Skip Header

 
Contribute Send feedback

Reviewed, UniProtKB/Swiss-Prot O43099 (PMP20_ASPFU)

Last modified November 25, 2008. Version 44. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Putative peroxiredoxin pmp20
    EC=1.11.1.15
Alternative name(s):
    Thioredoxin reductase
    Peroxisomal membrane protein pmp20
    Allergen=Asp f 3
Gene names
Name: pmp20
ORF Names: AFUA_6G02280
OrganismAspergillus fumigatus (Sartorya fumigata) [Complete proteome]
Taxonomic identifier5085 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesTrichocomaceaemitosporic TrichocomaceaeAspergillus

Protein attributes

Sequence length168 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH.

Subcellular location

PeroxisomePotential.

Allergenic properties

Causes an allergic reaction in human. Shares common IgE-binding epitopes with allergen Cand b 2 of Candida boidinii.

Sequence similarities

Belongs to the peroxiredoxin 2 family.

Contains 1 thioredoxin domain.

Ontologies

Keywords

   Cellular componentPeroxisome
   DiseaseAllergen
   DomainRedox-active center
   Molecular functionOxidoreductase
Peroxidase
   Technical termComplete proteome

Gene Ontology (GO)

   Biological processcell redox homeostasis

Inferred from electronic annotation. Source: InterPro

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentperoxisome

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionperoxiredoxin activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 168168Putative peroxiredoxin pmp20
PRO_0000056603

Regions

Domain4 – 158155Thioredoxin

Sequences

Sequence LengthMass (Da)Tools
O43099-1 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: AFFCD72C5A1CCBB2

FASTA16818,453
        10         20         30         40         50         60 
MSGLKAGDSF PSDVVFSYIP WSEDKGEITA CGIPINYNAS KEWADKKVIL FALPGAFTPV 

        70         80         90        100        110        120 
CSARHVPEYI EKLPEIRAKG VDVVAVLAYN DAYVMSAWGK ANQVTGDDIL FLSDPDARFS 

       130        140        150        160 
KSIGWADEEG RTKRYALVID HGKITYAALE PAKNHLEFSS AETVLKHL 

« Hide

References

« Hide 'large scale' references
[1]"Allergens of Aspergillus fumigatus and Candida boidinii share IgE-binding epitopes."
Hemmann S., Blaser K., Crameri R.
Am. J. Respir. Crit. Care Med. 156:1956-1962(1997) [PubMed: 9412580] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: ATCC 42202 / AF-102 / Ag 507.
[2]"Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus."
Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L. expand/collapse author list , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W.
Nature 438:1151-1156(2005) [PubMed: 16372009] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Af293 / CBS 101355 / FGSC A1100.

Cross-references

Sequence databases

U58050 mRNA. Translation: AAB95638.1.
AAHF01000012 Genomic DNA. Translation: EAL85811.1.
RefSeqXP_747849.1.

3D structure databases

HSSPHSSP built from PDB template 1HD2 based on UniProtKB P30044.
ModBaseSearch...

Genome annotation databases

GeneID3505266.
KEGGafm:AFUA_6G02280.

Phylogenomic databases

HOGENOMO43099.

Family and domain databases

InterProIPR013740. Redoxin.
IPR012335. Thioredoxin_fold.
[Graphical view]
Gene3DG3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
PfamPF08534. Redoxin. 1 hit.
[Graphical view]
PROSITEPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePMP20_ASPFU
AccessionPrimary (citable) accession number: O43099
Secondary accession number(s): Q4WCS7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: June 1, 1998
Last modified: November 25, 2008
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

Allergens

Nomenclature of allergens and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents