ID   NCAP_PHODV              Reviewed;         523 AA.
AC   P35944;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 2.
DT   02-JUN-2021, entry version 66.
DE   RecName: Full=Nucleoprotein;
DE   AltName: Full=Nucleocapsid protein;
DE            Short=NP;
DE            Short=Protein N;
GN   Name=N; Synonyms=NP;
OS   Phocine distemper virus (PDV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC   Morbillivirus.
OX   NCBI_TaxID=11240;
OH   NCBI_TaxID=9709; Phocidae (true seals).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate DK88-4A;
RX   PubMed=1634877; DOI=10.1099/0022-1317-73-4-885;
RA   Blixenkrone-Moeller M., Sharma B., Varsanyi T., Hu A., Norrby E.,
RA   Koevamees J.;
RT   "Sequence analysis of the genes encoding the nucleocapsid protein and
RT   phosphoprotein (P) of phocid distemper virus, and editing of the P gene
RT   transcript.";
RL   J. Gen. Virol. 73:885-893(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 392-523.
RC   STRAIN=Isolate Ulster/88;
RX   PubMed=1588321; DOI=10.1099/0022-1317-73-5-1189;
RA   Curran M.D., O'Loan D., Kennedy S., Rima B.K.;
RT   "Molecular characterization of phocine distemper virus: gene order and
RT   sequence of the gene encoding the attachment (H) protein.";
RL   J. Gen. Virol. 73:1189-1194(1992).
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 (By
CC       similarity). {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; X75717; CAA53376.1; -; Genomic_RNA.
DR   EMBL; D10371; BAA01202.1; -; Genomic_RNA.
DR   PIR; JQ1608; JQ1608.
DR   SMR; P35944; -.
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..523
FT                   /note="Nucleoprotein"
FT                   /id="PRO_0000142665"
FT   REGION          1..400
FT                   /note="Ncore"
FT                   /evidence="ECO:0000250"
FT   REGION          401..523
FT                   /note="Ntail"
FT                   /evidence="ECO:0000250"
FT   REGION          423..442
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          500..523
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VARIANT         491..492
FT                   /note="DG -> EA (in strain: Isolate Ulster/88)"
FT   VARIANT         516
FT                   /note="H -> Y (in strain: Isolate Ulster/88)"
SQ   SEQUENCE   523 AA;  58259 MW;  BABB471329F56443 CRC64;
     MASLLKSLSL FKKTREQPPL ASGSGGAIRG IKHVIIVLIP GDSSIVTRSR LLDRLVRMVG
     DPEVSGPKLT GVLISILSLF VESPGQLIQR IIDDPDISIK LVEVIPSINS TCGLTFASRG
     ASLDAEADEF FGTMDEGSKD HNQMGWLENK DIIDIEVNDA EQFNILLASI LAQIWILLAK
     AVTAPDTAAD SEMRRWIKYT QQRRVIGEFR MNKIWLDIVR NRIAEDLSLR RFMVALILDI
     KRSPGNKPRI AEMICDIDNY IVEAGLASFI LTIKFGIETM YPALGLHEFS GELTTIESLM
     VLYQQMGETA PYMVILENSV QNKFSAGSYP LLWSYAMGVG VELENSMGGL NFGRSYFDPA
     YFRLGQEMVR RSAGKVSSTF AAEFGITKEE AQLVSEIVSR TTEDRTTRAT GPKQSQITFL
     HSERNEAPNQ RLPPITMKSE FQGGDKYSNQ LIDDRLSGYT SDVQSSEWDE SRQITQLTQE
     GDHDNDQQSM DGLAKMRQLT KILNQSDTNG EVSPAHNDRD LLS