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InterPro: IPR000297 Peptidyl-prolyl cis-trans isomerase, PpiC-type

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UniProtKB

Matches:

3960 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR000297 PPIase_PpiC

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF00639	Rotamase	3897
PROSITE pattern	PS01096	PPIC_PPIASE_1	1757
PROSITE profile	PS50198	PPIC_PPIASE_2	3918
Signatures in BioMart

InterPro Relationships Help

Found in

IPR014282 Nitrogen fixation protein NifM

GO Term annotation Help

Function

GO:0016853 isomerase activity

InterPro annotation

Entry Details in BioMart

Abstract

Recommended name: Peptidylprolyl isomerase

Synonyms for proteins with this domain are: Peptidyl-prolyl cis-trans isomerase, PPIase, rotamase, cyclophilin, FKBP65

Peptidylprolyl isomerase (EC:5.2.1.8) is an enzyme that accelerates protein folding by catalyzing the cis-trans isomerization of proline imidic peptide bonds in oligopeptides [1]. It has been reported in bacteria and eukayotes.

Structural links Help

PDB - click here

SCOP: d.26.1.1

CATH: 3.10.50.40

Database links Help

PDBe-motif: PS01096

Enzyme: EC:5.2.1.8

PROSITE doc: PDOC00840

PANDIT: PF00639

Blocks: IPB000297

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR000297

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P22696 Peptidyl-prolyl cis-trans isomerase ESS1

P54353 Protein dodo

Q13526 Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1

Q9CWW6 Peptidyl-prolyl cis-trans isomerase NIMA-interacting 4

Q9SL42 Peptidyl-prolyl cis-trans isomerase 1

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR000297	Peptidyl-prolyl cis-trans isomerase, PpiC-type
IPR001202	WW/Rsp5/WWP
	SWISS-MODEL
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Open in usermanual
1.	Fischer G, Schmid FX. The mechanism of protein folding. Implications of in vitro refolding models for de novo protein folding and translocation in the cell. Biochemistry 29 2205-12 1990 [PubMed: 2186809] http://dx.doi.org/10.1021/bi00461a001

Additional Reading Open in usermanual
	Li Z, Li H, Devasahayam G, Gemmill T, Chaturvedi V, Hanes SD, Van Roey P. The structure of the Candida albicans Ess1 prolyl isomerase reveals a well-ordered linker that restricts domain mobility. Biochemistry 44 2005 6180-9 [PubMed: 15835905] http://dx.doi.org/10.1021/bi050115l
	Zhang Y, Daum S, Wildemann D, Zhou XZ, Verdecia MA, Bowman ME, Lucke C, Hunter T, Lu KP, Fischer G, Noel JP. Structural basis for high-affinity peptide inhibition of human Pin1. ACS Chem. Biol. 2 2007 320-8 [PubMed: 17518432]
	Rahfeld JU, Rucknagel KP, Schelbert B, Ludwig B, Hacker J, Mann K, Fischer G. Confirmation of the existence of a third family among peptidyl-prolyl cis/trans isomerases. Amino acid sequence and recombinant production of parvulin. FEBS Lett. 352 1994 180-4 [PubMed: 7925971] http://dx.doi.org/10.1016/0014-5793(94)00932-5
	Xu X, Wang S, Hu YX, McKay DB. The periplasmic bacterial molecular chaperone SurA adapts its structure to bind peptides in different conformations to assert a sequence preference for aromatic residues. J. Mol. Biol. 373 2007 367-81 [PubMed: 17825319] http://dx.doi.org/10.1016/j.jmb.2007.07.069
	Tossavainen H, Permi P, Purhonen SL, Sarvas M, Kilpelainen I, Seppala R. NMR solution structure and characterization of substrate binding site of the PPIase domain of PrsA protein from Bacillus subtilis. FEBS Lett. 580 2006 1822-6 [PubMed: 16516208] http://dx.doi.org/10.1016/j.febslet.2006.02.042
	Jager M, Zhang Y, Bieschke J, Nguyen H, Dendle M, Bowman ME, Noel JP, Gruebele M, Kelly JW. Structure-function-folding relationship in a WW domain. Proc. Natl. Acad. Sci. U.S.A. 103 2006 10648-53 [PubMed: 16807295] http://dx.doi.org/10.1073/pnas.0600511103

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