Q6CD24

PR
Gene name
TFB4 (YALI0C04367g)
Protein name
General transcription and DNA repair factor IIH subunit TFB4
Names
TFIIH subunit TFB4, RNA polymerase II transcription factor B subunit 4
Species
Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica)
KEGG Pathway
yli:YALI0C04367g
EC number
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

58-144 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q6CD24

Entry ID Method Resolution Chain Position Source
AF-Q6CD24-F1 Predicted AlphaFoldDB

No variants for Q6CD24

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q6CD24

No associated diseases with Q6CD24

No regional properties for Q6CD24

Type Name Position InterPro Accession
No domain, repeats, and functional sites for Q6CD24

Functions

Description
EC Number
Subcellular Localization
  • Nucleus
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
nucleotide-excision repair factor 3 complex One of several protein complexes involved in nucleotide-excision repair; possesses endodeoxynuclease and DNA helicase activities. In S. cerevisiae, it is composed of Rad2p and the core TFIIH-Ssl2p complex (core TFIIH is composed of Rad3p, Tfb1p, Tfb2p, Ssl1p, Tfb4p and Tfb5p. Note that Ssl2p is also called Rad25p).
transcription factor TFIIH core complex The 7 subunit core of TFIIH that is a part of either the general transcription factor holo-TFIIH or the nucleotide-excision repair factor 3 complex. In S. cerevisiae/humans the complex is composed of: Ssl2/XPB, Tfb1/p62, Tfb2/p52, Ssl1/p44, Tfb4/p34, Tfb5/p8 and Rad3/XPD.
transcription factor TFIIH holo complex A complex that is capable of kinase activity directed towards the C-terminal Domain (CTD) of the largest subunit of RNA polymerase II and is essential for initiation at RNA polymerase II promoters in vitro. It is composed of the core TFIIH complex and the TFIIK complex.

1 GO annotations of molecular function

Name Definition
metal ion binding Binding to a metal ion.

3 GO annotations of biological process

Name Definition
nucleotide-excision repair A DNA repair process in which a small region of the strand surrounding the damage is removed from the DNA helix as an oligonucleotide. The small gap left in the DNA helix is filled in by the sequential action of DNA polymerase and DNA ligase. Nucleotide excision repair recognizes a wide range of substrates, including damage caused by UV irradiation (pyrimidine dimers and 6-4 photoproducts) and chemicals (intrastrand cross-links and bulky adducts).
phosphorylation of RNA polymerase II C-terminal domain The process of introducing a phosphate group on to an amino acid residue in the C-terminal domain of RNA polymerase II. Typically, this occurs during the transcription cycle and results in production of an RNA polymerase II enzyme where the carboxy-terminal domain (CTD) of the largest subunit is extensively phosphorylated, often referred to as hyperphosphorylated or the II(0) form. Specific types of phosphorylation within the CTD are usually associated with specific regions of genes, though there are exceptions. The phosphorylation state regulates the association of specific complexes such as the capping enzyme or 3'-RNA processing machinery to the elongating RNA polymerase complex.
transcription initiation at RNA polymerase II promoter A transcription initiation process that takes place at a RNA polymerase II gene promoter. Messenger RNAs (mRNA) genes, as well as some non-coding RNAs, are transcribed by RNA polymerase II.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MNAIDGTSRQ LKDTEDQTLD DTPSLLSIII DAHVPSWEEI KSQISISEAV ASILVFINAH
70 80 90 100 110 120
LALHNSNSVN VIGYNASGAR ILYPPKSGVE STRSKEREER SESVSDGEQA PSKKDHSMYR
130 140 150 160 170 180
QFKTVDEVVQ TELWNMLNHT NYVEEEKQHN SAISGALSLA LGFINKHVFV DESRMRARIL
190 200 210 220 230 240
LLTVGHKNET IQYIPTMNCI FAAQKLKIPV DVCKLGPGSD QVFLQQACDS THGIYMDISE
250 260 270 280 290 300
KNSKTPKGLV QYLLSGFISD PSLRPHIVLP TQSNVDFRAA CFLTKQVVDI GYVCSVCLCI
310 320 330
MSQIPSNRRC PTCDTTYSEK TLAGLGRKPL KKKKKKVVKP