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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
 
 
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