Q2FPD1
Gene name |
priS |
Protein name |
DNA primase small subunit PriS |
Names |
|
Species |
Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 / JF-1) |
KEGG Pathway |
mhu:Mhun_1132 |
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 Q2FPD1
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q2FPD1-F1 | Predicted | AlphaFoldDB |
No variants for Q2FPD1
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q2FPD1 | |||||
No associated diseases with Q2FPD1
No regional properties for Q2FPD1
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for Q2FPD1 | |||
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| DNA-directed RNA polymerase complex | A protein complex that possesses DNA-directed RNA polymerase activity. |
| 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. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| 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 |
| MRPATRIFIK | QRFTDYYDKA | RISPPSSVKE | REFGFIFFDD | RYPDDIRMRR | HIGFSSGDEM |
| 70 | 80 | 90 | 100 | 110 | 120 |
| QEYVKSLVPA | HAYYSTAYYR | TPQAPTMGDK | EWLGADLIFD | LDADHIMRGS | YEAMLERIKG |
| 130 | 140 | 150 | 160 | 170 | 180 |
| EAEKLLDVLD | NELGIDMRTI | KLVFSGGRGY | HVHVQELAFR | DFEPAERREL | VDYVCGTGIS |
| 190 | 200 | 210 | 220 | 230 | 240 |
| PSLLLHDWKP | GRRGWHDRFR | LVLTRYLQDL | STRPIKEVKA | ELSSLRGVGQ | VMAERFAGMI |
| 250 | 260 | 270 | 280 | 290 | 300 |
| PELITLLNTN | PSSILLRDQT | VRTVFGALTS | ERESTLLPHI | REAAVQADEP | VTTDTRRLIR |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LPGSLHAKSG | FKVVPMEVKE | LHDFDPLIDA | VAFGEREVII | ESEREYSFSL | LGSSYDIPKG |
| 370 | 380 | ||||
| RLKVPEAVGV | FLCCRGMAEI | GGVLDHAS |