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NCAP_CVTNC
ID   NCAP_CVTNC              Reviewed;         409 AA.
AC   Q9PZ49; Q9WSB1;
DT   16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   02-JUN-2021, entry version 79.
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 NC95) (TCoV) (TCV).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC   Gammacoronavirus; Igacovirus.
OX   NCBI_TaxID=231431;
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; AF111997; AAF23873.1; -; Genomic_RNA.
DR   EMBL; AF072912; AAD39042.1; -; Genomic_RNA.
DR   SMR; Q9PZ49; -.
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_0000106021"
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          122..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          238..258
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          327..409
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        30..44
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        166..180
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        328..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;  45130 MW;  C73E1DE84456904B CRC64;
     MASGKATGKT DAPAPIIKLG GPKPPKVGSS GNASWFQSIK AKKLNSPQPK FEGSGVPDNE
     NIKTSQQHGY WRRQARFKPG KGGRKPVPDA WYFYYTGTGP AADLNWGDTQ DGIVWVAAKG
     ADVKSRSNQG TRDPDKFDQY PLRFSDGGPD SNFRWDFIPL HRGRSGRSTA ASSAASSRAP
     SRDGSRGRRS GSEDDLIARA AKIIQDQQKK GSRITKAKAD EMAHRRYCKR TVPPGYKVDQ
     VFGPRTKGKE GNFGDDKMNE EGIKDGRVTA MLNLVPSSHA CLFGSRVTPK LQPDGLHLRF
     EFTTVVPRDD PQFDNYVTIC DQCVDGIGTR PKDNEPRPKS RPSSRPATRG NSPAPRQQRP
     KKEKKPKKQD DEVDKALTSD EERNNAQLEF DDEPKVINWG DSALGENHL
 
 
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