ID   NCAP_RINDU              Reviewed;         525 AA.
AC   P41359;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   02-JUN-2021, entry version 67.
DE   RecName: Full=Nucleoprotein;
DE   AltName: Full=Nucleocapsid protein;
DE            Short=NP;
DE            Short=Protein N;
GN   Name=N; Synonyms=NP;
OS   Rinderpest virus (strain Kuwait 82/1) (RDV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC   Morbillivirus.
OX   NCBI_TaxID=39006;
OH   NCBI_TaxID=9915; Bos indicus (Zebu).
OH   NCBI_TaxID=9913; Bos taurus (Bovine).
OH   NCBI_TaxID=89462; Bubalus bubalis (Domestic water buffalo).
OH   NCBI_TaxID=9925; Capra hircus (Goat).
OH   NCBI_TaxID=9933; Gazella (gazelles).
OH   NCBI_TaxID=9894; Giraffa camelopardalis (Giraffe).
OH   NCBI_TaxID=9832; Hippopotamus.
OH   NCBI_TaxID=9940; Ovis aries (Sheep).
OH   NCBI_TaxID=9821; Suidae (pigs).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=7897350; DOI=10.1099/0022-1317-76-3-593;
RA   Baron M.D., Barrett T.;
RT   "Sequencing and analysis of the nucleocapsid (N) and polymerase (L) genes
RT   and the terminal extragenic domains of the vaccine strain of rinderpest
RT   virus.";
RL   J. Gen. Virol. 76:593-602(1995).
CC   -!- FUNCTION: Encapsidates the genome in a ratio of 1 N per 6
CC       ribonucleotides, protecting it from nucleases. The nucleocapsid (NC)
CC       has a helical structure. The encapsidated genomic RNA is termed the NC
CC       and serves as template for transcription and replication. During
CC       replication, encapsidation by N is coupled to RNA synthesis and all
CC       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}.
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DR   EMBL; Z34262; CAA84017.1; -; Genomic_RNA.
DR   PIR; S47308; S47308.
DR   SMR; P41359; -.
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   3: Inferred from homology;
KW   Capsid protein; Helical capsid protein; Host cytoplasm; Ribonucleoprotein;
KW   RNA-binding; Viral nucleoprotein; Virion.
FT   CHAIN           1..525
FT                   /note="Nucleoprotein"
FT                   /id="PRO_0000142678"
FT   REGION          1..400
FT                   /note="Ncore"
FT                   /evidence="ECO:0000250"
FT   REGION          401..525
FT                   /note="Ntail"
FT                   /evidence="ECO:0000250"
FT   REGION          402..490
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          506..525
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        402..429
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        430..465
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   525 AA;  58253 MW;  9AD1BD2699AB1F00 CRC64;
     MASLLKSLAL FKKNKDKPPL AAGSGGAIRG IKHVIIVPIP GDSSITTRSR LLDRLVKMVG
     DPDISGPKLT GALISILSLF VESPGQLIQR ITDDPDISIK LVEVVQSDKT QSGLTFASRG
     TSMDDEADRY FTYDEPNDGE ERQSYWFENR EIQDIEVQDP EGFNMILATI LAQIWILLAK
     AVTAPDTAAD SELRRWVKYT QQRRVIGEFK LDKGWLDTVR NRIAEDLSLR RFMVALILDI
     KRTPGNKPRI AEMICDIDTY IVEAGLASFI LTIKFGIETM YPALGLHEFA GELSTIESLM
     NLYQQMGELA PYMVILENSI QNKFSAGAYP LLWSYAMGVG VELENSMGGL NFGRSYFDPA
     YFRLGQEMVR RSAGKVSSNL ASELGITEEE ARLVSEIAAY TGDDRNNRTS GPKQAQVSFL
     RTDQGGETQN NASKRDEARA PQIRKEARTS SKSDKYKEDT DKEPMSPSVK TLIDVDTTPE
     VDTDPLGSKK SAEALIRLQA MASILEDSTF GNDSPRAYND RDLLS