Q756A7
PR
Gene name |
SPT16 (AER360C) |
Protein name |
FACT complex subunit SPT16 |
Names |
Facilitates chromatin transcription complex subunit SPT16 |
Species |
Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Eremothecium gossypii) |
KEGG Pathway |
ago:AGOS_AER360C |
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
2 structures for Q756A7
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 6A8M | X-ray | 170 A | A | 2-460 | PDB |
| AF-Q756A7-F1 | Predicted | AlphaFoldDB |
No variants for Q756A7
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q756A7 | |||||
No associated diseases with Q756A7
4 regional properties for Q756A7
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Peptidase M24 | 200 - 423 | IPR000994 |
| domain | Histone chaperone RTT106/FACT complex subunit SPT16-like, middle domain | 830 - 920 | IPR013719 |
| domain | FACT complex subunit Spt16 domain | 550 - 703 | IPR013953 |
| domain | FACT complex subunit Spt16, N-terminal lobe domain | 6 - 169 | IPR029148 |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| FACT complex | A histone chaperone complex that facilitates nucleosome disassembly and reassembly upon DNA or RNA polymerase passage. |
| replication fork protection complex | A protein complex conserved in eukaryotes and associated with the replication fork; the complex stabilizes stalled replication forks and is thought to be involved in coordinating leading- and lagging-strand synthesis and in replication checkpoint signaling. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| histone binding | Binding to a histone, any of a group of water-soluble proteins found in association with the DNA of eukaryotic or archaeal chromosomes. They are involved in the condensation and coiling of chromosomes during cell division and have also been implicated in gene regulation and DNA replication. They may be chemically modified (methylated, acetlyated and others) to regulate gene transcription. |
| nucleosome binding | Binding to a nucleosome, a complex comprised of DNA wound around a multisubunit core and associated proteins, which forms the primary packing unit of DNA into higher order structures. |
7 GO annotations of biological process
| Name | Definition |
|---|---|
| DNA repair | The process of restoring DNA after damage. Genomes are subject to damage by chemical and physical agents in the environment (e.g. UV and ionizing radiations, chemical mutagens, fungal and bacterial toxins, etc.) and by free radicals or alkylating agents endogenously generated in metabolism. DNA is also damaged because of errors during its replication. A variety of different DNA repair pathways have been reported that include direct reversal, base excision repair, nucleotide excision repair, photoreactivation, bypass, double-strand break repair pathway, and mismatch repair pathway. |
| DNA-templated DNA replication | A DNA replication process that uses parental DNA as a template for the DNA-dependent DNA polymerases that synthesize the new strands. |
| nucleosome assembly | The aggregation, arrangement and bonding together of a nucleosome, the beadlike structural units of eukaryotic chromatin composed of histones and DNA. |
| positive regulation of RNA polymerase II transcription preinitiation complex assembly | Any process that activates or increases the frequency, rate or extent of RNA polymerase II transcriptional preinitiation complex assembly. |
| positive regulation of transcription elongation by RNA polymerase II | Any process that activates or increases the frequency, rate or extent of transcription elongation, the extension of an RNA molecule after transcription initiation and promoter clearance by the addition of ribonucleotides, catalyzed by RNA polymerase II. |
| regulation of sister chromatid cohesion | Any process that modulates the frequency, rate or extent of sister chromatid cohesion. |
| transcription elongation by RNA polymerase II promoter | The extension of an RNA molecule after transcription initiation and promoter clearance at an RNA polymerase II promoter by the addition of ribonucleotides catalyzed 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 |
| MSEVIIDFST | FENRLLALRD | RFPSFDGSPS | SLVFILGSAD | EENPYQKTTI | LHNWLLGYEF |
| 70 | 80 | 90 | 100 | 110 | 120 |
| PTTLIAVFKE | GCVVITSAAK | TRYLEEGVAQ | MNKKLENTFK | IELWQSSKEP | GHNLKLFEDL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| VERVREAGSA | VGLATKDSYQ | GKFITEWKGV | WDTAVEKHGL | NGVDVSLGLS | SLWAVKDEKE |
| 190 | 200 | 210 | 220 | 230 | 240 |
| QAYLQVSSRG | SDKFMNLLSD | ELVRAVDEEI | KITDAKLSDN | VENEIDKSRF | LKKLSPELTP |
| 250 | 260 | 270 | 280 | 290 | 300 |
| LCPKGEKFDV | NYLDWAYSPI | IQSGPKYDLR | VSARSSETQL | DGNGCILASC | GIRYKNYCSN |
| 310 | 320 | 330 | 340 | 350 | 360 |
| ISRTFLIDPS | DEMTDNYDFL | LLLQEEIINN | LLRVGATPKQ | IYDGAVNYIN | SKKPELSAGF |
| 370 | 380 | 390 | 400 | 410 | 420 |
| TKNVGSLMGL | EFRDSQFVLN | NKNDYRKVEN | GDCFNISLGF | NNLKDSKTGA | SYALQLADTV |
| 430 | 440 | 450 | 460 | 470 | 480 |
| QLTSGGPKVL | TNYTKSRSQI | SFYFNNEDDG | TTKVKSEESK | TASIPTKPDP | KSKILRSKLR |
| 490 | 500 | 510 | 520 | 530 | 540 |
| GESRAEDDEK | EQIRKENQRK | LHEKLQREGL | LRFTDTDAAD | KDQKPVVHFK | KYESYVRETQ |
| 550 | 560 | 570 | 580 | 590 | 600 |
| IPNTVRDLRI | HVDWKNQTFI | LPIYGRPVPF | HINSYKNGSK | NEEGEYTYIR | LNFHSPGTGG |
| 610 | 620 | 630 | 640 | 650 | 660 |
| VSKKTEELPY | EDSPDHQFVR | SLTLRSKDGD | RMADIFKQIT | ELKKESTKRE | QERKVLADVV |
| 670 | 680 | 690 | 700 | 710 | 720 |
| EQAKLVENRT | GRTKRLDQIF | VRPSPDTKRV | PGTVFIHENG | IRYQSPLRTD | SRIDILFSNV |
| 730 | 740 | 750 | 760 | 770 | 780 |
| KNLFFQPCKG | ELIVIIHIHL | KNPILMGKKK | IQDVQFYREA | SDMAVDETGN | GRRNQMKFRR |
| 790 | 800 | 810 | 820 | 830 | 840 |
| YGDEDELEQE | QEERRKRAAL | DKEFRYFAEA | IAEASNGLVE | VDHPFRDLGF | QGVPSRSAVF |
| 850 | 860 | 870 | 880 | 890 | 900 |
| CMPTRDCLIQ | LVEPPFLVVN | LSEVEICILE | RVQFGLKNFD | MVFVYKDFTK | PVTHINTIPI |
| 910 | 920 | 930 | 940 | 950 | 960 |
| EQLEFIKSWL | TDVDIPYTVS | TINLNWATIM | KSLQDDPHQF | FLDGGWSFLA | TGSDDEMSGT |
| 970 | 980 | 990 | 1000 | 1010 | 1020 |
| SEEEVSEYEV | SDEDPSDEEV | DSEDDYSEGD | NEEFSDEGSE | DFSGEESEEG | EDWDELEKKA |
| 1030 | |||||
| AKADRGNRFA | D |