FKBP_CANGA
ID FKBP_CANGA Reviewed; 114 AA.
AC Q6FMA3;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 98.
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=CAGL0K09724g;
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: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family. FKBP1 subfamily.
CC {ECO:0000305}.
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DR EMBL; CR380957; CAG61604.1; -; Genomic_DNA.
DR RefSeq; XP_448641.1; XM_448641.1.
DR PDB; 5HT1; X-ray; 2.65 A; A=1-114.
DR PDB; 5HUA; X-ray; 1.30 A; A=1-114.
DR PDBsum; 5HT1; -.
DR PDBsum; 5HUA; -.
DR AlphaFoldDB; Q6FMA3; -.
DR SMR; Q6FMA3; -.
DR STRING; 5478.XP_448641.1; -.
DR EnsemblFungi; CAG61604; CAG61604; CAGL0K09724g.
DR GeneID; 2890244; -.
DR KEGG; cgr:CAGL0K09724g; -.
DR CGD; CAL0134605; FPR1.
DR VEuPathDB; FungiDB:CAGL0K09724g; -.
DR eggNOG; KOG0544; Eukaryota.
DR HOGENOM; CLU_013615_12_1_1; -.
DR InParanoid; Q6FMA3; -.
DR OMA; RVIAGWD; -.
DR Proteomes; UP000002428; Chromosome K.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Isomerase; Reference proteome; Rotamase.
FT CHAIN 1..114
FT /note="FK506-binding protein 1"
FT /id="PRO_0000233321"
FT DOMAIN 26..114
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT STRAND 2..4
FT /evidence="ECO:0007829|PDB:5HT1"
FT HELIX 6..8
FT /evidence="ECO:0007829|PDB:5HUA"
FT STRAND 10..15
FT /evidence="ECO:0007829|PDB:5HUA"
FT STRAND 28..37
FT /evidence="ECO:0007829|PDB:5HUA"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:5HUA"
FT TURN 46..50
FT /evidence="ECO:0007829|PDB:5HUA"
FT STRAND 53..56
FT /evidence="ECO:0007829|PDB:5HUA"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:5HUA"
FT HELIX 64..69
FT /evidence="ECO:0007829|PDB:5HUA"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:5HUA"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:5HUA"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:5HUA"
FT TURN 88..92
FT /evidence="ECO:0007829|PDB:5HUA"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:5HUA"
FT STRAND 104..113
FT /evidence="ECO:0007829|PDB:5HUA"
SQ SEQUENCE 114 AA; 12157 MW; 68C72F2294BCE84A CRC64;
MSETIEGGVK IDRLSPGDGK TFPKQGDLVT IHYTGTLENG QKFDSSVDRG SPFQCNIGVG
QVIKGWDAGI PKLSVGEKAR LTIPGPYAYG PRGFPGLIPP NATLIFDVEL LKVN
