NCAP_SFSV
ID NCAP_SFSV Reviewed; 246 AA.
AC P12793;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Nucleoprotein;
DE AltName: Full=Nucleocapsid protein;
DE Short=Protein N;
GN Name=N;
OS Sandfly fever sicilian virus (SFS).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Ellioviricetes; Bunyavirales; Phenuiviridae; Phlebovirus;
OC Sicilian phlebovirus.
OX NCBI_TaxID=28292;
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=29031; Phlebotomus papatasi (Sandfly).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2705301; DOI=10.1016/0042-6822(89)90159-1;
RA Marriott A.C., Ward V.K., Nuttall P.A.;
RT "The S RNA segment of Sandfly Fever Sicilian virus: evidence for an
RT ambisense genome.";
RL Virology 169:341-345(1989).
RN [2]
RP SEQUENCE REVISION.
RA Marriott A.C., Ward V.K., Nuttall P.A.;
RL Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Encapsidates the genomic RNA, protecting it from nucleases.
CC Displays high affinity for single-stranded nucleic acid. The
CC encapsidated genomic RNA is termed the nucleocapsid (NC) or
CC ribonucleoprotein. The ribonucleoprotein has a non-helical structure
CC (By similarity). Serves as template for viral transcription and
CC replication. After replication, the nucleocapsid is recruited to the
CC host Golgi apparatus by glycoprotein Gn for packaging into virus
CC particles (By similarity). {ECO:0000250|UniProtKB:D3K5I7,
CC ECO:0000250|UniProtKB:P21700}.
CC -!- SUBUNIT: Homodimer. Homohexamer; ring-shaped, necessary to form the
CC nucleocapsid (By similarity). Homopentamers; opened pentamers in
CC solution (By similarity). Binds to viral genomic RNA (By similarity).
CC Interacts with glycoprotein Gn; this interaction allows packaging of
CC nucleocapsids into virions (By similarity).
CC {ECO:0000250|UniProtKB:D3K5I7, ECO:0000250|UniProtKB:P21700,
CC ECO:0000250|UniProtKB:P21701}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:D3K5I7}. Host
CC cytoplasm {ECO:0000250|UniProtKB:D3K5I7}. Host nucleus
CC {ECO:0000250|UniProtKB:D3K5I7}. Host endoplasmic reticulum-Golgi
CC intermediate compartment {ECO:0000250|UniProtKB:I6WJ72}. Host Golgi
CC apparatus {ECO:0000250|UniProtKB:I6WJ72}.
CC -!- SIMILARITY: Belongs to the phlebovirus nucleocapsid protein family.
CC {ECO:0000305}.
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DR EMBL; J04418; AAA47458.1; -; Genomic_RNA.
DR PIR; A30180; VHVUSS.
DR SMR; P12793; -.
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 InterPro; IPR009522; Capsid_Phlebovir/Tenuivir.
DR InterPro; IPR015971; Nucleocapsid_Phlebovirus.
DR Pfam; PF05733; Tenui_N; 1.
DR PIRSF; PIRSF003953; N_PhelboV; 1.
PE 3: Inferred from homology;
KW Capsid protein; Helical capsid protein; Host cytoplasm;
KW Host Golgi apparatus; Host nucleus; Ribonucleoprotein; RNA-binding;
KW Viral nucleoprotein; Virion.
FT CHAIN 1..246
FT /note="Nucleoprotein"
FT /id="PRO_0000221996"
FT SITE 30
FT /note="RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:D3K5I7"
FT SITE 33
FT /note="RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:D3K5I7"
FT SITE 66
FT /note="RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:D3K5I7"
FT SITE 67
FT /note="RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:D3K5I7"
FT SITE 99
FT /note="RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:D3K5I7"
FT SITE 106
FT /note="RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:D3K5I7"
SQ SEQUENCE 246 AA; 27896 MW; 7ED416E06F3449F1 CRC64;
MDEYQKIAVE FGEQAIDETV IQDWLQAFAY QGFDARTIIH NLVQLGGKSW EEDAKKMIIL
SLTRGNKPKK MVERMSPEGA REVKSLVAKY KIVEGRPGRN GITLSRVLQP WLGGQSKLWK
WLKTSYQSQG AQWTALCGQT YPRQMMHPSF AGLIDPSLDQ EDFNAVLDAH KLFLFMFSKT
INVSLRGAQK RDIEESFSQP MLAAINSSFI DNTQRRAFLT KFGILTSGAR ATAVVKKIAE
VYRKLE