NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|18203409|sp|Q9R0P5|]
View 

RecName: Full=Destrin; AltName: Full=Actin-depolymerizing factor; Short=ADF; AltName: Full=Sid 23

Protein Classification

actin-binding ADF family protein( domain architecture ID 10181692)

actin-binding ADF family protein is an actin regulatory protein that enhance the turnover rate of actin, and interact with actin monomers (G-actin) as well as actin filaments (F-actin); such as actin depolymerization factor (ADF) and cofilin

CATH:  3.40.20.10
Gene Ontology:  GO:0003779|GO:0015629|GO:0030042
PubMed:  10461190|24836399|10611961|12049672
SCOP:  4001833

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ADF_cofilin_like cd11286
Cofilin, Destrin, and related actin depolymerizing factors; Actin depolymerization factor ...
 3-152 1.26e-50

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: 158.49  E-value: 1.26e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18203409   3 SGVQVADEVCRIFYDMKVRKCstpeeikkrKKAVIFCLSADKKCIVVEEgkeilVGDVGATitdpFKHFVGMLPEKDCRY 82
Cdd:cd11286   1 SGVKVSDECITAFNELKLKKK---------HKYIIFKISDDKKEIVVEK-----VGERDAS----YDDFLEKLPENECRY 62

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18203409  83 ALYDASFETK-ESRKEELMFFLWAPEQAPLKSKMIYASSKDAIKKKFPGIKHEYQANGPEDLNRTCIAEKL 152
Cdd:cd11286  63 AVYDFEYETKdGGKRSKLVFISWCPDTAPIKSKMLYASSKDALKKKLNGIKKEIQATDLSELSEEEILEKL 133
 
Name Accession Description Interval E-value
ADF_cofilin_like cd11286
Cofilin, Destrin, and related actin depolymerizing factors; Actin depolymerization factor ...
 3-152 1.26e-50

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: 158.49  E-value: 1.26e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18203409   3 SGVQVADEVCRIFYDMKVRKCstpeeikkrKKAVIFCLSADKKCIVVEEgkeilVGDVGATitdpFKHFVGMLPEKDCRY 82
Cdd:cd11286   1 SGVKVSDECITAFNELKLKKK---------HKYIIFKISDDKKEIVVEK-----VGERDAS----YDDFLEKLPENECRY 62

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18203409  83 ALYDASFETK-ESRKEELMFFLWAPEQAPLKSKMIYASSKDAIKKKFPGIKHEYQANGPEDLNRTCIAEKL 152
Cdd:cd11286  63 AVYDFEYETKdGGKRSKLVFISWCPDTAPIKSKMLYASSKDALKKKLNGIKKEIQATDLSELSEEEILEKL 133
ADF smart00102
Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin ...
 19-153 1.28e-44

Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin monomers.


Pssm-ID: 214516  Cd Length: 127  Bit Score: 143.19  E-value: 1.28e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18203409     19 KVRKCSTPEEIKKRK-KAVIFCLSADKKCIVVEEgkeilVGDVGatitDPFKHFVGMLPEKDCRYALYDASFETKESRKE 97
Cdd:smart00102   1 EDCKEAFNELKKKRKhSAIIFKIDKDNEEIVVEE-----VGSTE----DSYDEFVEELPEDECRYALYDYKFTTEESKKS 71

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 18203409     98 ELMFFLWAPEQAPLKSKMIYASSKDAIKKKFPGIKHEYQANGPEDLNRTCIAEKLG 153
Cdd:smart00102  72 KIVFIFWSPDGAPVKSKMLYASSKDTLKKELGGIQVEVQATDEDDLDEEALKEKLK 127
Cofilin_ADF pfam00241
Cofilin/tropomyosin-type actin-binding protein; Severs actin filaments and binds to actin ...
 27-150 6.62e-30

Cofilin/tropomyosin-type actin-binding protein; Severs actin filaments and binds to actin monomers.


Pssm-ID: 459727  Cd Length: 123  Bit Score: 105.35  E-value: 6.62e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18203409    27 EEIKKRKK--AVIFCLSADKKCIVVEEgkeilVGDVGATITDpfkhFVGMLPEKDCRYALYDASFETKESRK-EELMFFL 103
Cdd:pfam00241   6 QELRSDKKtnWIIFKIDDDKEEIVVEE-----TGEGGLSYDE----FLEELPDDEPRYAVYRFEYTHDDGSKrSKLVFIT 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 18203409   104 WAPEQAPLKSKMIYASSKDAIKKKFPGIKHEYQANGPEDLNRTCIAE 150
Cdd:pfam00241  77 WCPDGAPIKRKMLYASSKAALKRELKGIHVEIQATDPSELTEEEILE 123
PLN03216 PLN03216
actin depolymerizing factor; Provisional
 3-143 1.71e-19

actin depolymerizing factor; Provisional


Pssm-ID: 178755  Cd Length: 141  Bit Score: 79.58  E-value: 1.71e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18203409    3 SGVQVADEVCRIFYDMKvrkcstpeeIKKRKKAVIFCLSadkkcivvEEGKEILVGDVGATiTDPFKHFVGMLPEKDCRY 82
Cdd:PLN03216   8 TGMWVTDECKNSFMEMK---------WKKVHRYIVFKID--------EKSRKVTVDKVGGP-GESYDDLAASLPTDDCRY 69

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18203409   83 ALYDASFETKES-RKEELMFFLWAPEQAPLKSKMIYASSKDAIKKKFPGIKHEYQANGPEDL 143
Cdd:PLN03216  70 AVFDFDFVTVDNcRKSKIFFIAWSPEASRIRAKMLYATSKDGLRRVLDGVHYELQATDPTEM 131
 
Name Accession Description Interval E-value
ADF_cofilin_like cd11286
Cofilin, Destrin, and related actin depolymerizing factors; Actin depolymerization factor ...
 3-152 1.26e-50

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: 158.49  E-value: 1.26e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18203409   3 SGVQVADEVCRIFYDMKVRKCstpeeikkrKKAVIFCLSADKKCIVVEEgkeilVGDVGATitdpFKHFVGMLPEKDCRY 82
Cdd:cd11286   1 SGVKVSDECITAFNELKLKKK---------HKYIIFKISDDKKEIVVEK-----VGERDAS----YDDFLEKLPENECRY 62

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18203409  83 ALYDASFETK-ESRKEELMFFLWAPEQAPLKSKMIYASSKDAIKKKFPGIKHEYQANGPEDLNRTCIAEKL 152
Cdd:cd11286  63 AVYDFEYETKdGGKRSKLVFISWCPDTAPIKSKMLYASSKDALKKKLNGIKKEIQATDLSELSEEEILEKL 133
ADF smart00102
Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin ...
 19-153 1.28e-44

Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin monomers.


Pssm-ID: 214516  Cd Length: 127  Bit Score: 143.19  E-value: 1.28e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18203409     19 KVRKCSTPEEIKKRK-KAVIFCLSADKKCIVVEEgkeilVGDVGatitDPFKHFVGMLPEKDCRYALYDASFETKESRKE 97
Cdd:smart00102   1 EDCKEAFNELKKKRKhSAIIFKIDKDNEEIVVEE-----VGSTE----DSYDEFVEELPEDECRYALYDYKFTTEESKKS 71

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 18203409     98 ELMFFLWAPEQAPLKSKMIYASSKDAIKKKFPGIKHEYQANGPEDLNRTCIAEKLG 153
Cdd:smart00102  72 KIVFIFWSPDGAPVKSKMLYASSKDTLKKELGGIQVEVQATDEDDLDEEALKEKLK 127
Cofilin_ADF pfam00241
Cofilin/tropomyosin-type actin-binding protein; Severs actin filaments and binds to actin ...
 27-150 6.62e-30

Cofilin/tropomyosin-type actin-binding protein; Severs actin filaments and binds to actin monomers.


Pssm-ID: 459727  Cd Length: 123  Bit Score: 105.35  E-value: 6.62e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18203409    27 EEIKKRKK--AVIFCLSADKKCIVVEEgkeilVGDVGATITDpfkhFVGMLPEKDCRYALYDASFETKESRK-EELMFFL 103
Cdd:pfam00241   6 QELRSDKKtnWIIFKIDDDKEEIVVEE-----TGEGGLSYDE----FLEELPDDEPRYAVYRFEYTHDDGSKrSKLVFIT 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 18203409   104 WAPEQAPLKSKMIYASSKDAIKKKFPGIKHEYQANGPEDLNRTCIAE 150
Cdd:pfam00241  77 WCPDGAPIKRKMLYASSKAALKRELKGIHVEIQATDPSELTEEEILE 123
PLN03216 PLN03216
actin depolymerizing factor; Provisional
 3-143 1.71e-19

actin depolymerizing factor; Provisional


Pssm-ID: 178755  Cd Length: 141  Bit Score: 79.58  E-value: 1.71e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18203409    3 SGVQVADEVCRIFYDMKvrkcstpeeIKKRKKAVIFCLSadkkcivvEEGKEILVGDVGATiTDPFKHFVGMLPEKDCRY 82
Cdd:PLN03216   8 TGMWVTDECKNSFMEMK---------WKKVHRYIVFKID--------EKSRKVTVDKVGGP-GESYDDLAASLPTDDCRY 69

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18203409   83 ALYDASFETKES-RKEELMFFLWAPEQAPLKSKMIYASSKDAIKKKFPGIKHEYQANGPEDL 143
Cdd:PLN03216  70 AVFDFDFVTVDNcRKSKIFFIAWSPEASRIRAKMLYATSKDGLRRVLDGVHYELQATDPTEM 131
ADF_gelsolin cd00013
Actin depolymerization factor/cofilin- and gelsolin-like domains; Actin depolymerization ...
 34-138 9.09e-16

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: 68.64  E-value: 9.09e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18203409  34 KAVIFCLSADKKCIVVEEgkeilvgdvgaTITDPFKHFVGMLPEKDCRYALYDASFETKESRKEELMFFLWAPEQAPLKS 113
Cdd:cd00013   1 DWVLFKVDAKKEEIVVGS-----------TGAGFLDEFLEELPEDDPRYAFYRFKYPHSDDKRSKFVFISWIPDGVSIKQ 69

                        90       100
                ....*....|....*....|....*
gi 18203409 114 KMIYASSKDAIKKKFPGIKHEYQAN 138
Cdd:cd00013  70 KMVYATNKQTLKEALFGLAVPVQIR 94
PTZ00152 PTZ00152
cofilin/actin-depolymerizing factor 1-like protein; Provisional
 1-131 1.12e-14

cofilin/actin-depolymerizing factor 1-like protein; Provisional


Pssm-ID: 173441  Cd Length: 122  Bit Score: 66.51  E-value: 1.12e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18203409    1 MASGVQVADEVCRIFYDMKVRKCStpeeikkrkKAVIFclsadkkcivVEEGKEILVGDVGATITdpFKHFVGMLPEKD- 79
Cdd:PTZ00152   1 MISGIRVNDNCVTEFNNMKIRKTC---------RWIIF----------VIENCEIIIHSKGATTT--LTELVGSIDKNDk 59

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 18203409   80 --CRYALYDASfetkesrkEELMFFLWAPEQAPLKSKMIYASSKDAIKKKFPGI 131
Cdd:PTZ00152  60 iqCAYVVFDAV--------NKIHFFMYARESSNSRDRMTYASSKQALLKKIEGV 105
ADF_Twf-N_like cd11285
N-terminal ADF domain of twinfilin and related proteins; Actin depolymerization factor ...
 75-144 2.31e-07

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: 47.24  E-value: 2.31e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18203409  75 LPEKDCRYALYDASFETKESrkeELMFFLWAPEQAPLKSKMIYASSKDAIKKKFPG--IKHEYQANGPEDLN 144
Cdd:cd11285  59 LEEKEPCYILYRLDSKSAGY---EWVFISFVPDSAPVRQKMLYASTRATLKRELGSnhIKDELFATELEELT 127
ADF_GMF-beta_like cd11283
ADF-homology domain of glia maturation factor beta and related proteins; Actin ...
 75-129 8.16e-05

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: 40.30  E-value: 8.16e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 18203409  75 LPEKDCRYALYDASFETKESRKEELMFFL-WAPEQAPLKSKMIYASSKDAIKKKFP 129
Cdd:cd11283  53 LPEHSPRFVLYSYKMKHDDGRISYPLVLIyWSPQGCSPELQMLYAGAKELLVKEAE 108
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH