STUA_COLGL
ID STUA_COLGL Reviewed; 617 AA.
AC A8JPF9;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2016, sequence version 2.
DT 25-MAY-2022, entry version 50.
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:17849713};
OS Colletotrichum gloeosporioides (Anthracnose fungus) (Glomerella cingulata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum gloeosporioides species complex.
OX NCBI_TaxID=474922;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=17849713; DOI=10.1094/mpmi-20-9-1102;
RA Tong X.Z., Zhang X., Plummer K.M., Stowell K.M., Sullivan P.A.,
RA Farley P.C.;
RT "GcSTUA, an APSES transcription factor, is required for generation of
RT appressorial turgor pressure and full pathogenicity of Glomerella
RT cingulata.";
RL Mol. Plant Microbe Interact. 20:1102-1111(2007).
CC -!- FUNCTION: Transcription factor that regulates asexual reproduction (By
CC similarity). Binds the StuA-response elements (StRE) with the consensus
CC sequence 5'-(A/T)CGCG(T/A)N(A/C)-3' at the promoters of target genes
CC (By similarity). Required for the formation of aerial hyphae, efficient
CC conidiation, and the formation of perithecia (PubMed:17849713).
CC Essential for the generation of normal turgor pressure within the
CC appressorium (PubMed:17849713). Required for infection of intact apple
CC fruit and penetration of onion epidermal cells (PubMed:17849713).
CC {ECO:0000250|UniProtKB:P36011, ECO:0000269|PubMed:17849713}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P36011}.
CC -!- DISRUPTION PHENOTYPE: Impairs conidiation and ability of their
CC appressoria to form a penetration peg, leading to unability to infect
CC unwounded Granny Smith apples or onion (PubMed:17849713).
CC {ECO:0000269|PubMed:17849713}.
CC -!- SIMILARITY: Belongs to the EFG1/PHD1/stuA family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABQ43358.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=ABQ43363.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=ABV00676.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; EF408244; ABQ43358.1; ALT_INIT; Genomic_DNA.
DR EMBL; EF408244; ABQ43363.1; ALT_INIT; Genomic_DNA.
DR EMBL; EF634312; ABV00676.1; ALT_INIT; mRNA.
DR AlphaFoldDB; A8JPF9; -.
DR SMR; A8JPF9; -.
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..617
FT /note="Cell pattern formation-associated protein STUA"
FT /id="PRO_0000435972"
FT DOMAIN 106..212
FT /note="HTH APSES-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00630"
FT DNA_BIND 140..161
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00630"
FT REGION 1..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 463..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 569..593
FT /note="Nuclear localization domain"
FT /evidence="ECO:0000250|UniProtKB:P36011"
FT COMPBIAS 16..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..385
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..449
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..531
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..562
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..595
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 617 AA; 66198 MW; 7761C77F072BFFFE CRC64;
MNQPAADMYY SQHMSAGQAP PPQTVTSGAM SYHSQHPPLQ PTHMPQYAPQ PQYSQYGYAN
GLTSPQSAQP ASQMGQNVLP LPGVATQGFQ GFDTTGQVAP PGMKPRVTAT LWEDEGSLCF
QVEARGICVA RREDNHMING TKLLNVAGMT RGRRDGILKS EKVRHVVKIG PMHLKGVWIP
FERALDFANK EKITELLYPL FVHNIGALLY HPTNQTRTNQ VMAAAERRKQ EQNQMRGAPQ
TGAPGLPSIQ QHHHHMSLPG PQQSLPSHAQ MGRPSLDRAH TFPTPPTSAS SVMGGNMNAS
DSGFQWAQGQ GMGSAQGANP MSIDTGLSNA RSMPATPAST PPGTTIQNMQ SYQSGAQQYD
NSRPMYNPSA QQSPYQATNP ASQDRPVYGQ PDPYAKNDMG PPTTRPATSG APQDQKPANG
IIHADQSGGQ PAGDEEAEHD HDAEYTHDSG AYDASRASYN YSAPAVGNLP AEHQHLSPEM
TGSPSHPPAS GRATPRTAAA PQPYYSQQAG YNTPPRVPQQ PSSNLYNVMS NDRGTAAGAG
TGDVYQPQAD MGSMSNGYAS QMNGAGGIKR GRDEDDDLQR PSSGGGMDLK RRKTLLDSQV
PAMAYAPPVM AQQPRRR
