ID   PPIL1_RHIO9             Reviewed;         165 AA.
AC   P0C1I4; I1BYB1;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase-like 1;
DE            Short=PPIase;
DE            EC=5.2.1.8;
DE   AltName: Full=Rotamase;
GN   Name=cyp3; ORFNames=RO3G_05896;
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. PPIL1
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EIE81191.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; CH476735; EIE81191.1; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; P0C1I4; -.
DR   SMR; P0C1I4; -.
DR   STRING; 936053.P0C1I4; -.
DR   EnsemblFungi; EIE81191; EIE81191; RO3G_05896.
DR   eggNOG; KOG0881; Eukaryota.
DR   InParanoid; P0C1I4; -.
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; IPR024936; Cyclophilin-type_PPIase.
DR   InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR   InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR   InterPro; IPR044666; Cyclophilin_A-like.
DR   PANTHER; PTHR45625; PTHR45625; 1.
DR   Pfam; PF00160; Pro_isomerase; 1.
DR   PIRSF; PIRSF001467; Peptidylpro_ismrse; 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..165
FT                   /note="Peptidyl-prolyl cis-trans isomerase-like 1"
FT                   /id="PRO_0000244717"
FT   DOMAIN          3..157
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
SQ   SEQUENCE   165 AA;  18257 MW;  7DA1BBC4C1402242 CRC64;
     MSEREEVILD TSMGSIHIEL YWDHAPRTCK NFYELAKRGY YDGVSFHRII ADFMIQGGDP
     TGTGRGGTSI YGERFADEIN PGLQHTGAGI LSMANAGPNT NGSQFFITLA PTPWLDGKHT
     IFGRVSDGMN VVKRMGLVKT DANDRLFIVQ KILYALNAVD LNKEL