| General information | | DisProt: | DP00629 | | Name: | Nucleoprotein | | Synonym(s): | NCAP_SENDF
Nucleocapsid protein
NP
Protein N
| | First appeared in release: | Release 5.2 (08/07/2010) | | UniProt: | Q07097 | | UniGene: | | | SwissProt: | NCAP_SENDF | | TrEMBL: | | | NCBI (GI): | 127928 | | Source organism: | Sendai virus (strain Fushimi)(SeV) | | Sequence length: | 524 | | Percent disordered: | 23% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MAGLLSTFDT FSSRRSESIN KSGGGAVIPG QRSTVSVFVL GPSVTDDADK LFIATTFLAH - 60
SLDTDKQHSQ RGGFLVSLLA MAYSSPELYL TTNGVNADVK YVIYNIEKDP KRTKTDGFIV - 120
KTRDMEYERT TEWLFGPMVN KSPLFQGQRV AADPDTLLQT YGYPACLGAI IVQVWIVLVK - 180
AITSSAGLRK GFFNRLEAFR QDGTVKGALV FTGETVEGIG SVMRSQQSLV SLMVETLVTM - 240
NTARSDLTTL EKNIQIVGNY IRDAGLASFM NTIKYGVETK MAALTLSNLR PDINKLRSLI - 300
DTYLSKGPRA PFICILKDPV HGEFAPGNYP ALWSYAMGVA VVQNKAMQQY VTGGTYLDME - 360
MFLLGQAVAK DAESKISSAL EDELGVTDTA KERLRHHLAN LSGGDGAYHE PTGGGAIEVA - 420
LDNADIDLET EAHADQDARG WGGESGERWA RQVSGGHFVT LHGAERLEEE TNDEDVSDIE - 480
RRIAMRLAER RQEDSATHGD EGRNNGVDHD EDDDAAAVAG IGGI
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| Functional narrative |
Encapsidates the genome in a ratio of one N per six ribonucleotides, protecting it from nucleases. The nucleocapsid (NC) has a helical structure with 13.07 N per turn. The encapsidated genomic RNA is termed the NC and serves as template for transcription and replication. Replication is dependent on intracellular concentration of newly synthesized N, termed N0, which corresponds to the protein not associated with RNA. In contrast, when associated with RNA, it is termed N. During replication, encapsidation by N0 is coupled to RNA synthesis and all replicative products are resistant to nucleases.
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| 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.
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| Region 1 | | Type: | Disordered - Extended | | Name: | N-tail | | Location: | 402 - 524 | | Length: | 123 | | Region sequence: |
SGGDGAYHKPTGGGAIEVALDNADIDLETEAHADQDARGWGGESGERWARQVSGGHFVTL
HGAERLEEETNDEDVSDIERRIAMRLAERRQEDSATHGDEGRNNGVDHDEDDDAAAVAGI
GGI | | Modification type: | Engineered
Fragment
| | PDB: | | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | Molecular recognition effectors
Molecular assembly
Entropic chain
| | Functional subclasses: | Protein-DNA binding
Protein-protein binding
| Detection methods:
- SDS-PAGE gel, Aberrant mobility on (293 K; pH: 8; Imidazole (elution buffer) 30 uL; NaCl (0, 100, 300 or 500 uM); Ni beads (QIAGEN) 50 uL; SeV N-tail (protein) 8 ug; SeV PX, His-tagged (binding partner) 5 Ug; Tris-HCL (buffer) 50 mM)
- Nuclear magnetic resonance (NMR) (298 K; pH: 6; D2O 10 %; KPO4 (buffer) 50 mM; NaCl 500 mM; NaN3 (protease cocktail inhibitor) 0.02 %; SeV N-tail (protein) 0.73 mM; SeV PX, 15N-labelled (binding partner, plus DTT) 0.33 mM)
| References:
- Houben K, Marion D, Tarbouriech N, Ruigrok RW, Blanchard L. "Interaction of the C-terminal domains of sendai virus N and P proteins: comparison of polymerase-nucleocapsid interactions within the paramyxovirus family." J Virol. 2007; 81(13): 6807-16. PubMed: 17459940
| Comments:Houben, et al (2007), used a synthetic coding of the Harris strain of SeV N-Tail that has the same amino acid sequence as the Fushimi strain (UniProt Q07097, used as the basis of this DisProt record), excepting a single mutation (E410K).
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| References |
- Houben K, Marion D, Tarbouriech N, Ruigrok RW, Blanchard L. "Interaction of the C-terminal domains of sendai virus N and P proteins: comparison of polymerase-nucleocapsid interactions within the paramyxovirus family." J Virol. 2007; 81(13): 6807-16. PubMed: 17459940
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