ID   CYP9_SCHPO              Reviewed;         610 AA.
AC   O74942;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 159.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase 9;
DE            Short=PPIase cyp9;
DE            EC=5.2.1.8;
DE   AltName: Full=Cyclophilin 9;
DE   AltName: Full=Rotamase cyp9;
GN   Name=cyp9; ORFNames=SPCC553.04;
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 [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).
RN   [2]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RX   PubMed=18257517; DOI=10.1021/pr7006335;
RA   Wilson-Grady J.T., Villen J., Gygi S.P.;
RT   "Phosphoproteome analysis of fission yeast.";
RL   J. Proteome Res. 7:1088-1097(2008).
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:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC       {ECO:0000305}.
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DR   EMBL; CU329672; CAA19257.1; -; Genomic_DNA.
DR   PIR; T41399; T41399.
DR   RefSeq; NP_587769.1; NM_001022762.2.
DR   AlphaFoldDB; O74942; -.
DR   SMR; O74942; -.
DR   BioGRID; 276118; 2.
DR   STRING; 4896.SPCC553.04.1; -.
DR   iPTMnet; O74942; -.
DR   MaxQB; O74942; -.
DR   PaxDb; O74942; -.
DR   PRIDE; O74942; -.
DR   EnsemblFungi; SPCC553.04.1; SPCC553.04.1:pep; SPCC553.04.
DR   GeneID; 2539557; -.
DR   KEGG; spo:SPCC553.04; -.
DR   PomBase; SPCC553.04; cyp9.
DR   VEuPathDB; FungiDB:SPCC553.04; -.
DR   eggNOG; KOG0882; Eukaryota.
DR   HOGENOM; CLU_012062_31_0_1; -.
DR   InParanoid; O74942; -.
DR   OMA; GGMVEYW; -.
DR   PhylomeDB; O74942; -.
DR   PRO; PR:O74942; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; ISM:PomBase.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IBA:GO_Central.
DR   Gene3D; 2.130.10.10; -; 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; IPR044666; Cyclophilin_A-like.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   PANTHER; PTHR45625; PTHR45625; 1.
DR   Pfam; PF00160; Pro_isomerase; 1.
DR   PRINTS; PR00153; CSAPPISMRASE.
DR   SMART; SM00320; WD40; 4.
DR   SUPFAM; SSF50891; SSF50891; 1.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS00170; CSA_PPIASE_1; 1.
DR   PROSITE; PS50072; CSA_PPIASE_2; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 1.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   Isomerase; Nucleus; Phosphoprotein; Reference proteome; Repeat; Rotamase;
KW   WD repeat.
FT   CHAIN           1..610
FT                   /note="Peptidyl-prolyl cis-trans isomerase 9"
FT                   /id="PRO_0000358863"
FT   REPEAT          45..83
FT                   /note="WD 1"
FT   REPEAT          88..127
FT                   /note="WD 2"
FT   REPEAT          177..216
FT                   /note="WD 3"
FT   DOMAIN          453..607
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT   MOD_RES         13
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   610 AA;  69048 MW;  28D06D189C76DF3B CRC64;
     MMDGASPVDR DVSPVGLPKK RIKQNHDQVF LHNLPDAPRY TKSYMHNAEI YKCFPTKSNY
     ILSVSYDGYV KFWHKTPNGV EYIKEFHAHN AMLLSAELSQ DERLFITGAD DKSLKVFDVE
     SIDLVNIIDL EFLPKAICCF NSPSLKTSLI AVSSAESPLI FFFESGGDGE VLYTVKKHTA
     PVHCLRYLST LDCFLSIDIG GMVEYWSPEE PFQKPDTAEL FNMKSQTDLY IFKKQKSVPT
     SLEVSHFENF WSTISYPDCK VRVFDTKSGR AILELDENPS NAAKKVEALF EKEDTESSYY
     MSHVELGRRI AIERDIEKHG LTVGTTAIFD ESEKYLLYGS IVGIKVVSID NGTVVRIYGK
     DEAVRFTRLS LYQQAPKKSN LPSLDVIASN NPLVEESFQK DPTLFATAWK KQRFYLFSNM
     STKFTLSDRD VYNEQVLPVT NNEGRQENGN ILLGKAAIIH TTQGDISIKL YPEEAPKAVQ
     NFTTHAENGY YDNTIFHRII KNFMIQGGDP LGDGTGGESI WKKDFEDEIS PNLKHDRPFT
     VSMANSGPNT NGSQFFITTD LTPWLDGKHT IFARAYAGLD VVHRIEQGET DKYDRPLEPT
     KIINISIVYT