O00060 (CYPH_UROFA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Alternative name(s):
Cyclophilin
Cyclosporin A-binding protein
Planta-induced rust protein 28
Rotamase

Gene names

Name:

PIG28

Organism

Uromyces fabae (Rust fungus)

Taxonomic identifier

55588 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Basidiomycota › Pucciniomycotina › Pucciniomycetes › Pucciniales › Pucciniaceae › Uromyces

Protein attributes

Sequence length	163 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Catalytic activity	Peptidylproline (omega=180) = peptidylproline (omega=0).
Enzyme regulation	Binds cyclosporin A (CsA). CsA mediates some of its effects via an inhibitory action on PPIase.
Subcellular location	Cytoplasm By similarity.
Developmental stage	Haustoria and rust-infected leaves. Also observed, in lower levels, in spores or hyphae formed in vitro.
Sequence similarities	Belongs to the cyclophilin-type PPIase family. PPIase A subfamily. Contains 1 PPIase cyclophilin-type domain.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Cyclosporin
Molecular function	Isomerase Rotamase
Gene Ontology (GO)
Biological process	protein folding Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	peptide binding Inferred from electronic annotation. Source: UniProtKB-KW peptidyl-prolyl cis-trans isomerase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 163	163	Peptidyl-prolyl cis-trans isomerase		PRO_0000064131
Regions
	Domain	5 – 162	158	PPIase cyclophilin-type

Sequences

	Sequence		Length	Mass (Da)
	O00060 [UniParc]. Last modified July 1, 1997. Version 1. Checksum: A00A641CBA0DBD1D	FASTA	163	17,992
	10 20 30 40 50 60 MANCYFDVSS NGKPLGRIVF ELYDDVVPRT TNNFRQLCLN PPGKGFKHSI FHRVIPDFMI 70 80 90 100 110 120 QGGDFTNGNG TGGESIYGKK FEDENFQKKH VERGMLSMAN AGPNTNGSQF FITVTKTPWL 130 140 150 160 DGKHVVFGKV IEGYDQVVKA MEKTGSQSGK TSSVLKIEDC GTL

References

[1]	"Characterization of in planta-induced rust genes isolated from a haustorium-specific cDNA library." Hahn M., Mendgen K. Mol. Plant Microbe Interact. 10:427-437(1997) [PubMed: 9150592] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: I2. Tissue: Haustorium.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U81792 mRNA. Translation: AAB39880.1.
3D structure databases
ProteinModelPortal	O00060.
SMR	O00060. Positions 1-161.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
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.
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

CYPH_UROFA

Accession

Primary (citable) accession number: O00060

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	July 1, 1997
Last modified:	January 25, 2012
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program