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Database: UniProt
Entry: C4JFL3_UNCRE
LinkDB: C4JFL3_UNCRE
Original site: C4JFL3_UNCRE 
ID   C4JFL3_UNCRE            Unreviewed;       447 AA.
AC   C4JFL3;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   RecName: Full=FK506-binding protein {ECO:0000256|PIRNR:PIRNR001473};
DE            EC=5.2.1.8 {ECO:0000256|PIRNR:PIRNR001473};
GN   ORFNames=UREG_01027 {ECO:0000313|EMBL:EEP76178.1};
OS   Uncinocarpus reesii (strain UAMH 1704).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Uncinocarpus.
OX   NCBI_TaxID=336963 {ECO:0000313|EMBL:EEP76178.1, ECO:0000313|Proteomes:UP000002058};
RN   [1] {ECO:0000313|Proteomes:UP000002058}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 1704 {ECO:0000313|Proteomes:UP000002058};
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(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:0000256|ARBA:ARBA00002221}.
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:0000256|ARBA:ARBA00000971,
CC         ECO:0000256|PIRNR:PIRNR001473, ECO:0000256|PROSITE-ProRule:PRU00277};
CC   -!- SUBUNIT: Binds to histones H3 and H4. {ECO:0000256|ARBA:ARBA00011865}.
CC   -!- SIMILARITY: Belongs to the FKBP-type PPIase family. FKBP3/4 subfamily.
CC       {ECO:0000256|ARBA:ARBA00007838}.
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DR   EMBL; CH476615; EEP76178.1; -; Genomic_DNA.
DR   RefSeq; XP_002541511.1; XM_002541465.1.
DR   AlphaFoldDB; C4JFL3; -.
DR   STRING; 336963.C4JFL3; -.
DR   GeneID; 8438231; -.
DR   KEGG; ure:UREG_01027; -.
DR   VEuPathDB; FungiDB:UREG_01027; -.
DR   eggNOG; KOG0552; Eukaryota.
DR   HOGENOM; CLU_022297_3_1_1; -.
DR   InParanoid; C4JFL3; -.
DR   OMA; DEPNGGP; -.
DR   OrthoDB; 25281at2759; -.
DR   Proteomes; UP000002058; Unassembled WGS sequence.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.50.40; -; 1.
DR   Gene3D; 2.60.120.340; Nucleoplasmin core domain; 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   PANTHER; PTHR43811:SF19; 39 KDA FK506-BINDING NUCLEAR PROTEIN; 1.
DR   PANTHER; PTHR43811; FKBP-TYPE PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FKPA; 1.
DR   Pfam; PF00254; FKBP_C; 1.
DR   Pfam; PF17800; NPL; 1.
DR   PIRSF; PIRSF001473; FK506-bp_FPR3; 1.
DR   SUPFAM; SSF54534; FKBP-like; 1.
DR   PROSITE; PS50059; FKBP_PPIASE; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|PIRNR:PIRNR001473, ECO:0000256|PROSITE-
KW   ProRule:PRU00277}; Reference proteome {ECO:0000313|Proteomes:UP000002058};
KW   Rotamase {ECO:0000256|PIRNR:PIRNR001473, ECO:0000256|PROSITE-
KW   ProRule:PRU00277}.
FT   DOMAIN          361..447
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50059"
FT   REGION          1..97
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          173..362
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        37..60
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        178..217
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        218..263
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        327..356
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   447 AA;  48922 MW;  CEF734ABA3149309 CRC64;
     MAAIDPDALP EYEDEASSNK PPRATLRIIR APPGVGFDED DEDDSDYDLE DDDESSDDEA
     NGGPSDLTKA KLAKQAAKLK EMEDAMDEDD SDSDGDDVDL KAAISKLIKG KDKVTDDDGS
     ESSEGLELDE AVVCTLDPEK HYQQPLDFVI TEDERVFFKV TGTHAVYLTG NFVVPLDQAD
     EDESDEEDDD YDDYDLSPDE DELALMGEID EESDDLDDMA NPRIMEIDTD DDEKVSSKAP
     KKDGKGKNKR PAEDSEENLD DMMSKTMKPA TNGEPPLSKK QQKKLKKNNG QAVEAQQQAP
     AAAKTDKKVQ FAKNLEQGPS GSAQQKKEAP KQEEPKSTVK EVQGVKIEDK KTGKGPVAKK
     GNRVSMRYIG KLENGKVFDS NKKGKPFSFK IGAGEVIKGW DIGIPGMAVG SERRITVPSH
     LAYGKSSLPG IPANSKLIFD VKLLEIK
//
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