ID   NCAP_DUGBV              Reviewed;         441 AA.
AC   P15190;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   08-NOV-2023, entry version 69.
DE   RecName: Full=Nucleoprotein;
DE   AltName: Full=Nucleocapsid protein;
DE            Short=Protein N;
GN   Name=N;
OS   Dugbe virus.
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC   Ellioviricetes; Bunyavirales; Nairoviridae; Orthonairovirus.
OX   NCBI_TaxID=3052514;
OH   NCBI_TaxID=34610; Amblyomma variegatum (Tropical bont tick).
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=72862; Hyalomma rufipes (Tick) (Hyalomma marginatum rufipes).
OH   NCBI_TaxID=72855; Hyalomma truncatum.
OH   NCBI_TaxID=34630; Rhipicephalus.
OH   NCBI_TaxID=34611; Rhipicephalus annulatus.
OH   NCBI_TaxID=60189; Rhipicephalus decoloratus (African blue tick) (Boophilus decoloratus).
OH   NCBI_TaxID=136141; Rhipicephalus geigyi.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate ARD 44313;
RX   PubMed=2327076; DOI=10.1016/0042-6822(90)90436-u;
RA   Ward V.K., Marriott A.C., El-Ghorr A.A., Nuttall P.A.;
RT   "Coding strategy of the S RNA segment of Dugbe virus (Nairovirus;
RT   Bunyaviridae).";
RL   Virology 175:518-524(1990).
CC   -!- FUNCTION: Binds dsRNA and ssRNA and probably participates in the
CC       packaging of viral genome. In the dsRNA binding mode, the nucleocapsid
CC       protein specifically binds to the vRNA panhandle secondary structure
CC       formed at the termini of viral genome. Does not discriminate between
CC       viral and nonviral RNAs through ssRNA binding mode. Displays dsDNA
CC       endonuclease activity that is sequence non-specific.
CC       {ECO:0000250|UniProtKB:P89522}.
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:P89522};
CC       Note=Stimulated by divalent cations such as Mn2+, Co2+, and Mg2+.
CC       {ECO:0000250|UniProtKB:P89522};
CC   -!- SUBUNIT: Probable homooligomer; forms a double superhelical polymer.
CC       Monomer. {ECO:0000250|UniProtKB:P89522}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:P27318}.
CC       Note=Internal protein of virus particle.
CC       {ECO:0000250|UniProtKB:P89522}.
CC   -!- DOMAIN: The DEVD motif is a CASP3/caspase 3 cleavage site essential for
CC       viral replication in host cell (By similarity). However, the importance
CC       for viral replication is apprently not linked to caspase cleavage (By
CC       similarity). This motif is involved in homooligomerization (By
CC       similarity). {ECO:0000250|UniProtKB:P27318,
CC       ECO:0000250|UniProtKB:P89522}.
CC   -!- PTM: Cleaved at the DEVD motif by host CASP3/caspase 3 in mammalian
CC       cells giving rise to cleavage products that remain associated. Only the
CC       monomeric form is cleaved. Little or no cleavage in tick cells. Caspase
CC       cleavage reduces the viral polymerase activity (By similarity). Caspase
CC       cleavage is not required for productive infection in mammalian or tick
CC       host cells (By similarity). {ECO:0000250|UniProtKB:P27318,
CC       ECO:0000250|UniProtKB:P89522}.
CC   -!- SIMILARITY: Belongs to the nairovirus 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; M25150; AAA42975.1; -; Genomic_RNA.
DR   PIR; A34748; VHVUDU.
DR   SMR; P15190; -.
DR   GO; GO:0019029; C:helical viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR   GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.58.1110; -; 1.
DR   InterPro; IPR003486; Nairo_nucleocap.
DR   Pfam; PF02477; Nairo_nucleo; 1.
DR   PIRSF; PIRSF003950; N_NairoV; 1.
PE   3: Inferred from homology;
KW   Capsid protein; Helical capsid protein; Ribonucleoprotein; RNA-binding;
KW   Viral nucleoprotein; Virion.
FT   CHAIN           1..441
FT                   /note="Nucleoprotein"
FT                   /id="PRO_0000222007"
FT   MOTIF           266..269
FT                   /note="DEVD"
FT                   /evidence="ECO:0000250|UniProtKB:P89522"
FT   SITE            213
FT                   /note="Homooligomerization"
FT                   /evidence="ECO:0000250|UniProtKB:P27318"
FT   SITE            269..270
FT                   /note="Cleavage by host CASP3/caspase 3"
FT                   /evidence="ECO:0000250|UniProtKB:P89522"
FT   SITE            277
FT                   /note="Homooligomerization"
FT                   /evidence="ECO:0000250|UniProtKB:P27318"
FT   SITE            352
FT                   /note="Homooligomerization"
FT                   /evidence="ECO:0000250|UniProtKB:P27318"
SQ   SEQUENCE   441 AA;  49436 MW;  91762EAF0C424070 CRC64;
     MENQIKANNK KEFDEWFKPF SEKLQLRSNL TNSASLCDRV PDLALAEMKM ALATDDKEKD
     SVFSNALVEA TRFCAPIYEC AWTCSTGVVQ KSLSWFDKNK DFIKLWDAKY MDLKKGIPEP
     EQLVSYQQAA QKWRKDVGYE INQFTRSLTH PVVAEYKVPG ELLLMSRMLS DMIRRRNVLL
     NGDGENAGKK VLISREHVSW GRELAGGKFQ VVFNPPWGDI NKCGKSGIPL AATAMVKVAE
     LDGSKKLEDI RQALLDLKKW VEDNKDALED GKGNELVQTM TKHLAKHVEL SKKSNALRAQ
     GAQIDTPFSA YYWAWSAGVK PETFFTLSQF LFEMGQSARG GKKMIKALTS TPLRWGKGLI
     NLFADDDFLG NRLYMHPAVL TPGRMSEMGA CFGVIPVASP EDAILGSGHS KNILNFKIDT
     SVQNPCASTI VQLIQNPEIW L
//