ID A0A2H3IS40_9EURO Unreviewed; 487 AA.
AC A0A2H3IS40;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Transcription factor Jun {ECO:0000313|EMBL:PCH08277.1};
GN ORFNames=PENO1_007710 {ECO:0000313|EMBL:PCH08277.1};
OS Penicillium occitanis (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=290292 {ECO:0000313|EMBL:PCH08277.1, ECO:0000313|Proteomes:UP000218381};
RN [1] {ECO:0000313|EMBL:PCH08277.1, ECO:0000313|Proteomes:UP000218381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL100 {ECO:0000313|EMBL:PCH08277.1,
RC ECO:0000313|Proteomes:UP000218381};
RX PubMed=28951729; DOI=10.3389/fmicb.2017.01627;
RA Bravo-Ruiz G., Sassi A.H., Marcet-Houben M., Di Pietro A., Gargouri A.,
RA Gabaldon T., Roncero M.I.G.;
RT "Regulatory Mechanisms of a Highly Pectinolytic Mutant of Penicillium
RT occitanis and Functional Analysis of a Candidate Gene in the Plant Pathogen
RT Fusarium oxysporum.";
RL Front. Microbiol. 8:1627-1627(2017).
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:PCH08277.1}.
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DR EMBL; NPFK01000010; PCH08277.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3IS40; -.
DR STRING; 290292.A0A2H3IS40; -.
DR Proteomes; UP000218381; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR CDD; cd14687; bZIP_ATF2; 1.
DR Gene3D; 1.20.5.170; -; 1.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR002112; Leuzip_Jun.
DR InterPro; IPR021755; TF_Aft1_HRA.
DR InterPro; IPR021756; TF_Aft1_HRR.
DR InterPro; IPR020956; TF_Aft1_OSM.
DR PANTHER; PTHR19304; CYCLIC-AMP RESPONSE ELEMENT BINDING PROTEIN; 1.
DR PANTHER; PTHR19304:SF43; TRANSCRIPTION FACTOR ATF1-RELATED; 1.
DR Pfam; PF11786; Aft1_HRA; 1.
DR Pfam; PF11787; Aft1_HRR; 1.
DR Pfam; PF11785; Aft1_OSA; 1.
DR Pfam; PF00170; bZIP_1; 1.
DR PRINTS; PR00043; LEUZIPPRJUN.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; Leucine zipper domain; 1.
DR PROSITE; PS50217; BZIP; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000218381}.
FT DOMAIN 376..439
FT /note="BZIP"
FT /evidence="ECO:0000259|PROSITE:PS50217"
FT REGION 1..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 142..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 253..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 401..435
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 13..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..300
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..380
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 487 AA; 51626 MW; 888F7989106BC33A CRC64;
MSAAVAQRAP LGRTSSPMDT KNIMKSEDSS ATTKDQKPAT DTEASQSIPP PPRPAASGPG
DTPDYFNSLH NPFSLEPNPF EQSFGNPSAE TPGKSLLPPV ASITSPALPG ASSAGYNWPN
SLRSGPLSPA MLAGPTGSDY FDSIGRGFPT PNESSLRTGL TPGGGGSMFP APSPNTQAIL
SQLQSGGATP STLEFHRTAL NAAKRSGFNV PTSNPTSEPE QLQNMDKKTA PPIVDQFTHH
DAADAANGLF MLAKGGQPSN DAFSATNKPA DIPDTKRSTR NAHNSVSSGR EMTAEGSDTQ
GEQAKPAAKG KGKKNTPAKQ TSSANGRRKA EEAPKGSNKR AKTNSGPMEV TPEEESDDDD
MKDDLNGKDP KKMTDEEKRK NFLERNRVAA LKCRQRKKQW LANLQAKVEL FTTENDALTA
TVTQLREEIV NLKTLLLAHK DCPVSQAQGL GPLIMNGMSA GFDPHPYNLA SNMAMQPGAP
MAQAIRR
//
