NCAP_DOBV
ID NCAP_DOBV Reviewed; 429 AA.
AC Q805Q9;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Nucleoprotein;
DE EC=3.1.-.- {ECO:0000250|UniProtKB:Q89462};
DE AltName: Full=Nucleocapsid protein;
DE Short=Protein N;
GN Name=N;
OS Dobrava-Belgrade orthohantavirus (DOBV) (Dobrava virus).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Ellioviricetes; Bunyavirales; Hantaviridae; Mammantavirinae;
OC Orthohantavirus.
OX NCBI_TaxID=1980467;
OH NCBI_TaxID=39030; Apodemus agrarius (Eurasian field mouse).
OH NCBI_TaxID=54292; Apodemus flavicollis (Yellow-necked field mouse).
OH NCBI_TaxID=134909; Apodemus ponticus (Caucasus field mouse).
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=DOBV/Ano-Poroia/13Af/99, and Isolate DOBV/Ano-Poroia/Afl9/1999;
RX PubMed=12526053; DOI=10.1002/jmv.10304;
RA Nemirov K., Vapalahti O., Papa A., Plyusnina A., Lundkvist A.,
RA Antoniadis A., Plyusnin A.;
RT "Genetic characterization of new Dobrava hantavirus isolate from Greece.";
RL J. Med. Virol. 69:408-416(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate DOB/Gola/242Af/07 {ECO:0000312|EMBL:AGR50902.1},
RC Isolate DOB/Gola/291Af/07 {ECO:0000312|EMBL:AGR50903.1}, and
RC Isolate DOB/Pecs/210Af/07 {ECO:0000312|EMBL:AGR50900.1};
RA Nemeth V.;
RT "Not all hantavirus sequences derived from Apodemus agrarius belongs to
RT Saaremaa virus.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Isolate DOBV/Croatia_Gerovo/Af894/2008
RC {ECO:0000312|EMBL:AGO27859.1},
RC Isolate DOBV/Croatia_Gerovo/Af903/2008 {ECO:0000312|EMBL:AGO27860.1},
RC Isolate DOBV/Croatia_Gerovo/Af910/2008 {ECO:0000312|EMBL:AGO27861.1},
RC Isolate DOBV/Croatia_Gerovo/Af957/2008 {ECO:0000312|EMBL:AGO27864.1},
RC Isolate DOBV/Croatia_Gerovo/Af965/2008 {ECO:0000312|EMBL:AGO27866.1},
RC Isolate DOBV/Croatia_Gerovo/Af966/2008 {ECO:0000312|EMBL:AGO27867.1},
RC Isolate DOBV/Croatia_Gerovo/Af967/2008 {ECO:0000312|EMBL:AGO27868.1},
RC Isolate DOBV/Croatia_Gerovo/Af968/2008 {ECO:0000312|EMBL:AGO27869.1},
RC Isolate DOBV/Croatia_Gerovo/Af970/2008 {ECO:0000312|EMBL:AGO27870.1},
RC Isolate DOBV/Croatia_Zutica/Af813/2007 {ECO:0000312|EMBL:AGO27871.1},
RC Isolate DOBV/Croatia_Zutica/Af815/2007 {ECO:0000312|EMBL:AGO27872.1},
RC Isolate DOBV/Croatia_Zutica/As822/2007 {ECO:0000312|EMBL:AGO27875.1}, and
RC Isolate DOBV/Croatia_Zutica/As825/2007 {ECO:0000312|EMBL:AGO27877.1};
RX PubMed=24866325; DOI=10.1089/vbz.2013.1457;
RA Svoboda P., Dobler G., Markotic A., Kurolt I.C., Speck S., Habus J.,
RA Vucelja M., Krajinovic L.C., Tadin A., Margaletic J., Essbauer S.;
RT "Survey for hantaviruses, tick-borne encephalitis virus, and Rickettsia
RT spp. in small rodents in Croatia.";
RL Vector Borne Zoonotic Dis. 14:523-530(2014).
CC -!- FUNCTION: Encapsidates the genome protecting it from nucleases
CC (Probable). The encapsidated genomic RNA is termed the nucleocapsid
CC (NC) and serves as template for transcription and replication
CC (Probable). The nucleocapsid has a left-handed helical structure (By
CC similarity). As a trimer, specifically binds and acts as a chaperone to
CC unwind the panhandle structure formed by the viral RNA (vRNA) termini
CC (By similarity). Involved in the transcription and replication
CC initiation of vRNA by mediating primer annealing (By similarity). Plays
CC a role in cap snatching by sequestering capped RNAs in P bodies for use
CC by the viral RdRp during transcription initiation (By similarity).
CC Substitutes for the cellular cap-binding complex (eIF4F) to
CC preferentially facilitate the translation of capped mRNAs (By
CC similarity). Initiates the translation by specifically binding to the
CC cap and 40S ribosomal subunit (By similarity). Prevents the viral
CC glycoprotein N (Gn) from autophagy-dependent breakdown maybe by
CC blocking autophagosome formation (By similarity). Inhibits host
CC EIF2AK2/PKR dimerization to prevent PKR-induced translational shutdown
CC in cells and thus the activation of the antiviral state (By
CC similarity). Also displays sequence-unspecific DNA endonuclease
CC activity (By similarity). {ECO:0000250|UniProtKB:O36307,
CC ECO:0000250|UniProtKB:P05133, ECO:0000250|UniProtKB:Q89462,
CC ECO:0000305}.
CC -!- SUBUNIT: Homotrimer (By similarity). Homomultimer (By similarity).
CC Homomultimerizes and binds to viral genomic RNA to form the
CC nucleocapsid (By similarity). Interacts with host MAP1LC3B; this
CC interaction participates to the protection of Gn from virus-triggered
CC autophagy (By similarity). Interacts with host SNAP29; this interaction
CC participates to the protection of glycoprotein N from virus-triggered
CC autophagy (By similarity). Interacts (via N-terminus) with host RPS19;
CC this interaction probably mediates the loading of the 40S ribosomal
CC subunit on viral capped mRNA during N-mediated translation initiation
CC (By similarity). Interacts with the viral RdRp (By similarity).
CC Interacts with host SUMO1 (via N-terminus) (By similarity). Interacts
CC with host DAXX (By similarity). Interacts with the viral glycoprotein N
CC (via C-terminus) (By similarity). Interacts with the viral glycoprotein
CC C (via C-terminus) (By similarity). {ECO:0000250|UniProtKB:P05133,
CC ECO:0000250|UniProtKB:P27313, ECO:0000250|UniProtKB:Q88918,
CC ECO:0000250|UniProtKB:Q89462}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:P05133}. Host
CC cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P05133}. Host
CC Golgi apparatus, host cis-Golgi network {ECO:0000250|UniProtKB:P05133}.
CC Note=Internal protein of virus particle.
CC {ECO:0000250|UniProtKB:P05133}.
CC -!- DOMAIN: The N-terminus is required for chaperone activity and, in
CC trimeric form, this region likely serves in high affinity vRNA
CC panhandle recognition (By similarity). The N-terminus also contains a
CC coiled coil region, which probably participates in but is insufficient
CC to initiate N trimerization (By similarity). The YxxL motif is
CC indispensable for the interaction with host MAP1LC3B (By similarity).
CC The central region is involved in specific RNA-binding (By similarity).
CC Has distinct cap- and RNA-binding sites so it can bind simultaneously
CC both the vRNA and mRNA cap (By similarity).
CC {ECO:0000250|UniProtKB:P05133, ECO:0000250|UniProtKB:Q89462}.
CC -!- SIMILARITY: Belongs to the hantavirus nucleocapsid protein family.
CC {ECO:0000305}.
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DR EMBL; AJ410615; CAC85163.1; -; Genomic_RNA.
DR EMBL; AJ410619; CAC85166.1; -; Genomic_RNA.
DR EMBL; KC848494; AGR50900.1; -; Viral_cRNA.
DR EMBL; KC848496; AGR50902.1; -; Viral_cRNA.
DR EMBL; KC848497; AGR50903.1; -; Viral_cRNA.
DR EMBL; KC676590; AGO27859.1; -; Viral_cRNA.
DR EMBL; KC676591; AGO27860.1; -; Viral_cRNA.
DR EMBL; KC676592; AGO27861.1; -; Viral_cRNA.
DR EMBL; KC676595; AGO27864.1; -; Viral_cRNA.
DR EMBL; KC676597; AGO27866.1; -; mRNA.
DR EMBL; KC676598; AGO27867.1; -; mRNA.
DR EMBL; KC676599; AGO27868.1; -; mRNA.
DR EMBL; KC676600; AGO27869.1; -; mRNA.
DR EMBL; KC676601; AGO27870.1; -; mRNA.
DR EMBL; KC676602; AGO27871.1; -; mRNA.
DR EMBL; KC676603; AGO27872.1; -; mRNA.
DR EMBL; KC676606; AGO27875.1; -; mRNA.
DR EMBL; KC676608; AGO27877.1; -; mRNA.
DR RefSeq; NP_942553.1; NC_005233.1.
DR SMR; Q805Q9; -.
DR GeneID; 2656266; -.
DR KEGG; vg:2656266; -.
DR Proteomes; UP000202548; Genome.
DR GO; GO:0019029; C:helical viral capsid; IEA:UniProtKB-UniRule.
DR GO; GO:0044177; C:host cell Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0044220; C:host cell perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-UniRule.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR InterPro; IPR002214; Hanta_nucleocap.
DR Pfam; PF00846; Hanta_nucleocap; 1.
DR PIRSF; PIRSF003949; N_HantaV; 1.
PE 2: Evidence at transcript level;
KW Chaperone; Coiled coil; Endonuclease; Host cytoplasm; Host Golgi apparatus;
KW Hydrolase; Nuclease; Ribonucleoprotein; RNA-binding; Viral nucleoprotein;
KW Virion.
FT CHAIN 1..429
FT /note="Nucleoprotein"
FT /id="PRO_0000455184"
FT REGION 1..175
FT /note="Viral panhandle binding"
FT /evidence="ECO:0000250|UniProtKB:Q89462"
FT REGION 1..100
FT /note="Chaperone activity"
FT /evidence="ECO:0000250|UniProtKB:Q89462"
FT REGION 1..79
FT /note="Homomultimerization"
FT /evidence="ECO:0000250|UniProtKB:Q88918"
FT REGION 1..50
FT /note="RdRP binding"
FT /evidence="ECO:0000250|UniProtKB:Q89462"
FT REGION 27..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 80..248
FT /note="Interaction with glycoprotein N"
FT /evidence="ECO:0000250|UniProtKB:Q88918"
FT REGION 100..125
FT /note="Homomultimerization"
FT /evidence="ECO:0000250|UniProtKB:P05133"
FT REGION 150..175
FT /note="Interaction with host RPS19"
FT /evidence="ECO:0000250|UniProtKB:Q89462"
FT REGION 175..217
FT /note="Viral RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P05133"
FT REGION 188..191
FT /note="Interaction with host UBE2I/UBC9"
FT /evidence="ECO:0000250|UniProtKB:P05133"
FT REGION 373..429
FT /note="Interaction with host DAXX"
FT /evidence="ECO:0000250|UniProtKB:P27313"
FT REGION 373..421
FT /note="Homomultimerization"
FT /evidence="ECO:0000250|UniProtKB:Q88918"
FT COILED 4..31
FT /evidence="ECO:0000255"
FT MOTIF 178..181
FT /note="YxxL"
FT /evidence="ECO:0000250|UniProtKB:P05133"
FT COMPBIAS 27..45
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 88
FT /note="Important for the endonuclease activity"
FT /evidence="ECO:0000250|UniProtKB:Q89462"
FT SITE 103
FT /note="Important for the endonuclease activity"
FT /evidence="ECO:0000250|UniProtKB:Q89462"
SQ SEQUENCE 429 AA; 48148 MW; 1C30A0F61E13A6D2 CRC64;
MATLEELQKE INNHEGQLVI ARQKVKDAEK QYEKDPDDLN KRALSDRESI AQSIQGKIDE
LRRQLADRVA AGKNIGKERD PTGLDPGDHL KEKSMLSYGN VIDLNHLDID EPTGQTADWL
SIVVYLTSFV VPILLKALYM LTTRGRQTTK DNKGMRIRFK DDSSFEDVNG IRKPKHLFLS
MPNAQSSMKA DEITPGRFRT AICGLYPAQV KARNLISPVM SVIGFLALAK NWTERVEEWL
DLPCKLLSEP SPTSLTKGPS TNRDYLNQRQ GALAKMETKE AQAVRKHAID AGCNLIDHID
SPSSIWVFAG APDRCPPTCL FIAGMAELGA FFAVLQDMRN TIMASKTIGT SEEKLKKKSS
FYQSYLRRTQ SMGIQLDQRI IVLFMVDWGK EAVDSFHLGD DMDPELRGLA QALIDQKVKE
ISNQEPLKL
