ID F0UK78_AJEC8 Unreviewed; 854 AA.
AC F0UK78;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 46.
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=HCEG_05928 {ECO:0000313|EMBL:EGC46713.1};
OS Ajellomyces capsulatus (strain H88) (Darling's disease fungus) (Histoplasma
OS capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=544711 {ECO:0000313|Proteomes:UP000008142};
RN [1] {ECO:0000313|Proteomes:UP000008142}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H88 {ECO:0000313|Proteomes:UP000008142};
RA Champion M., Cuomo C., Ma L.-J., Henn M.R., Sil A., Goldman B., Young S.K.,
RA Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A., Borenstein D.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B.,
RA Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C., Klein B.,
RA McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA San-Blas G., Taylor J., Mendoza L., Galagan J., Nusbaum C., Birren B.;
RT "Annotation of Ajellomyces capsulatus strain H88.";
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; DS990639; EGC46713.1; -; Genomic_DNA.
DR AlphaFoldDB; F0UK78; -.
DR STRING; 544711.F0UK78; -.
DR VEuPathDB; FungiDB:I7I53_05790; -.
DR HOGENOM; CLU_009666_1_1_1; -.
DR OMA; RGVEVCR; -.
DR Proteomes; UP000008142; 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 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 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; PF13637; Ank_4; 1.
DR Pfam; PF04383; KilA-N; 1.
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; PS51299; HTH_APSES; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Conidiation {ECO:0000256|ARBA:ARBA00023321};
KW Reference proteome {ECO:0000313|Proteomes:UP000008142};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Sporulation {ECO:0000256|ARBA:ARBA00022969};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 89..196
FT /note="HTH APSES-type"
FT /evidence="ECO:0000259|PROSITE:PS51299"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 253..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 664..715
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 271..311
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..331
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 854 AA; 93880 MW; 01069E35A6CC62BE CRC64;
MSFSRDSLGP SNGASSQNQV ASFNNASQSV ASTPAATPPP RLSQQSNMSM SFPSNGASRN
SLQRTSFGAY DDTNGYGQVI PYEEYKPQIY TAVYSNVSVY EMEVNGVAVM RRRSDSWLNA
TQILKVAGVM KARRTKTLEK EVAAGEHEKV QGGYGKYQGT WVNYERGVEL CRHYHVLELL
RPLLEYDMGQ DGTGPAGRGA VETPTKEQAM AAQRKRLYRT MDGQGMSQTQ QGTYFQNISR
TAVSAVNAIN KARFDSPLGK GPDGRRSSMK VPSHVGSQES QVQSGSQQSL HSIASDSGFG
SNMQNSQQAG LLEHADEPLE PPRKRMRSLS AHERSFQSPN VIGPNSSMIE PSPTEPNDSF
YQVHPGAGLP DRYQKMKLVM TLFLDKRAKD FSNHPAFLNL SAEDLEIPLD KYYNSALHWA
AMLARMPLVH ALKAKGVSIY RLNGAGETAL QKAVGTRNNL DYRSFSKLLH VLSPTIEVVD
YHGRTVLHHI AMMAATGGGG HVAAKHYLES LLEFIVRYGG PAGSINASAN GSSDQPTAGV
IGLGKFMSEM VNIQDDQGDT ALNLAGRART VLVPQLLEVG ANPHIANNTG LRPADYGVGV
DMVNGGLSGQ NGDSESFANR LSKTRRELLD FSSLVEQSFS SIDNELSSGL GKKQEEFEHW
HNKIRESAKA RQIEQKQLDD MKQRARDRIE LDRQIKNLER SSEELTALLK SIQGDQFNAK
ILSIGNADDA LGFDMSQFNT LFPDDFDIST TGGFSDQQVA FLQSLPSIEI LTSQLGCYRE
HNAEICKEVE SLKSKNVVLG ENYRRMVMAC TGWTEKQVDD AADGLTECIK DLNEHPLPED
VAIEILMKDR GQDW
//
