Q8IDR3
Gene name |
MyoA |
Protein name |
Myosin-A |
Names |
PfMyoA |
Species |
Plasmodium falciparum (isolate 3D7) |
KEGG Pathway |
pfa:PF3D7_1342600 |
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
17 structures for Q8IDR3
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 4AOM | X-ray | 194 A | T | 799-816 | PDB |
| 4MZJ | X-ray | 147 A | T | 799-816 | PDB |
| 4MZK | X-ray | 182 A | T | 799-816 | PDB |
| 4MZL | X-ray | 201 A | C/D | 800-816 | PDB |
| 4R1E | X-ray | 198 A | B | 803-816 | PDB |
| 6I7D | X-ray | 282 A | A/B/C/D | 1-768 | PDB |
| 6I7E | X-ray | 349 A | A | 1-768 | PDB |
| 6TU7 | EM | 310 A | AP1/GP1 | 2-818 | PDB |
| 6YCX | X-ray | 399 A | A/B | 1-818 | PDB |
| 6YCY | X-ray | 255 A | A | 1-818 | PDB |
| 6YCZ | X-ray | 327 A | A | 1-818 | PDB |
| 6ZN3 | X-ray | 251 A | C/F/I/L/O | 775-816 | PDB |
| 7ALN | EM | 377 A | F | 1-818 | PDB |
| 8A12 | X-ray | 203 A | A | 1-818 | PDB |
| 8CDM | X-ray | 235 A | A | 1-818 | PDB |
| 8CDQ | X-ray | 221 A | A | 1-818 | PDB |
| AF-Q8IDR3-F1 | Predicted | AlphaFoldDB |
No variants for Q8IDR3
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q8IDR3 | |||||
No associated diseases with Q8IDR3
5 GO annotations of cellular component
| Name | Definition |
|---|---|
| actin cytoskeleton | The part of the cytoskeleton (the internal framework of a cell) composed of actin and associated proteins. Includes actin cytoskeleton-associated complexes. |
| inner membrane pellicle complex | A membrane structure formed of two closely aligned lipid bilayers that lie beneath the plasma membrane and form part of the pellicle surrounding an apicomplexan parasite cell. |
| myosin complex | A protein complex, formed of one or more myosin heavy chains plus associated light chains and other proteins, that functions as a molecular motor; uses the energy of ATP hydrolysis to move actin filaments or to move vesicles or other cargo on fixed actin filaments; has magnesium-ATPase activity and binds actin. Myosin classes are distinguished based on sequence features of the motor, or head, domain, but also have distinct tail regions that are believed to bind specific cargoes. |
| pellicle | The structure enclosing certain parasite cells such as certain apicomplexa and Euglenozoa; consists of the cell membrane with its associated infrastructure of microtubules, microfilaments and other organelles. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
5 GO annotations of molecular function
| Name | Definition |
|---|---|
| actin binding | Binding to monomeric or multimeric forms of actin, including actin filaments. |
| actin filament binding | Binding to an actin filament, also known as F-actin, a helical filamentous polymer of globular G-actin subunits. |
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| cytoskeletal motor activity | Generation of force resulting in movement, for example along a microfilament or microtubule, or in torque resulting in membrane scission or rotation of a flagellum. The energy required is obtained either from the hydrolysis of a nucleoside triphosphate or by an electrochemical proton gradient (proton-motive force). |
| microfilament motor activity | A motor activity that generates movement along a microfilament, driven by ATP hydrolysis. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| actin filament organization | A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of cytoskeletal structures comprising actin filaments. Includes processes that control the spatial distribution of actin filaments, such as organizing filaments into meshworks, bundles, or other structures, as by cross-linking. |
| vesicle transport along actin filament | Movement of a vesicle along an actin filament, mediated by motor proteins. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MAVTNEEIKT | ASKIVRRVSN | VEAFDKSGSV | FKGYQIWTDI | SPTIENDPNI | MFVKCVVQQG |
| 70 | 80 | 90 | 100 | 110 | 120 |
| SKKEKLTVVQ | IDPPGTGTPY | DIDPTHAWNC | NSQVDPMSFG | DIGLLNHTNI | PCVLDFLKHR |
| 130 | 140 | 150 | 160 | 170 | 180 |
| YLKNQIYTTA | VPLIVAINPY | KDLGNTTNEW | IRRYRDTADH | TKLPPHVFTC | AREALSNLHG |
| 190 | 200 | 210 | 220 | 230 | 240 |
| VNKSQTIIVS | GESGAGKTEA | TKQIMRYFAS | SKSGNMDLRI | QTAIMAANPV | LEAFGNAKTI |
| 250 | 260 | 270 | 280 | 290 | 300 |
| RNNNSSRFGR | FMQLVISHEG | GIRYGSVVAF | LLEKSRIITQ | DDNERSYHIF | YQFLKGANST |
| 310 | 320 | 330 | 340 | 350 | 360 |
| MKSKFGLKGV | TEYKLLNPNS | TEVSGVDDVK | DFEEVIESLK | NMELSESDIE | VIFSIVAGIL |
| 370 | 380 | 390 | 400 | 410 | 420 |
| TLGNVRLIEK | QEAGLSDAAA | IMDEDMGVFN | KACELMYLDP | ELIKREILIK | VTVAGGTKIE |
| 430 | 440 | 450 | 460 | 470 | 480 |
| GRWNKNDAEV | LKSSLCKAMY | EKLFLWIIRH | LNSRIEPEGG | FKTFMGMLDI | FGFEVFKNNS |
| 490 | 500 | 510 | 520 | 530 | 540 |
| LEQLFINITN | EMLQKNFVDI | VFERESKLYK | DEGISTAELK | YTSNKEVINV | LCEKGKSVLS |
| 550 | 560 | 570 | 580 | 590 | 600 |
| YLEDQCLAPG | GTDEKFVSSC | ATNLKENNKF | TPAKVASNKN | FIIQHTIGPI | QYCAESFLLK |
| 610 | 620 | 630 | 640 | 650 | 660 |
| NKDVLRGDLV | EVIKDSPNPI | VQQLFEGQVI | EKGKIAKGSL | IGSQFLNQLT | SLMNLINSTE |
| 670 | 680 | 690 | 700 | 710 | 720 |
| PHFIRCIKPN | ENKKPLEWCE | PKILIQLHAL | SILEALVLRQ | LGYSYRRTFE | EFLYQYKFVD |
| 730 | 740 | 750 | 760 | 770 | 780 |
| IAAAEDSSVE | NQNKCVNILK | LSGLSESMYK | IGKSMVFLKQ | EGAKILTKIQ | REKLVEWENC |
| 790 | 800 | 810 | |||
| VSVIEAAILK | HKYKQKVNKN | IPSLLRVQAH | IRKKMVAQ |