ID   VP30_EBORE              Reviewed;         287 AA.
AC   Q91DD6;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   RecName: Full=Transcriptional activator VP30 {ECO:0000250|UniProtKB:Q05323};
DE   AltName: Full=EbolaVP30 {ECO:0000250|UniProtKB:Q05323};
DE            Short=eVP30 {ECO:0000250|UniProtKB:Q05323};
DE   AltName: Full=Minor nucleoprotein VP30;
GN   Name=VP30;
OS   Reston ebolavirus (strain Philippines-96) (REBOV) (Reston Ebola virus).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Filoviridae; Orthoebolavirus;
OC   Orthoebolavirus restonense; Reston ebolavirus.
OX   NCBI_TaxID=129003;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=9541; Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OH   NCBI_TaxID=77225; Pteropodinae.
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=11722021; DOI=10.1007/s007050170049;
RA   Ikegami T., Calaor A.B., Miranda M.E., Niikura M., Saijo M., Kurane I.,
RA   Yoshikawa Y., Morikawa S.;
RT   "Genome structure of Ebola virus subtype Reston: differences among Ebola
RT   subtypes.";
RL   Arch. Virol. 146:2021-2027(2001).
CC   -!- FUNCTION: Multifunctional protein that acts as a viral transcriptional
CC       activator. Promotes read-through of an RNA hairpin in the NP open
CC       reading frame to enhance viral transcription. Mechanistically,
CC       nonphosphorylated VP30 hexamers form a ternary complex with the viral
CC       leader RNA. Clamps the RNA template and the complex VP35-polymerase L
CC       together, thereby increasing the polymerase affinity for the RNA
CC       template to increase transcription initiation despite the presence of
CC       RNA secondary structures. Assists also stop-start transcription at gene
CC       junctions to promote transcription of downstream genes. Interaction
CC       with NP plays a critical role in transcription initiation by
CC       recognizing the RNA stem loop (By similarity). Interaction with host
CC       RBBP6 interferes with NP-VP30 interaction and inhibits viral RNA
CC       synthesis. Also acts as a suppressor of RNA silencing by interacting
CC       with host DICER1 and TARBP2/TRBP (By similarity).
CC       {ECO:0000250|UniProtKB:Q05323, ECO:0000250|UniProtKB:Q77DJ5}.
CC   -!- SUBUNIT: Homohexamer; hexamerization is essential for RNA binding.
CC       Interacts with the nucleoprotein/NP; this interaction plays both
CC       essential and inhibitory roles in viral RNA synthesis. Interacts with
CC       VP35. Interacts with host STAU1 (By similarity). Interacts (via C-
CC       terminus) with host RBBP6 isoform 1 (By similarity). Interacts with
CC       host DICER1; this interaction prevents TARBP2/TRBP binding to DICER1
CC       and thus allows the virus to counteract host RNA silencing (By
CC       similarity). Interacts with host TARBP2/TRBP; this interaction, which
CC       occurs only in the presence of siRNA, prevents TARBP2 binding to DICER1
CC       and thus allows the virus to counteract host RNA silencing (By
CC       similarity). {ECO:0000250|UniProtKB:Q05323,
CC       ECO:0000250|UniProtKB:Q77DJ5}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:Q05323}. Host
CC       cytoplasm {ECO:0000250|UniProtKB:Q05323}. Note=Present in viral
CC       inclusion bodies due to its interaction with NP.
CC       {ECO:0000250|UniProtKB:Q05323}.
CC   -!- PTM: Phosphorylated by host. Phosphorylation negatively regulates the
CC       transcription activation. Phosphorylation and dephosphorylation take
CC       place in viral inclusion bodies and are largely influenced by the
CC       presence of NP. Dephosphorylated by host PPP2R5C; this
CC       dephosphorylation enhances viral transcription and is mediated by NP.
CC       {ECO:0000250|UniProtKB:Q05323}.
CC   -!- SIMILARITY: Belongs to the filoviridae transcriptional activator VP30
CC       family. {ECO:0000305}.
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DR   EMBL; AB050936; BAB69008.1; -; Genomic_RNA.
DR   SMR; Q91DD6; -.
DR   Proteomes; UP000002322; Genome.
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:0008270; F:zinc ion binding; IEA:InterPro.
DR   Gene3D; 1.20.120.1160; -; 1.
DR   InterPro; IPR014459; VP30_FiloV.
DR   Pfam; PF11507; Transcript_VP30; 1.
DR   PIRSF; PIRSF011356; VP30_FiloV; 1.
PE   3: Inferred from homology;
KW   Activator; Host cytoplasm; Host-virus interaction;
KW   Inhibition of host innate immune response by virus; Metal-binding;
KW   Phosphoprotein; RNA-binding; Suppressor of RNA silencing; Transcription;
KW   Viral immunoevasion; Viral nucleoprotein; Virion; Zinc; Zinc-finger.
FT   CHAIN           1..287
FT                   /note="Transcriptional activator VP30"
FT                   /id="PRO_0000245071"
FT   ZN_FING         72..90
FT                   /note="C3H1-type; atypical"
FT   REGION          1..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          26..40
FT                   /note="RNA-binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q05323"
FT   REGION          94..112
FT                   /note="Oligomerization"
FT                   /evidence="ECO:0000250"
FT   REGION          180..197
FT                   /note="Interaction with the nucleoprotein"
FT                   /evidence="ECO:0000250"
FT   REGION          268..287
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..39
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   287 AA;  32389 MW;  F4CFBDA604A77920 CRC64;
     MEHSRERGRS SNMRHNSREP YENPSRSRSL SRDPNQVDRR QPRSASQIRV PNLFHRKKTD
     ALIVPPAPKD ICPTLKKGFL CDSKFCKKDH QLDSLNDHEL LLLIARRTCG IIESNSQITS
     PKDMRLANPT AEDFSQGNSP KLTLAVLLQI AEHWATRDLR QIEDSKLRAL LTLCAVLTRK
     FSKSQLGLLC ETHLRHEGLG QDQADSVLEV YQRLHSDKGG NFEAALWQQW DRQSLIMFIS
     AFLNIALQTP CESSSVVVSG LATLYPAQDN STPSEATNDT TWSSTVE
//