Q6BGW8
Gene name |
TFB2 (DEHA2G23254g) |
Protein name |
General transcription and DNA repair factor IIH subunit TFB2 |
Names |
TFIIH subunit TFB2, RNA polymerase II transcription factor B subunit 2 |
Species |
Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii) |
KEGG Pathway |
dha:DEHA2G23254g |
EC number |
|
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for Q6BGW8
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q6BGW8-F1 | Predicted | AlphaFoldDB |
No variants for Q6BGW8
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q6BGW8 | |||||
No associated diseases with Q6BGW8
1 regional properties for Q6BGW8
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Transcription factor Tfb2, C-terminal domain | 443 - 509 | IPR040662 |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| 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. |
1 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATPase activator activity | Binds to and increases the activity of an ATP hydrolysis activity. |
1 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). |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSSSNLFKAT | VNEHLEGLPK | QVQSRLYEAP | ATCLSIYRLL | PPIAKFYIMT | MLFYETPVAL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| KDLDKWCKPT | SRKFQFDSLK | RLRALHLIEE | DSSGSHIRLH | PTFRQNFRDC | LTGSQARNAF |
| 130 | 140 | 150 | 160 | 170 | 180 |
| GNLSTTPDEQ | SVSIKFLDSF | ALQKWESILH | FMVGTELSVT | PSNSVLSLLK | SGGLMEGTNK |
| 190 | 200 | 210 | 220 | 230 | 240 |
| GGNRLNITNS | GFQFLLQDIN | AQIWTLLLQY | LNLTQDLNMD | PVDVLNFIFI | LGSLELGKGY |
| 250 | 260 | 270 | 280 | 290 | 300 |
| TVSSLSETQI | SMLADLRDYG | LIYQRSENSE | RFYPTRLATT | LTSDSAALKS | PSMAMEQALE |
| 310 | 320 | 330 | 340 | 350 | 360 |
| STTETEEQQN | LASNSNQGTI | ILETNFKIYA | YTNSPLEIAI | LNLFVHLKTR | FSNMVCGQIT |
| 370 | 380 | 390 | 400 | 410 | 420 |
| RESIRNALYN | GITADQIIKF | LETHAHSQMK | ILAKERLDKK | IEFDTSNNIN | TAGGAPQSQM |
| 430 | 440 | 450 | 460 | 470 | 480 |
| MTNENGTTVA | QHKLEVLPPT | VVDQIKLWQL | ELDRIQTFEG | YLFKDFASQQ | EFEALSNYAS |
| 490 | 500 | 510 | |||
| EIGVLLWSNK | SKMKFFVTKD | GISQVADFAS | RNQRR |