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Minor nucleoprotein VP30 (Transcription activator VP30)

 VP30_EBOZM              Reviewed;         288 AA.
Q05323; Q9YMG1;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
30-MAY-2000, sequence version 2.
10-MAY-2017, entry version 83.
RecName: Full=Minor nucleoprotein VP30;
AltName: Full=Transcription activator VP30;
Name=VP30;
Zaire ebolavirus (strain Mayinga-76) (ZEBOV) (Zaire Ebola virus).
Viruses; ssRNA viruses; ssRNA negative-strand viruses;
Mononegavirales; Filoviridae; Ebolavirus.
NCBI_TaxID=128952;
NCBI_TaxID=77231; Epomops franqueti (Franquet's epauleted fruit bat).
NCBI_TaxID=9606; Homo sapiens (Human).
NCBI_TaxID=77243; Myonycteris torquata (Little collared fruit bat).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=8237108; DOI=10.1016/0168-1702(93)90063-S;
Sanchez A., Kiley M.P., Holloway B.P., Auperin D.D.;
"Sequence analysis of the Ebola virus genome: organization, genetic
elements, and comparison with the genome of Marburg virus.";
Virus Res. 29:215-240(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
Wilson J.A., Kondig J.P., Kuehne A.I., Hart M.K.;
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate guinea pig-adapted;
PubMed=11062045; DOI=10.1006/viro.2000.0572;
Volchkov V.E., Chepurnov A.A., Volchkova V.A., Ternovoj V.A.,
Klenk H.D.;
"Molecular characterization of guinea pig-adapted variants of Ebola
virus.";
Virology 277:147-155(2000).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
Ichou M.A., Paragas J., Jahrling P.B., Ibrahim M.S., Lofts L.,
Hevey M., Schmaljohn A.;
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
[5]
PHOSPHORYLATION.
PubMed=12052831; DOI=10.1074/jbc.M203775200;
Modrof J., Muhlberger E., Klenk H.D., Becker S.;
"Phosphorylation of VP30 impairs ebola virus transcription.";
J. Biol. Chem. 277:33099-33104(2002).
[6]
FUNCTION.
PubMed=12163572; DOI=10.1128/JVI.76.17.8532-8539.2002;
Weik M., Modrof J., Klenk H.D., Becker S., Muhlberger E.;
"Ebola virus VP30-mediated transcription is regulated by RNA secondary
structure formation.";
J. Virol. 76:8532-8539(2002).
[7]
INTERACTION WITH THE NUCLEOPROTEIN.
PubMed=12191476; DOI=10.1016/S1097-2765(02)00588-9;
Huang Y., Xu L., Sun Y., Nabel G.J.;
"The assembly of Ebola virus nucleocapsid requires virion-associated
proteins 35 and 24 and posttranslational modification of
nucleoprotein.";
Mol. Cell 10:307-316(2002).
[8]
ZINC-FINGER.
PubMed=12584359; DOI=10.1128/JVI.77.5.3334-3338.2003;
Modrof J., Becker S., Muhlberger E.;
"Ebola virus transcription activator VP30 is a zinc-binding protein.";
J. Virol. 77:3334-3338(2003).
[9]
MUTAGENESIS OF LEU-100 AND LEU-102.
PubMed=12912982; DOI=10.1074/jbc.M307036200;
Hartlieb B., Modrof J., Muhlberger E., Klenk H.D., Becker S.;
"Oligomerization of Ebola virus VP30 is essential for viral
transcription and can be inhibited by a synthetic peptide.";
J. Biol. Chem. 278:41830-41836(2003).
[10]
RNA-BINDING.
PubMed=17567691; DOI=10.1128/JVI.02523-06;
John S.P., Wang T., Steffen S., Longhi S., Schmaljohn C.S.,
Jonsson C.B.;
"Ebola virus VP30 is an RNA binding protein.";
J. Virol. 81:8967-8976(2007).
-!- FUNCTION: Acts as a transcription anti-termination factor
immediately after transcription initiation, but does not affect
transcription elongation. This function has been found to be
dependent on the formation of an RNA stem-loop at the
transcription start site of the first gene. Binds to RNA.
{ECO:0000269|PubMed:12163572}.
-!- SUBUNIT: Homohexamer or homodimer. Interacts with the
nucleoprotein (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Virion. Host cytoplasm.
-!- PTM: Phosphorylated by host. Phosphorylation negatively regulates
the transcription activation. {ECO:0000269|PubMed:12052831}.
-!- SIMILARITY: Belongs to the filoviridae minor nucleoprotein VP30
family. {ECO:0000305}.
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EMBL; L11365; AAB81005.1; -; Genomic_RNA.
EMBL; AF086833; AAD14587.1; -; Genomic_RNA.
EMBL; AF499101; AAM76036.1; -; Genomic_RNA.
EMBL; AY142960; AAN37509.1; -; Genomic_RNA.
EMBL; AF272001; AAG40169.1; -; Genomic_RNA.
RefSeq; NP_066249.1; NC_002549.1.
PDB; 5DVW; X-ray; 1.75 A; A/B/C/D=142-272.
PDB; 5T3T; X-ray; 2.20 A; A/B/C/D/E/F/G/H/I/J=139-288.
PDBsum; 5DVW; -.
PDBsum; 5T3T; -.
DisProt; DP00627; -.
ProteinModelPortal; Q05323; -.
SMR; Q05323; -.
GeneID; 911826; -.
KEGG; vg:911826; -.
OrthoDB; VOG090000JS; -.
Proteomes; UP000007209; Genome.
Proteomes; UP000109874; Genome.
Proteomes; UP000149419; Genome.
Proteomes; UP000150973; Genome.
GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:1990904; C:ribonucleoprotein complex; IMP:CAFA.
GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
GO; GO:0003727; F:single-stranded RNA binding; IMP:CAFA.
GO; GO:0008270; F:zinc ion binding; IDA:CAFA.
GO; GO:0050434; P:positive regulation of viral transcription; IDA:CACAO.
GO; GO:0051260; P:protein homooligomerization; IDA:CAFA.
GO; GO:0044414; P:suppression of host defenses; IMP:CACAO.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR014459; VP30_FiloV.
Pfam; PF11507; Transcript_VP30; 1.
PIRSF; PIRSF011356; VP30_FiloV; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Host cytoplasm; Metal-binding;
Phosphoprotein; Reference proteome; RNA-binding; Transcription;
Viral nucleoprotein; Virion; Zinc; Zinc-finger.
CHAIN 1 288 Minor nucleoprotein VP30.
/FTId=PRO_0000222158.
ZN_FING 72 90 C3H1-type; atypical.
REGION 1 44 Intrinsically disordered. {ECO:0000255}.
REGION 26 40 RNA-binding.
REGION 94 112 Oligomerization. {ECO:0000250}.
REGION 121 140 Intrinsically disordered. {ECO:0000255}.
REGION 180 197 Interaction with the nucleoprotein.
{ECO:0000250}.
REGION 268 288 Intrinsically disordered. {ECO:0000255}.
MUTAGEN 100 100 L->A: Complete loss of homo-
oligomerization.
{ECO:0000269|PubMed:12912982}.
MUTAGEN 102 102 L->A: Complete loss of homo-
oligomerization.
{ECO:0000269|PubMed:12912982}.
CONFLICT 256 288 VVVSGLRTLVPQSDNEEASTNPGTCSWSDEGTP -> ALFQ
G (in Ref. 1; AAB81005). {ECO:0000305}.
HELIX 144 155 {ECO:0000244|PDB:5DVW}.
STRAND 160 162 {ECO:0000244|PDB:5T3T}.
HELIX 164 178 {ECO:0000244|PDB:5DVW}.
HELIX 183 185 {ECO:0000244|PDB:5DVW}.
HELIX 186 196 {ECO:0000244|PDB:5DVW}.
HELIX 201 203 {ECO:0000244|PDB:5DVW}.
HELIX 204 215 {ECO:0000244|PDB:5DVW}.
HELIX 221 229 {ECO:0000244|PDB:5DVW}.
HELIX 232 246 {ECO:0000244|PDB:5DVW}.
HELIX 254 257 {ECO:0000244|PDB:5DVW}.
TURN 258 260 {ECO:0000244|PDB:5DVW}.
HELIX 261 264 {ECO:0000244|PDB:5DVW}.
SEQUENCE 288 AA; 32521 MW; 1FE40E93AB80454B CRC64;
MEASYERGRP RAARQHSRDG HDHHVRARSS SRENYRGEYR QSRSASQVRV PTVFHKKRVE
PLTVPPAPKD ICPTLKKGFL CDSSFCKKDH QLESLTDREL LLLIARKTCG SVEQQLNITA
PKDSRLANPT ADDFQQEEGP KITLLTLIKT AEHWARQDIR TIEDSKLRAL LTLCAVMTRK
FSKSQLSLLC ETHLRREGLG QDQAEPVLEV YQRLHSDKGG SFEAALWQQW DRQSLIMFIT
AFLNIALQLP CESSAVVVSG LRTLVPQSDN EEASTNPGTC SWSDEGTP


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