ID   PPID_SCHPO              Reviewed;         356 AA.
AC   Q11004;
DT   06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 149.
DE   RecName: Full=40 kDa peptidyl-prolyl cis-trans isomerase;
DE            Short=PPIase;
DE            EC=5.2.1.8;
DE   AltName: Full=Cyclophilin-40;
DE            Short=CYP-40;
DE   AltName: Full=Rotamase;
GN   Name=wis2; Synonyms=cyp5; ORFNames=SPAC1B3.03c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8599928; DOI=10.1002/j.1460-2075.1996.tb00377.x;
RA   Weisman R., Creanor J., Fantes P.A.;
RT   "A multicopy suppressor of a cell cycle defect in S. pombe encodes a heat
RT   shock-inducible 40 kDa cyclophilin-like protein.";
RL   EMBO J. 15:447-456(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
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   -!- INDUCTION: By heat shock.
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase D
CC       subfamily. {ECO:0000305}.
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DR   EMBL; X91981; CAA63034.1; -; Genomic_DNA.
DR   EMBL; CU329670; CAB11232.1; -; Genomic_DNA.
DR   PIR; S62327; S62327.
DR   RefSeq; NP_594787.1; NM_001020215.2.
DR   AlphaFoldDB; Q11004; -.
DR   SMR; Q11004; -.
DR   BioGRID; 278998; 56.
DR   STRING; 4896.SPAC1B3.03c.1; -.
DR   iPTMnet; Q11004; -.
DR   MaxQB; Q11004; -.
DR   PaxDb; Q11004; -.
DR   PRIDE; Q11004; -.
DR   EnsemblFungi; SPAC1B3.03c.1; SPAC1B3.03c.1:pep; SPAC1B3.03c.
DR   GeneID; 2542541; -.
DR   KEGG; spo:SPAC1B3.03c; -.
DR   PomBase; SPAC1B3.03c; wis2.
DR   VEuPathDB; FungiDB:SPAC1B3.03c; -.
DR   eggNOG; KOG0546; Eukaryota.
DR   HOGENOM; CLU_012062_37_0_1; -.
DR   InParanoid; Q11004; -.
DR   OMA; CKDFGNK; -.
DR   PhylomeDB; Q11004; -.
DR   PRO; PR:Q11004; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0032991; C:protein-containing complex; NAS:PomBase.
DR   GO; GO:0016018; F:cyclosporin A binding; IBA:GO_Central.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:PomBase.
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   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   Coiled coil; Cytoplasm; Isomerase; Reference proteome; Repeat; Rotamase;
KW   Stress response; TPR repeat.
FT   CHAIN           1..356
FT                   /note="40 kDa peptidyl-prolyl cis-trans isomerase"
FT                   /id="PRO_0000064177"
FT   DOMAIN          6..166
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT   REPEAT          204..237
FT                   /note="TPR 1"
FT   REPEAT          259..292
FT                   /note="TPR 2"
FT   REPEAT          297..330
FT                   /note="TPR 3"
FT   COILED          328..354
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   356 AA;  40162 MW;  8418E3255F48B8DE CRC64;
     MSTYAYFKIS IDGKIQPTIY FELFDNVVPK TVKNFASLCN GFEKDGRCLT YKGSRFHRVI
     KNFMLQGGDF TRGNGTGGES IYGEKFEDEN FELKHDKPFL LSMANAGPNT NGSQFFITTV
     PTPHLDGKHV VFGKVIQGKS TVRTIENLET KNDDPVVPVV IEECGTCTKD QIEAPKPDVT
     GDSLEEFPDD YEGDKSETAI FKIASDLKGI ANKQFAQQNL DTAVAKWQKA LRYLMEYPVP
     NDDSKESPDF WKEYNALRYS IYANLALVAL KQNKPQEAIR NANIVIEASN STELEKQKAY
     YRLGCAQGLL KNFEESEKAL AKAGNDPAIS KKLAEIRQKK KDYKKRQQKA YAKMFQ