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Protein

Peptidyl-prolyl cis-trans isomerase

Gene

Mal s 6

Organism
Malassezia sympodialis (Atopic eczema-associated yeast)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

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).UniRule annotationSAAS annotation

GO - Molecular functioni

GO - Biological processi

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)
Short name:
PPIaseUniRule annotation
Gene namesi
Name:Mal s 6Imported
OrganismiMalassezia sympodialis (Atopic eczema-associated yeast)Imported
Taxonomic identifieri76777 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaUstilaginomycotinaMalasseziomycetesMalassezialesMalasseziaceaeMalassezia

Pathology & Biotechi

Protein family/group databases

Allergomei3370. Mala s 6.0101.
472. Mala s 6.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CFEX-ray1.50A1-162[»]
ProteinModelPortaliO93970.
SMRiO93970. Positions 1-162.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO93970.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 161157PPIase cyclophilin-typeInterPro annotationAdd
BLAST

Sequence similaritiesi

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

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]
PANTHERiPTHR11071. PTHR11071. 1 hit.
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.

O93970-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNVFFDITK NGAPLGTIKF KLFDDVVPKT AANFRALCTG EKGFGYAGSH
60 70 80 90 100
FHRVIPDFML QGGDFTAGNG TGGKSIYGAK FADENFQLKH NKPGLLSMAN
110 120 130 140 150
AGPNTNGSQF FITTVVTSWL DGKHVVFGEV IDGMNVVKAI EAEGSGSGKP
160
RSRIEIAKCG VC
Length:162
Mass (Da):17,213
Last modified:May 1, 1999 - v1
Checksum:i8C23000AC0251B5C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ011956 mRNA. Translation: CAA09884.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ011956 mRNA. Translation: CAA09884.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CFEX-ray1.50A1-162[»]
ProteinModelPortaliO93970.
SMRiO93970. Positions 1-162.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

Allergomei3370. Mala s 6.0101.
472. Mala s 6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiO93970.

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]
PANTHERiPTHR11071. PTHR11071. 1 hit.
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]
ProtoNetiSearch...

Publicationsi

  1. Raool P.R.
    Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: ATCC no. 42132Imported.
  2. "Selective cloning of Malassezia furfur allergens by phage surface display."
    Lindborg M., Magnusson C.G., Zargari A., Schmidt M., Scheynius A., Crameri R., Whitley P.
    J. Invest. Dermatol. 113:156-161(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: ATCC no. 42132Imported.
  3. "Analysis of the cross-reactivity and of the 1.5 A crystal structure of the Malassezia sympodialis Mala s 6 allergen, a member of the cyclophilin pan-allergen family."
    Glaser A.G., Limacher A., Fluckiger S., Scheynius A., Scapozza L., Crameri R.
    Biochem. J. 396:41-49(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS).

Entry informationi

Entry nameiO93970_MALSM
AccessioniPrimary (citable) accession number: O93970
Entry historyi
Integrated into UniProtKB/TrEMBL: May 1, 1999
Last sequence update: May 1, 1999
Last modified: April 13, 2016
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.