ID   CWC27_USTMA             Reviewed;         485 AA.
AC   Q4P7H2;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   16-JUN-2009, entry version 28.
DE   RecName: Full=Peptidyl-prolyl isomerase CWC27;
DE            EC=5.2.1.8;
GN   Name=CWC27; ORFNames=UM03941;
OS   Ustilago maydis (Smut fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX   NCBI_TaxID=5270;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=521;
RX   PubMed=17080091; DOI=10.1038/nature05248;
RA   Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T.,
RA   Saville B.J., Banuett F., Kronstad J.W., Gold S.E., Mueller O.,
RA   Perlin M.H., Woesten H.A.B., de Vries R., Ruiz-Herrera J.,
RA   Reynaga-Pena C.G., Snetselaar K., McCann M., Perez-Martin J.,
RA   Feldbruegge M., Basse C.W., Steinberg G., Ibeas J.I., Holloman W.,
RA   Guzman P., Farman M.L., Stajich J.E., Sentandreu R.,
RA   Gonzalez-Prieto J.M., Kennell J.C., Molina L., Schirawski J.,
RA   Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N., Scherer M.,
RA   Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B., Meng S.,
RA   Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA   Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA   Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA   Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA   Chen F., Vysotskaia V., Mannhaupt G., Gueldener U.,
RA   Muensterkoetter M., Haase D., Oesterheld M., Mewes H.-W.,
RA   Mauceli E.W., DeCaprio D., Wade C.M., Butler J., Young S.K.,
RA   Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E., Birren B.W.;
RT   "Insights from the genome of the biotrophic fungal plant pathogen
RT   Ustilago maydis.";
RL   Nature 444:97-101(2006).
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; AACP01000136; EAK85086.1; -; Genomic_DNA.
DR   RefSeq; XP_760088.1; -.
DR   GeneID; 3632039; -.
DR   KEGG; uma:UM03941.1; -.
DR   BRENDA; 5.2.1.8; 2320.
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   Complete proteome; Cytoplasm; Isomerase; mRNA processing;
KW   mRNA splicing; Nucleus; Rotamase; Spliceosome.
FT   CHAIN         1    485       Peptidyl-prolyl isomerase CWC27.
FT                                /FTId=PRO_0000064187.
FT   DOMAIN       11    167       PPIase cyclophilin-type.
SQ   SEQUENCE   485 AA;  54023 MW;  B3F21234EC915BAE CRC64;
     MTSQYVTEPP SSGLVDLVTS KGTISIALFP TQAPLACRNF LTLALEGFYD NLVFHRLIPN
     FILQTGDPSA TGTGGESIYG EPFPIESHSR LKFNRRGLLG MAANQDRTNE SQFFLTLDAT
     PELTGKHTLM GKVEGKSIYT LVELVEGVEL VDGDRPRYPI KLHEVRVVEN PFDDLQPRTT
     KKQRIAEERR KKHEMETRVA EEQKRKRSKA KKNTGLLSFG AEEEAEDEVA LKGPKSSHDL
     LKDDKHLSRQ TIETSKSTKA NTPAVSANIS SKEKRFLAQS SSSTTPPAVT KQASKDGTSD
     APHPTATLKS EHSGPSDQKA SSSTGRDFLA SQRAKYLSSS HPSTAKQDDS YSALLSFQSR
     LRTRPSSTTP IAKPLPSVGV DEVEEEAGEY GASDDDDDWR SHRLDAGGQP LVAGQNAGKD
     TLEDYEVLDP RDHTDRERNP KAESSRDGKR GRDWVEHDRK YQNDRSRRHR EHDKHPQQRR
     QRSII
//