Q8IDR3 · MYOA_PLAF7
- ProteinMyosin-A
- GeneMyoA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids818 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails are presumed to bind to membranous compartments, which would be moved relative to actin filaments (By similarity).
Features
Showing features for binding site.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | actin cytoskeleton | |
Cellular Component | cytoplasm | |
Cellular Component | glideosome | |
Cellular Component | inner membrane pellicle complex | |
Cellular Component | membrane | |
Cellular Component | myosin complex | |
Cellular Component | pellicle | |
Cellular Component | plasma membrane | |
Molecular Function | actin binding | |
Molecular Function | actin filament binding | |
Molecular Function | ATP binding | |
Molecular Function | cytoskeletal motor activity | |
Molecular Function | microfilament motor activity | |
Biological Process | actin filament organization |
Keywords
- Molecular function
- Ligand
Names & Taxonomy
Protein names
- Recommended nameMyosin-A
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Sar > Alveolata > Apicomplexa > Aconoidasida > Haemosporida > Plasmodiidae > Plasmodium > Plasmodium (Laverania)
Accessions
- Primary accessionQ8IDR3
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Peripheral membrane protein
Note: Tightly associated with the plasma membrane.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000123374 | 1-818 | UniProt | Myosin-A | |||
Sequence: MAVTNEEIKTASKIVRRVSNVEAFDKSGSVFKGYQIWTDISPTIENDPNIMFVKCVVQQGSKKEKLTVVQIDPPGTGTPYDIDPTHAWNCNSQVDPMSFGDIGLLNHTNIPCVLDFLKHRYLKNQIYTTAVPLIVAINPYKDLGNTTNEWIRRYRDTADHTKLPPHVFTCAREALSNLHGVNKSQTIIVSGESGAGKTEATKQIMRYFASSKSGNMDLRIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLVISHEGGIRYGSVVAFLLEKSRIITQDDNERSYHIFYQFLKGANSTMKSKFGLKGVTEYKLLNPNSTEVSGVDDVKDFEEVIESLKNMELSESDIEVIFSIVAGILTLGNVRLIEKQEAGLSDAAAIMDEDMGVFNKACELMYLDPELIKREILIKVTVAGGTKIEGRWNKNDAEVLKSSLCKAMYEKLFLWIIRHLNSRIEPEGGFKTFMGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVDIVFERESKLYKDEGISTAELKYTSNKEVINVLCEKGKSVLSYLEDQCLAPGGTDEKFVSSCATNLKENNKFTPAKVASNKNFIIQHTIGPIQYCAESFLLKNKDVLRGDLVEVIKDSPNPIVQQLFEGQVIEKGKIAKGSLIGSQFLNQLTSLMNLINSTEPHFIRCIKPNENKKPLEWCEPKILIQLHALSILEALVLRQLGYSYRRTFEEFLYQYKFVDIAAAEDSSVENQNKCVNILKLSGLSESMYKIGKSMVFLKQEGAKILTKIQREKLVEWENCVSVIEAAILKHKYKQKVNKNIPSLLRVQAHIRKKMVAQ | |||||||
Modified residue | 19 | UniProt | Phosphoserine; by PKG | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 19 | PTMeXchange | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 61 | PTMeXchange | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 558 | PTMeXchange | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Developmental stage
Expressed during the asexual blood stage (at protein level).
Interaction
Subunit
Component of the glideosome complex composed of GAP50, GAP45, MTIP and MyoA; the complex is formed during the late schizont stage and in merozoites (PubMed:16750579).
MyoA, MTIP and GAP45 probably form an initial complex in the cytoplasm which is then recruited to the outer face of the inner membrane complex via the interaction with GAP50 (PubMed:16750579).
Interacts with ACT1
MyoA, MTIP and GAP45 probably form an initial complex in the cytoplasm which is then recruited to the outer face of the inner membrane complex via the interaction with GAP50 (PubMed:16750579).
Interacts with ACT1
Protein-protein interaction databases
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 97-771 | Myosin motor | ||||
Sequence: MSFGDIGLLNHTNIPCVLDFLKHRYLKNQIYTTAVPLIVAINPYKDLGNTTNEWIRRYRDTADHTKLPPHVFTCAREALSNLHGVNKSQTIIVSGESGAGKTEATKQIMRYFASSKSGNMDLRIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLVISHEGGIRYGSVVAFLLEKSRIITQDDNERSYHIFYQFLKGANSTMKSKFGLKGVTEYKLLNPNSTEVSGVDDVKDFEEVIESLKNMELSESDIEVIFSIVAGILTLGNVRLIEKQEAGLSDAAAIMDEDMGVFNKACELMYLDPELIKREILIKVTVAGGTKIEGRWNKNDAEVLKSSLCKAMYEKLFLWIIRHLNSRIEPEGGFKTFMGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVDIVFERESKLYKDEGISTAELKYTSNKEVINVLCEKGKSVLSYLEDQCLAPGGTDEKFVSSCATNLKENNKFTPAKVASNKNFIIQHTIGPIQYCAESFLLKNKDVLRGDLVEVIKDSPNPIVQQLFEGQVIEKGKIAKGSLIGSQFLNQLTSLMNLINSTEPHFIRCIKPNENKKPLEWCEPKILIQLHALSILEALVLRQLGYSYRRTFEEFLYQYKFVDIAAAEDSSVENQNKCVNILKLSGLSESMYKIGKSMVFLKQEGAKILTKIQR | ||||||
Region | 661-671 | Actin-binding | ||||
Sequence: PHFIRCIKPNE | ||||||
Region | 773-818 | Tail | ||||
Sequence: KLVEWENCVSVIEAAILKHKYKQKVNKNIPSLLRVQAHIRKKMVAQ |
Domain
This protein differs from the typical myosin heavy chain structure in having head and tail domains but no discernible neck domain.
Sequence similarities
Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Myosin family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length818
- Mass (Da)92,277
- Last updated2003-03-01 v1
- ChecksumF397875C52B3B19E
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AL844509 EMBL· GenBank· DDBJ | CAD52556.1 EMBL· GenBank· DDBJ | Genomic DNA |