ABAA_ASPFU
ID ABAA_ASPFU Reviewed; 797 AA.
AC E9RD40;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 25-MAY-2022, entry version 55.
DE RecName: Full=Conidiophore development regulator abaA {ECO:0000305};
GN Name=abaA {ECO:0000303|PubMed:20966095}; ORFNames=AFUA_1G04830;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
RN [2]
RP INDUCTION, FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20966095; DOI=10.1099/mic.0.044271-0;
RA Tao L., Yu J.H.;
RT "AbaA and WetA govern distinct stages of Aspergillus fumigatus
RT development.";
RL Microbiology 157:313-326(2011).
RN [3]
RP INDUCTION.
RX PubMed=22822234; DOI=10.1128/ec.00032-12;
RA Lamoth F., Juvvadi P.R., Fortwendel J.R., Steinbach W.J.;
RT "Heat shock protein 90 is required for conidiation and cell wall integrity
RT in Aspergillus fumigatus.";
RL Eukaryot. Cell 11:1324-1332(2012).
RN [4]
RP FUNCTION.
RX PubMed=24123270; DOI=10.1128/ec.00217-13;
RA Upadhyay S., Torres G., Lin X.;
RT "Laccases involved in 1,8-dihydroxynaphthalene melanin biosynthesis in
RT Aspergillus fumigatus are regulated by developmental factors and copper
RT homeostasis.";
RL Eukaryot. Cell 12:1641-1652(2013).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26032501; DOI=10.1016/j.bbrc.2015.05.090;
RA Shin K.S., Kim Y.H., Yu J.H.;
RT "Proteomic analyses reveal the key roles of BrlA and AbaA in biogenesis of
RT gliotoxin in Aspergillus fumigatus.";
RL Biochem. Biophys. Res. Commun. 463:428-433(2015).
RN [6]
RP INDUCTION.
RX PubMed=26190922; DOI=10.5941/myco.2015.43.2.150;
RA Seo Y.H., Kim S.S., Shin K.S.;
RT "In vitro antifungal activity and mode of action of 2',4'-dihydroxychalcone
RT against Aspergillus fumigatus.";
RL Mycobiology 43:150-156(2015).
CC -!- FUNCTION: BrlA, abaA and wetA are pivotal regulators of conidiophore
CC development and conidium maturation (By similarity). They act
CC individually and together to regulate their own expression and that of
CC numerous other sporulation-specific genes (By similarity). Binds to the
CC sequence 5'-CATTCY-3', where Y is a pyrimidine, making both major- and
CC minor-groove contacts (By similarity). Essential for differentiation
CC and functionality of phialides as conidiogenous cells
CC (PubMed:20966095). Regulates autolysis and cell death
CC (PubMed:20966095). Positively regulates expression of the gliotoxin
CC biosynthetic gene cluster in actively growing vegetative cells, and
CC likely bridges morphological and chemical development during the life-
CC cycle (PubMed:26032501). Negatively regulates expression of the melanin
CC biosynthetic gene cluster (PubMed:24123270).
CC {ECO:0000250|UniProtKB:P20945, ECO:0000269|PubMed:20966095,
CC ECO:0000269|PubMed:24123270, ECO:0000269|PubMed:26032501}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:I1S4T3}.
CC Note=localizes to the nuclei of phialides and terminal cells of mature
CC conidia (By similarity). {ECO:0000250|UniProtKB:I1S4T3}.
CC -!- INDUCTION: Highly expressed during conidiation (PubMed:20966095).
CC Expression is positively regulated by hsp90 (PubMed:22822234).
CC Expression is decreased by 2',4'-Dihydroxychalcone (2',4'-DHC)
CC (PubMed:26190922). {ECO:0000269|PubMed:20966095,
CC ECO:0000269|PubMed:22822234, ECO:0000269|PubMed:26190922}.
CC -!- DISRUPTION PHENOTYPE: Results in the formation of aberrant
CC conidiophores exhibiting reiterated cylinder-like terminal cells
CC lacking spores and causes delayed autolysis and cell death
CC (PubMed:20966095). Reduces significantly expression of the gliotoxin
CC biosynthetic gene cluster including gliM, gliP, gliT, and gliZ
CC (PubMed:26032501). {ECO:0000269|PubMed:20966095,
CC ECO:0000269|PubMed:26032501}.
CC -!- SIMILARITY: Belongs to the TEC1 family. {ECO:0000305}.
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DR EMBL; AAHF01000007; EAL88194.1; -; Genomic_DNA.
DR RefSeq; XP_750232.1; XM_745139.1.
DR AlphaFoldDB; E9RD40; -.
DR SMR; E9RD40; -.
DR STRING; 746128.CADAFUBP00000511; -.
DR EnsemblFungi; EAL88194; EAL88194; AFUA_1G04830.
DR GeneID; 3507334; -.
DR KEGG; afm:AFUA_1G04830; -.
DR VEuPathDB; FungiDB:Afu1g04830; -.
DR eggNOG; KOG3841; Eukaryota.
DR HOGENOM; CLU_356362_0_0_1; -.
DR InParanoid; E9RD40; -.
DR OMA; MWVSAPQ; -.
DR OrthoDB; 258258at2759; -.
DR Proteomes; UP000002530; Chromosome 1.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043936; P:asexual sporulation resulting in formation of a cellular spore; IMP:AspGD.
DR GO; GO:0001896; P:autolysis; IDA:CACAO.
DR GO; GO:0070787; P:conidiophore development; IMP:CACAO.
DR GO; GO:0048315; P:conidium formation; IEA:UniProtKB-KW.
DR GO; GO:0043945; P:positive regulation of asexual sporulation resulting in formation of a cellular spore; IMP:AspGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 6.10.20.40; -; 1.
DR InterPro; IPR000818; TEA/ATTS_dom.
DR InterPro; IPR038096; TEA/ATTS_sf.
DR Pfam; PF01285; TEA; 1.
DR PRINTS; PR00065; TEADOMAIN.
DR SMART; SM00426; TEA; 1.
DR PROSITE; PS00554; TEA_1; 1.
DR PROSITE; PS51088; TEA_2; 1.
PE 2: Evidence at transcript level;
KW Activator; Conidiation; Nucleus; Reference proteome; Sporulation;
KW Transcription; Transcription regulation.
FT CHAIN 1..797
FT /note="Conidiophore development regulator abaA"
FT /id="PRO_0000435933"
FT DNA_BIND 130..204
FT /note="TEA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00505"
FT REGION 696..797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 696..725
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 729..743
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 797 AA; 88925 MW; 7EC69A54EFF8A74F CRC64;
MATDWQPECI APQHQSGLEN IGHHTDRALQ NTSGNVQSYS DAILHGGMSG RDDHLQHLAY
KYSHAPVHPQ PMQTATTLHP HHILNARVQA KKLRRVQSLG PNHAGARRGR SYLKSQKYLE
YRARPRRDTG KDGEPVWSDE LEDAFQQALE ANPPMGRRKW SERGKSYGRN ELIAEYIYKV
TGKKRTRKQV SSHLQVLDSF LKGDPDWERL VREQPADRSG NQHQPVGPKW RTSLDHPLPS
HYGGHMHATY HDHLSPVQPY VGELPPPHYT LGSNMHERST DTIHGFNFDM WVSAPQQANQ
GDKAFHVYTC LQGDQYHPVA PPMPLENVRD WRTTFPHLNS VMEELDGPLD CEIILLEASL
KLMNDFPPPG SKLGIQLDID FAPPGMTDAT VLSQMDNWTC STYIYEDGNR LSKADHNLAR
PLSTKVKPPF ESSWWAKLFT ELTQDKQMAE KSGRHQNADD HIRQFFRSLS AVQEIRAISQ
NSRRVSQGSG HPGDCSKRMA ILLWKFRQTL PDEVGLTTWR KLIPPPDRTM MNSPKPATGI
DLPPLSLDSI LLKPQPPNVY QNPQGHDLLH QNGTSQPHWP LYPPPHESMS NMYHSTGSFD
FLNSVSKAED GLPDRTAVTS ILDSFPAMPP QETSQPSSLN VSSGGPVMLN VHDMSLSHHN
LAGYALSHDN HYVPSQQHGV SVHDSSNVLN NIFGPGSQPM DEIGNSQSAW GPPIPSTTIP
SDVGSNHYTH LPYHHHDHQT SASRESHPPN GFEGLMGPDD LMDKIVGSMP DDPGMNGAGP
DHASAAYADT NATEAVQ