Q8TUF8
Gene name |
priL |
Protein name |
DNA primase large subunit PriL |
Names |
|
Species |
Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A) |
KEGG Pathway |
mac:MA_0109 |
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 Q8TUF8
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q8TUF8-F1 | Predicted | AlphaFoldDB |
No variants for Q8TUF8
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q8TUF8 | |||||
No associated diseases with Q8TUF8
No regional properties for Q8TUF8
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for Q8TUF8 | |||
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| primosome complex | Any of a family of protein complexes that form at the origin of replication or stalled replication forks and function in replication primer synthesis in all organisms. Early complexes initiate double-stranded DNA unwinding. The core unit consists of a replicative helicase and a primase. The helicase further unwinds the DNA and recruits the polymerase machinery. The primase synthesizes RNA primers that act as templates for complementary stand replication by the polymerase machinery. The primosome contains a number of associated proteins and protein complexes and contributes to the processes of replication initiation, lagging strand elongation, and replication restart. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| 4 iron, 4 sulfur cluster binding | Binding to a 4 iron, 4 sulfur (4Fe-4S) cluster; this cluster consists of four iron atoms, with the inorganic sulfur atoms found between the irons and acting as bridging ligands. |
| DNA primase activity | Catalysis of the synthesis of a short RNA primer on a DNA template, providing a free 3'-OH that can be extended by DNA-directed DNA polymerases. |
| metal ion binding | Binding to a metal ion. |
No GO annotations of biological process
| Name | Definition |
|---|---|
| No GO annotations for biological process |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MQAEKLAYYP | FISEASAHVG | DLGISLESLL | NSRAYRTARA | RGIERVKEAL | EGEIKKPPVS |
| 70 | 80 | 90 | 100 | 110 | 120 |
| EEAQVLSELL | SYPFARMLVA | CVDDQLFTRR | YALAEAKAAY | TFLRNETPDF | LLEFGEDFGI |
| 130 | 140 | 150 | 160 | 170 | 180 |
| SAEIRDSHFS | MHFTDYIRFS | NSLKEPSWKL | TNRQFRAGKI | KITKEEFARL | LEEAVRERIE |
| 190 | 200 | 210 | 220 | 230 | 240 |
| QSFPIPEIPP | EVSAFCAPYV | AEIKEQFEVQ | KKKFGATDFG | AVEPELFPPC | ISHALANVQG |
| 250 | 260 | 270 | 280 | 290 | 300 |
| GVNLAHSMRF | AMTSFLLNVG | MSVEEILNLF | NVSPDFDAEK | TLYQIEHIAG | ATGNEYKPPA |
| 310 | 320 | 330 | 340 | 350 | 360 |
| CDTMRTYGNC | IGKDGLCAKI | SHPLGYYERR | IFLKNKEREK | EEGKEKGNEE | KKEKREEHEK |
| 370 | |||||
| KNEKGNEIKE | K |