ID   VP30_MABVR              Reviewed;         281 AA.
AC   Q1PDC6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Transcriptional activator VP30 {ECO:0000250|UniProtKB:Q05323};
DE   AltName: Full=Minor nucleoprotein VP30;
GN   Name=VP30;
OS   Lake Victoria marburgvirus (strain Ravn-87) (MARV) (Marburg virus (strain
OS   Kenya/Ravn/1987)).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Filoviridae; Marburgvirus.
OX   NCBI_TaxID=378809;
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].
RX   PubMed=16775337; DOI=10.1128/jvi.00069-06;
RA   Towner J.S., Khristova M.L., Sealy T.K., Vincent M.J., Erickson B.R.,
RA   Bawiec D.A., Hartman A.L., Comer J.A., Zaki S.R., Stroeher U.,
RA   Gomes da Silva F., del Castillo F., Rollin P.E., Ksiazek T.G., Nichol S.T.;
RT   "Marburgvirus genomics and association with a large hemorrhagic fever
RT   outbreak in Angola.";
RL   J. Virol. 80:6497-6516(2006).
CC   -!- FUNCTION: Acts as a transcription anti-termination factor immediately
CC       after transcription initiation, but does not affect transcription
CC       elongation. This function has been found to be dependent on the
CC       formation of an RNA secondary structure at the transcription start site
CC       of the first gene (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homooligomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion. Host cytoplasm {ECO:0000250}.
CC       Note=Tightly bound in the nucleocapsid.
CC   -!- PTM: Phosphorylated by host. Phosphorylation negatively regulates the
CC       transcription activation (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the filoviridae transcriptional activator VP30
CC       family. {ECO:0000305}.
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DR   EMBL; DQ447649; ABE27072.1; -; Genomic_RNA.
DR   SMR; Q1PDC6; -.
DR   Proteomes; UP000008239; 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:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR014459; VP30_FiloV.
DR   Pfam; PF11507; Transcript_VP30; 1.
DR   PIRSF; PIRSF011356; VP30_FiloV; 1.
PE   3: Inferred from homology;
KW   Host cytoplasm; Metal-binding; Phosphoprotein; Reference proteome;
KW   Transcription; Viral nucleoprotein; Virion; Zinc; Zinc-finger.
FT   CHAIN           1..281
FT                   /note="Transcriptional activator VP30"
FT                   /id="PRO_0000314994"
FT   ZN_FING         78..96
FT                   /note="C3H1-type; atypical"
FT                   /evidence="ECO:0000250"
FT   REGION          1..74
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          120..141
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..64
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        120..138
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   281 AA;  31629 MW;  E486B1EBA40F6643 CRC64;
     MQQPRGRSRN RSHQVALSTY HENQLPSKPQ YINHHPRARS MSSTRSSTEG SPTNHASRAR
     PLSTFNLSKP PPPPKDMCRN MKIGLPCTDP ACNRDHDLDN LTNRELLLLM ARKMLPNTDK
     AFKSQQDCGS PSLSKGLSKD KQEQAKDVLT LENLGHILNY LHRSEIGKLD ETSLRAALSL
     TCAGIRKTNR SLINTMTELH INHENLPQDQ NGVIKQTYTG IHLDKGGQFE AALWQGWDKK
     SISLFVQAAL YVMNNIPCES SISVQASYDH FILPRNQGER Q