PPIH_CRYNB
ID PPIH_CRYNB Reviewed; 179 AA.
AC P0CP83; Q55L87; Q5KA96;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 45.
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=CNBJ0970;
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 -!- 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; AAEY01000049; EAL18455.1; -; Genomic_DNA.
DR RefSeq; XP_773102.1; XM_768009.1.
DR AlphaFoldDB; P0CP83; -.
DR SMR; P0CP83; -.
DR EnsemblFungi; AAW46023; AAW46023; CNJ02490.
DR EnsemblFungi; EAL18455; EAL18455; CNBJ0970.
DR GeneID; 4938437; -.
DR KEGG; cnb:CNBJ0970; -.
DR VEuPathDB; FungiDB:CNBJ0970; -.
DR HOGENOM; CLU_012062_4_3_1; -.
DR Proteomes; UP000001435; Chromosome 10.
DR GO; GO:0005634; C:nucleus; 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 Isomerase; Nucleus; Rotamase.
FT CHAIN 1..179
FT /note="Peptidyl-prolyl cis-trans isomerase H"
FT /id="PRO_0000410201"
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