ID   FKBP4_RHIO9             Reviewed;         382 AA.
AC   P0C1J6; I1BTK1;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 1.
DT   25-MAY-2022, entry version 62.
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=FKBP4; Synonyms=fpr4; ORFNames=RO3G_04236;
OS   Rhizopus delemar (strain RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL
OS   43880) (Mucormycosis agent) (Rhizopus arrhizus var. delemar).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX   NCBI_TaxID=246409;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL 43880;
RX   PubMed=19578406; DOI=10.1371/journal.pgen.1000549;
RA   Ma L.-J., Ibrahim A.S., Skory C., Grabherr M.G., Burger G., Butler M.,
RA   Elias M., Idnurm A., Lang B.F., Sone T., Abe A., Calvo S.E.,
RA   Corrochano L.M., Engels R., Fu J., Hansberg W., Kim J.-M., Kodira C.D.,
RA   Koehrsen M.J., Liu B., Miranda-Saavedra D., O'Leary S.,
RA   Ortiz-Castellanos L., Poulter R., Rodriguez-Romero J., Ruiz-Herrera J.,
RA   Shen Y.-Q., Zeng Q., Galagan J., Birren B.W., Cuomo C.A., Wickes B.L.;
RT   "Genomic analysis of the basal lineage fungus Rhizopus oryzae reveals a
RT   whole-genome duplication.";
RL   PLoS Genet. 5:E1000549-E1000549(2009).
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; CH476734; EIE79531.1; -; Genomic_DNA.
DR   AlphaFoldDB; P0C1J6; -.
DR   SMR; P0C1J6; -.
DR   STRING; 936053.P0C1J6; -.
DR   EnsemblFungi; EIE79531; EIE79531; RO3G_04236.
DR   VEuPathDB; FungiDB:RO3G_04236; -.
DR   eggNOG; KOG0552; Eukaryota.
DR   InParanoid; P0C1J6; -.
DR   OMA; CQEELIG; -.
DR   OrthoDB; 402681at2759; -.
DR   Proteomes; UP000009138; 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..382
FT                   /note="FK506-binding protein 4"
FT                   /id="PRO_0000244729"
FT   DOMAIN          295..382
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT   REGION          139..274
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        143..171
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        172..273
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   382 AA;  42904 MW;  519C1D8881CD048D CRC64;
     MSVQGFWGLQ LVPGKTYSQV VSAPFRITMA SLAADAEAGK RTSVSVLVDE KEFVLCTLVP
     NKIEQQPLDI TFVEGEEVTF SAKGQNNIHL TGNYVFQDDE DDEMGASMID SDEEDNVEDF
     LKKLPPNASK EDINKALLGL EVDEEIESDE EVESDEEIES DEEIESEEEE EEPVPVSKKR
     PAEEVKEIAS KKQKAEKKEQ PKKEKSKKEE PKKEEPKKEQ PKKEEPKKKE EPKKKEEPKK
     KEEPKKKEEP KKKEEPKKKE EPKKKEEPKK KITKLPNGLI IEDIKMGEGA SCKNGQRVGM
     RYIGKLTNGK VFDKNVSGKP FSFLLGRGEV IKGWDLGIAG MKAGGERKLT IPAPLAYGKR
     GAPPDIPKNA TLVFDVKLLS MK