SEBA_ASPFU
ID SEBA_ASPFU Reviewed; 618 AA.
AC Q4WPF5;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=C2H2 finger domain transcription factor sebA {ECO:0000305};
DE AltName: Full=Stress response element-binding protein A {ECO:0000305};
GN Name=sebA {ECO:0000303|PubMed:22345349}; ORFNames=AFUA_4G09080;
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 FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=22345349; DOI=10.1128/ec.00016-12;
RA Dinamarco T.M., Almeida R.S., de Castro P.A., Brown N.A., dos Reis T.F.,
RA Ramalho L.N., Savoldi M., Goldman M.H., Goldman G.H.;
RT "Molecular characterization of the putative transcription factor SebA
RT involved in virulence in Aspergillus fumigatus.";
RL Eukaryot. Cell 11:518-531(2012).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=33705521; DOI=10.1093/genetics/iyab036;
RA Rocha M.C., Fabri J.H.T.M., da Silva L.P., Angolini C.F.F., Bertolini M.C.,
RA da Cunha A.F., Valiante V., Goldman G.H., Fill T.P., Malavazi I.;
RT "Transcriptional control of the production of Aspergillus fumigatus
RT conidia-borne secondary metabolite fumiquinazoline C important for
RT phagocytosis protection.";
RL Genetics 0:0-0(2021).
CC -!- FUNCTION: Transcription factor that is involved in the response to heat
CC shock, oxidative stress, and poor nutrient conditions
CC (PubMed:22345349). Controls expression of oxidative stress response
CC genes such as ccp1, cat1, cat2, sod2; as well as of heat shock genes
CC such as hsf1, hsp30 and hsp90 (PubMed:22345349). Negatively controls
CC the expression of the fumiquinazoline (fmq) cluster via binding to the
CC STRE motifs at the fmqA-D promoters (PubMed:33705521). Plays a role in
CC virulence (PubMed:22345349, PubMed:33705521).
CC {ECO:0000269|PubMed:22345349, ECO:0000269|PubMed:33705521}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22345349}. Cytoplasm
CC {ECO:0000269|PubMed:22345349}. Note=Accumulates in the nucleus upon
CC exposure to oxidative stress and heat shock conditions.
CC {ECO:0000269|PubMed:22345349}.
CC -!- DISRUPTION PHENOTYPE: Increases sensitivity calcium and to oxidative
CC stress factors, such as paraquat and H(2)O(2) (PubMed:22345349). Leads
CC to attenuated virulence in a murine model of invasive pulmonary
CC aspergillosis through increased killing by the murine alveolar
CC macrophages (PubMed:22345349). Increases the expression of the
CC fumiquinazoline (fmq) cluster and leads to overproduction of
CC fumiquinazoline C (PubMed:33705521). {ECO:0000269|PubMed:22345349,
CC ECO:0000269|PubMed:33705521}.
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DR EMBL; AAHF01000005; EAL89879.1; -; Genomic_DNA.
DR RefSeq; XP_751917.1; XM_746824.1.
DR AlphaFoldDB; Q4WPF5; -.
DR SMR; Q4WPF5; -.
DR STRING; 330879.Q4WPF5; -.
DR EnsemblFungi; EAL89879; EAL89879; AFUA_4G09080.
DR GeneID; 3509523; -.
DR KEGG; afm:AFUA_4G09080; -.
DR VEuPathDB; FungiDB:Afu4g09080; -.
DR eggNOG; KOG1721; Eukaryota.
DR HOGENOM; CLU_030977_1_0_1; -.
DR InParanoid; Q4WPF5; -.
DR OMA; EGVKQGC; -.
DR OrthoDB; 483385at2759; -.
DR Proteomes; UP000002530; Chromosome 4.
DR GO; GO:0005829; C:cytosol; IDA:AspGD.
DR GO; GO:0005634; C:nucleus; IDA:AspGD.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0071277; P:cellular response to calcium ion; IMP:AspGD.
DR GO; GO:0034605; P:cellular response to heat; IMP:AspGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:AspGD.
DR GO; GO:1900409; P:positive regulation of cellular response to oxidative stress; IMP:AspGD.
DR GO; GO:0043619; P:regulation of transcription from RNA polymerase II promoter in response to oxidative stress; IBA:GO_Central.
DR GO; GO:0042594; P:response to starvation; IBA:GO_Central.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 2.
DR SMART; SM00355; ZnF_C2H2; 2.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE 4: Predicted;
KW Cytoplasm; Metal-binding; Nucleus; Reference proteome; Repeat;
KW Stress response; Transcription; Transcription regulation; Virulence; Zinc;
KW Zinc-finger.
FT CHAIN 1..618
FT /note="C2H2 finger domain transcription factor sebA"
FT /id="PRO_0000435645"
FT ZN_FING 493..516
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 522..544
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 394..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 582..618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..473
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..604
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 618 AA; 67084 MW; ACAD1DF4B7021F05 CRC64;
MDATYTMAQT PVQGQPSFAY YPTESQSRQQ HFTSHPFEMQ YYGQVSSYPQ QQAQQQHSMP
EQQPVYAAQP MLNMHQMATT NAFRGALSMT PIASPQPTHL KPTIIVQQDS PALMPLDTRF
VSNDFYGFPS TPPLSTSGST ISSPPSSNGS LHTPINDCFF SFEKVEGVKE GCESDVHCEL
LANTDWSRSD SPPLTPVFIQ PQSLTASQSS DLLSAQIPCP SLSPSPSPDS ATFISHPQSI
LSAEPSGSDF CDPRQLTVES SVGAPAELPP LPTLSCNEEE PKVVLGSATV TLPVHEGLSP
SFSSSSEDPL GSLPTFDSFS DLDSEDEFAN KLVDFHPIGN TYFQGDKRQR LGTYLLDEDE
FLSERSLEDL DDQEAFAQSG LPSVESTDFL AVEGDATQST EEMSSKKRVT SRRSLKKAST
SESSSDSLAK KTQASATSRS GHSDTTSTVQ QSTASSRQNS TANTSNSESP AAPVSVNRRG
RKQSLTDDPS KTFVCSLCSR RFRRQEHLKR HYRSLHTQDK PFECHECGKK FSRSDNLAQH
ARTHGGGSIV MGVIDTNSSN TQPAFDEPEP RALGLALYEA ANAATSKSTT SESSDGTISD
TSSVGGRPAK KRRRDDHV
