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Q4WHY9

- Q4WHY9_ASPFU

UniProt

Q4WHY9 - Q4WHY9_ASPFU

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Protein

Peptidyl-prolyl cis-trans isomerase

Gene

AFUA_2G03720

Organism
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Status
Unreviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli

Functioni

PPIases accelerate the folding of proteins.UniRule annotation
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.UniRule annotation

Catalytic activityi

Peptidylproline (omega=180) = peptidylproline (omega=0).SAAS annotation

GO - Molecular functioni

  1. peptidyl-prolyl cis-trans isomerase activity Source: UniProtKB-KW

GO - Biological processi

  1. protein folding Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, RotamaseUniRule annotationSAAS annotation

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-prolyl cis-trans isomeraseUniRule annotation (EC:5.2.1.8UniRule annotation)
Gene namesi
ORF Names:AFUA_2G03720Imported
OrganismiNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)Imported
Taxonomic identifieri330879 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000002530: Chromosome 2

PTM / Processingi

Proteomic databases

PRIDEiQ4WHY9.

Interactioni

Protein-protein interaction databases

STRINGi5085.CADAFUAP00003559.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2C3BX-ray1.85A/B1-205[»]
ProteinModelPortaliQ4WHY9.
SMRiQ4WHY9. Positions 1-205.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ4WHY9.

Family & Domainsi

Sequence similaritiesi

Belongs to the cyclophilin-type PPIase family.UniRule annotation
Contains 1 PPIase cyclophilin-type domain.UniRule annotation
Contains PPIase cyclophilin-type domain.SAAS annotation

Phylogenomic databases

HOGENOMiHOG000065981.
InParanoidiQ4WHY9.
KOiK01802.
OMAiVFFDVEY.
OrthoDBiEOG757D7G.

Family and domain databases

Gene3Di2.40.100.10. 1 hit.
InterProiIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view]
PfamiPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PIRSFiPIRSF001467. Peptidylpro_ismrse. 1 hit.
PRINTSiPR00153. CSAPPISMRASE.
SUPFAMiSSF50891. SSF50891. 1 hit.
PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q4WHY9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSQVFFDVEY APVGTAETSA RNCAQSGLDA FGLQSILSIL FTDGILLRAV
60 70 80 90 100
TAKVGRIVFN LFDKDVPKTA KNFRELCKRP AGEGYRESTF HRIIPNFMIQ
110 120 130 140 150
GGDFTRGNGT GGRSIYGDKF ADENFSRKHD KKGILSMANA GPNTNGSQFF
160 170 180 190 200
ITTAVTSWLD GKHVVFGEVA DEKSYSVVKE IEALGSSSGS VRSNTRPKIV

NCGEL
Length:205
Mass (Da):22,290
Last modified:July 5, 2005 - v1
Checksum:i28B077F443AA78D8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAHF01000008 Genomic DNA. Translation: EAL87466.1.
RefSeqiXP_749504.1. XM_744411.1.

Genome annotation databases

EnsemblFungiiCADAFUAT00003559; CADAFUAP00003559; CADAFUAG00003559.
GeneIDi3506781.
KEGGiafm:AFUA_2G03720.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAHF01000008 Genomic DNA. Translation: EAL87466.1 .
RefSeqi XP_749504.1. XM_744411.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2C3B X-ray 1.85 A/B 1-205 [» ]
ProteinModelPortali Q4WHY9.
SMRi Q4WHY9. Positions 1-205.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 5085.CADAFUAP00003559.

Proteomic databases

PRIDEi Q4WHY9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADAFUAT00003559 ; CADAFUAP00003559 ; CADAFUAG00003559 .
GeneIDi 3506781.
KEGGi afm:AFUA_2G03720.

Phylogenomic databases

HOGENOMi HOG000065981.
InParanoidi Q4WHY9.
KOi K01802.
OMAi VFFDVEY.
OrthoDBi EOG757D7G.

Miscellaneous databases

EvolutionaryTracei Q4WHY9.

Family and domain databases

Gene3Di 2.40.100.10. 1 hit.
InterProi IPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view ]
Pfami PF00160. Pro_isomerase. 1 hit.
[Graphical view ]
PIRSFi PIRSF001467. Peptidylpro_ismrse. 1 hit.
PRINTSi PR00153. CSAPPISMRASE.
SUPFAMi SSF50891. SSF50891. 1 hit.
PROSITEi PS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.
    , Fedorova N., Fedorova N., 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., Haas H., Harris D., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafon 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., 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., Yu J.H., Fraser C., Galagan J.E., Asai K., Machida M., Hall N., Barrell B., 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 A1100Imported.
  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), ACTIVE SITE.

Entry informationi

Entry nameiQ4WHY9_ASPFU
AccessioniPrimary (citable) accession number: Q4WHY9
Entry historyi
Integrated into UniProtKB/TrEMBL: July 5, 2005
Last sequence update: July 5, 2005
Last modified: November 26, 2014
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Caution

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

Keywords - Technical termi

3D-structureImported, Complete proteome, Reference proteomeImported

External Data

Dasty 3