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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

  • peptidyl-prolyl cis-trans isomerase activity Source: AspGD

GO - Biological processi

Keywordsi

Molecular functionIsomerase, Rotamase

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

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 23Sequence analysisAdd BLAST23
ChainiPRO_000023304424 – 212Peptidyl-prolyl cis-trans isomerase BAdd BLAST189

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi139N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Glycoprotein

Proteomic databases

PRIDEiQ8X166.

Structurei

3D structure databases

ProteinModelPortaliQ8X166.
SMRiQ8X166.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini38 – 195PPIase cyclophilin-typePROSITE-ProRule annotationAdd BLAST158

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi209 – 212Prevents secretion from ER4

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG0880. Eukaryota.
ENOG410Z0G4. LUCA.

Family and domain databases

Gene3Di2.40.100.10. 1 hit.
InterProiView protein in InterPro
IPR029000. Cyclophilin-like_dom_sf.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
PANTHERiPTHR11071. PTHR11071. 1 hit.
PfamiView protein in Pfam
PF00160. Pro_isomerase. 1 hit.
PIRSFiPIRSF001467. Peptidylpro_ismrse. 1 hit.
PRINTSiPR00153. CSAPPISMRASE.
SUPFAMiSSF50891. SSF50891. 1 hit.
PROSITEiView protein in PROSITE
PS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
PS00014. ER_TARGET. 1 hit.

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.

Similar proteinsi

Entry informationi

Entry nameiPPIB_ASPNG
AccessioniPrimary (citable) accession number: Q8X166
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 18, 2006
Last sequence update: March 1, 2002
Last modified: January 31, 2018
This is version 79 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families