ID A0A319ET51_ASPSB Unreviewed; 1098 AA.
AC A0A319ET51;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=FAD/NAD(P)-binding domain-containing protein {ECO:0000313|EMBL:PYI10318.1};
GN ORFNames=BO78DRAFT_426899 {ECO:0000313|EMBL:PYI10318.1};
OS Aspergillus sclerotiicarbonarius (strain CBS 121057 / IBT 28362).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448318 {ECO:0000313|EMBL:PYI10318.1, ECO:0000313|Proteomes:UP000248423};
RN [1] {ECO:0000313|EMBL:PYI10318.1, ECO:0000313|Proteomes:UP000248423}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121057 {ECO:0000313|EMBL:PYI10318.1,
RC ECO:0000313|Proteomes:UP000248423};
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00108,
CC ECO:0000256|RuleBase:RU000682}.
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DR EMBL; KZ826323; PYI10318.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A319ET51; -.
DR STRING; 1448318.A0A319ET51; -.
DR Proteomes; UP000248423; 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:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd00086; homeodomain; 1.
DR Gene3D; 3.90.660.10; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017970; Homeobox_CS.
DR InterPro; IPR001356; Homeobox_dom.
DR PANTHER; PTHR10742; FLAVIN MONOAMINE OXIDASE; 1.
DR PANTHER; PTHR10742:SF404; POLYAMINE OXIDASE FMS1; 1.
DR Pfam; PF01593; Amino_oxidase; 1.
DR Pfam; PF00046; Homeodomain; 1.
DR PRINTS; PR00419; ADXRDTASE.
DR SMART; SM00389; HOX; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR PROSITE; PS00027; HOMEOBOX_1; 1.
DR PROSITE; PS50071; HOMEOBOX_2; 1.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PROSITE-
KW ProRule:PRU00108};
KW Homeobox {ECO:0000256|ARBA:ARBA00023155, ECO:0000256|PROSITE-
KW ProRule:PRU00108};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW ProRule:PRU00108}; Reference proteome {ECO:0000313|Proteomes:UP000248423}.
FT DOMAIN 55..115
FT /note="Homeobox"
FT /evidence="ECO:0000259|PROSITE:PS50071"
FT DNA_BIND 57..116
FT /note="Homeobox"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00108"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 45..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 107..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 345..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 415..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 495..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..82
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..121
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..245
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..263
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..522
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1098 AA; 121214 MW; C2F637C7F5C695D9 CRC64;
MSDPEPSAAA AAAACASSPP PAQPSESAAA LNYAFLVHSQ KTLTQNLPPR VDNKLLARQK
RRRTSPEDHA ILESEYQRNP KPDKTARASI VSRVSLGEKE VQIWFQNRRQ NDRRKSKPLQ
PHELLAPRSD VPDASKPTTT DDNLPTEPGS SSGTENSEDN CQETNPATQS SDNASFESDV
VHGDKNELEQ AGLSSQTSLA TEAVEDSQKA PDETMPDPEP AQIHDEPLDE SHQNSAKRKR
SFSDIRGNRP FVQGSSTPGM FQDMKSPPSL RISLSFDGEA MVRKEGELTP SPPKGRNALR
IAMSSDGKAV IRADGEPSPS KNRISMFSAR KPRFAGLRRS NSAVAFSTPR GGSMETERMF
GRSRDPRNWE SFFDTDARSA LSTPTSSQSA PNAGSPAFFR ARGQRSLTRS MSARHSALNH
SDYLNTPVPK PTGEKRRKIS RTVSSLGRLE TGRATLGDKL SNAKMLSTKE DDLELQWGDS
DKENWIPGTR VSHMRRRATS HHHARRPILR EASTRDGKTN RDLASTGRYS RASHSHHRAS
GVVGKDAPEV DAEHNRRVLH AVNTKDVQSL LQSREDPFLF HKTIAMGKRS NVAVIGAGLS
GLRCTDILIQ NGARVTLFEA RNRVGGRVHQ EKIHTHLIDM GPNWIHGTGK NPIAAIAEAT
ETVLEDFEGN QALISPDGKA IDDGLASRIS EVLWTIIENA FEYSNAHKDT IPPDRSLLDF
FREQVEKTDL SATEKELCIE SSRLWGAYVG DPIERQSLKL FCLEECIDGN NFFVASTYKN
VLKHVSRAAL QRADVRFNQP IVKIESESRK DLRSPGKVTL TTASGETFQF DEVVVTCPLG
WLKRNKRAFT PELPPRLDQA IDSISYGRLE KVYVSFPRAF WHAGTETATT NGSNLKYSSF
ENPTFAQFLN PEYTEHPNGI LWNQECISLA ALPSSCAHPT LLFYTFGPCS TYIVSKLADI
DPSSKEYYTF LNNFLRPFYS RLYGYSESSP DCKPLAFTAT QWQNDPYAGN GSYCNFQVGL
TQGDRDIEVL RAGLGADRGV WFAGEHTAPF VALGTTTGAY WSGERAAGQI CNLYGLGRLG
IGLERDDSLP SATPKGHL
//
