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Protein

Capsid protein F

Gene

F

Organism
Enterobacteria phage phiX174 (Isolate Sanger) (Bacteriophage phi-X174)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Assembles to form an icosahedral capsid with a T=1 symmetry, about 30 nm in diameter, and consisting of 60 capsid proteins F.1 Publication

GO - Molecular functioni

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Capsid protein F
Alternative name(s):
F protein
GPF
Gene namesi
Name:F
OrganismiEnterobacteria phage phiX174 (Isolate Sanger) (Bacteriophage phi-X174)
Taxonomic identifieri1217068 [NCBI]
Taxonomic lineageiVirusesssDNA virusesMicroviridaeMicrovirus
Virus hostiEscherichia coli C [TaxID: 498388]
Proteomesi
  • UP000005893 Componenti: Genome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Capsid protein, Host cytoplasm, T=1 icosahedral capsid protein, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved; by host1 Publication
Chaini2 – 427426Capsid protein FPRO_0000164890Add
BLAST

Interactioni

Subunit structurei

Pentamerizes and interacts with H protein, G and B pentamers to form 12S pre-assembly complex. By binding with protein D, induces joining of twelve 12S complex to form the procapsid. Upon genome packaging, interacts with protein J.1 Publication

Protein-protein interaction databases

DIPiDIP-6198N.

Structurei

Secondary structure

1
427
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni6 – 83Combined sources
Beta strandi11 – 144Combined sources
Beta strandi17 – 237Combined sources
Beta strandi25 – 3612Combined sources
Beta strandi41 – 5212Combined sources
Beta strandi55 – 584Combined sources
Beta strandi63 – 7311Combined sources
Helixi74 – 8815Combined sources
Helixi89 – 913Combined sources
Beta strandi97 – 993Combined sources
Turni104 – 1074Combined sources
Helixi108 – 1103Combined sources
Beta strandi119 – 1213Combined sources
Helixi122 – 13514Combined sources
Helixi149 – 1513Combined sources
Helixi154 – 1596Combined sources
Turni169 – 1713Combined sources
Helixi193 – 21119Combined sources
Helixi216 – 2227Combined sources
Turni229 – 2335Combined sources
Beta strandi236 – 24510Combined sources
Beta strandi248 – 2514Combined sources
Turni255 – 2595Combined sources
Beta strandi261 – 2644Combined sources
Beta strandi266 – 27712Combined sources
Beta strandi280 – 29112Combined sources
Beta strandi296 – 2994Combined sources
Helixi302 – 3054Combined sources
Beta strandi306 – 3083Combined sources
Helixi311 – 3144Combined sources
Helixi318 – 3214Combined sources
Beta strandi327 – 3304Combined sources
Helixi331 – 3333Combined sources
Beta strandi343 – 3464Combined sources
Helixi350 – 3523Combined sources
Helixi361 – 3633Combined sources
Helixi380 – 3845Combined sources
Helixi388 – 3947Combined sources
Beta strandi402 – 41514Combined sources
Helixi420 – 4245Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AL0X-ray3.50F2-427[»]
1CD3X-ray3.50F2-427[»]
1KVPelectron microscopy27.00A2-427[»]
1PHXmodel-11-427[»]
2BPAX-ray3.0012-427[»]
ProteinModelPortaliP03641.
SMRiP03641. Positions 2-427.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03641.

Family & Domainsi

Sequence similaritiesi

Belongs to the microviridae F protein family.Curated

Family and domain databases

Gene3Di2.60.169.10. 1 hit.
InterProiIPR016184. Capsid/spike_ssDNA_virus.
IPR003514. Microviridae_protein_F.
[Graphical view]
PfamiPF02305. Phage_F. 1 hit.
[Graphical view]
SUPFAMiSSF88645. SSF88645. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P03641-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNIQTGAER MPHDLSHLGF LAGQIGRLIT ISTTPVIAGD SFEMDAVGAL
60 70 80 90 100
RLSPLRRGLA IDSTVDIFTF YVPHRHVYGE QWIKFMKDGV NATPLPTVNT
110 120 130 140 150
TGYIDHAAFL GTINPDTNKI PKHLFQGYLN IYNNYFKAPW MPDRTEANPN
160 170 180 190 200
ELNQDDARYG FRCCHLKNIW TAPLPPETEL SRQMTTSTTS IDIMGLQAAY
210 220 230 240 250
ANLHTDQERD YFMQRYHDVI SSFGGKTSYD ADNRPLLVMR SNLWASGYDV
260 270 280 290 300
DGTDQTSLGQ FSGRVQQTYK HSVPRFFVPE HGTMFTLALV RFPPTATKEI
310 320 330 340 350
QYLNAKGALT YTDIAGDPVL YGNLPPREIS MKDVFRSGDS SKKFKIAEGQ
360 370 380 390 400
WYRYAPSYVS PAYHLLEGFP FIQEPPSGDL QERVLIRHHD YDQCFQSVQL
410 420
LQWNSQVKFN VTVYRNLPTT RDSIMTS
Length:427
Mass (Da):48,483
Last modified:January 23, 2007 - v2
Checksum:i837DE99C73F426BC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02482 Genomic DNA. Translation: AAA32578.1.
PIRiB93185. ZFBPF4.
RefSeqiNP_040711.1. NC_001422.1.

Genome annotation databases

GeneIDi2546408.
KEGGivg:2546408.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02482 Genomic DNA. Translation: AAA32578.1.
PIRiB93185. ZFBPF4.
RefSeqiNP_040711.1. NC_001422.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AL0X-ray3.50F2-427[»]
1CD3X-ray3.50F2-427[»]
1KVPelectron microscopy27.00A2-427[»]
1PHXmodel-11-427[»]
2BPAX-ray3.0012-427[»]
ProteinModelPortaliP03641.
SMRiP03641. Positions 2-427.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-6198N.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi2546408.
KEGGivg:2546408.

Miscellaneous databases

EvolutionaryTraceiP03641.

Family and domain databases

Gene3Di2.60.169.10. 1 hit.
InterProiIPR016184. Capsid/spike_ssDNA_virus.
IPR003514. Microviridae_protein_F.
[Graphical view]
PfamiPF02305. Phage_F. 1 hit.
[Graphical view]
SUPFAMiSSF88645. SSF88645. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: SEQUENCE REVISION.
  3. "Amino acid sequences from the gene F (capsid) protein of bacteriophage phiX174."
    Air G.M.
    J. Mol. Biol. 107:433-443(1976) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-95.
  4. "Nucleotide sequence of the F protein coding region of bacteriophage phiX174 and the amino acid sequence of its product."
    Air G.M., Coulson A.R., Fiddes J.C., Friedmann T., Hutchison C.A. III, Sanger F., Slocombe P.M., Smith A.J.H.
    J. Mol. Biol. 125:247-254(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 86-427.
  5. "phi X174 genome-capsid interactions influence the biophysical properties of the virion: evidence for a scaffolding-like function for the genome during the final stages of morphogenesis."
    Hafenstein S., Fane B.A.
    J. Virol. 76:5350-5356(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Atomic structure of single-stranded DNA bacteriophage phi X174 and its functional implications."
    McKenna R., Xia D., Williangmann P., Ilag L.L., Krishnaswamy S., Rossmann M.G., Olson N.H., Baker T.S., Incardona N.L.
    Nature 355:137-143(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: CRYSTALLIZATION.
  7. "Analysis of the single-stranded DNA bacteriophage phi X174, refined at a resolution of 3.0 A."
    McKenna R., Ilag L.L., Rossmann M.G.
    J. Mol. Biol. 237:517-543(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
  8. Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS), INTERACTION WITH J PROTEIN.

Entry informationi

Entry nameiCAPSD_BPPHS
AccessioniPrimary (citable) accession number: P03641
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.