ID   CWC27_CRYNB             Reviewed;         491 AA.
AC   P0CP93; Q55L68; Q5KAB3;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 48.
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=CNBJ1160;
OS   Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS   (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=283643;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B-3501A;
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(2005).
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; AAEY01000049; EAL18474.1; -; Genomic_DNA.
DR   RefSeq; XP_773121.1; XM_768028.1.
DR   AlphaFoldDB; P0CP93; -.
DR   SMR; P0CP93; -.
DR   EnsemblFungi; AAW45928; AAW45928; CNJ02320.
DR   EnsemblFungi; EAL18474; EAL18474; CNBJ1160.
DR   GeneID; 4938456; -.
DR   KEGG; cnb:CNBJ1160; -.
DR   VEuPathDB; FungiDB:CNBJ1160; -.
DR   HOGENOM; CLU_012062_14_4_1; -.
DR   Proteomes; UP000001435; Chromosome 10.
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   PRINTS; PR00153; CSAPPISMRASE.
DR   SUPFAM; SSF50891; SSF50891; 1.
DR   PROSITE; PS50072; CSA_PPIASE_2; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Cytoplasm; Isomerase; mRNA processing; mRNA splicing; Nucleus;
KW   Rotamase; Spliceosome.
FT   CHAIN           1..491
FT                   /note="Peptidyl-prolyl isomerase CWC27"
FT                   /id="PRO_0000410206"
FT   DOMAIN          11..167
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT   REGION          186..427
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          464..491
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          277..327
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        186..209
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        223..253
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        269..354
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        363..392
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        475..491
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   491 AA;  55194 MW;  70251B0DC9BD42D2 CRC64;
     MSNLYATEPA TNGKVIIDTT AGEIEVELWG KECPKAVRNF LALTMEGYYD GVIFHRVVPG
     FIIQSGDPTG TGMGGESFYG EPFEDEIHGR LKFNRRGLLG MANNGSRNSN TSQFFITLDA
     APELTNKHTM FGKIVGNTIF NVLNIGNLDT DKEERPLIPP KIRRIHIIEN PFDDIVPRIT
     AEEKKAQQKA KLEAKKDMEQ RERRAKAKKN TGLLSFGDSE EIPEEEVTVK KKSMTRQDLV
     DPSEAEHTKS KTSKMTETFV NIPPSLKDLG KSRENEASEE KKAVDLKNIR AQHEREKAGG
     SAARQAEIKR MEEDLRRLKK RSGSVSDSES DSSSRARRKG PSYLEQELAK YASKRGRAAM
     KAGNKRGRRD EEEDVLTEMR KFSKRVMQAG DEPEEEQAEE IEEGEAKEEG TGIGAAMAEE
     EGGIEVDDDV GWLTHKLKFQ VDDKELTRRA EDEYAVIDPR AKARDLLGKP DKKKLKGNPN
     RRTVRNSGRN R