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NCAP_LYCVW
ID   NCAP_LYCVW              Reviewed;         558 AA.
AC   P07400;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1988, sequence version 1.
DT   03-AUG-2022, entry version 78.
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   Lymphocytic choriomeningitis virus (strain WE) (LCMV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC   Ellioviricetes; Bunyavirales; Arenaviridae; Mammarenavirus.
OX   NCBI_TaxID=11627;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=10036; Mesocricetus auratus (Golden hamster).
OH   NCBI_TaxID=10090; Mus musculus (Mouse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=4060885; DOI=10.1016/0168-1702(85)90001-2;
RA   Romanowski V., Matsuura Y., Bishop D.H.L.;
RT   "Complete sequence of the S RNA of lymphocytic choriomeningitis virus (WE
RT   strain) compared to that of Pichinde arenavirus.";
RL   Virus Res. 3:101-114(1985).
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; M22017; AAA46267.1; -; Genomic_RNA.
DR   PIR; B23481; VHXPLC.
DR   SMR; P07400; -.
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..558
FT                   /note="Nucleoprotein"
FT                   /id="PRO_0000079194"
FT   REGION          54..237
FT                   /note="Binding site for the cap structure m7GTP"
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         384
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04085"
FT   BINDING         392
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         502
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            459
FT                   /note="Important for exonuclease activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04085"
SQ   SEQUENCE   558 AA;  62152 MW;  DE032851A22EE889 CRC64;
     MSLSKEVKSF QWTQALRREL QGFTSDVKAA VIKDATSLLN GLDFSEVSNV QRIMRKERRD
     DKDLQRLRSL NQTVHSLVDP KSTSKKNVLK VGRLSAEELM TLAADLEKLK AKIMRTERPQ
     ASGVYMGNLT AQQLDQRSQI LQMVGMRRPQ QGASGVVRVW DVKDSSLLNN QFGTMPSLTM
     ACMAKQSQTP LNDVVQALTD LGLLYTVKYP NLSDLERLKD KHPVLGVITE QQSSINISGY
     NFSLGAAVKA GAALLHGGNM LESILIKPSN SEDLLKAVLG AKKKLNMFVS DQVGDRNPYE
     NILYKVCLSG EGWPYIACRT SVVGRAWENT TIDLTNEKLV ANSSRPVPGA AGPPQVGLSY
     SQTMLLKDLM GGIDPNAPTW IDIEGRFNDP VEIAIFQPQN GQFIHFYREP TDQKQFKQDS
     KYSHGMDLAD LFNAQAGLTS SVIGALPQGM VLSCQGSDDI RKLLDSQNRR DIKLIDVEMT
     KEASREYEDK VWDKYGWLCK MHTGVVRDKK KKEITPHCAL MDCIIFESAS KARLPDLKTV
     HNILPHDLIF RGPNVVTL
 
 
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