ID   PPIH_CRYNJ              Reviewed;         179 AA.
AC   P0CP82; Q55L87; Q5KA96;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase H;
DE            Short=PPIase H;
DE            EC=5.2.1.8;
DE   AltName: Full=Rotamase H;
GN   Name=CYP3; OrderedLocusNames=CNJ02490;
OS   Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS   MYA-565) (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=214684;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JEC21 / ATCC MYA-565;
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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase H
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AE017350; AAW46023.1; -; Genomic_DNA.
DR   RefSeq; XP_567540.1; XM_567540.1.
DR   AlphaFoldDB; P0CP82; -.
DR   SMR; P0CP82; -.
DR   STRING; 5207.AAW46023; -.
DR   PaxDb; P0CP82; -.
DR   EnsemblFungi; AAW46023; AAW46023; CNJ02490.
DR   GeneID; 3254213; -.
DR   KEGG; cne:CNJ02490; -.
DR   VEuPathDB; FungiDB:CNJ02490; -.
DR   eggNOG; KOG0879; Eukaryota.
DR   HOGENOM; CLU_012062_4_3_1; -.
DR   InParanoid; P0CP82; -.
DR   OMA; RHPNNPV; -.
DR   OrthoDB; 1403619at2759; -.
DR   Proteomes; UP000002149; Chromosome 10.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016018; F:cyclosporin A binding; IBA:GO_Central.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IBA:GO_Central.
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   Isomerase; Nucleus; Reference proteome; Rotamase.
FT   CHAIN           1..179
FT                   /note="Peptidyl-prolyl cis-trans isomerase H"
FT                   /id="PRO_0000232955"
FT   DOMAIN          16..178
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
SQ   SEQUENCE   179 AA;  19606 MW;  8DBACF5948E326FF CRC64;
     MSSIDPPAGH TRPIVFFDIS IGDTPAGRIK MELFDDITPK TAENFRQLCT GEHRINSVPQ
     GYKKATFHRV IPQFMVQGGD FVRGDGTGSF SIYGAQFEDE NFKVKHTGPG LLSMANSGPN
     TNGCQFFITT APAEFLDGKH CVFGRVIDGL LTVRKIENVP TGANNRPKLQ VRIAECGEM