ID   PPIL4_SCHPO             Reviewed;         432 AA.
AC   Q9UUE4;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase cyp6;
DE            Short=PPIase cyp6;
DE            EC=5.2.1.8;
DE   AltName: Full=Rotamase cyp6;
GN   Name=cyp6; ORFNames=SPBC17G9.05;
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   INDUCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=16134115; DOI=10.1002/yea.1288;
RA   Pemberton T.J., Kay J.E.;
RT   "The cyclophilin repertoire of the fission yeast Schizosaccharomyces
RT   pombe.";
RL   Yeast 22:927-945(2005).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206, 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:16134115}.
CC   -!- INDUCTION: Induced during the meiotic cycle.
CC       {ECO:0000269|PubMed:16134115}.
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIL4
CC       subfamily. {ECO:0000305}.
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DR   EMBL; CU329671; CAB52803.1; -; Genomic_DNA.
DR   PIR; T39728; T39728.
DR   RefSeq; NP_595894.1; NM_001021801.2.
DR   AlphaFoldDB; Q9UUE4; -.
DR   SMR; Q9UUE4; -.
DR   BioGRID; 276486; 6.
DR   STRING; 4896.SPBC17G9.05.1; -.
DR   iPTMnet; Q9UUE4; -.
DR   MaxQB; Q9UUE4; -.
DR   PaxDb; Q9UUE4; -.
DR   PRIDE; Q9UUE4; -.
DR   EnsemblFungi; SPBC17G9.05.1; SPBC17G9.05.1:pep; SPBC17G9.05.
DR   GeneID; 2539942; -.
DR   KEGG; spo:SPBC17G9.05; -.
DR   PomBase; SPBC17G9.05; -.
DR   VEuPathDB; FungiDB:SPBC17G9.05; -.
DR   eggNOG; KOG0415; Eukaryota.
DR   HOGENOM; CLU_018791_2_0_1; -.
DR   InParanoid; Q9UUE4; -.
DR   OMA; APKCCEN; -.
DR   PhylomeDB; Q9UUE4; -.
DR   PRO; PR:Q9UUE4; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0000785; C:chromatin; IDA:PomBase.
DR   GO; GO:0005634; C:nucleus; IDA:PomBase.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; NAS:PomBase.
DR   GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:InterPro.
DR   GO; GO:1901407; P:regulation of phosphorylation of RNA polymerase II C-terminal domain; IBA:GO_Central.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IGI:PomBase.
DR   CDD; cd01921; cyclophilin_RRM; 1.
DR   Gene3D; 2.40.100.10; -; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   InterPro; IPR035542; CRIP.
DR   InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR   InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR   InterPro; IPR035538; Cyclophilin_PPIL4.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   PANTHER; PTHR45843; PTHR45843; 1.
DR   Pfam; PF00160; Pro_isomerase; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   PRINTS; PR00153; CSAPPISMRASE.
DR   SMART; SM00360; RRM; 1.
DR   SUPFAM; SSF50891; SSF50891; 1.
DR   SUPFAM; SSF54928; SSF54928; 1.
DR   PROSITE; PS50072; CSA_PPIASE_2; 1.
DR   PROSITE; PS50102; RRM; 1.
PE   1: Evidence at protein level;
KW   Isomerase; Nucleus; Phosphoprotein; Reference proteome; RNA-binding;
KW   Rotamase.
FT   CHAIN           1..432
FT                   /note="Peptidyl-prolyl cis-trans isomerase cyp6"
FT                   /id="PRO_0000232980"
FT   DOMAIN          1..168
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT   DOMAIN          244..322
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          330..432
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         206
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   432 AA;  50776 MW;  16FE19301626561C CRC64;
     MSVLIETTVG DLVIDLFVKE APKTCENFLK LCKLKYYNFC PFYNIQHNYT CQTGDPLGPT
     GDGGRCVWNV LNKGTRFFKA EFNPSLVHNK MGLVSMSTAT ISSRDDKLLV CGSQFIITLS
     DNLEGLDERY PIYGQVAEGF DTLLKINDAI CDEEGQPYRD IRIKHTIILD DPFEDPPDLV
     EPLRSPSPTP EQLATVRIGE NEQIESETSE DKLQREKEME AEAEAVTLEM IGDLPFAHVA
     PPENVLFVCK LNPVTQDEDL ELIFSRFGKI ISCQVIRDKE TGDSLQYAFI EFDNKESVEK
     AYFKMQNVLI DDSRIHVDFS QSVARYRQYY NSNRDRKRSS SRSDDREYHR RSDGRYDRSN
     YRDDYRHRRK ERDHRDDQSS FRNERFSNYY GDDRSYHKRR NTGNKNCDDH LRDKSPERRY
     RYDRRYRDDR YR