ID   FKBP6_DICDI             Reviewed;         366 AA.
AC   Q54Y27;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 103.
DE   RecName: Full=FK506-binding protein 6;
DE            EC=5.2.1.8;
DE   AltName: Full=Peptidyl-prolyl cis-trans isomerase;
DE            Short=PPIase;
DE   AltName: Full=Rotamase;
GN   Name=fkbp6; ORFNames=DDB_G0278455;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- FUNCTION: PPIases accelerate the folding of proteins by catalyzing the
CC       cis-trans isomerization of proline imidic peptide bonds in
CC       oligopeptides. {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   -!- SIMILARITY: Belongs to the FKBP-type PPIase family. {ECO:0000305}.
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DR   EMBL; AAFI02000023; EAL68400.1; -; Genomic_DNA.
DR   RefSeq; XP_642375.1; XM_637283.1.
DR   AlphaFoldDB; Q54Y27; -.
DR   SMR; Q54Y27; -.
DR   STRING; 44689.DDB0205465; -.
DR   PaxDb; Q54Y27; -.
DR   EnsemblProtists; EAL68400; EAL68400; DDB_G0278455.
DR   GeneID; 8621580; -.
DR   KEGG; ddi:DDB_G0278455; -.
DR   dictyBase; DDB_G0278455; -.
DR   eggNOG; KOG0543; Eukaryota.
DR   HOGENOM; CLU_757432_0_0_1; -.
DR   InParanoid; Q54Y27; -.
DR   OMA; CIEESKG; -.
DR   PhylomeDB; Q54Y27; -.
DR   PRO; PR:Q54Y27; -.
DR   Proteomes; UP000002195; Chromosome 3.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   Gene3D; 1.25.40.10; -; 1.
DR   Gene3D; 3.10.50.40; -; 1.
DR   InterPro; IPR046357; PPIase_dom_sf.
DR   InterPro; IPR001179; PPIase_FKBP_dom.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR001440; TPR_1.
DR   InterPro; IPR019734; TPR_repeat.
DR   Pfam; PF00254; FKBP_C; 1.
DR   Pfam; PF00515; TPR_1; 1.
DR   SMART; SM00028; TPR; 3.
DR   SUPFAM; SSF48452; SSF48452; 1.
DR   PROSITE; PS50059; FKBP_PPIASE; 1.
DR   PROSITE; PS50005; TPR; 2.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   3: Inferred from homology;
KW   Isomerase; Reference proteome; Repeat; Rotamase; TPR repeat.
FT   CHAIN           1..366
FT                   /note="FK506-binding protein 6"
FT                   /id="PRO_0000331285"
FT   DOMAIN          123..211
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT   REPEAT          227..260
FT                   /note="TPR 1"
FT   REPEAT          279..312
FT                   /note="TPR 2"
FT   REPEAT          314..347
FT                   /note="TPR 3"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          47..97
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        47..96
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   366 AA;  40987 MW;  89077DE043C7EDB3 CRC64;
     MNLSLPLNKD NSGNSGNSGN SGGSVCSSNN TLSPILSNSI LSSPISSPRL ISSSNNNNNN
     NNNNNNNNNN NNNNNNNNTI NSDSNNNNNI NNKPRKAGIQ LDSDGCLIKR IIKEGYGEIP
     PPRSIVTVHY EGYLSNQVLF DSSVQRNSPF TFQMGTKSVI DAIELSISTM KVGQEAEIVT
     TQRYAFGKLG LPPFIPPNVS VIYKIKLLSY KLKSNDFTNF ESLINKSKEE KEIGNQFFQK
     SNYKKSIRHY VKSIWILNDP EQTLGLNEME NKLLKDTLII LYLNLASCNI KLKDGKRGIS
     NCEKILELGG NTTAKFYYRM GQAYSLNKQY DSAKRCLVQA IRLEPNDKLL RDELENIKKL
     QEENNK