ID   T2EA_PONAB              Reviewed;         439 AA.
AC   Q5R8H5;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=General transcription factor IIE subunit 1;
DE   AltName: Full=Transcription initiation factor IIE subunit alpha;
DE            Short=TFIIE-alpha;
GN   Name=GTF2E1;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Recruits TFIIH to the initiation complex and stimulates the
CC       RNA polymerase II C-terminal domain kinase and DNA-dependent ATPase
CC       activities of TFIIH. Both TFIIH and TFIIE are required for promoter
CC       clearance by RNA polymerase (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Tetramer of two alpha and two beta chains. Interacts with
CC       TAF6/TAFII80. Interacts with ATF7IP. Interacts with SND1.
CC       {ECO:0000250|UniProtKB:P29083}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P29083}.
CC   -!- SIMILARITY: Belongs to the TFIIE alpha subunit family. {ECO:0000305}.
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DR   EMBL; CR859777; CAH91935.1; -; mRNA.
DR   RefSeq; NP_001127483.1; NM_001134011.1.
DR   AlphaFoldDB; Q5R8H5; -.
DR   SMR; Q5R8H5; -.
DR   STRING; 9601.ENSPPYP00000015098; -.
DR   Ensembl; ENSPPYT00000015701; ENSPPYP00000015098; ENSPPYG00000013500.
DR   GeneID; 100174557; -.
DR   KEGG; pon:100174557; -.
DR   CTD; 2960; -.
DR   eggNOG; KOG2593; Eukaryota.
DR   GeneTree; ENSGT00390000016696; -.
DR   HOGENOM; CLU_051021_1_0_1; -.
DR   InParanoid; Q5R8H5; -.
DR   OMA; EYYSHMY; -.
DR   OrthoDB; 1343016at2759; -.
DR   TreeFam; TF313429; -.
DR   Proteomes; UP000001595; Chromosome 3.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005669; C:transcription factor TFIID complex; IEA:Ensembl.
DR   GO; GO:0097550; C:transcription preinitiation complex; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; IEA:Ensembl.
DR   GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IEA:InterPro.
DR   Gene3D; 3.30.40.10; -; 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   InterPro; IPR013137; Znf_TFIIB.
DR   PANTHER; PTHR13097; PTHR13097; 1.
DR   Pfam; PF08271; TF_Zn_Ribbon; 1.
DR   Pfam; PF11521; TFIIE-A_C; 1.
DR   Pfam; PF02002; TFIIE_alpha; 1.
DR   SMART; SM00531; TFIIE; 1.
DR   PROSITE; PS51344; HTH_TFE_IIE; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW   Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P29083"
FT   CHAIN           2..439
FT                   /note="General transcription factor IIE subunit 1"
FT                   /id="PRO_0000260324"
FT   DOMAIN          14..104
FT                   /note="HTH TFE/IIEalpha-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00676"
FT   ZN_FING         129..157
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255"
FT   REGION          333..392
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        361..378
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P29083"
FT   MOD_RES         67
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P29083"
FT   MOD_RES         268
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P29083"
SQ   SEQUENCE   439 AA;  49531 MW;  EB3D21B2FF8EA8EC CRC64;
     MADPDVLTEV PAALKRLAKY VIRGFYGIEH ALALDILIRN PCVKEEDMLE LLKFDRKQLR
     SVLNNLKGDK FIKCRMRVET AADGKTTRHN YYFINYRTLV NVVKYKLDHM RRRIETDERD
     STNRASFKCP VCSSTFTDLE ANQLFDPMTG TFRCTFCHTE VEEDESAMPK KDARTLLARF
     NEQIEPIYAL LRETEDVNLA YEILEPEPTE IPALKQSKDH AATTAGAASL AGGHHREAWA
     TKGPSYEDLY TQNVVINMDD HEDLHRASLE GKSAKERPIW LRESTVQGAY SSEDMKEGGI
     DMDAFQEHEE GRAGPDDNEE VMRALLIHEK KTSSAMAGSV GAAAPVTTAN GSDSESETSE
     SDDDSPPRPA AVAVHKREED EEEDDEFEEV ADDPIVMVAG RPFSYSEVSQ RPELVAQMTP
     EEKEAYIAMG QRMFEDLFE