ID A0A0G2I3R3_9EURO Unreviewed; 495 AA.
AC A0A0G2I3R3;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=peptidylprolyl isomerase {ECO:0000256|PROSITE-ProRule:PRU00277};
DE EC=5.2.1.8 {ECO:0000256|PROSITE-ProRule:PRU00277};
GN ORFNames=EMCG_09232 {ECO:0000313|EMBL:KKZ64855.1};
OS Emmonsia crescens UAMH 3008.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Emmonsia.
OX NCBI_TaxID=1247875 {ECO:0000313|EMBL:KKZ64855.1, ECO:0000313|Proteomes:UP000034164};
RN [1] {ECO:0000313|Proteomes:UP000034164}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 3008 {ECO:0000313|Proteomes:UP000034164};
RX PubMed=26439490; DOI=10.1371/journal.pgen.1005493;
RA Munoz J.F., Gauthier G.M., Desjardins C.A., Gallo J.E., Holder J.,
RA Sullivan T.D., Marty A.J., Carmen J.C., Chen Z., Ding L., Gujja S.,
RA Magrini V., Misas E., Mitreva M., Priest M., Saif S., Whiston E.A.,
RA Young S., Zeng Q., Goldman W.E., Mardis E.R., Taylor J.W., McEwen J.G.,
RA Clay O.K., Klein B.S., Cuomo C.A.;
RT "The dynamic genome and transcriptome of the human fungal pathogen
RT Blastomyces and close relative Emmonsia.";
RL PLoS Genet. 11:E1005493-E1005493(2015).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKZ64855.1}.
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DR EMBL; LCZI01000730; KKZ64855.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G2I3R3; -.
DR VEuPathDB; FungiDB:EMCG_09232; -.
DR Proteomes; UP000034164; 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|PROSITE-ProRule:PRU00277,
KW ECO:0000313|EMBL:KKZ64855.1};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00277}.
FT DOMAIN 409..495
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
FT REGION 39..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 215..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..98
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..265
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 495 AA; 53750 MW; 622107D0B139874E CRC64;
MSSTHPVALY AVKVPPGGIL IPAGADASAM FRVTMAAIDP DSQPEFDAET EGKPPRATLK
IVRPPPGMDL EDDSDDDDYD EEDGDEDEDE EDSEDESNGG PSDPAKLLLA RQAAELKDII
DHCDDDSSDG ENFDLKAAIS RLIKGKDKAT WDGDDASDIS EGLEMEEVVV CTLDPTKNCQ
QTLDFVVGEN ERIFFKVTGT HPVYITGNYV MPSHGHQDMD DSSDEGDGYG EYDLSPDEDE
LDLMDEDEES DELDELNDPR ITEIDTDEEE SEKATAKKDK KDKKKGKKRP AEDSGDEGAN
LDDMMSKALK SGSEPATNGE TKLSKKQQKK LKKNNGEAVE IPVKTTAEPA KSDKKVQFAK
NLEQGPTPSP PKKDGDKKAS VTGNLGVKEV QGVKLDDKKL GTGRVAKKGD RVSMRYIGKL
ENGKVFDANK KGPPFSFKLG SGEVIKGWDI GIPGMAVGGE RRVTIPPHHA YGKKALPGIP
ANSKLIFDVK LLDIK
//
