ID   PPID_YARLI              Reviewed;         367 AA.
AC   Q6CBP4;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 105.
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=YALI0C16775g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
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; CR382129; CAG82238.1; -; Genomic_DNA.
DR   RefSeq; XP_501918.1; XM_501918.1.
DR   AlphaFoldDB; Q6CBP4; -.
DR   SMR; Q6CBP4; -.
DR   STRING; 4952.CAG82238; -.
DR   PRIDE; Q6CBP4; -.
DR   EnsemblFungi; CAG82238; CAG82238; YALI0_C16775g.
DR   GeneID; 2909297; -.
DR   KEGG; yli:YALI0C16775g; -.
DR   VEuPathDB; FungiDB:YALI0_C16775g; -.
DR   HOGENOM; CLU_012062_37_0_1; -.
DR   InParanoid; Q6CBP4; -.
DR   OMA; CKDFGNK; -.
DR   Proteomes; UP000001300; Chromosome C.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0016018; F:cyclosporin A binding; IBA:GO_Central.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IBA:GO_Central.
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; 2.
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..367
FT                   /note="Peptidyl-prolyl cis-trans isomerase D"
FT                   /id="PRO_0000232952"
FT   DOMAIN          7..171
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT   REPEAT          213..246
FT                   /note="TPR 1"
FT   REPEAT          264..297
FT                   /note="TPR 2"
FT   REPEAT          302..335
FT                   /note="TPR 3"
SQ   SEQUENCE   367 AA;  40061 MW;  34FBD2C5DC9F24F7 CRC64;
     MTNPRVFFEV AIGGKTIGKI YFELFADKVP KTAENFRALC TGEKGNTQAG IPLHFKGSSF
     HRVIKDFMVQ GGDFTAGNGT GGESIYGEKF PDEAFPYPHD QPFLLSMANA GPNTNGSQFF
     ITTTETPHLD NKHVVFGKLL SGKGIVRQIE RTETGEQDRP KQPVTIVDCG ELPADFQVPV
     GNVDDGTGDD YEDFLKDNDN VDVNDPASVL GAIEKLKSIG TKLFKEGNAE GALKKYLKAT
     TYLEDYLPDD LSEENIAKVH ALRISCYLNV ALMALKVNQP KVAIKAATSA LDDETVANKE
     KAKALFRRGS GYAALKNETD ALKDLNAALE LEPADGAIKN KIEEVKQAAQ RRREAEKKKY
     AGFFGGK