ID NCAP_HAZVJ Reviewed; 485 AA. AC P27318; M4PWE6; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1992, sequence version 1. DT 08-NOV-2023, entry version 63. DE RecName: Full=Nucleoprotein; DE EC=3.1.-.- {ECO:0000250|UniProtKB:P89522}; DE AltName: Full=Nucleocapsid protein; DE Short=Protein N; GN Name=N; OS Hazara virus (isolate JC280). OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina; OC Ellioviricetes; Bunyavirales; Nairoviridae; Orthonairovirus; OC Orthonairovirus hazaraense. OX NCBI_TaxID=11597; OH NCBI_TaxID=6944; Ixodes. RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RX PubMed=1641991; DOI=10.1016/0042-6822(92)90609-s; RA Marriott A.C., Nuttall P.A.; RT "Comparison of the S RNA segments and nucleoprotein sequences of Crimean- RT Congo hemorrhagic fever, Hazara, and Dugbe viruses."; RL Virology 189:795-799(1992). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Chamberlain J., Hewson R.; RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Lewandowski K.S., Bell A.J., Wooldridge D., Chamberlain J., Afrough B., RA Dowall S., Vipond R., Gharbia S., Hewson R.; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. RN [4] RP PROTEOLYTIC CLEAVAGE, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-272. RX PubMed=30720418; DOI=10.1099/jgv.0.001211; RA Fuller J., Surtees R.A., Shaw A.B., Alvarez-Rodriguez B., Slack G.S., RA Bell-Sakyi L., Mankouri J., Edwards T.A., Hewson R., Barr J.N.; RT "Hazara nairovirus elicits differential induction of apoptosis and RT nucleocapsid protein cleavage in mammalian and tick cells."; RL J. Gen. Virol. 100:392-402(2019). RN [5] RP DOMAIN, MUTAGENESIS OF 266-ASP--ASP-269 AND ASP-269, AND PROTEOLYTIC RP CLEAVAGE. RX PubMed=31118258; DOI=10.1128/jvi.00616-19; RA Fuller J., Surtees R.A., Slack G.S., Mankouri J., Hewson R., Barr J.N.; RT "Rescue of Infectious Recombinant Hazara Nairovirus from cDNA Reveals the RT Nucleocapsid Protein DQVD Caspase Cleavage Motif Performs an Essential Role RT other than Cleavage."; RL J. Virol. 93:0-0(2019). RN [6] {ECO:0007744|PDB:5A97} RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS). RX PubMed=26715309; DOI=10.1186/s12900-015-0051-3; RA Surtees R., Ariza A., Punch E.K., Trinh C.H., Dowall S.D., Hewson R., RA Hiscox J.A., Barr J.N., Edwards T.A.; RT "The crystal structure of the Hazara virus nucleocapsid protein."; RL BMC Struct. Biol. 15:24-24(2015). RN [7] {ECO:0007744|PDB:4XZE} RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS), 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). CC -!- FUNCTION: Binds dsRNA and ssRNA and probably participates in the CC packaging of viral genome (By similarity). In the dsRNA binding mode, CC the nucleocapsid protein specifically binds to the vRNA panhandle CC secondary structure formed at the termini of viral genome (By CC similarity). Does not discriminate between viral and nonviral RNAs CC through ssRNA binding mode (By similarity). Displays dsDNA endonuclease CC activity that is sequence non-specific (By similarity). CC {ECO:0000250|UniProtKB:P89522}. 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:26246561}; CC -!- SUBUNIT: Probable homooligomer; forms a double superhelical polymer (By CC similarity). Monomer (By similarity). {ECO:0000250|UniProtKB:P89522}. CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:30720418}. CC Note=Internal protein of virus particle. CC -!- DOMAIN: The DQVD motif is a CASP3/caspase 3 cleavage site essential for CC viral replication in host cell (PubMed:31118258). However, the CC importance for viral replication is apprently not linked to caspase CC cleavage (PubMed:31118258). This motif is involved in CC homooligomerization (By similarity). {ECO:0000250|UniProtKB:P89522, CC ECO:0000269|PubMed:31118258}. CC -!- PTM: Cleaved at the DQVD 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:31118258, CC PubMed:30720418). Only the monomeric form is cleaved (By similarity). CC Little or no cleavage in tick cells (PubMed:30720418). Caspase cleavage CC reduces the viral polymerase activity (By similarity). Caspase cleavage CC is not required for productive infection in mammalian or tick host CC cells (PubMed:31118258). {ECO:0000250|UniProtKB:P89522, CC ECO:0000269|PubMed:30720418, ECO:0000269|PubMed:31118258}. 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; M86624; AAA43842.1; -; Genomic_RNA. DR EMBL; KC344857; AGH10339.1; -; Viral_cRNA. DR EMBL; KP406725; AJW66843.1; -; Viral_cRNA. DR PIR; A42990; VHVUHJ. DR PDB; 4XZE; X-ray; 2.90 A; A/B/C/D=1-485. DR PDB; 5A97; X-ray; 2.70 A; A/B/C/D=1-485. DR PDBsum; 4XZE; -. DR PDBsum; 5A97; -. DR SMR; P27318; -. DR OrthoDB; 7392at10239; -. DR Proteomes; UP000170142; 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..485 FT /note="Nucleoprotein" FT /id="PRO_0000222008" FT MOTIF 269..272 FT /note="DQVD" FT /evidence="ECO:0000269|PubMed:31118258" FT SITE 216 FT /note="Homooligomerization" FT /evidence="ECO:0000269|PubMed:26715309" FT SITE 263 FT /note="Homooligomerization" FT /evidence="ECO:0000269|PubMed:26715309" FT SITE 270 FT /note="Homooligomerization" FT /evidence="ECO:0000269|PubMed:26715309" FT SITE 271 FT /note="Homooligomerization" FT /evidence="ECO:0000269|PubMed:26715309" FT SITE 272..273 FT /note="Cleavage by host CASP3/caspase 3" FT /evidence="ECO:0000269|PubMed:30720418, FT ECO:0000269|PubMed:31118258" FT SITE 275 FT /note="Homooligomerization" FT /evidence="ECO:0000269|PubMed:26715309" FT SITE 279 FT /note="Homooligomerization" FT /evidence="ECO:0000269|PubMed:26715309" FT SITE 355 FT /note="Homooligomerization" FT /evidence="ECO:0000269|PubMed:26715309" FT MUTAGEN 269..272 FT /note="DQVD->AQVA: Complete loss of viral replication." FT /evidence="ECO:0000269|PubMed:31118258" FT MUTAGEN 269 FT /note="D->E: Complete loss of cleavage by host FT CASP3/caspase 3. No effect on virus repliication in FT mammlian or tick cells." FT /evidence="ECO:0000269|PubMed:31118258" FT MUTAGEN 272 FT /note="D->A: Complete loss of cleavage by host FT CASP3/caspase 3." FT /evidence="ECO:0000269|PubMed:30720418" FT MUTAGEN 272 FT /note="D->E: Complete loss of cleavage by host FT CASP3/caspase 3. No effect on virus repliication in FT mammlian or tick cells." FT /evidence="ECO:0000269|PubMed:31118258" FT CONFLICT 296 FT /note="L -> Q (in Ref. 2; AGH10339 and 3; AJW66843)" FT /evidence="ECO:0000305" FT CONFLICT 317 FT /note="P -> L (in Ref. 2; AGH10339 and 3; AJW66843)" FT /evidence="ECO:0000305" FT HELIX 10..24 FT /evidence="ECO:0007829|PDB:5A97" FT STRAND 29..33 FT /evidence="ECO:0007829|PDB:5A97" FT HELIX 44..52 FT /evidence="ECO:0007829|PDB:5A97" FT HELIX 56..71 FT /evidence="ECO:0007829|PDB:5A97" FT TURN 72..74 FT /evidence="ECO:0007829|PDB:4XZE" FT HELIX 77..84 FT /evidence="ECO:0007829|PDB:5A97" FT HELIX 86..99 FT /evidence="ECO:0007829|PDB:5A97" FT HELIX 103..109 FT /evidence="ECO:0007829|PDB:5A97" FT HELIX 112..115 FT /evidence="ECO:0007829|PDB:5A97" FT HELIX 122..139 FT /evidence="ECO:0007829|PDB:5A97" FT HELIX 145..147 FT /evidence="ECO:0007829|PDB:5A97" FT STRAND 156..159 FT /evidence="ECO:0007829|PDB:5A97" FT TURN 162..164 FT /evidence="ECO:0007829|PDB:5A97" FT HELIX 165..183 FT /evidence="ECO:0007829|PDB:5A97" FT HELIX 199..208 FT /evidence="ECO:0007829|PDB:5A97" FT HELIX 212..216 FT /evidence="ECO:0007829|PDB:5A97" FT STRAND 228..232 FT /evidence="ECO:0007829|PDB:5A97" FT HELIX 233..245 FT /evidence="ECO:0007829|PDB:5A97" FT HELIX 248..266 FT /evidence="ECO:0007829|PDB:5A97" FT HELIX 268..270 FT /evidence="ECO:0007829|PDB:5A97" FT HELIX 273..296 FT /evidence="ECO:0007829|PDB:5A97" FT HELIX 298..303 FT /evidence="ECO:0007829|PDB:5A97" FT HELIX 309..319 FT /evidence="ECO:0007829|PDB:5A97" FT TURN 324..326 FT /evidence="ECO:0007829|PDB:5A97" FT HELIX 327..337 FT /evidence="ECO:0007829|PDB:5A97" FT HELIX 344..353 FT /evidence="ECO:0007829|PDB:5A97" FT STRAND 354..356 FT /evidence="ECO:0007829|PDB:5A97" FT HELIX 357..364 FT /evidence="ECO:0007829|PDB:5A97" FT STRAND 368..370 FT /evidence="ECO:0007829|PDB:5A97" FT HELIX 375..377 FT /evidence="ECO:0007829|PDB:5A97" FT HELIX 388..395 FT /evidence="ECO:0007829|PDB:5A97" FT STRAND 396..398 FT /evidence="ECO:0007829|PDB:4XZE" FT HELIX 403..408 FT /evidence="ECO:0007829|PDB:5A97" FT HELIX 413..418 FT /evidence="ECO:0007829|PDB:5A97" FT HELIX 423..425 FT /evidence="ECO:0007829|PDB:5A97" FT HELIX 428..443 FT /evidence="ECO:0007829|PDB:5A97" FT TURN 446..448 FT /evidence="ECO:0007829|PDB:5A97" FT STRAND 449..451 FT /evidence="ECO:0007829|PDB:5A97" FT HELIX 453..462 FT /evidence="ECO:0007829|PDB:5A97" FT HELIX 479..481 FT /evidence="ECO:0007829|PDB:4XZE" FT STRAND 483..485 FT /evidence="ECO:0007829|PDB:5A97" SQ SEQUENCE 485 AA; 54186 MW; 6053892EB6DB05EC CRC64; MENKIVASTK EEFNTWYKQF AEKHKLNNKY TESASFCAEI PQLDTYKYKM ELASTDNERD AIYSSALIEA TRFCAPIMEC AWASCTGTVK RGLEWFDKNK DSDTVKVWDA NYQKLRTETP PAEALLAYQK AALNWRKDVG FSIGEYTSIL KKAVAAEYKV PGTVINNIKE MLSDMIRRRN RIINGGSDDA PKRGPVGREH LDWCREFASG KFLNAFNPPW GEINKAGKSG YPLLATGLAK LVELEGKDVM DKAKASIAQL EGWVKENKDQ VDQDKAEDLL KGVRESYKTA LALAKLSNAF RAQGAQIDTV FSSYYWPWKA GVTPVTFPSV SQFLFELGKN PKGQKKMQKA LINTPLKWGK RLIELFADND FTENRIYMHP CVLTSGRMSE LGISFGAVPV TSPDDAAQGS GHTKAVLNYK TKTEVGNPCA CIISSLFEIQ KAGYDIESMD IVASEHLLHQ SLVGKRSPFQ NAYLIKGNAT NINII //