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actin-depolymerizing factor 5-like [Carya illinoinensis]
actin-depolymerizing factor 5( domain architecture ID 10791535)
actin-depolymerizing factor 5 (ADF-5) participates in drought stress by regulating stomatal closure, and may also serve as a potential downstream target of the drought stress/ABA signaling pathway via members of the ABF/AREB transcription factors family
List of domain hits
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Name | Accession | Description | Interval | E-value | |||
PLN03216 | PLN03216 | actin depolymerizing factor; Provisional |
32-172 | 6.50e-108 | |||
actin depolymerizing factor; Provisional : Pssm-ID: 178755 Cd Length: 141 Bit Score: 304.16 E-value: 6.50e-108
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Name | Accession | Description | Interval | E-value | |||
PLN03216 | PLN03216 | actin depolymerizing factor; Provisional |
32-172 | 6.50e-108 | |||
actin depolymerizing factor; Provisional Pssm-ID: 178755 Cd Length: 141 Bit Score: 304.16 E-value: 6.50e-108
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ADF_cofilin_like | cd11286 | Cofilin, Destrin, and related actin depolymerizing factors; Actin depolymerization factor ... |
39-171 | 4.82e-61 | |||
Cofilin, Destrin, and related actin depolymerizing factors; Actin depolymerization factor/cofilin-like domains (ADF domains) are present in a family of essential eukaryotic actin regulatory proteins. These proteins enhance the turnover rate of actin, and interact with actin monomers (G-actin) as well as actin filaments (F-actin), typically with a preference for ADP-G-actin subunits. The basic function of cofilin is to promote disassembly of aged actin filaments. Vertebrates have three isoforms of cofilin: cofilin-1 (Cfl1, non-muscle cofilin), cofilin-2 (muscle cofilin), and ADF (destrin). When bound to actin monomers, cofilins inhibit their spontaneous exchange of nucleotides. The cooperative binding to (aged) ADP-F-actin induces a local change in the actin filament structure and further promotes aging. Pssm-ID: 200442 Cd Length: 133 Bit Score: 185.07 E-value: 4.82e-61
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ADF | smart00102 | Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin ... |
45-172 | 3.19e-51 | |||
Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin monomers. Pssm-ID: 214516 Cd Length: 127 Bit Score: 160.14 E-value: 3.19e-51
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Cofilin_ADF | pfam00241 | Cofilin/tropomyosin-type actin-binding protein; Severs actin filaments and binds to actin ... |
47-169 | 2.88e-47 | |||
Cofilin/tropomyosin-type actin-binding protein; Severs actin filaments and binds to actin monomers. Pssm-ID: 459727 Cd Length: 123 Bit Score: 150.03 E-value: 2.88e-47
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Name | Accession | Description | Interval | E-value | |||
PLN03216 | PLN03216 | actin depolymerizing factor; Provisional |
32-172 | 6.50e-108 | |||
actin depolymerizing factor; Provisional Pssm-ID: 178755 Cd Length: 141 Bit Score: 304.16 E-value: 6.50e-108
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ADF_cofilin_like | cd11286 | Cofilin, Destrin, and related actin depolymerizing factors; Actin depolymerization factor ... |
39-171 | 4.82e-61 | |||
Cofilin, Destrin, and related actin depolymerizing factors; Actin depolymerization factor/cofilin-like domains (ADF domains) are present in a family of essential eukaryotic actin regulatory proteins. These proteins enhance the turnover rate of actin, and interact with actin monomers (G-actin) as well as actin filaments (F-actin), typically with a preference for ADP-G-actin subunits. The basic function of cofilin is to promote disassembly of aged actin filaments. Vertebrates have three isoforms of cofilin: cofilin-1 (Cfl1, non-muscle cofilin), cofilin-2 (muscle cofilin), and ADF (destrin). When bound to actin monomers, cofilins inhibit their spontaneous exchange of nucleotides. The cooperative binding to (aged) ADP-F-actin induces a local change in the actin filament structure and further promotes aging. Pssm-ID: 200442 Cd Length: 133 Bit Score: 185.07 E-value: 4.82e-61
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ADF | smart00102 | Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin ... |
45-172 | 3.19e-51 | |||
Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin monomers. Pssm-ID: 214516 Cd Length: 127 Bit Score: 160.14 E-value: 3.19e-51
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Cofilin_ADF | pfam00241 | Cofilin/tropomyosin-type actin-binding protein; Severs actin filaments and binds to actin ... |
47-169 | 2.88e-47 | |||
Cofilin/tropomyosin-type actin-binding protein; Severs actin filaments and binds to actin monomers. Pssm-ID: 459727 Cd Length: 123 Bit Score: 150.03 E-value: 2.88e-47
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ADF_gelsolin | cd00013 | Actin depolymerization factor/cofilin- and gelsolin-like domains; Actin depolymerization ... |
61-158 | 1.24e-22 | |||
Actin depolymerization factor/cofilin- and gelsolin-like domains; Actin depolymerization factor/cofilin-like domains are present in a family of essential eukaryotic actin regulatory proteins; these proteins enhance the turnover rate of actin and interact with actin monomers as well as actin filaments. Pssm-ID: 200435 Cd Length: 97 Bit Score: 86.36 E-value: 1.24e-22
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PTZ00152 | PTZ00152 | cofilin/actin-depolymerizing factor 1-like protein; Provisional |
39-150 | 1.77e-16 | |||
cofilin/actin-depolymerizing factor 1-like protein; Provisional Pssm-ID: 173441 Cd Length: 122 Bit Score: 71.14 E-value: 1.77e-16
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ADF_Twf-C_like | cd11284 | C-terminal ADF domain of twinfilin and related proteins; Actin depolymerization factor ... |
32-169 | 5.44e-12 | |||
C-terminal ADF domain of twinfilin and related proteins; Actin depolymerization factor/cofilin-like domains (ADF domains) are present in a family of essential eukaryotic actin regulatory proteins. Twinfilin contains two ADF domains, and inhibits the assembly of actin filaments by strongly interacting with monomeric ADP-actin (ADP-G-actin) in a 1:1 stochiometry (with it's C-terminal ADF domain, Twf-C) and inhibiting the actin monomer's nucleotide exchange. Mammalian twinfilin may also cap the barbed ends of F-actin filaments and prevent further assembly (or disassembly), in a process which requires both ADF domains. The N-terminal ADF domain (Twf-N) binds G-actin with a lower affinity than Twf-C; Twf-C can also bind F-actin. During capping, Twf-N may interact with the terminal actin subunit, and Twf-C may bind between two adjacent subunits at the side of the filament. Pssm-ID: 200440 Cd Length: 132 Bit Score: 59.94 E-value: 5.44e-12
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ADF_GMF-beta_like | cd11283 | ADF-homology domain of glia maturation factor beta and related proteins; Actin ... |
63-148 | 1.63e-10 | |||
ADF-homology domain of glia maturation factor beta and related proteins; Actin depolymerization factor/cofilin-like domains (ADF domains) are present in a family of essential eukaryotic actin regulatory proteins. Most of these proteins enhance the turnover rate of actin and interact with actin monomers as well as actin filaments. The glia maturation factor (GMF), however, does not bind actin but interacts with the Arp2/3 complex (which contains actin-related proteins, amongst others) and suppresses Arp2/3 activity, inducing the dissociation of branched daughter filaments from their mother filaments. This family includes both mammalian GMF isoforms, GMF-beta and GMF-gamma. GMF-beta regulates cellular growth, fission, differentiation and apoptosis. GMF-gamma is important in myeloid cell development and is an important regulator for cell migration and polarity in neutrophils. Pssm-ID: 200439 [Multi-domain] Cd Length: 122 Bit Score: 55.71 E-value: 1.63e-10
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ADF_Twf-N_like | cd11285 | N-terminal ADF domain of twinfilin and related proteins; Actin depolymerization factor ... |
39-162 | 2.16e-08 | |||
N-terminal ADF domain of twinfilin and related proteins; Actin depolymerization factor/cofilin-like domains (ADF domains) are present in a family of essential eukaryotic actin regulatory proteins. Twinfilin contains two ADF domains, and inhibits the assembly of actin filaments by strongly interacting with monomeric ADP-actin (ADP-G-actin) in a 1:1 stochiometry (with it's C-terminal ADF domain, Twf-C) and inhibiting the actin monomer's nucleotide exchange. Mammalian twinfilin may also cap the barbed ends of F-actin filaments and prevent further assembly (or disassembly), in a process which requires both ADF domains. The N-terminal ADF domain (Twf-N) binds G-actin with a lower affinity than Twf-C; Twf-C can also bind F-actin. During capping, Twf-N may interact with the terminal actin subunit, and Twf-C may bind between two adjacent subunits at the side of the filament. Pssm-ID: 200441 Cd Length: 139 Bit Score: 50.32 E-value: 2.16e-08
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ADF_coactosin_like | cd11282 | Coactosin-like members of the ADF homology domain family; Actin depolymerization factor ... |
63-162 | 5.97e-06 | |||
Coactosin-like members of the ADF homology domain family; Actin depolymerization factor/cofilin-like domains (ADF domains) are present in a family of essential eukaryotic actin regulatory proteins. Many of these proteins enhance the turnover rate of actin and interact with actin monomers as well as actin filaments. The function of coactosins is not well understood. They appear to interfere with the capping of actin filaments in Dictyostelium, and may not be able to bind monomeric globular actin. A role for coactosins as chaperones stabilizing 5-lipoxygenase (5LO) has been suggested; 5LO plays a crucial role in leukotriene synthesis. Pssm-ID: 200438 Cd Length: 114 Bit Score: 43.01 E-value: 5.97e-06
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