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0MYO3A_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameMYO3A
DescriptionMyosin iiia (ec 2.7.1.37).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GON/A
Domain Architecture (Details)
InterPro domains unassigned to SynO:
Eukaryotic protein kinases are enzymesthat belong to a very extensive family of proteins which share a conserved catalytic core common withboth serine/threonine and tyrosine protein kinases. There are a number of conserved regions in thecatalytic domain of protein kinases. In the N-terminal extremity of the catalytic domain there is aglycine-rich stretch of residues in the vicinity of a lysine residue.hich has been shown to be involvedin ATP binding. In the central part of the catalytic domain there is a conserved aspartic acid residuewhich is important for the catalytic activity of the enzyme . CAUTION: Despite SMART having created two different HMMs for Serine/Threonine protein kinase and for Tyrosine protein kinase.arge number of proteins match both signatures.s SMART considers it to be natural for these two closely related families.
  IPR002290:Serine/threonine protein kinase
Calmodulin (CaM) is recognized as a major calcium sensor and orchestrator of regulatory events through its interaction with a diverse group of cellular proteins. Three classes of recognition motifs exist for many of the known CaM binding proteins; the IQ motif as a consensus for Ca2+-independent binding and two related motifs for Ca2+-dependent binding.ermed18-14 and 1-5-10 based on the position of conserved hydrophobic residues .The regulatory domain of scallop myosin is a three-chain protein complex that switches on this motor in response to Ca2+ binding. Side-chain interactions link the two light chains in tandem to adjacent segments of the heavy chain bearing the IQ-sequence motif. The Ca2+-binding site is a novel EF-hand motif on the essential light chain and is stabilized by linkages involving the heavy chain and both light chains.ccounting for the requirement of all three chains for Ca2+ binding and regulation in the intact myosin molecule .
  IPR000048:IQ calmodulin-binding region
Eukaryotic protein kinases are enzymesthat belong to a very extensive family of proteins which share a conserved catalytic core common withboth serine/threonine and tyrosine protein kinases. There are a number of conserved regions in thecatalytic domain of protein kinases. In the N-terminal extremity of the catalytic domain there is aglycine-rich stretch of residues in the vicinity of a lysine residue.hich has been shown to be involvedin ATP binding. In the central part of the catalytic domain there is a conserved aspartic acid residuewhich is important for the catalytic activity of the enzyme . This entry includes protein kinases from eukaryotes and viruses and may include some bacterial hits too.
  IPR000719:Protein kinase
Muscle contraction is caused by sliding between the thick and thin filaments of the myofibril. Myosin is a major component of thick filaments and exists as a hexamer of 2 heavy chains . alkali light chains.nd 2 regulatory light chains. The heavy chain can be subdivided into the N-terminal globular head and the C-terminal coiled-coil rod-like tail.lthough some forms have a globular region in their C-terminal. There are many cell-specific isoforms of myosin heavy chains.oded for by a multi-gene family . Myosin interacts with actin to convert chemical energy.n the form of ATP.o mechanical energy . The 3-D structure of the head portion of myosin has been determined and a model for actin-myosin complex has been constructed .The globular head is well conserved.ome highly-conserved regions possibly relating to functional and structural domains . The rod-like tail starts with an invariant proline residue.nd contains many repeats of a 28 residue region.nterrupted at 4 regularly-spaced points known as skip residues. Although the sequence of the tail is not well conserved.he chemical character is.ydrophobic.harged and skip residues occuring in a highly ordered and repeated fashion .
  IPR001609:Myosin head, motor region
Protein kinases () catalyze the phosphotransfer reaction fundamental to most signalling and regulatory processes in the eukaryotic cell . The catalytic subunit contains a core that is common to both serine/threonine and tyrosine protein kinases. The catalytic domain contains the nucleotide-binding site and the catalytic apparatus in an inter-lobe cleft. Structurally it shares functional and structural similarities with the ATP-grasp fold.hich is found in enzymes that catalyse the formation of an amide bond.nd with PIPK (phosphoinositol phosphate kinase). The three-dimensional fold of the protein kinase catalytic domain is similar to domains found in several other proteins. These include the catalytic domain of actin-fragmin kinase.n atypical protein kinase that regulates the F-actin capping activity in plasmodia ; the catalytic domain of phosphoinositide-3-kinase (PI3K).hich phosphorylates phosphoinositides and as such is involved in a number of fundamental cellular processes such as apoptosis.roliferation.otility and adhesion ; the catalytic domain of the MHCK/EF2 kinase.n atypical protein kinase that includes the TRP (transient channel potential) calcium-channel kinase involved in the modulation of calcium channels in eukaryotic cells in response to external signals ; choline kinase.hich catalyses the ATP-dependent phosphorylation of choline during the biosynthesis of phosphatidylcholine ; and 3.-aminoglycoside phosphotransferase type IIIa. bacterial enzyme that confers resistance to a range of aminoglycoside antibiotics .
  IPR011009:Protein kinase-like
IPR001609:MYSc 
Evalue:-248.49485002168 
Location:332-1054IPR002290:S_TKc 
Evalue:-89.8239087409443 
Location:21-287IPR000048:IQ 
Evalue:-2.33724212646484 
Location:1347-1367IPR000048:IQ 
Evalue:-1.49485003948212 
Location:1056-1076IPR000048:IQ 
Evalue:-1.05060994625092 
Location:1083-1103IPR008271:PROTEIN_KINASE_ST 
Evalue:0 
Location:0-0
SequencesProtein: MYO3A_HUMAN (1616 aa)
mRNA: NM_017433
Local Annotation
Synapse Ontology
transport of vesicles in the presynaptic neuron
sdb:0017 Mobilization: synapsins, CAM kinase I  (Evidence:keywords)
activation of protein kinase C
sdb:0206 activation of protein kinase C  (Evidence:keywords)
KO assignmentK00870
  Level 3 annotation:
    protein kinase
  Level 2 annotation:
    Signal transduction mechanisms
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 21 residues, 26263201-26263263Exon2: 31 residues, 26264678-26264765Exon3: 63 residues, 26281028-26281213Exon4: 47 residues, 26283808-26283943Exon5: 37 residues, 26325424-26325529Exon6: 35 residues, 26326093-26326193Exon7: 27 residues, 26345754-26345831Exon8: 50 residues, 26350437-26350583Exon9: 24 residues, 26352956-26353022Exon10: 54 residues, 26355311-26355467Exon11: 35 residues, 26395909-26396009Exon12: 41 residues, 26397702-26397819Exon13: 37 residues, 26399045-26399150Exon14: 30 residues, 26399252-26399336Exon15: 69 residues, 26417137-26417340Exon16: 35 residues, 26425315-26425414Exon17: 40 residues, 26425502-26425617Exon18: 44 residues, 26449610-26449737Exon19: 72 residues, 26454332-26454543Exon20: 51 residues, 26457325-26457473Exon21: 53 residues, 26472382-26472536Exon22: 31 residues, 26474380-26474469Exon23: 45 residues, 26476364-26476494Exon24: 28 residues, 26482784-26482864Exon25: 28 residues, 26483680-26483758Exon26: 70 residues, 26486244-26486450Exon27: 39 residues, 26495001-26495113Exon28: 56 residues, 26497646-26497809Exon29: 43 residues, 26499350-26499474Exon30: 300 residues, 26502597-26503492Exon31: 50 residues, 26505635-26505780Exon32: 37 residues, 26522139-26522246Exon33: 15 residues, 26530199-26530240Exon34: 50 residues, 26531898-26532042Exon35: 230 residues, 26540777-26541461Exon36: 2 residues, -Jump to MYO3A_HUMAN  
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