ID   Q86ZF8_BEABA PRELIMINARY;      PRT;   164 AA.
AC   Q86ZF8;
DT   01-JUN-2003 (TrEMBLrel. 24, Created)
DT   01-JUN-2003 (TrEMBLrel. 24, Last sequence update)
DT   01-OCT-2003 (TrEMBLrel. 25, Last annotation update)
DE   Cyclophilin A.
OS   Beauveria bassiana (Tritirachium shiotae).
OC   Eukaryota; Fungi; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Cordyceps.
OX   NCBI_TaxID=176275;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Condia;
RA   Zhang Y., Fang W., Hou L., Yang X., Xiao Y., Pei Y.;
RL   Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: PPIases accelerate the folding of proteins (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline
CC       (omega=0).
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
DR   EMBL; AF542516; AAN39296.1; -.
DR   HSSP; P52011; 1E3B.
DR   GO; GO:0016853; F:isomerase activity; IEA.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA.
DR   GO; GO:0006457; P:protein folding; IEA.
DR   InterPro; IPR002130; CSA_PPIase.
DR   Pfam; PF00160; Pro_isomerase; 1.
DR   PRINTS; PR00153; CSAPPISMRASE.
DR   PROSITE; PS00170; CSA_PPIASE_1; 1.
DR   PROSITE; PS50072; CSA_PPIASE_2; 1.
KW   Isomerase; Rotamase.
SQ   SEQUENCE   164 AA;  17531 MW;  202053D61F8EC8A2 CRC64;
     MANPKVFFEV SANGEPLGKI VMELRKDVVP KTAENFRALC TGEKGYGFKG SSFHRVIPGF
     MCQGGDFTNH NGTGGKSIYG EKFADENFQL KHTGPGILSM ANAGPNTNGS QFFLCTATTG
     WLDGKHVVFG KVVEGLDVVK KVEKFGSDSG KTSKKIVIDA SGEC
//