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Protein

Peptidyl-prolyl cis-trans isomerase cypE

Gene

cypE

Organism
Dictyostelium discoideum (Slime mold)
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 (By similarity).By similarity

Catalytic activityi

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

GO - Molecular functioni

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

GO - Biological processi

Keywordsi

Molecular functionIsomerase, Rotamase

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-prolyl cis-trans isomerase cypE (EC:5.2.1.8)
Short name:
PPIase cypE
Alternative name(s):
Cyclophilin cypE
Rotamase cypE
Gene namesi
Name:cypE
ORF Names:DDB_G0269216
OrganismiDictyostelium discoideum (Slime mold)
Taxonomic identifieri44689 [NCBI]
Taxonomic lineageiEukaryotaAmoebozoaMycetozoaDictyostelidsDictyostelialesDictyosteliaceaeDictyostelium
Proteomesi
  • UP000002195 Componentsi: Chromosome 1, Unassembled WGS sequence

Organism-specific databases

dictyBaseiDDB_G0269216 cypE

Subcellular locationi

  • Cytoplasm 1 Publication
  • Nucleus 1 Publication

GO - Cellular componenti

  • cytosol Source: dictyBase
  • nucleus Source: dictyBase

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000641701 – 156Peptidyl-prolyl cis-trans isomerase cypEAdd BLAST156

Proteomic databases

PaxDbiQ9NI62

Interactioni

Subunit structurei

Interacts with snwA.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
snwAP547055EBI-1810601,EBI-1810591

Protein-protein interaction databases

IntActiQ9NI62 1 interactor.
STRINGi44689.DDB0191208

Structurei

3D structure databases

ProteinModelPortaliQ9NI62
SMRiQ9NI62
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 155PPIase cyclophilin-typePROSITE-ProRule annotationAdd BLAST154

Sequence similaritiesi

Belongs to the cyclophilin-type PPIase family.Curated

Phylogenomic databases

eggNOGiKOG0881 Eukaryota
COG0652 LUCA
InParanoidiQ9NI62
KOiK12733
OMAiTSIYGQK
PhylomeDBiQ9NI62

Family and domain databases

Gene3Di2.40.100.101 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.

Q9NI62-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTEQTVTLQT TVGDITLELY YNHAPKACKN FYELSKRGYY DNTIFHRLIK
60 70 80 90 100
DFMIQGGDPL GNGRGGESIY GKKFEDEITK ELKHTGAGIL SMANSGVNSN
110 120 130 140 150
GSQFFITFGP TPWLDGKHTI FGRVKSGMKV VQKMNAMQTN NDKPIDEIRI

IKATAN
Length:156
Mass (Da):17,415
Last modified:October 1, 2000 - v1
Checksum:iD0E02E03DBA06DA3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF215865 mRNA Translation: AAF28343.2
AAFI02000005 Genomic DNA Translation: EAL71958.1
RefSeqiXP_646239.1, XM_641147.1

Genome annotation databases

EnsemblProtistsiEAL71958; EAL71958; DDB_G0269216
GeneIDi8617195
KEGGiddi:DDB_G0269216

Similar proteinsi

Entry informationi

Entry nameiCYPE_DICDI
AccessioniPrimary (citable) accession number: Q9NI62
Secondary accession number(s): Q55D92
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: October 1, 2000
Last modified: February 28, 2018
This is version 98 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome