ID A0A165STU8_9AGAM Unreviewed; 467 AA.
AC A0A165STU8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=HTH TFE/IIEalpha-type domain-containing protein {ECO:0000259|PROSITE:PS51344};
GN ORFNames=NEOLEDRAFT_1133163 {ECO:0000313|EMBL:KZT25667.1};
OS Neolentinus lepideus HHB14362 ss-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Gloeophyllales; Gloeophyllaceae; Neolentinus.
OX NCBI_TaxID=1314782 {ECO:0000313|EMBL:KZT25667.1, ECO:0000313|Proteomes:UP000076761};
RN [1] {ECO:0000313|EMBL:KZT25667.1, ECO:0000313|Proteomes:UP000076761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB14362 ss-1 {ECO:0000313|EMBL:KZT25667.1,
RC ECO:0000313|Proteomes:UP000076761};
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).
CC -!- SIMILARITY: Belongs to the TFIIE alpha subunit family.
CC {ECO:0000256|ARBA:ARBA00008947}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KV425570; KZT25667.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165STU8; -.
DR STRING; 1314782.A0A165STU8; -.
DR InParanoid; A0A165STU8; -.
DR OrthoDB; 7984at2759; -.
DR Proteomes; UP000076761; Unassembled WGS sequence.
DR GO; GO:0006367; P:transcription initiation at RNA polymerase II promoter; IEA:InterPro.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR039997; TFE.
DR InterPro; IPR017919; TFIIE/TFIIEa_HTH.
DR InterPro; IPR002853; TFIIE_asu.
DR InterPro; IPR021600; TFIIE_asu_C.
DR InterPro; IPR024550; TFIIEa/SarR/Rpc3_HTH_dom.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR13097:SF7; GENERAL TRANSCRIPTION FACTOR IIE, POLYPEPTIDE 1, ALPHA; 1.
DR PANTHER; PTHR13097; TRANSCRIPTION INITIATION FACTOR IIE, ALPHA SUBUNIT; 1.
DR Pfam; PF11521; TFIIE-A_C; 1.
DR Pfam; PF02002; TFIIE_alpha; 1.
DR SMART; SM00531; TFIIE; 1.
DR SUPFAM; SSF57783; Zinc beta-ribbon; 1.
DR PROSITE; PS51344; HTH_TFE_IIE; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000076761};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 10..101
FT /note="HTH TFE/IIEalpha-type"
FT /evidence="ECO:0000259|PROSITE:PS51344"
FT REGION 212..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 245..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 347..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 384..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..261
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..402
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 467 AA; 52805 MW; 845671238C928B1F CRC64;
MSTKEEQETL RLLVQHVSRS FYEPKFIVIL DQLARHPVLK DDDLAGRMGL QAKELNKLMA
VLNNDRLIRV HRQNELKEGA QRSVGRAYYY IDYQHFCNVV KWRVAEMWRI IDNSLRNELD
NKGYICPQCG KSFTPLEVDK LIDFSRGVFV CDDCKGELVD NENAESVKGS QDRMQRFNRQ
MAFIQEGLRK TEDMVLPAFD VEAWVRNNLS EAEKQRNAEP GAGLKIAGSG PKTEDAGIGV
VISMDKDEET RKQERDAEAA AKRQQNLMPS WHLKSTITGD LTALGEAENS RVPDGAATLS
SNDAILRGLA PVNPPSTSQT IVEDVKPRTE EVDYYDQYYA SLEASNAVSS QGTPYSNGAN
GTEEEEDIKP SIEYLDSLNE YRKRSRSQLP DGNAEPRKAA RLDESLYVPP PVEEPPMEKT
PLVDPADDPI VQVNGHPVRY SEVTEEHQEM MTPEEYQAYY EVIQAQL
//
