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Protein

Peptidyl-prolyl cis-trans isomerase B

Gene

CYPB

Organism
Orpinomyces sp. (strain PC-2)
Status
Reviewed-Annotation score: -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.

Catalytic activityi

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

Enzyme regulationi

Inhibited by cyclosporin A (CsA).

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei147Cyclosporin ASequence analysis1

GO - Molecular functioni

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):
Cyclophilin B
Rotamase B
Gene namesi
Name:CYPB
OrganismiOrpinomyces sp. (strain PC-2)
Taxonomic identifieri50059 [NCBI]
Taxonomic lineageiEukaryotaFungiFungi incertae sedisChytridiomycotaNeocallimastigomycetesNeocallimastigalesNeocallimastigaceaeOrpinomyces

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 – 221 PublicationAdd BLAST22
ChainiPRO_000002548523 – 203Peptidyl-prolyl cis-trans isomerase BAdd BLAST181

Proteomic databases

PRIDEiQ01490

Structurei

3D structure databases

ProteinModelPortaliQ01490
SMRiQ01490
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini33 – 190PPIase cyclophilin-typePROSITE-ProRule annotationAdd BLAST158

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi200 – 203Prevents secretion from ERBy similarity4

Sequence similaritiesi

Keywords - Domaini

Signal

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

Sequencei

Sequence statusi: Complete.

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

Q01490-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNFSIKSVIF LAIVALATLV SASTNPKVTN KVYFDIKQGD KDLGRIVLGL
60 70 80 90 100
YGEVVPKTVE NFRALATGEK GYGYKNSKFH RVIKDFMIQG GDFTRGDGTG
110 120 130 140 150
GKSIYGERFA DENFKLRHTG PGILSMANAG RDTNGSQFFI TTVTTSWLDG
160 170 180 190 200
RHVVFGKVIE GMDVVTAIET TKTLPGDRPA TPVIIADCGE LPVSNNNDAK

AEL
Length:203
Mass (Da):21,969
Last modified:November 1, 1996 - v1
Checksum:iA5748C94305B8BE0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U17900 mRNA Translation: AAD04195.1

Entry informationi

Entry nameiPPIB_ORPSP
AccessioniPrimary (citable) accession number: Q01490
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 17, 2003
Last sequence update: November 1, 1996
Last modified: May 23, 2018
This is version 84 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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