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NCAP_CHAVB
ID   NCAP_CHAVB              Reviewed;         562 AA.
AC   B2C4J1;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 54.
DE   RecName: Full=Nucleoprotein {ECO:0000255|HAMAP-Rule:MF_04085};
DE            EC=3.1.13.- {ECO:0000255|HAMAP-Rule:MF_04085};
DE   AltName: Full=Nucleocapsid protein {ECO:0000255|HAMAP-Rule:MF_04085};
DE   AltName: Full=Protein N {ECO:0000255|HAMAP-Rule:MF_04085};
GN   Name=N {ECO:0000255|HAMAP-Rule:MF_04085};
OS   Chapare mammarenavirus (isolate Human/Bolivia/810419/2003).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC   Ellioviricetes; Bunyavirales; Arenaviridae; Mammarenavirus.
OX   NCBI_TaxID=499556;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=18421377; DOI=10.1371/journal.ppat.1000047;
RA   Delgado S., Erickson B.R., Agudo R., Blair P.J., Vallejo E., Albarino C.G.,
RA   Vargas J., Comer J.A., Rollin P.E., Ksiazek T.G., Olson J.G., Nichol S.T.;
RT   "Chapare virus, a newly discovered arenavirus isolated from a fatal
RT   hemorrhagic fever case in Bolivia.";
RL   PLoS Pathog. 4:E1000047-E1000047(2008).
CC   -!- FUNCTION: Encapsidates the genome, protecting it from nucleases. The
CC       encapsidated genomic RNA is termed the nucleocapsid (NC). Serves as
CC       template for viral transcription and replication. The increased
CC       presence of protein N in host cell does not seem to trigger the switch
CC       from transcription to replication as observed in other negative strain
CC       RNA viruses. Through the interaction with host IKBKE, strongly inhibits
CC       the phosphorylation and nuclear translocation of host IRF3, a protein
CC       involved in interferon activation pathway, leading to the inhibition of
CC       interferon-beta and IRF3-dependent promoters activation. Encodes also a
CC       functional 3'-5' exoribonuclease that degrades preferentially dsRNA
CC       substrates and thereby participates in the suppression of interferon
CC       induction. {ECO:0000255|HAMAP-Rule:MF_04085}.
CC   -!- SUBUNIT: Homomultimerizes to form the nucleocapsid. Binds to viral
CC       genomic RNA. Interacts with glycoprotein G2. Interacts with protein Z;
CC       this interaction probably directs the encapsidated genome to budding
CC       sites. Interacts with protein L; this interaction does not interfere
CC       with Z-L interaction. Interacts with host IKBKE (via Protein kinase
CC       domain); the interaction inhibits IKBKE kinase activity.
CC       {ECO:0000255|HAMAP-Rule:MF_04085}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04085}. Host
CC       cytoplasm {ECO:0000255|HAMAP-Rule:MF_04085}.
CC   -!- DOMAIN: The N-terminal region is important for the cap-binding activity
CC       while the C-terminal region contains the 3'-5' exoribonuclease
CC       activity. A CCHE zinc binding site is present in the C-terminal region
CC       and may thus contribute to the substrate binding and/or the specificity
CC       of the exonuclease activity. {ECO:0000255|HAMAP-Rule:MF_04085}.
CC   -!- SIMILARITY: Belongs to the arenaviridae nucleocapsid protein family.
CC       {ECO:0000255|HAMAP-Rule:MF_04085}.
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DR   EMBL; EU260463; ABY87069.1; -; Genomic_RNA.
DR   RefSeq; YP_001816783.1; NC_010562.1.
DR   SMR; B2C4J1; -.
DR   GeneID; 6216303; -.
DR   KEGG; vg:6216303; -.
DR   Proteomes; UP000008449; Genome.
DR   GO; GO:0019029; C:helical viral capsid; IEA:UniProtKB-UniRule.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-UniRule.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0039689; P:negative stranded viral RNA replication; ISS:UniProtKB.
DR   GO; GO:0039696; P:RNA-templated viral transcription; ISS:UniProtKB.
DR   GO; GO:0039724; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of IKBKE activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.420.410; -; 1.
DR   HAMAP; MF_04085; ARENA_NCAP; 1.
DR   InterPro; IPR000229; Nucleocapsid_arenaviridae.
DR   InterPro; IPR035084; Nucleocapsid_C_arenaviridae.
DR   InterPro; IPR038115; Nucleocapsid_C_sf.
DR   InterPro; IPR035083; Nucleocapsid_N_arenaviridae.
DR   Pfam; PF17290; Arena_ncap_C; 1.
DR   Pfam; PF00843; Arena_nucleocap; 1.
DR   PIRSF; PIRSF004029; N_ArenaV; 1.
PE   3: Inferred from homology;
KW   Capsid protein; Helical capsid protein; Host cytoplasm;
KW   Host-virus interaction; Hydrolase; Inhibition of host IKBKE by virus;
KW   Inhibition of host innate immune response by virus;
KW   Inhibition of host RLR pathway by virus;
KW   Interferon antiviral system evasion; Manganese; Metal-binding;
KW   Ribonucleoprotein; RNA-binding; Viral immunoevasion; Viral nucleoprotein;
KW   Virion; Zinc.
FT   CHAIN           1..562
FT                   /note="Nucleoprotein"
FT                   /id="PRO_0000361005"
FT   REGION          54..237
FT                   /note="Binding site for the cap structure m7GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04085"
FT   BINDING         381
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04085"
FT   BINDING         383
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04085"
FT   BINDING         391
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04085"
FT   BINDING         498
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04085"
FT   BINDING         501
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04085"
FT   BINDING         523
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04085"
FT   BINDING         527
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04085"
FT   SITE            458
FT                   /note="Important for exonuclease activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04085"
SQ   SEQUENCE   562 AA;  62546 MW;  A367BC3FBC151DF1 CRC64;
     MSNSKEIPSF RWTQSLRREL SSFTIPVKSD VLKDAKMIAD GLDFSQVALV QRVLRKTKRT
     DGDLDKLRDL NREVDNLMAM KSAQKNTILK LGDLNKSELM DLASDLEKLK KKVGQTERSP
     VGGVYLGNLS QSQLSKRTDL LRRLGFQQPQ VRSTGVVRIW DVADPTRLNN QFGSVPALTI
     ACMTVQGGDT MGNVVQALTS LGLLYTVKFP NLADLEKLAA EHDCLQIITK DESAINISGY
     NFSLSAAVKA GATFLDGGNM LETIKVTPDN FSTIIKTVLG VKKRENMFID ERPGNRNPYE
     NLLYKLCLSG EGWPYIGSRS QVKGRSWENT TVDLSLKPTQ GPKAPEKVGL NVRLSHLTEI
     QESVVREAMS KINPSHTTWI DIEGTSNDPV ELALYQPESG NYILCYRKPH DEKGFKNGSR
     HSHGMLLKDL ESAQPGLLSY IIGLLPQDMV LTAQGSDDIK RLLDTHGRKD LKVVDVKLSS
     DQARNYEEQV WSDFGHLCKK HNGVVVPKKK KDKDPSQSTE PHCALLDCLM FQSVIDGQPP
     QIKLQSLLPE VLLFTMKPAF AI
 
 
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