ABAA_PEND2
ID ABAA_PEND2 Reviewed; 796 AA.
AC K9GDC6;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2013, sequence version 1.
DT 03-AUG-2022, entry version 30.
DE RecName: Full=Conidiophore development regulator abaA {ECO:0000305};
GN Name=abaA {ECO:0000303|PubMed:25530311}; ORFNames=PDIG_51120;
OS Penicillium digitatum (strain PHI26 / CECT 20796) (Green mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1170229;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHI26 / CECT 20796;
RX PubMed=23171342; DOI=10.1186/1471-2164-13-646;
RA Marcet-Houben M., Ballester A.-R., de la Fuente B., Harries E.,
RA Marcos J.F., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome sequence of the necrotrophic fungus Penicillium digitatum, the main
RT postharvest pathogen of citrus.";
RL BMC Genomics 13:646-646(2012).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25530311; DOI=10.1016/j.resmic.2014.12.003;
RA Wang M., Sun X., Zhu C., Xu Q., Ruan R., Yu D., Li H.;
RT "PdbrlA, PdabaA and PdwetA control distinct stages of conidiogenesis in
RT Penicillium digitatum.";
RL Res. Microbiol. 166:56-65(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). Plays an essential role in the
CC differentiation and functionality of phialides (PubMed:25530311).
CC {ECO:0000250|UniProtKB:P22022, ECO:0000269|PubMed:25530311}.
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 -!- DISRUPTION PHENOTYPE: completely abolishes conidia formation and leads
CC to the formation of compact white colonies (PubMed:25530311). Produces
CC extremely elongated and immature phialides with defective morphology
CC (PubMed:25530311). {ECO:0000269|PubMed:25530311}.
CC -!- SIMILARITY: Belongs to the TEC1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AKCT01000207; EKV11276.1; -; Genomic_DNA.
DR AlphaFoldDB; K9GDC6; -.
DR SMR; K9GDC6; -.
DR STRING; 1170229.K9GDC6; -.
DR PRIDE; K9GDC6; -.
DR EnsemblFungi; EKV11276; EKV11276; PDIG_51120.
DR eggNOG; KOG3841; Eukaryota.
DR HOGENOM; CLU_356362_0_0_1; -.
DR InParanoid; K9GDC6; -.
DR OMA; MWVSAPQ; -.
DR OrthoDB; 258258at2759; -.
DR Proteomes; UP000009882; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
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; 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 3: Inferred from homology;
KW Activator; Conidiation; Nucleus; Reference proteome; Sporulation;
KW Transcription; Transcription regulation.
FT CHAIN 1..796
FT /note="Conidiophore development regulator abaA"
FT /id="PRO_0000435938"
FT DNA_BIND 128..202
FT /note="TEA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00505"
FT REGION 61..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 210..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 728..757
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 775..796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..135
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 735..749
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 796 AA; 88403 MW; 698671118A5B4E3E CRC64;
MATGWQPECL VTQNQSSLGP VEAHSDRALQ NTTGNVQSYS DHLTHADIAA REDQLHQLGF
KYPHAPHHPQ PLSASGLDQQ HVAARLHQRK LRRLHSVGPN SQSRRARSSY LKSQKYLEYR
RRPRRDTGKD GEPVWSDELE DAFQQALEAN PPMGRRKWSE RGKSYGRNEL IAEYIFKLTG
KRRTRKQVSS HLQVLDSFLK GDPDWERLVR EASPERSSSV HGSAPAPKWR TAVEHTSASS
HYGSHTHGSY HDHMRSMQPY AGDLPPPHYT LGSNMQEAAA STIHGFNFDM WVTAPQQANR
IGKALHTYTR LQGDLHHSAA SSMPLEHVNG WRSSFPQLAS MVDDINNPMD CDIILLEVNL
ELMTDFPPAR SQLGIQLDLD FGHPSAGDVF GVSQMDNWTC STHIYEDGQK LIESHDDLPK
TQSTKVKPLF ESSWWAKMFT KVTQDKRMAE DSGNPQVARE ADDNTRNFFR SLSAVQELRA
TSPSSHRLSN QYQGHHGDES KRMAVLVWKF RQTRPGQVGT TTWRRLIPAP DRTSNNSPLA
VSGIDLPPLS LDSILLNKAS HQGMYQTPQP HDLIPHPSQS HSQWSLYHPP HDNVANLFNP
SGHLDFLASI SKAEDTINDK IAVTSVLDSF STSLAPESIP STSLHGPSGA PVMLNVHDLP
LSHPGIGYAM GHEASHYVPS HQHSVNMHDS NGVLHSFFGS NMQPLDDLSH SHASWGAHST
SIPGDVGAGS YHLSYHPEHH GHGPVSRESQ QPHHFDSLLP SEDLMDKIVG RMSNGASMHG
AGPDAAGYDN STVDSV