Q9NI62 (CYPE_DICDI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Peptidyl-prolyl cis-trans isomerase cypE
Short name=PPIase cypE
EC=5.2.1.8

Alternative name(s):
Cyclophilin cypE
Rotamase cypE

Gene names

Name:	cypE
ORF Names:	DDB_G0269216

Organism

Dictyostelium discoideum (Slime mold)

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	156 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides By similarity.
Catalytic activity	Peptidylproline (omega=180) = peptidylproline (omega=0).
Subunit structure	Interacts with snwA. Ref.1
Subcellular location	Cytoplasm. Nucleus Ref.1.
Sequence similarities	Belongs to the cyclophilin-type PPIase family. Contains 1 PPIase cyclophilin-type domain.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Molecular function	Isomerase Rotamase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	protein folding Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Inferred from direct assay Ref.1. Source: dictyBase nucleus Inferred from direct assay Ref.1. Source: dictyBase
Molecular function	peptidyl-prolyl cis-trans isomerase activity Inferred from direct assay Ref.1. Source: dictyBase protein binding Inferred from physical interaction Ref.1. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
snwA	P54705	5	EBI-1810601,EBI-1810591

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 156	156	Peptidyl-prolyl cis-trans isomerase cypE		PRO_0000064170
Regions
	Domain	2 – 155	154	PPIase cyclophilin-type

Sequences

	Sequence		Length	Mass (Da)
	Q9NI62 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: D0E02E03DBA06DA3	FASTA	156	17,415
	10 20 30 40 50 60 MTEQTVTLQT TVGDITLELY YNHAPKACKN FYELSKRGYY DNTIFHRLIK DFMIQGGDPL 70 80 90 100 110 120 GNGRGGESIY GKKFEDEITK ELKHTGAGIL SMANSGVNSN GSQFFITFGP TPWLDGKHTI 130 140 150 FGRVKSGMKV VQKMNAMQTN NDKPIDEIRI IKATAN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cyclophilins of a novel subfamily interact with SNW/SKIP coregulator in Dictyostelium discoideum and Schizosaccharomyces pombe." Skruzny M., Ambrozkova M., Fukova I., Martinkova K., Blahuskova A., Hamplova L., Puta F., Folk P. Biochim. Biophys. Acta 1521:146-151(2001) [PubMed: 11690648] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, INTERACTION WITH SNWA. Strain: AX3.
[2]	"The genome of the social amoeba Dictyostelium discoideum." Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A. Nature 435:43-57(2005) [PubMed: 15875012] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF215865 mRNA. Translation: AAF28343.2. AAFI02000005 Genomic DNA. Translation: EAL71958.1.
RefSeq	XP_646239.1. XM_641147.1.
3D structure databases
ProteinModelPortal	Q9NI62.
SMR	Q9NI62. Positions 6-153.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9NI62. 1 interaction.
STRING	Q9NI62.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblProtists	DDB0191208; DDB0191208; DDB_G0269216.
GeneID	8617195.
GenomeReviews	Gene locus cypE in contig CM000150_GR.
KEGG	ddi:DDB_G0269216.
Organism-specific databases
dictyBase	DDB_G0269216. cypE.
Phylogenomic databases
eggNOG	KOG0881.
GeneTree	EPrGT00050000001714.
HOGENOM	HBG610621.
OMA	HDRPKTE.
PhylomeDB	Q9NI62.
ProtClustDB	CLSZ2431400.
Family and domain databases
InterPro	IPR002130. Cyclophilin-like_PPIase_dom. IPR024936. Cyclophilin-type_PPIase. IPR020892. Cyclophilin-type_PPIase_CS. [Graphical view]
Gene3D	G3DSA:2.40.100.10. PPIase_cyclophilin. 1 hit.
KO	K12733.
Pfam	PF00160. Pro_isomerase. 1 hit. [Graphical view]
PIRSF	PIRSF001467. Peptidylpro_ismrse. 1 hit.
PRINTS	PR00153. CSAPPISMRASE.
SUPFAM	SSF50891. CSA_PPIase. 1 hit.
PROSITE	PS00170. CSA_PPIASE_1. 1 hit. PS50072. CSA_PPIASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CYPE_DICDI

Accession

Primary (citable) accession number: Q9NI62
Secondary accession number(s): Q55D92

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 23, 2003
Last sequence update:	October 1, 2000
Last modified:	January 25, 2012
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)