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Database: UniProt
Entry: A0A316U3Q3_9BASI
LinkDB: A0A316U3Q3_9BASI
Original site: A0A316U3Q3_9BASI 
ID   A0A316U3Q3_9BASI        Unreviewed;       837 AA.
AC   A0A316U3Q3;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Apses-domain-containing protein {ECO:0000313|EMBL:PWN19926.1};
GN   ORFNames=BCV69DRAFT_250169 {ECO:0000313|EMBL:PWN19926.1};
OS   Pseudomicrostroma glucosiphilum.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Exobasidiomycetes; Microstromatales; Microstromatales incertae sedis;
OC   Pseudomicrostroma.
OX   NCBI_TaxID=1684307 {ECO:0000313|EMBL:PWN19926.1, ECO:0000313|Proteomes:UP000245942};
RN   [1] {ECO:0000313|EMBL:PWN19926.1, ECO:0000313|Proteomes:UP000245942}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCA 4718 {ECO:0000313|EMBL:PWN19926.1,
RC   ECO:0000313|Proteomes:UP000245942};
RX   PubMed=29771364; DOI=10.1093/molbev/msy072;
RA   Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA   Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA   Spatafora J.W., Aime M.C.;
RT   "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT   clade Ustilaginomycotina.";
RL   Mol. Biol. Evol. 0:0-0(2018).
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DR   EMBL; KZ819329; PWN19926.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A316U3Q3; -.
DR   STRING; 1684307.A0A316U3Q3; -.
DR   OrthoDB; 3019647at2759; -.
DR   Proteomes; UP000245942; Unassembled WGS sequence.
DR   GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IEA:UniProt.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:UniProt.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR   Gene3D; 3.10.260.10; Transcription regulator HTH, APSES-type DNA-binding domain; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR036887; HTH_APSES_sf.
DR   InterPro; IPR018004; KilA/APSES_HTH.
DR   InterPro; IPR003163; Tscrpt_reg_HTH_APSES-type.
DR   PANTHER; PTHR43828; ASPARAGINASE; 1.
DR   PANTHER; PTHR43828:SF3; REGULATORY PROTEIN SWI6; 1.
DR   Pfam; PF00023; Ank; 1.
DR   Pfam; PF04383; KilA-N; 1.
DR   SMART; SM00248; ANK; 2.
DR   SMART; SM01252; KilA-N; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF54616; DNA-binding domain of Mlu1-box binding protein MBP1; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 1.
DR   PROSITE; PS51299; HTH_APSES; 1.
PE   4: Predicted;
KW   ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW   ProRule:PRU00023}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245942};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          18..124
FT                   /note="HTH APSES-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51299"
FT   REPEAT          531..563
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REGION          119..176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          208..359
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          597..642
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        134..176
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        208..256
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        257..275
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        341..359
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   837 AA;  89108 MW;  B5F063218E41D290 CRC64;
     MGGSFSAEGA SSAPQPTVYL ATYSNVPVYE MTIRGIAVMR RRTDGFLNAT QILKVAGIEK
     AKRTKILEKE ILTGEHEKVQ GGYGKYQGTW IPLKRAQELA GSYNVAHLLR PVLEFDPRTA
     DQVPTAGPKK RPNPNAPANS SYFKNGPGAV KSSTPKSSGS AAPEASTLRA PTQQPRFLQL
     RAPPSASTSD EAASGIMAPG SASLIGALSA SGGTSGTEGI PPGSTPSMRQ ALSNYSQFGY
     TPQGVPLPSS STTAVGKRAE RDADDSMESM QGREAPAKRA RAGSPGGSPP SRAEVPMIAL
     GPSPVKDLSA LAGPDSSLRG ASHPRPQQVA LGPPDELVRR SGGTRFADRP RPVKAQDEGE
     RRMRDRLIAL FMGSEGDVTA ISLGGSAPAS SESGPAPCVD AVIDDHGHTA LHWAAALCKL
     PLVSMLVARP VTERGANLHA GNYAGETALH RSVLVTNAYD SSNFPDLLEI LAPSLHTRDF
     KNRTVLHHIA LVAALKGRAT PARYYLASVL EYIAKKEGGK FASLVDAQDE DGETALGIAA
     RQGNNSMVKM LLEVGARKDL SNIFGLRPSD WGIDGGSTSG GPSDLVTSLM RPPQPPIQKS
     QDVLTQLRSL LDELTSTSAK ELAEKQEALQ VTQSHLQSAT RELTSRRKGI STAMAKVAEL
     EERKLRVGNL KRRLFRVVTH GVESGGGAPA VEGEVEEEAS PALITELLRL ESDFSSSSST
     SPEEGLVRVR SEDLSRLSLS PSQKQIEHLL LTRFLHHHFT LSNDSLRSAT EAVQVEARQK
     EEKCRRVVSM YSRIEETQVE EILDELVAAV ESNAEVDLAR VAGFLARTGG TVVGLKK
//
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