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1  structure 1  species 0  interactions 1  sequence 1  architecture

Protein: Q4WHY9_ASPFU (Q4WHY9)

Summary

This is the summary of UniProt entry Q4WHY9_ASPFU (Q4WHY9).

Description: Peptidyl-prolyl cis-trans isomerase EC=5.2.1.8
Source organism: Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) (NCBI taxonomy ID 330879)
View Pfam proteome data.
Length: 205 amino acids

Please note: when we start each new Pfam data release, we take a copy of the UniProt sequence database. This snapshot of UniProt forms the basis of the overview that you see here. It is important to note that, although some UniProt entries may be removed after a Pfam release, these entries will not be removed from Pfam until the next Pfam data release.

Pfam domains

Source Domain Start End
Pfam A Pro_isomerase 46 204
low_complexity n/a 101 113
disorder n/a 136 137
disorder n/a 195 196

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Sequence annotations

This section shows a graphical representation of this sequence, with Pfam domains shown in the standard Pfam format. Under the Pfam domain image we show various tracks, illustrating features on this sequence that we found in other databases. You can choose which databases to include using the drop-down panel under the image. More...

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Sequence information

This is the amino acid sequence of the UniProt sequence database entry with the accession Q4WHY9. This sequence is stored in the Pfam database and updated with each new Pfam release, but this means that the sequence we store may differ from that stored by UniProt.

Sequence:
1
MSQVFFDVEY APVGTAETSA RNCAQSGLDA FGLQSILSIL FTDGILLRAV
50
51
TAKVGRIVFN LFDKDVPKTA KNFRELCKRP AGEGYRESTF HRIIPNFMIQ
100
101
GGDFTRGNGT GGRSIYGDKF ADENFSRKHD KKGILSMANA GPNTNGSQFF
150
151
ITTAVTSWLD GKHVVFGEVA DEKSYSVVKE IEALGSSSGS VRSNTRPKIV
200
201
NCGEL                                                 
205
 

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Checksums:
CRC64:28B077F443AA78D8
MD5:86c46bc54a022c5fca3ae6600fa4ac42

Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the MSD group, to allow us to map Pfam domains onto UniProt three-dimensional structures. The table below shows the mapping between Pfam domains, this UniProt entry and a corresponding three dimensional structure.

Pfam family UniProt residues PDB ID PDB chain ID PDB residues View
Pro_isomerase 53 - 204 2C3B A 19 - 170 Jmol AstexViewer SPICE
B 19 - 170 Jmol AstexViewer SPICE