T2EA_YEAST
ID T2EA_YEAST Reviewed; 482 AA.
AC P36100; D6VXQ6;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Transcription initiation factor IIE subunit alpha;
DE Short=TFIIE-alpha;
DE AltName: Full=Factor A 66 kDa subunit;
DE AltName: Full=Transcription factor A large subunit;
GN Name=TFA1; OrderedLocusNames=YKL028W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 66-71; 102-108 AND
RP 206-220, AND SUBUNIT.
RC STRAIN=ATCC 208279 / BJ926;
RX PubMed=7961670; DOI=10.1016/s0021-9258(18)47019-6;
RA Feaver W.J., Henry N.L., Bushnell D.A., Sayre M.H., Brickner J.H.,
RA Gileadi O., Kornberg R.D.;
RT "Yeast TFIIE. Cloning, expression, and homology to vertebrate proteins.";
RL J. Biol. Chem. 269:27549-27553(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
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: TFIIE is a tetramer of two alpha (TFA1) and two beta (TFA2)
CC subunits. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 35900 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the TFIIE alpha subunit family. {ECO:0000305}.
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; U12825; AAA62665.1; -; Genomic_DNA.
DR EMBL; Z28028; CAA81863.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09126.1; -; Genomic_DNA.
DR PIR; S37845; S37845.
DR RefSeq; NP_012897.3; NM_001179594.3.
DR PDB; 5FMF; EM; 6.00 A; R=1-160.
DR PDB; 5FYW; EM; 4.35 A; W=1-482.
DR PDB; 5FZ5; EM; 8.80 A; W=1-482.
DR PDB; 5OQJ; EM; 4.70 A; W=1-482.
DR PDB; 5OQM; EM; 5.80 A; W=332-482.
DR PDB; 5SVA; EM; 15.30 A; h=1-482.
DR PDB; 6GYL; EM; 4.80 A; W=1-482.
DR PDB; 6GYM; EM; 6.70 A; W=1-482.
DR PDB; 7O4I; EM; 3.20 A; W=1-482.
DR PDB; 7O4J; EM; 2.90 A; W=1-482.
DR PDB; 7O4K; EM; 3.60 A; W=1-482.
DR PDB; 7O4L; EM; 3.40 A; W=1-482.
DR PDB; 7O72; EM; 3.40 A; W=1-482.
DR PDB; 7O73; EM; 3.40 A; W=1-482.
DR PDB; 7O75; EM; 3.20 A; W=1-482.
DR PDBsum; 5FMF; -.
DR PDBsum; 5FYW; -.
DR PDBsum; 5FZ5; -.
DR PDBsum; 5OQJ; -.
DR PDBsum; 5OQM; -.
DR PDBsum; 5SVA; -.
DR PDBsum; 6GYL; -.
DR PDBsum; 6GYM; -.
DR PDBsum; 7O4I; -.
DR PDBsum; 7O4J; -.
DR PDBsum; 7O4K; -.
DR PDBsum; 7O4L; -.
DR PDBsum; 7O72; -.
DR PDBsum; 7O73; -.
DR PDBsum; 7O75; -.
DR AlphaFoldDB; P36100; -.
DR SMR; P36100; -.
DR BioGRID; 34103; 173.
DR ComplexPortal; CPX-1658; General transcription factor complex TFIIE.
DR DIP; DIP-1700N; -.
DR IntAct; P36100; 7.
DR MINT; P36100; -.
DR STRING; 4932.YKL028W; -.
DR MaxQB; P36100; -.
DR PaxDb; P36100; -.
DR PRIDE; P36100; -.
DR EnsemblFungi; YKL028W_mRNA; YKL028W; YKL028W.
DR GeneID; 853840; -.
DR KEGG; sce:YKL028W; -.
DR SGD; S000001511; TFA1.
DR VEuPathDB; FungiDB:YKL028W; -.
DR eggNOG; KOG2593; Eukaryota.
DR GeneTree; ENSGT00390000016696; -.
DR HOGENOM; CLU_035744_2_0_1; -.
DR InParanoid; P36100; -.
DR OMA; EYYSHMY; -.
DR BioCyc; YEAST:G3O-31834-MON; -.
DR Reactome; R-SCE-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-SCE-6807505; RNA polymerase II transcribes snRNA genes.
DR Reactome; R-SCE-73776; RNA Polymerase II Promoter Escape.
DR Reactome; R-SCE-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR Reactome; R-SCE-75953; RNA Polymerase II Transcription Initiation.
DR Reactome; R-SCE-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR PRO; PR:P36100; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P36100; protein.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR GO; GO:0005673; C:transcription factor TFIIE complex; IDA:SGD.
DR GO; GO:0097550; C:transcription preinitiation complex; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000993; F:RNA polymerase II complex binding; IPI:SGD.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:SGD.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IDA:ComplexPortal.
DR GO; GO:0001113; P:transcription open complex formation at RNA polymerase II promoter; IDA:SGD.
DR DisProt; DP01237; -.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR039997; TFE.
DR InterPro; IPR017919; TFIIE/TFIIEa_HTH.
DR InterPro; IPR002853; TFIIE_asu.
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; PF02002; TFIIE_alpha; 1.
DR SMART; SM00531; TFIIE; 1.
DR PROSITE; PS51344; HTH_TFE_IIE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Metal-binding; Nucleus;
KW Reference proteome; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..482
FT /note="Transcription initiation factor IIE subunit alpha"
FT /id="PRO_0000211225"
FT DOMAIN 9..99
FT /note="HTH TFE/IIEalpha-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00676"
FT ZN_FING 124..152
FT /note="C4-type"
FT /evidence="ECO:0000255"
FT REGION 274..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 321..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..291
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..343
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..416
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..435
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..458
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..482
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 4..20
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 23..34
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 40..47
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 51..63
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 66..74
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 82..88
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 91..116
FT /evidence="ECO:0007829|PDB:7O4J"
FT TURN 125..127
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 133..136
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 144..148
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 165..178
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 180..191
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 199..203
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 259..265
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 267..288
FT /evidence="ECO:0007829|PDB:7O4J"
FT TURN 293..295
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 299..301
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 350..368
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 414..416
FT /evidence="ECO:0007829|PDB:7O4J"
SQ SEQUENCE 482 AA; 54742 MW; 3E789DFC4247EF8A CRC64;
MDRPIDDIVK NLLKFVVRGF YGGSFVLVLD AILFHSVLAE DDLKQLLSIN KTELGPLIAR
LRSDRLISIH KQREYPPNSK SVERVYYYVK YPHAIDAIKW KVHQVVQRLK DDLDKNSEPN
GYMCPICLTK YTQLEAVQLL NFDRTEFLCS LCDEPLVEDD SGKKNKEKQD KLNRLMDQIQ
PIIDSLKKID DSRIEENTFE IALARLIPPQ NQSHAAYTYN PKKGSTMFRP GDSAPLPNLM
GTALGNDSSR RAGANSQATL HINITTASDE VAQRELQERQ AEEKRKQNAV PEWHKQSTIG
KTALGRLDNE EEFDPVVTAS AMDSINPDNE PAQETSYQNN RTLTEQEMEE RENEKTLNDY
YAALAKKQAK LNKEEEEEEE EEEDEEEEEE EEMEDVMDDN DETARENALE DEFEDVTDTA
GTAKTESNTS NDVKQESIND KTEDAVNATA TASGPSANAK PNDGDDDDDD DDDEMDIEFE
DV
