ID   PPIB_CRYNB              Reviewed;         231 AA.
AC   P0CP79; Q55P39; Q5KEB7;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 52.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase B;
DE            Short=PPIase B;
DE            EC=5.2.1.8;
DE   AltName: Full=Rotamase B;
DE   Flags: Precursor;
GN   Name=CPR2; OrderedLocusNames=CNBG3730;
OS   Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS   (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=283643;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B-3501A;
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(2005).
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: Inhibited by cyclosporin A (CsA). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase B
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AAEY01000038; EAL19745.1; -; Genomic_DNA.
DR   RefSeq; XP_774392.1; XM_769299.1.
DR   AlphaFoldDB; P0CP79; -.
DR   SMR; P0CP79; -.
DR   EnsemblFungi; AAW44558; AAW44558; CNG01060.
DR   EnsemblFungi; EAL19745; EAL19745; CNBG3730.
DR   GeneID; 4937409; -.
DR   KEGG; cnb:CNBG3730; -.
DR   VEuPathDB; FungiDB:CNBG3730; -.
DR   HOGENOM; CLU_012062_4_2_1; -.
DR   Proteomes; UP000001435; Chromosome 7.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; 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; IPR020892; Cyclophilin-type_PPIase_CS.
DR   InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR   Pfam; PF00160; Pro_isomerase; 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   Endoplasmic reticulum; Glycoprotein; Isomerase; Rotamase; Signal.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000255"
FT   CHAIN           36..231
FT                   /note="Peptidyl-prolyl cis-trans isomerase B"
FT                   /id="PRO_0000410199"
FT   DOMAIN          48..211
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT   MOTIF           228..231
FT                   /note="Prevents secretion from ER"
FT   CARBOHYD        155
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   231 AA;  24958 MW;  9D639C2FF7802571 CRC64;
     MNTSHPIPTT MASKSFLSLL VALFVAICFV LSPGVDAAKG PVITNKVYFD IEHGGKPLGR
     IVMGLYGKTV PKTAENFRAL ATGKNSDGED LGYGYEGSSF HRIIKNFMIQ GGDFTKGDGT
     GGKSIYGSKF PDENFKLKHT GPGVLSMANA GRDTNGSQFF ICTVKTAWLD NRHVVFGHVL
     EGMDVVYAME NVKTSRGDKP VEPITIAASG ELPIEHEVDE QGNQVPFRIE L