Q54MD4
Gene name |
rfc4 (DDB_G0286027) |
Protein name |
Probable replication factor C subunit 4 |
Names |
Activator 1 subunit 4 |
Species |
Dictyostelium discoideum (Slime mold) |
KEGG Pathway |
ddi:DDB_G0286027 |
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 Q54MD4
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q54MD4-F1 | Predicted | AlphaFoldDB |
No variants for Q54MD4
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q54MD4 | |||||
No associated diseases with Q54MD4
3 GO annotations of cellular component
| Name | Definition |
|---|---|
| DNA replication factor C complex | A complex that loads the DNA polymerase processivity factor proliferating cell nuclear antigen (PCNA) onto DNA, thereby permitting processive DNA synthesis catalyzed by DNA polymerase. In eukaryotes the complex consists of five polypeptides. |
| Elg1 RFC-like complex | A pentameric replication factor C (RLC) complex, which unloads the DNA polymerase processivity factor proliferating cell nuclear antigen (PCNA) from chromatin and has roles in telomere length regulation and other aspects of genome stability. In Saccharomyces the subunits are known as Elg1p, Rfc2p, Rfc3p, Rfc4p, and Rfc5p. |
| nucleus | A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| ATP hydrolysis activity | Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient. |
| DNA binding | Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid). |
| DNA clamp loader activity | Facilitating the opening of the ring structure of the PCNA complex, or any of the related sliding clamp complexes, and their closing around the DNA duplex, driven by ATP hydrolysis. |
3 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. |
| leading strand elongation | The process in which an existing DNA strand is extended continuously in a 5' to 3' direction by activities including the addition of nucleotides to the 3' end of the strand, complementary to an existing template, as part of DNA replication. Leading strand elongation proceeds in the same direction as the replication fork. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSKIQKKDTE | PWVAKYRPKT | VDDVSYQEDV | ISALKKSLNT | GNLPHLLFYG | PPGTGKTSTI |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LAIAMDIYGP | ELMKQRVLEL | NASDERGIEV | VRTKIKNFAG | YAVNKTTTGT | SNPGATFKLI |
| 130 | 140 | 150 | 160 | 170 | 180 |
| ILDEADSMTT | DAQAALRRTI | ETTSKTTRFC | LLCNYISRII | DPLASRCAKF | RFKPLDTVAT |
| 190 | 200 | 210 | 220 | 230 | 240 |
| IERLKFISQQ | EGIKCEESVY | QAIQVVSNGD | MRKAITYLQS | AFRFFANKIS | EDVIYNIAGS |
| 250 | 260 | 270 | 280 | 290 | 300 |
| LPPQLIKQLV | DCCKKNSFDR | LQSMVQSIIA | QGYPVSQVIS | QLFDYVLTTK | DLNQSQKSHI |
| 310 | 320 | 330 | 340 | ||
| TMKIGNVDRN | LIDGSEEFLQ | LFDLSSYIMK | QLNNNSTSTN | GDDMLIG |