ID   FKBP3_CANGA             Reviewed;         437 AA.
AC   Q6FKH7;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=FK506-binding protein 3;
DE            EC=5.2.1.8;
DE   AltName: Full=Peptidyl-prolyl cis-trans isomerase;
DE            Short=PPIase;
DE   AltName: Full=Rotamase;
GN   Name=FPR3; OrderedLocusNames=CAGL0L11484g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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: Nucleus, nucleolus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the FKBP-type PPIase family. FKBP3/4 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; CR380958; CAG62241.1; -; Genomic_DNA.
DR   RefSeq; XP_449267.1; XM_449267.1.
DR   AlphaFoldDB; Q6FKH7; -.
DR   SMR; Q6FKH7; -.
DR   STRING; 5478.XP_449267.1; -.
DR   EnsemblFungi; CAG62241; CAG62241; CAGL0L11484g.
DR   GeneID; 2890967; -.
DR   KEGG; cgr:CAGL0L11484g; -.
DR   CGD; CAL0135700; FPR3.
DR   VEuPathDB; FungiDB:CAGL0L11484g; -.
DR   eggNOG; KOG0552; Eukaryota.
DR   HOGENOM; CLU_022297_3_1_1; -.
DR   InParanoid; Q6FKH7; -.
DR   OMA; CPPHMAY; -.
DR   Proteomes; UP000002428; Chromosome L.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   Isomerase; Nucleus; Reference proteome; Rotamase.
FT   CHAIN           1..437
FT                   /note="FK506-binding protein 3"
FT                   /id="PRO_0000233077"
FT   DOMAIN          351..437
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT   REGION          42..146
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          179..328
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        65..93
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        94..111
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        112..136
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        188..250
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        268..328
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   437 AA;  49671 MW;  DEAA67DE23626C91 CRC64;
     MSDMLPLATY SLNVLPYIPT PAIDIEMPVT VRITMAALDP EALDDQKQPS TLRIVKRNPN
     FDDEEYDDLL NGDYDEDEMA SDDEEEEEEE EEEEKPAKKS KKSKGKKKDE SEDEEEEEES
     DSDLDEEDDD DEFEEYVLAT LSPKTQYQQT LDLTIAPEEE IQFIVTGSYA ISLVGNYIKH
     PFDTPMGDMD DSEDEDGSDY DDELSDSYYN DQYSDDDAED SDEHDLTPDE DELAPAGSVE
     EIEASEEEES EEEEKKSKHK KHDHHHHHDH DHDHDHEHKS KNKKRKQEEE EPKKEHKDKK
     VKFKKDLEEG PTKKEKAESK KADKTPKRRT LEGGVVIEDR TVGDGPAAKK GDRVGMRYIG
     KLKNGKVFDK NTSGKPFVFK LGRGEVIKGW DVGVAGMSVG SERRIIIPAP YAYGKQALPG
     IPANSELTFD VKLVSIK