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NCAP_IBVBU
ID   NCAP_IBVBU              Reviewed;         409 AA.
AC   P69598; Q89902;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2005, sequence version 1.
DT   02-JUN-2021, entry version 72.
DE   RecName: Full=Nucleoprotein {ECO:0000255|HAMAP-Rule:MF_04097};
DE   AltName: Full=Nucleocapsid protein {ECO:0000255|HAMAP-Rule:MF_04097};
DE            Short=NC {ECO:0000255|HAMAP-Rule:MF_04097};
DE            Short=Protein N {ECO:0000255|HAMAP-Rule:MF_04097};
GN   Name=N {ECO:0000255|HAMAP-Rule:MF_04097}; ORFNames=6;
OS   Avian infectious bronchitis virus (strain Beaudette US) (IBV).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC   Gammacoronavirus; Igacovirus.
OX   NCBI_TaxID=160750;
OH   NCBI_TaxID=9031; Gallus gallus (Chicken).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=11711626; DOI=10.1128/jvi.75.24.12359-12369.2001;
RA   Casais R., Thiel V., Siddell S.G., Cavanagh D., Britton P.;
RT   "Reverse genetics system for the avian coronavirus infectious bronchitis
RT   virus.";
RL   J. Virol. 75:12359-12369(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_04097}.
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_04097}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04097}. Host
CC       endoplasmic reticulum-Golgi intermediate compartment
CC       {ECO:0000255|HAMAP-Rule:MF_04097}. Host Golgi apparatus
CC       {ECO:0000255|HAMAP-Rule:MF_04097}. 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_04097}.
CC   -!- PTM: ADP-ribosylated. The ADP-ribosylation is retained in the virion
CC       during infection. {ECO:0000255|HAMAP-Rule:MF_04097}.
CC   -!- PTM: Phosphorylated on serine and threonine residues.
CC       {ECO:0000255|HAMAP-Rule:MF_04097}.
CC   -!- SIMILARITY: Belongs to the gammacoronavirus nucleocapsid protein
CC       family. {ECO:0000255|HAMAP-Rule:MF_04097}.
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DR   EMBL; AJ311362; CAC39307.1; -; Genomic_RNA.
DR   PDB; 2BTL; X-ray; 1.95 A; B=29-160.
DR   PDB; 2BXX; X-ray; 1.85 A; A/B=29-160.
DR   PDB; 2C86; X-ray; 3.00 A; A/B=29-160.
DR   PDBsum; 2BTL; -.
DR   PDBsum; 2BXX; -.
DR   PDBsum; 2C86; -.
DR   SMR; P69598; -.
DR   EvolutionaryTrace; P69598; -.
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_04097; GAMMA_CORONA_NCAP; 1.
DR   InterPro; IPR044344; N_prot_C_CoV.
DR   InterPro; IPR044345; N_prot_N_CoV.
DR   InterPro; IPR042547; NCAP_gCoV.
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   1: Evidence at protein level;
KW   3D-structure; ADP-ribosylation; Disulfide bond; Host Golgi apparatus;
KW   Phosphoprotein; Ribonucleoprotein; RNA-binding; Transcription;
KW   Transcription regulation; Viral nucleoprotein; Virion.
FT   CHAIN           1..409
FT                   /note="Nucleoprotein"
FT                   /id="PRO_0000105978"
FT   DOMAIN          31..156
FT                   /note="CoV N NTD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01276"
FT   DOMAIN          215..331
FT                   /note="CoV N CTD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01277"
FT   REGION          1..84
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          29..160
FT                   /note="RNA-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04097"
FT   REGION          121..194
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          226..333
FT                   /note="Dimerization"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04097"
FT   REGION          327..396
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        126..140
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        165..179
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        327..342
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        356..389
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         190
FT                   /note="Phosphoserine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04097"
FT   MOD_RES         192
FT                   /note="Phosphoserine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04097"
FT   MOD_RES         378
FT                   /note="Phosphothreonine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04097"
FT   MOD_RES         379
FT                   /note="Phosphoserine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04097"
FT   DISULFID        281..308
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04097"
FT   DISULFID        320..323
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04097"
FT   STRAND          39..45
FT                   /evidence="ECO:0007829|PDB:2C86"
FT   STRAND          51..53
FT                   /evidence="ECO:0007829|PDB:2C86"
FT   STRAND          60..62
FT                   /evidence="ECO:0007829|PDB:2C86"
FT   HELIX           64..66
FT                   /evidence="ECO:0007829|PDB:2C86"
FT   STRAND          68..73
FT                   /evidence="ECO:0007829|PDB:2C86"
FT   STRAND          80..83
FT                   /evidence="ECO:0007829|PDB:2C86"
FT   STRAND          90..95
FT                   /evidence="ECO:0007829|PDB:2C86"
FT   TURN            100..103
FT                   /evidence="ECO:0007829|PDB:2C86"
FT   STRAND          113..117
FT                   /evidence="ECO:0007829|PDB:2C86"
FT   TURN            134..136
FT                   /evidence="ECO:0007829|PDB:2C86"
SQ   SEQUENCE   409 AA;  45032 MW;  562F39C475DB8872 CRC64;
     MASGKAAGKT DAPAPVIKLG GPKPPKVGSS GNASWFQAIK AKKLNTPPPK FEGSGVPDNE
     NIKPSQQHGY WRRQARFKPG KGGRKPVPDA WYFYYTGTGP AADLNWGDTQ DGIVWVAAKG
     ADTKSRSNQG TRDPDKFDQY PLRFSDGGPD GNFRWDFIPL NRGRSGRSTA ASSAAASRAP
     SREGSRGRRS DSGDDLIARA AKIIQDQQKK GSRITKAKAD EMAHRRYCKR TIPPNYRVDQ
     VFGPRTKGKE GNFGDDKMNE EGIKDGRVTA MLNLVPSSHA CLFGSRVTPK LQLDGLHLRF
     EFTTVVPCDD PQFDNYVKIC DQCVDGVGTR PKDDEPKPKS RSSSRPATRG NSPAPRQQRP
     KKEKKLKKQD DEADKALTSD EERNNAQLEF YDEPKVINWG DAALGENEL
 
 
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