NCAP_IHNVR
ID NCAP_IHNVR Reviewed; 391 AA.
AC P19691;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 2.
DT 29-SEP-2021, entry version 74.
DE RecName: Full=Nucleoprotein;
DE Short=NP;
DE AltName: Full=Nucleocapsid protein;
DE Short=Protein N;
GN Name=N;
OS Infectious hematopoietic necrosis virus (strain Round Butte) (IHNV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Rhabdoviridae; Gammarhabdovirinae;
OC Novirhabdovirus.
OX NCBI_TaxID=11291;
OH NCBI_TaxID=8028; Salmo.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3201758; DOI=10.1016/s0042-6822(88)90130-4;
RA Gilmore R.D. Jr., Leong J.-A.;
RT "The nucleocapsid gene of infectious hematopoietic necrosis virus, a fish
RT rhabdovirus.";
RL Virology 167:644-648(1988).
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 -!- SIMILARITY: Belongs to the novirhabdovirus nucleocapsid protein family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA46240.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; J04321; AAA46240.1; ALT_FRAME; Genomic_RNA.
DR PIR; A31834; VHVNIH.
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 InterPro; IPR004902; Rhabdo_ncap_2.
DR Pfam; PF03216; Rhabdo_ncap_2; 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..391
FT /note="Nucleoprotein"
FT /id="PRO_0000222815"
FT REGION 347..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..385
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 391 AA; 42137 MW; 880DE4D7BE7E5331 CRC64;
MTSALRETFT GLRDIKGGVL EDPETEYRPG TITLPLFFSK ADFDLEMIKR AVSHVGGEGT
RRALGLLCAF VIAETVPSGR GTVAELLEAL GFLLESLETG APLEVTFADP NNKLAETIVK
ENVLEVVTGL LFTCALLTKY DVDKMATYCQ NKLERLATSQ GIGELVNFNA NRGVLARIGA
VLRPGQKLTK AIYGIILINL SDPATAARAK ALCAMRLSGT GMTMVGLFNQ AAKNLGALPA
DLLEDLCMKS VVESARRIVR LMRIVAEAPG VAAKYGVMMS RMLGVGYFKA YGINENARIT
CILMNINDRY DDGTSGGLTG LKVSDPFRKL AREIARLLVL KYDGDGSTGE GASDLIRRAE
MASRGPDMGE EEEEDEEDDD SSEPGDSDSF L
