Q4R965
Gene name |
SRP54 (QtsA-10644) |
Protein name |
Signal recognition particle 54 kDa protein |
Names |
SRP54 |
Species |
Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey) |
KEGG Pathway |
mcf:101926767 |
EC number |
3.6.5.4: Acting on GTP; involved in cellular and subcellular movement |
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 Q4R965
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q4R965-F1 | Predicted | AlphaFoldDB |
No variants for Q4R965
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q4R965 | |||||
No associated diseases with Q4R965
4 regional properties for Q4R965
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Signal recognition particle, SRP54 subunit, GTPase domain | 101 - 296 | IPR000897 |
| domain | AAA+ ATPase domain | 100 - 277 | IPR003593 |
| domain | Signal recognition particle, SRP54 subunit, M-domain | 326 - 431 | IPR004125 |
| domain | Signal recognition particle SRP54, helical bundle | 2 - 87 | IPR013822 |
Functions
| Description | ||
|---|---|---|
| EC Number | 3.6.5.4 | Acting on GTP; involved in cellular and subcellular movement |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
4 GO annotations of cellular component
| Name | Definition |
|---|---|
| endoplasmic reticulum | The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached). |
| nuclear speck | A discrete extra-nucleolar subnuclear domain, 20-50 in number, in which splicing factors are seen to be localized by immunofluorescence microscopy. |
| 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. |
| signal recognition particle, endoplasmic reticulum targeting | A ribonucleoprotein particle of 325 kDa composed of a 7S (300 nucleotide) RNA molecule and a complex of six different polypeptides. This binds both to the N-terminal signal peptide for proteins destined for the endoplasmic reticulum as they emerge from the large ribosomal subunit and also to the ribosome. This binding arrests further translation thereby preventing the proteins from being released into the cytosol. The SRP-ribosome complex then diffuses to the endoplasmic reticulum where it is bound to the signal recognition particle receptor, which allows resumption of protein synthesis and facilitates the passage of the growing polypeptide chain through the translocon. Through a process involving GTP hydrolysis, the SRP-SRP receptor complex dissociates and SRP returns to the cytosol. Of the six polypeptides of SRP the 54 kDa subunit (SRP54) is the central player. It contains an N-terminal GTPase domain and a C-terminal domain that binds directly to the signal peptide and the SRP RNA. Examples of this component are found in Mus musculus, Saccharomyces cerevisiae and Arabidopsis thaliana. |
5 GO annotations of molecular function
| Name | Definition |
|---|---|
| 7S RNA binding | Binding to a 7S RNA, the RNA component of the signal recognition particle (SRP). |
| endoplasmic reticulum signal peptide binding | Binding to an endoplasmic reticulum signal peptide, a specific peptide sequence that acts as a signal to localize the protein within the endoplasmic reticulum. |
| GDP binding | Binding to GDP, guanosine 5'-diphosphate. |
| GTP binding | Binding to GTP, guanosine triphosphate. |
| GTPase activity | Catalysis of the reaction: GTP + H2O = GDP + H+ + phosphate. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| protein targeting to ER | The process of directing proteins towards the endoplasmic reticulum (ER) using signals contained within the protein. One common mechanism uses a 16- to 30-residue signal sequence, typically located at the N-terminus of the protein and containing positively charged amino acids followed by a continuous stretch of hydrophobic residues, which directs the ribosome to the ER membrane and initiates transport of the growing polypeptide across the ER membrane. |
| SRP-dependent cotranslational protein targeting to membrane | The targeting of proteins to a membrane that occurs during translation and is dependent upon two key components, the signal-recognition particle (SRP) and the SRP receptor. SRP is a cytosolic particle that transiently binds to the endoplasmic reticulum (ER) signal sequence in a nascent protein, to the large ribosomal unit, and to the SRP receptor in the ER membrane. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MVLADLGRKI | TSALRSLSNA | TIINEEVLNA | MLKEVCTALL | EADVNIKLVK | QLRENVKSAI |
| 70 | 80 | 90 | 100 | 110 | 120 |
| DLEEMASGLN | KRKMIQHAVF | KELVKLVDPG | VKAWTPTKGK | QNVIMFVGLQ | GSGKTTTCSK |
| 130 | 140 | 150 | 160 | 170 | 180 |
| LAYYYQRKGW | KTCLICADTF | RAGAFDQLKQ | NATKARIPFY | GSYTEMDPVI | IASEGVEKFK |
| 190 | 200 | 210 | 220 | 230 | 240 |
| NENFEIIIVD | TSGRHKQEDS | LFEEMLQVAN | AIQPDNIVYV | MDASIGQACE | AQAKAFKDKV |
| 250 | 260 | 270 | 280 | 290 | 300 |
| DVASVIVTKL | DGHAKGGGAL | SAVAATKSPI | IFIGTGEHID | DFEPFKTQPF | ISKLLGMGDI |
| 310 | 320 | 330 | 340 | 350 | 360 |
| EGLIDKVNEL | KLDDNEALIE | KLKHGQFTLR | DMYEQFQNIM | KMGPFSQILG | MIPGFGTDFM |
| 370 | 380 | 390 | 400 | 410 | 420 |
| SKGNEQESMA | RLKKLMTIMD | SMNDQELDST | DGAKVFSKQP | GRIQRVARGS | GVSTRDVQEL |
| 430 | 440 | 450 | 460 | 470 | 480 |
| LTQYTKFAQM | VKKMGGIKGL | FKGGDMSKNV | SQSQMAKLNQ | QMAKMMDPRV | LHHMGGMAGL |
| 490 | 500 | ||||
| QSMMRQFQQG | AAGNMKGMMG | FNNM |