NCAP_CVTIN
ID NCAP_CVTIN Reviewed; 409 AA.
AC Q9PZ51; Q9WSA9;
DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 02-JUN-2021, entry version 80.
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};
OS Turkey coronavirus (strain Indiana) (TCoV) (TCV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Gammacoronavirus; Igacovirus.
OX NCBI_TaxID=231429;
OH NCBI_TaxID=9103; Meleagris gallopavo (Wild turkey).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=10581391; DOI=10.1016/s0168-1702(99)00117-3;
RA Breslin J.J., Smith L.G., Fuller F.J., Guy J.S.;
RT "Sequence analysis of the turkey coronavirus nucleocapsid protein gene and
RT 3' untranslated region identifies the virus as a close relative of
RT infectious bronchitis virus.";
RL Virus Res. 65:187-193(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-55.
RX PubMed=10393500; DOI=10.1159/000024956;
RA Breslin J.J., Smith L.G., Fuller F.J., Guy J.S.;
RT "Sequence analysis of the matrix/nucleocapsid gene region of turkey
RT coronavirus.";
RL Intervirology 42:22-29(1999).
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; AF111995; AAF23871.1; -; Genomic_RNA.
DR EMBL; AF072913; AAD39044.1; -; Genomic_RNA.
DR SMR; Q9PZ51; -.
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 3: Inferred from homology;
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_0000106019"
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..31
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 46..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 164..193
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..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..73
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; 45005 MW; D84D3C50F610FFA1 CRC64;
MASGKATGKT DAPAPVIKLG GPKPPKVGSS GSVSWFQAIK AKKLNSPQPK FEGSGVPDNE
NLKTSQQHGY WRRQARFKSS RGGRKPVPDA WYFYYTGTGP AADLQWGDSQ AGIVWVAAKG
ADVKSKSNQG TRDPDKFDQY PLRFSDGGPD GNFRWDFIPL NRGRSGRSTA VSSAASSRAP
SREGSRGRRS GAEDDLIARA AKIIQDQQKK GSRITKAKAE EMAHRRYCKR TVPPGYKVEQ
VFGPRTKGKE GNFGDDKMNE EGIKDGRVTA MLNLVPSSHA CLFASKLTPK LQPDGLHLKF
EFTTVVPRDD PQFDNYVSIC DQCVDGVGTR PKDDEPRPKS RASSRPATRG NSPAPRQQRL
KKEKKPKKQD DEVDKALTSD EERNNAQLEF DDEPKVINWG DSALGENEL
