NCAP_BCHK5
ID NCAP_BCHK5 Reviewed; 427 AA.
AC A3EXD7;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 25-MAY-2022, entry version 77.
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 HKU5 (BtCoV) (BtCoV/HKU5/2004).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Betacoronavirus; Merbecovirus.
OX NCBI_TaxID=694008;
OH NCBI_TaxID=105295; Pipistrellus abramus (Japanese pipistrelle) (Pipistrellus javanicus abramus).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate HKU5-1;
RX PubMed=17121802; DOI=10.1128/jvi.02182-06;
RA Woo P.C.Y., Wang M., Lau S.K.P., Xu H.F., Poon R.W.S., Guo R., Wong B.H.L.,
RA Gao K., Tsoi H.-W., Huang Y., Li K.S.M., Lam C.S.F., Chan K.-H.,
RA Zheng B.-J., Yuen K.-Y.;
RT "Comparative analysis of twelve genomes of three novel group 2c and group
RT 2d coronaviruses reveals unique group and subgroup features.";
RL J. Virol. 81:1574-1585(2007).
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; EF065509; ABN10882.1; -; Genomic_RNA.
DR RefSeq; YP_001039969.1; NC_009020.1.
DR SMR; A3EXD7; -.
DR IntAct; A3EXD7; 2.
DR GeneID; 4836000; -.
DR KEGG; vg:4836000; -.
DR Proteomes; UP000007451; 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..427
FT /note="Nucleoprotein"
FT /id="PRO_0000290260"
FT DOMAIN 38..163
FT /note="CoV N NTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01276"
FT DOMAIN 238..361
FT /note="CoV N CTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01277"
FT REGION 1..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 34..172
FT /note="RNA-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04096"
FT REGION 144..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 249..359
FT /note="Dimerization"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04096"
FT REGION 361..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 132
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04096"
FT MOD_RES 147
FT /note="Phosphothreonine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04096"
SQ SEQUENCE 427 AA; 46295 MW; 2CEA6C16319F738D CRC64;
MATPAPPRAV VFANDNETPT NSQRSGRPRT KPRPAPNTTV SWFTGLTQHG KQPLAFPPGQ
GVPLNANSTP AQNAGYWRRQ DRKINTGNGT KPLAPRWYFY YTGTGPEANL PFRSVKDGII
WVHENGATDA PSVFGTRNPA NDPAIVTQFA PGTTLPKNFH IEGTGGNSQS SSRASSRSSS
RSSSRNGRSN NSSRNASPAP HGVGDVVGAG TLSVLLDLQK RLADLEAGKG NKQPKVITKK
DAQAAKQKMR HKRVATKGYN VVQAFGMRGP GPLQSNFGDM QYNKLGTEDP RWPQIAELAP
SASAFMSTSQ FKVTHQSNDE NGEPVYFLSY SGAIKLDPKN PNYNKWMEIL DANIDAYKSF
PKKERKQKPS GDDAATAPAT SQMEDVPELP PKQQRKKRVV QGSIPQRSAG VPSFEDVVDA
IFPDSEA
