Q8IDR3 · MYOA_PLAF7

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.

1818100200300400500600700800
TypeIDPosition(s)Description
Binding site191-198ATP (UniProtKB | ChEBI)

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentactin cytoskeleton
Cellular Componentcytoplasm
Cellular Componentglideosome
Cellular Componentinner membrane pellicle complex
Cellular Componentmembrane
Cellular Componentmyosin complex
Cellular Componentpellicle
Cellular Componentplasma membrane
Molecular Functionactin binding
Molecular Functionactin filament binding
Molecular FunctionATP binding
Molecular Functioncytoskeletal motor activity
Molecular Functionmicrofilament motor activity
Biological Processactin filament organization

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Myosin-A
  • Alternative names
    • PfMyoA

Gene names

    • Name
      MyoA
    • ORF names
      PF13_0233, PF3D7_1342600

Organism names

Accessions

  • Primary accession
    Q8IDR3

Proteomes

Organism-specific databases

Subcellular Location

Cell membrane
; Peripheral membrane protein
Note: Tightly associated with the plasma membrane.

Keywords

PTM/Processing

Features

Showing features for chain, modified residue, modified residue (large scale data).

TypeIDPosition(s)SourceDescription
ChainPRO_00001233741-818UniProtMyosin-A
Modified residue19UniProtPhosphoserine; by PKG
Modified residue (large scale data)19PTMeXchangePhosphoserine
Modified residue (large scale data)61PTMeXchangePhosphoserine
Modified residue (large scale data)558PTMeXchangePhosphoserine

Keywords

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

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain97-771Myosin motor
Region661-671Actin-binding
Region773-818Tail

Domain

This protein differs from the typical myosin heavy chain structure in having head and tail domains but no discernible neck domain.

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    818
  • Mass (Da)
    92,277
  • Last updated
    2003-03-01 v1
  • Checksum
    F397875C52B3B19E
MAVTNEEIKTASKIVRRVSNVEAFDKSGSVFKGYQIWTDISPTIENDPNIMFVKCVVQQGSKKEKLTVVQIDPPGTGTPYDIDPTHAWNCNSQVDPMSFGDIGLLNHTNIPCVLDFLKHRYLKNQIYTTAVPLIVAINPYKDLGNTTNEWIRRYRDTADHTKLPPHVFTCAREALSNLHGVNKSQTIIVSGESGAGKTEATKQIMRYFASSKSGNMDLRIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLVISHEGGIRYGSVVAFLLEKSRIITQDDNERSYHIFYQFLKGANSTMKSKFGLKGVTEYKLLNPNSTEVSGVDDVKDFEEVIESLKNMELSESDIEVIFSIVAGILTLGNVRLIEKQEAGLSDAAAIMDEDMGVFNKACELMYLDPELIKREILIKVTVAGGTKIEGRWNKNDAEVLKSSLCKAMYEKLFLWIIRHLNSRIEPEGGFKTFMGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVDIVFERESKLYKDEGISTAELKYTSNKEVINVLCEKGKSVLSYLEDQCLAPGGTDEKFVSSCATNLKENNKFTPAKVASNKNFIIQHTIGPIQYCAESFLLKNKDVLRGDLVEVIKDSPNPIVQQLFEGQVIEKGKIAKGSLIGSQFLNQLTSLMNLINSTEPHFIRCIKPNENKKPLEWCEPKILIQLHALSILEALVLRQLGYSYRRTFEEFLYQYKFVDIAAAEDSSVENQNKCVNILKLSGLSESMYKIGKSMVFLKQEGAKILTKIQREKLVEWENCVSVIEAAILKHKYKQKVNKNIPSLLRVQAHIRKKMVAQ

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AL844509
EMBL· GenBank· DDBJ
CAD52556.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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