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UniProtKB/Swiss-Prot entry O43099


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PMP20_ASPFU
Primary accession number O43099
Secondary accession number Q4WCS7
Integrated into Swiss-Prot on December 15, 1998
Sequence was last modified on June 1, 1998 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 44)
Name and origin of the protein
Protein name Putative peroxiredoxin pmp20
Synonyms EC 1.11.1.15
Thioredoxin reductase
Peroxisomal membrane protein pmp20
Allergen Asp f 3
Gene name
Name: pmp20
ORFNames: AFUA_6G02280
From
Aspergillus fumigatus (Sartorya fumigata) [TaxID: 5085] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; Eurotiomycetidae; Eurotiales; Trichocomaceae; mitosporic Trichocomaceae; Aspergillus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=ATCC 42202 / AF-102 / Ag 507;
PubMed=9412580 [NCBI, ExPASy, EBI, Israel, Japan]
Hemmann S., Blaser K., Crameri R.;
"Allergens of Aspergillus fumigatus and Candida boidinii share IgE-binding epitopes.";
Am. J. Respir. Crit. Care Med. 156:1956-1962(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Af293 / CBS 101355 / FGSC A1100;
DOI=10.1038/nature04332; PubMed=16372009 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus.";
Nature 438:1151-1156(2005).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U58050; AAB95638.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AAHF01000012; EAL85811.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq XP_747849.1; -.
3D structure databases
HSSP P30044; 1HD2. [HSSP ENTRY / PDB]
ModBase O43099.
Ontologies
GO
GO:0005777; Cellular component: peroxisome (inferred from electronic annotation from UniProtKB-KW).
GO:0051920; Molecular function: peroxiredoxin activity (inferred from electronic annotation from EC).
GO:0045454; Biological process: cell redox homeostasis (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR013740; Redoxin.
IPR012335; Thioredoxin_fold.
Graphical view of domain structure.
Gene3D G3DSA:3.40.30.10; Thioredoxin_fold; 1.
Pfam PF08534; Redoxin; 1.
Pfam graphical view of domain structure.
PROSITE PS51352; THIOREDOXIN_2; 1.
PROSITE graphical view of domain structure (profiles).
Genome annotation databases
GeneID 3505266; -.
KEGG afm:AFUA_6G02280; -.
Phylogenomic databases
HOGENOM O43099; -.
Other
ProtoNet O43099.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Allergen; Complete proteome; Oxidoreductase; Peroxidase; Peroxisome; Redox-active center.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom To Length Description FTId
CHAIN   1   168  168     Putative peroxiredoxin pmp20. PRO_0000056603
DOMAIN   4   158  155     Thioredoxin. 
Sequence information
Length: 168 AA [This is the length of the unprocessed precursor] Molecular weight: 18453 Da [This is the MW of the unprocessed precursor] CRC64: AFFCD72C5A1CCBB2 [This is a checksum on the sequence]
        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 

O43099 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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BLAST logo BLAST submission on ExPASy/SIB
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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NPSA logo NPSA Sequence analysis tools

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