ID   PPID_AMAMU              Reviewed;         371 AA.
AC   Q5U8Z7;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase D;
DE            Short=PPIase D;
DE            EC=5.2.1.8;
DE   AltName: Full=Rotamase D;
GN   Name=Cyp40;
OS   Amanita muscaria (Fly agaric).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Amanitaceae; Amanita.
OX   NCBI_TaxID=41956;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=16159334; DOI=10.1111/j.1469-8137.2005.01518.x;
RA   Schrey S.D., Schellhammer M., Ecke M., Hampp R., Tarkka M.T.;
RT   "Mycorrhiza helper bacterium Streptomyces AcH 505 induces differential gene
RT   expression in the ectomycorrhizal fungus Amanita muscaria.";
RL   New Phytol. 168:205-216(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: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase D
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AY773481; AAV40687.1; -; mRNA.
DR   AlphaFoldDB; Q5U8Z7; -.
DR   SMR; Q5U8Z7; -.
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; 1.25.40.10; -; 1.
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   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   Pfam; PF00160; Pro_isomerase; 1.
DR   PRINTS; PR00153; CSAPPISMRASE.
DR   SUPFAM; SSF48452; SSF48452; 1.
DR   SUPFAM; SSF50891; SSF50891; 1.
DR   PROSITE; PS00170; CSA_PPIASE_1; 1.
DR   PROSITE; PS50072; CSA_PPIASE_2; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Isomerase; Repeat; Rotamase; TPR repeat.
FT   CHAIN           1..371
FT                   /note="Peptidyl-prolyl cis-trans isomerase D"
FT                   /id="PRO_0000232940"
FT   DOMAIN          8..172
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT   REPEAT          212..245
FT                   /note="TPR 1"
FT   REPEAT          265..303
FT                   /note="TPR 2"
FT   REPEAT          308..341
FT                   /note="TPR 3"
FT   REGION          175..202
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   371 AA;  40735 MW;  E811F5099217B699 CRC64;
     MDDRPIVFFD IAIGGQLAGR VAFRLYSDLV PKTAENFRAL CTGEKGLGQS GKPLWYKGSA
     FHRVIKGFMC QGGDFTAGNG TGGESIYGEK FEDEGFPVHH SRPFLLSMAN AGPNTNGSQF
     FITVSATPHL DGKHVVFGEV IKGRSVVRTI ENNPATNGDV PKEPVVIADC GQLSSDDPFL
     AERTSTDGDP YEDYPDDEDQ ELGNPETVLQ IAKTIREVAN RLYKQGDISG ALQKYSKSIR
     YLDVHQELPE NSPPDLNEQY KSLLAPLLLN SALAAIRIEP HSAANAMNAV ANTSRALNRL
     ELSNADKAKA YYRRGLAKTI MRDEVGAEQD LKTANELLPE DGAIAAELAK IIQKKKEQRE
     REKKAYKKMF A