ID   CWC27_DEBHA             Reviewed;         327 AA.
AC   Q6BWH6;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Peptidyl-prolyl isomerase CWC27;
DE            Short=PPIase CWC27;
DE            EC=5.2.1.8;
DE   AltName: Full=Rotamase CWC27;
GN   Name=CWC27; OrderedLocusNames=DEHA2B11308g;
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. Involved in pre-mRNA splicing (By similarity).
CC       {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   -!- SUBUNIT: Associated with the spliceosome. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. CWC27
CC       subfamily. {ECO:0000305}.
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DR   EMBL; CR382134; CAG85447.1; -; Genomic_DNA.
DR   RefSeq; XP_457443.1; XM_457443.1.
DR   AlphaFoldDB; Q6BWH6; -.
DR   SMR; Q6BWH6; -.
DR   STRING; 4959.XP_457443.1; -.
DR   EnsemblFungi; CAG85447; CAG85447; DEHA2B11308g.
DR   GeneID; 2913378; -.
DR   KEGG; dha:DEHA2B11308g; -.
DR   VEuPathDB; FungiDB:DEHA2B11308g; -.
DR   eggNOG; KOG0885; Eukaryota.
DR   HOGENOM; CLU_012062_14_0_1; -.
DR   InParanoid; Q6BWH6; -.
DR   OMA; RNTWFIT; -.
DR   OrthoDB; 1392223at2759; -.
DR   Proteomes; UP000000599; Chromosome B.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:InterPro.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.100.10; -; 1.
DR   InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR   InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR   InterPro; IPR044666; Cyclophilin_A-like.
DR   PANTHER; PTHR45625; PTHR45625; 1.
DR   Pfam; PF00160; Pro_isomerase; 1.
DR   SUPFAM; SSF50891; SSF50891; 1.
DR   PROSITE; PS50072; CSA_PPIASE_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Isomerase; mRNA processing; mRNA splicing; Nucleus;
KW   Reference proteome; Rotamase; Spliceosome.
FT   CHAIN           1..327
FT                   /note="Peptidyl-prolyl isomerase CWC27"
FT                   /id="PRO_0000064183"
FT   DOMAIN          8..158
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT   REGION          223..307
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        227..301
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   327 AA;  37319 MW;  2C4F4D829F337B2F CRC64;
     MSSLEPATTA KVALITTKGP IEIELWAKEV PNITRVFIQN CLDKKYIGTT FNKVIKDYLV
     QTSKIKEPAT LKLKDEFHSR LKFNKRGLVG AVHDDKRNSN NVDSLFITLK PTPEFNNNYV
     LFGKIMGDSI YNVVKINESE LKSEETPMYP AEITDIKILV QYFDDLVESK EHIAEPAKKK
     AKKAKKPRVK LDYTLEDEED TGFKMKSAHD LLSDSKLSNK LYANKKKGPS ENNEKQKTIE
     KAQDSSMETK KIVPERPDYK GSEEIENETK ITSSENMNHE TKQDKPNYKA KLDRNPNIDS
     DYDSDLDLSS SESIDLFAFK QSNFQSS