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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}.
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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
 
 
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