NCAP_LBV
ID NCAP_LBV Reviewed; 450 AA.
AC Q82994;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Nucleoprotein;
DE Short=NP;
DE AltName: Full=Nucleocapsid protein;
DE Short=Protein N;
GN Name=N;
OS Lagos bat virus (LBV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC Lyssavirus.
OX NCBI_TaxID=38766;
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=40674; Mammalia.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Nigeria/8619/1958;
RX PubMed=7778285; DOI=10.1006/viro.1995.1285;
RA Kissi B., Tordo N., Bourhy H.;
RT "Genetic polymorphism in the rabies virus nucleoprotein gene.";
RL Virology 209:526-537(1995).
CC -!- FUNCTION: Encapsidates the genome, protecting it from nucleases. If
CC expressed without protein P it binds non-specifically RNA and therefore
CC can bind it's own mRNA. Interaction with protein P abolishes any non-
CC specific RNA binding, and prevents phosphorylation. The soluble N-P
CC complex encapsidates specifically the genomic RNA, with protein N
CC protecting the genome like a pearl necklace. The encapsidated genomic
CC RNA is termed the nucleocapsid (NC) and serves as template for viral
CC transcription and replication. Protein N binds protein P in the NC
CC through a different interaction, and can be phosphorylated. Subsequent
CC viral replication is dependent on intracellular concentration of newly
CC synthesized protein N. During replication, encapsidation by protein N
CC is coupled to RNA synthesis and all replicative products are resistant
CC to nucleases (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homomultimerizes to form the nucleocapsid. Binds to viral
CC genomic RNA (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Virion. Host cytoplasm {ECO:0000250}.
CC -!- PTM: Phosphorylated by host. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the lyssavirus nucleocapsid protein family.
CC {ECO:0000305}.
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DR EMBL; U22842; AAA80290.1; -; Genomic_RNA.
DR SMR; Q82994; -.
DR PRIDE; Q82994; -.
DR GO; GO:0019029; C:helical viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR Gene3D; 1.10.3570.10; -; 1.
DR Gene3D; 1.10.3610.10; -; 1.
DR InterPro; IPR000448; Rhabdo_ncapsid.
DR InterPro; IPR023331; Rhabdovirus_ncapsid_C.
DR InterPro; IPR023330; Rhabdovirus_ncapsid_N.
DR InterPro; IPR035961; Rhabdovirus_nucleoprotein-like.
DR Pfam; PF00945; Rhabdo_ncap; 1.
DR SUPFAM; SSF140809; SSF140809; 1.
PE 3: Inferred from homology;
KW Capsid protein; Helical capsid protein; Host cytoplasm; Phosphoprotein;
KW Ribonucleoprotein; RNA-binding; Viral nucleoprotein; Virion.
FT CHAIN 1..450
FT /note="Nucleoprotein"
FT /id="PRO_0000297611"
FT MOD_RES 389
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000250"
SQ SEQUENCE 450 AA; 50520 MW; 9D0ED65939133239 CRC64;
MDSERIVFRV HNQVVSLKPE IISDQYEYKY PAITDGKKPG ITLGRAPDLS TAYKSILSGM
NAAKLDSDDV CSYLAAAMQL FEGVCPEDWI SYGIHIATKG ETITPDVLID VTRTNVEGNW
AQAGGTDMTR DPTIAEHASL VGLLLCLYRL SKIVGQNTAN YKTNVADRME QIFETAPFVK
VVEHHTLMTV HKMCANWSTI PNFRFLAGTY DMFFARVEHL YSALRVGTVV TAYEDCSGLV
SFTGFIKQIN LSARDALLYF FHKKFEEEIK RMFEPGQETA VPHPYFIHFR ALGVSGKSPY
SSTAVGHHFN LIHFIGCYMG QVKSLNATVI QTCAPHEMSV LGGYLGEEFF GKGTFERRFF
RDEKEMQDYA DLEGARVEAS LADDGTVDSD DEDFFSGETR SPEAVYSRIM MNNGRLKKSH
IRRYVSVSSN HQARPNSFAE FLNKVYSESS
