NCAP_PI3B
ID NCAP_PI3B Reviewed; 515 AA.
AC P06161;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 23-FEB-2022, 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 Bovine parainfluenza 3 virus (BPIV-3).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC Respirovirus.
OX NCBI_TaxID=11215;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate 910N;
RX PubMed=3031614; DOI=10.1093/nar/15.7.2927;
RA Sakai Y., Suzu S., Shioda T., Shibuta H.;
RT "Nucleotide sequence of the bovine parainfluenza 3 virus genome: its 3' end
RT and the genes of NP, P, C and M proteins.";
RL Nucleic Acids Res. 15:2927-2944(1987).
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 (By similarity).
CC {ECO:0000250}.
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 -!- 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; Y00114; CAA68293.1; -; Genomic_DNA.
DR EMBL; D84095; BAA12213.1; -; Genomic_RNA.
DR SMR; P06161; -.
DR Proteomes; UP000133413; 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 3: Inferred from homology;
KW Capsid protein; Helical capsid protein; Host cytoplasm; Ribonucleoprotein;
KW RNA-binding; Viral nucleoprotein; Virion.
FT CHAIN 1..515
FT /note="Nucleoprotein"
FT /id="PRO_0000142666"
FT REGION 1..400
FT /note="Ncore"
FT /evidence="ECO:0000250"
FT REGION 401..515
FT /note="Ntail"
FT /evidence="ECO:0000250"
FT REGION 424..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..492
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..515
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 515 AA; 57355 MW; 0A25ACA65AF24B4D CRC64;
MLSLFDTFSA RRQENITKSA GGAVIPGQKN TVSIFALGPS ITDDNDKMTL ALLFLSHSLD
NEKQHAQRAG FLVSLLSMAY ANPELYLTSN GSNADVKYVI YMIEKDPGRQ KYGGLVVKTR
EMVYEKTTDW MFGSDLEYDQ DNMLQNGRST STIEDLVHTF GYPSCLGALI IQVWIILVKA
ITSISGLRKG FFTRLEAFRQ DGTVKSSLVL SGDAVEQIGS IMRSQQSLVT LMVETLITMN
TGRNDLTTIE KNIQIVGNYI RDAGLASFFN TIRYGIETRM AALTLSTLRP DINRLKALIE
LYLSKGPRAP FICILRDPVH GEFAPGNYPA LWSYAMGVAV VQNKAMQQYV TGRSYLDIEM
FQLGQAVARD AESQMSSILE DELGVTQEAK QSLKKHMKNI SSSDTTFHKP TGGSAIEMAI
DEEAEQPESR GDQDQGNEPQ SSIVPYAWAD ETRSDTQTES VTEIESIKTE QRNIRDRLNK
RLNEKRKQSD PKSTNIANDT NQTEIDDLFS AFGNN
