NCAP_IBVSA
ID NCAP_IBVSA Reviewed; 409 AA.
AC Q8JMI6;
DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 02-JUN-2021, entry version 75.
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 SAIB20) (IBV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Gammacoronavirus; Igacovirus.
OX NCBI_TaxID=231426;
OH NCBI_TaxID=9031; Gallus gallus (Chicken).
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Hongning W., Sheng Z., Chun L.;
RT "Sequence analysis of the N nucleocapsid protein gene of infectious
RT bronchitis virus strains in Sichuan, China.";
RL Submitted (JUN-2002) 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; AY121092; AAM82281.1; -; mRNA.
DR EMBL; AY167730; AAO46049.1; -; mRNA.
DR SMR; Q8JMI6; -.
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_0000105986"
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 44..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 238..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 326..409
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..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 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 320..323
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04097"
SQ SEQUENCE 409 AA; 45116 MW; 24E6B244117B584A CRC64;
MASGKATGKT DAPAPVIKLG GPRPPKVGSS GNASWFQAIK AKKLNSPQPK FEGSGVPDNE
NLKTSQQHGY WRRQARFKPG KGGRKPVPDA WYFYYTGTGP AADLNWGDSQ DGIVWVAAKG
ADVKSRSNQG TRDPDKFDQY PLRFSDGGPD GNFRWDFIPL NRGRSGRSTA ASSAASSRPP
SREGSRGRRS GSEDDLIARA AKIIQDQQKK GSRITKAKAD EMAHRRYCKR TIPPGYKVDQ
VFGPRTKGKE GNFGDDKMNE EGIKDGRVTA MLNLVPSSHA CLFGSRVTPK LQPDGLHLKF
EFTTVVPRDD PQFDNYVKIC DQCVDGVGTR PKDDEPKPKS RSSSRPATRT SSPAPRQQRL
KKEKRPKKQD DEVDKALTSD EERNNAQLEF DDEPKVINWG DSALGENEL
