ID   SREA_ARTBC              Reviewed;         542 AA.
AC   D4B3J8;
DT   20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   25-MAY-2022, entry version 46.
DE   RecName: Full=GATA-type transcription factor sreA {ECO:0000303|PubMed:26960149};
DE   AltName: Full=Siderophore uptake regulator sreA {ECO:0000303|PubMed:26960149};
GN   Name=sreA {ECO:0000303|PubMed:26960149}; ORFNames=ARB_03037;
OS   Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS   mentagrophytes).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4681 / CBS 112371;
RX   PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA   Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA   Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA   Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA   Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA   Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT   "Comparative and functional genomics provide insights into the
RT   pathogenicity of dermatophytic fungi.";
RL   Genome Biol. 12:R7.1-R7.16(2011).
RN   [2]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=26960149; DOI=10.1371/journal.pone.0150701;
RA   Kroeber A., Scherlach K., Hortschansky P., Shelest E., Staib P.,
RA   Kniemeyer O., Brakhage A.A.;
RT   "HapX mediates iron homeostasis in the pathogenic dermatophyte Arthroderma
RT   benhamiae but is dispensable for virulence.";
RL   PLoS ONE 11:E0150701-E0150701(2016).
CC   -!- FUNCTION: GATA-type transcription repressor that regulates iron
CC       acquisition genes through specific binding the GATA sequence elements
CC       of target promoters (PubMed:26960149). SreA targets include genes
CC       encoding a number of key iron-regulated factors such as the siderophore
CC       biosynthesis genes (PubMed:26960149). Is dispensable for growth on
CC       keratin substrates (PubMed:26960149). SreA represses the expression of
CC       hapX and the siderophore system during iron sufficient conditions by an
CC       iron-sensing mechanism, while hapX represses sreA and activates the
CC       siderophore system during iron-limiting conditions resulting in
CC       efficient iron uptake and inhibition of iron-consuming pathways
CC       (PubMed:26960149). {ECO:0000305|PubMed:26960149}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- INDUCTION: Expression is repressed by the transcription factor hapX
CC       during iron starvation (PubMed:26960149).
CC       {ECO:0000269|PubMed:26960149}.
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}.
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DR   EMBL; ABSU01000034; EFE29696.1; -; Genomic_DNA.
DR   RefSeq; XP_003010336.1; XM_003010290.1.
DR   AlphaFoldDB; D4B3J8; -.
DR   SMR; D4B3J8; -.
DR   STRING; 663331.D4B3J8; -.
DR   EnsemblFungi; EFE29696; EFE29696; ARB_03037.
DR   GeneID; 9525606; -.
DR   KEGG; abe:ARB_03037; -.
DR   eggNOG; KOG1601; Eukaryota.
DR   HOGENOM; CLU_021761_1_0_1; -.
DR   OMA; CYRPTTM; -.
DR   Proteomes; UP000008866; 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:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
DR   CDD; cd00202; ZnF_GATA; 1.
DR   Gene3D; 3.30.50.10; -; 1.
DR   InterPro; IPR039355; Transcription_factor_GATA.
DR   InterPro; IPR000679; Znf_GATA.
DR   InterPro; IPR013088; Znf_NHR/GATA.
DR   PANTHER; PTHR10071; PTHR10071; 1.
DR   Pfam; PF00320; GATA; 1.
DR   PRINTS; PR00619; GATAZNFINGER.
DR   SMART; SM00401; ZnF_GATA; 1.
DR   PROSITE; PS00344; GATA_ZN_FINGER_1; 1.
DR   PROSITE; PS50114; GATA_ZN_FINGER_2; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Metal-binding; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..542
FT                   /note="GATA-type transcription factor sreA"
FT                   /id="PRO_0000444402"
FT   ZN_FING         250..274
FT                   /note="GATA-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00094"
FT   REGION          1..172
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          178..196
FT                   /note="Cystein-rich region (CRR)"
FT                   /evidence="ECO:0000250|UniProtKB:Q1K8E7"
FT   REGION          210..248
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          289..408
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          461..525
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          510..542
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        69..117
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        133..172
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        216..248
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        310..342
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        366..388
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        462..479
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        480..507
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        510..525
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   542 AA;  56626 MW;  8160DCAE71DC0A69 CRC64;
     MLTLRSSSDT VRGFPATKRD MIRQPSAEDL DAAHQLVSSA RGVADLRPDS FDASRSPDGD
     KASVDTGAAM DDTASSDQNH SESQQQQQQQ QQQHSQASEQ VSAPESSSRS RASPKASRNT
     EVFLGHQCVP TNRIRDSGAN ANSGYANSST SDPRASPAAS DASAQNASGC GSTPAGTCPG
     GGSCNGTGGA VGCDGCPAYN NRVYKAAPRA PSARQARASP SAQTSEEQAQ SGLDALDSAS
     QDASGMPKAC QNCGTTLTPL WRRDDQGNTI CNACGLYYRL HGSHRPVAMK KTVIKRRKRV
     VPALRDRSPG AGSSDNSSVS PELHSASLAT SNADTNAYPP SENGGPSYGA AQFPHSAPPP
     IDFTGYYSKP TQSTSSPGLN TLINHSPNTK KRTHSESTSA ESAPPATRIQ SDISASAHLP
     PINPASARAL PNSGRLSSIS SLLNHTDPSF TESHVDAALG SNAPARSQTQ TQPQPGTRSY
     SPNPVNPPTT QPAHGSHSIP PPPLTPAADD KVKAARRAQL QREAENMREA LRAKERELAS
     LK