ID   FKBP_CRYNH              Reviewed;         108 AA.
AC   O94746; J9VFP5;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 79.
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=FRR1; ORFNames=CNAG_03682;
OS   Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 /
OS   CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=235443;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=H99 / ATCC 208821 / CBS 10515 / FGSC 9487;
RX   PubMed=10330150; DOI=10.1128/mcb.19.6.4101;
RA   Cruz M.C., Cavallo L.M., Goerlach J.M., Cox G., Perfect J.R.,
RA   Cardenas M.E., Heitman J.;
RT   "Rapamycin antifungal action is mediated via conserved complexes with
RT   FKBP12 and TOR kinase homologs in Cryptococcus neoformans.";
RL   Mol. Cell. Biol. 19:4101-4112(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H99 / ATCC 208821 / CBS 10515 / FGSC 9487;
RX   PubMed=24743168; DOI=10.1371/journal.pgen.1004261;
RA   Janbon G., Ormerod K.L., Paulet D., Byrnes E.J. III, Yadav V.,
RA   Chatterjee G., Mullapudi N., Hon C.-C., Billmyre R.B., Brunel F.,
RA   Bahn Y.-S., Chen W., Chen Y., Chow E.W.L., Coppee J.-Y., Floyd-Averette A.,
RA   Gaillardin C., Gerik K.J., Goldberg J., Gonzalez-Hilarion S., Gujja S.,
RA   Hamlin J.L., Hsueh Y.-P., Ianiri G., Jones S., Kodira C.D., Kozubowski L.,
RA   Lam W., Marra M., Mesner L.D., Mieczkowski P.A., Moyrand F., Nielsen K.,
RA   Proux C., Rossignol T., Schein J.E., Sun S., Wollschlaeger C., Wood I.A.,
RA   Zeng Q., Neuveglise C., Newlon C.S., Perfect J.R., Lodge J.K., Idnurm A.,
RA   Stajich J.E., Kronstad J.W., Sanyal K., Heitman J., Fraser J.A.,
RA   Cuomo C.A., Dietrich F.S.;
RT   "Analysis of the genome and transcriptome of Cryptococcus neoformans var.
RT   grubii reveals complex RNA expression and microevolution leading to
RT   virulence attenuation.";
RL   PLoS Genet. 10:E1004261-E1004261(2014).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AFR93187.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AF097889; AAD16172.1; -; mRNA.
DR   EMBL; AF097888; AAD16171.1; -; Genomic_DNA.
DR   EMBL; CP003821; AFR93187.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; XP_012047386.1; XM_012191996.1.
DR   PDB; 6TZ8; X-ray; 3.30 A; C/F=2-108.
DR   PDBsum; 6TZ8; -.
DR   AlphaFoldDB; O94746; -.
DR   SMR; O94746; -.
DR   SwissPalm; O94746; -.
DR   PRIDE; O94746; -.
DR   EnsemblFungi; AFR93187; AFR93187; CNAG_03682.
DR   GeneID; 23887158; -.
DR   HOGENOM; CLU_013615_12_1_1; -.
DR   Proteomes; UP000010091; Chromosome 2.
DR   GO; GO:0005737; C:cytoplasm; 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; 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; Rotamase.
FT   CHAIN           1..108
FT                   /note="FK506-binding protein 1"
FT                   /id="PRO_0000233323"
FT   DOMAIN          20..108
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT   STRAND          3..9
FT                   /evidence="ECO:0007829|PDB:6TZ8"
FT   STRAND          22..26
FT                   /evidence="ECO:0007829|PDB:6TZ8"
FT   STRAND          28..30
FT                   /evidence="ECO:0007829|PDB:6TZ8"
FT   STRAND          36..39
FT                   /evidence="ECO:0007829|PDB:6TZ8"
FT   HELIX           40..42
FT                   /evidence="ECO:0007829|PDB:6TZ8"
FT   STRAND          47..50
FT                   /evidence="ECO:0007829|PDB:6TZ8"
FT   TURN            51..54
FT                   /evidence="ECO:0007829|PDB:6TZ8"
FT   HELIX           58..63
FT                   /evidence="ECO:0007829|PDB:6TZ8"
FT   HELIX           64..66
FT                   /evidence="ECO:0007829|PDB:6TZ8"
FT   STRAND          72..77
FT                   /evidence="ECO:0007829|PDB:6TZ8"
FT   HELIX           79..81
FT                   /evidence="ECO:0007829|PDB:6TZ8"
FT   TURN            82..86
FT                   /evidence="ECO:0007829|PDB:6TZ8"
FT   STRAND          89..92
FT                   /evidence="ECO:0007829|PDB:6TZ8"
FT   STRAND          98..107
FT                   /evidence="ECO:0007829|PDB:6TZ8"
SQ   SEQUENCE   108 AA;  11608 MW;  40BC60788B0BF26D CRC64;
     MGVTVENISA GDGKTFPQPG DNVTIHYVGT LLDGSKFDSS RDRGTPFVCR IGQGQVIRGW
     DEGVPQLSVG QKANLICTPD YAYGARGFPP VIPPNSTLKF EVELLKVN