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Q4WHY9 (Q4WHY9_ASPFU) Unreviewed, UniProtKB/TrEMBL

Last modified April 16, 2014. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Protein attributes

Sequence length205 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

PPIases accelerate the folding of proteins By similarity. RuleBase RU000493

PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides By similarity. RuleBase RU004223

Catalytic activity

Peptidylproline (omega=180) = peptidylproline (omega=0). RuleBase RU000493 SAAS SAAS020892

Sequence similarities

Contains PPIase cyclophilin-type domain. SAAS SAAS020892

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data. EMBL EAL87466.1

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region67 – 693Sulfate binding PDB 2C3B

Sequences

Sequence LengthMass (Da)Tools
Q4WHY9 [UniParc].

Last modified July 5, 2005. Version 1.
Checksum: 28B077F443AA78D8

FASTA20522,290
        10         20         30         40         50         60 
MSQVFFDVEY APVGTAETSA RNCAQSGLDA FGLQSILSIL FTDGILLRAV TAKVGRIVFN 

        70         80         90        100        110        120 
LFDKDVPKTA KNFRELCKRP AGEGYRESTF HRIIPNFMIQ GGDFTRGNGT GGRSIYGDKF 

       130        140        150        160        170        180 
ADENFSRKHD KKGILSMANA GPNTNGSQFF ITTAVTSWLD GKHVVFGEVA DEKSYSVVKE 

       190        200 
IEALGSSSGS VRSNTRPKIV NCGEL 

« Hide

References

« Hide 'large scale' references
[1]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.
[2]"The crystal structure of Aspergillus fumigatus cyclophilin reveals 3D domain swapping of a central element."
Limacher A., Kloer D.P., Fluckiger S., Folkers G., Crameri R., Scapozza L.
Structure 14:185-195(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AAHF01000008 Genomic DNA. Translation: EAL87466.1.
RefSeqXP_749504.1. XM_744411.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2C3BX-ray1.85A/B1-205[»]
ProteinModelPortalQ4WHY9.
SMRQ4WHY9. Positions 1-205.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5085.CADAFUAP00003559.

Proteomic databases

PRIDEQ4WHY9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAFUAT00003559; CADAFUAP00003559; CADAFUAG00003559.
GeneID3506781.
KEGGafm:AFUA_2G03720.

Phylogenomic databases

HOGENOMHOG000065981.
KOK01802.
OMAVEYAPVG.
OrthoDBEOG757D7G.

Family and domain databases

InterProIPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view]
PfamPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PIRSFPIRSF001467. Peptidylpro_ismrse. 1 hit.
PRINTSPR00153. CSAPPISMRASE.
PROSITEPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ4WHY9.

Entry information

Entry nameQ4WHY9_ASPFU
AccessionPrimary (citable) accession number: Q4WHY9
Entry history
Integrated into UniProtKB/TrEMBL: July 5, 2005
Last sequence update: July 5, 2005
Last modified: April 16, 2014
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)