Q3B8D5
Gene name |
katnal2 |
Protein name |
Katanin p60 ATPase-containing subunit A-like 2 |
Names |
Katanin p60 subunit A-like 2, p60 katanin-like 2 |
Species |
Xenopus laevis (African clawed frog) |
KEGG Pathway |
xla:734847 |
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 Q3B8D5
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q3B8D5-F1 | Predicted | AlphaFoldDB |
No variants for Q3B8D5
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q3B8D5 | |||||
No associated diseases with Q3B8D5
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. |
| spindle | The array of microtubules and associated molecules that forms between opposite poles of a eukaryotic cell during mitosis or meiosis and serves to move the duplicated chromosomes apart. |
| spindle pole | Either of the ends of a spindle, where spindle microtubules are organized; usually contains a microtubule organizing center and accessory molecules, spindle microtubules and astral microtubules. |
5 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 binding | Binding to a microtubule, a filament composed of tubulin monomers. |
| 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. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| microtubule severing | The process in which a microtubule is broken down into smaller segments. Severing enzymes remove dimers from the middle of the filament to create new ends, unlike depolymerizing kinesins that use ATP to uncap microtubules at their ends. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MELSYQALRV | ASQNREAEEL | RTEARRKNLL | ILIMHYLLQE | GYVDSANSLE | QETKISSRRF |
| 70 | 80 | 90 | 100 | 110 | 120 |
| EVCDNVDLET | ILMEYESYYY | IKFQKYPKIT | KKALDHDSRV | QPKPRSAGKL | RRAGSNSTQG |
| 130 | 140 | 150 | 160 | 170 | 180 |
| LPRIGQQQVI | HRPVSSSYYR | TNGHQKALSR | ENSKQESGGN | SPQEASEVGL | NVSAISKASG |
| 190 | 200 | 210 | 220 | 230 | 240 |
| EGSHTRRRQV | IDFRSMIQDT | IKGASQEIAL | NSLNCNPDPS | ERLIKPVGAF | IGGNSEMREL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| AAVISRDIYL | QNPNVRWDDI | IGLDAAKRLV | KEAVVYPIRY | PQLFTGILSP | WKGLLLYGPP |
| 310 | 320 | 330 | 340 | 350 | 360 |
| GTGKTLLAKA | VATECNTTFF | NISASTIVSK | WRGDSEKLVR | VLFELARYHA | PSTIFLDELE |
| 370 | 380 | 390 | 400 | 410 | 420 |
| SVMSQRGTGP | GELDYAMLRR | LEKRILVDLP | SKEARQAMIQ | HWLPPISNSS | GVELRMDLDY |
| 430 | 440 | 450 | 460 | 470 | 480 |
| STLGEETDGY | SGSDIRLVCK | EAAMRPVRKI | FDALENHHSE | HKKLPVISLE | TVTTSDFSEV |
| 490 | 500 | ||||
| LAHTKPSAKS | LAEKYSAWQN | EFESV |