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Q4WP12 (PPIB_ASPFU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peptidyl-prolyl cis-trans isomerase B

Short name=PPIase B
EC=5.2.1.8
Alternative name(s):
Rotamase B
Gene names
Name:cpr2
ORF Names:AFUA_4G07650
OrganismNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) [Reference proteome]
Taxonomic identifier330879 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length209 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

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

Catalytic activity

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

Enzyme regulation

Inhibited by cyclosporin A (CsA) By similarity.

Subcellular location

Endoplasmic reticulum lumen By similarity.

Sequence similarities

Belongs to the cyclophilin-type PPIase family. PPIase B subfamily.

Contains 1 PPIase cyclophilin-type domain.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
   DomainSignal
   LigandCyclosporin
   Molecular functionIsomerase
Rotamase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processprotein folding

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentendoplasmic reticulum lumen

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionpeptide binding

Inferred from electronic annotation. Source: UniProtKB-KW

peptidyl-prolyl cis-trans isomerase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 209186Peptidyl-prolyl cis-trans isomerase B
PRO_0000233043

Regions

Domain39 – 196158PPIase cyclophilin-type
Motif206 – 2094Prevents secretion from ER

Amino acid modifications

Glycosylation1401N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q4WP12 [UniParc].

Last modified July 5, 2005. Version 1.
Checksum: 4DF86787CAA2B426

FASTA20922,960
        10         20         30         40         50         60 
MNFKSLFLSF FLVFAVGLAL VHAEETKEPR GPKITSKVFF DIEHGDKPLG RIVLGLYGKT 

        70         80         90        100        110        120 
VPKTAENFRA LATGEKGFGY EGSTFHRVIK SFMIQGGDFT RGDGTGGKSI YGEKFADENF 

       130        140        150        160        170        180 
KLRHTRKGLL SMANAGKDTN GSQFFITTVP TPWLDGRHVV FGEVLEGYEV VEQIENVPKG 

       190        200 
PGDKPAETVK IVKSGQIKDE STKGSHEEL 

« Hide

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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AAHF01000005 Genomic DNA. Translation: EAL90022.1.
RefSeqXP_752060.1. XM_746967.1.

3D structure databases

ProteinModelPortalQ4WP12.
SMRQ4WP12. Positions 30-197.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5085.CADAFUAP00008354.

Proteomic databases

PRIDEQ4WP12.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAFUAT00008354; CADAFUAP00008354; CADAFUAG00008354.
GeneID3509715.
KEGGafm:AFUA_4G07650.

Phylogenomic databases

eggNOGCOG0652.
HOGENOMHOG000065981.
KOK03768.
OMAKIQNVPK.
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.
PS00014. ER_TARGET. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePPIB_ASPFU
AccessionPrimary (citable) accession number: Q4WP12
Entry history
Integrated into UniProtKB/Swiss-Prot: April 18, 2006
Last sequence update: July 5, 2005
Last modified: April 16, 2014
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families