ID Q0UFK6_PHANO Unreviewed; 504 AA.
AC Q0UFK6;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 103.
DE RecName: Full=peptidylprolyl isomerase {ECO:0000256|PROSITE-ProRule:PRU00277};
DE EC=5.2.1.8 {ECO:0000256|PROSITE-ProRule:PRU00277};
GN ORFNames=SNOG_09458 {ECO:0000313|EMBL:EAT82723.1};
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614 {ECO:0000313|EMBL:EAT82723.1, ECO:0000313|Proteomes:UP000001055};
RN [1] {ECO:0000313|Proteomes:UP000001055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173
RC {ECO:0000313|Proteomes:UP000001055};
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G., Solomon P.S., Tan K.C., Schoch C.L., Spatafora J.W.,
RA Crous P.W., Kodira C., Birren B.W., Galagan J.E., Torriani S.F.,
RA McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
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, ECO:0000256|PROSITE-
CC 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; CH445339; EAT82723.1; -; Genomic_DNA.
DR RefSeq; XP_001799751.1; XM_001799699.1.
DR AlphaFoldDB; Q0UFK6; -.
DR STRING; 321614.Q0UFK6; -.
DR EnsemblFungi; SNOT_09458; SNOT_09458; SNOG_09458.
DR GeneID; 5976656; -.
DR KEGG; pno:SNOG_09458; -.
DR VEuPathDB; FungiDB:JI435_094580; -.
DR eggNOG; KOG0552; Eukaryota.
DR HOGENOM; CLU_022297_3_1_1; -.
DR InParanoid; Q0UFK6; -.
DR OMA; DEPNGGP; -.
DR OrthoDB; 25281at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
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|PROSITE-ProRule:PRU00277};
KW Reference proteome {ECO:0000313|Proteomes:UP000001055};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00277}.
FT DOMAIN 417..504
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
FT REGION 63..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..182
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..281
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..334
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..365
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..415
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 504 AA; 54561 MW; B16156E56ACEC63F CRC64;
MSGPVAAGVW GRRVPAGGIP ILASIDPSAA FRITMAALDP SAPAQTDEEN QVLRATLKLI
RVPTDFDDED DEDDYDPEDI EAITARLREA GALPAEELES SEEDDSENEK NGGPSDPVKA
KKAKKAALTK KMQQELEDEM EIDNSLTNGV NGKSKGKAKV TDDDDISDED EDEDDDDEEP
EEFVLCTLNP ENHYQQPLDI TVREGEEVYL CVNGTHDIYV TGNYIILPEQ EDSEDDDEDD
GLEQLGYDIG SDEDELEIDG MDEDESDELD DLEDPRITEV DSEEEEVPKL VATSKKANKK
RPAESEDDAT LDDLMSKANG DEKVSKKQAK KLKKNDGQAV AGAEPAKKAE KADAPSSDKK
KVQFAKNLEL GPTGSPLTKV EAPKAEAKKE AAKGPRVVSG VTVEDKKEGK GKAAKKGDRV
EMRYIGKLKN GKVFDSNKKG KPFAFKLGVG QVIKGWDVGV AGMTPGGERR LTIPAALAYG
KKGAPPDIPA NSDLIFDIKC ISVG
//
