SREA_ASPFU
ID SREA_ASPFU Reviewed; 546 AA.
AC Q4WV91;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=GATA-type transcription factor sreA {ECO:0000303|PubMed:18721228};
DE AltName: Full=Siderophore uptake regulator sreA {ECO:0000303|PubMed:18721228};
GN Name=sreA {ECO:0000303|PubMed:18721228}; ORFNames=AFUA_5G11260;
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, AND DISRUPTION PHENOTYPE.
RX PubMed=18721228; DOI=10.1111/j.1365-2958.2008.06376.x;
RA Schrettl M., Kim H.S., Eisendle M., Kragl C., Nierman W.C., Heinekamp T.,
RA Werner E.R., Jacobsen I., Illmer P., Yi H., Brakhage A.A., Haas H.;
RT "SreA-mediated iron regulation in Aspergillus fumigatus.";
RL Mol. Microbiol. 70:27-43(2008).
RN [3]
RP INDUCTION.
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=21062375; DOI=10.1111/j.1365-2958.2010.07389.x;
RA Liu H., Gravelat F.N., Chiang L.Y., Chen D., Vanier G., Ejzykowicz D.E.,
RA Ibrahim A.S., Nierman W.C., Sheppard D.C., Filler S.G.;
RT "Aspergillus fumigatus AcuM regulates both iron acquisition and
RT gluconeogenesis.";
RL Mol. Microbiol. 78:1038-1054(2010).
CC -!- FUNCTION: GATA-type transcription repressor that regulates
CC iron- acquisition genes through specific binding the GATA sequence
CC element 5'-ATCWGATAA-3' of target promoters (PubMed:18721228). Iron
CC acquisition regulation is critical for survival under both iron-
CC limiting conditions (to acquire essential iron) and iron-replete
CC conditions (to limit iron toxicity) (PubMed:18721228). SreA targets
CC include genes encoding a number of key iron-regulated factors such as
CC those involved in siderophore biosynthesis (PubMed:18721228).
CC {ECO:0000269|PubMed:18721228}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- INDUCTION: Expression is repressed by the zinc cluster transcription
CC factor acuM in order to stimulate expression of genes involved in both
CC reductive iron assimilation and siderophore-mediated iron uptake
CC (PubMed:21062375). {ECO:0000269|PubMed:21062375}.
CC -!- DOMAIN: The conserved cystein-rich region (CRR) localized between the
CC zinc fingers is also involved in DNA-binding and transcription
CC repressor activity (By similarity). {ECO:0000250|UniProtKB:Q1K8E7}.
CC -!- DISRUPTION PHENOTYPE: During iron-replete conditions, partially
CC derepresses synthesis of triacetylfusarinine C (TAFC) and uptake of
CC iron resulting in increased cellular accumulation of both iron and
CC ferricrocin (FC) (PubMed:18721228). Increases sensitivity to iron and
CC oxidative stress (PubMed:18721228). {ECO:0000269|PubMed:18721228}.
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DR EMBL; AAHF01000003; EAL91485.1; -; Genomic_DNA.
DR RefSeq; XP_753523.1; XM_748430.1.
DR AlphaFoldDB; Q4WV91; -.
DR STRING; 746128.CADAFUBP00005755; -.
DR EnsemblFungi; EAL91485; EAL91485; AFUA_5G11260.
DR GeneID; 3510986; -.
DR KEGG; afm:AFUA_5G11260; -.
DR VEuPathDB; FungiDB:Afu5g11260; -.
DR eggNOG; KOG1601; Eukaryota.
DR HOGENOM; CLU_021761_1_0_1; -.
DR InParanoid; Q4WV91; -.
DR OMA; CYRPTTM; -.
DR OrthoDB; 1466754at2759; -.
DR Proteomes; UP000002530; Chromosome 5.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IMP:AspGD.
DR GO; GO:0010106; P:cellular response to iron ion starvation; IEP:AspGD.
DR GO; GO:0034757; P:negative regulation of iron ion transport; IMP:AspGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd00202; ZnF_GATA; 2.
DR Gene3D; 3.30.50.10; -; 2.
DR InterPro; IPR039355; Transcription_factor_GATA.
DR InterPro; IPR000679; Znf_GATA.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR PANTHER; PTHR10071; PTHR10071; 2.
DR Pfam; PF00320; GATA; 2.
DR PRINTS; PR00619; GATAZNFINGER.
DR SMART; SM00401; ZnF_GATA; 2.
DR PROSITE; PS00344; GATA_ZN_FINGER_1; 2.
DR PROSITE; PS50114; GATA_ZN_FINGER_2; 2.
PE 2: Evidence at transcript level;
KW Coiled coil; Metal-binding; Nucleus; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..546
FT /note="GATA-type transcription factor sreA"
FT /id="PRO_0000444400"
FT ZN_FING 103..127
FT /note="GATA-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00094"
FT ZN_FING 253..277
FT /note="GATA-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00094"
FT REGION 1..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 138..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 180..198
FT /note="Cystein-rich region (CRR)"
FT /evidence="ECO:0000250|UniProtKB:Q1K8E7"
FT REGION 217..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 301..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 508..546
FT /evidence="ECO:0000255"
FT COMPBIAS 44..60
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..329
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..471
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..531
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 546 AA; 58568 MW; 27F9086A98391918 CRC64;
MLASVPQMDS VRSLPRNHDV VARHASAEDL DAAQQLISSA QAGREHTTDR HRDEKVTAPV
RHQMKTSMNG QRWPEQQRTA PPAEKTSTSP KAQKDTSFLG HSCSNCGTKS TPLWRRSPTG
AMICNACGLY LKARNVARPT KRNRMEPGSE AGGQQTGHGI AQSESASQGH CQSNSGGGSC
PGGGNCNGTG GAEGCDGCPA YNNRVYKSAA RGTVPIHSWR ATNSGSDRPL AETENDAGKN
GATVEGGNML VSCQNCGTTV TPLWRRDENG HPICNACGLY YKLHGCYRPT TMKKSIIKRR
KRVVPALRDQ SPSGATYSSN GSSASPEASP AVLAHSHDDH YRYLSSDPTL QANHQRHYAV
APPPVDFTHF SATGSLSLPH HPPPPRLLEP ERLSAPSHSP IPQFGRRSIS PSTSGSAKKR
TLAETTSSTD TASVPTTLES GSNQLPPIIS TANPSPPGRL SSISTLLNHS GPHDESRLDP
SLAALSRQQQ HHKATPLPPH PPSQPLPGVS ELESLKEDRR AKLQREAEEM REMLRAKERE
LAELGA
