ID   PPID_CANGA              Reviewed;         371 AA.
AC   Q6FNU6;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase D;
DE            Short=PPIase D;
DE            EC=5.2.1.8;
DE   AltName: Full=Rotamase D;
GN   Name=CPR6; OrderedLocusNames=CAGL0J08954g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC       cis-trans isomerization of proline imidic peptide bonds in
CC       oligopeptides (By similarity). {ECO:0000250}.
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase D
CC       subfamily. {ECO:0000305}.
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DR   EMBL; CR380956; CAG61049.1; -; Genomic_DNA.
DR   RefSeq; XP_448098.1; XM_448098.1.
DR   AlphaFoldDB; Q6FNU6; -.
DR   SMR; Q6FNU6; -.
DR   STRING; 5478.XP_448098.1; -.
DR   EnsemblFungi; CAG61049; CAG61049; CAGL0J08954g.
DR   GeneID; 2889473; -.
DR   KEGG; cgr:CAGL0J08954g; -.
DR   CGD; CAL0129771; CPR6.
DR   VEuPathDB; FungiDB:CAGL0J08954g; -.
DR   eggNOG; KOG0546; Eukaryota.
DR   HOGENOM; CLU_012062_37_0_1; -.
DR   InParanoid; Q6FNU6; -.
DR   OMA; CKDFGNK; -.
DR   Proteomes; UP000002428; Chromosome J.
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:0043022; F:ribosome binding; IEA:EnsemblFungi.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:EnsemblFungi.
DR   GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:InterPro.
DR   GO; GO:0042026; P:protein refolding; IEA:EnsemblFungi.
DR   Gene3D; 1.25.40.10; -; 1.
DR   Gene3D; 2.40.100.10; -; 1.
DR   InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR   InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR   InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   Pfam; PF00160; Pro_isomerase; 1.
DR   PRINTS; PR00153; CSAPPISMRASE.
DR   SMART; SM00028; TPR; 1.
DR   SUPFAM; SSF48452; SSF48452; 1.
DR   SUPFAM; SSF50891; SSF50891; 1.
DR   PROSITE; PS00170; CSA_PPIASE_1; 1.
DR   PROSITE; PS50072; CSA_PPIASE_2; 1.
DR   PROSITE; PS50005; TPR; 2.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Isomerase; Reference proteome; Repeat; Rotamase; TPR repeat.
FT   CHAIN           1..371
FT                   /note="Peptidyl-prolyl cis-trans isomerase D"
FT                   /id="PRO_0000232945"
FT   DOMAIN          7..174
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT   REPEAT          219..252
FT                   /note="TPR 1"
FT   REPEAT          270..303
FT                   /note="TPR 2"
FT   REPEAT          308..341
FT                   /note="TPR 3"
SQ   SEQUENCE   371 AA;  41646 MW;  2FCCF06AFD0EEA8B CRC64;
     MTRPKAYFDI SIGGTPKGRI VFELYKDVVP KTAENFLKLC EGKSGMAKSK PDVPLSYKGS
     IFHRVIKDFM IQFGDFTNFD GTGGESIYGE KFEDENFEIK HDKPFLLSMA NAGPNTNGSQ
     AFITCVPTPH LDGKHVVFGE VIEGKRLVRL IEKQQTEDGT DKPMHDVKVE GCGLLPDDYE
     VPADAEQTPT DEFGDNYEES LKDDAKVDLK KVETVIKAIE TVKDIGTKQF KEQNYEVALA
     KYKKCDKFLK EYFPDDLNEE DMKKINDFKV TVPLNIAIAA LKSKDYRSVM VACSEVLYAE
     AADAKAKAKA LYRRGLAYYH VNDTDMALAD LEMATTFQPN DAAIAKAIND TIKKRKQETE
     KQKKSLSKMF G