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NCAP_CVBLU
ID   NCAP_CVBLU              Reviewed;         448 AA.
AC   Q8V432;
DT   16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   02-JUN-2021, entry version 76.
DE   RecName: Full=Nucleoprotein {ECO:0000255|HAMAP-Rule:MF_04096};
DE   AltName: Full=Nucleocapsid protein {ECO:0000255|HAMAP-Rule:MF_04096};
DE            Short=NC {ECO:0000255|HAMAP-Rule:MF_04096};
DE            Short=Protein N {ECO:0000255|HAMAP-Rule:MF_04096};
GN   Name=N {ECO:0000255|HAMAP-Rule:MF_04096}; ORFNames=7a;
OS   Bovine coronavirus (strain 98TXSF-110-LUN) (BCoV-LUN) (BCV).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC   Betacoronavirus; Embecovirus.
OX   NCBI_TaxID=233264;
OH   NCBI_TaxID=9913; Bos taurus (Bovine).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=11714968; DOI=10.1099/0022-1317-82-12-2927;
RA   Chouljenko V.N., Lin X.Q., Storz J., Kousoulas K.G., Gorbalenya A.E.;
RT   "Comparison of genomic and predicted amino acid sequences of respiratory
RT   and enteric bovine coronaviruses isolated from the same animal with fatal
RT   shipping pneumonia.";
RL   J. Gen. Virol. 82:2927-2933(2001).
CC   -!- FUNCTION: Packages the positive strand viral genome RNA into a helical
CC       ribonucleocapsid (RNP) and plays a fundamental role during virion
CC       assembly through its interactions with the viral genome and membrane
CC       protein M. Plays an important role in enhancing the efficiency of
CC       subgenomic viral RNA transcription as well as viral replication.
CC       {ECO:0000255|HAMAP-Rule:MF_04096}.
CC   -!- SUBUNIT: Homooligomer. Both monomeric and oligomeric forms interact
CC       with RNA. Interacts with protein M. Interacts with NSP3; this
CC       interaction serves to tether the genome to the newly translated
CC       replicase-transcriptase complex at a very early stage of infection.
CC       {ECO:0000255|HAMAP-Rule:MF_04096}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04096}. Host
CC       endoplasmic reticulum-Golgi intermediate compartment
CC       {ECO:0000255|HAMAP-Rule:MF_04096}. Host Golgi apparatus
CC       {ECO:0000255|HAMAP-Rule:MF_04096}. Note=Located inside the virion,
CC       complexed with the viral RNA. Probably associates with ER-derived
CC       membranes where it participates in viral RNA synthesis and virus
CC       budding. {ECO:0000255|HAMAP-Rule:MF_04096}.
CC   -!- PTM: ADP-ribosylated. The ADP-ribosylation is retained in the virion
CC       during infection. {ECO:0000255|HAMAP-Rule:MF_04096}.
CC   -!- PTM: Phosphorylated on serine and threonine residues.
CC       {ECO:0000255|HAMAP-Rule:MF_04096}.
CC   -!- SIMILARITY: Belongs to the betacoronavirus nucleocapsid protein family.
CC       {ECO:0000255|HAMAP-Rule:MF_04096}.
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DR   EMBL; AF391542; AAL57313.1; -; Genomic_RNA.
DR   SMR; Q8V432; -.
DR   PRIDE; Q8V432; -.
DR   Proteomes; UP000008571; Genome.
DR   GO; GO:0044172; C:host cell endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell.
DR   GO; GO:0044177; C:host cell Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   CDD; cd21595; CoV_N-CTD; 1.
DR   CDD; cd21554; CoV_N-NTD; 1.
DR   HAMAP; MF_04096; BETA_CORONA_NCAP; 1.
DR   InterPro; IPR044344; N_prot_C_CoV.
DR   InterPro; IPR044345; N_prot_N_CoV.
DR   InterPro; IPR043505; NCAP_bCoV.
DR   InterPro; IPR001218; Nucleocap_CoV.
DR   InterPro; IPR037179; Nucleocapsid_C.
DR   InterPro; IPR037195; Nucleocapsid_N.
DR   Pfam; PF00937; CoV_nucleocap; 1.
DR   PIRSF; PIRSF003888; Corona_nucleocap; 1.
DR   SUPFAM; SSF103068; SSF103068; 1.
DR   SUPFAM; SSF110304; SSF110304; 1.
DR   PROSITE; PS51929; COV_N_CTD; 1.
DR   PROSITE; PS51928; COV_N_NTD; 1.
PE   3: Inferred from homology;
KW   ADP-ribosylation; Host Golgi apparatus; Phosphoprotein; Ribonucleoprotein;
KW   RNA-binding; Transcription; Transcription regulation; Viral nucleoprotein;
KW   Virion.
FT   CHAIN           1..448
FT                   /note="Nucleoprotein"
FT                   /id="PRO_0000105992"
FT   DOMAIN          61..190
FT                   /note="CoV N NTD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01276"
FT   DOMAIN          259..384
FT                   /note="CoV N CTD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01277"
FT   REGION          1..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          52..194
FT                   /note="RNA-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04096"
FT   REGION          158..231
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          266..384
FT                   /note="Dimerization"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04096"
FT   REGION          383..420
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        191..231
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         167
FT                   /note="Phosphoserine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04096"
FT   MOD_RES         174
FT                   /note="Phosphothreonine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04096"
FT   MOD_RES         191
FT                   /note="Phosphoserine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04096"
FT   MOD_RES         390
FT                   /note="Phosphoserine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04096"
FT   MOD_RES         427
FT                   /note="Phosphothreonine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04096"
SQ   SEQUENCE   448 AA;  49285 MW;  F2B6BB2485D3F8FB CRC64;
     MSFTPGKQSS SRASSGNRSG NGILKWADQS DQSRNVQTRG RRAQSKQTAT SQQPSGGNVV
     PYYSWFSGIT QFQKGKEFEF AEGQGVPIAP GVPATEAKGY WYRHNRRSFK TADGNQRQLL
     PRWYFYYLGT GPHAKDQYGT DIDGVYWVAS NQADVNTPAD ILDRDPSSDE AIPTRFPPGT
     VLPQGYYIEG SGRSAPNSRS TSRASSRASS AGSRSRANSG NRTPTSGVTP DMADQIASLV
     LAKLGKDAAK PQQVTKQTAK EIRQKILNKP RQKRSPNKQC TVQQCFGKRG PNQNFGGGEM
     LKLGTSDPQF PILAELAPTA GAFFFGSRLE LAKVQNLSGN LDEPQKDVYE LRYNGAIRFD
     STLSGFETIM KVLNENLNAY QQQDGTMNMS PKPQRQRGQK NGQGENDNIS VAAPKSRVQQ
     NKIRELTAED ISLLKKMDEP FTEDTSEI
 
 
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