ID   PPID_DEBHA              Reviewed;         370 AA.
AC   Q6BXZ7;
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=DEHA2A13640g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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; CR382133; CAG84900.1; -; Genomic_DNA.
DR   RefSeq; XP_456922.1; XM_456922.1.
DR   AlphaFoldDB; Q6BXZ7; -.
DR   SMR; Q6BXZ7; -.
DR   STRING; 4959.XP_456922.1; -.
DR   EnsemblFungi; CAG84900; CAG84900; DEHA2A13640g.
DR   GeneID; 2899475; -.
DR   KEGG; dha:DEHA2A13640g; -.
DR   VEuPathDB; FungiDB:DEHA2A13640g; -.
DR   eggNOG; KOG0546; Eukaryota.
DR   HOGENOM; CLU_012062_37_0_1; -.
DR   InParanoid; Q6BXZ7; -.
DR   OMA; CKDFGNK; -.
DR   OrthoDB; 1403619at2759; -.
DR   Proteomes; UP000000599; Chromosome A.
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; 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; 1.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Isomerase; Reference proteome; Repeat; Rotamase; TPR repeat.
FT   CHAIN           1..370
FT                   /note="Peptidyl-prolyl cis-trans isomerase D"
FT                   /id="PRO_0000232947"
FT   DOMAIN          11..176
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT   REPEAT          218..251
FT                   /note="TPR 1"
FT   REPEAT          269..302
FT                   /note="TPR 2"
FT   REPEAT          307..340
FT                   /note="TPR 3"
SQ   SEQUENCE   370 AA;  40748 MW;  4F24FFD31A5FF060 CRC64;
     MSDKLNRPKV FFDISADGKP KGRVVFELYN DVVPKTAENF RALCTGEKGA SESSGKQLHY
     KGSIFHRIIK DFMCQGGDFT HGSGIGGESI YGEKFEDENF QLTHDKPFLL SMANAGANTN
     GSQFFITTVP TPHLNGKHVV FGEVIQGKSI VRQLERCDKG ENDKPVEDWI ISDCGELPSD
     YVPVPTSVDD GTGDIYEEVM ADDDNINVND PESVFKAVTT LKDIGTKQLK DGNVAAAYEK
     YNKASGFLND YFPEDLSEEN LSKLHALKLS CYLNAALVAL KLKDGKKTIN AASNALEVEA
     IDDKSKTKAL YRKGMGYLLA KDEESAQKSL EEALQLSPED GAIIKGLQDV KTTIKARRDK
     QKKAMSKFFS