VP30_MABVM
ID VP30_MABVM Reviewed; 281 AA.
AC P35258; Q38L41; Q6T6T9;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 3.
DT 02-JUN-2021, entry version 89.
DE RecName: Full=Transcriptional activator VP30 {ECO:0000250|UniProtKB:Q05323};
DE AltName: Full=Minor nucleoprotein VP30;
GN Name=VP30;
OS Lake Victoria marburgvirus (strain Musoke-80) (MARV) (Marburg virus (strain
OS Kenya/Musoke/1980)).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Filoviridae; Marburgvirus.
OX NCBI_TaxID=33727;
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 [MRNA].
RC STRAIN=Isolate Feldmann;
RX PubMed=1626422; DOI=10.1016/0168-1702(92)90027-7;
RA Feldmann H., Muehlberger E., Randolf A., Will C., Kiley M.P., Sanchez A.,
RA Klenk H.-D.;
RT "Marburg virus, a filovirus: messenger RNAs, gene order, and regulatory
RT elements of the replication cycle.";
RL Virus Res. 24:1-19(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=pp3/guinea pig lethal, and pp4/guinea pig nonlethal;
RA Chain P.S.G., Malfatti S.A., Hajjaj A., Vergez L.M., Do L.H., Smith K.L.,
RA McCready P.M.;
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=pp3/guinea pig lethal, and pp4/guinea pig nonlethal;
RA Ichou M.A., Paragas J., Jahrling P.B., Ibrahim M.S., Lofts L., Hevey M.,
RA Schmaljohn A.;
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=16379005; DOI=10.1128/jvi.80.2.1038-1043.2006;
RA Enterlein S., Volchkov V., Weik M., Kolesnikova L., Volchkova V.,
RA Klenk H.-D., Muehlberger E.;
RT "Rescue of recombinant Marburg virus from cDNA is dependent on nucleocapsid
RT protein VP30.";
RL J. Virol. 80:1038-1043(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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA78118.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; Z12132; CAA78118.1; ALT_FRAME; mRNA.
DR EMBL; AY430365; AAR85464.1; -; Genomic_RNA.
DR EMBL; AY430366; AAR85457.1; -; Genomic_RNA.
DR EMBL; DQ217792; ABA87128.1; -; Genomic_RNA.
DR RefSeq; YP_001531157.1; NC_001608.3.
DR PDB; 5T3W; X-ray; 3.25 A; A/B/C/D/E/F/G/H=146-281.
DR PDBsum; 5T3W; -.
DR SMR; P35258; -.
DR DNASU; 920942; -.
DR GeneID; 920942; -.
DR KEGG; vg:920942; -.
DR Proteomes; UP000007771; Genome.
DR Proteomes; UP000137266; Genome.
DR Proteomes; UP000160614; Genome.
DR Proteomes; UP000180448; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0019013; C:viral nucleocapsid; IDA:CACAO.
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 1: Evidence at protein level;
KW 3D-structure; Host cytoplasm; Metal-binding; Phosphoprotein;
KW Reference proteome; Transcription; Viral nucleoprotein; Virion; Zinc;
KW Zinc-finger.
FT CHAIN 1..281
FT /note="Transcriptional activator VP30"
FT /id="PRO_0000222159"
FT ZN_FING 78..96
FT /note="C3H1-type; atypical"
FT /evidence="ECO:0000250"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 118..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 124
FT /note="S -> M (in strain: Isolate Feldmann)"
FT HELIX 151..162
FT /evidence="ECO:0007829|PDB:5T3W"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:5T3W"
FT HELIX 171..187
FT /evidence="ECO:0007829|PDB:5T3W"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:5T3W"
FT HELIX 193..204
FT /evidence="ECO:0007829|PDB:5T3W"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:5T3W"
FT HELIX 211..223
FT /evidence="ECO:0007829|PDB:5T3W"
FT HELIX 228..236
FT /evidence="ECO:0007829|PDB:5T3W"
FT HELIX 239..253
FT /evidence="ECO:0007829|PDB:5T3W"
FT HELIX 262..272
FT /evidence="ECO:0007829|PDB:5T3W"
SQ SEQUENCE 281 AA; 31650 MW; 464167106F87D145 CRC64;
MQQPRGRSRT RNHQVTPTIY HETQLPSKPH YTNYHPRARS MSSTRSSAES SPTNHIPRAR
PPSTFNLSKP PPPPKDMCRN MKIGLPCADP TCNRDHDLDN LTNRELLLLM ARKMLPNTDK
TFRSPQDCGS PSLSKGLSKD KQEQTKDVLT LENLGHILSY LHRSEIGKLD ETSLRAALSL
TCAGIRKTNR SLINTMTELH MNHENLPQDQ NGVIKQTYTG IHLDKGGQFE AALWQGWDKR
SISLFVQAAL YVMNNIPCES SISVQASYDH FILPQSQGKG Q
