ID   CYP11_RHIO9             Reviewed;         338 AA.
AC   P0C1I9; I1CJI2;
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 cis-trans isomerase cyp11;
DE            Short=PPIase cyp11;
DE            EC=5.2.1.8;
DE   AltName: Full=Cyclophilin cyp11;
DE   AltName: Full=Rotamase cyp11;
GN   Name=cyp11; ORFNames=RO3G_13323;
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).
RN   [2]
RP   REVISION OF GENE MODEL.
RX   PubMed=16995943; DOI=10.1186/1471-2164-7-244;
RA   Pemberton T.J.;
RT   "Identification and comparative analysis of sixteen fungal peptidyl-prolyl
RT   cis/trans isomerase repertoires.";
RL   BMC Genomics 7:244-244(2006).
CC   -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC       cis-trans isomerization of proline imidic peptide bonds in
CC       oligopeptides (By similarity). {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   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EIE88612.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; CH476743; EIE88612.1; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; P0C1I9; -.
DR   SMR; P0C1I9; -.
DR   STRING; 936053.P0C1I9; -.
DR   EnsemblFungi; EIE88612; EIE88612; RO3G_13323.
DR   eggNOG; KOG0546; Eukaryota.
DR   InParanoid; P0C1I9; -.
DR   OrthoDB; 1392223at2759; -.
DR   Proteomes; UP000009138; Unassembled WGS sequence.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:InterPro.
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   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   Isomerase; Reference proteome; Rotamase.
FT   CHAIN           1..338
FT                   /note="Peptidyl-prolyl cis-trans isomerase cyp11"
FT                   /id="PRO_0000244722"
FT   DOMAIN          7..172
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT   REGION          186..338
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        188..209
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        225..245
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        246..314
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   338 AA;  39077 MW;  4500A1482E987432 CRC64;
     MINPRVFFDI DVDGNRIGRI VIELFADQVP KTAENFRALC TGEKGIGKVS NMPLHYKGSI
     FHRIIKGFMC QGGDFTHRTG KGGESIYGAN FPDESFSRKH DTHGLLSMAN RGPNTQTSQF
     FITTRPTPHL DGKHVVFGRV VSGYNVVEMM ENEPVDDQDR PLHNVMIANC GELVLKLPPG
     ALLKKASAVS DESEDEIKNR KRSRSSDDDS SSDEDSEEEE RKRTKKKRSR KHSKKDKKKK
     KRESSNRKRS PEANRHVSRE RRDISREKRD NSRERRLSRK EDDRRSPSDK RKEDRRSLSP
     EKRSSERRVA RPVRPRLNYN DPNVEVKGRG RFKYRPTY