O59668
Gene name |
SPBC29A3.03c |
Protein name |
LisH domain-containing protein C29A3.03c |
Names |
|
Species |
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
KEGG Pathway |
spo:SPBC29A3.03c |
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 O59668
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-O59668-F1 | Predicted | AlphaFoldDB |
No variants for O59668
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for O59668 | |||||
No associated diseases with O59668
6 regional properties for O59668
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | LIS1 homology motif | 99 - 131 | IPR006594 |
| domain | CRA domain | 192 - 309 | IPR013144 |
| domain | CTLH/CRA C-terminal to LisH motif domain | 139 - 303 | IPR024964 |
| domain | Zinc finger, RING-type, eukaryotic | 341 - 382 | IPR027370 |
| domain | Rmd5, degenerated RING (dRING) finger | 339 - 387 | IPR037683 |
| domain | Gid-type RING finger domain | 341 - 384 | IPR044063 |
4 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
| GID complex | A protein complex with ubiquitin ligase activity that is involved in proteasomal degradation of fructose-1,6-bisphosphatase (FBPase) and phosphoenolpyruvate carboxykinase during the transition from gluconeogenic to glycolytic growth conditions. In S. cerevisiae, the GID (Glucose Induced degradation Deficient) complex consists of Vid30p, Rmd5p, Vid24p, Vid28p, Gid7p, Gid8p, and Fyv10p. |
| 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. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| ubiquitin protein ligase activity | Catalysis of the transfer of ubiquitin to a substrate protein via the reaction X-ubiquitin + S -> X + S-ubiquitin, where X is either an E2 or E3 enzyme, the X-ubiquitin linkage is a thioester bond, and the S-ubiquitin linkage is an amide bond: an isopeptide bond between the C-terminal glycine of ubiquitin and the epsilon-amino group of lysine residues in the substrate or, in the linear extension of ubiquitin chains, a peptide bond the between the C-terminal glycine and N-terminal methionine of ubiquitin residues. |
| zinc ion binding | Binding to a zinc ion (Zn). |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| negative regulation of gluconeogenesis | Any process that stops, prevents, or reduces the frequency, rate or extent of gluconeogenesis. |
| proteasome-mediated ubiquitin-dependent protein catabolic process | The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of ubiquitin, and mediated by the proteasome. |
| protein modification by small protein conjugation or removal | A protein modification process in which one or more groups of a small protein, such as ubiquitin or a ubiquitin-like protein, are covalently attached to or removed from a target protein. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MNIDEWQRIE | ETAPGNKCLA | KLNELESILK | DAKKSCLKDP | TTSMKELVAC | SEKTQQVFDD |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LKRTEKKFHT | SLNRFGKTLE | KKFNFDLEDI | KLHSSFESKK | REIDTALSLH | FFRQGDVELA |
| 130 | 140 | 150 | 160 | 170 | 180 |
| HLFCKEAGIE | EPSESLHVFT | LLKSIVQGIR | DKDLKLPIEW | ASQCRGYLER | KGSSLEYTLQ |
| 190 | 200 | 210 | 220 | 230 | 240 |
| KYRLVSNYLT | TKDIMAAIRY | CRTNMAEFQK | KHLADIQKTM | IALFFCSRNE | VLSGTNDSHD |
| 250 | 260 | 270 | 280 | 290 | 300 |
| SIHHIISNNA | QLNIPQEYID | VLDLDWKSLE | LLFVREFCAA | LGMSLESPLD | IVVNAGAIAL |
| 310 | 320 | 330 | 340 | 350 | 360 |
| PILLKMSSIM | KKKHTEWTSQ | GELPVEIFLP | SSYHFHSVFT | CPVSKEQATE | ENPPMMMSCG |
| 370 | 380 | 390 | |||
| HVIVKESLRQ | LSRNGSQRFK | CPYCPNENVA | ADAIRVYF |