ID A0A1L9RQH7_ASPWE Unreviewed; 373 AA.
AC A0A1L9RQH7;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=General transcription and DNA repair factor IIH subunit TFB4 {ECO:0000256|ARBA:ARBA00021280, ECO:0000256|RuleBase:RU368090};
DE Short=TFIIH subunit TFB4 {ECO:0000256|RuleBase:RU368090};
DE AltName: Full=RNA polymerase II transcription factor B subunit 4 {ECO:0000256|ARBA:ARBA00033341, ECO:0000256|RuleBase:RU368090};
GN ORFNames=ASPWEDRAFT_108298 {ECO:0000313|EMBL:OJJ37206.1};
OS Aspergillus wentii DTO 134E9.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Cremei.
OX NCBI_TaxID=1073089 {ECO:0000313|EMBL:OJJ37206.1, ECO:0000313|Proteomes:UP000184383};
RN [1] {ECO:0000313|Proteomes:UP000184383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DTO 134E9 {ECO:0000313|Proteomes:UP000184383};
RX PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT "Comparative genomics reveals high biological diversity and specific
RT adaptations in the industrially and medically important fungal genus
RT Aspergillus.";
RL Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
CC -!- FUNCTION: Component of the general transcription and DNA repair factor
CC IIH (TFIIH) core complex, which is involved in general and
CC transcription-coupled nucleotide excision repair (NER) of damaged DNA
CC and, when complexed to TFIIK, in RNA transcription by RNA polymerase
CC II. In NER, TFIIH acts by opening DNA around the lesion to allow the
CC excision of the damaged oligonucleotide and its replacement by a new
CC DNA fragment. In transcription, TFIIH has an essential role in
CC transcription initiation. When the pre-initiation complex (PIC) has
CC been established, TFIIH is required for promoter opening and promoter
CC escape. Phosphorylation of the C-terminal tail (CTD) of the largest
CC subunit of RNA polymerase II by the kinase module TFIIK controls the
CC initiation of transcription. {ECO:0000256|ARBA:ARBA00002817,
CC ECO:0000256|RuleBase:RU368090}.
CC -!- SUBUNIT: Component of the 7-subunit TFIIH core complex composed of
CC XPB/SSL2, XPD/RAD3, SSL1, TFB1, TFB2, TFB4 and TFB5, which is active in
CC NER. The core complex associates with the 3-subunit CTD-kinase module
CC TFIIK composed of CCL1, KIN28 and TFB3 to form the 10-subunit
CC holoenzyme (holo-TFIIH) active in transcription.
CC {ECO:0000256|RuleBase:RU368090}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU368090}.
CC -!- SIMILARITY: Belongs to the TFB4 family. {ECO:0000256|ARBA:ARBA00005273,
CC ECO:0000256|RuleBase:RU368090}.
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DR EMBL; KV878211; OJJ37206.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L9RQH7; -.
DR STRING; 1073089.A0A1L9RQH7; -.
DR VEuPathDB; FungiDB:ASPWEDRAFT_108298; -.
DR OrthoDB; 45434at2759; -.
DR Proteomes; UP000184383; Unassembled WGS sequence.
DR GO; GO:0000439; C:transcription factor TFIIH core complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005675; C:transcription factor TFIIH holo complex; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006289; P:nucleotide-excision repair; IEA:UniProtKB-UniRule.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR InterPro; IPR004600; TFIIH_Tfb4/GTF2H3.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR12831:SF0; GENERAL TRANSCRIPTION FACTOR IIH SUBUNIT 3; 1.
DR PANTHER; PTHR12831; TRANSCRIPTION INITIATION FACTOR IIH TFIIH , POLYPEPTIDE 3-RELATED; 1.
DR Pfam; PF03850; Tfb4; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|RuleBase:RU368090};
KW DNA repair {ECO:0000256|RuleBase:RU368090};
KW Metal-binding {ECO:0000256|RuleBase:RU368090};
KW Nucleus {ECO:0000256|RuleBase:RU368090};
KW Reference proteome {ECO:0000313|Proteomes:UP000184383};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU368090};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW ECO:0000256|RuleBase:RU368090}; Zinc {ECO:0000256|RuleBase:RU368090};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|RuleBase:RU368090}.
FT REGION 84..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 346..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 373 AA; 40071 MW; 5EC592F9D9B16427 CRC64;
MNSLDATEHY ETSANDPAPS LLTVVIDTNP HAWTLLEDSL PLSKAIANIL VFINAHLACN
YANEVAVVAS HSQKATWLYP CEQHPGSKSS TDQDGDVAMN GPDHSPAQVN KYRPFRIVEE
QVTRNLRHLM ESTAASDIQA TTSTMMAGAL TLALSHINRR TIAWAEAHGA DTAAGATATG
VAPSGSRSAA ENGNEGLQSR ILIVSVSSST DSAHQYIPIM NGIFACQRLH IPIDVCKLSG
DAVFLQQASD ATRGIYMSLT EPRGLLQYLM MAFLPDQRSR RHMVLPTRVD VDFRAACFCH
RRVVDVGFVC SICLSIFCEP PANGDCLTCG THLEMGDYGA KPAVVARKKK KKKARPNGAS
GTATPMSTPT PGP
//
