VP30_MABVA
ID VP30_MABVA Reviewed; 281 AA.
AC Q1PD56;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Transcriptional activator VP30 {ECO:0000250|UniProtKB:Q05323};
DE AltName: Full=Minor nucleoprotein VP30;
GN Name=VP30;
OS Lake Victoria marburgvirus (strain Angola/2005) (MARV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Filoviridae; Marburgvirus.
OX NCBI_TaxID=378830;
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].
RC STRAIN=Isolate Ang0126, Isolate Ang0214, Isolate Ang0215, Isolate Ang0754,
RC Isolate Ang1379c, Isolate Ang1381, and Isolate Ang1386;
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; DQ447653; ABE27016.1; -; Genomic_RNA.
DR EMBL; DQ447654; ABE27023.1; -; Genomic_RNA.
DR EMBL; DQ447655; ABE27030.1; -; Genomic_RNA.
DR EMBL; DQ447656; ABE27037.1; -; Genomic_RNA.
DR EMBL; DQ447657; ABE27044.1; -; Genomic_RNA.
DR EMBL; DQ447658; ABE27051.1; -; Genomic_RNA.
DR EMBL; DQ447659; ABE27058.1; -; Genomic_RNA.
DR SMR; Q1PD56; -.
DR Proteomes; UP000008242; Genome.
DR Proteomes; UP000097432; Genome.
DR Proteomes; UP000102513; Genome.
DR Proteomes; UP000115353; Genome.
DR Proteomes; UP000130744; Genome.
DR Proteomes; UP000168007; Genome.
DR Proteomes; UP000171838; 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_0000314992"
FT ZN_FING 78..96
FT /note="C3H1-type; atypical"
FT /evidence="ECO:0000250"
FT REGION 1..77
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"
SQ SEQUENCE 281 AA; 31594 MW; 3851A3596877760F CRC64;
MQQPRGRSRT RNHQATPSIY HETQLPSKPH YTNHHPRARS MSSTRSSAES SPTNHIPRAR
PPSTFNLSKP PPPPKDMCRN MKIGLPCTDP TCNRDHDLDN LTNRELLLLM ARKMLPNTDK
TFRSPQDCGS PSLSKGLSKD KQEQTKDVLT LENLGHILSY LHRSEIGKLD ETSLRAALSL
TCAGIRKTNR SLINTMTELH INHENLPQDQ NGVIKQTYTG IHLDKGGQFE AALWQGWDKR
SISLFVQAAL YVMNNIPCES SISVQASYDH FILPQSQGKG Q