Q1RI08
Gene name |
priA |
Protein name |
Primosomal protein N' |
Names |
ATP-dependent helicase PriA |
Species |
Rickettsia bellii (strain RML369-C) |
KEGG Pathway |
rbe:RBE_0925 |
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 Q1RI08
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q1RI08-F1 | Predicted | AlphaFoldDB |
No variants for Q1RI08
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q1RI08 | |||||
No associated diseases with Q1RI08
6 regional properties for Q1RI08
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Helicase, C-terminal | 393 - 548 | IPR001650 |
| domain | DEAD/DEAH box helicase domain | 125 - 283 | IPR011545 |
| domain | Helicase superfamily 1/2, ATP-binding domain | 118 - 312 | IPR014001 |
| domain | PriA DNA helicase, Cys-rich region (CRR) domain | 367 - 392 | IPR040498 |
| domain | Primosomal protein N', 3' DNA-binding domain | 15 - 98 | IPR041222 |
| domain | Primosomal protein N, C-terminal domain | 555 - 644 | IPR041236 |
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. |
5 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| DNA binding | Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid). |
| DNA helicase activity | Unwinding of a DNA helix, driven by ATP hydrolysis. |
| hydrolase activity | Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc. |
| zinc ion binding | Binding to a zinc ion (Zn). |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| DNA replication, synthesis of RNA primer | The synthesis of a short RNA polymer, usually 4-15 nucleotides long, using one strand of unwound DNA as a template; the RNA then serves as a primer from which DNA polymerases extend synthesis. |
| DNA unwinding involved in DNA replication | The process in which interchain hydrogen bonds between two strands of DNA are broken or 'melted', generating unpaired template strands for DNA replication. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MQIAKILLSA | VKLFPLDYLI | PEDLSLNIGD | LVVVPFRNKE | LTGIVWEFSN | VPEVKKLKTI |
| 70 | 80 | 90 | 100 | 110 | 120 |
| KEKVPLNLTI | TSEVLDLIKW | MSNYYMAELG | SIAKLVLPVD | IAEKPIKVKE | QKINNNFTLP |
| 130 | 140 | 150 | 160 | 170 | 180 |
| DLSEEQKQAL | QMLNDSNKPI | LIKGVTGSGK | TEVYFYLIAE | YLAKGKQALV | MLPEIALSTQ |
| 190 | 200 | 210 | 220 | 230 | 240 |
| IINRFKERFG | FDPIIWNSSV | TKAQKKMILR | GILEDKVKIV | IGARSSLFLP | FKNLGLIVID |
| 250 | 260 | 270 | 280 | 290 | 300 |
| EEHDDSYKQD | DGVLYNARDT | AIVRSTFDKA | QIVLCSATPS | IETMYNANIG | KYSVINLSSR |
| 310 | 320 | 330 | 340 | 350 | 360 |
| YKNAVLPNIE | MIDMTKEELP | KNCYLSNILI | KAIKNNLENK | EQTLLFLNRR | GYAPLMLCKS |
| 370 | 380 | 390 | 400 | 410 | 420 |
| CGHKFTCKYC | SSWMVVHKSS | KKLECHHCGY | QSKIFNSCPE | CLEDESLAIC | GPGIERIEEE |
| 430 | 440 | 450 | 460 | 470 | 480 |
| AKTLFPNSKI | AVISKDHVKN | PEKIAQLLHQ | MENLEIDILI | GTQMITKGYH | FPNLTLVGVV |
| 490 | 500 | 510 | 520 | 530 | 540 |
| DADLGSNHAD | LRSSERAFQL | LHQVGGRAGR | GNSKGMVYLQ | SYYPDNIIFS | YIKDEREDNF |
| 550 | 560 | 570 | 580 | 590 | 600 |
| FVNELEVRKA | ADMPPFSKMA | SVILSGTNEH | KILEVAKNMV | RIAPEAQVKI | LGPASSLMSK |
| 610 | 620 | 630 | 640 | ||
| LAGKYRFRIL | IIADKKFNLQ | KYLKFWLELI | KIPSFCHIKI | DIDPKSFY |