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NCAP_IBVVI
ID   NCAP_IBVVI              Reviewed;         409 AA.
AC   Q96598;
DT   16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   02-JUN-2021, entry version 87.
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 Vic S) (IBV).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC   Gammacoronavirus; Igacovirus.
OX   NCBI_TaxID=231428;
OH   NCBI_TaxID=9031; Gallus gallus (Chicken).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8955062; DOI=10.1006/viro.1996.0670;
RA   Sapats S.I., Ashton F., Wright P.J., Ignjatovic J.;
RT   "Novel variation in the N protein of avian infectious bronchitis virus.";
RL   Virology 226:412-417(1996).
RN   [2]
RP   SEQUENCE REVISION.
RA   Sapats S.I., Ashton F., Wright P.J., Ignjatovic J.;
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
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; U52594; AAB48155.1; -; mRNA.
DR   SMR; Q96598; -.
DR   PRIDE; Q96598; -.
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   2: Evidence at transcript level;
KW   ADP-ribosylation; Disulfide bond; Host Golgi apparatus; Phosphoprotein;
KW   Ribonucleoprotein; RNA-binding; Transcription; Transcription regulation;
KW   Viral nucleoprotein; Virion.
FT   CHAIN           1..409
FT                   /note="Nucleoprotein"
FT                   /id="PRO_0000105988"
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..32
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          47..84
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          121..145
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          164..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          326..409
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        54..68
FT                   /note="Polar residues"
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..180
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..396
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         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        320..323
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04097"
SQ   SEQUENCE   409 AA;  45149 MW;  F846ABB5C7A7F59A CRC64;
     MASGKAAGKS DAPTPIIKLG GPKPPKIGSS GNASWFQAIK AKKLNVPQPK FEGSGVPDNN
     NIKPSQQHGY WRRQARYKPG KSGRKPVPDA WYFYYTGTGP AADLNWGENQ DGIVWVAAKG
     ADTKSRSNQG TRDPDKFDQY PLRFSDGGPD GNFRWDFIPL NRGRSGRSTA ASSAASSRAP
     SREGSRGRRS GAEDDLIARA AKIIQDQQKR GSRITKAKAD EMAHRRYCKR TIPPGYRVDQ
     VFGPRTKGKE GNFGDDKMNE EGIKDGRVTA TLNLIPSSHA CLFGSRVTPK LQPDGLHLKF
     EFTTVVPRDD PQFDNYVKIC DQCVDGVGTR PKDDEPRPKS RSSSRPATRG NSPAPRQQRP
     KKEKKPKKQD DEVDKALTSD EERNNAQLEF DDEPKVINWG DSALGENEL
 
 
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