STUA_TALMA
ID STUA_TALMA Reviewed; 632 AA.
AC Q8NKF5;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 63.
DE RecName: Full=Cell pattern formation-associated protein stuA {ECO:0000305};
DE AltName: Full=Stunted protein A {ECO:0000250|UniProtKB:P36011};
GN Name=stuA {ECO:0000303|PubMed:11994146};
OS Talaromyces marneffei (Penicillium marneffei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=37727;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, FUNCTION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=11994146; DOI=10.1046/j.1365-2958.2002.02906.x;
RA Borneman A.R., Hynes M.J., Andrianopoulos A.;
RT "A basic helix-loop-helix protein with similarity to the fungal
RT morphological regulators, Phd1p, Efg1p and StuA, controls conidiation but
RT not dimorphic growth in Penicillium marneffei.";
RL Mol. Microbiol. 44:621-631(2002).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20465521; DOI=10.3109/13693781003801219;
RA Kummasook A., Cooper C.R. Jr., Vanittanakom N.;
RT "An improved Agrobacterium-mediated transformation system for the
RT functional genetic analysis of Penicillium marneffei.";
RL Med. Mycol. 48:1066-1074(2010).
CC -!- FUNCTION: Transcription factor that regulates asexual reproduction
CC (PubMed:11994146, PubMed:20465521). Binds the StuA-response elements
CC (StRE) with the consensus sequence 5'-(A/T)CGCG(T/A)N(A/C)-3' at the
CC promoters of target genes (By similarity). Required for accurate
CC spatial organization of the developing conidiophore (PubMed:11994146,
CC PubMed:20465521). Primarily involved in the formation of the
CC uninucleate sterigmata, which arise by budding in this multicellular
CC structure (PubMed:11994146). Required for metula and phialide formation
CC during conidiation but is not required for dimorphic growth
CC (PubMed:11994146). {ECO:0000250|UniProtKB:P36011,
CC ECO:0000269|PubMed:11994146, ECO:0000269|PubMed:20465521}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P36011}.
CC -!- INDUCTION: Only expressed at detectable levels in conidiating cells,
CC but not in vegetative hyphae or yeast cells (PubMed:11994146).
CC {ECO:0000269|PubMed:11994146}.
CC -!- DISRUPTION PHENOTYPE: Leads to conidiophores that lack both metulae and
CC phialides and that consist of a stalk from which chains of conidia bud
CC directly (PubMed:11994146, PubMed:20465521).
CC {ECO:0000269|PubMed:11994146, ECO:0000269|PubMed:20465521}.
CC -!- SIMILARITY: Belongs to the EFG1/PHD1/stuA family. {ECO:0000305}.
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DR EMBL; AF436076; AAM27919.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8NKF5; -.
DR SMR; Q8NKF5; -.
DR VEuPathDB; FungiDB:PMAA_070290; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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; 3.10.260.10; -; 1.
DR InterPro; IPR029790; EFG1/Phd1/StuA.
DR InterPro; IPR036887; HTH_APSES_sf.
DR InterPro; IPR018004; KilA_N/APSES_HTH.
DR InterPro; IPR003163; Tscrpt_reg_HTH_APSES-type.
DR PANTHER; PTHR47792; PTHR47792; 1.
DR SMART; SM01252; KilA-N; 1.
DR SUPFAM; SSF54616; SSF54616; 1.
DR PROSITE; PS51299; HTH_APSES; 1.
PE 2: Evidence at transcript level;
KW Conidiation; DNA-binding; Nucleus; Sporulation; Transcription;
KW Transcription regulation.
FT CHAIN 1..632
FT /note="Cell pattern formation-associated protein stuA"
FT /id="PRO_0000435983"
FT DOMAIN 128..234
FT /note="HTH APSES-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00630"
FT DNA_BIND 162..183
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00630"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 246..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 340..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 403..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 473..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 578..604
FT /note="Nuclear localization domain"
FT /evidence="ECO:0000250|UniProtKB:P36011"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..315
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..460
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..546
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 555..576
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..606
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 632 AA; 68054 MW; A0C839C0A8CC9439 CRC64;
MNQTQSYMDV HTSHFSSPQP YGSHGATAGG MVPYSHYQQP PPLLPPGSAG YPSTPGSYSY
PYSNGVASTT QPASNSISSQ VPAQILPLPA MTSHTVTPHG YVSGAAQSQQ NAVHDPTGQT
CPPGAKPRVT ATLWEDEGSL CYQVEAKGVC VARREDNHMI NGTKLLNVAG MTRGRRDGIL
KSEKVRHVVK IGPMHLKGVW IPYERALDFA NKEKITDLLY PLFVHNIGGL LYHPANSNRT
NMVVHDSQQR RLEGSQTART SQGPQAPALH HHHSMNGSVP SHMPQASAST PQTNGRPELN
RAHTFPTPPA SASSLIGIPN QGSTYDWNSQ NINSTVQTSQ NVPIDNGLNS TRSMPTTPAT
TPPGNNLQGM PPYQNQPAYD SSKSYYSAAP SSQAQYASQP LPAHSLTYGQ PMMKDLGSSG
RPPLGPVEQE HDEVKVDRYN QPNGQVTNGT EEENGQQQEP EYVQDNVAGS YANRNSYTYT
TNPSVSSLSG DHSQLGGSPS HQNGSDRMTP RTAGTNPPPQ WSQGYNTPPR AVPAGSISNI
VSDTRGAPNG DSYAPGTAYA SNYSGYSSVN GSSMGSTKRM RDDDDDHLSR SDGRENEYET
KRRKTLTEPP VGGAFMQMQQ QPVPAGGVMR RR
