ID S0DIH0_GIBF5 Unreviewed; 464 AA.
AC S0DIH0;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=FK506-binding protein {ECO:0000256|PIRNR:PIRNR001473};
DE EC=5.2.1.8 {ECO:0000256|PIRNR:PIRNR001473};
GN ORFNames=FFUJ_01248 {ECO:0000313|EMBL:CCT62219.1};
OS Gibberella fujikuroi (strain CBS 195.34 / IMI 58289 / NRRL A-6831) (Bakanae
OS and foot rot disease fungus) (Fusarium fujikuroi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=1279085 {ECO:0000313|EMBL:CCT62219.1, ECO:0000313|Proteomes:UP000016800};
RN [1] {ECO:0000313|Proteomes:UP000016800}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 195.34 / IMI 58289 / NRRL A-6831
RC {ECO:0000313|Proteomes:UP000016800};
RX PubMed=23825955; DOI=10.1371/journal.ppat.1003475;
RA Wiemann P., Sieber C.M., von Bargen K.W., Studt L., Niehaus E.M.,
RA Espino J.J., Huss K., Michielse C.B., Albermann S., Wagner D.,
RA Bergner S.V., Connolly L.R., Fischer A., Reuter G., Kleigrewe K., Bald T.,
RA Wingfield B.D., Ophir R., Freeman S., Hippler M., Smith K.M., Brown D.W.,
RA Proctor R.H., Munsterkotter M., Freitag M., Humpf H.U., Guldener U.,
RA Tudzynski B.;
RT "Deciphering the cryptic genome: genome-wide analyses of the rice pathogen
RT Fusarium fujikuroi reveal complex regulation of secondary metabolism and
RT novel metabolites.";
RL PLoS Pathog. 9:E1003475-E1003475(2013).
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; HF679023; CCT62219.1; -; Genomic_DNA.
DR AlphaFoldDB; S0DIH0; -.
DR STRING; 1279085.S0DIH0; -.
DR EnsemblFungi; CCT62219; CCT62219; FFUJ_01248.
DR VEuPathDB; FungiDB:FFUJ_01248; -.
DR HOGENOM; CLU_022297_3_1_1; -.
DR OrthoDB; 25281at2759; -.
DR Proteomes; UP000016800; Chromosome 1.
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:UP000016800};
KW Rotamase {ECO:0000256|PIRNR:PIRNR001473, ECO:0000256|PROSITE-
KW ProRule:PRU00277}.
FT DOMAIN 378..464
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
FT REGION 66..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 215..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 261..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 303..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..150
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..168
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 464 AA; 50611 MW; B94170957B3EBBC4 CRC64;
MSAVPGPVYG LEVPPGEILI PATMEFPASF RITMAAVDPT EEPEADSEGN IPTVPRSTLR
LVKRALPGLD EDEDDEIDDE YMKALLAGSD DEEDSDEEAN GGPSDPVKAK KQRQAAAIKK
LLESAQEESD EEMEDARPNG KAKGKAKATE EDEEEDDDSD DDSEEGADLE NFVICTLDTE
RNYQQPLDIT VNHGEKVFFV VTGTHTIYLT GNYIMDDDED DEDDEDEDDY DLSPDELEYA
LEGEESDESD ELDGVQDPRV QEIESDEEEA PKLVSVQKGK NKRAAEEATE GLDELISKDD
AKLSKKQQKK LKNNKGEAVA TEEKKDAKKV QFAKNLEQGP TGSAEKAKQG KATTGVKVVQ
GVTIDDRTIG NGRTVKNGDT VGVRYIGKLQ NGKQFDANKK GKPFSFKAGK GQVIKGWDIG
VIGMAIGGER RLTIPAHLAY GSRGLPGIPA NSTLIFDVKL LEIK
//
