NCAP_BUNLC
ID NCAP_BUNLC Reviewed; 235 AA.
AC P04873;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 29-SEP-2021, entry version 75.
DE RecName: Full=Nucleoprotein;
DE AltName: Full=Nucleocapsid protein;
DE Short=Protein N;
GN Name=N;
OS Bunyavirus La Crosse.
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Ellioviricetes; Bunyavirales; Peribunyaviridae; Orthobunyavirus;
OC La Crosse orthobunyavirus.
OX NCBI_TaxID=11577;
OH NCBI_TaxID=9850; Cervidae (deer).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=7162; Ochlerotatus triseriatus (Eastern treehole mosquito) (Aedes triseriatus).
OH NCBI_TaxID=13712; Tamias.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=6834480; DOI=10.1128/jvi.45.3.1155-1158.1983;
RA Akashi H., Bishop D.H.L.;
RT "Comparison of the sequences and coding of La Crosse and snowshoe hare
RT bunyavirus S RNA species.";
RL J. Virol. 45:1155-1158(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=6684362; DOI=10.1016/0042-6822(83)90271-4;
RA Cabradilla C.D. Jr., Holloway B.P., Obijeski J.F.;
RT "Molecular cloning and sequencing of the La Crosse virus S RNA.";
RL Virology 128:463-468(1983).
CC -!- FUNCTION: Encapsidates the genome protecting it from nucleases. The
CC encapsidated genomic RNA is termed the nucleocapsid (NC) and serves as
CC template for transcription and replication. Seems to participate in the
CC nuclear relocalization of host PABP1, thereby inhibiting host cellular
CC translation (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homomultimerizes to form the nucleocapsid. Binds to viral
CC genomic RNA. Interacts with host PABP1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Virion. Note=Internal protein of virus particle.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=N;
CC IsoId=P04873-1; Sequence=Displayed;
CC Name=NSS;
CC IsoId=P04874-1; Sequence=External;
CC -!- SIMILARITY: Belongs to the orthobunyavirus nucleocapsid protein family.
CC {ECO:0000305}.
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; K00610; AAA42782.1; -; Genomic_RNA.
DR EMBL; K00108; AAA42779.1; -; Genomic_RNA.
DR PIR; A04104; VHVULV.
DR PDB; 4BGP; X-ray; 1.80 A; A=1-235.
DR PDB; 4BHH; X-ray; 3.40 A; B/D/F/Z=1-235.
DR PDBsum; 4BGP; -.
DR PDBsum; 4BHH; -.
DR SMR; P04873; -.
DR Proteomes; UP000232774; Genome.
DR GO; GO:0019029; C:helical viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0039657; P:suppression by virus of host gene expression; IEA:UniProtKB-KW.
DR Gene3D; 1.10.472.180; -; 1.
DR Gene3D; 1.20.142.20; -; 1.
DR InterPro; IPR001784; Bunya_nucleocap.
DR InterPro; IPR043011; Bunya_nucleocap_C.
DR InterPro; IPR043012; Bunya_nucleocap_N.
DR Pfam; PF00952; Bunya_nucleocap; 1.
DR PIRSF; PIRSF003947; N_OrthobunV; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative initiation; Capsid protein;
KW Eukaryotic host gene expression shutoff by virus;
KW Eukaryotic host translation shutoff by virus; Helical capsid protein;
KW Host gene expression shutoff by virus; Host-virus interaction;
KW Reference proteome; Ribonucleoprotein; RNA-binding; Viral nucleoprotein;
KW Virion.
FT CHAIN 1..235
FT /note="Nucleoprotein"
FT /id="PRO_0000221990"
FT TURN 1..4
FT /evidence="ECO:0007829|PDB:4BGP"
FT HELIX 19..30
FT /evidence="ECO:0007829|PDB:4BGP"
FT TURN 31..33
FT /evidence="ECO:0007829|PDB:4BGP"
FT HELIX 36..53
FT /evidence="ECO:0007829|PDB:4BGP"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:4BGP"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:4BGP"
FT HELIX 92..109
FT /evidence="ECO:0007829|PDB:4BGP"
FT HELIX 113..122
FT /evidence="ECO:0007829|PDB:4BGP"
FT HELIX 126..130
FT /evidence="ECO:0007829|PDB:4BGP"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:4BGP"
FT HELIX 139..143
FT /evidence="ECO:0007829|PDB:4BGP"
FT HELIX 149..152
FT /evidence="ECO:0007829|PDB:4BGP"
FT TURN 153..158
FT /evidence="ECO:0007829|PDB:4BGP"
FT HELIX 159..169
FT /evidence="ECO:0007829|PDB:4BGP"
FT HELIX 175..178
FT /evidence="ECO:0007829|PDB:4BGP"
FT HELIX 179..182
FT /evidence="ECO:0007829|PDB:4BGP"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:4BHH"
FT HELIX 191..197
FT /evidence="ECO:0007829|PDB:4BGP"
FT HELIX 199..210
FT /evidence="ECO:0007829|PDB:4BGP"
FT HELIX 221..228
FT /evidence="ECO:0007829|PDB:4BGP"
FT TURN 229..231
FT /evidence="ECO:0007829|PDB:4BGP"
SQ SEQUENCE 235 AA; 26530 MW; 56EBB4D64AD04A96 CRC64;
MSDLVFYDVA STGANGFDPD AGYMDFCVKN AESLNLAAVR IFFLNAAKAK AALSRKPERK
ANPKFGEWQV EVINNHFPGN RNNPIGNNDL TIHRLSGYLA RWVLDQYNEN DDESQHELIR
TTIINPIAES NGVGWDSGPE IYLSFFPGTE MFLETFKFYP LTIGIHRVKQ GMMDPQYLKK
ALRQRYGTLT ADKWMSQKVA AIAKSLKDVE QLKWGKGGLS DTAKTFLQKF GIRLP