NCAP_CVCAK
ID NCAP_CVCAK Reviewed; 382 AA.
AC Q04700;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 02-JUN-2021, entry version 83.
DE RecName: Full=Nucleoprotein {ECO:0000255|HAMAP-Rule:MF_04095};
DE AltName: Full=Nucleocapsid protein {ECO:0000255|HAMAP-Rule:MF_04095};
DE Short=NC {ECO:0000255|HAMAP-Rule:MF_04095};
DE Short=Protein N {ECO:0000255|HAMAP-Rule:MF_04095};
GN Name=N {ECO:0000255|HAMAP-Rule:MF_04095};
OS Canine coronavirus (strain K378) (CCoV) (Canine enteric coronavirus).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Alphacoronavirus; Tegacovirus.
OX NCBI_TaxID=33732;
OH NCBI_TaxID=9615; Canis lupus familiaris (Dog) (Canis familiaris).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=1329312; DOI=10.1016/0042-6822(92)90174-n;
RA Vennema H., Rossen J.W.A., Wesseling J., Horzinek M.C., Rottier P.J.M.;
RT "Genomic organization and expression of the 3' end of the canine and feline
RT enteric coronaviruses.";
RL Virology 191:134-140(1992).
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_04095}.
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_04095}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04095}. Host
CC endoplasmic reticulum-Golgi intermediate compartment
CC {ECO:0000255|HAMAP-Rule:MF_04095}. Host Golgi apparatus
CC {ECO:0000255|HAMAP-Rule:MF_04095}. 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_04095}.
CC -!- PTM: ADP-ribosylated. The ADP-ribosylation is retained in the virion
CC during infection. {ECO:0000255|HAMAP-Rule:MF_04095}.
CC -!- PTM: Phosphorylated on serine and threonine residues.
CC {ECO:0000255|HAMAP-Rule:MF_04095}.
CC -!- SIMILARITY: Belongs to the alphacoronavirus nucleocapsid protein
CC family. {ECO:0000255|HAMAP-Rule:MF_04095}.
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DR EMBL; X66717; CAA47246.1; -; Genomic_RNA.
DR PIR; A44056; A44056.
DR SMR; Q04700; -.
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-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR CDD; cd21595; CoV_N-CTD; 1.
DR CDD; cd21554; CoV_N-NTD; 1.
DR HAMAP; MF_04095; ALPHA_CORONA_NCAP; 1.
DR InterPro; IPR044344; N_prot_C_CoV.
DR InterPro; IPR044345; N_prot_N_CoV.
DR InterPro; IPR042548; NCAP_aCoV.
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; Host Golgi apparatus; Phosphoprotein; Ribonucleoprotein;
KW RNA-binding; Transcription; Transcription regulation; Viral nucleoprotein;
KW Virion.
FT CHAIN 1..382
FT /note="Nucleoprotein"
FT /id="PRO_0000105997"
FT DOMAIN 31..153
FT /note="CoV N NTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01276"
FT DOMAIN 224..337
FT /note="CoV N CTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01277"
FT REGION 33..159
FT /note="RNA-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04095"
FT REGION 152..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 231..334
FT /note="Dimerization"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04095"
FT REGION 331..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..240
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..355
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 156
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04095"
FT MOD_RES 254
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04095"
FT MOD_RES 256
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04095"
SQ SEQUENCE 382 AA; 43332 MW; 3DCBE17971A4150F CRC64;
MANQGQRVQW GVDITKKRGL SNSRGRKNNT IPLSFFNPIT LQQGSKFWNL CPRDFVPKGI
GNKDQQIGYW NRQSRYRMVK GQRKELPERW FFYYLGTGPH ADAKFKDRID GVVWVAKDGA
MNKPTTLGNR GANNESKALK FDGKVPGEFQ LEVNQSRDNS RSPSQSRSQS RNRSQSRGRQ
QSNNKKDDSV EQAVLAALKK LGVDTEKQQQ RSRSKSKERS NSKTRDTTPK NENKHTWKRT
AGKGDVTKFY GARSSSANFG DSDLVANGNG AKHYPQLAEC VPSVSSILFG SYWTAKEDGD
QIEVTFTHKY HLPKDDPKTG QFLQQINAYA RPSEVAKEQR QRKARSKSAE RVEQEVVPDA
LTENYTDVFD DTQVEIIDEV TN
