ID A0A1F5LA00_9EURO Unreviewed; 479 AA.
AC A0A1F5LA00;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=FK506-binding protein {ECO:0000256|PIRNR:PIRNR001473};
DE EC=5.2.1.8 {ECO:0000256|PIRNR:PIRNR001473};
GN ORFNames=PENARI_c018G07493 {ECO:0000313|EMBL:OGE50034.1};
OS Penicillium arizonense.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1835702 {ECO:0000313|EMBL:OGE50034.1, ECO:0000313|Proteomes:UP000177622};
RN [1] {ECO:0000313|EMBL:OGE50034.1, ECO:0000313|Proteomes:UP000177622}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 141311 {ECO:0000313|EMBL:OGE50034.1,
RC ECO:0000313|Proteomes:UP000177622};
RX PubMed=27739446; DOI=10.1038/srep35112;
RA Grijseels S., Nielsen J.C., Randelovic M., Nielsen J., Nielsen K.F.,
RA Workman M., Frisvad J.C.;
RT "Penicillium arizonense, a new, genome sequenced fungal species, reveals a
RT high chemical diversity in secreted metabolites.";
RL Sci. Rep. 6:35112-35112(2016).
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}.
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:OGE50034.1}.
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DR EMBL; LXJU01000018; OGE50034.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5LA00; -.
DR STRING; 1835702.A0A1F5LA00; -.
DR OrthoDB; 25281at2759; -.
DR Proteomes; UP000177622; 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:UP000177622};
KW Rotamase {ECO:0000256|PIRNR:PIRNR001473, ECO:0000256|PROSITE-
KW ProRule:PRU00277}.
FT DOMAIN 393..479
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
FT REGION 41..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 214..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 306..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..96
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..268
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..294
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..350
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 479 AA; 52053 MW; 7D4EA1B5A8AD0F51 CRC64;
MSAVQPVAVY ALRVPPGAMV AAVPNAAASF RISMAAIDPD EVPEYEDDAD SSKPARATLK
IVRTPPGLDL DEEDSDDEDY SDEDEEEDSD EEEETNGGPS DKEKARKLKE AAAMKDLEDA
MEEDSDEGDD EDFDLKAAIS KLIKGKGPAL DDEDDESEEG LELDENVICT LSPTQNCQQT
LDITVCEGEP VFFKVTGNHT VFLTGNYVIG LDEGHDHDHD HDDEDDEDDY DLSPDEDELD
MDEIMAMQDD DESDDLDEMD DPRVTEVDSE EEAEAPKLVE AKKGKNKRAA EEEVSLDDLM
AKANKAKSTK AEEPALTKAQ QKKLKKNNGD AAAVEPEAKK EAKTDKKVQF AKNLEQGPTP
SGDKPTGSLG VKEVRGVKMD DKKLGKGVAA KSGNVVAMRY IGKLEDGKVF DSNKKGKPFT
FKLGKGEVIK GWDIGVAGMA VGGERRISIP PSLAYGKKAL PGIPANSKLI FDVKLLEIK
//
