ID   PPIA2_RHIO9             Reviewed;         161 AA.
AC   P0C1H8; I1BNJ9;
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 A2;
DE            Short=PPIase A2;
DE            EC=5.2.1.8;
DE   AltName: Full=Cyclophilin A2;
DE   AltName: Full=Cyclosporin A-binding protein;
DE   AltName: Full=Rotamase A2;
GN   Name=cyp1; ORFNames=RO3G_02483;
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   -!- ACTIVITY REGULATION: Binds cyclosporin A (CsA). CsA mediates some of
CC       its effects via an inhibitory action on PPIase (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase A
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EIE77779.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; CH476733; EIE77779.1; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; P0C1H8; -.
DR   SMR; P0C1H8; -.
DR   STRING; 936053.P0C1H8; -.
DR   PRIDE; P0C1H8; -.
DR   EnsemblFungi; EIE77779; EIE77779; RO3G_02483.
DR   eggNOG; KOG0865; Eukaryota.
DR   InParanoid; P0C1H8; -.
DR   OrthoDB; 1403619at2759; -.
DR   Proteomes; UP000009138; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   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   Cytoplasm; Isomerase; Reference proteome; Rotamase.
FT   CHAIN           1..161
FT                   /note="Peptidyl-prolyl cis-trans isomerase A2"
FT                   /id="PRO_0000244711"
FT   DOMAIN          4..160
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
SQ   SEQUENCE   161 AA;  17351 MW;  D9B133F811CDEDBA CRC64;
     MSVYFDISID GKPAGRIEFQ LFEDVVPKTA KNFRALCTGE QGFGYKGSKF HRVIPQFMLQ
     GGDFTRGDGT GGKSIYGEKF ADENFKLKHS EPGLLSMANA GPNTNGSQFF ITTVPCSWLD
     GAHVVFGKVT KNMELVSKIE SLGSASGAVK AKVVIEDCGV L