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Database: UniProt
Entry: A0A1C1C9R0_9EURO
LinkDB: A0A1C1C9R0_9EURO
Original site: A0A1C1C9R0_9EURO 
ID   A0A1C1C9R0_9EURO        Unreviewed;       445 AA.
AC   A0A1C1C9R0;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
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=CLCR_05801 {ECO:0000313|EMBL:OCT45265.1};
OS   Cladophialophora carrionii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC   Cladophialophora.
OX   NCBI_TaxID=86049 {ECO:0000313|EMBL:OCT45265.1, ECO:0000313|Proteomes:UP000094526};
RN   [1] {ECO:0000313|Proteomes:UP000094526}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KSF {ECO:0000313|Proteomes:UP000094526};
RA   Teixeira M.M., Souza R.C., Almeida L.G., Vicente V.A., de Hoog S.,
RA   Bocca A.L., de Almeida S.R., Vasconcelos A.T., Felipe M.S.;
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OCT45265.1}.
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DR   EMBL; LGRB01000020; OCT45265.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C1C9R0; -.
DR   STRING; 86049.A0A1C1C9R0; -.
DR   VEuPathDB; FungiDB:CLCR_05801; -.
DR   VEuPathDB; FungiDB:G647_07916; -.
DR   eggNOG; KOG2487; Eukaryota.
DR   Proteomes; UP000094526; 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; 2.
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:UP000094526};
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          87..148
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          426..445
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        90..105
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        106..148
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   445 AA;  47349 MW;  4F116DC6DC6A825A CRC64;
     MNAVDASEHY DKPSHSTEQS PSLLTIILDT NPAAWSLLSS TLPLSSAVAD LLVFINAHLA
     ANYTNKVAVI ASHCDKAQWL YPSPTEQKLP RSAADRHHAK RQSQAGDQLR DTSLSDSAKR
     LKLNGPSPDT TSIRLNLKPP SSSVHSGSKY RPFRLVEEEL LHNLTLLLSS TSPEAITAST
     STMIAGALTL ALSYINRESI LVSESLIGTS LNTGNADGPG PGPGEGAPQT LQSRILLISA
     SPSTDLAHQY IPIMNAIFAC QRLSIPIDIL QLPLPHPDSH IPSTAQAPSR DSSNPNSTVF
     LQQAADATHG IFIPAHLSPS ANPSNKHSKL GSTTTTAQTT AASQALLTYL LTSFLPSPST
     RSAHLILPTR IDVDFRAACF CHRNVVSVGF VCSICLSIFC EPPERGECLT CGTVLAVSDG
     VGRRPVVAGG KRKTKQSQGN EVNTR
//
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