| General information | | DisProt: | DP00697 | | Name: | Nucleoprotein | | Synonym(s): | NCAP_NIPAV
Nucleocapsid protein
Protein N
| | First appeared in release: | Release 5.2 (08/07/2010) | | UniProt: | Q9IK92 | | UniGene: | | | SwissProt: | NCAP_NIPAV | | TrEMBL: | | | NCBI (GI): | | | Source organism: | Nipah virus | | Sequence length: | 532 | | Percent disordered: | 25% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
| | | | | |
MSDIFEEAAS FRSYQSKLGR DGRASAATAT LTTKIRIFVP ATNSPELRWE LTLFALDVIR - 60
SPSAAESMKV GAAFTLISMY SERPGALIRS LLNDPDIEAV IIDVGSMVNG IPVMERRGDK - 120
AQEEMEGLMR ILKTARDSSK GKTPFVDSRA YGLRITDMST LVSAVITIEA QIWILIAKAV - 180
TAPDTAEESE TRRWAKYVQQ KRVNPFFALT QQWLTEMRNL LSQSLSVRKF MVEILIEVKK - 240
GGSAKGRAVE IISDIGNYVE ETGMAGFFAT IRFGLETRYP ALALNEFQSD LNTIKSLMLL - 300
YREIGPRAPY MVLLEESIQT KFAPGGYPLL WSFAMGVATT IDRSMGALNI NRGYLEPMYF - 360
RLGQKSARHH AGGIDQNMAN RLGLSSDQVA ELAAAVQETS AGRQESNVQA REAKFAAGGV - 420
LIGGSDQDID EGEEPIEQSG RQSVTFKREM SISSLANSVP SSSVSTSGGT RLTNSLLNLR - 480
SRLAAKAAKE AASSNATDDP AISNRTQGES EKKNNQDLKP AQNDLDFVRA DV
|
| Functional narrative |
Function: Encapsidates the genome protecting it from nucleases. The encapsidated genomic RNA is termed the nucleocapsid (NC) and serves as template for transcription and replication (By similarity).
SUBUNIT: Homomultimerizes to form the nucleocapsid. Binds to viral genomic RNA. N in nucleocapsid binds the P protein and thereby positions the polymerase on the template (By similarity).
Subcellular Location: Virion. Host cytoplasm (By similarity).
SIMILARITY: Belongs to the paramyxoviruses nucleocapsid family.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
|
| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
|
| Region 1 | | Type: | Disordered - Pre-Molten Globule | | Name: | N tail | | Location: | 400 - 532 | | Length: | 133 | | Region sequence: |
SAGRQESNVQAREAKFAAGGVLIGGSDQDIDEGEEPIEQSGRQSVTFKREMSISSLANSV
PSSSVSTSGGTRLTNSLLNLRSRLAAKAAKEAASSNATDDPAISNRTQGESEKKNNQDLK
PAQNDLDFVRADV | | Modification type: | Fragment
Native
| | PDB: | | | Structural/functional type: | Function arises via a pre-molten globule to order transition
| | Functional classes: | Molecular recognition effectors
| | Functional subclasses: | Protein-protein binding
| Detection methods:
- Sensitivity to proteolysis (299 K; pH: 8; thermolysin)
- Nuclear magnetic resonance (NMR) (300 K; pH: 7; D2O 10 %; NaCl 150 mM; N tail 0.1 mM; sodium phosphate 10 mM)
- Circular dichroism (CD) spectroscopy, far-UV (293 K; pH: 7; )
- Dynamic light scattering (298 K; pH: 8; )
- SDS-PAGE gel, Aberrant mobility on
| References:
- Habchi J, Mamelli L, Darbon H, Longhi S. "Structural disorder within Henipavirus nucleoprotein and phosphoprotein: from predictions to experimental assessment." PLoS ONE. 2010; 5(7): e11684. PubMed: 20657787
| Comments:Habchi et al. (2010) found that "Henipah" virus N-tail contained four putative Molecular Recognition Features (MoRF): two alpha-MoRFs at aa 408-422 and 473-493, an irregular I-MoRF at aa 523-532, and a beta-MoRF at aa 444-464. However, based on the experimental CD in TFE studies and the Hydrophobic Cluster Analysis (HCA) plot, the predicted beta-MoRF is more likely an alpha-MoRF.
|
| References |
- Habchi J, Mamelli L, Darbon H, Longhi S. "Structural disorder within Henipavirus nucleoprotein and phosphoprotein: from predictions to experimental assessment." PLoS ONE. 2010; 5(7): e11684. PubMed: 20657787
|
| Comments |
[AV 08/06/2010 PMID 20657787]
|
| If you have any comments or wish to provide additional references to this protein or its disordered region(s), please click here to e-mail us. |
Disprot-footer
|
