ID   PPID_NEUCR              Reviewed;         375 AA.
AC   Q9P3X9;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 135.
DE   RecName: Full=41 kDa peptidyl-prolyl cis-trans isomerase;
DE            Short=PPIase;
DE            EC=5.2.1.8;
DE   AltName: Full=Cyclophilin-41;
DE            Short=CyP41;
DE   AltName: Full=Rotamase;
GN   Name=cyp41; ORFNames=NCU03853;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH CYPBP37.
RC   STRAIN=74A;
RX   PubMed=14568539; DOI=10.1016/j.jmb.2003.09.003;
RA   Faou P., Tropschug M.;
RT   "A novel binding protein for a member of CyP40-type Cyclophilins: N.crassa
RT   CyPBP37, a growth and thiamine regulated protein homolog to yeast Thi4p.";
RL   J. Mol. Biol. 333:831-844(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
CC   -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC       cis-trans isomerization of proline imidic peptide bonds in
CC       oligopeptides.
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   -!- SUBUNIT: Interacts with CyPBP37. {ECO:0000269|PubMed:14568539}.
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; AJ292563; CAC00484.1; -; mRNA.
DR   EMBL; CM002241; EAA26627.1; -; Genomic_DNA.
DR   RefSeq; XP_955863.1; XM_950770.2.
DR   AlphaFoldDB; Q9P3X9; -.
DR   SMR; Q9P3X9; -.
DR   STRING; 5141.EFNCRP00000003630; -.
DR   PRIDE; Q9P3X9; -.
DR   EnsemblFungi; EAA26627; EAA26627; NCU03853.
DR   GeneID; 3872010; -.
DR   KEGG; ncr:NCU03853; -.
DR   VEuPathDB; FungiDB:NCU03853; -.
DR   HOGENOM; CLU_012062_37_0_1; -.
DR   InParanoid; Q9P3X9; -.
DR   OMA; CKDFGNK; -.
DR   Proteomes; UP000001805; Chromosome 5, Linkage Group VI.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
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; 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   InterPro; IPR019734; TPR_repeat.
DR   Pfam; PF00160; Pro_isomerase; 1.
DR   PRINTS; PR00153; CSAPPISMRASE.
DR   SMART; SM00028; TPR; 2.
DR   SUPFAM; SSF48452; SSF48452; 1.
DR   SUPFAM; SSF50891; SSF50891; 1.
DR   PROSITE; PS00170; CSA_PPIASE_1; 1.
DR   PROSITE; PS50072; CSA_PPIASE_2; 1.
DR   PROSITE; PS50005; TPR; 2.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Isomerase; Reference proteome; Repeat; Rotamase; TPR repeat.
FT   CHAIN           1..375
FT                   /note="41 kDa peptidyl-prolyl cis-trans isomerase"
FT                   /id="PRO_0000064156"
FT   DOMAIN          15..178
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT   REPEAT          222..255
FT                   /note="TPR 1"
FT   REPEAT          274..307
FT                   /note="TPR 2"
FT   REPEAT          312..345
FT                   /note="TPR 3"
SQ   SEQUENCE   375 AA;  40571 MW;  F5A1B3C078800994 CRC64;
     MSSTDDVKQA RSRVFFDITI GGKAAGRIVF ELYNDIVPKT AENFRALCTG EKGVGKLGKP
     LHYKGSTFHR VIKQFMIQGG DFTAGNGTGG ESIYGAKFED ENFQLKHDRP FLLSMANAGP
     GTNGSQFFVT TVPTPHLDGK HVVFGEVLSG KSVVRQIENL KTQGDKPTKD AVIADCGELS
     GDAAVSADTK TADAYGDEYE DFPEDEATDG QPLSASKILK IATDCKDFGN KAFKAGDLPV
     ALDKYQKGLR YLNEDPELDN EPADTKQKLD ALRVSLNSNA ALMNMKLSAW DECIRSADGA
     LAVATISDKD RAKALYRRGY AQVRIKDEDS ALTSLEEAKK LAPEDGAIVN ELAAVKKAAA
     ARMAKEKAAY KKFFS