I7GVL4 · NCAP_BCCV
- ProteinNucleoprotein
- GeneN
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids428 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Encapsidates the genome protecting it from nucleases (Probable). The encapsidated genomic RNA is termed the nucleocapsid (NC) and serves as template for transcription and replication (Probable). The nucleocapsid has a left-handed helical structure (By similarity).
As a trimer, specifically binds and acts as a chaperone to unwind the panhandle structure formed by the viral RNA (vRNA) termini (By similarity).
Involved in the transcription and replication initiation of vRNA by mediating primer annealing (By similarity).
Plays a role in cap snatching by sequestering capped RNAs in P bodies for use by the viral RdRp during transcription initiation (By similarity).
Substitutes for the cellular cap-binding complex (eIF4F) to preferentially facilitate the translation of capped mRNAs (By similarity).
Initiates the translation by specifically binding to the cap and 40S ribosomal subunit (By similarity).
Prevents the viral glycoprotein N (Gn) from autophagy-dependent breakdown maybe by blocking autophagosome formation (By similarity).
Inhibits host EIF2AK2/PKR dimerization to prevent PKR-induced translational shutdown in cells and thus the activation of the antiviral state (By similarity).
Also displays sequence-unspecific DNA endonuclease activity (By similarity).
As a trimer, specifically binds and acts as a chaperone to unwind the panhandle structure formed by the viral RNA (vRNA) termini (By similarity).
Involved in the transcription and replication initiation of vRNA by mediating primer annealing (By similarity).
Plays a role in cap snatching by sequestering capped RNAs in P bodies for use by the viral RdRp during transcription initiation (By similarity).
Substitutes for the cellular cap-binding complex (eIF4F) to preferentially facilitate the translation of capped mRNAs (By similarity).
Initiates the translation by specifically binding to the cap and 40S ribosomal subunit (By similarity).
Prevents the viral glycoprotein N (Gn) from autophagy-dependent breakdown maybe by blocking autophagosome formation (By similarity).
Inhibits host EIF2AK2/PKR dimerization to prevent PKR-induced translational shutdown in cells and thus the activation of the antiviral state (By similarity).
Also displays sequence-unspecific DNA endonuclease activity (By similarity).
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 88 | Important for the endonuclease activity | ||||
Sequence: D | ||||||
Site | 103 | Important for the endonuclease activity | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | host cell Golgi apparatus | |
Cellular Component | host cell perinuclear region of cytoplasm | |
Cellular Component | ribonucleoprotein complex | |
Cellular Component | viral nucleocapsid | |
Molecular Function | endonuclease activity | |
Molecular Function | RNA binding |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameNucleoprotein
- EC number
- Alternative names
Gene names
Organism names
- Taxonomic lineageViruses > Riboviria > Orthornavirae > Negarnaviricota > Polyploviricotina > Ellioviricetes > Bunyavirales > Hantaviridae > Mammantavirinae > Orthohantavirus
- Virus hosts
Accessions
- Primary accessionI7GVL4
Subcellular Location
UniProt Annotation
GO Annotation
Note: Internal protein of virus particle.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000455185 | 1-428 | Nucleoprotein | |||
Sequence: MSNLKEVQDNITTHEQQLVAARQKLKDAERTVGVDPDDVNKSTLQNRRAAVSALEAKIGELKRQLADLVAAQKLATKSVDPTGIEPDDHLKEKSSLRYGNVLDVNSIDLEEPSGQTADWKAIGTYILSFVLPIVLKALYMLSTRGRQTVKENKGTRIRFKDDSSYEDVNGIRKPKHLYVSLPTAQSTMKADEITPGRFRTIVCGLFPAQIKARNIISPVMGVIGFSFFVKDWVDKIEDFLRAECPFLPKPRAQAESFLSTNGAYFMNRQTQVEESKVQDILDLIDTAESGGATLFDNIASPQSAWIFACAPDRCPPTALYVAGVPELGAFFSILQDMRNTIMASKSVGTAEEKLKKKSAFYQSYLRRTQSMGIQLDQKIIILYMINWGKEAVNHFHLGDDMDPELRQLAQALVDTKVKEISNQEPLKI |
Interaction
Subunit
Homotrimer (By similarity).
Homomultimer (By similarity).
Homomultimerizes and binds to viral genomic RNA to form the nucleocapsid (By similarity).
Interacts with host MAP1LC3B; this interaction participates to the protection of Gn from virus-triggered autophagy (By similarity).
Interacts with host SNAP29; this interaction participates to the protection of glycoprotein N from virus-triggered autophagy (By similarity).
Interacts (via N-terminus) with host RPS19; this interaction probably mediates the loading of the 40S ribosomal subunit on viral capped mRNA during N-mediated translation initiation (By similarity).
Interacts with the viral RdRp (By similarity).
Interacts with host SUMO1 (via N-terminus) (By similarity).
Interacts with host DAXX (By similarity).
Interacts with the viral glycoprotein N (via C-terminus) (By similarity).
Interacts with the viral glycoprotein C (via C-terminus) (By similarity).
Homomultimer (By similarity).
Homomultimerizes and binds to viral genomic RNA to form the nucleocapsid (By similarity).
Interacts with host MAP1LC3B; this interaction participates to the protection of Gn from virus-triggered autophagy (By similarity).
Interacts with host SNAP29; this interaction participates to the protection of glycoprotein N from virus-triggered autophagy (By similarity).
Interacts (via N-terminus) with host RPS19; this interaction probably mediates the loading of the 40S ribosomal subunit on viral capped mRNA during N-mediated translation initiation (By similarity).
Interacts with the viral RdRp (By similarity).
Interacts with host SUMO1 (via N-terminus) (By similarity).
Interacts with host DAXX (By similarity).
Interacts with the viral glycoprotein N (via C-terminus) (By similarity).
Interacts with the viral glycoprotein C (via C-terminus) (By similarity).
Family & Domains
Features
Showing features for region, coiled coil, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-50 | RdRP binding | ||||
Sequence: MSNLKEVQDNITTHEQQLVAARQKLKDAERTVGVDPDDVNKSTLQNRRAA | ||||||
Region | 1-79 | Homomultimerization | ||||
Sequence: MSNLKEVQDNITTHEQQLVAARQKLKDAERTVGVDPDDVNKSTLQNRRAAVSALEAKIGELKRQLADLVAAQKLATKSV | ||||||
Region | 1-100 | Chaperone activity | ||||
Sequence: MSNLKEVQDNITTHEQQLVAARQKLKDAERTVGVDPDDVNKSTLQNRRAAVSALEAKIGELKRQLADLVAAQKLATKSVDPTGIEPDDHLKEKSSLRYGN | ||||||
Region | 1-175 | Viral panhandle binding | ||||
Sequence: MSNLKEVQDNITTHEQQLVAARQKLKDAERTVGVDPDDVNKSTLQNRRAAVSALEAKIGELKRQLADLVAAQKLATKSVDPTGIEPDDHLKEKSSLRYGNVLDVNSIDLEEPSGQTADWKAIGTYILSFVLPIVLKALYMLSTRGRQTVKENKGTRIRFKDDSSYEDVNGIRKPK | ||||||
Coiled coil | 4-71 | |||||
Sequence: LKEVQDNITTHEQQLVAARQKLKDAERTVGVDPDDVNKSTLQNRRAAVSALEAKIGELKRQLADLVAA | ||||||
Region | 80-248 | Interaction with glycoprotein N | ||||
Sequence: DPTGIEPDDHLKEKSSLRYGNVLDVNSIDLEEPSGQTADWKAIGTYILSFVLPIVLKALYMLSTRGRQTVKENKGTRIRFKDDSSYEDVNGIRKPKHLYVSLPTAQSTMKADEITPGRFRTIVCGLFPAQIKARNIISPVMGVIGFSFFVKDWVDKIEDFLRAECPFLP | ||||||
Region | 100-125 | Homomultimerization | ||||
Sequence: NVLDVNSIDLEEPSGQTADWKAIGTY | ||||||
Region | 150-175 | Interaction with host RPS19 | ||||
Sequence: KENKGTRIRFKDDSSYEDVNGIRKPK | ||||||
Region | 175-217 | Viral RNA-binding | ||||
Sequence: KHLYVSLPTAQSTMKADEITPGRFRTIVCGLFPAQIKARNIIS | ||||||
Motif | 178-181 | YxxL | ||||
Sequence: YVSL | ||||||
Region | 188-191 | Interaction with host UBE2I/UBC9 | ||||
Sequence: MKAD | ||||||
Region | 372-420 | Homomultimerization | ||||
Sequence: GIQLDQKIIILYMINWGKEAVNHFHLGDDMDPELRQLAQALVDTKVKEI | ||||||
Region | 372-428 | Interaction with host DAXX | ||||
Sequence: GIQLDQKIIILYMINWGKEAVNHFHLGDDMDPELRQLAQALVDTKVKEISNQEPLKI |
Domain
The N-terminus is required for chaperone activity and, in trimeric form, this region likely serves in high affinity vRNA panhandle recognition (By similarity).
The N-terminus also contains a coiled coil region, which probably participates in but is insufficient to initiate N trimerization (By similarity).
The YxxL motif is indispensable for the interaction with host MAP1LC3B (By similarity).
The central region is involved in specific RNA-binding (By similarity).
Has distinct cap- and RNA-binding sites so it can bind simultaneously both the vRNA and mRNA cap (By similarity).
The N-terminus also contains a coiled coil region, which probably participates in but is insufficient to initiate N trimerization (By similarity).
The YxxL motif is indispensable for the interaction with host MAP1LC3B (By similarity).
The central region is involved in specific RNA-binding (By similarity).
Has distinct cap- and RNA-binding sites so it can bind simultaneously both the vRNA and mRNA cap (By similarity).
Sequence similarities
Belongs to the hantavirus nucleocapsid protein family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length428
- Mass (Da)47,804
- Last updated2012-10-03 v1
- Checksum02360769A5F48F3D