NCAP_CVPV
ID NCAP_CVPV Reviewed; 457 AA.
AC P59713;
DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2003, sequence version 1.
DT 02-JUN-2021, entry version 71.
DE RecName: Full=Nucleoprotein {ECO:0000255|HAMAP-Rule:MF_04096};
DE AltName: Full=Nucleocapsid protein {ECO:0000255|HAMAP-Rule:MF_04096};
DE Short=NC {ECO:0000255|HAMAP-Rule:MF_04096};
DE Short=Protein N {ECO:0000255|HAMAP-Rule:MF_04096};
GN Name=N {ECO:0000255|HAMAP-Rule:MF_04096};
OS Puffinosis coronavirus (PV) (Puffinosis virus).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Betacoronavirus; Embecovirus.
OX NCBI_TaxID=76583;
OH NCBI_TaxID=48688; Puffinus puffinus (Manx shearwater).
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Wu H.Y., Guy J.S., Yoo D., Vlasak R., Urbach E., Brian D.A.;
RT "Common RNA replication signals exist among group 2 coronaviruses despite
RT two clusters of 5' and 3'UTR sequence patterns.";
RL Submitted (FEB-2003) 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_04096}.
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_04096}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04096}. Host
CC endoplasmic reticulum-Golgi intermediate compartment
CC {ECO:0000255|HAMAP-Rule:MF_04096}. Host Golgi apparatus
CC {ECO:0000255|HAMAP-Rule:MF_04096}. 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_04096}.
CC -!- PTM: ADP-ribosylated. The ADP-ribosylation is retained in the virion
CC during infection. {ECO:0000255|HAMAP-Rule:MF_04096}.
CC -!- PTM: Phosphorylated on serine and threonine residues.
CC {ECO:0000255|HAMAP-Rule:MF_04096}.
CC -!- SIMILARITY: Belongs to the betacoronavirus nucleocapsid protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04096}.
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DR EMBL; AJ544718; CAD67607.1; -; mRNA.
DR SMR; P59713; -.
DR PRIDE; P59713; -.
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_04096; BETA_CORONA_NCAP; 1.
DR InterPro; IPR044344; N_prot_C_CoV.
DR InterPro; IPR044345; N_prot_N_CoV.
DR InterPro; IPR043505; NCAP_bCoV.
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; Host Golgi apparatus; Phosphoprotein; Ribonucleoprotein;
KW RNA-binding; Transcription; Transcription regulation; Viral nucleoprotein;
KW Virion.
FT CHAIN 1..457
FT /note="Nucleoprotein"
FT /id="PRO_0000106022"
FT DOMAIN 64..193
FT /note="CoV N NTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01276"
FT DOMAIN 260..383
FT /note="CoV N CTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01277"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 56..197
FT /note="RNA-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04096"
FT REGION 158..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 190..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 249..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..384
FT /note="Dimerization"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04096"
FT REGION 382..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 170
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04096"
FT MOD_RES 177
FT /note="Phosphothreonine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04096"
FT MOD_RES 194
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04096"
FT MOD_RES 390
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04096"
FT MOD_RES 431
FT /note="Phosphothreonine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04096"
SQ SEQUENCE 457 AA; 50207 MW; A13281EA004141A3 CRC64;
MSFVPGQENA GSRSSSGNRA GNGILKKTTW ADQTERGSNN QNRGRRNQPK QTATTQPNSG
SVVPHYSWFS GITQFQKGKE FKFAEGQGVP IANGIPATEQ KGYWFRHNRR SFKSPDGQQK
QLLPRWYFYY LGTGPYAGAE YGDDVEGVCW VANKQADTRT SADIAERDPS SHEAIPTRFA
PGTFLPQGYY VEGSGRSAPA SRSGSRSQSR GPNNRARSSS NQRQPASIVK PDMAEEIAAL
VLAKLGKDAG QPKQVTKQSA KEVRQKILNK PRQKRTPNKQ CPVQQCFGKR GPNQNFGGPE
MLKLGTSDPQ FPILAELAPT AGAFFFGSKL ELVKKNSVGV DEPTKDVYEL QYSGAVRFDS
TLPGFETIMK VLRENLNAYQ NQDGGADVVS PKPQRKRGQR QVAQKKNDEV DNVSVAKPKS
AVQRNVNREL TPEDRSLLAQ ILDDGVVPDG LEDDSNV
