ID   CWC27_RHIO9             Reviewed;         524 AA.
AC   P0C1J2; I1BUC8;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 1.
DT   03-AUG-2022, entry version 62.
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; ORFNames=RO3G_04513;
OS   Rhizopus delemar (strain RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL
OS   43880) (Mucormycosis agent) (Rhizopus arrhizus var. delemar).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX   NCBI_TaxID=246409;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL 43880;
RX   PubMed=19578406; DOI=10.1371/journal.pgen.1000549;
RA   Ma L.-J., Ibrahim A.S., Skory C., Grabherr M.G., Burger G., Butler M.,
RA   Elias M., Idnurm A., Lang B.F., Sone T., Abe A., Calvo S.E.,
RA   Corrochano L.M., Engels R., Fu J., Hansberg W., Kim J.-M., Kodira C.D.,
RA   Koehrsen M.J., Liu B., Miranda-Saavedra D., O'Leary S.,
RA   Ortiz-Castellanos L., Poulter R., Rodriguez-Romero J., Ruiz-Herrera J.,
RA   Shen Y.-Q., Zeng Q., Galagan J., Birren B.W., Cuomo C.A., Wickes B.L.;
RT   "Genomic analysis of the basal lineage fungus Rhizopus oryzae reveals a
RT   whole-genome duplication.";
RL   PLoS Genet. 5:E1000549-E1000549(2009).
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; CH476734; EIE79808.1; -; Genomic_DNA.
DR   AlphaFoldDB; P0C1J2; -.
DR   SMR; P0C1J2; -.
DR   STRING; 936053.P0C1J2; -.
DR   EnsemblFungi; EIE79808; EIE79808; RO3G_04513.
DR   VEuPathDB; FungiDB:RO3G_04513; -.
DR   eggNOG; KOG0885; Eukaryota.
DR   InParanoid; P0C1J2; -.
DR   OMA; GTYGSQF; -.
DR   OrthoDB; 1392223at2759; -.
DR   Proteomes; UP000009138; Unassembled WGS sequence.
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:0006457; P:protein folding; IEA:InterPro.
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; IPR020892; Cyclophilin-type_PPIase_CS.
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; PS00170; CSA_PPIASE_1; 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..524
FT                   /note="Peptidyl-prolyl isomerase cwc27"
FT                   /id="PRO_0000244725"
FT   DOMAIN          11..166
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT   REGION          243..371
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          389..417
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          451..524
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        252..327
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        338..371
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        451..503
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        504..524
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   524 AA;  61050 MW;  087BDD7CF342A2D5 CRC64;
     MSNIYALEPH TNAKVILHTT SGDIEIELWG KEAPRATRNF IQLCLEGYYD NTIFHRIVPG
     FLVQGGDPTG TGQGGESVYE DGFPDEFHSR LRFNRRGLVG VANTGQNDNG SQFFITLDRA
     DELTKRHTLF GRVAGDTLFN VMKMTELEID ENERPLYPPR IKRTEIVINP FDDILPRITE
     REKRQQKELE KKKMLEEAKK KKAPKKKQLN LLSFGEEAAE LEPPSHTVEK TKMKSAYDFM
     ETSAPTPTEL IEELKKPVKE ESTVISEKKD DAKQEEENKK AEEEERKRKK ALEEERKRQK
     EEEKKKMQEN TSESRASAIE KLKQDIRNLS KTSSNTSDEL IPKKDKKRSL VELEREKYAS
     QKRKKMKKGD DTDVFNKLMS FQKKLSTAKE DEDAAAAKRD QPPCEIHGIP GCESCRDTTQ
     DAEEDVSDAG WISHKLIFEK DLKGKDLMKR RETVDDYVVI DPRDREAKAK QEEYERKKGI
     KSSSSSQRRD RMDHDDKRYR TEKRSRSDRH RRSRSRDRYD DRRR