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Database: UniProt
Entry: A0A150VBM3_9PEZI
LinkDB: A0A150VBM3_9PEZI
Original site: A0A150VBM3_9PEZI 
ID   A0A150VBM3_9PEZI        Unreviewed;       328 AA.
AC   A0A150VBM3;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=HMG box domain-containing protein {ECO:0000259|PROSITE:PS50118};
GN   ORFNames=M433DRAFT_2491 {ECO:0000313|EMBL:KYG47875.1};
OS   Acidomyces richmondensis BFW.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Acidomyces.
OX   NCBI_TaxID=766039 {ECO:0000313|EMBL:KYG47875.1, ECO:0000313|Proteomes:UP000075602};
RN   [1] {ECO:0000313|EMBL:KYG47875.1, ECO:0000313|Proteomes:UP000075602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BFW {ECO:0000313|EMBL:KYG47875.1,
RC   ECO:0000313|Proteomes:UP000075602};
RX   PubMed=26973616; DOI=10.3389/fmicb.2016.00238;
RA   Mosier A.C., Miller C.S., Frischkorn K.R., Ohm R.A., Li Z., LaButti K.,
RA   Lapidus A., Lipzen A., Chen C., Johnson J., Lindquist E.A., Pan C.,
RA   Hettich R.L., Grigoriev I.V., Singer S.W., Banfield J.F.;
RT   "Fungi Contribute Critical but Spatially Varying Roles in Nitrogen and
RT   Carbon Cycling in Acid Mine Drainage.";
RL   Front. Microbiol. 7:238-238(2016).
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:KYG47875.1}.
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DR   EMBL; JPDO01000064; KYG47875.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A150VBM3; -.
DR   STRING; 766039.A0A150VBM3; -.
DR   Proteomes; UP000075602; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   CDD; cd00084; HMG-box_SF; 1.
DR   Gene3D; 1.10.30.10; High mobility group box domain; 2.
DR   InterPro; IPR009071; HMG_box_dom.
DR   InterPro; IPR036910; HMG_box_dom_sf.
DR   PANTHER; PTHR48112; HIGH MOBILITY GROUP PROTEIN DSP1; 1.
DR   PANTHER; PTHR48112:SF22; TRANSCRIPTION FACTOR A, MITOCHONDRIAL; 1.
DR   SMART; SM00398; HMG; 2.
DR   SUPFAM; SSF47095; HMG-box; 2.
DR   PROSITE; PS50118; HMG_BOX_2; 1.
PE   4: Predicted;
KW   DNA-binding {ECO:0000256|PROSITE-ProRule:PRU00267};
KW   Nucleus {ECO:0000256|PROSITE-ProRule:PRU00267};
KW   Reference proteome {ECO:0000313|Proteomes:UP000075602}.
FT   DOMAIN          250..316
FT                   /note="HMG box"
FT                   /evidence="ECO:0000259|PROSITE:PS50118"
FT   DNA_BIND        250..316
FT                   /note="HMG box"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00267"
FT   REGION          67..126
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        67..96
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        102..126
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   328 AA;  36521 MW;  3DF006978C63EED4 CRC64;
     MFGRRMGVLL RWPARARLPS ASATLQNRRD LPLRTLVVPQ ARLYATPGRP KSVVGEPSKT
     VKRAVKRAAA TNTSSGTLPA KNTANKGSAK AASKKSSAAK KTTRKPLTEE QKAARAAKQQ
     RELKKALRAA ALDPPKVAHS NAYQQFFADR MKAFFSAAQT GSAPRIAKEN SRAIAQEWKQ
     LGPAEIEHYN HIARVAKEKG LAEYKAWVES HTPEQIIAAN RARMKLRRDF TPKGKKHAYK
     WPLIHDERAV KKALTPYMQF ARSRLSSGDF KNIPLLEGAK LVGQEWKALS AGEKMKYEQL
     YQEDKKRWAA EYEELLGHPP PGRANAAA
//
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