ID A0A2H3IX90_9EURO Unreviewed; 1085 AA.
AC A0A2H3IX90;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Winged helix-turn-helix transcription repressor DNA-binding {ECO:0000313|EMBL:PCH00549.1};
GN ORFNames=PENO1_047470 {ECO:0000313|EMBL:PCH00549.1};
OS Penicillium occitanis (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=290292 {ECO:0000313|EMBL:PCH00549.1, ECO:0000313|Proteomes:UP000218381};
RN [1] {ECO:0000313|EMBL:PCH00549.1, ECO:0000313|Proteomes:UP000218381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL100 {ECO:0000313|EMBL:PCH00549.1,
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 flavin monoamine oxidase family.
CC {ECO:0000256|ARBA:ARBA00005995}.
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:PCH00549.1}.
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DR EMBL; NPFK01000117; PCH00549.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3IX90; -.
DR STRING; 290292.A0A2H3IX90; -.
DR OrthoDB; 5402444at2759; -.
DR Proteomes; UP000218381; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0140993; F:histone modifying activity; IEA:UniProt.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR GO; GO:0010558; P:negative regulation of macromolecule biosynthetic process; IEA:UniProt.
DR Gene3D; 3.90.660.10; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 1.10.30.10; High mobility group box domain; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR007526; SWIRM.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR10742; FLAVIN MONOAMINE OXIDASE; 1.
DR PANTHER; PTHR10742:SF386; LYSINE-SPECIFIC HISTONE DEMETHYLASE 1A; 1.
DR Pfam; PF01593; Amino_oxidase; 2.
DR Pfam; PF04433; SWIRM; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF47095; HMG-box; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR PROSITE; PS50118; HMG_BOX_2; 1.
DR PROSITE; PS50934; SWIRM; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|PROSITE-ProRule:PRU00267,
KW ECO:0000313|EMBL:PCH00549.1};
KW Nucleus {ECO:0000256|PROSITE-ProRule:PRU00267};
KW Reference proteome {ECO:0000313|Proteomes:UP000218381}.
FT DOMAIN 183..278
FT /note="SWIRM"
FT /evidence="ECO:0000259|PROSITE:PS50934"
FT DOMAIN 978..1058
FT /note="HMG box"
FT /evidence="ECO:0000259|PROSITE:PS50118"
FT DNA_BIND 978..1058
FT /note="HMG box"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00267"
FT REGION 30..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 95..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 907..953
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 907..933
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1085 AA; 120130 MW; FDB2F9EAAD399011 CRC64;
MATGQGDNNA RMRAGASKPI TFKHYAFTPA PQQLPIPPSK RRRINEPAPA YPSIKGGDLD
ISTQGMNGSY NVNYINQPPQ NGISHHTVLG NTASFSSQSA SEMSYPAEQD SDLTGHNTPN
TSVSNTSPWP QIKSMSPAAA ATEPADLPKQ VYAADVEAPN YEEFKPRSSI PSTLPGPVYA
QQCITAAYSS RLNPFALHKN EQNALQHHLC HLHVTTYLNI RNGILRLWTR NPMISVTREE
ALGCAKDFRW MGLADFAYGW LIRNGYINFG CVEVPQALIP AKKGRRKDDG PVIVIVGAGV
AGLACARQLE GLYQQYRDKV TSLKIIVLEG RRRIGGRIYS HPLKSHQKTS LPKGLRPTAE
MGAQIIVGFD RGNPLDPIIR SQLALRYHLL RDISTIYDID GSAVDEMQDA MDERLYNDVL
DRSGNYRHKA AIQSTAEGDR EMINHGRDIP IDDGVTVHQY EEARAAGTHH LMLPAARFRR
GIGHNASRIL PPPSTAQISD LGPDEELPAA MECQSMGWKL RDGVSPRTDL QLDKIAQNSP
IQTLGAVMDE GVRQYQHMLP LTPKDMRLLN WHYANLEYAN ATNLNALSLS GWDQDMGNEF
EGEHSQVIGG YQQLPRGLWA FPTKLDVRTN ETVVNITYDA AGKSKNRKTT VHTENGPISA
DHVVYTGSLG TLKHRSVEFA PALPQWKIGA VDRLGFGVLN KVVLVFEQPF WDTNRDMFGL
LRDAEVPGSM SQAHYAKNRG RFYLFWNCIK TSGIPVLIAL MAGDAAHQAE AMPDKEIVSE
VLSELRNIFK SKTVPDPLET IVTRWKADKF TRGTYSYVAA DALPGDYDLM AQAVGNLHFA
GEATCATHPA TVHGAYLSGL RAAAEIMEEI LGPIAIPTPL VPPSSKPNTN ITPGRYPTVD
LLKQSISTPV KQSPKTSTPS KTKPVNKSST SKPITPPAPI PTASTAVPTE EQRRQQLYKQ
ALEKHIRVTI GDPPAKPAKI ALNPFLTFQK DYWIRAKQQC EENKRKATNN PEAKAARDEI
RAVLGQMWRE ADEETKRPYQ EQMLVNRKTN DEMAKTWGEA MKEYEIKSVE VAKGFTFEMW
AAMNP
//
