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Database: UniProt
Entry: A0A0J6YAA1_COCIT
LinkDB: A0A0J6YAA1_COCIT
Original site: A0A0J6YAA1_COCIT 
ID   A0A0J6YAA1_COCIT        Unreviewed;       867 AA.
AC   A0A0J6YAA1;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 35.
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=CIRG_05277 {ECO:0000313|EMBL:KMP05596.1};
OS   Coccidioides immitis RMSCC 2394.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=404692 {ECO:0000313|EMBL:KMP05596.1, ECO:0000313|Proteomes:UP000054565};
RN   [1] {ECO:0000313|Proteomes:UP000054565}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RMSCC 2394 {ECO:0000313|Proteomes:UP000054565};
RX   PubMed=20516208; DOI=10.1101/gr.103911.109;
RA   Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA   Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA   Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA   FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA   Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA   Taylor J.W., Rounsley S.D.;
RT   "Population genomic sequencing of Coccidioides fungi reveals recent
RT   hybridization and transposon control.";
RL   Genome Res. 20:938-946(2010).
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DR   EMBL; DS028095; KMP05596.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0J6YAA1; -.
DR   STRING; 404692.A0A0J6YAA1; -.
DR   Proteomes; UP000054565; 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   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          87..194
FT                   /note="HTH APSES-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51299"
FT   REGION          1..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          249..280
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          294..348
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          680..731
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..31
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        257..280
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        294..308
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        321..348
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   867 AA;  95347 MW;  491D4452F7A9EA1A CRC64;
     MSASQSSVAP PNGPPLSRSH RTSFSASQPP ASGPAASPPP PASQQSNMSV SFSNGGGGGR
     LMESRSFGGY GDNSGHGLYN GNYRPQIYTA VYSNVSVYEM EVNGVAVMRR RSDSWLNATQ
     ILKVAGVVKA RRTKTLEKEV VSGEHEKVQG GYGKYQGTWV SYQRGVELCR RYHVEDLLRP
     LLEYDMGQDG VSQAGQGAID TPTKEQAMAA QRKRLYYGMD SQGSSSHGTF FQSISRTAAS
     AVSAINKARF DSPASRGPDS RQPSAMRRSS QMSSQESHIP LGSQQSMYSV ASDSGFASNM
     QPSQRSMIDH GEETQEPPRK RMRSCSSLQP RSFNASMNDP TPTEPSESFY EQIEAQTDGA
     SDYAHGLKPL PAATTPERYQ KMKLIMTLFL DKRAKDFSTH PAFLTLSSED LEIPLDEYLN
     SALHWAAMLA RMPLLHALVA KGVSIHRLNA AGETALQKAV GTRNNLDYRT FSKLLQVLAP
     TIEIIDHHGR TVLHHIAMMA ATGGDGHVAA KHYLECLLEF IVRHGGPSNS QQSTVNGANN
     VLGPQSMEII GLGRFMSDMV NIQDDKGDTA LNLAGRARTI LVPQLLEVGA SPHIPNHTGL
     RPADYGVGVD MVNSGGQGQL NGDANDSFSN QLARTKKDIL NSTIVQITSA IEESFSMVDK
     DLSDDLSQKQ QEFDHWHAKI RESARLRQIE QNELDEIKRR ARERVELQRQ TRNLEQSADE
     LAATLKEMQA VDASDGNAGG NSKRKAIFDA DRFYALFPDT FDPSSELSDE QKSYLLEQPS
     PDQLQTLLEA YEEHNKSINE EIEVLKSKNV VLGEQYRRMV MACTGWSAEQ VDAAAEGLME
     CVKDLNQDPM SEEMALEILM QDRGQDW
//
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