ID A0A0W0F611_9AGAR Unreviewed; 487 AA.
AC A0A0W0F611;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=HMG box domain-containing protein {ECO:0000259|PROSITE:PS50118};
GN ORFNames=WG66_15651 {ECO:0000313|EMBL:KTB31767.1};
OS Moniliophthora roreri.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=221103 {ECO:0000313|EMBL:KTB31767.1, ECO:0000313|Proteomes:UP000054988};
RN [1] {ECO:0000313|EMBL:KTB31767.1, ECO:0000313|Proteomes:UP000054988}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2952 {ECO:0000313|EMBL:KTB31767.1,
RC ECO:0000313|Proteomes:UP000054988};
RA Aime M.C., Diaz-Valderrama J.R., Kijpornyongpan T., Phillips-Mora W.;
RT "Draft genome sequence of Moniliophthora roreri, the causal agent of frosty
RT pod rot of cacao.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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:KTB31767.1}.
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DR EMBL; LATX01002292; KTB31767.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0W0F611; -.
DR eggNOG; KOG0527; Eukaryota.
DR Proteomes; UP000054988; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR CDD; cd01389; HMG-box_ROX1-like; 1.
DR Gene3D; 1.10.30.10; High mobility group box domain; 1.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR PANTHER; PTHR10270:SF161; SOX DOMAIN-CONTAINING PROTEIN DICHAETE-RELATED; 1.
DR PANTHER; PTHR10270; SOX TRANSCRIPTION FACTOR; 1.
DR Pfam; PF00505; HMG_box; 1.
DR SMART; SM00398; HMG; 1.
DR SUPFAM; SSF47095; HMG-box; 1.
DR PROSITE; PS50118; HMG_BOX_2; 1.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PROSITE-
KW ProRule:PRU00267}; Nucleus {ECO:0000256|PROSITE-ProRule:PRU00267};
KW Reference proteome {ECO:0000313|Proteomes:UP000054988}.
FT DOMAIN 159..236
FT /note="HMG box"
FT /evidence="ECO:0000259|PROSITE:PS50118"
FT DNA_BIND 159..236
FT /note="HMG box"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00267"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 129..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..256
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..360
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..389
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 487 AA; 54497 MW; 8FFD57C34C7B02EF CRC64;
MPAVRNRDTQ DDLTRDLPPL PSFPDSYDHP PSAFKFEFPP WNNDLNDSPF LADPYSPCRP
DISTPTINAP PPTIYSPTPR AFNTFLDSPY CPPDLPMINL RSIPTPFPRY FLSPSPPLDH
LKIPHHHLKT SYHHPKPSQP ASASIDIKCR PRKGGKDYIP RPENAFILFR RKVVKDRQQA
LGEAAADPMT KKQRHADLSK AIGQQWKTLQ PEERRHWEDL AKEKKKEHER LYPNYASRPA
RERDRVGIEK NRLRTAELGK SGPPVAEQGD VPSTSSEARN DHSTPSEASN AHENPSEARN
NHHTPPETHN APNHNTPPET SSAHDNPSEA QNNHNTTPET HDTPNHNTPS EAINNHDTRN
ITSESESDDR NNLPNGQHDQ GPTIFSHSSG FTISGGQFNN VHGDQVNSVA FHAFGLPQFI
QFHPIPDESA VTGLLGSIPV FLYDQLSLLA SSLDLSVVQL LFLLTYHSFE PQVIQLISGT
PLRQLLG
//
