoronavirus![]() | ||
| Virus host | Pipistrellus abramus (Japanese pipistrelle) (Pipistrellus javanicus abramus) [TaxID: 105295] |
Protein attributes
| Sequence length | 4481 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | The papain-like proteinase (PL-PRO) is responsible for the cleavages located at the N-terminus of 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. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF-3 By similarity. The main proteinase 3CL-PRO is 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. Also contains an ADP-ribose-1''-phosphate (ADRP)-binding function By similarity. Nsp7-nsp8 hexadecamer may possibly confer processivity to the polymerase, maybe by binding to dsRNA or by producing primers utilized by the latter By similarity. Nsp9 is a ssRNA-binding protein By similarity. |
| Catalytic activity | TSAVLQ-|-SGFRK-NH2 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 structure | 3CL-PRO exists as monomer and homodimer. Eight copies of nsp7 and eight copies of nsp8 assemble to form a heterohexadecamer. Nsp9 is a dimer. Nsp10 forms a dodecamer By similarity. |
| Subcellular location | Non-structural protein 3: Host membrane; Multi-pass membrane protein Potential. Non-structural protein 4: Host membrane; Multi-pass membrane protein Potential. Non-structural protein 6: Host membrane; Multi-pass membrane protein Potential. Non-structural protein 7: Host cytoplasm › host perinuclear region By similarity. Note: nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes By similarity. Non-structural protein 8: Host cytoplasm › host perinuclear region By similarity. Note: nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes By similarity. Non-structural protein 9: Host cytoplasm › host perinuclear region By similarity. Note: nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes By similarity. Non-structural protein 10: Host cytoplasm › host perinuclear region By similarity. Note: nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes By similarity. |
| Domain | The hydrophobic domains (HD) could mediate the membrane association of the replication complex and thereby alter the architecture of the host cell membrane By similarity. |
| Post-translational modification | Specific enzymatic cleavages in vivo by its own proteases yield mature proteins. 3CL-PRO and PL-PRO proteinases are autocatalytically processed By similarity. |
| Sequence similarities | Belongs to the coronaviruses polyprotein 1ab family. Contains 1 Macro domain. Contains 1 peptidase C16 domain. Contains 1 peptidase C30 domain. |
Ontologies
Alternative products
| This entry describes 2 isoforms produced by ribosomal frameshifting. [Align] [Select] | ||||||
| Isoform Replicase polyprotein 1a (identifier: P0C6T5-1) Also known as: pp1a; ORF1a polyprotein; This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | ||||||
| Note: Produced by conventional translation. | ||||||
| Isoform Replicase polyprotein 1ab (identifier: P0C6W4-1) Also known as: pp1ab; The sequence of this isoform can be found in the external entry P0C6W4. Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly. | ||||||
| Note: Produced by -1 ribosomal frameshifting at the 1a-1b genes boundary. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 4481 | 4481 | Replicase polyprotein 1a | PRO_0000338098 | |||||
| Chain | 1 – 195 | 195 | Non-structural protein 1 Potential | PRO_0000338099 | |||||
| Chain | 196 – 851 | 656 | Non-structural protein 2 Potential | PRO_0000338100 | |||||
| Chain | 852 – 2830 | 1979 | Non-structural protein 3 Potential | PRO_0000338101 | |||||
| Chain | 2831 – 3338 | 508 | Non-structural protein 4 Potential | PRO_0000338102 | |||||
| Chain | 3339 – 3644 | 306 | 3C-like proteinase Potential | PRO_0000338103 | |||||
| Chain | 3645 – 3936 | 292 | Non-structural protein 6 Potential | PRO_0000338104 | |||||
| Chain | 3937 – 4019 | 83 | Non-structural protein 7 Potential | PRO_0000338105 | |||||
| Chain | 4020 – 4218 | 199 | Non-structural protein 8 Potential | PRO_0000338106 | |||||
| Chain | 4219 – 4328 | 110 | Non-structural protein 9 Potential | PRO_0000338107 | |||||
| Chain | 4328 – 4481 | 154 | Non-structural protein 11 Potential | PRO_0000338109 | |||||
| Chain | 4329 – 4467 | 139 | Non-structural protein 10 Potential | PRO_0000338108 | |||||
Regions | |||||||||
| Transmembrane | 2196 – 2216 | 21 | Helical; Potential | ||||||
| Transmembrane | 2268 – 2288 | 21 | Helical; Potential | ||||||
| Transmembrane | 2372 – 2392 | 21 | Helical; Potential | ||||||
| Transmembrane | 2396 – 2416 | 21 | Helical; Potential | ||||||
| Transmembrane | 2421 – 2441 | 21 | Helical; Potential | ||||||
| Transmembrane | 2848 – 2868 | 21 | Helical; Potential | ||||||
| Transmembrane | 3119 – 3139 | 21 | Helical; Potential | ||||||
| Transmembrane | 3152 – 3172 | 21 | Helical; Potential | ||||||
| Transmembrane | 3203 – 3223 | 21 | Helical; Potential | ||||||
| Transmembrane | 3650 – 3670 | 21 | Helical; Potential | ||||||
| Transmembrane | 3684 – 3704 | 21 | Helical; Potential | ||||||
| Transmembrane | 3709 – 3729 | 21 | Helical; Potential | ||||||
| Transmembrane | 3760 – 3777 | 18 | Helical; Potential | ||||||
| Transmembrane | 3782 – 3802 | 21 | Helical; Potential | ||||||
| Transmembrane | 3823 – 3843 | 21 | Helical; Potential | ||||||
| Transmembrane | 3855 – 3875 | 21 | Helical; Potential | ||||||
| Domain | 1186 – 1345 | 160 | Macro | ||||||
| Domain | 1628 – 1902 | 275 | Peptidase C16 | ||||||
| Domain | 3339 – 3644 | 306 | Peptidase C30 | ||||||
| Zinc finger | 1748 – 1785 | 38 | C4-type By similarity | ||||||
| Zinc finger | 4402 – 4418 | 17 | By similarity | ||||||
| Zinc finger | 4444 – 4457 | 14 | By similarity | ||||||
| Region | 2158 – 2441 | 284 | HD1 By similarity | ||||||
| Region | 2848 – 3223 | 376 | HD2 By similarity | ||||||
| Region | 3650 – 3875 | 226 | HD3 By similarity | ||||||
| Compositional bias | 964 – 1066 | 103 | Glu-rich | ||||||
Sites | |||||||||
| Active site | 1668 | 1 | For PL-PRO activity By similarity | ||||||
| Active site | 1838 | 1 | For PL-PRO activity By similarity | ||||||
| Active site | 3379 | 1 | For 3CL-PRO activity By similarity | ||||||
| Active site | 3486 | 1 | For 3CL-PRO activity By similarity | ||||||
| Site | 195 – 196 | 2 | Cleavage Potential | ||||||
| Site | 851 – 852 | 2 | Cleavage; by PL-PRO Potential | ||||||
| Site | 2830 – 2831 | 2 | Cleavage; by PL-PRO Potential | ||||||
| Site | 3338 – 3339 | 2 | Cleavage; by 3CL-PRO Potential | ||||||
| Site | 3644 – 3645 | 2 | Cleavage; by 3CL-PRO Potential | ||||||
| Site | 3936 – 3937 | 2 | Cleavage; by 3CL-PRO Potential | ||||||
| Site | 4019 – 4020 | 2 | Cleavage; by 3CL-PRO Potential | ||||||
| Site | 4218 – 4219 | 2 | Cleavage; by 3CL-PRO Potential | ||||||
| Site | 4328 – 4329 | 2 | Cleavage; by 3CL-PRO Potential | ||||||
| Site | 4467 – 4468 | 2 | Cleavage; by 3CL-PRO Potential | ||||||
Sequences
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References
| [1] | "Comparative analysis of twelve genomes of three novel group 2c and group 2d coronaviruses reveals unique group and subgroup features." Woo P.C.Y., Wang M., Lau S.K.P., Xu H.F., Poon R.W.S., Guo R., Wong B.H.L., Gao K., Tsoi H.-W., Huang Y., Li K.S.M., Lam C.S.F., Chan K.-H., Zheng B.-J., Yuen K.-Y. J. Virol. 81:1574-1585(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA]. Strain: Isolate HKU5-1. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | EF065509 Genomic RNA. No translation available. |
3D structure databases | |
| ProteinModelPortal | P0C6T5. |
| SMR | P0C6T5. Positions 3937-4007, 4268-4328, 4335-4459. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| InterPro | IPR002589. A1pp. IPR024375. Nsp3_coronavir. IPR014828. NSP7. IPR014829. NSP8. IPR014822. NSP9. IPR008740. Peptidase_C30. IPR013016. Peptidase_C30/C16. IPR018995. RNA_synth_NSP10_coronavirus. IPR009003. Trypsin-like_Pept_dom. IPR014827. Viral_protease. [Graphical view] |
| Pfam | PF01661. Macro. 1 hit. PF09401. NSP10. 1 hit. PF11633. Nsp3. 1 hit. PF08716. nsp7. 1 hit. PF08717. nsp8. 1 hit. PF08710. nsp9. 1 hit. PF05409. Peptidase_C30. 1 hit. PF08715. Viral_protease. 1 hit. [Graphical view] |
| SUPFAM | SSF101816. Nsp9. 1 hit. SSF50494. Pept_Ser_Cys. 1 hit. SSF144246. SSF144246. 1 hit. |
| PROSITE | PS51442. M_PRO. 1 hit. PS51154. MACRO. 1 hit. PS51124. PEPTIDASE_C16. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | R1A_BCHK5 | ||||||||
| Accession | Primary (citable) accession number: P0C6T5 Secondary accession number(s): A3EXC9 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Viral Protein Annotation Program | ||||||||
Relevant documents
| Peptidase families Classification of peptidase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with
