ID   CYPH_UROFA              Reviewed;         163 AA.
AC   O00060;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase;
DE            Short=PPIase;
DE            EC=5.2.1.8;
DE   AltName: Full=Cyclophilin;
DE   AltName: Full=Cyclosporin A-binding protein;
DE   AltName: Full=Planta-induced rust protein 28;
DE   AltName: Full=Rotamase;
GN   Name=PIG28;
OS   Uromyces fabae (Rust fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Pucciniomycetes; Pucciniales; Pucciniaceae; Uromyces.
OX   NCBI_TaxID=55588;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=I2; TISSUE=Haustorium;
RX   PubMed=9150592; DOI=10.1094/mpmi.1997.10.4.427;
RA   Hahn M., Mendgen K.;
RT   "Characterization of in planta-induced rust genes isolated from a
RT   haustorium-specific cDNA library.";
RL   Mol. Plant Microbe Interact. 10:427-437(1997).
CC   -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC       cis-trans isomerization of proline imidic peptide bonds in
CC       oligopeptides.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC         peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC         COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC         ChEBI:CHEBI:83834; EC=5.2.1.8;
CC   -!- ACTIVITY REGULATION: Binds cyclosporin A (CsA). CsA mediates some of
CC       its effects via an inhibitory action on PPIase.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- DEVELOPMENTAL STAGE: Haustoria and rust-infected leaves. Also observed,
CC       in lower levels, in spores or hyphae formed in vitro.
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase A
CC       subfamily. {ECO:0000305}.
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DR   EMBL; U81792; AAB39880.1; -; mRNA.
DR   AlphaFoldDB; O00060; -.
DR   SMR; O00060; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:InterPro.
DR   Gene3D; 2.40.100.10; -; 1.
DR   InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR   InterPro; IPR024936; Cyclophilin-type_PPIase.
DR   InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR   InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR   Pfam; PF00160; Pro_isomerase; 1.
DR   PIRSF; PIRSF001467; Peptidylpro_ismrse; 1.
DR   PRINTS; PR00153; CSAPPISMRASE.
DR   SUPFAM; SSF50891; SSF50891; 1.
DR   PROSITE; PS00170; CSA_PPIASE_1; 1.
DR   PROSITE; PS50072; CSA_PPIASE_2; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Isomerase; Rotamase.
FT   CHAIN           1..163
FT                   /note="Peptidyl-prolyl cis-trans isomerase"
FT                   /id="PRO_0000064131"
FT   DOMAIN          5..162
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
SQ   SEQUENCE   163 AA;  17992 MW;  A00A641CBA0DBD1D CRC64;
     MANCYFDVSS NGKPLGRIVF ELYDDVVPRT TNNFRQLCLN PPGKGFKHSI FHRVIPDFMI
     QGGDFTNGNG TGGESIYGKK FEDENFQKKH VERGMLSMAN AGPNTNGSQF FITVTKTPWL
     DGKHVVFGKV IEGYDQVVKA MEKTGSQSGK TSSVLKIEDC GTL