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Database: UniProt
Entry: A0A2H3IEM0_9EURO
LinkDB: A0A2H3IEM0_9EURO
Original site: A0A2H3IEM0_9EURO 
ID   A0A2H3IEM0_9EURO        Unreviewed;       895 AA.
AC   A0A2H3IEM0;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 12.
DE   SubName: Full=Transcription factor {ECO:0000313|EMBL:PCG96016.1};
GN   ORFNames=PENO1_070500 {ECO:0000313|EMBL:PCG96016.1};
OS   Penicillium occitanis (nom. inval.).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=290292 {ECO:0000313|EMBL:PCG96016.1, ECO:0000313|Proteomes:UP000218381};
RN   [1] {ECO:0000313|EMBL:PCG96016.1, ECO:0000313|Proteomes:UP000218381}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CL100 {ECO:0000313|EMBL:PCG96016.1,
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   -!- SIMILARITY: Belongs to the FAH family. {ECO:0000256|ARBA:ARBA00010211}.
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:PCG96016.1}.
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DR   EMBL; NPFK01000225; PCG96016.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2H3IEM0; -.
DR   STRING; 290292.A0A2H3IEM0; -.
DR   Proteomes; UP000218381; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR   CDD; cd12148; fungal_TF_MHR; 1.
DR   Gene3D; 3.90.850.10; Fumarylacetoacetase-like, C-terminal domain; 1.
DR   InterPro; IPR011234; Fumarylacetoacetase-like_C.
DR   InterPro; IPR036663; Fumarylacetoacetase_C_sf.
DR   InterPro; IPR007219; Transcription_factor_dom_fun.
DR   PANTHER; PTHR11820; ACYLPYRUVASE; 1.
DR   PANTHER; PTHR11820:SF112; FUMARYLACETOACETATE HYDROLASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_1G02370)-RELATED; 1.
DR   Pfam; PF01557; FAA_hydrolase; 1.
DR   Pfam; PF04082; Fungal_trans; 1.
DR   SMART; SM00906; Fungal_trans; 1.
DR   SUPFAM; SSF56529; FAH; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000218381}.
FT   DOMAIN          504..576
FT                   /note="Transcription factor"
FT                   /evidence="ECO:0000259|SMART:SM00906"
SQ   SEQUENCE   895 AA;  99931 MW;  1FA625AA18DDC645 CRC64;
     MSTVWNRFVR FISTDDRELC GEPDSSVTDV GLALSKNEVV PVKVLDVASP LQDGGKFTSE
     TATIKKLLSP LAAKEVGTIR CIGMNYRDHV AEMKGTIPTV PEVFTKPSTT LIGPSDPIIL
     PKIAPDAVDL EVELAVVIGK DCKNVDAESA MDYVLGYTVA NDLTCRDVQN GILQWGYCKG
     YDSFCPIGPV LVSSKTIVDP AKLQLGSIVR GKTLQSSSTS ELIFKVPEII SYVSRGTTLP
     KGTLILTGTP AGIGHSHNPP LLRTDLNMQG WLDAEDADQL YLDTTSASLR VDSRQSLPPS
     NVGRLWNTRG APTYHGNSYF GYQSAADMIE VESPQLPTGM NNIGVRSTYD GRRTYSYRSE
     RGSYSHIWEL LGYLPREKAV VDKLVTAFIE HLNQVYDGLH EETFMTRYEA FWNRKWSDDD
     RSVIDLRWLS LLFIVLAFGE LLECPANASR DIRELSEEAS LQFYWASRTA ITLAMTFYGE
     STDAVRCGIL ITRYLVYLGR KTEAWLASSF SIRFAQAQGM HIDGESWGLP PKVLETRRRL
     WCSAHALDKY ISLGLGRPSA TSDKNSMEMK IRNVWIDDKA HDEAQVAMER PENDPTPSVF
     YIHQQKLSKI LGLIQEECFL LTPLTTSYTS YAKVLNLDEI LLAWAASLPE YFQVENPLTT
     MDNSRPYLYW QRLYLHFAFH FARVTLHKTY VLLDSIADRF EYSRDVCINS ASADLKLKLS
     ISNTTMADRL RAGATMHSLL SSGLVLGVLV VRDPLSARAA LILEDLTAYC EKQNSDPWAN
     EFALAEVRVI ELCISSARRS RQESGIMEER TTSTHSQDVN FVEANPPHQN GLPGLYRSPI
     MTTNPAAPGP VTNTENDPVD NDTWLENWFG PTRSLPEPGD FQSWERLIGS LAPLQ
//
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