NCAP_PIV5
ID NCAP_PIV5 Reviewed; 509 AA.
AC Q88435;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Nucleoprotein;
DE AltName: Full=Nucleocapsid protein;
DE Short=NP;
DE Short=Protein N;
GN Name=NP; Synonyms=N;
OS Parainfluenza virus 5 (strain W3) (PIV5) (Simian virus 5).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Rubulavirinae;
OC Orthorubulavirus; Mammalian orthorubulavirus 5.
OX NCBI_TaxID=11208;
OH NCBI_TaxID=9615; Canis lupus familiaris (Dog) (Canis familiaris).
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=1320792; DOI=10.1016/0168-1702(92)90057-g;
RA Parks G.D., Ward C.D., Lamb R.A.;
RT "Molecular cloning of the NP and L genes of simian virus 5: identification
RT of highly conserved domains in paramyxovirus NP and L proteins.";
RL Virus Res. 22:259-279(1992).
RN [2]
RP INTERACTION WITH PROTEIN P AND PROTEIN V.
RX PubMed=8862406; DOI=10.1006/viro.1996.0513;
RA Randall R.E., Bermingham A.;
RT "NP:P and NP:V interactions of the paramyxovirus simian virus 5 examined
RT using a novel protein:protein capture assay.";
RL Virology 224:121-129(1996).
CC -!- FUNCTION: Encapsidates the genome, protecting it from nucleases. The
CC nucleocapsid (NC) has a helical structure. The encapsidated genomic RNA
CC is termed the NC and serves as template for transcription and
CC replication. During replication, encapsidation by N is coupled to RNA
CC synthesis and all replicative products are resistant to nucleases.
CC -!- SUBUNIT: Homomultimerizes to form the nucleocapsid. Binds to viral
CC genomic RNA. In nucleocapsid, binds the P protein and thereby positions
CC the polymerase on the template. Binds to P and V protein, which might
CC be chaperones to keep nucleoprotein soluble before multimerization on
CC viral replicated RNA.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}. Host cytoplasm
CC {ECO:0000250}.
CC -!- DOMAIN: Ncore is globular and carries regions required for N self-
CC assembly and RNA-binding. Ntail is an intrinsically disordered
CC monomeric domain (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the paramyxoviruses nucleocapsid family.
CC {ECO:0000305}.
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DR EMBL; M81442; AAA47880.1; -; Genomic_RNA.
DR EMBL; AF052755; AAC95511.1; -; Genomic_RNA.
DR PDB; 4XJN; X-ray; 3.11 A; A/B/C/D/E/F/G/H/I/J/K/L/M=1-509.
DR PDB; 5WKN; X-ray; 2.65 A; A/B=32-372.
DR PDBsum; 4XJN; -.
DR PDBsum; 5WKN; -.
DR SMR; Q88435; -.
DR Proteomes; UP000007232; Genome.
DR GO; GO:0019029; C:helical viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR InterPro; IPR002021; Paramyx_ncap.
DR Pfam; PF00973; Paramyxo_ncap; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Capsid protein; Helical capsid protein; Host cytoplasm;
KW Ribonucleoprotein; RNA-binding; Viral nucleoprotein; Virion.
FT CHAIN 1..509
FT /note="Nucleoprotein"
FT /id="PRO_0000142686"
FT REGION 1..400
FT /note="Ncore"
FT /evidence="ECO:0000250"
FT REGION 401..509
FT /note="Ntail"
FT /evidence="ECO:0000250"
FT REGION 452..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 4..17
FT /evidence="ECO:0007829|PDB:4XJN"
FT STRAND 18..22
FT /evidence="ECO:0007829|PDB:4XJN"
FT HELIX 45..60
FT /evidence="ECO:0007829|PDB:5WKN"
FT HELIX 66..78
FT /evidence="ECO:0007829|PDB:5WKN"
FT HELIX 82..88
FT /evidence="ECO:0007829|PDB:5WKN"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:5WKN"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:5WKN"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:5WKN"
FT HELIX 124..134
FT /evidence="ECO:0007829|PDB:5WKN"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:4XJN"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:5WKN"
FT STRAND 145..149
FT /evidence="ECO:0007829|PDB:5WKN"
FT HELIX 160..176
FT /evidence="ECO:0007829|PDB:5WKN"
FT TURN 177..179
FT /evidence="ECO:0007829|PDB:4XJN"
FT HELIX 195..201
FT /evidence="ECO:0007829|PDB:5WKN"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:5WKN"
FT HELIX 213..225
FT /evidence="ECO:0007829|PDB:5WKN"
FT HELIX 227..240
FT /evidence="ECO:0007829|PDB:5WKN"
FT TURN 245..247
FT /evidence="ECO:0007829|PDB:5WKN"
FT HELIX 249..261
FT /evidence="ECO:0007829|PDB:5WKN"
FT TURN 262..265
FT /evidence="ECO:0007829|PDB:5WKN"
FT HELIX 267..275
FT /evidence="ECO:0007829|PDB:5WKN"
FT STRAND 277..279
FT /evidence="ECO:0007829|PDB:5WKN"
FT HELIX 282..285
FT /evidence="ECO:0007829|PDB:5WKN"
FT HELIX 287..289
FT /evidence="ECO:0007829|PDB:5WKN"
FT HELIX 290..306
FT /evidence="ECO:0007829|PDB:5WKN"
FT HELIX 307..312
FT /evidence="ECO:0007829|PDB:5WKN"
FT TURN 313..317
FT /evidence="ECO:0007829|PDB:5WKN"
FT HELIX 321..324
FT /evidence="ECO:0007829|PDB:5WKN"
FT HELIX 326..328
FT /evidence="ECO:0007829|PDB:5WKN"
FT HELIX 330..343
FT /evidence="ECO:0007829|PDB:5WKN"
FT HELIX 345..347
FT /evidence="ECO:0007829|PDB:5WKN"
FT HELIX 359..370
FT /evidence="ECO:0007829|PDB:5WKN"
FT STRAND 372..374
FT /evidence="ECO:0007829|PDB:4XJN"
FT HELIX 378..383
FT /evidence="ECO:0007829|PDB:4XJN"
FT HELIX 388..400
FT /evidence="ECO:0007829|PDB:4XJN"
SQ SEQUENCE 509 AA; 56535 MW; EE2B8BDB35DECB94 CRC64;
MSSVLKAYER FTLTQELQDQ SEEGTIPPTT LKPVIRVFIL TSNNPELRSR LLLFCLRIVL
SNGARDSHRF GALLTMFSLP SATMLNHVKL ADQSPEADIE RVEIDGFEEG SFRLIPNARS
GMSRGEINAY AALAEDLPDT LNHATPFVDS EVEGTAWDEI ETFLDMCYSV LMQAWIVTCK
CMTAPDQPAA SIEKRLQKYR QQGRINPRYL LQPEARRIIQ NVIRKGMVVR HFLTFELQLA
RAQSLVSNRY YAMVGDVGKY IENCGMGGFF LTLKYALGTR WPTLALAAFS GELTKLKSLM
ALYQTLGEQA RYLALLESPH LMDFAAANYP LLYSYAMGIG YVLDVNMRNY AFSRSYMNKT
YFQLGMETAR KQQGAVDMRM AEDLGLTQAE RTEMANTLAK LTTANRGADT RGGVNPFSSV
TGTTQVPAAA TGDTLESYMA ADRLRQRYAD AGTHDDEMPP LEEEEEDDTS AGPRTGPTLE
QVALDIQNAA VGAPIHTDDL NAALGDLDI
