ID NCAP_CCHFI Reviewed; 482 AA. AC P89522; DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1997, sequence version 1. DT 08-NOV-2023, entry version 70. DE RecName: Full=Nucleoprotein; DE EC=3.1.-.- {ECO:0000269|PubMed:22421137}; DE AltName: Full=Nucleocapsid protein; DE Short=Protein N; GN Name=N; OS Crimean-Congo hemorrhagic fever virus (strain Nigeria/IbAr10200/1970) OS (CCHFV). OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina; OC Ellioviricetes; Bunyavirales; Nairoviridae; Orthonairovirus; OC Orthonairovirus haemorrhagiae. OX NCBI_TaxID=652961; OH NCBI_TaxID=9913; Bos taurus (Bovine). OH NCBI_TaxID=9925; Capra hircus (Goat). OH NCBI_TaxID=9606; Homo sapiens (Human). OH NCBI_TaxID=34625; Hyalomma. OH NCBI_TaxID=9940; Ovis aries (Sheep). OH NCBI_TaxID=6941; Rhipicephalus microplus (Cattle tick) (Boophilus microplus). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RA Lofts R., Hodgson L., Smith J.F.; RT "Crimean-Congo hemorrhagic fever virus S segment."; RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases. RN [2] RP PROTEOLYTIC CLEAVAGE, AND MUTAGENESIS OF ASP-266 AND ASP-269. RX PubMed=21123175; DOI=10.1074/jbc.m110.149369; RA Karlberg H., Tan Y.J., Mirazimi A.; RT "Induction of caspase activation and cleavage of the viral nucleocapsid RT protein in different cell types during Crimean-Congo hemorrhagic fever RT virus infection."; RL J. Biol. Chem. 286:3227-3234(2011). RN [3] RP PROTEOLYTIC CLEAVAGE, AND COFACTOR. RX PubMed=26246561; DOI=10.1128/jvi.01680-15; RA Wang W., Liu X., Wang X., Dong H., Ma C., Wang J., Liu B., Mao Y., Wang Y., RA Li T., Yang C., Guo Y.; RT "Structural and Functional Diversity of Nairovirus-Encoded RT Nucleoproteins."; RL J. Virol. 89:11740-11749(2015). RN [4] RP RNA-BINDING, AND FUNCTION. RX PubMed=28922369; DOI=10.1371/journal.pone.0184935; RA Jeeva S., Pador S., Voss B., Ganaie S.S., Mir M.A.; RT "Crimean-Congo hemorrhagic fever virus nucleocapsid protein has dual RNA RT binding modes."; RL PLoS ONE 12:e0184935-e0184935(2017). RN [5] RP DOMAIN, AND MUTAGENESIS OF 266-ASP--ASP-269. RX PubMed=30482897; DOI=10.1038/s41426-018-0192-0; RA Salata C., Monteil V., Karlberg H., Celestino M., Devignot S., Leijon M., RA Bell-Sakyi L., Bergeron E., Weber F., Mirazimi A.; RT "The DEVD motif of Crimean-Congo hemorrhagic fever virus nucleoprotein is RT essential for viral replication in tick cells."; RL Emerg. Microbes Infect. 7:190-190(2018). RN [6] {ECO:0007744|PDB:4AQF, ECO:0007744|PDB:4AQG} RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS), PROTEOLYTIC CLEAVAGE, SUBUNIT, AND RP DOMAIN. RX PubMed=22951837; DOI=10.1128/jvi.01627-12; RA Wang Y., Dutta S., Karlberg H., Devignot S., Weber F., Hao Q., Tan Y.J., RA Mirazimi A., Kotaka M.; RT "Structure of Crimean-Congo hemorrhagic fever virus nucleoprotein: RT superhelical homo-oligomers and the role of caspase-3 cleavage."; RL J. Virol. 86:12294-12303(2012). RN [7] {ECO:0007829|PDB:3U3I} RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS), SUBUNIT, PROTEOLYTIC CLEAVAGE, RP MUTAGENESIS OF TYR-374; ARG-384; GLU-387; LYS-411; HIS-453 AND GLN-457, RP COFACTOR, AND CATALYTIC ACTIVITY. RC STRAIN=YL04057; RX PubMed=22421137; DOI=10.1073/pnas.1200808109; RA Guo Y., Wang W., Ji W., Deng M., Sun Y., Zhou H., Yang C., Deng F., RA Wang H., Hu Z., Lou Z., Rao Z.; RT "Crimean-Congo hemorrhagic fever virus nucleoprotein reveals endonuclease RT activity in bunyaviruses."; RL Proc. Natl. Acad. Sci. U.S.A. 109:5046-5051(2012). CC -!- FUNCTION: Binds dsRNA and ssRNA and probably participates in the CC packaging of viral genome. In the dsRNA binding mode, the nucleocapsid CC protein specifically binds to the vRNA panhandle secondary structure CC formed at the termini of viral genome. Does not discriminate between CC viral and nonviral RNAs through ssRNA binding mode (PubMed:28922369). CC Displays dsDNA endonuclease activity that is sequence non-specific CC (PubMed:22421137). {ECO:0000269|PubMed:22421137, CC ECO:0000269|PubMed:28922369}. CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Note=Endonuclease activity is stimulated by divalent cations such as CC Mn2+, Co2+, and Mg2+. {ECO:0000269|PubMed:22421137, CC ECO:0000269|PubMed:26246561}; CC -!- SUBUNIT: Probable homooligomer; forms a double superhelical polymer CC (PubMed:22951837). Monomer (PubMed:22421137). CC {ECO:0000269|PubMed:22421137, ECO:0000269|PubMed:22951837}. CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:P27318}. CC Note=Internal protein of virus particle. CC -!- DOMAIN: The DEVD motif is a CASP3/caspase 3 cleavage site essential for CC viral replication in host cell (PubMed:30482897, PubMed:21123175). CC However, the importance for viral replication is apprently not linked CC to caspase cleavage (By similarity). This motif is involved in CC homooligomerization (PubMed:22951837). {ECO:0000250|UniProtKB:P27318, CC ECO:0000269|PubMed:21123175, ECO:0000269|PubMed:22951837, CC ECO:0000269|PubMed:30482897}. CC -!- PTM: Cleaved at the DEVD motif by host CASP3/caspase 3 in mammalian CC cells at 48 hours postinfection giving rise to cleavage products of CC about 30 kDa and 22 kDa that remain associated (PubMed:21123175) CC (Probable). Only the monomeric form is cleaved (PubMed:22951837). CC Little or no cleavage in tick cells (PubMed:21123175). Caspase cleavage CC reduces the viral polymerase activity (PubMed:22951837). Caspase CC cleavage is not required for productive infection in mammalian or tick CC host cells (By similarity). {ECO:0000250|UniProtKB:P27318, CC ECO:0000269|PubMed:21123175, ECO:0000269|PubMed:22951837, CC ECO:0000305|PubMed:26246561}. CC -!- SIMILARITY: Belongs to the nairovirus nucleocapsid protein family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U88410; AAB48501.1; -; Genomic_RNA. DR PDB; 3U3I; X-ray; 2.30 A; A=1-482. DR PDB; 4AQF; X-ray; 3.10 A; A/B/C=1-482. DR PDB; 4AQG; X-ray; 2.80 A; A=1-482. DR PDBsum; 3U3I; -. DR PDBsum; 4AQF; -. DR PDBsum; 4AQG; -. DR SMR; P89522; -. DR Proteomes; UP000008767; Genome. DR GO; GO:0019029; C:helical viral capsid; IEA:UniProtKB-KW. DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW. DR GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR Gene3D; 1.20.58.1110; -; 1. DR InterPro; IPR003486; Nairo_nucleocap. DR Pfam; PF02477; Nairo_nucleo; 1. DR PIRSF; PIRSF003950; N_NairoV; 1. PE 1: Evidence at protein level; KW 3D-structure; Capsid protein; Helical capsid protein; Hydrolase; KW Reference proteome; Ribonucleoprotein; RNA-binding; Viral nucleoprotein; KW Virion. FT CHAIN 1..482 FT /note="Nucleoprotein" FT /id="PRO_0000406568" FT MOTIF 266..269 FT /note="DEVD" FT /evidence="ECO:0000269|PubMed:30482897" FT SITE 213 FT /note="Homooligomerization" FT /evidence="ECO:0000250|UniProtKB:P27318" FT SITE 267 FT /note="Homooligomerization" FT /evidence="ECO:0000250|UniProtKB:P27318" FT SITE 268 FT /note="Homooligomerization" FT /evidence="ECO:0000250|UniProtKB:P27318" FT SITE 269..270 FT /note="Cleavage by host CASP3/caspase 3" FT /evidence="ECO:0000269|PubMed:21123175, FT ECO:0000269|PubMed:22421137" FT SITE 276 FT /note="Homooligomerization" FT /evidence="ECO:0000250|UniProtKB:P27318" FT SITE 352 FT /note="Homooligomerization" FT /evidence="ECO:0000250|UniProtKB:P27318" FT MUTAGEN 266..269 FT /note="DEVD->AEVA: Almost complete loss of production of FT viral RNA in tick cell." FT /evidence="ECO:0000269|PubMed:30482897" FT MUTAGEN 266 FT /note="D->A: Complete loss of cleavage by host FT CASP3/caspase 3." FT /evidence="ECO:0000269|PubMed:21123175" FT MUTAGEN 269 FT /note="D->A: Complete loss of cleavage by host FT CASP3/caspase 3." FT /evidence="ECO:0000269|PubMed:21123175" FT MUTAGEN 374 FT /note="Y->A: Slight loss of DNA endonuclease activity." FT /evidence="ECO:0000269|PubMed:22421137" FT MUTAGEN 384 FT /note="R->A: Loss of DNA endonuclease activity." FT /evidence="ECO:0000269|PubMed:22421137" FT MUTAGEN 387 FT /note="E->A: Loss of DNA endonuclease activity." FT /evidence="ECO:0000269|PubMed:22421137" FT MUTAGEN 411 FT /note="K->A: Loss of DNA endonuclease activity." FT /evidence="ECO:0000269|PubMed:22421137" FT MUTAGEN 453 FT /note="H->A: Loss of DNA endonuclease activity." FT /evidence="ECO:0000269|PubMed:22421137" FT MUTAGEN 457 FT /note="Q->A: Almost complete loss of DNA endonuclease FT activity." FT /evidence="ECO:0000269|PubMed:22421137" FT HELIX 10..22 FT /evidence="ECO:0007829|PDB:3U3I" FT STRAND 29..33 FT /evidence="ECO:0007829|PDB:3U3I" FT HELIX 44..51 FT /evidence="ECO:0007829|PDB:3U3I" FT STRAND 55..57 FT /evidence="ECO:0007829|PDB:3U3I" FT HELIX 60..71 FT /evidence="ECO:0007829|PDB:3U3I" FT TURN 72..74 FT /evidence="ECO:0007829|PDB:4AQG" FT HELIX 77..84 FT /evidence="ECO:0007829|PDB:3U3I" FT HELIX 86..94 FT /evidence="ECO:0007829|PDB:3U3I" FT HELIX 96..98 FT /evidence="ECO:0007829|PDB:3U3I" FT HELIX 100..107 FT /evidence="ECO:0007829|PDB:3U3I" FT HELIX 110..113 FT /evidence="ECO:0007829|PDB:3U3I" FT HELIX 120..137 FT /evidence="ECO:0007829|PDB:3U3I" FT STRAND 141..143 FT /evidence="ECO:0007829|PDB:3U3I" FT TURN 160..162 FT /evidence="ECO:0007829|PDB:3U3I" FT HELIX 163..178 FT /evidence="ECO:0007829|PDB:3U3I" FT HELIX 197..206 FT /evidence="ECO:0007829|PDB:3U3I" FT HELIX 210..213 FT /evidence="ECO:0007829|PDB:3U3I" FT STRAND 216..219 FT /evidence="ECO:0007829|PDB:3U3I" FT STRAND 223..228 FT /evidence="ECO:0007829|PDB:3U3I" FT HELIX 229..237 FT /evidence="ECO:0007829|PDB:3U3I" FT TURN 238..240 FT /evidence="ECO:0007829|PDB:3U3I" FT HELIX 246..263 FT /evidence="ECO:0007829|PDB:3U3I" FT HELIX 265..267 FT /evidence="ECO:0007829|PDB:3U3I" FT HELIX 270..301 FT /evidence="ECO:0007829|PDB:3U3I" FT HELIX 306..317 FT /evidence="ECO:0007829|PDB:3U3I" FT HELIX 321..323 FT /evidence="ECO:0007829|PDB:3U3I" FT HELIX 324..334 FT /evidence="ECO:0007829|PDB:3U3I" FT HELIX 341..350 FT /evidence="ECO:0007829|PDB:3U3I" FT HELIX 355..361 FT /evidence="ECO:0007829|PDB:3U3I" FT TURN 365..367 FT /evidence="ECO:0007829|PDB:4AQG" FT HELIX 372..374 FT /evidence="ECO:0007829|PDB:4AQG" FT TURN 382..384 FT /evidence="ECO:0007829|PDB:4AQG" FT HELIX 385..392 FT /evidence="ECO:0007829|PDB:3U3I" FT STRAND 393..395 FT /evidence="ECO:0007829|PDB:3U3I" FT HELIX 400..405 FT /evidence="ECO:0007829|PDB:3U3I" FT HELIX 410..415 FT /evidence="ECO:0007829|PDB:3U3I" FT STRAND 420..422 FT /evidence="ECO:0007829|PDB:3U3I" FT HELIX 425..440 FT /evidence="ECO:0007829|PDB:3U3I" FT STRAND 443..447 FT /evidence="ECO:0007829|PDB:3U3I" FT HELIX 450..459 FT /evidence="ECO:0007829|PDB:3U3I" FT STRAND 464..466 FT /evidence="ECO:0007829|PDB:4AQF" SQ SEQUENCE 482 AA; 53891 MW; 3E37B8A17F1B8F5D CRC64; MENKIEVNNK DEMNRWFEEF KKGNGLVDTF TNSYSFCESV PNLDRFVFQM ASATDDAQKD SIYASALVEA TKFCAPIYEC AWVSSTGIVK KGLEWFEKNA GTIKSWDESY TELKVDVPKI EQLTGYQQAA LKWRKDIGFR VNANTAALSN KVLAEYKVPG EIVMSVKEML SDMIRRRNLI LNRGGDENPR GPVSHEHVDW CREFVKGKYI MAFNPPWGDI NKSGRSGIAL VATGLAKLAE TEGKGIFDEA KKTVEALNGY LDKHKDEVDR ASADSMITNL LKHIAKAQEL YKNSSALRAQ SAQIDTAFSS YYWLYKAGVT PETFPTVSQF LFELGKQPRG TKKMKKALLS TPMKWGKKLY ELFADDSFQQ NRIYMHPAVL TAGRISEMGV CFGTIPVANP DDAAQGSGHT KSILNLRTNT ETNNPCAKTI VKLFEVQKTG FNIQDMDIVA SEHLLHQSLV GKQSPFQNAY NVKGNATSAN II //