A8XV40
Gene name |
spas-1 (CBG19220) |
Protein name |
Probable spastin homolog spas-1 |
Names |
|
Species |
Caenorhabditis briggsae |
KEGG Pathway |
|
EC number |
5.6.1.1: Enzymes altering polypeptide conformation or assembly |
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 A8XV40
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A8XV40-F1 | Predicted | AlphaFoldDB |
No variants for A8XV40
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A8XV40 | |||||
No associated diseases with A8XV40
Functions
| Description | ||
|---|---|---|
| EC Number | 5.6.1.1 | Enzymes altering polypeptide conformation or assembly |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
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. |
| microtubule | Any of the long, generally straight, hollow tubes of internal diameter 12-15 nm and external diameter 24 nm found in a wide variety of eukaryotic cells; each consists (usually) of 13 protofilaments of polymeric tubulin, staggered in such a manner that the tubulin monomers are arranged in a helical pattern on the microtubular surface, and with the alpha/beta axes of the tubulin subunits parallel to the long axis of the tubule; exist in equilibrium with pool of tubulin monomers and can be rapidly assembled or disassembled in response to physiological stimuli; concerned with force generation, e.g. in the spindle. |
| microtubule cytoskeleton | The part of the cytoskeleton (the internal framework of a cell) composed of microtubules and associated proteins. |
| perinuclear region of cytoplasm | Cytoplasm situated near, or occurring around, the nucleus. |
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. |
| isomerase activity | Catalysis of the geometric or structural changes within one molecule. Isomerase is the systematic name for any enzyme of EC class 5. |
| microtubule severing ATPase activity | Catalysis of the reaction: ATP + H2O = ADP + phosphate. Catalysis of the severing of a microtubule at a specific spot along its length, coupled to the hydrolysis of ATP. |
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 |
| MFAFSKAPAG | CSTYERVTQK | FQDGSNKLRA | AIEMDELTKQ | NGTINEKLQT | AELYKQARQM |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LKEANEFNIM | DIPESKRSEV | REKREKTLNL | EKSAQDRLIK | ICNEVDPNMK | RASTAADPCR |
| 130 | 140 | 150 | 160 | 170 | 180 |
| AARITPRNTR | ATVPGDKKVS | KVKQTEKAPH | VCSRGDRCGA | HQPPPEKKST | PLKPVNQIRT |
| 190 | 200 | 210 | 220 | 230 | 240 |
| RVKENKNPIG | VQQQVFSFIL | SCCMRRNCRR | PHYLFPCMIS | LKMNYFKFQA | TLPNQLNTVN |
| 250 | 260 | 270 | 280 | 290 | 300 |
| RSNLLKGVDK | AIGERLLDEI | LDSTGVRMDD | VAGCHSAKAT | LEEAVILPAL | NPNLFSGLRQ |
| 310 | 320 | 330 | 340 | 350 | 360 |
| PVKGILLFGP | PGNGKTLLAK | AVAGESKQMF | FNISASSLTS | KWVGDSEKTI | RGLFQIARNG |
| 370 | 380 | 390 | 400 | 410 | 420 |
| QPSIIFIDEI | DSILCERSEK | DAEVSRRMKT | EFLVQFDGAT | SSPDDRILVI | GATNRPYELD |
| 430 | 440 | 450 | 460 | 470 | 480 |
| DAVLRRFPKR | IMLNLPDTEA | RKELITNTLK | KHDMMDGLSS | SDIRYIASNT | SGFSNSDLVA |
| 490 | 500 | 510 | 520 | 530 | 540 |
| LCKEAAMVPV | REIHRSKLSV | TDGDKIRKIR | ASDFDTALRT | IRPSTSDRIL | SKLSDFSRNF |
| GC |