ID   CWC27_ASHGO             Reviewed;         303 AA.
AC   Q75A74;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 104.
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=ADR044C;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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; AE016817; AAS51964.1; -; Genomic_DNA.
DR   RefSeq; NP_984140.1; NM_209493.1.
DR   AlphaFoldDB; Q75A74; -.
DR   SMR; Q75A74; -.
DR   STRING; 33169.AAS51964; -.
DR   EnsemblFungi; AAS51964; AAS51964; AGOS_ADR044C.
DR   GeneID; 4620289; -.
DR   KEGG; ago:AGOS_ADR044C; -.
DR   eggNOG; KOG0885; Eukaryota.
DR   HOGENOM; CLU_012062_14_0_1; -.
DR   InParanoid; Q75A74; -.
DR   OMA; ELDIRLW; -.
DR   Proteomes; UP000000591; Chromosome IV.
DR   GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
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: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.
PE   3: Inferred from homology;
KW   Cytoplasm; Isomerase; mRNA processing; mRNA splicing; Nucleus;
KW   Reference proteome; Rotamase; Spliceosome.
FT   CHAIN           1..303
FT                   /note="Peptidyl-prolyl isomerase CWC27"
FT                   /id="PRO_0000064180"
FT   DOMAIN          7..153
FT                   /note="PPIase cyclophilin-type"
FT   REGION          155..195
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          208..274
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   303 AA;  32485 MW;  2E69CE291FE0C98A CRC64;
     MSSEPSASGK CVLYTTKGEL QIELWAKECP KTVRSFLQSI QDGKWDGIVL GKVAEDAVWA
     PAGLCACSAE INGRLRFNRR GLVGMAPGQD QPFFTLASRG ELDGRAVVFG TLVGQSVYRL
     MEIAQGEVGD DGKTFVYPAE VRRAEVTIPY FDGLSGQKRR AEPEQQAAPR PRKIATRVRL
     EYEESEDEAS DPPLDVRIRA AHDILQDERL TDALHGDSPP PRPAEAPRGS DSAPCVASPD
     RRAEAAPPTD GPPSRCASLA GPAPASPGPV TDLAPQLSAR EQGTLSSLAE FRCKRGGKNP
     LLG