STUA_PENRW
ID STUA_PENRW Reviewed; 818 AA.
AC B6H2G9;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 03-AUG-2022, entry version 65.
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:21148688}; ORFNames=Pc13g04920;
OS Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS 54-1255) (Penicillium chrysogenum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC Penicillium chrysogenum species complex.
OX NCBI_TaxID=500485;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255;
RX PubMed=18820685; DOI=10.1038/nbt.1498;
RA van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA Bovenberg R.A.L.;
RT "Genome sequencing and analysis of the filamentous fungus Penicillium
RT chrysogenum.";
RL Nat. Biotechnol. 26:1161-1168(2008).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21148688; DOI=10.1128/aem.01557-10;
RA Sigl C., Haas H., Specht T., Pfaller K., Kuernsteiner H., Zadra I.;
RT "Among developmental regulators, StuA but not BrlA is essential for
RT penicillin V production in Penicillium chrysogenum.";
RL Appl. Environ. Microbiol. 77:972-982(2011).
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=11810244; DOI=10.1007/s00438-001-0591-z;
RA Banuelos O., Casqueiro J., Steidl S., Gutierrez S., Brakhage A.,
RA Martin J.F.;
RT "Subcellular localization of the homocitrate synthase in Penicillium
RT chrysogenum.";
RL Mol. Genet. Genomics 266:711-719(2002).
CC -!- FUNCTION: Transcription factor that regulates asexual reproduction
CC (PubMed:21148688). Binds the StuA-response elements (StRE) with the
CC consensus sequence 5'-(A/T)CGCG(T/A)N(A/C)-3' at the promoters of
CC target genes (By similarity). Controls the expression of the penicillin
CC gene cluster (PubMed:21148688). {ECO:0000250|UniProtKB:P36011,
CC ECO:0000269|PubMed:21148688}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11810244}.
CC -!- DISRUPTION PHENOTYPE: Blocks conidiation and causes aberrant hyphal
CC morphology (PubMed:21148688). Decreases expression of developmental
CC regulators brlA and abaA (PubMed:21148688).
CC {ECO:0000269|PubMed:21148688}.
CC -!- SIMILARITY: Belongs to the EFG1/PHD1/stuA family. {ECO:0000305}.
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DR EMBL; AM920428; CAP91561.1; -; Genomic_DNA.
DR RefSeq; XP_002558927.1; XM_002558881.1.
DR AlphaFoldDB; B6H2G9; -.
DR SMR; B6H2G9; -.
DR STRING; 1108849.XP_002558927.1; -.
DR EnsemblFungi; CAP91561; CAP91561; PCH_Pc13g04920.
DR GeneID; 8312363; -.
DR KEGG; pcs:Pc13g04920; -.
DR VEuPathDB; FungiDB:PCH_Pc13g04920; -.
DR eggNOG; ENOG502QW2C; Eukaryota.
DR HOGENOM; CLU_016460_0_0_1; -.
DR OMA; MDVHSSH; -.
DR OrthoDB; 311987at2759; -.
DR BioCyc; PCHR:PC13G04920-MON; -.
DR Proteomes; UP000000724; Contig Pc00c13.
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 3: Inferred from homology;
KW Conidiation; DNA-binding; Nucleus; Reference proteome; Sporulation;
KW Transcription; Transcription regulation.
FT CHAIN 1..818
FT /note="Cell pattern formation-associated protein stuA"
FT /id="PRO_0000435981"
FT DOMAIN 320..426
FT /note="HTH APSES-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00630"
FT DNA_BIND 354..375
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00630"
FT REGION 100..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 583..818
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 765..788
FT /note="Nuclear localization domain"
FT /evidence="ECO:0000250|UniProtKB:P36011"
FT COMPBIAS 456..486
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..571
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 650..698
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 716..762
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 764..789
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 818 AA; 87533 MW; 793FB1910A4FD45A CRC64;
MCSTIVNDLD DYCASLNSSF SKSLYCASHD GRHLRRPLLA SSLYSKPFIR ATEKLELPSI
SQVHTRGPAD IPWYNPHAAE RPLLPGDKLP ALSLPTATQG LSRTAYPDPS VTNSTNSSAR
TSLSSASVPV NEPRSPPSSA DLSGTQGRLS LDSSAPTEYS LPPSVNEGYY PSPTSLGSMN
QTQPYMDVHS HMSSAQSYAP QGATAGAMSQ YQYHGQPPVM QPASSYAPAA YPQYGYPTGV
TSPPTGHPPS SMGGQMPAQL LPLPGKLQSQ NVIEDYSDRY QVSNHAVAPP SGYGNSTGAP
LQGFVFDGTG QVAPPGAKPR VTATLWEDEG SLCYQVEAKG VCVARREDNH MINGTKLLNV
AGMTRGRRDG ILKSEKLRHV VKIGPMHLKG VWIPFERALE FANKEKITDL LYPLFVHNIG
GLLYHPANQT RTNMVVQESQ QRRLEGPPPG PQRTPSGSQQ GPIHHHHPSL QTPMSSHMSQ
GPMNGQPGSR PGLERANTFP TPPASASSMM NQGSSYEWGG QVPHTQPLSI DTTLSNQRSM
PTTPATTPPG NNMQGLPAYQ GQGYDSSKPY YSAAPQTHAQ YAPHTPLTQS GMSSYGQPLA
GGYMKSEMAP PNPRPGVSEP ETSERDSNRY SQSNGPGETV AEHDQEYMQD HNAGYNSNRG
SYTYTTNPSV SSLTGEHSQL TPEMTSSPSQ QNGSGRMTPR TGAGPPPHWA SGYNTPPRPA
ATTLYNAVSD TRGTPANGAS DPYSMASTTA PVYPTGNGSL SAGSKRMRED DDIRAESTAE
YETSKRRKTI TDATLGGPVG GPPILQPMKP SGVMARHR