NCAP_IBVG
ID NCAP_IBVG Reviewed; 409 AA.
AC P32923;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 2.
DT 02-JUN-2021, entry version 89.
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}; ORFNames=6;
OS Avian infectious bronchitis virus (strain Gray) (IBV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Gammacoronavirus; Igacovirus.
OX NCBI_TaxID=31624;
OH NCBI_TaxID=9031; Gallus gallus (Chicken).
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1966426; DOI=10.1007/978-1-4684-5823-7_51;
RA Collisson E.W., Williams A.K., Vonder Haar R., Li W., Sneed L.W.;
RT "Sequence comparisons of the 3' end of the genomes of five strains of avian
RT infectious bronchitis virus.";
RL Adv. Exp. Med. Biol. 276:373-377(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=1332275; DOI=10.1016/0168-1702(92)90135-v;
RA Williams A.K., Wang L., Sneed L.W., Collisson E.W.;
RT "Comparative analyses of the nucleocapsid genes of several strains of
RT infectious bronchitis virus and other coronaviruses.";
RL Virus Res. 25:213-222(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA Williams A.K., Wang L., Sneed L.W., Collisson E.W.;
RT "Nucleocapsid gene sequence analysis of several strains of infectious
RT bronchitis virus describing the evolutionary relationship of IBV within the
RT coronaviridae family.";
RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 22-160, X-RAY CRYSTALLOGRAPHY (2.0
RP ANGSTROMS) OF 226-333, RNA-BINDING, AND DIMERIZATION DOMAIN.
RX PubMed=16775348; DOI=10.1128/jvi.00157-06;
RA Jayaram H., Fan H., Bowman B.R., Ooi A., Jayaram J., Collisson E.W.,
RA Lescar J., Prasad B.V.V.;
RT "X-ray structures of the N- and C-terminal domains of a coronavirus
RT nucleocapsid protein: implications for nucleocapsid formation.";
RL J. Virol. 80:6612-6620(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_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 -!- INTERACTION:
CC P32923; P32923: N; NbExp=2; IntAct=EBI-25638681, EBI-25638681;
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; S55229; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; S48137; AAB24054.1; -; Genomic_RNA.
DR EMBL; M85245; AAA91856.1; -; Genomic_RNA.
DR PIR; A43574; VHIHG1.
DR PIR; A48559; A48559.
DR PDB; 2GE7; X-ray; 2.00 A; A/B=226-333.
DR PDB; 2GE8; X-ray; 2.20 A; A/B/C/D/F/G/I/J=220-333.
DR PDB; 2GEC; X-ray; 1.30 A; A/B=22-160.
DR PDBsum; 2GE7; -.
DR PDBsum; 2GE8; -.
DR PDBsum; 2GEC; -.
DR SMR; P32923; -.
DR EvolutionaryTrace; P32923; -.
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:0042802; F:identical protein binding; IPI:IntAct.
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 1: Evidence at protein level;
KW 3D-structure; ADP-ribosylation; Disulfide bond; Host Golgi apparatus;
KW Phosphoprotein; Ribonucleoprotein; RNA-binding; Transcription;
KW Transcription regulation; Viral nucleoprotein; Virion.
FT CHAIN 1..409
FT /note="Nucleoprotein"
FT /id="PRO_0000105981"
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..32
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 46..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..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..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 326..409
FT /note="Disordered"
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 165..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..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"
FT CONFLICT 223..243
FT /note="AHRRYCKRTIPPGYKVDQVFG -> VIAGIASALFHLVIRLIKFLV (in
FT Ref. 1)"
FT CONFLICT 245
FT /note="R -> G (in Ref. 1)"
FT STRAND 39..43
FT /evidence="ECO:0007829|PDB:2GEC"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:2GEC"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:2GEC"
FT STRAND 68..78
FT /evidence="ECO:0007829|PDB:2GEC"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:2GEC"
FT STRAND 85..95
FT /evidence="ECO:0007829|PDB:2GEC"
FT TURN 100..103
FT /evidence="ECO:0007829|PDB:2GEC"
FT STRAND 113..117
FT /evidence="ECO:0007829|PDB:2GEC"
FT TURN 134..136
FT /evidence="ECO:0007829|PDB:2GEC"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:2GE7"
FT HELIX 239..242
FT /evidence="ECO:0007829|PDB:2GE7"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:2GE7"
FT HELIX 256..261
FT /evidence="ECO:0007829|PDB:2GE7"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:2GE7"
FT HELIX 266..272
FT /evidence="ECO:0007829|PDB:2GE7"
FT HELIX 278..284
FT /evidence="ECO:0007829|PDB:2GE7"
FT STRAND 285..292
FT /evidence="ECO:0007829|PDB:2GE7"
FT STRAND 295..307
FT /evidence="ECO:0007829|PDB:2GE7"
FT HELIX 313..323
FT /evidence="ECO:0007829|PDB:2GE7"
SQ SEQUENCE 409 AA; 45249 MW; 5C15F07A0A60BE80 CRC64;
MASGKATGKT DAPAPVIKLG GPRPPKVGSS GNASWFQAIK AKKLNSPQPK FEGSGVPDNE
NFKTSQQHGY WRRQARFKPG KGRRKPVPDA WYFYYTGTGP AADLNWGDSQ DGIVWVAAKG
ADVKSRSNQG TRDPDKFDQY PLRFSDGGPD GNFRWDFIPL NRGRSGRSTA ASSAASSRPP
SREGSRGRRS GSEDDLIARA AKIIQDQQKK GSRITKAKAD EMAHRRYCKR TIPPGYKVDQ
VFGPRTKGKE GNFGDDKMNE EGIKDGRVTA MLNLVPSSHA CLFGSRVTPK LQPDGLHLKF
EFTTVVPRDD PQFDNYVKIC DQCVDGVGTR PKDDEPKPKS RSSSRPATRT SSPAPRQQRL
KKEKRPKKQD DEVDKALTSD EERNNAQLEF DDEPKVINWG DSALGENEL
