ID   PPIE_RHIO9              Reviewed;         315 AA.
AC   P0C1I2; I1BQY7;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase E;
DE            Short=PPIase E;
DE            EC=5.2.1.8;
DE   AltName: Full=Cyclophilin E;
DE   AltName: Full=Rotamase E;
GN   Name=cyp10; ORFNames=RO3G_03321;
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. Combines RNA-binding and PPIase activities (By
CC       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. PPIase E
CC       subfamily. {ECO:0000305}.
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DR   EMBL; CH476733; EIE78617.1; -; Genomic_DNA.
DR   AlphaFoldDB; P0C1I2; -.
DR   SMR; P0C1I2; -.
DR   STRING; 936053.P0C1I2; -.
DR   PRIDE; P0C1I2; -.
DR   EnsemblFungi; EIE78617; EIE78617; RO3G_03321.
DR   VEuPathDB; FungiDB:RO3G_03321; -.
DR   eggNOG; KOG0111; Eukaryota.
DR   InParanoid; P0C1I2; -.
DR   OMA; KIVIYAC; -.
DR   OrthoDB; 1484092at2759; -.
DR   Proteomes; UP000009138; Unassembled WGS sequence.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:InterPro.
DR   CDD; cd12347; RRM_PPIE; 1.
DR   Gene3D; 2.40.100.10; -; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR   InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR   InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR016304; PPIE.
DR   InterPro; IPR034168; PPIE_RRM.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   Pfam; PF00160; Pro_isomerase; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   PIRSF; PIRSF001475; PPI_cyclophilin_E; 1.
DR   PRINTS; PR00153; CSAPPISMRASE.
DR   SMART; SM00360; RRM; 1.
DR   SUPFAM; SSF50891; SSF50891; 1.
DR   SUPFAM; SSF54928; SSF54928; 1.
DR   PROSITE; PS00170; CSA_PPIASE_1; 1.
DR   PROSITE; PS50072; CSA_PPIASE_2; 1.
DR   PROSITE; PS50102; RRM; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Isomerase; Reference proteome; RNA-binding; Rotamase.
FT   CHAIN           1..315
FT                   /note="Peptidyl-prolyl cis-trans isomerase E"
FT                   /id="PRO_0000244715"
FT   DOMAIN          12..93
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          158..314
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT   REGION          119..148
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          114..142
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        119..136
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   315 AA;  34739 MW;  34A5506E00B8DB7E CRC64;
     MPSVNITKNN KTTLYISGLD QQVNEAVLHA AFIPFGEIIA VQMATDTEID SNNIHRGFGF
     VEYELAEDCQ AAMDNMHLSE LYGKVIKVQL AKTINVTTTS NRAVWTDESW LQKYGNVEDV
     EEKQEDEKEN NQETTSEKKE VSSYIPSSEK RGKKSRVYLD IQIGNTLAGR IEIELRGDVV
     PKTAENFRAL CTGEAGFGYK KSSFHRIIPQ FMCQGGDFTK GNGTGGKSIY GGKFEDENFV
     LKHTGPGTLS MANAGSNTNG SQFFICTEKT TWLDGKHVVF GQVVSGMNVV REMERCGSAS
     GKPSKRVVIV DCGEL