ID   CWC27_GIBZE             Reviewed;         548 AA.
AC   Q4IPB3;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2005, sequence version 1.
DT   16-JUN-2009, entry version 27.
DE   RecName: Full=Peptidyl-prolyl isomerase CWC27;
DE            EC=5.2.1.8;
GN   Name=CWC27; ORFNames=FG00945;
OS   Gibberella zeae (Fusarium graminearum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Nectriaceae;
OC   Gibberella.
OX   NCBI_TaxID=5518;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PH-1 / NRRL 31084;
RX   PubMed=17823352; DOI=10.1126/science.1143708;
RA   Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G.,
RA   Di Pietro A., Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G.,
RA   Antoniw J., Baldwin T., Calvo S.E., Chang Y.-L., DeCaprio D.,
RA   Gale L.R., Gnerre S., Goswami R.S., Hammond-Kosack K., Harris L.J.,
RA   Hilburn K., Kennell J.C., Kroken S., Magnuson J.K., Mannhaupt G.,
RA   Mauceli E.W., Mewes H.-W., Mitterbauer R., Muehlbauer G.,
RA   Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T., Qi W.,
RA   Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA   Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT   "The Fusarium graminearum genome reveals a link between localized
RT   polymorphism and pathogen specialization.";
RL   Science 317:1400-1402(2007).
CC   -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes
CC       the cis-trans isomerization of proline imidic peptide bonds in
CC       oligopeptides. Involved in pre-mRNA splicing (By similarity).
CC   -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline
CC       (omega=0).
CC   -!- SUBUNIT: Associated with the spliceosome (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. CWC27
CC       subfamily.
CC   -!- SIMILARITY: Contains 1 PPIase cyclophilin-type domain.
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DR   EMBL; AACM01000046; EAA69496.1; -; Genomic_DNA.
DR   RefSeq; XP_381121.1; -.
DR   GeneID; 2783469; -.
DR   KEGG; fgr:FG00945.1; -.
DR   BRENDA; 5.2.1.8; 74326.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005681; C:spliceosome; 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:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   InterPro; IPR002130; PPIase_cyclophilin.
DR   Gene3D; G3DSA:2.40.100.10; PPIase_cyclophilin; 1.
DR   Pfam; PF00160; Pro_isomerase; 1.
DR   PRINTS; PR00153; CSAPPISMRASE.
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   Rotamase; Spliceosome.
FT   CHAIN         1    548       Peptidyl-prolyl isomerase CWC27.
FT                                /FTId=PRO_0000064185.
FT   DOMAIN       11    193       PPIase cyclophilin-type.
SQ   SEQUENCE   548 AA;  60927 MW;  CD8C59B37B323541 CRC64;
     MSAIYNLEPQ PTASVIIHTT RGELSVELFA KQAPLTCRNF LQLALDGYYD NTIFHRLVPG
     FILQGGDPTG TGNGGESIYD GGAFSGDLDP WPMDQRMGKN AGPTGINFKD EFHSRLKFNR
     RGLLGSANES RPDTNSSQFF FTLDTAEELN GKNTMFGRIA GDTVYNLAKM GEGEVDEATE
     RPTYPVKIER IEILINPFED MKKRSRVAAV APSKTTTTKD KKKKRKGGKQ LLSFGDDEGD
     DEMPVLKKKK FDPRIVMEAP EEAPEQDEVR SKPTKAKKER ASEKRVSIAQ EEQDNSDQTT
     PREPPKEVRQ KPAPPVKMEI EDESPEPEAP RKTALERANE EMAALKASMR RTIHSEEPVK
     EKKKSALESM IPETSMRGRK RRPGAANTSA ADDAKALRML KAFQSRLEKA PPEKENEPAA
     RETTKDGEDA QAGDEEAELC DLHFIANCQS CTSWDKQEKD ESDDEGWMSH ALSFAADKLG
     KDLSNRRKAE EELVVIDPRE KARTLKDEKK AARDARQGNS GRAWDQARDA ARNAKMAQAA
     SLAGRGAK
//