ID   A0A319DBK2_9EURO        Unreviewed;       949 AA.
AC   A0A319DBK2;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=PLP-dependent transferase {ECO:0000313|EMBL:PYH94534.1};
GN   ORFNames=BO71DRAFT_325194 {ECO:0000313|EMBL:PYH94534.1};
OS   Aspergillus ellipticus CBS 707.79.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1448320 {ECO:0000313|EMBL:PYH94534.1, ECO:0000313|Proteomes:UP000247810};
RN   [1] {ECO:0000313|EMBL:PYH94534.1, ECO:0000313|Proteomes:UP000247810}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 707.79 {ECO:0000313|EMBL:PYH94534.1,
RC   ECO:0000313|Proteomes:UP000247810};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
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DR   EMBL; KZ825869; PYH94534.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A319DBK2; -.
DR   STRING; 1448320.A0A319DBK2; -.
DR   Proteomes; UP000247810; Unassembled WGS sequence.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0016829; F:lyase activity; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR   CDD; cd12148; fungal_TF_MHR; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR001597; ArAA_b-elim_lyase/Thr_aldolase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   InterPro; IPR007219; Transcription_factor_dom_fun.
DR   PANTHER; PTHR47338:SF19; ZN(II)2CYS6 TRANSCRIPTION FACTOR (EUROFUNG); 1.
DR   PANTHER; PTHR47338; ZN(II)2CYS6 TRANSCRIPTION FACTOR (EUROFUNG)-RELATED; 1.
DR   Pfam; PF01212; Beta_elim_lyase; 1.
DR   Pfam; PF04082; Fungal_trans; 1.
DR   SMART; SM00906; Fungal_trans; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   4: Predicted;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Reference proteome {ECO:0000313|Proteomes:UP000247810};
KW   Transferase {ECO:0000313|EMBL:PYH94534.1}.
FT   DOMAIN          516..594
FT                   /note="Transcription factor"
FT                   /evidence="ECO:0000259|SMART:SM00906"
FT   REGION          359..399
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          722..746
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        359..382
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   949 AA;  105934 MW;  46CA4CBE988B34A6 CRC64;
     MIVKITSPYS FLDDYSEGAH PQLLQSLLRT NTVQQTGYGS DEYSCDARQL LLSHMHASDE
     EVTIHFVPSG TAANLISIAS CLRPYEAVLA VQTGHIIDKE AGAIEATGHK IIPVPGVHGK
     MTPSNLEVVL DRNTFFPHMA KPRLVYISNA TEVGTVYTRT ELVALSELCR RRGLLLLVDG
     ARLGVALCKS DLTLRDLVDY TDIFWIGGTK MGALLGEAVV VRKELAEGFE FHIKQRGALL
     AKSRIIGVQF AELFREQDGL FFDLARHANA MAARISAQIK RIGWELASTT ETNQVFAVVP
     TELIGLLEER IRFYQWDKRE NTTVIRLVTS WATDETEVKC VHEGQPPCRR CQRLQRDSCE
     LTDPRSPRTP RRASRTTLDS RRSRRPSTAT PSAALPAAPV TVPAAPNPIS ALPPATLITA
     CDLYRKKFPV VNFLHYPSLI ADLSHDVPVE PVFLAVLLSL CARFMPESAL GPSETYAEYA
     RAQLAHRALE APSLYLAQSL VMISLYEWGS GRPYRAWMYS GMATYMIQSL LKTADDTMEQ
     AHPAPLDPIT YEQLVRTYWC CFAQDCELSS GARQHVALSF RHISVPLPIS DADFTFGKAS
     PRLMPAELTR QSPLARNLSI DRGLMIVTRG FDIFVRILRF ANESRRGRAR GSEPSSLRMW
     ETLKGELDEW RGLQDATVRY PETSAQAHVA LGYGELFAYI NLVYFMSILF LYRDRFLSVP
     KSSSTSPHQH PSPANPKDNE KEEEDEAISH LFSTAQHINA ILTSLSASST PVITPYAGFS
     VFVAAHINMY GTVCPGRYPG GLERAEREKR MNFEYLERLC GFWDVGESWW RTLQEAHRFY
     ETARSTATAP AGEHLTLAGT LDEYGDIRVE RPRSEAPRRR GTVVLGSGTP VGVAVAERAE
     SGVRRMELAE MVEPTELHDL EAEMLQWPFI DENWSLGFDT GFEGWPGLG
//