ID A0A165I5H6_9BASI Unreviewed; 398 AA.
AC A0A165I5H6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=GATA-type domain-containing protein {ECO:0000259|PROSITE:PS50114};
GN ORFNames=CALCODRAFT_142315 {ECO:0000313|EMBL:KZT60157.1};
OS Calocera cornea HHB12733.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Calocera.
OX NCBI_TaxID=1353952 {ECO:0000313|EMBL:KZT60157.1, ECO:0000313|Proteomes:UP000076842};
RN [1] {ECO:0000313|EMBL:KZT60157.1, ECO:0000313|Proteomes:UP000076842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12733 {ECO:0000313|EMBL:KZT60157.1,
RC ECO:0000313|Proteomes:UP000076842};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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DR EMBL; KV423933; KZT60157.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165I5H6; -.
DR STRING; 1353952.A0A165I5H6; -.
DR InParanoid; A0A165I5H6; -.
DR OrthoDB; 1451543at2759; -.
DR Proteomes; UP000076842; Unassembled WGS sequence.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00202; ZnF_GATA; 1.
DR Gene3D; 3.30.50.10; Erythroid Transcription Factor GATA-1, subunit A; 1.
DR InterPro; IPR000679; Znf_GATA.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR Pfam; PF00320; GATA; 1.
DR SMART; SM00401; ZnF_GATA; 1.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR PROSITE; PS50114; GATA_ZN_FINGER_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00094};
KW Reference proteome {ECO:0000313|Proteomes:UP000076842};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00094};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00094}.
FT DOMAIN 178..231
FT /note="GATA-type"
FT /evidence="ECO:0000259|PROSITE:PS50114"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 119..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 343..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 398 AA; 43451 MW; 6BF77F8569667225 CRC64;
MKLDRLQHEA SPELYYSAPA PPQHISQPMP QPWNYTPEAE LPDQIDAAAG VQHGMAYGAP
ADAGTLLRSS SYTSFGSEHG MQMDYSSDSD GNIYASAAIP LTADPSALHD GRLVTYRSGS
ETGYDVKEER RSPELGGYSR PGSSSSHHSV QPLVFRPQMM QVMHTDDAAS KETQFLRRKC
HNCHTTEPPS WRRSTLTPGK IVCNKCGLYE RTHGRTRPHR FDELRCGTKV RKTTKIVSVI
SRETSPNTAA RFRAMAAVKG EDAFPRRAST LESEASDASR SVSRNGSAYN SPNPGHAYPS
DSPIRVPQAP MKSATLPMPA PYDPSARPLS SSADYYAYQR RSSLPNFGMP ADRTDSGLST
PDGRRHSAAV GMPGIPEATG WQTIPVSELT ASPSRKRN
//
