ID A0A0L1JBS5_ASPNO Unreviewed; 691 AA.
AC A0A0L1JBS5;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=ANOM_002536 {ECO:0000313|EMBL:KNG89204.1};
OS Aspergillus nomiae NRRL 13137.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1509407 {ECO:0000313|EMBL:KNG89204.1, ECO:0000313|Proteomes:UP000037505};
RN [1] {ECO:0000313|EMBL:KNG89204.1, ECO:0000313|Proteomes:UP000037505}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 13137 {ECO:0000313|EMBL:KNG89204.1,
RC ECO:0000313|Proteomes:UP000037505};
RA Moore M.G., Shannon B.M., Brian M.M.;
RT "The Genome of the Aflatoxigenic Filamentous Fungus Aspergillus nomius.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KNG89204.1}.
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DR EMBL; JNOM01000036; KNG89204.1; -; Genomic_DNA.
DR RefSeq; XP_015410127.1; XM_015547793.1.
DR AlphaFoldDB; A0A0L1JBS5; -.
DR STRING; 1509407.A0A0L1JBS5; -.
DR GeneID; 26804340; -.
DR OrthoDB; 3019647at2759; -.
DR Proteomes; UP000037505; 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:SF15; TRANSCRIPTION FACTOR MBP1; 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 Conidiation {ECO:0000256|ARBA:ARBA00023321};
KW Reference proteome {ECO:0000313|Proteomes:UP000037505};
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 9..111
FT /note="HTH APSES-type"
FT /evidence="ECO:0000259|PROSITE:PS51299"
FT REPEAT 258..290
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 104..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 659..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 511..565
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 419..433
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 691 AA; 76478 MW; 0C1C46BBA1AA4913 CRC64;
MAGVDFSKIY SATYSSVPVY EFKLDNDSVM RRRADDWINA THILKVAGFD KPARTRILER
EVQKGVHEKV QGGYGTWIPL PEGRMLAERN NIIDKLRPIF DYVAGDRSPP PAPKHTSAAS
KPRAQKNAAA NKRVVHEEVF SAVKPHRSMA PPSFTHEQYE MNPGFDEDES IEQATLESSS
MVADEEMMHI TQNGNYSRKR KRGMNEVTAM SISEQEHILY GDQLLDYFMT VGDAPEATRI
PPPEPPANFQ VDRSIDDSGN TALHWACAMG DLEIVKDLLR RGADVKTLSV HEETPLVRAV
LFTNNYEKRT FPPLLDLLLD TVSFRDWFGA TIFHHIAETT RSKGKWKSSR YYCEVLLDKL
RVTCAPEEID VLLSCQDSNG DTAALVAARN GAFRLVHLLL THCSRAGDLV NKKGETAASI
TQRANQSDRH IPPPPSSITM GNDHIDGEVA GPMNADQSVA PPQDSSPSTS ALLAKIGVIM
AEANKKLAVG YGSSKANQPD PDDVANPEAL YEQLELDRQK IQQQTADLAA KETKEERIDA
QFERYEQLRG RYESLLEQIQ QARLKERIAS STLPTNEDPN PPSTDQNKLL TVYQLARRLC
SAQKARRAAV RDLAQQTADA GVSTKFDVHR KLVSLATGLK EEELDPMAAE LVETLEFDRM
NGKGAGGESP EPEPQGSATF PLAGPPVSVD A
//
