ID A0A0D2F5N0_9EURO Unreviewed; 895 AA.
AC A0A0D2F5N0;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 02-APR-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=PV04_10072 {ECO:0000313|EMBL:KIW63208.1};
OS Phialophora macrospora.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX NCBI_TaxID=1851006 {ECO:0000313|EMBL:KIW63208.1, ECO:0000313|Proteomes:UP000054266};
RN [1] {ECO:0000313|EMBL:KIW63208.1, ECO:0000313|Proteomes:UP000054266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 27337 {ECO:0000313|EMBL:KIW63208.1,
RC ECO:0000313|Proteomes:UP000054266};
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 Capronia semiimmersa CBS27337.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KN846962; KIW63208.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D2F5N0; -.
DR STRING; 5601.A0A0D2F5N0; -.
DR HOGENOM; CLU_009666_1_1_1; -.
DR Proteomes; UP000054266; 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; PF13637; Ank_4; 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; 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:UP000054266};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Sporulation {ECO:0000256|ARBA:ARBA00022969}.
FT DOMAIN 108..215
FT /note="HTH APSES-type"
FT /evidence="ECO:0000259|PROSITE:PS51299"
FT REPEAT 441..473
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 587..619
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 264..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 683..744
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 813..840
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 18..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..69
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 895 AA; 97515 MW; 9BF3A63CD8BD760C CRC64;
MASGGIYAQP PPSFPQHGHS NSMNTSFQQA PSPMGPYEAQ SVASTPAPTP LPPRPASQHH
QQGQTQQQQL AYSTNGGMMA APNSFGGYSE ANMFAQPNLY SNGVKPQIYT AVYSNVSVFE
MEVNGVAVMR RRADSWLNAT QILKVAGVDK GKRTKVLEKE ITGEHEKVQG GYGKYQGTWV
NYQRGREFCR QYGVEQLLLP LLEYDISSDG MSGASQGIET PTKEQAMAAQ RKRMYGGDGR
PPGQSVGGTF FKNMSSTAAN AIHALNRTRL DSPNMDGRRS AGPRRQSQPF NYSQEPLYGS
QQSMPSMTTQ DSFGTNGGIM SQGASFAEFP NTDAQEPPRK RIRPSPQTSF LYDGAIDLSM
QDGTPTDPNV SFFSQPSQSF IASDPLHYGI EPLPHPSGPL EDQKKDLLLD LFIDPERTDF
DDHPAFLRLS GDEFEVPIDG SCNTALHWAA TLARIALVRK LLDKGFNMRR ANSGGETALI
AACQARNNLD RSSFPALLEL LGPSIEVRDG RGRTLLHHIA VSSAMKGRAS VGKYYLESLL
EYVIRQGTAS QSVMSFDTMN GVNGQSHPNP MTLARFMSEI VNAQDKAGDT ALNLAARTST
TAIIDQLIEV GADTSIANRG GLAPVDFGVQ GQATGGITDP SLPNLFEQPS MANGSPEKSF
EDAQEGLMTS IREVLSQSEA DFAAEMKEKK DILDKTNAAL KESGNALAEE RRRLEDARAR
VREKDELEQK IANLRQATSK LRTELSAMDP PATIQEHVAV GEADKGLDLD GQLPVIAQSL
QNGEADPGNM AMNQEQANLL ASLERAEVMS GRAKVYQRHN QQLEQTAKAL KARSGELEER
YKKIVSLCTG ADEDKVDELL DNLVQAVISE QKEMSNNSQL PRVREFLRLV QGSGN
//
