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Database: UniProt
Entry: A0A0D2C1I1_9EURO
LinkDB: A0A0D2C1I1_9EURO
Original site: A0A0D2C1I1_9EURO 
ID   A0A0D2C1I1_9EURO        Unreviewed;       904 AA.
AC   A0A0D2C1I1;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   05-FEB-2025, entry version 40.
DE   RecName: Full=Cell pattern formation-associated protein stuA {ECO:0000256|ARBA:ARBA00019309};
DE   AltName: Full=Stunted protein A {ECO:0000256|ARBA:ARBA00031907};
GN   ORFNames=PV05_03112 {ECO:0000313|EMBL:KIW58611.1};
OS   Exophiala xenobiotica.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=348802 {ECO:0000313|EMBL:KIW58611.1, ECO:0000313|Proteomes:UP000054342};
RN   [1] {ECO:0000313|EMBL:KIW58611.1, ECO:0000313|Proteomes:UP000054342}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 118157 {ECO:0000313|EMBL:KIW58611.1,
RC   ECO:0000313|Proteomes:UP000054342};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Exophiala xenobiotica CBS118157.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KN847318; KIW58611.1; -; Genomic_DNA.
DR   RefSeq; XP_013319195.1; XM_013463741.1.
DR   AlphaFoldDB; A0A0D2C1I1; -.
DR   STRING; 348802.A0A0D2C1I1; -.
DR   GeneID; 25325020; -.
DR   HOGENOM; CLU_009666_1_1_1; -.
DR   OrthoDB; 6718656at2759; -.
DR   Proteomes; UP000054342; Unassembled WGS sequence.
DR   GO; GO:0030907; C:MBF transcription complex; IEA:TreeGrafter.
DR   GO; GO:0033309; C:SBF transcription complex; IEA:TreeGrafter.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:UniProtKB-ARBA.
DR   GO; GO:0003713; F:transcription coactivator activity; IEA:TreeGrafter.
DR   GO; GO:0048315; P:conidium formation; IEA:UniProtKB-KW.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR   FunFam; 3.10.260.10:FF:000001; APSES transcription factor (MbpA); 1.
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; IPR051642; SWI6-like.
DR   InterPro; IPR003163; Tscrpt_reg_HTH_APSES-type.
DR   PANTHER; PTHR43828; ASPARAGINASE; 1.
DR   PANTHER; PTHR43828:SF3; CHROMO DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00023; Ank; 1.
DR   Pfam; PF13637; Ank_4; 1.
DR   Pfam; PF04383; KilA-N; 1.
DR   SMART; SM00248; ANK; 3.
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; 2.
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   Conidiation {ECO:0000256|ARBA:ARBA00023321};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054342};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Sporulation {ECO:0000256|ARBA:ARBA00022969}.
FT   DOMAIN          113..220
FT                   /note="HTH APSES-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51299"
FT   REPEAT          455..487
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          596..628
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REGION          1..65
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          270..360
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          709..753
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          822..856
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        273..285
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        291..300
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        309..335
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   904 AA;  98784 MW;  F996C26C639F3450 CRC64;
     MMASGGLQPG VYAQPPPSFP QHGHSSSMNA SYPHPPLGYA EAHSVNNTPA PTPPPPRPAS
     QHQQQQQMVY NMNGGNPMAN GGMMAAPNSY GGYAEQNVFP QPNYYVNGNK PQIYTAVYSN
     VSVFEMEVNG IAVMRRRADS WLNATQILKV AGVDKGKRTK VLEKEITGEH EKVQGGYGKY
     QGTWVNYQRG REFTRQYGVE QLLLPLLEYD ITSDGMPGMG QGMETPTKEQ AMAAQRKRLY
     GGDGRPLSQT SGGTFFKNMS STAANAIHAL NRTRLDSPSH ADGRRSIGPR RQSQSQSFTY
     GTDGLYGQAG SQQSMPSMTS QDSFGTNGGI MSQGASFADF PSVDAQEPPR KRIRPSPQTS
     FLAGPYDASL EMALADGTPT EPNASFFSQP SQSFMALDPL SYGLEPLPHP SGAIDEQKRD
     LLLDLFIDPH RTDFEDHPAF LRLSGEEFEF PIDGSCNTVL HWAATLARIP LVQKLLQKGF
     NMRRANSGGE TALIAACQAR NNLDQSSFPA LLDLLGPSIE VRDGRGRTIL HHIAVSSAMK
     GRGAVGKYYL ESLLEYVVKQ GATQSMSFDG LNMSNQGNKM TLNRFMSEIV NAQDKAGDTA
     LNLAARTNTT TIIEQLIEVG ADPHIQNRGG LCPVDFGVGG GQVKSQMLDQ SMTMFEQPSA
     ANGLPQKSFE EAQEGLMTSI REILSQSEAD FTAEMKEKKE ILDKTNAALK ESGTSLAEER
     RRLEDARAKV REKEDLEQKI QNLRQAAAKL RAELHQSNPP TTIQENVGVG EADKGLDLDG
     QLPMVAQLFA DGETDPSNMA LTQEQANFLG CLERVEVLSG RASVYQRHNQ QLEQIAKTLK
     ARSAELEERY KKIVSLCTGA DEDKVDGLLD NLVQAVISEQ KEMNNNSQLG RVRDFLRLVK
     GSGN
//
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