CATH Superfamily 1.20.58.530
The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_0). At the point of the last release, this superfamily was: waiting to be named.
FunFam 10: Myosin IIIA
Please note: GO annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.
There are 25 GO terms relating to "molecular function"
The search results have been sorted with the annotations that are found most frequently at the top of the
list. The results can be filtered by typing text into the search box at the top of the table.
GO Term | Annotations | Evidence |
---|---|---|
Microfilament motor activity GO:0000146
Catalysis of movement along a microfilament, coupled to the hydrolysis of a nucleoside triphosphate (usually ATP).
|
3 | Q1EG27 (/IDA) Q8K3H5 (/IDA) Q8NEV4 (/IDA) |
Protein binding GO:0005515
Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules).
|
3 | Q1EG27 (/IPI) Q8K3H5 (/IPI) Q8NEV4 (/IPI) |
Motor activity GO:0003774
Catalysis of the generation of force resulting either in movement along a microfilament or microtubule, or in torque resulting in membrane scission, coupled to the hydrolysis of a nucleoside triphosphate.
|
2 | Q381F5 (/ISM) Q4Q4N5 (/ISM) |
Protein serine/threonine kinase activity GO:0004674
Catalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate, and ATP + protein threonine = ADP + protein threonine phosphate.
|
2 | Q1EG27 (/IDA) Q8K3H5 (/IDA) |
Calmodulin binding GO:0005516
Interacting selectively and non-covalently with calmodulin, a calcium-binding protein with many roles, both in the calcium-bound and calcium-free states.
|
2 | Q8NEV4 (/IDA) Q9DG88 (/IDA) |
Microfilament motor activity GO:0000146
Catalysis of movement along a microfilament, coupled to the hydrolysis of a nucleoside triphosphate (usually ATP).
|
1 | Q8NEV4 (/IMP) |
Microfilament motor activity GO:0000146
Catalysis of movement along a microfilament, coupled to the hydrolysis of a nucleoside triphosphate (usually ATP).
|
1 | Q8K3H5 (/ISO) |
Microfilament motor activity GO:0000146
Catalysis of movement along a microfilament, coupled to the hydrolysis of a nucleoside triphosphate (usually ATP).
|
1 | Q8K3H5 (/ISS) |
Actin binding GO:0003779
Interacting selectively and non-covalently with monomeric or multimeric forms of actin, including actin filaments.
|
1 | Q9DG88 (/IDA) |
Protein kinase activity GO:0004672
Catalysis of the phosphorylation of an amino acid residue in a protein, usually according to the reaction: a protein + ATP = a phosphoprotein + ADP.
|
1 | Q8NEV4 (/IDA) |
Protein kinase activity GO:0004672
Catalysis of the phosphorylation of an amino acid residue in a protein, usually according to the reaction: a protein + ATP = a phosphoprotein + ADP.
|
1 | Q8K3H5 (/ISO) |
Protein kinase activity GO:0004672
Catalysis of the phosphorylation of an amino acid residue in a protein, usually according to the reaction: a protein + ATP = a phosphoprotein + ADP.
|
1 | Q8K3H5 (/ISS) |
Calmodulin binding GO:0005516
Interacting selectively and non-covalently with calmodulin, a calcium-binding protein with many roles, both in the calcium-bound and calcium-free states.
|
1 | Q8K3H5 (/ISO) |
Calmodulin binding GO:0005516
Interacting selectively and non-covalently with calmodulin, a calcium-binding protein with many roles, both in the calcium-bound and calcium-free states.
|
1 | Q8K3H5 (/ISS) |
Actin-dependent ATPase activity GO:0030898
Catalysis of the reaction: ATP + H2O = ADP + phosphate. This reaction requires the presence of an actin filament to accelerate release of ADP and phosphate.
|
1 | Q8NEV4 (/IDA) |
Actin-dependent ATPase activity GO:0030898
Catalysis of the reaction: ATP + H2O = ADP + phosphate. This reaction requires the presence of an actin filament to accelerate release of ADP and phosphate.
|
1 | Q8K3H5 (/ISO) |
Actin-dependent ATPase activity GO:0030898
Catalysis of the reaction: ATP + H2O = ADP + phosphate. This reaction requires the presence of an actin filament to accelerate release of ADP and phosphate.
|
1 | Q8K3H5 (/ISS) |
ADP binding GO:0043531
Interacting selectively and non-covalently with ADP, adenosine 5'-diphosphate.
|
1 | Q8NEV4 (/IDA) |
ADP binding GO:0043531
Interacting selectively and non-covalently with ADP, adenosine 5'-diphosphate.
|
1 | Q8K3H5 (/ISO) |
ADP binding GO:0043531
Interacting selectively and non-covalently with ADP, adenosine 5'-diphosphate.
|
1 | Q8K3H5 (/ISS) |
Protein-containing complex binding GO:0044877
Interacting selectively and non-covalently with a macromolecular complex.
|
1 | Q381F5 (/IPI) |
Actin filament binding GO:0051015
Interacting selectively and non-covalently with an actin filament, also known as F-actin, a helical filamentous polymer of globular G-actin subunits.
|
1 | Q8K3H5 (/IDA) |
Plus-end directed microfilament motor activity GO:0060002
Catalysis of movement along a microfilament towards the plus end, coupled to the hydrolysis of a nucleoside triphosphate (usually ATP). The plus end of an actin filament is the end that preferentially adds actin monomers.
|
1 | Q8NEV4 (/IDA) |
Plus-end directed microfilament motor activity GO:0060002
Catalysis of movement along a microfilament towards the plus end, coupled to the hydrolysis of a nucleoside triphosphate (usually ATP). The plus end of an actin filament is the end that preferentially adds actin monomers.
|
1 | Q8K3H5 (/ISO) |
Plus-end directed microfilament motor activity GO:0060002
Catalysis of movement along a microfilament towards the plus end, coupled to the hydrolysis of a nucleoside triphosphate (usually ATP). The plus end of an actin filament is the end that preferentially adds actin monomers.
|
1 | Q8K3H5 (/ISS) |
There are 16 GO terms relating to "biological process"
The search results have been sorted with the annotations that are found most frequently at the top of the
list. The results can be filtered by typing text into the search box at the top of the table.
GO Term | Annotations | Evidence |
---|---|---|
Sensory perception of sound GO:0007605
The series of events required for an organism to receive an auditory stimulus, convert it to a molecular signal, and recognize and characterize the signal. Sonic stimuli are detected in the form of vibrations and are processed to form a sound.
|
3 | Q1EG27 (/IMP) Q8K3H5 (/IMP) Q8NEV4 (/IMP) |
Sensory perception of sound GO:0007605
The series of events required for an organism to receive an auditory stimulus, convert it to a molecular signal, and recognize and characterize the signal. Sonic stimuli are detected in the form of vibrations and are processed to form a sound.
|
3 | Q8K3H5 (/ISS) Q8NEV4 (/ISS) Q8WXR4 (/ISS) |
Protein autophosphorylation GO:0046777
The phosphorylation by a protein of one or more of its own amino acid residues (cis-autophosphorylation), or residues on an identical protein (trans-autophosphorylation).
|
3 | Q1EG27 (/IDA) Q8K3H5 (/IDA) Q8NEV4 (/IDA) |
Sensory perception of sound GO:0007605
The series of events required for an organism to receive an auditory stimulus, convert it to a molecular signal, and recognize and characterize the signal. Sonic stimuli are detected in the form of vibrations and are processed to form a sound.
|
2 | Q1EG27 (/IGI) Q8K3H5 (/IGI) |
Peptidyl-serine phosphorylation GO:0018105
The phosphorylation of peptidyl-serine to form peptidyl-O-phospho-L-serine.
|
2 | Q1EG27 (/IDA) Q8K3H5 (/IDA) |
Peptidyl-threonine phosphorylation GO:0018107
The phosphorylation of peptidyl-threonine to form peptidyl-O-phospho-L-threonine.
|
2 | Q1EG27 (/IDA) Q8K3H5 (/IDA) |
Auditory receptor cell stereocilium organization GO:0060088
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a stereocilium. A stereocilium is an actin-based protrusion from the apical surface of auditory hair cells.
|
2 | Q1EG27 (/IGI) Q8K3H5 (/IGI) |
Auditory receptor cell stereocilium organization GO:0060088
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a stereocilium. A stereocilium is an actin-based protrusion from the apical surface of auditory hair cells.
|
2 | Q1EG27 (/IMP) Q8K3H5 (/IMP) |
Cochlea morphogenesis GO:0090103
The process in which the cochlea is generated and organized.
|
2 | Q1EG27 (/IMP) Q8K3H5 (/IMP) |
Cochlea morphogenesis GO:0090103
The process in which the cochlea is generated and organized.
|
2 | Q8NEV4 (/ISS) Q8WXR4 (/ISS) |
Sensory perception of sound GO:0007605
The series of events required for an organism to receive an auditory stimulus, convert it to a molecular signal, and recognize and characterize the signal. Sonic stimuli are detected in the form of vibrations and are processed to form a sound.
|
1 | Q8K3H5 (/ISO) |
Protein autophosphorylation GO:0046777
The phosphorylation by a protein of one or more of its own amino acid residues (cis-autophosphorylation), or residues on an identical protein (trans-autophosphorylation).
|
1 | Q8K3H5 (/ISO) |
Protein autophosphorylation GO:0046777
The phosphorylation by a protein of one or more of its own amino acid residues (cis-autophosphorylation), or residues on an identical protein (trans-autophosphorylation).
|
1 | Q8K3H5 (/ISS) |
Inner ear development GO:0048839
The process whose specific outcome is the progression of the inner ear over time, from its formation to the mature structure.
|
1 | Q8K3H5 (/IMP) |
Positive regulation of filopodium assembly GO:0051491
Any process that activates or increases the frequency, rate or extent of the assembly of a filopodium, a thin, stiff protrusion extended by the leading edge of a motile cell such as a crawling fibroblast or amoeba, or an axonal growth cone.
|
1 | Q8K3H5 (/IGI) |
Positive regulation of filopodium assembly GO:0051491
Any process that activates or increases the frequency, rate or extent of the assembly of a filopodium, a thin, stiff protrusion extended by the leading edge of a motile cell such as a crawling fibroblast or amoeba, or an axonal growth cone.
|
1 | Q1EG27 (/IPI) |
There are 19 GO terms relating to "cellular component"
The search results have been sorted with the annotations that are found most frequently at the top of the
list. The results can be filtered by typing text into the search box at the top of the table.
GO Term | Annotations | Evidence |
---|---|---|
Photoreceptor inner segment GO:0001917
The inner segment of a vertebrate photoreceptor containing mitochondria, ribosomes and membranes where opsin molecules are assembled and passed to be part of the outer segment discs.
|
2 | Q1EG27 (/IDA) Q8K3H5 (/IDA) |
Myosin complex GO:0016459
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.
|
2 | Q381F5 (/ISM) Q4Q4N5 (/ISM) |
Filopodium GO:0030175
Thin, stiff, actin-based protrusion extended by the leading edge of a motile cell such as a crawling fibroblast or amoeba, or an axonal or dendritic growth cone, or a dendritic shaft.
|
2 | Q8NEV4 (/IDA) Q9DG88 (/IDA) |
Stereocilium tip GO:0032426
A distinct compartment at the tip of a stereocilium, distal to the site of attachment to the apical cell surface. It consists of a dense matrix bridging the barbed ends of the stereocilium actin filaments with the overlying plasma membrane, is dynamic compared to the shaft, and is required for stereocilium elongation.
|
2 | Q1EG27 (/EXP) Q8K3H5 (/EXP) |
Stereocilium tip GO:0032426
A distinct compartment at the tip of a stereocilium, distal to the site of attachment to the apical cell surface. It consists of a dense matrix bridging the barbed ends of the stereocilium actin filaments with the overlying plasma membrane, is dynamic compared to the shaft, and is required for stereocilium elongation.
|
2 | Q1EG27 (/IDA) Q8K3H5 (/IDA) |
Stereocilium tip GO:0032426
A distinct compartment at the tip of a stereocilium, distal to the site of attachment to the apical cell surface. It consists of a dense matrix bridging the barbed ends of the stereocilium actin filaments with the overlying plasma membrane, is dynamic compared to the shaft, and is required for stereocilium elongation.
|
2 | Q8NEV4 (/ISS) Q8WXR4 (/ISS) |
Filopodium tip GO:0032433
The end of a filopodium distal to the body of the cell.
|
2 | Q8K3H5 (/IDA) Q8NEV4 (/IDA) |
Photoreceptor outer segment GO:0001750
The outer segment of a vertebrate photoreceptor that contains a stack of membrane discs embedded with photoreceptor proteins.
|
1 | Q1EG27 (/IDA) |
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
1 | Q8NEV4 (/IDA) |
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
1 | Q8K3H5 (/ISO) |
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
1 | Q8K3H5 (/ISS) |
Actin filament GO:0005884
A filamentous structure formed of a two-stranded helical polymer of the protein actin and associated proteins. Actin filaments are a major component of the contractile apparatus of skeletal muscle and the microfilaments of the cytoskeleton of eukaryotic cells. The filaments, comprising polymerized globular actin molecules, appear as flexible structures with a diameter of 5-9 nm. They are organized into a variety of linear bundles, two-dimensional networks, and three dimensional gels. In the cytoskeleton they are most highly concentrated in the cortex of the cell just beneath the plasma membrane.
|
1 | Q9DG88 (/IDA) |
Filopodium GO:0030175
Thin, stiff, actin-based protrusion extended by the leading edge of a motile cell such as a crawling fibroblast or amoeba, or an axonal or dendritic growth cone, or a dendritic shaft.
|
1 | Q8K3H5 (/ISO) |
Filopodium GO:0030175
Thin, stiff, actin-based protrusion extended by the leading edge of a motile cell such as a crawling fibroblast or amoeba, or an axonal or dendritic growth cone, or a dendritic shaft.
|
1 | Q8K3H5 (/ISS) |
Filamentous actin GO:0031941
A two-stranded helical polymer of the protein actin.
|
1 | Q8NEV4 (/IDA) |
Filamentous actin GO:0031941
A two-stranded helical polymer of the protein actin.
|
1 | Q8K3H5 (/ISO) |
Filamentous actin GO:0031941
A two-stranded helical polymer of the protein actin.
|
1 | Q8K3H5 (/ISS) |
Filopodium tip GO:0032433
The end of a filopodium distal to the body of the cell.
|
1 | Q1EG27 (/IPI) |
Filopodium tip GO:0032433
The end of a filopodium distal to the body of the cell.
|
1 | Q8K3H5 (/ISO) |