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Database: UniProt
Entry: A0A167VW62_9EURO
LinkDB: A0A167VW62_9EURO
Original site: A0A167VW62_9EURO 
ID   A0A167VW62_9EURO        Unreviewed;       547 AA.
AC   A0A167VW62;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   02-APR-2025, entry version 28.
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=AAP_05149 {ECO:0000313|EMBL:KZZ88089.1};
OS   Ascosphaera apis ARSEF 7405.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ascosphaeraceae; Ascosphaera.
OX   NCBI_TaxID=392613 {ECO:0000313|EMBL:KZZ88089.1, ECO:0000313|Proteomes:UP000242877};
RN   [1] {ECO:0000313|EMBL:KZZ88089.1, ECO:0000313|Proteomes:UP000242877}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARSEF 7405 {ECO:0000313|EMBL:KZZ88089.1,
RC   ECO:0000313|Proteomes:UP000242877};
RX   PubMed=27071652; DOI=10.1093/gbe/evw082;
RA   Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT   "Divergent and convergent evolution of fungal pathogenicity.";
RL   Genome Biol. Evol. 8:1374-1387(2016).
CC   -!- SIMILARITY: Belongs to the EFG1/PHD1/stuA family.
CC       {ECO:0000256|ARBA:ARBA00007247}.
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:KZZ88089.1}.
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DR   EMBL; AZGZ01000028; KZZ88089.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A167VW62; -.
DR   VEuPathDB; FungiDB:AAP_05149; -.
DR   OrthoDB; 5407653at2759; -.
DR   Proteomes; UP000242877; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:TreeGrafter.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:TreeGrafter.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:TreeGrafter.
DR   GO; GO:0048315; P:conidium formation; IEA:UniProtKB-KW.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:TreeGrafter.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.260.10; Transcription regulator HTH, APSES-type DNA-binding domain; 1.
DR   InterPro; IPR029790; EFG1/Phd1/StuA.
DR   InterPro; IPR036887; HTH_APSES_sf.
DR   InterPro; IPR018004; KilA/APSES_HTH.
DR   InterPro; IPR003163; Tscrpt_reg_HTH_APSES-type.
DR   PANTHER; PTHR47792; PROTEIN SOK2-RELATED; 1.
DR   PANTHER; PTHR47792:SF1; PROTEIN SOK2-RELATED; 1.
DR   Pfam; PF04383; KilA-N; 1.
DR   SMART; SM01252; KilA-N; 1.
DR   SUPFAM; SSF54616; DNA-binding domain of Mlu1-box binding protein MBP1; 1.
DR   PROSITE; PS51299; HTH_APSES; 1.
PE   3: Inferred from homology;
KW   Conidiation {ECO:0000256|ARBA:ARBA00023321};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000313|EMBL:KZZ88089.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000242877};
KW   Sporulation {ECO:0000256|ARBA:ARBA00022969};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   DOMAIN          118..224
FT                   /note="HTH APSES-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51299"
FT   REGION          86..114
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          253..297
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          325..454
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          492..547
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        94..103
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        280..297
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        343..364
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        373..392
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        402..412
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        538..547
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   547 AA;  58596 MW;  273673B3D94941D2 CRC64;
     MNQTQSYMEV HPAHMPSAQA YPAHPPAAPL GHYNHYPSTV MTPSQYAPSA SSYYGYGSVT
     SPQSATHPPM SSQVGGQILP HPVAASAHGY VSDPSGSGQG SPPFDTTGQV PPPGIKPRVT
     ATLWEDEGSL CFQVEAKGIC VARRDDNDMI NGTKLLNVAG MTRGRRDGIL KSEKQRHVVK
     IGPMHLKGVW IPYDRALEFA NKEKITHLLY PLFVHNIGSL LMHPQNPSRA NALIAASERR
     RLENRTPAIT TQAPAMYHQP MGAPQQLPGP LHSRHESGRS HTFPTPPGSS ASILNGHNSG
     YEWSANVQSQ QPLTIDTNLA AARSLPATPA TTPPGPQVHG IPSYQNAGSY DTKPYYTSTS
     SAPQFPSHAS MAHPHEISHA SHADGESQDS HGEYASNGGY GSSRPSYPYS APTQVATLPH
     DSPQVSPIVN ESGPADTRPE RIHSRHGSQS NWYPRAGGSS VYSVMSDPRA TDSYSAGTGS
     TYGQTAINAY SKRSREDDAT AESKILAESQ ANDGSEGKRR RTLVEATRPS IALHTRPGSA
     SSVGRRL
//
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