NCAP_MABVO
ID NCAP_MABVO Reviewed; 695 AA.
AC Q6UY69;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Nucleoprotein;
DE AltName: Full=Nucleocapsid protein;
GN Name=NP;
OS Lake Victoria marburgvirus (strain Ozolin-75) (MARV) (Marburg virus (strain
OS South Africa/Ozolin/1975)).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Filoviridae; Marburgvirus.
OX NCBI_TaxID=482820;
OH NCBI_TaxID=9534; Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9407; Rousettus aegyptiacus (Egyptian rousette) (Egyptian fruit bat).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA Bowen M.D., Thurman K., Minor E., Ibrahim M.S., Meyer R.F., Malfatti S.A.,
RA Do L.H., Smith K.L., McCready P.M., Chain P.S.G.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Encapsidates the genome, protecting it from nucleases. The
CC encapsidated genomic RNA is termed the nucleocapsid and serves as
CC template for transcription and replication. During replication,
CC encapsidation by NP is coupled to RNA synthesis and all replicative
CC products are resistant to nucleases (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homooligomer. Homomultimerizes to form the nucleocapsid. Binds
CC to viral genomic RNA. Interacts with VP35 and VP30 to form the
CC nucleocapsid. Also interacts with VP24 and VP40 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Virion. Host cytoplasm {ECO:0000250}.
CC -!- DOMAIN: This protein can be divided into a hydrophobic N-terminal half,
CC and a hydrophilic and highly acidic C-terminal half. {ECO:0000250}.
CC -!- DOMAIN: The coiled coil region is critical for homooligomerization, for
CC the interaction with VP35 and for NP function in RNA synthesis.
CC {ECO:0000250}.
CC -!- DOMAIN: Late-budding domains (L domains) are short sequence motifs
CC essential for viral particle budding. They recruit proteins of the host
CC ESCRT machinery (Endosomal Sorting Complex Required for Transport) or
CC ESCRT-associated proteins. Nucleoprotein contains one L domain: a
CC PTAP/PSAP motif, which interacts with the UEV domain of TSG101 (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the filoviruses nucleoprotein family.
CC {ECO:0000305}.
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DR EMBL; AY358025; AAQ55255.1; -; Genomic_RNA.
DR PDB; 5F5M; X-ray; 2.90 A; A/B=19-370.
DR PDB; 5F5O; X-ray; 2.20 A; A/C/E=19-370.
DR PDB; 5XSQ; X-ray; 2.60 A; A/C/E=18-344.
DR PDBsum; 5F5M; -.
DR PDBsum; 5F5O; -.
DR PDBsum; 5XSQ; -.
DR SMR; Q6UY69; -.
DR Proteomes; UP000000838; Genome.
DR GO; GO:0019029; C:helical viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0039702; P:viral budding via host ESCRT complex; IEA:UniProtKB-KW.
DR GO; GO:0019074; P:viral RNA genome packaging; IEA:InterPro.
DR InterPro; IPR008609; Ebola_NP.
DR Pfam; PF05505; Ebola_NP; 1.
DR PIRSF; PIRSF003900; N_FiloV; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Capsid protein; Coiled coil; Helical capsid protein;
KW Host cytoplasm; Host-virus interaction; Phosphoprotein; Reference proteome;
KW Ribonucleoprotein; RNA-binding; Viral budding;
KW Viral budding via the host ESCRT complexes; Viral nucleoprotein;
KW Viral release from host cell; Virion.
FT CHAIN 1..695
FT /note="Nucleoprotein"
FT /id="PRO_0000314974"
FT REGION 424..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 483..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 316..341
FT /evidence="ECO:0000255"
FT COILED 372..399
FT /evidence="ECO:0000255"
FT MOTIF 603..606
FT /note="PTAP/PSAP motif"
FT /evidence="ECO:0000250"
FT COMPBIAS 483..502
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 571..585
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 22..27
FT /evidence="ECO:0007829|PDB:5F5O"
FT HELIX 31..43
FT /evidence="ECO:0007829|PDB:5F5O"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:5F5O"
FT HELIX 52..65
FT /evidence="ECO:0007829|PDB:5F5O"
FT HELIX 69..73
FT /evidence="ECO:0007829|PDB:5F5O"
FT HELIX 76..83
FT /evidence="ECO:0007829|PDB:5F5O"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:5F5O"
FT HELIX 99..102
FT /evidence="ECO:0007829|PDB:5F5O"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:5F5O"
FT HELIX 110..117
FT /evidence="ECO:0007829|PDB:5F5O"
FT HELIX 127..137
FT /evidence="ECO:0007829|PDB:5F5O"
FT HELIX 138..145
FT /evidence="ECO:0007829|PDB:5F5O"
FT HELIX 147..163
FT /evidence="ECO:0007829|PDB:5F5O"
FT HELIX 171..174
FT /evidence="ECO:0007829|PDB:5F5O"
FT HELIX 176..188
FT /evidence="ECO:0007829|PDB:5F5O"
FT HELIX 190..201
FT /evidence="ECO:0007829|PDB:5F5O"
FT HELIX 211..221
FT /evidence="ECO:0007829|PDB:5F5O"
FT TURN 222..226
FT /evidence="ECO:0007829|PDB:5F5O"
FT HELIX 227..234
FT /evidence="ECO:0007829|PDB:5F5O"
FT STRAND 237..240
FT /evidence="ECO:0007829|PDB:5F5M"
FT STRAND 243..246
FT /evidence="ECO:0007829|PDB:5F5M"
FT TURN 248..251
FT /evidence="ECO:0007829|PDB:5F5O"
FT HELIX 253..255
FT /evidence="ECO:0007829|PDB:5F5O"
FT HELIX 256..270
FT /evidence="ECO:0007829|PDB:5F5O"
FT HELIX 271..278
FT /evidence="ECO:0007829|PDB:5F5O"
FT TURN 279..283
FT /evidence="ECO:0007829|PDB:5F5O"
FT HELIX 292..294
FT /evidence="ECO:0007829|PDB:5F5O"
FT HELIX 296..308
FT /evidence="ECO:0007829|PDB:5F5O"
FT HELIX 320..322
FT /evidence="ECO:0007829|PDB:5F5O"
FT HELIX 323..334
FT /evidence="ECO:0007829|PDB:5F5O"
SQ SEQUENCE 695 AA; 77673 MW; D94A87F0C12FD85A CRC64;
MDLHSLLELG TKPTAPHVRN KKVILFDTNH QVSICNQIID AINSGIDLGD LLEGGLLTLC
VEHYYNSDKD KFNTSPIAKY LRDAGYEFDV IKNADATRFL DVIPNEPHYS PLILALKTLE
STESQRGRIG LFLSFCSLFL PKLVVGDRAS IEKALRQVTV HQEQGIVTYP NHWLTTGHMK
VIFGILRSSF ILKFVLIHQG VNLVTGHDAY DSIISNSVGQ TRFSGLLIVK TVLEFILQKT
DSGVTLHPLV RTSKVKNEVA SFKQALSNLA RHGEYAPFAR VLNLSGINNL EHGLYPQLSA
IALGVATAHG STLAGVNVGE QYQQLREAAH DAEVKLQRRH EHQEIQAIAE DDEERKILEQ
FHLQKTEITH SQTLAVLSQK REKLARLAAE IENNIVEDQG FKQSQNRVSQ SFLNDPTPVE
VTVQARPVNR PTALPPPVDD KIEHESTEDS SSSSSFVDLN DPFALLNEDE DTLDDSVMIP
STTSREFQGI PESPGQSQDL DNSQGKQEDE STNPIKKQFL RYQELPPVQE DDESEYTTDS
QESIDQPGSD NEQGVDLPPP PLYTQEKRQD PIQHPAASSQ DPFGSIGDVN GDILEPIRSP
SSPSAPQEDT RAREAYELSP DFTNYEDNQQ NWPQRVVTKK GRTFLYPNDL LQTSPPESLV
TALVEEYQNP VSAKELQADW PDMSFDERRH VAMNL
