NCAP_BC133
ID NCAP_BC133 Reviewed; 424 AA.
AC Q0Q4E6;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 85.
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}; ORFNames=6;
OS Bat coronavirus 133/2005 (BtCoV) (BtCoV/133/2005).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Betacoronavirus; Merbecovirus.
OX NCBI_TaxID=389230;
OH NCBI_TaxID=258959; Tylonycteris pachypus (Lesser bamboo bat) (Vespertilio pachypus).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=16840328; DOI=10.1128/jvi.00697-06;
RA Tang X.C., Zhang J.X., Zhang S.Y., Wang P., Fan X.H., Li L.F., Li G.,
RA Dong B.Q., Liu W., Cheung C.L., Xu K.M., Song W.J., Vijaykrishna D.,
RA Poon L.L.M., Peiris J.S.M., Smith G.J., Chen H., Guan Y.;
RT "Prevalence and genetic diversity of coronaviruses in bats from China.";
RL J. Virol. 80:7481-7490(2006).
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; DQ648794; ABG47058.1; -; Genomic_RNA.
DR SMR; Q0Q4E6; -.
DR Proteomes; UP000007449; Genome.
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 3: Inferred from homology;
KW ADP-ribosylation; Host Golgi apparatus; Phosphoprotein; Reference proteome;
KW Ribonucleoprotein; RNA-binding; Transcription; Transcription regulation;
KW Viral nucleoprotein; Virion.
FT CHAIN 1..424
FT /note="Nucleoprotein"
FT /id="PRO_0000290258"
FT DOMAIN 39..164
FT /note="CoV N NTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01276"
FT DOMAIN 240..363
FT /note="CoV N CTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01277"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 33..175
FT /note="RNA-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04096"
FT REGION 159..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 251..360
FT /note="Dimerization"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04096"
FT REGION 365..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..246
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..424
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 133
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04096"
FT MOD_RES 406
FT /note="Phosphothreonine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04096"
SQ SEQUENCE 424 AA; 45952 MW; 4431AC2086660AAB CRC64;
MATPAAPRTI SFADNNDNQP NQQQRGRGRN PKPRPAPNNT VSWYTGLTQH GKNPLAFPPG
QGVPLNANST TAQNAGYWRR QDRKINTGNG VKQLAPRWFF YYTGTGPEAN LPFRSVKDGI
VWVYEEGATD APSVFGTRNP ANDAAIVCQF APGTLIPKNF HIEGTGGNSQ SSSRASSNSR
NSSRSNSRGG RSTSNSRGTS PVSHGVGSAE SLAALPLLLD LQKRLADLES GKSKQPKVVT
KKDAAAAKNK MRHKRVATKG FNVTQAFGLR GPGPLQGNFG DMNYNKFGTE DPRWPQMAEL
APSASAFMSM SQFKLTHQSN DDKGDPIYFL SYSGAIKLDP KNPNYKKWLE LLEANIDAYK
TFPKKERKPK TTEDGAVVAS SSASQMEDVD AKPQRKPKSR VAGSITMRSG SSPALQDVTF
DSEA
