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Protein

Peptidyl-prolyl cis-trans isomerase B

Gene

cypB

Organism
Aspergillus niger
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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

Catalytic activityi

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

Enzyme regulationi

Inhibited by cyclosporin A (CsA).By similarity

GO - Molecular functioni

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

GO - Biological processi

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

Keywords - Molecular functioni

Isomerase, Rotamase

Keywords - Ligandi

Cyclosporin

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-prolyl cis-trans isomerase B (EC:5.2.1.8)
Short name:
PPIase B
Alternative name(s):
Rotamase B
Gene namesi
Name:cypB
OrganismiAspergillus niger
Taxonomic identifieri5061 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Subcellular locationi

Endoplasmic reticulum lumen PROSITE-ProRule annotation

GO - Cellular componenti

  1. endoplasmic reticulum lumen Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence AnalysisAdd
BLAST
Chaini24 – 212189Peptidyl-prolyl cis-trans isomerase BPRO_0000233044Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi139 – 1391N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PRIDEiQ8X166.

Structurei

3D structure databases

ProteinModelPortaliQ8X166.
SMRiQ8X166. Positions 30-199.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini38 – 195158PPIase cyclophilin-typePROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi209 – 2124Prevents secretion from ER

Sequence similaritiesi

Contains 1 PPIase cyclophilin-type domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0652.

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.
PS00014. ER_TARGET. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8X166-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNFKNIFLSF FFVLAVGLAL VHAEDAQPRG PKITSKVFFD IEHGDKPLGR
60 70 80 90 100
VVLGLYGKTV PKTAENFRAL ATGEKGFGYE GSTFHRVIKD FMIQGGDFTR
110 120 130 140 150
GDGTGGKSIY GEKFADENFK LRHTRKGLLS MANAGKDTNG SQFFITTVPT
160 170 180 190 200
PWLDGRHVVF GEVLEGYEIV AQIENVPKGR SDRPVETVKI VKSGELESED
210
KAGEKGSSHE EL
Length:212
Mass (Da):23,302
Last modified:March 1, 2002 - v1
Checksum:iFA00BA7D1E50019C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY005867 Genomic DNA. Translation: AAF98447.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY005867 Genomic DNA. Translation: AAF98447.1.

3D structure databases

ProteinModelPortaliQ8X166.
SMRiQ8X166. Positions 30-199.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ8X166.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiCOG0652.

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.
PS00014. ER_TARGET. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The foldase CYPB is a component of the secretory pathway of Aspergillus niger and contains the endoplasmic reticulum retention signal HEEL."
    Derkx P.M.F., Madrid S.M.
    Mol. Gen. Genet. 266:537-545(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiPPIB_ASPNG
AccessioniPrimary (citable) accession number: Q8X166
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 18, 2006
Last sequence update: March 1, 2002
Last modified: January 7, 2015
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.