ID   NCAP_SV41               Reviewed;         543 AA.
AC   P27018;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   02-JUN-2021, entry version 80.
DE   RecName: Full=Nucleoprotein;
DE   AltName: Full=Nucleocapsid protein;
DE            Short=NP;
DE            Short=Protein N;
GN   Name=N; Synonyms=NP;
OS   Simian virus 41 (SV41).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Paramyxoviridae; Rubulavirinae;
OC   Orthorubulavirus.
OX   NCBI_TaxID=2560766;
OH   NCBI_TaxID=314293; Simiiformes.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Toshiba/Chanock;
RX   PubMed=1654380; DOI=10.1099/0022-1317-72-9-2289;
RA   Tsurudome M., Oki N., Higuchi Y., Miyahara K., Yoshimoto M., Mutsuga N.,
RA   Kitada S., Ogawa M., Miyahara Y., Okamoto K., Kawano M., Komada H.,
RA   Matsumura H., Kusagawa S., Nishio M., Ito Y.;
RT   "Molecular relationships between human parainfluenza virus type 2, and
RT   simian viruses 41 and 5: determination of nucleoprotein gene sequences of
RT   simian viruses 41 and 5.";
RL   J. Gen. Virol. 72:2289-2292(1991).
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 (By similarity). {ECO:0000250}.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; S56065; AAB19770.1; -; mRNA.
DR   EMBL; X64275; CAA45570.1; -; Genomic_RNA.
DR   PIR; JQ1270; JQ1270.
DR   SMR; P27018; -.
DR   Proteomes; UP000108270; 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   2: Evidence at transcript level;
KW   Capsid protein; Helical capsid protein; Host cytoplasm; Reference proteome;
KW   Ribonucleoprotein; RNA-binding; Viral nucleoprotein; Virion.
FT   CHAIN           1..543
FT                   /note="Nucleoprotein"
FT                   /id="PRO_0000142685"
FT   REGION          1..400
FT                   /note="Ncore"
FT                   /evidence="ECO:0000250"
FT   REGION          401..543
FT                   /note="Ntail"
FT                   /evidence="ECO:0000250"
FT   REGION          448..543
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        461..475
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        503..517
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   543 AA;  60576 MW;  3992B016A89766E4 CRC64;
     MSSVLKTFER FTIQQELQDH EEDTPVPLET IRPLIRVFVV NSNDPALRAQ LLLFNLRIIM
     SNTARESHKT GALLSMFSLP AAAMGNHLKL ATRSPEASID RVEITGFEGR SFRVVPDARS
     TMSRAEVLAY EAIAEDIPDT LNHKTPFVNA DVEQGDYDET EGFLELCYSV LMQAWIVTCK
     CMTAPDQPPI SIEKRMAKYQ QQGRINPRFI LQPEARRIIQ NAIRKAMVVR HFLTYELQMA
     QSKTLLANRY YAMVGDVGKY IEHSGMGGFF CTLKYGLGTR WPTLALAAFS GELQKLKALM
     LHYQSLGPMA KYMALLESPK LMDFAPAEYP LMYSYAMGIG TVIDTNMRNY AYGRSYLNPQ
     YFQLGVETAR KQQGAVDHRT AEDLGMSQAD KVELAATLAK LTIGQGGRGR QPLDDPFAGA
     AGDYQGAAAG GAQGFDYASR RVRKYNDYES DEEAGMDDDY EQEAREGRGY DDDDARQGIG
     GQSGFDFSVP QRAPGMSDEE FQAQMTKYIQ HVQQHYQEAQ EGAEDGGYNQ TTDDQGAGGD
     FDT