NCAP_LATVB
ID NCAP_LATVB Reviewed; 557 AA.
AC Q8BDE6; Q8BD29;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 62.
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 Latino mammarenavirus (isolate Rat/Bolivia/MARU 1924/1965) (LATV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Ellioviricetes; Bunyavirales; Arenaviridae; Mammarenavirus.
OX NCBI_TaxID=45221;
OH NCBI_TaxID=56210; Calomys callosus (Large vesper mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=12504568; DOI=10.1006/viro.2002.1695;
RA Archer A.M., Rico-Hesse R.;
RT "High genetic divergence and recombination in Arenaviruses from the
RT Americas.";
RL Virology 304:274-281(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=12207889; DOI=10.1016/s0006-291x(02)02053-3;
RA Charrel R.N., Feldmann H., Fulhorst C.F., Khelifa R., de Chesse R.,
RA de Lamballerie X.;
RT "Phylogeny of New World arenaviruses based on the complete coding sequences
RT of the small genomic segment identified an evolutionary lineage produced by
RT intrasegmental recombination.";
RL Biochem. Biophys. Res. Commun. 296:1118-1124(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=18602020; DOI=10.1016/j.mib.2008.06.001;
RA Charrel R.N., de Lamballerie X., Emonet S.;
RT "Phylogeny of the genus Arenavirus.";
RL Curr. Opin. Microbiol. 11:362-368(2008).
RN [4]
RP INTERACTION WITH HOST IKBKE.
RX PubMed=22532683; DOI=10.1128/jvi.00187-12;
RA Pythoud C., Rodrigo W.W., Pasqual G., Rothenberger S., Martinez-Sobrido L.,
RA de la Torre J.C., Kunz S.;
RT "Arenavirus nucleoprotein targets interferon regulatory factor-activating
RT kinase IKKepsilon.";
RL J. Virol. 86:7728-7738(2012).
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 (PubMed:22532683). {ECO:0000255|HAMAP-Rule:MF_04085,
CC ECO:0000269|PubMed:22532683}.
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; AF485259; AAN09941.1; -; Genomic_RNA.
DR EMBL; AF512830; AAN32960.1; -; Genomic_RNA.
DR RefSeq; YP_001936022.1; NC_010758.1.
DR SMR; Q8BDE6; -.
DR GeneID; 6334522; -.
DR KEGG; vg:6334522; -.
DR Proteomes; UP000009262; 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 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 Reference proteome; Ribonucleoprotein; RNA-binding; Viral immunoevasion;
KW Viral nucleoprotein; Virion; Zinc.
FT CHAIN 1..557
FT /note="Nucleoprotein"
FT /id="PRO_0000361009"
FT REGION 54..235
FT /note="Binding site for the cap structure m7GTP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04085"
FT BINDING 379
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
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 389
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04085"
FT BINDING 496
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04085"
FT BINDING 499
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04085"
FT BINDING 518
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04085"
FT BINDING 522
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04085"
FT SITE 456
FT /note="Important for exonuclease activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04085"
FT VARIANT 214
FT /note="D -> N"
FT VARIANT 279
FT /note="V -> I"
SQ SEQUENCE 557 AA; 61870 MW; DA1A83B1BD7DC0C0 CRC64;
MSGASEVPSF RWTQSLRRGL SHFTTSAKGD VLRDAKSLVD GLDFNQVSQV QRVMRKDKRS
DDDLSKLRDL NRSVDSLMVM KNKQNNVSLK IGSLSKDELM DLATDLEKLK RKINLGDRQG
PGVYQGNLTS AQLEKRSEIL KSLGFQPRAN QNGVVKVWDI KNPKLLINQF GSIPALTIAC
MSVQGAEQMN DVVQGLTSLG LLYTVKYPNL DDLDKLSKDH PCLEFITKEE SANNISGYNL
SLSAAVKAGA CLVDGGNMLE TILVKPDNFQ DIVKSLLVVK RQEKMFVNEK PGLRNPYENI
LYKLCLSGEG WPYIGSRSQI VGRAWENTTV DLSKEVVYGP SAPVKNGGNM RLSPLSDTQE
AVIKEAIGKL DMDETIWIDI EGPPNDPVEL AIYQPSTGNY IHCFRVPHDE KGFKNGSKYS
HGILLRDIEN ARSGLLSRIL MRLPQKVVFT CQGSDDIQKL LQMNGRPDIA TIDMSFSSEQ
ARFFEGVVWE KFGHLCTRHN GVVLSRKKKG GNSGEPHCAL LDCIIFQAAF EGQVTGQIPK
PLLPNSLIFK DEPRVAM
