VP30_MABVO
ID VP30_MABVO Reviewed; 281 AA.
AC Q6UY65;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Transcriptional activator VP30 {ECO:0000250|UniProtKB:Q05323};
DE AltName: Full=Minor nucleoprotein VP30;
GN Name=VP30;
OS Lake Victoria marburgvirus (strain Ozolin-75) (MARV) (Marburg virus (strain
OS South Africa/Ozolin/1975)).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Filoviridae; Marburgvirus.
OX NCBI_TaxID=482820;
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].
RA Bowen M.D., Thurman K., Minor E., Ibrahim M.S., Meyer R.F., Malfatti S.A.,
RA Do L.H., Smith K.L., McCready P.M., Chain P.S.G.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
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; AY358025; AAQ55259.1; -; Genomic_RNA.
DR SMR; Q6UY65; -.
DR Proteomes; UP000000838; 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_0000314993"
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 120..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 123..138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 281 AA; 31626 MW; EEA9A93FE500566F CRC64;
MQQPRGRSRT RNHQAIPSIY HETQLPSKPN YTNHHPRARS MSSTRSSTES SPTNHIPRAR
PPSTFNLSKP PPPPKDMCRN MKIGLPCTDL TCNRDHDLDN LTNRELLLLM ARKMLPNTDK
VFKSPQDCGS PSLSKGLSKD KQEQTKDVLT LENLGHILNY LHRSEIGKLD ETSLRAALSL
TCAGIRKTNR SLINTMTELH INHENLPQDQ NGVIKQTYTG IHLDKGGQFE AALWQGWDKR
SISLFVQAAL YVMNNIPCES SISVQASYDH FILPQSQGKG Q