ID   FKBP_KLULA              Reviewed;         114 AA.
AC   Q6CX30;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=FK506-binding protein 1;
DE            Short=FKBP;
DE            EC=5.2.1.8;
DE   AltName: Full=Peptidyl-prolyl cis-trans isomerase;
DE            Short=PPIase;
DE   AltName: Full=Rapamycin-binding protein;
GN   Name=FPR1; OrderedLocusNames=KLLA0A11704g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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   -!- ACTIVITY REGULATION: Inhibited by both FK506 and rapamycin.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the FKBP-type PPIase family. FKBP1 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; CR382121; CAH03097.1; -; Genomic_DNA.
DR   RefSeq; XP_451509.1; XM_451509.1.
DR   AlphaFoldDB; Q6CX30; -.
DR   SMR; Q6CX30; -.
DR   STRING; 28985.XP_451509.1; -.
DR   EnsemblFungi; CAH03097; CAH03097; KLLA0_A11704g.
DR   GeneID; 2896522; -.
DR   KEGG; kla:KLLA0_A11704g; -.
DR   eggNOG; KOG0544; Eukaryota.
DR   HOGENOM; CLU_013615_12_1_1; -.
DR   InParanoid; Q6CX30; -.
DR   OMA; RVIAGWD; -.
DR   Proteomes; UP000000598; Chromosome A.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005527; F:macrolide binding; IEA:EnsemblFungi.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006325; P:chromatin organization; IEA:EnsemblFungi.
DR   GO; GO:0006457; P:protein folding; IEA:EnsemblFungi.
DR   GO; GO:1901710; P:regulation of homoserine biosynthetic process; IEA:EnsemblFungi.
DR   Gene3D; 3.10.50.40; -; 1.
DR   InterPro; IPR046357; PPIase_dom_sf.
DR   InterPro; IPR001179; PPIase_FKBP_dom.
DR   Pfam; PF00254; FKBP_C; 1.
DR   PROSITE; PS50059; FKBP_PPIASE; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Isomerase; Reference proteome; Rotamase.
FT   CHAIN           1..114
FT                   /note="FK506-binding protein 1"
FT                   /id="PRO_0000233328"
FT   DOMAIN          26..114
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
SQ   SEQUENCE   114 AA;  12211 MW;  CC97C384D69C2B15 CRC64;
     MSETIEGNVQ ILRLSPGDST NFPKPGDLVT IHYTGTLENG QKFDSSVDRG SPFQCNIGVG
     QVIKGWDAAI PKLSVGEKAR LTIPGPYAYG PRGFPGLIPP NATLVFDVEL LKIN