P69486 (D_BPPHS) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 51.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: External scaffolding protein D Short name=GPD | ||
| Gene names |
| ||
| Organism | Enterobacteria phage phiX174 (Isolate Sanger) (Bacteriophage phi-X174) [Complete proteome] | ||
| Taxonomic identifier | 1217068 [NCBI] | ||
| Taxonomic lineage | Viruses › ssDNA viruses › Microviridae › Microvirus › ![]() | ||
| Virus host | Escherichia coli C [TaxID: 498388] |
Protein attributes
| Sequence length | 152 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence 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 | |
| Sequence similarities | Belongs to the microvirus D protein family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Host cytoplasm |
| Molecular function | Viral capsid scaffolding protein |
| Technical term | 3D-structure Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | viral procapsid maturation Inferred from electronic annotation. Source: InterPro |
| Cellular_component | host cell cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||||||||||
Molecule processing | ||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed; by host | |||||||||||||||||||||||||||
| Chain | 2 – 152 | 151 | External scaffolding protein D | PRO_0000164880 | ||||||||||||||||||||||||||
Experimental info | ||||||||||||||||||||||||||||||
| Mutagenesis | 61 | 1 | G → D: Confers a lethal phenotype. Ref.5 | |||||||||||||||||||||||||||
| Mutagenesis | 61 | 1 | G → E: Confers a lethal phenotype. Ref.5 | |||||||||||||||||||||||||||
| Mutagenesis | 61 | 1 | G → V: Confers a lethal phenotype. Ref.5 | |||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||
| Helix | 5 – 23 | 19 | ||||||||||||||||||||||||||||
| Helix | 31 – 38 | 8 | ||||||||||||||||||||||||||||
| Beta strand | 39 – 41 | 3 | ||||||||||||||||||||||||||||
| Helix | 45 – 47 | 3 | ||||||||||||||||||||||||||||
| Helix | 48 – 59 | 12 | ||||||||||||||||||||||||||||
| Helix | 61 – 65 | 5 | ||||||||||||||||||||||||||||
| Helix | 75 – 85 | 11 | ||||||||||||||||||||||||||||
| Helix | 88 – 97 | 10 | ||||||||||||||||||||||||||||
| Turn | 98 – 100 | 3 | ||||||||||||||||||||||||||||
| Helix | 104 – 109 | 6 | ||||||||||||||||||||||||||||
| Helix | 117 – 129 | 13 | ||||||||||||||||||||||||||||
| Helix | 140 – 143 | 4 | ||||||||||||||||||||||||||||
Sequences
| ||||||||||||||||||
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. | ||||||||||||||||||||||||
| PIR | ZDBPF4. A04245. | ||||||||||||||||||||||||
3D structure databases | |||||||||||||||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||||||||||||||
| ProteinModelPortal | P69486. | ||||||||||||||||||||||||
| SMR | P69486. Positions 7-152. | ||||||||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||||||||
Protocols and materials databases | |||||||||||||||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||||||||
| ProtClustDB | PHA0006. | ||||||||||||||||||||||||
Family and domain databases | |||||||||||||||||||||||||
| Gene3D | 1.10.1850.10. 1 hit. | ||||||||||||||||||||||||
| InterPro | IPR004196. Scaffold_D_phage. [Graphical view] | ||||||||||||||||||||||||
| Pfam | PF02925. gpD. 1 hit. [Graphical view] | ||||||||||||||||||||||||
| ProDom | PD016331. Bact_scaffold_pD. 1 hit. [Graphical view] [Entries sharing at least one domain] | ||||||||||||||||||||||||
| SUPFAM | SSF48045. Bact_scaffold_pD. 1 hit. | ||||||||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||||||||
Other | |||||||||||||||||||||||||
| EvolutionaryTrace | P69486. | ||||||||||||||||||||||||
Entry information
| Entry name | D_BPPHS | ||||||||
| Accession | Primary (citable) accession number: P69486 Secondary accession number(s): P03637 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Viral Protein Annotation Program | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
