位置:首页 > 蛋白库 > NCAP_IBVDE
NCAP_IBVDE
ID   NCAP_IBVDE              Reviewed;         409 AA.
AC   Q9J4B0;
DT   16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   02-JUN-2021, entry version 71.
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 DE072) (IBV).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC   Gammacoronavirus; Igacovirus.
OX   NCBI_TaxID=233265;
OH   NCBI_TaxID=9031; Gallus gallus (Chicken).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=11087096; DOI=10.1007/s007050070044;
RA   Lee C.-W., Jackwood M.W.;
RT   "Evidence of genetic diversity generated by recombination among avian
RT   coronavirus IBV.";
RL   Arch. Virol. 145:2135-2148(2000).
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   -!- 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF203001; AAF69116.1; -; Genomic_RNA.
DR   SMR; Q9J4B0; -.
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_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   3: Inferred from homology;
KW   ADP-ribosylation; Disulfide bond; Host Golgi apparatus; Phosphoprotein;
KW   Ribonucleoprotein; RNA-binding; Transcription; Transcription regulation;
KW   Viral nucleoprotein; Virion.
FT   CHAIN           1..409
FT                   /note="Nucleoprotein"
FT                   /id="PRO_0000105980"
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          44..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          121..145
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          164..195
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        343..357
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        358..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"
SQ   SEQUENCE   409 AA;  45018 MW;  0FCC6A10E276E7EF CRC64;
     MASGKATGKT DAPAPVIKLG GPKPPKVGSS GNASWFQAIK AKKLNSPQPK FEGSGVPDNE
     NLKTSQQHGY WRRQLRFKPS KGGRKPVPDA WYFYYTGTGP AADLNWGDSQ DGIVWVAAKG
     ADVKSRSNQG TRDPDKFDQY PLRFSDGGPD GNFRWDFIPL NRGRSGRSTA ASSAASSRAP
     SRDGSRGRRS GSEGDLIARA AKIIQDQQKR GSRITKAKAD EMAHRRYCKR TIPPGYKVDQ
     VFGPRTKGKE GNFGDDKMNE EGIKDGRVTA MLNLVPSSHA CLFGSRVTPK LQPDGLHLKI
     EFTTVVSRDD PQFDNYVKIC DQCVDGVGTR PKDDEPRPKS RSSSRPATRT SSPALRQQPQ
     KKEKKPKKQD DEVDKALTSD EERNNAQLEF DDEPKVINWG DSALGENEL
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024