NCAP_IBVV1
ID NCAP_IBVV1 Reviewed; 409 AA.
AC Q96605;
DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 02-JUN-2021, entry version 85.
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 V18/91) (IBV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Gammacoronavirus; Igacovirus.
OX NCBI_TaxID=231427;
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; U52601; AAB48162.1; -; mRNA.
DR SMR; Q96605; -.
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_0000105987"
FT DOMAIN 32..157
FT /note="CoV N NTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01276"
FT DOMAIN 217..333
FT /note="CoV N CTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01277"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 30..161
FT /note="RNA-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04097"
FT REGION 167..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 228..335
FT /note="Dimerization"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04097"
FT REGION 327..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..197
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..343
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 192
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04097"
FT MOD_RES 374
FT /note="Phosphothreonine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04097"
FT DISULFID 322..325
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04097"
SQ SEQUENCE 409 AA; 45793 MW; 2C4A5E0AEBBC2B93 CRC64;
MSAGKLKFDS PAPILKLSKN TGSTPPKVGG TGQASWFQSL KEKKRTGTPP TFEGSGVPDN
SNVKPQFQHG YWKRQHRYKP GKGGRKPVAD AWYFYYTGTG PFGDLKWGDS NDDVVWVKAK
GADTSKIGNY GVRDPDKFDQ APLRFTEGGP DNNYRWDFIA LNRGRSRNSS AVTSRENSRP
GSRDSSRGRQ RSRVDDDLID RAAKIIMQQQ KNGSRISKQK ANEMAERKYH KRAIAPGKRI
DEVFGQRRKG QAPNFGDDKM IEEGVKDGRL TAMLNLVPTP HACLLGSMVT AKLQPDGLHV
RFSFETVVKR EDPQFANYSK ICDECVDGVG TRPKDDPTPR SRAASKDRNS APATPKQQRA
KKVHKKKEEE SSLTEEEEEV NKQLEYDDDV TDIPNKIDWG EGAFDDINI
