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Conserved domains on  [gi|5031635|ref|NP_005498|]
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cofilin-1 [Homo sapiens]

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

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List of domain hits

 Name Accession Description Interval E-value
ADF_cofilin_like cd11286
Cofilin, Destrin, and related actin depolymerizing factors; Actin depolymerization factor ...
 3-153 1.94e-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: 158.10  E-value: 1.94e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031635    3 SGVAVSDGVIKVFNDMKVRKSstpeevkkrKKAVLFCLSEDKKNIILEEgkeilVGDVgqtvDDPYATFVKMLPDKDCRY 82
Cdd:cd11286   1 SGVKVSDECITAFNELKLKKK---------HKYIIFKISDDKKEIVVEK-----VGER----DASYDDFLEKLPENECRY 62

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5031635   83 ALYDATYETK-ESKKEDLVFIFWAPESAPLKSKMIYASSKDAIKKKLTGIKHELQANCYEEVkDRCTLAEKL 153
Cdd:cd11286  63 AVYDFEYETKdGGKRSKLVFISWCPDTAPIKSKMLYASSKDALKKKLNGIKKEIQATDLSEL-SEEEILEKL 133
 
Name Accession Description Interval E-value
ADF_cofilin_like cd11286
Cofilin, Destrin, and related actin depolymerizing factors; Actin depolymerization factor ...
 3-153 1.94e-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: 158.10  E-value: 1.94e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031635    3 SGVAVSDGVIKVFNDMKVRKSstpeevkkrKKAVLFCLSEDKKNIILEEgkeilVGDVgqtvDDPYATFVKMLPDKDCRY 82
Cdd:cd11286   1 SGVKVSDECITAFNELKLKKK---------HKYIIFKISDDKKEIVVEK-----VGER----DASYDDFLEKLPENECRY 62

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5031635   83 ALYDATYETK-ESKKEDLVFIFWAPESAPLKSKMIYASSKDAIKKKLTGIKHELQANCYEEVkDRCTLAEKL 153
Cdd:cd11286  63 AVYDFEYETKdGGKRSKLVFISWCPDTAPIKSKMLYASSKDALKKKLNGIKKEIQATDLSEL-SEEEILEKL 133
ADF smart00102
Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin ...
 19-154 6.61e-43

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


Pssm-ID: 214516  Cd Length: 127  Bit Score: 138.96  E-value: 6.61e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031635      19 KVRKSSTPEEVKKRK-KAVLFCLSEDKKNIILEEgkeilvgdVGQTvDDPYATFVKMLPDKDCRYALYDATYETKESKKE 97
Cdd:smart00102   1 EDCKEAFNELKKKRKhSAIIFKIDKDNEEIVVEE--------VGST-EDSYDEFVEELPEDECRYALYDYKFTTEESKKS 71

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 5031635      98 DLVFIFWAPESAPLKSKMIYASSKDAIKKKLTGIKHELQANCYEEVkDRCTLAEKLG 154
Cdd:smart00102  72 KIVFIFWSPDGAPVKSKMLYASSKDTLKKELGGIQVEVQATDEDDL-DEEALKEKLK 127
Cofilin_ADF pfam00241
Cofilin/tropomyosin-type actin-binding protein; Severs actin filaments and binds to actin ...
 27-143 4.93e-32

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


Pssm-ID: 459727  Cd Length: 123  Bit Score: 111.13  E-value: 4.93e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031635     27 EEVKKRKK--AVLFCLSEDKKNIILEEgkeilVGDVGQTVDDpyatFVKMLPDKDCRYALYDATYETK-ESKKEDLVFIF 103
Cdd:pfam00241   6 QELRSDKKtnWIIFKIDDDKEEIVVEE-----TGEGGLSYDE----FLEELPDDEPRYAVYRFEYTHDdGSKRSKLVFIT 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 5031635    104 WAPESAPLKSKMIYASSKDAIKKKLTGIKHELQANCYEEV 143
Cdd:pfam00241  77 WCPDGAPIKRKMLYASSKAALKRELKGIHVEIQATDPSEL 116
PLN03216 PLN03216
actin depolymerizing factor; Provisional
 3-146 3.96e-19

actin depolymerizing factor; Provisional


Pssm-ID: 178755  Cd Length: 141  Bit Score: 78.43  E-value: 3.96e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031635     3 SGVAVSDGVIKVFNDMKVrksstpeevKKRKKAVLFCLSEDKKNIILEEgkeilVGDVGQTVDDPYATfvkmLPDKDCRY 82
Cdd:PLN03216   8 TGMWVTDECKNSFMEMKW---------KKVHRYIVFKIDEKSRKVTVDK-----VGGPGESYDDLAAS----LPTDDCRY 69

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031635    83 ALYDATYETKES-KKEDLVFIFWAPESAPLKSKMIYASSKDAIKKKLTGIKHELQAN-----CYEEVKDR 146
Cdd:PLN03216  70 AVFDFDFVTVDNcRKSKIFFIAWSPEASRIRAKMLYATSKDGLRRVLDGVHYELQATdptemGFDVIRDR 139
 
Name Accession Description Interval E-value
ADF_cofilin_like cd11286
Cofilin, Destrin, and related actin depolymerizing factors; Actin depolymerization factor ...
 3-153 1.94e-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: 158.10  E-value: 1.94e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031635    3 SGVAVSDGVIKVFNDMKVRKSstpeevkkrKKAVLFCLSEDKKNIILEEgkeilVGDVgqtvDDPYATFVKMLPDKDCRY 82
Cdd:cd11286   1 SGVKVSDECITAFNELKLKKK---------HKYIIFKISDDKKEIVVEK-----VGER----DASYDDFLEKLPENECRY 62

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5031635   83 ALYDATYETK-ESKKEDLVFIFWAPESAPLKSKMIYASSKDAIKKKLTGIKHELQANCYEEVkDRCTLAEKL 153
Cdd:cd11286  63 AVYDFEYETKdGGKRSKLVFISWCPDTAPIKSKMLYASSKDALKKKLNGIKKEIQATDLSEL-SEEEILEKL 133
ADF smart00102
Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin ...
 19-154 6.61e-43

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


Pssm-ID: 214516  Cd Length: 127  Bit Score: 138.96  E-value: 6.61e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031635      19 KVRKSSTPEEVKKRK-KAVLFCLSEDKKNIILEEgkeilvgdVGQTvDDPYATFVKMLPDKDCRYALYDATYETKESKKE 97
Cdd:smart00102   1 EDCKEAFNELKKKRKhSAIIFKIDKDNEEIVVEE--------VGST-EDSYDEFVEELPEDECRYALYDYKFTTEESKKS 71

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 5031635      98 DLVFIFWAPESAPLKSKMIYASSKDAIKKKLTGIKHELQANCYEEVkDRCTLAEKLG 154
Cdd:smart00102  72 KIVFIFWSPDGAPVKSKMLYASSKDTLKKELGGIQVEVQATDEDDL-DEEALKEKLK 127
Cofilin_ADF pfam00241
Cofilin/tropomyosin-type actin-binding protein; Severs actin filaments and binds to actin ...
 27-143 4.93e-32

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


Pssm-ID: 459727  Cd Length: 123  Bit Score: 111.13  E-value: 4.93e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031635     27 EEVKKRKK--AVLFCLSEDKKNIILEEgkeilVGDVGQTVDDpyatFVKMLPDKDCRYALYDATYETK-ESKKEDLVFIF 103
Cdd:pfam00241   6 QELRSDKKtnWIIFKIDDDKEEIVVEE-----TGEGGLSYDE----FLEELPDDEPRYAVYRFEYTHDdGSKRSKLVFIT 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 5031635    104 WAPESAPLKSKMIYASSKDAIKKKLTGIKHELQANCYEEV 143
Cdd:pfam00241  77 WCPDGAPIKRKMLYASSKAALKRELKGIHVEIQATDPSEL 116
PLN03216 PLN03216
actin depolymerizing factor; Provisional
 3-146 3.96e-19

actin depolymerizing factor; Provisional


Pssm-ID: 178755  Cd Length: 141  Bit Score: 78.43  E-value: 3.96e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031635     3 SGVAVSDGVIKVFNDMKVrksstpeevKKRKKAVLFCLSEDKKNIILEEgkeilVGDVGQTVDDPYATfvkmLPDKDCRY 82
Cdd:PLN03216   8 TGMWVTDECKNSFMEMKW---------KKVHRYIVFKIDEKSRKVTVDK-----VGGPGESYDDLAAS----LPTDDCRY 69

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031635    83 ALYDATYETKES-KKEDLVFIFWAPESAPLKSKMIYASSKDAIKKKLTGIKHELQAN-----CYEEVKDR 146
Cdd:PLN03216  70 AVFDFDFVTVDNcRKSKIFFIAWSPEASRIRAKMLYATSKDGLRRVLDGVHYELQATdptemGFDVIRDR 139
ADF_gelsolin cd00013
Actin depolymerization factor/cofilin- and gelsolin-like domains; Actin depolymerization ...
 53-138 5.52e-18

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: 74.42  E-value: 5.52e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031635   53 KEILVGDVGQTVDDpyaTFVKMLPDKDCRYALYDATYETKESKKEDLVFIFWAPESAPLKSKMIYASSKDAIKKKLTGIK 132
Cdd:cd00013  12 EEIVVGSTGAGFLD---EFLEELPEDDPRYAFYRFKYPHSDDKRSKFVFISWIPDGVSIKQKMVYATNKQTLKEALFGLA 88


                ....*.
gi 5031635  133 HELQAN 138
Cdd:cd00013  89 VPVQIR 94
PTZ00152 PTZ00152
cofilin/actin-depolymerizing factor 1-like protein; Provisional
 1-131 1.03e-14

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


Pssm-ID: 173441  Cd Length: 122  Bit Score: 66.51  E-value: 1.03e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031635     1 MASGVAVSDGVIKVFNDMKVRKSStpeevkkrkKAVLFCLsEDKKNIILEEGKeilvgdvGQTVDDpyatFVKMLPDKD- 79
Cdd:PTZ00152   1 MISGIRVNDNCVTEFNNMKIRKTC---------RWIIFVI-ENCEIIIHSKGA-------TTTLTE----LVGSIDKNDk 59

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 5031635    80 --CRYALYDATYETKeskkedlvFIFWAPESAPLKSKMIYASSKDAIKKKLTGI 131
Cdd:PTZ00152  60 iqCAYVVFDAVNKIH--------FFMYARESSNSRDRMTYASSKQALLKKIEGV 105
ADF_Twf-N_like cd11285
N-terminal ADF domain of twinfilin and related proteins; Actin depolymerization factor ...
 3-135 6.23e-11

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: 56.87  E-value: 6.23e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031635    3 SGVAVSDGVIKVFNDMKVRKSstpeevkkrkkavLFCLSEDKKNIILEEGKEIlvgDVGQTVDDPYATFV-KMLPDKDCR 81
Cdd:cd11285   2 SGITASEELLDAFKSAKSSGS-------------VRAIKITIENEELVPDATI---ETTGSWEQDFDLLVlPLLEEKEPC 65

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 5031635   82 YALYDATYETKESkkeDLVFIFWAPESAPLKSKMIYASSKDAIKKKLTG--IKHEL 135
Cdd:cd11285  66 YILYRLDSKSAGY---EWVFISFVPDSAPVRQKMLYASTRATLKRELGSnhIKDEL 118
ADF_GMF-beta_like cd11283
ADF-homology domain of glia maturation factor beta and related proteins; Actin ...
 7-128 1.21e-06

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: 45.31  E-value: 1.21e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031635    7 VSDGVIKVFNDMKVRKSSTPEE--VKKRKKAVLFCLSEDKKNIILEEGKEILvgdvgqtvddpyatfvkmlPDKDCRYAL 84
Cdd:cd11283   2 ISDEVKEALKKFRFRKSKANAAliLKIDKEKQEIVVDEELEDISIEELAEEL-------------------PEHSPRFVL 62

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 5031635   85 YDATYETKESKKE-DLVFIFWAPESAPLKSKMIYASSKDAIKKKL 128
Cdd:cd11283  63 YSYKMKHDDGRISyPLVLIYWSPQGCSPELQMLYAGAKELLVKEA 107
ADF_coactosin_like cd11282
Coactosin-like members of the ADF homology domain family; Actin depolymerization factor ...
 50-143 1.03e-03

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: 36.85  E-value: 1.03e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031635   50 EEGKEILVGDVGQTVDDpyaTFVKMLPDKDCRYALYDATYETKESKKEDLVFIFWAPESAPLKSKMIYASSKDAIKKKLT 129
Cdd:cd11282  24 ESSNTLVLRGSGSGGID---ELKAQLPDDEVLFGYVRITLGDGESKRSKFVFITWIGENVSVLRRAKVSVHKGDVKEVLS 100

                        90
                ....*....|....
gi 5031635  130 GIKHELQANCYEEV 143
Cdd:cd11282 101 PFHVELTASSKDEL 114
ADF_Twf-C_like cd11284
C-terminal ADF domain of twinfilin and related proteins; Actin depolymerization factor ...
 73-121 1.57e-03

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: 36.83  E-value: 1.57e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 5031635   73 KMLPDKDCRYALYdaTYetKESKKEDLVFIFWAPESAPLKSKMIYASSK 121
Cdd:cd11284  53 SLIPSDHPRYHFY--RY--PHTYLSSVVFIYSCPSGSKVKERMLYASSK 97
 
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.
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