NCAP_VSIVN
ID NCAP_VSIVN Reviewed; 422 AA.
AC Q77E03;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 29-SEP-2021, entry version 68.
DE RecName: Full=Nucleoprotein;
DE Short=NP;
DE AltName: Full=Nucleocapsid protein;
DE Short=Protein N;
GN Name=N;
OS Vesicular stomatitis Indiana virus (strain 98COE North America) (VSIV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC Vesiculovirus.
OX NCBI_TaxID=434488;
OH NCBI_TaxID=7158; Aedes.
OH NCBI_TaxID=9913; Bos taurus (Bovine).
OH NCBI_TaxID=58271; Culicoides.
OH NCBI_TaxID=9793; Equus asinus (Donkey) (Equus africanus asinus).
OH NCBI_TaxID=9796; Equus caballus (Horse).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=252607; Lutzomyia.
OH NCBI_TaxID=7370; Musca domestica (House fly).
OH NCBI_TaxID=7190; Simuliidae (black flies).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=12237430; DOI=10.1099/0022-1317-83-10-2475;
RA Rodriguez L.L., Pauszek S.J., Bunch T.A., Schumann K.R.;
RT "Full-length genome analysis of natural isolates of vesicular stomatitis
RT virus (Indiana 1 serotype) from North, Central and South America.";
RL J. Gen. Virol. 83:2475-2483(2002).
CC -!- FUNCTION: Encapsidates the genome in a ratio of one N per nine
CC ribonucleotides, protecting it from nucleases. The encapsidated genomic
CC RNA is termed the NC and serves as template for transcription and
CC replication. Replication is dependent on intracellular concentration of
CC newly synthesized N, termed N(0), which corresponds to the protein not
CC associated with RNA. In contrast, when associated with RNA, it is
CC termed N. During replication, encapsidation by N(0) is coupled to RNA
CC synthesis and all replicative products are resistant to nucleases (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homomultimerizes to form the nucleocapsid. Binds to viral
CC genomic RNA. N in nucleocapsid binds the P protein and thereby
CC positions the polymerase on the template. Interaction of N(0) with the
CC P protein prevents the uncontrolled aggregation of N(0) (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Virion. Host cytoplasm. Note=The nucleocapsid is
CC synthesized in the cytoplasm, and is subsequently transported via
CC microtubules to the cell periphery. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the vesiculovirus nucleocapsid protein family.
CC {ECO:0000305}.
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DR EMBL; AF473864; AAN16980.1; -; Genomic_RNA.
DR RefSeq; NP_041712.1; NC_001560.1.
DR PDB; 3HHW; X-ray; 2.70 A; K/L/M/N/O=2-422.
DR PDB; 3HHZ; X-ray; 3.50 A; K/L/M/N/O=2-422.
DR PDBsum; 3HHW; -.
DR PDBsum; 3HHZ; -.
DR SMR; Q77E03; -.
DR DNASU; 1489831; -.
DR GeneID; 1489831; -.
DR KEGG; vg:1489831; -.
DR EvolutionaryTrace; Q77E03; -.
DR Proteomes; UP000007624; 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 Gene3D; 1.10.3570.10; -; 1.
DR Gene3D; 1.10.3610.10; -; 1.
DR InterPro; IPR000448; Rhabdo_ncapsid.
DR InterPro; IPR023331; Rhabdovirus_ncapsid_C.
DR InterPro; IPR023330; Rhabdovirus_ncapsid_N.
DR InterPro; IPR035961; Rhabdovirus_nucleoprotein-like.
DR Pfam; PF00945; Rhabdo_ncap; 1.
DR SUPFAM; SSF140809; SSF140809; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Capsid protein; Helical capsid protein; Host cytoplasm;
KW Ribonucleoprotein; RNA-binding; Viral nucleoprotein; Virion.
FT CHAIN 1..422
FT /note="Nucleoprotein"
FT /id="PRO_0000287270"
FT STRAND 5..7
FT /evidence="ECO:0007829|PDB:3HHW"
FT TURN 8..10
FT /evidence="ECO:0007829|PDB:3HHW"
FT HELIX 28..30
FT /evidence="ECO:0007829|PDB:3HHW"
FT TURN 31..34
FT /evidence="ECO:0007829|PDB:3HHW"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:3HHW"
FT HELIX 48..60
FT /evidence="ECO:0007829|PDB:3HHW"
FT HELIX 66..77
FT /evidence="ECO:0007829|PDB:3HHW"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:3HHW"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:3HHW"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:3HHW"
FT STRAND 101..104
FT /evidence="ECO:0007829|PDB:3HHW"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:3HHW"
FT HELIX 130..144
FT /evidence="ECO:0007829|PDB:3HHW"
FT HELIX 154..157
FT /evidence="ECO:0007829|PDB:3HHW"
FT TURN 158..160
FT /evidence="ECO:0007829|PDB:3HHW"
FT HELIX 161..166
FT /evidence="ECO:0007829|PDB:3HHW"
FT TURN 175..177
FT /evidence="ECO:0007829|PDB:3HHW"
FT HELIX 178..181
FT /evidence="ECO:0007829|PDB:3HHW"
FT HELIX 183..187
FT /evidence="ECO:0007829|PDB:3HHW"
FT HELIX 189..204
FT /evidence="ECO:0007829|PDB:3HHW"
FT HELIX 211..215
FT /evidence="ECO:0007829|PDB:3HHW"
FT HELIX 218..220
FT /evidence="ECO:0007829|PDB:3HHW"
FT TURN 221..224
FT /evidence="ECO:0007829|PDB:3HHW"
FT HELIX 226..238
FT /evidence="ECO:0007829|PDB:3HHW"
FT HELIX 242..247
FT /evidence="ECO:0007829|PDB:3HHW"
FT HELIX 252..261
FT /evidence="ECO:0007829|PDB:3HHW"
FT STRAND 264..266
FT /evidence="ECO:0007829|PDB:3HHW"
FT HELIX 275..277
FT /evidence="ECO:0007829|PDB:3HHW"
FT TURN 278..282
FT /evidence="ECO:0007829|PDB:3HHW"
FT HELIX 291..293
FT /evidence="ECO:0007829|PDB:3HHW"
FT HELIX 295..307
FT /evidence="ECO:0007829|PDB:3HHW"
FT HELIX 313..315
FT /evidence="ECO:0007829|PDB:3HHW"
FT STRAND 320..322
FT /evidence="ECO:0007829|PDB:3HHW"
FT HELIX 324..340
FT /evidence="ECO:0007829|PDB:3HHW"
FT STRAND 348..351
FT /evidence="ECO:0007829|PDB:3HHZ"
FT STRAND 357..360
FT /evidence="ECO:0007829|PDB:3HHZ"
FT HELIX 375..384
FT /evidence="ECO:0007829|PDB:3HHW"
FT TURN 385..387
FT /evidence="ECO:0007829|PDB:3HHW"
FT HELIX 391..401
FT /evidence="ECO:0007829|PDB:3HHW"
FT STRAND 409..411
FT /evidence="ECO:0007829|PDB:3HHW"
FT HELIX 412..420
FT /evidence="ECO:0007829|PDB:3HHW"
SQ SEQUENCE 422 AA; 47409 MW; 7345C01BAB3C710E CRC64;
MSVTVKRIID NTVIVPKLPA NEDPVEYPAD YFRKSKEIPL YINTTKSLSD LRGYVYQGLK
SGNVSIIHVN SYLYGALKDI RGKLDKDWSS FGINIGKAGD TIGIFDLVSL KALDGVLPDG
VSDASRTSAD DKWLPLYLLG LYRVGRTQMP EYRKKLMDGL TNQCKMINEQ FEPLVPEGRD
IFDVWGNDSN YTKIVAAVDM FFHMFKKHEC ASFRYGTIVS RFKDCAALAT FGHLCKITGM
STEDVTTWIL NREVADEMVQ MMLPGQEIDK ADSYMPYLID FGLSSKSPYS SVKNPAFHFW
GQLTALLLRS TRARNARQPD DIEYTSLTTA GLLYAYAVGS SADLAQQFCV GDNKYTPDDS
TGGLTTNAPP QGRDVVEWLG WFEDQNRKPT PDMMQYAKRA VMSLQGLREK TIGKYAKSEF
DK
