FKBPH_SCHPO
ID FKBPH_SCHPO Reviewed; 362 AA.
AC Q10175;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Probable peptidyl-prolyl cis-trans isomerase C27F1.06c;
DE Short=PPIase;
DE EC=5.2.1.8;
DE AltName: Full=Rotamase;
GN ORFNames=SPAC27F1.06c;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-69 AND SER-177, AND
RP IDENTIFICATION BY 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 -!- SIMILARITY: Belongs to the FKBP-type PPIase family. FKBP3/4 subfamily.
CC {ECO:0000305}.
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DR EMBL; CU329670; CAA93295.1; -; Genomic_DNA.
DR PIR; T38464; T38464.
DR RefSeq; NP_594535.1; NM_001019964.2.
DR AlphaFoldDB; Q10175; -.
DR SMR; Q10175; -.
DR BioGRID; 277981; 22.
DR STRING; 4896.SPAC27F1.06c.1; -.
DR iPTMnet; Q10175; -.
DR MaxQB; Q10175; -.
DR PaxDb; Q10175; -.
DR PRIDE; Q10175; -.
DR EnsemblFungi; SPAC27F1.06c.1; SPAC27F1.06c.1:pep; SPAC27F1.06c.
DR GeneID; 2541479; -.
DR KEGG; spo:SPAC27F1.06c; -.
DR PomBase; SPAC27F1.06c; -.
DR VEuPathDB; FungiDB:SPAC27F1.06c; -.
DR eggNOG; KOG0552; Eukaryota.
DR HOGENOM; CLU_022297_3_0_1; -.
DR InParanoid; Q10175; -.
DR OMA; YVKYVCM; -.
DR PhylomeDB; Q10175; -.
DR Reactome; R-SPO-166208; mTORC1-mediated signalling.
DR Reactome; R-SPO-2025928; Calcineurin activates NFAT.
DR PRO; PR:Q10175; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; HDA:PomBase.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; EXP:PomBase.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IBA:GO_Central.
DR GO; GO:0006334; P:nucleosome assembly; ISO:PomBase.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IBA:GO_Central.
DR Gene3D; 3.10.50.40; -; 1.
DR InterPro; IPR041232; NPL.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR InterPro; IPR023566; PPIase_Fpr3/Fpr4-like.
DR Pfam; PF00254; FKBP_C; 1.
DR Pfam; PF17800; NPL; 1.
DR PIRSF; PIRSF001473; FK506-bp_FPR3; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
PE 1: Evidence at protein level;
KW Isomerase; Phosphoprotein; Reference proteome; Rotamase.
FT CHAIN 1..362
FT /note="Probable peptidyl-prolyl cis-trans isomerase
FT C27F1.06c"
FT /id="PRO_0000075316"
FT DOMAIN 276..362
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT REGION 144..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..187
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..250
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 69
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 362 AA; 40540 MW; 88F1785FB95A7B8B CRC64;
MSKEETLYSV KVDQERVPLF DEDFYKGFRS ELSVRFTMAA LDPRAKSNDA VTVNVITRLE
HPEEDGEESD EELFQEEKFT LCTLKKGSVY QQPIDIIFSP GEEVFFERVG GDIPVYLSGT
CIITNIPEEE DSSDLENDFL YGADEFSSDE EEMDDISVTS SEEEEEENGA RIEELNSDEE
DAEQAEEEIL EKPVPKDEVA EKHSKDKLKK EEKEKKTAVD VSDSVNGKKR KTEPAGEGEQ
TEKKSKSTKT YPKQVLEGNV TVQDKVKGDG PAAKRKKRVS MRYIGRLTNG KVFDKNITGK
PFTFNLGLEE VIKGWDVGIV GMQVGGERTI HIPAAMAYGS KRLPGIPANS DLVFDVKLLA
VN
