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P69486 (D_BPPHS) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
External scaffolding protein D

Short name=GPD
Gene names
Name:D
OrganismEnterobacteria phage phiX174 (Isolate Sanger) (Bacteriophage phi-X174) [Complete proteome]
Taxonomic identifier1217068 [NCBI]
Taxonomic lineageVirusesssDNA virusesMicroviridaeMicrovirus
Virus hostEscherichia coli C [TaxID: 498388]

Protein attributes

Sequence length152 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Assembles the procapsid by joining twelve 12S pre-assembly complex into a T=1 icosahedral particle, called 108S procapsid. Ten proteins D bind each 12S complex, which are formed by three pentamers of F, G, B protein and a H protein. The scaffolding protein is released from the provirion after genome packaging to form the mature virion. Ref.4 Ref.6

Subunit structure

Component of the procapsid particle composed of 60 copies of the internally located B, 240 copies of the external scaffolding protein D, 60 copies of each of the viral structural proteins F and G, and 12 copies of protein H.

Subcellular location

Host cytoplasm.

Sequence similarities

Belongs to the microvirus D protein family.

Ontologies

Keywords
   Cellular componentHost cytoplasm
   Molecular functionViral capsid scaffolding protein
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological_processviral procapsid maturation

Inferred from electronic annotation. Source: InterPro

   Cellular_componenthost cell cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed; by host
Chain2 – 152151External scaffolding protein D
PRO_0000164880

Experimental info

Mutagenesis611G → D: Confers a lethal phenotype. Ref.5
Mutagenesis611G → E: Confers a lethal phenotype. Ref.5
Mutagenesis611G → V: Confers a lethal phenotype. Ref.5

Secondary structure

...................... 152
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P69486 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: E8C912DCBA48D5E4

FASTA15216,937
        10         20         30         40         50         60 
MSQVTEQSVR FQTALASIKL IQASAVLDLT EDDFDFLTSN KVWIATDRSR ARRCVEACVY 

        70         80         90        100        110        120 
GTLDFVGYPR FPAPVEFIAA VIAYYVHPVN IQTACLIMEG AEFTENIING VERPVKAAEL 

       130        140        150 
FAFTLRVRAG NTDVLTDAEE NVRQKLRAEG VM 

« Hide

References

[1]"Nucleotide sequence of bacteriophage phi X174 DNA."
Sanger F., Air G.M., Barrell B.G., Brown N.L., Coulson A.R., Fiddes J.C., Hutchison C.A. III, Slocombe P.M., Smith M.
Nature 265:687-695(1977) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Overlapping genes in bacteriophage phiX174."
Barrell B.G., Air G.M., Hutchison C.A. III
Nature 264:34-41(1976) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Role of premature translational termination in the regulation of expression of the phi X174 lysis gene."
Buckley K.J., Hayashi M.
J. Mol. Biol. 198:599-607(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-68.
[4]"Isolation and identification of bacteriophage phi X174 prohead."
Mukai R., Hamatake R.K., Hayashi M.
Proc. Natl. Acad. Sci. U.S.A. 76:4877-4881(1979) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PROCAPSID STRUCTURE.
[5]"Genetic analyses of putative conformation switching and cross-species inhibitory domains in Microviridae external scaffolding proteins."
Burch A.D., Fane B.A.
Virology 310:64-71(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF GLY-61.
[6]"Identification of an interacting coat-external scaffolding protein domain required for both the initiation of phiX174 procapsid morphogenesis and the completion of DNA packaging."
Uchiyama A., Fane B.A.
J. Virol. 79:6751-6756(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"Structure of a viral procapsid with molecular scaffolding."
Dokland T., McKenna R., Ilag L.L., Bowman B.R., Incardona N.L., Fane B.A., Rossmann M.G.
Nature 389:308-313(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J02482 Genomic DNA. Translation: AAA32575.1.
X07809 Genomic DNA. Translation: CAA30667.1.
PIRZDBPF4. A04245.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AL0X-ray3.501/2/3/41-152[»]
1CD3X-ray3.501/2/3/41-151[»]
1TX9X-ray3.31A/B2-152[»]
ProteinModelPortalP69486.
SMRP69486. Positions 7-152.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

ProtClustDBPHA0006.

Family and domain databases

Gene3D1.10.1850.10. 1 hit.
InterProIPR004196. Scaffold_D_phage.
[Graphical view]
PfamPF02925. gpD. 1 hit.
[Graphical view]
ProDomPD016331. Bact_scaffold_pD. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF48045. Bact_scaffold_pD. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP69486.

Entry information

Entry nameD_BPPHS
AccessionPrimary (citable) accession number: P69486
Secondary accession number(s): P03637
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: May 1, 2013
This is version 51 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families