ID   FKBP4_CRYNB             Reviewed;         405 AA.
AC   P0CP99; Q55TU1; Q5KIJ5;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   25-MAY-2022, entry version 47.
DE   RecName: Full=FK506-binding protein 4;
DE            EC=5.2.1.8 {ECO:0000250|UniProtKB:Q06205};
DE   AltName: Full=Histone proline isomerase {ECO:0000250|UniProtKB:Q06205};
DE   AltName: Full=Peptidyl-prolyl cis-trans isomerase;
DE            Short=PPIase;
DE   AltName: Full=Rotamase;
GN   Name=FPR4; OrderedLocusNames=CNBD3620;
OS   Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS   (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=283643;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B-3501A;
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(2005).
CC   -!- FUNCTION: PPIase that acts as a histone chaperone. Histone proline
CC       isomerase that increases the rate of cis-trans isomerization at
CC       prolines on the histone H3 N-terminal tail. Proline isomerization
CC       influences H3 methylation thereby regulating gene expression.
CC       {ECO:0000250|UniProtKB:Q06205}.
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         Evidence={ECO:0000250|UniProtKB:Q06205};
CC   -!- ACTIVITY REGULATION: Inhibited by both FK506 and rapamycin.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Binds to histones H3 and H4. {ECO:0000250|UniProtKB:Q06205}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q06205}.
CC   -!- SIMILARITY: Belongs to the FKBP-type PPIase family. FKBP3/4 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AAEY01000020; EAL21308.1; -; Genomic_DNA.
DR   RefSeq; XP_775955.1; XM_770862.1.
DR   AlphaFoldDB; P0CP99; -.
DR   SMR; P0CP99; -.
DR   EnsemblFungi; AAW42924; AAW42924; CND02730.
DR   EnsemblFungi; EAL21308; EAL21308; CNBD3620.
DR   GeneID; 4935751; -.
DR   KEGG; cnb:CNBD3620; -.
DR   VEuPathDB; FungiDB:CNBD3620; -.
DR   HOGENOM; CLU_022297_3_0_1; -.
DR   Proteomes; UP000001435; Chromosome 4.
DR   GO; GO:0005634; C:nucleus; 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   Chaperone; Isomerase; Nucleus; Rotamase.
FT   CHAIN           1..405
FT                   /note="FK506-binding protein 4"
FT                   /id="PRO_0000410209"
FT   DOMAIN          319..405
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT   REGION          49..117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          164..297
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        60..83
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        84..99
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        100..117
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        165..198
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        199..278
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   405 AA;  44436 MW;  6F4E8E57185E951D CRC64;
     MPLAMNLWSL TLLPGQQYPT YVRRDFQITN AALGEELRSK DGRSVVKVTH NPISQSMLES
     DDEWSDEDED EEILSEEDDG EMEVEEVKQK KGKKAEKVEE EDSEEEDEDE SDFEDELEET
     NVLCSLTAGK TEQASLNLTF VRGEVVVFEV TGDNVVHLMG NYIQQDEDSD DESDSDFDGE
     DDYSELYGSD DDLELDSEEE AAVAKITEIP DEPTPKTKKA LPAADKKPVP EAKPAQKRKA
     EELESPAKED AALSKAQKKK LAKKAKVEGE KAEEKPAAAA VAEKPATKKE AKAPQKKTLP
     SGLIIEDIKI GDGPVAKTGK RLGMRYIGKL TNGKQFDANT SGKPFSFVLG KGEVIRGWDE
     GLAGMAVGGE RRLTIPAALA YGNQKIPGIP KNSTLKFDVK LVSIN