ID   PPID_KLULA              Reviewed;         372 AA.
AC   Q6CL78;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 107.
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=KLLA0F05093g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CR382126; CAG98019.1; -; Genomic_DNA.
DR   RefSeq; XP_455311.1; XM_455311.1.
DR   AlphaFoldDB; Q6CL78; -.
DR   SMR; Q6CL78; -.
DR   STRING; 28985.XP_455311.1; -.
DR   EnsemblFungi; CAG98019; CAG98019; KLLA0_F05093g.
DR   GeneID; 2895751; -.
DR   KEGG; kla:KLLA0_F05093g; -.
DR   eggNOG; KOG0546; Eukaryota.
DR   HOGENOM; CLU_012062_37_0_1; -.
DR   InParanoid; Q6CL78; -.
DR   OMA; CKDFGNK; -.
DR   Proteomes; UP000000598; Chromosome F.
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; 3.
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; 3.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Isomerase; Reference proteome; Repeat; Rotamase; TPR repeat.
FT   CHAIN           1..372
FT                   /note="Peptidyl-prolyl cis-trans isomerase D"
FT                   /id="PRO_0000232950"
FT   DOMAIN          9..175
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT   REPEAT          220..253
FT                   /note="TPR 1"
FT   REPEAT          271..304
FT                   /note="TPR 2"
FT   REPEAT          309..342
FT                   /note="TPR 3"
SQ   SEQUENCE   372 AA;  41319 MW;  6B12351B45D87363 CRC64;
     MSETRPKTFF DISIGGKPAG RIVFELYSDV VPKTAENFLK LCEGNSGFAK SKPDIPLSYK
     GSIFHRVIKS FMCQFGDFTN FNGTGGESIY GEKFEDENFT LKHDKPFLLS MANAGANTNG
     SQCFITCVPT PHLDGKHVVF GEVIQGKRLV RTIENNATDE ADKPAKEVKI EDCGVLPSDY
     TVPADAEATP TDAYGDNYEE NITDDSKVDP NDVNSVLNAV EAVKEIGTKQ FKEKNFEVAL
     VKYEKSSQML KQYFPQDLPE EDVKKIDALR VSLFLNIALV SLKSKNYSRT LSAATEALHA
     DNTDDKSKAK ALYRRGLAYY YTKNAEMAVT DLELATTYQP HDTAIIKALQ DAKKAKKELI
     AKQKKSLSKM FS