ID   FKBP4_CHATD             Reviewed;         483 AA.
AC   G0SC91;
DT   16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT   16-MAR-2016, sequence version 2.
DT   25-MAY-2022, entry version 46.
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; ORFNames=CTHT_0056370;
OS   Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX   NCBI_TaxID=759272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1495 / CBS 144.50 / IMI 039719;
RX   PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA   Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA   Arumugam M., Bork P., Hurt E.;
RT   "Insight into structure and assembly of the nuclear pore complex by
RT   utilizing the genome of a eukaryotic thermophile.";
RL   Cell 146:277-289(2011).
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   -!- 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EGS19017.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; GL988045; EGS19017.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_006695962.1; XM_006695899.1.
DR   AlphaFoldDB; G0SC91; -.
DR   SMR; G0SC91; -.
DR   STRING; 759272.G0SC91; -.
DR   EnsemblFungi; EGS19017; EGS19017; CTHT_0056370.
DR   GeneID; 18259675; -.
DR   KEGG; cthr:CTHT_0056370; -.
DR   eggNOG; KOG0552; Eukaryota.
DR   eggNOG; KOG0605; Eukaryota.
DR   HOGENOM; CLU_005146_1_0_1; -.
DR   OrthoDB; 759391at2759; -.
DR   Proteomes; UP000008066; Unassembled WGS sequence.
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; Reference proteome; Rotamase.
FT   CHAIN           1..483
FT                   /note="FK506-binding protein 4"
FT                   /id="PRO_0000435811"
FT   DOMAIN          397..483
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT   REGION          41..171
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          208..371
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        47..61
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        69..94
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        95..121
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        130..152
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        153..167
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        215..233
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        274..371
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   483 AA;  53290 MW;  EC55ADF9847D4A55 CRC64;
     MSSLLPVAVY GLEVPPGDIL VPAQFEFPAT IRITMAAIDP TAEPETDGQG NVPTVPRSTL
     KLIKTTAEED DDEYLDIDGE DSEDDEESDD EEVNGGPSDP AKSKKARREA AIKKLLEATK
     EESDEEMEDA DAKPNGKGKK DSKGKAKASE SDDEKSDEDD EEGEPNFEEF VVCTLDTERT
     YQQPIDITIT EGEKVFFVVK GTHKVYLTGN YVLPEGQDEE DDEDEEDYSD EEYDLPHGIE
     LESDSDYESD ELDEIDGTPR IKEIDTDEEE EEAPKLVDTS KKGNKKRPAE EAENLDDLVA
     KDKKQAEKQK KLKNNKGEAV PAENKDVKKE GKSDKKVQFA KDLEQGPSGP AKDKLEKKEE
     KKDDKADLKK PSLGVKVVQG VTIDDRKLGT GRTVKSGDRV SLRYIGKLTN GKVFDANKKG
     APFTVRVGKG EVIKGWEIGL IGMQVGGERR LTIPPHLAYG SRAMPGIPAN STLVFDIKLL
     EIK