NCAP_PIARV
ID NCAP_PIARV Reviewed; 561 AA.
AC P03541;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 93.
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 Pichinde mammarenavirus (PICV) (Pichind mammarenavirus).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Ellioviricetes; Bunyavirales; Arenaviridae; Mammarenavirus.
OX NCBI_TaxID=2169993;
OH NCBI_TaxID=10144; Cavia cutleri (Guinea pig).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=530178; Nephelomys albigularis (Tomes's rice rat) (Oryzomys albigularis).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=6492264; DOI=10.1128/jvi.52.3.897-904.1984;
RA Auperin D.D., Romanowski V., Galinski M., Bishop D.H.L.;
RT "Sequencing studies of pichinde arenavirus S RNA indicate a novel coding
RT strategy, an ambisense viral S RNA.";
RL J. Virol. 52:897-904(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=6324469; DOI=10.1016/0042-6822(84)90286-1;
RA Auperin D.D., Galinski M., Bishop D.H.L.;
RT "The sequences of the N protein gene and intergenic region of the S RNA of
RT pichinde arenavirus.";
RL Virology 134:208-219(1984).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2435460; DOI=10.1007/978-3-642-71683-6_2;
RA Bishop D.H.L., Auperin D.D.;
RT "Arenavirus gene structure and organization.";
RL Curr. Top. Microbiol. Immunol. 133:5-17(1987).
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; K02734; AAA46825.1; -; Genomic_RNA.
DR EMBL; K02735; AAA46826.1; -; Genomic_RNA.
DR EMBL; M16734; AAA46823.1; -; Genomic_RNA.
DR PIR; A04150; VHXPNP.
DR RefSeq; YP_138544.1; NC_006447.1.
DR PDB; 3P4N; X-ray; 2.50 A; C/F=205-212.
DR PDBsum; 3P4N; -.
DR SMR; P03541; -.
DR GeneID; 5075742; -.
DR KEGG; vg:5075742; -.
DR Proteomes; UP000201514; 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 1: Evidence at protein level;
KW 3D-structure; 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..561
FT /note="Nucleoprotein"
FT /id="PRO_0000079196"
FT REGION 52..237
FT /note="Binding site for the cap structure m7GTP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04085"
FT REGION 336..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 380
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04085"
FT BINDING 382
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04085"
FT BINDING 390
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04085"
FT BINDING 497
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04085"
FT BINDING 500
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04085"
FT BINDING 521
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04085"
FT BINDING 525
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04085"
FT SITE 457
FT /note="Important for exonuclease activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04085"
FT CONFLICT 48
FT /note="V -> L (in Ref. 2; AAA46826)"
FT CONFLICT 258
FT /note="G -> A (in Ref. 2; AAA46826)"
SQ SEQUENCE 561 AA; 62983 MW; 73D5FC98634EB605 CRC64;
MSDNIPSFRW VQSLRRGLSN WTHPVKADVL SDTRALLSAL DFHKVAQVQR MVRKDKRTDS
DLTKLRDMNK EVDALMNMRS VQRDNVLKVG GLAKEELMEL ASDLDKLRKK VTRTEGLSQP
GVYEGNLTNT QLEQRAEILR SMGFANARPA GNRDGVVKVW DIKDNTLLIN QFGSMPALTI
ACMTEQGGEQ LNDVVQALSA LGLLYTVKFP NMTDLEKLTQ QHSALKIISH EPSALNISGY
NLSLSAAVKA AACMIDGGNM LETIQVKPSM FSTLIKSLLQ IKNREGMFVS TTPGQRNPYE
NLLYKICLSG DGWPYIGSRS QVQGRAWDNT TVDLDSKPSA IQPPVRNGGS PDLKQIPKEK
EDTVVSSIQM LDPRATTWID IEGTPNDPVE MAIYQPDTGN YIHCYRFPHD EKSFKEQSKY
SHGLLLKDLA DAQPGLISSI IRHLPQNMVF TAQGSDDIIR LFEMHGRRDL KVLDVKLSAE
QARTFEDEIW ERYNQLCTKH KGLVIKKKKK GAVQTTANPH CALLDTIMFD ATVTGWVRDQ
KPMRCLPIDT LYRNNTDLIN L
