CATH Superfamily 1.20.5.4820
The name of this superfamily has been modified since the most recent official CATH+ release (v4_4_0). At the point of the last release, this superfamily was: waiting to be named.
FunFam 18:
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 5 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 |
---|---|---|
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).
|
1 | P34109 (/IPI) |
Phosphatidylinositol-3,4,5-trisphosphate binding GO:0005547
Interacting selectively and non-covalently with phosphatidylinositol-3,4,5-trisphosphate, a derivative of phosphatidylinositol in which the inositol ring is phosphorylated at the 3', 4' and 5' positions.
|
1 | P34109 (/HDA) |
Phosphatidylinositol-3,4,5-trisphosphate binding GO:0005547
Interacting selectively and non-covalently with phosphatidylinositol-3,4,5-trisphosphate, a derivative of phosphatidylinositol in which the inositol ring is phosphorylated at the 3', 4' and 5' positions.
|
1 | P34109 (/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 | P34109 (/IDA) |
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 | P34109 (/IDA) |
There are 3 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 |
---|---|---|
Phagocytosis, engulfment GO:0006911
The internalization of bacteria, immune complexes and other particulate matter or of an apoptotic cell by phagocytosis, including the membrane and cytoskeletal processes required, which involves one of three mechanisms: zippering of pseudopods around a target via repeated receptor-ligand interactions, sinking of the target directly into plasma membrane of the phagocytosing cell, or induced uptake via an enhanced membrane ruffling of the phagocytosing cell similar to macropinocytosis.
|
1 | P34109 (/IGI) |
Actin filament polymerization GO:0030041
Assembly of actin filaments by the addition of actin monomers to a filament.
|
1 | P34109 (/IGI) |
Chemotaxis to cAMP GO:0043327
The directed movement of a motile cell or organism in response to the presence of 3',5'-cAMP.
|
1 | P34109 (/IGI) |
There are 8 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 |
---|---|---|
Cytosol GO:0005829
The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
|
1 | P34109 (/IDA) |
Plasma membrane GO:0005886
The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
|
1 | P34109 (/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.
|
1 | P34109 (/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 | P34109 (/IDA) |
Cell leading edge GO:0031252
The area of a motile cell closest to the direction of movement.
|
1 | P34109 (/IDA) |
Cell-cell contact zone GO:0044291
Extended zone of intimate apposition between two cells containing one or more types of intercellular junctions, e.g., the intercalated disk of muscle.
|
1 | P34109 (/IDA) |
Spindle midzone GO:0051233
The area in the center of the spindle where the spindle microtubules from opposite poles overlap.
|
1 | P34109 (/IDA) |
Leading edge of lamellipodium GO:0061851
That part of the lamellipodium which represents the distal part of the structure.
|
1 | P34109 (/IDA) |