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
//