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P35259 (VP35_MABVM) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 50. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Protein attributes

Sequence length329 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts as a polymerase cofactor in the RNA polymerase transcription and replication complex.

Subunit structure

Homooligomer. Homomultimerization via the coiled coil domain is a prerequisite for binding to L. Found in a trimeric complex in which VP35 bridges L and the nucleoprotein. Ref.5

Subcellular location

Virion. Host cytoplasm By similarity.

Sequence similarities

Belongs to the filoviridae polymerase cofactor VP35 family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 329329Polymerase cofactor VP35
PRO_0000222162

Regions

Coiled coil70 – 12051 Potential

Natural variations

Natural variant311E → K in strain: pp3/guinea pig lethal and pp4/guinea pig nonlethal.
Natural variant2961S → C in strain: pp3/guinea pig lethal, pp4/guinea pig nonlethal and Isolate Enterlein.

Experimental info

Mutagenesis901L → A: Complete loss of homo-oligomerization; when associated with A-104. Ref.5
Mutagenesis1041L → A: Complete loss of homo-oligomerization; when associated with A-90. Ref.5

Secondary structure

......................... 329
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P35259 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: 300EDE165A40938E

FASTA32936,143
        10         20         30         40         50         60 
MWDSSYMQQV SEGLMTGKVP IDQVFGANPL EKLYKRRKPK GTVGLQCSPC LMSKATSTDD 

        70         80         90        100        110        120 
IIWDQLIVKR TLADLLIPIN RQISDIQSTL SEVTTRVHEI ERQLHEITPV LKMGRTLEAI 

       130        140        150        160        170        180 
SKGMSEMLAK YDHLVISTGR TTAPAAAFDA YLNEHGVPPP QPAIFKDLGV AQQACSKGTM 

       190        200        210        220        230        240 
VKNATTDAAD KMSKVLELSE ETFSKPNLSA KDLALLLFTH LPGNNTPFHI LAQVLSKIAY 

       250        260        270        280        290        300 
KSGKSGAFLD AFHQILSEGE NAQAALTRLS RTFDAFLGVV PPVIRVKNFQ TVPRPSQKSL 

       310        320 
RAVPPNPTID KGWVCVYSSE QGETRALKI 

« Hide

References

[1]"Marburg virus, a filovirus: messenger RNAs, gene order, and regulatory elements of the replication cycle."
Feldmann H., Muehlberger E., Randolf A., Will C., Kiley M.P., Sanchez A., Klenk H.-D.
Virus Res. 24:1-19(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]Chain P.S.G., Malfatti S.A., Hajjaj A., Vergez L.M., Do L.H., Smith K.L., McCready P.M.
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
Strain: pp3/guinea pig lethal and pp4/guinea pig nonlethal.
[3]Ichou M.A., Paragas J., Jahrling P.B., Ibrahim M.S., Lofts L., Hevey M., Schmaljohn A.
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
Strain: pp3/guinea pig lethal and pp4/guinea pig nonlethal.
[4]"Rescue of recombinant Marburg virus from cDNA is dependent on nucleocapsid protein VP30."
Enterlein S., Volchkov V., Weik M., Kolesnikova L., Volchkova V., Klenk H.-D., Muehlberger E.
J. Virol. 80:1038-1043(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
Strain: Isolate Enterlein.
[5]"Homo-oligomerization of Marburgvirus VP35 is essential for its function in replication and transcription."
Moeller P., Pariente N., Klenk H.-D., Becker S.
J. Virol. 79:14876-14886(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, COILED-COIL DOMAIN, MUTAGENESIS OF LEU-90 AND LEU-104.
[6]"Nucleocapsid formation and RNA synthesis of Marburg virus is dependent on two coiled coil motifs in the nucleoprotein."
Dicarlo A., Moeller P., Lander A., Kolesnikova L., Becker S.
Virol. J. 4:105-105(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH THE NUCLEOPROTEIN, COILED-COIL DOMAIN.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z12132 mRNA. Translation: CAA78115.1.
AY430365 Genomic RNA. Translation: AAR85461.1.
AY430366 Genomic RNA. Translation: AAR85454.1.
DQ217792 Genomic RNA. Translation: ABA87125.1.
RefSeqYP_001531154.1. NC_001608.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4GH9X-ray1.65A204-329[»]
4GHAX-ray2.50A/C/E/G204-329[»]
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-60094N.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID920948.

Family and domain databases

InterProIPR002953. Filo_VP35.
[Graphical view]
PfamPF02097. Filo_VP35. 1 hit.
[Graphical view]
PIRSFPIRSF018326. VP35_FiloV. 1 hit.
PRINTSPR01240. FILOVP35.
ProtoNetSearch...

Entry information

Entry nameVP35_MABVM
AccessionPrimary (citable) accession number: P35259
Secondary accession number(s): Q38L44, Q6T6U2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: February 19, 2014
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references