NCAP_MOPEI
ID NCAP_MOPEI Reviewed; 570 AA.
AC P19239;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 83.
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 Mopeia virus (MOPV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Ellioviricetes; Bunyavirales; Arenaviridae; Mammarenavirus.
OX NCBI_TaxID=11629;
OH NCBI_TaxID=10112; Mastomys natalensis (African soft-furred rat) (Praomys natalensis).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=800150;
RX PubMed=1989384; DOI=10.1016/0042-6822(91)90068-m;
RA Wilson S.M., Clegg J.C.S.;
RT "Sequence analysis of the S RNA of the African arenavirus Mopeia: an
RT unusual secondary structure feature in the intergenic region.";
RL Virology 180:543-552(1991).
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; M33879; AAC08701.1; -; Genomic_RNA.
DR PIR; B38546; B38546.
DR PDB; 6T2A; X-ray; 2.00 A; A/B=365-570.
DR PDB; 6T6L; X-ray; 1.76 A; A/B/C=365-570.
DR PDBsum; 6T2A; -.
DR PDBsum; 6T6L; -.
DR SMR; P19239; -.
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..570
FT /note="Nucleoprotein"
FT /id="PRO_0000079195"
FT REGION 54..241
FT /note="Binding site for the cap structure m7GTP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04085"
FT BINDING 390
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04085"
FT BINDING 392
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04085"
FT BINDING 400
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04085"
FT BINDING 507
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04085"
FT BINDING 510
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04085"
FT BINDING 530
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04085"
FT BINDING 534
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04085"
FT SITE 467
FT /note="Important for exonuclease activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04085"
FT HELIX 368..378
FT /evidence="ECO:0007829|PDB:6T2A"
FT STRAND 388..393
FT /evidence="ECO:0007829|PDB:6T2A"
FT STRAND 399..404
FT /evidence="ECO:0007829|PDB:6T2A"
FT TURN 406..408
FT /evidence="ECO:0007829|PDB:6T2A"
FT STRAND 410..415
FT /evidence="ECO:0007829|PDB:6T2A"
FT HELIX 421..430
FT /evidence="ECO:0007829|PDB:6T2A"
FT HELIX 436..441
FT /evidence="ECO:0007829|PDB:6T2A"
FT HELIX 446..453
FT /evidence="ECO:0007829|PDB:6T2A"
FT STRAND 459..464
FT /evidence="ECO:0007829|PDB:6T2A"
FT HELIX 466..474
FT /evidence="ECO:0007829|PDB:6T2A"
FT STRAND 480..484
FT /evidence="ECO:0007829|PDB:6T2A"
FT HELIX 489..492
FT /evidence="ECO:0007829|PDB:6T2A"
FT TURN 493..495
FT /evidence="ECO:0007829|PDB:6T2A"
FT HELIX 496..503
FT /evidence="ECO:0007829|PDB:6T2A"
FT HELIX 504..506
FT /evidence="ECO:0007829|PDB:6T2A"
FT HELIX 531..543
FT /evidence="ECO:0007829|PDB:6T2A"
FT HELIX 557..560
FT /evidence="ECO:0007829|PDB:6T2A"
FT STRAND 561..563
FT /evidence="ECO:0007829|PDB:6T2A"
SQ SEQUENCE 570 AA; 63435 MW; 01C7716D9138F7F5 CRC64;
MSNSKEVKSF LWTQSLRREL SGYCSNIKIQ VIKDAQALLH GLDFSEVANV QRLMRKEKRD
DSDLKRLRDL NQAVNNLVEL KSVQQKNVLR VGTLTSDDLL VLAADLDRLK AKVIRGERPL
AAGVYMGNLT AQQLEQRRVL LQMVGMGGGF RAGNTLGDGI VRVWDVRNPE LLNNQFGTMP
SLTIACMCKQ GQADLNDVIQ SLSDLGLVYT AKYPNMSDLD KLSQTHPILG IIEPKKSAIN
ISGYNFSLSA AVKAGACLID GGNMLETIKV TKSNLEGILK AALKVKRSLG MFVSDTPGER
NPYENLLYKL CLSGEGWPYI ASRTSIVGRA WDNTTVDLSG DVQQNAKPDK GNSNRLAQAQ
GMPAGLTYSQ TMELKDSMLQ LDPNAKTWID IEGRPEDPVE IAIYQPNNGQ YIHFYREPTD
IKQFKQDSKH SHGIDIQDLF SVQPGLTSAV IESLPKNMVL SCQGADDIRK LLDSQNRRDI
KLIDVSMQKD DARKFEDKIW DEYKHLCRMH TGIVTQKKKR GGKEEVTPHC ALLDCLMFEA
AVIGSPQIPT PRPVLSRDLV FRTGPPRVVL
