ID   CYP15_RHIO9             Reviewed;         630 AA.
AC   P0C1J0; I1CP28;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase cyp15;
DE            Short=PPIase cyp15;
DE            EC=5.2.1.8;
DE   AltName: Full=Cyclophilin cyp15;
DE   AltName: Full=Rotamase cyp15;
GN   Name=cyp15; ORFNames=RO3G_14919;
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 (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}.
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DR   EMBL; CH476746; EIE90208.1; -; Genomic_DNA.
DR   AlphaFoldDB; P0C1J0; -.
DR   SMR; P0C1J0; -.
DR   STRING; 936053.P0C1J0; -.
DR   EnsemblFungi; EIE90208; EIE90208; RO3G_14919.
DR   VEuPathDB; FungiDB:RO3G_14919; -.
DR   eggNOG; KOG0882; Eukaryota.
DR   InParanoid; P0C1J0; -.
DR   OMA; GGMVEYW; -.
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; 2.130.10.10; -; 1.
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   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   PANTHER; PTHR45625; PTHR45625; 1.
DR   Pfam; PF00160; Pro_isomerase; 1.
DR   Pfam; PF00400; WD40; 1.
DR   PRINTS; PR00153; CSAPPISMRASE.
DR   SMART; SM00320; WD40; 4.
DR   SUPFAM; SSF50891; SSF50891; 1.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS00170; CSA_PPIASE_1; 1.
DR   PROSITE; PS50072; CSA_PPIASE_2; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 1.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   3: Inferred from homology;
KW   Isomerase; Reference proteome; Repeat; Rotamase; WD repeat.
FT   CHAIN           1..630
FT                   /note="Peptidyl-prolyl cis-trans isomerase cyp15"
FT                   /id="PRO_0000244723"
FT   REPEAT          70..108
FT                   /note="WD 1"
FT   REPEAT          113..152
FT                   /note="WD 2"
FT   REPEAT          157..198
FT                   /note="WD 3"
FT   REPEAT          203..242
FT                   /note="WD 4"
FT   REPEAT          258..301
FT                   /note="WD 5"
FT   DOMAIN          475..629
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT   REGION          1..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   630 AA;  71282 MW;  1B357E58EDBDAD47 CRC64;
     MPEDSNTNDN NKRPLEDNNA VDGESDDDIG PMLPPPPGED APRKKKRTLA HEKLYLDQLP
     CADMYEKSYM HRDVLSQVAV TKKDFIITTS VDGHLKFWKK TASGIEFVKH YKSHLSSIVD
     ISISANHELL ATISDDTTLK VYDITNFDMI NMIKLRYKPK SVCWIHQSGQ AQALVAVSEA
     DNSNIHIYDG HADGKPLHTL SKMHSKPVHI IEFNSRFNCV VSVDAIGMIE YWSPEAPFAL
     PDNLDFELKS QTDLYEFRKK KSVPTCLTFS PDGLSFATMS FPDRQVRLFK FLRGKMFREY
     DESLQAVSEM QQAGTTIHHL DDMEFGRRLA VEKELEKSNQ ARFVNAVFDN SGNFIIYGSL
     LGVKIVNIRT NKVVCLLGKS ESNRFVNVSL YQGAPKKKAV YTLAMIASEN AALKESQELD
     PTLFCTAFNK NRFYMMTRRE PFDDINQKAE RDIFNEKPSR EEQTVAATQE RKQILGTSAI
     IRTTSGDIHM RLFPDAAPKA VENFTTHAKN GYYDNLIFHR VIKGFMIQTG CPFGDGTGGE
     SIWGDDFEDE FSREFRHDRP YTVSMANAGP NTNGSQFFIT VAPTTWLDNK HSVFGRVTAG
     MDVVHSIESA KVDKTNKPLD DIKIINIDIR