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Q2UGK2 (PPIB_ASPOR) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 53. 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:AO090023000811
OrganismAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) [Complete proteome]
Taxonomic identifier510516 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length192 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
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 – ? Potential
Chain? – 192Peptidyl-prolyl cis-trans isomerase BPRO_0000233045

Regions

Domain23 – 180158PPIase cyclophilin-type
Motif189 – 1924Prevents secretion from ER

Amino acid modifications

Glycosylation1241N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q2UGK2 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: 2D8B5BD7770C20FA

FASTA19221,081
        10         20         30         40         50         60 
MTDLRSAEEI TSQQYSSGLA TVYFDIEHGN KPLGRVVLGL YGKTVPKTAE NFRALATGEK 

        70         80         90        100        110        120 
GFGYEGSTFH RVIKEFMIQG GDFTRGDGTG GKSIYGEKFK DENFKIRHTK KGLLSMANAG 

       130        140        150        160        170        180 
KDTNGSQFFI TTVATPWLDG RHVVFGEVLE GYEVVEAIEN VPKVPGDKPQ QVVKIVKSGE 

       190 
LESEDKGSHE EL 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP007157 Genomic DNA. Translation: BAE59313.1.

3D structure databases

ProteinModelPortalQ2UGK2.
SMRQ2UGK2. Positions 22-181.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5062.CADAORAP00007739.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAORAT00007900; CADAORAP00007739; CADAORAG00007900.

Phylogenomic databases

eggNOGCOG0652.
HOGENOMHOG000065981.
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_ASPOR
AccessionPrimary (citable) accession number: Q2UGK2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 18, 2006
Last sequence update: January 24, 2006
Last modified: April 16, 2014
This is version 53 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