NCAP_TACVF
ID NCAP_TACVF Reviewed; 570 AA.
AC P18140;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 88.
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 Tacaribe virus (strain Franze-Fernandez) (TCRV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Ellioviricetes; Bunyavirales; Arenaviridae; Mammarenavirus.
OX NCBI_TaxID=928313;
OH NCBI_TaxID=9416; Artibeus (neotropical fruit bats).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3617928; DOI=10.1016/0168-1702(87)90045-1;
RA Franze-Fernandez M.T., Zetina C., Iapalucci S., Lucero M.A., Bouissou C.,
RA Lopez R., Rey O., Daheli M., Cohen G.N., Zakin M.M.;
RT "Molecular structure and early events in the replication of Tacaribe
RT arenavirus S RNA.";
RL Virus Res. 7:309-324(1987).
RN [2]
RP INTERACTION WITH PROLEIN L.
RX PubMed=12970423; DOI=10.1128/jvi.77.19.10383-10393.2003;
RA Jacamo R., Lopez N., Wilda M., Franze-Fernandez M.T.;
RT "Tacaribe virus Z protein interacts with the L polymerase protein to
RT inhibit viral RNA synthesis.";
RL J. Virol. 77:10383-10393(2003).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) OF 364-570, AND ZINC BINDING.
RX PubMed=23615902; DOI=10.1074/jbc.m112.420521;
RA Jiang X., Huang Q., Wang W., Dong H., Ly H., Liang Y., Dong C.;
RT "Structures of arenaviral nucleoproteins with triphosphate dsRNA reveal a
RT unique mechanism of immune suppression.";
RL J. Biol. Chem. 288:16949-16959(2013).
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, ECO:0000269|PubMed:12970423}.
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; M20304; AAA47903.1; -; Genomic_RNA.
DR RefSeq; NP_694850.1; NC_004293.1.
DR PDB; 4GVE; X-ray; 1.73 A; A=364-570.
DR PDBsum; 4GVE; -.
DR SMR; P18140; -.
DR GeneID; 956597; -.
DR KEGG; vg:956597; -.
DR Proteomes; UP000008026; 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 Reference proteome; Ribonucleoprotein; RNA-binding; Viral immunoevasion;
KW Viral nucleoprotein; Virion; Zinc.
FT CHAIN 1..570
FT /note="Nucleoprotein"
FT /id="PRO_0000079197"
FT REGION 54..236
FT /note="Binding site for the cap structure m7GTP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04085"
FT REGION 332..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 386
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:23615902"
FT BINDING 386
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04085"
FT BINDING 388
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:23615902"
FT BINDING 388
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04085"
FT BINDING 396
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04085,
FT ECO:0000269|PubMed:23615902"
FT BINDING 503
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04085,
FT ECO:0000269|PubMed:23615902"
FT BINDING 506
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04085,
FT ECO:0000269|PubMed:23615902"
FT BINDING 531
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04085,
FT ECO:0000269|PubMed:23615902"
FT BINDING 535
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:23615902"
FT BINDING 535
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04085"
FT SITE 463
FT /note="Important for exonuclease activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04085"
FT HELIX 364..375
FT /evidence="ECO:0007829|PDB:4GVE"
FT STRAND 384..389
FT /evidence="ECO:0007829|PDB:4GVE"
FT STRAND 396..401
FT /evidence="ECO:0007829|PDB:4GVE"
FT HELIX 402..404
FT /evidence="ECO:0007829|PDB:4GVE"
FT STRAND 406..411
FT /evidence="ECO:0007829|PDB:4GVE"
FT HELIX 417..426
FT /evidence="ECO:0007829|PDB:4GVE"
FT HELIX 432..435
FT /evidence="ECO:0007829|PDB:4GVE"
FT HELIX 442..449
FT /evidence="ECO:0007829|PDB:4GVE"
FT STRAND 455..460
FT /evidence="ECO:0007829|PDB:4GVE"
FT HELIX 461..470
FT /evidence="ECO:0007829|PDB:4GVE"
FT STRAND 476..480
FT /evidence="ECO:0007829|PDB:4GVE"
FT HELIX 485..488
FT /evidence="ECO:0007829|PDB:4GVE"
FT TURN 489..491
FT /evidence="ECO:0007829|PDB:4GVE"
FT HELIX 492..499
FT /evidence="ECO:0007829|PDB:4GVE"
FT HELIX 500..502
FT /evidence="ECO:0007829|PDB:4GVE"
FT HELIX 532..544
FT /evidence="ECO:0007829|PDB:4GVE"
FT STRAND 553..556
FT /evidence="ECO:0007829|PDB:4GVE"
FT HELIX 558..560
FT /evidence="ECO:0007829|PDB:4GVE"
SQ SEQUENCE 570 AA; 63811 MW; E3DAFC8E55AB9355 CRC64;
MAQSKEVPSF RWTQSLRKGL SQFTQTVKSD ILKDAKLIAD SIDFNQVAQV QRVLRKTKRT
DDDLNKLRDL NIEVDRLMSM KSVQKNTIFK VGDLARDELM ELASDLEKLK DKIKRTESNG
TNAYMGNLPQ SQLNRRSEIL RTLGFAQQGG RPNGIVRVWD VKDSSKLNNQ FGSMPALTIA
CMTVQGGETM NNVVQALTSL GLLYTVKYPN LSDLDKLIPN HECLQIITKE ESSINISGYN
LSLLAAVKAG ASILDGGNML ETIRVSPDNF SSLIKNTLQV KRREGMFIDD RPGSRNPYEN
LLYKLCLSGD GWPYIGSRSQ IMGRSWDNTS VDLTKKPDAV PEPGAAPRPA ERKGQNLRLA
SLTEGQELIV RAAISELDPS NTIWLDIEDL QLDPVELALY QPAKKQYIHC FRKPHDEKGF
KNGSRHSHGI LMKDIEDAVP GVLSYVIGLL PPNMVITTQG SDDIRKLLDI HGRKDLKLID
VKFTSDQARL FEHQVWDKFG HLCKQHNGVI ISKKNKSKDS PPSPSPDEPH CALLDCIMFH
SAVSGELPKE EPIPLLPKEF LFFPKTAFAL
