ID   PPIL1_ASPNG             Reviewed;         162 AA.
AC   Q8X191;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 76.
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=cypC;
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Derkx P.M.F.;
RL   Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF455393; AAL57849.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8X191; -.
DR   SMR; Q8X191; -.
DR   STRING; 5061.CADANGAP00010101; -.
DR   VEuPathDB; FungiDB:An12g08680; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1183225; -.
DR   VEuPathDB; FungiDB:ATCC64974_34720; -.
DR   VEuPathDB; FungiDB:M747DRAFT_257237; -.
DR   eggNOG; KOG0881; Eukaryota.
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; Rotamase.
FT   CHAIN           1..162
FT                   /note="Peptidyl-prolyl cis-trans isomerase-like 1"
FT                   /id="PRO_0000232962"
FT   DOMAIN          1..155
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
SQ   SEQUENCE   162 AA;  17769 MW;  59803ACFADDDA9CB CRC64;
     MATDVAFDTS MGSFTVELYN AHAPKTCKNF ATLAQRGYYN NVIFHRIIPN FMVQTGDPTG
     TGRGGSSIYG EKFEDEINPN LKHTGAGILS MANSGPNNNG SQFFITLAPQ PWLDGKHTIF
     GRVKSGMRVI QRMGLVKTNS EDRPVDGVKI LRARIVEETG DE