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Conserved domains on  [gi|343887344|ref|NP_001230574|]
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cofilin-2 isoform 2 [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 ...
 10-136 5.87e-44

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: 141.16  E-value: 5.87e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887344  10 EEIKKRK--KAVLFCLSDDKRQIIVEEakqilVGDIGDTVEDpytsFVKLLPLNDCRYALYDATYETK-ESKKEDLVFIF 86
Cdd:cd11286   14 NELKLKKkhKYIIFKISDDKKEIVVEK-----VGERDASYDD----FLEKLPENECRYAVYDFEYETKdGGKRSKLVFIS 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 343887344  87 WAPESAPLKSKMIYASSKDAIKKKFTGIKHEWQVNGLDDIkDRSTLGEKL 136
Cdd:cd11286   85 WCPDTAPIKSKMLYASSKDALKKKLNGIKKEIQATDLSEL-SEEEILEKL 133
 
Name Accession Description Interval E-value
ADF_cofilin_like cd11286
Cofilin, Destrin, and related actin depolymerizing factors; Actin depolymerization factor ...
 10-136 5.87e-44

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: 141.16  E-value: 5.87e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887344  10 EEIKKRK--KAVLFCLSDDKRQIIVEEakqilVGDIGDTVEDpytsFVKLLPLNDCRYALYDATYETK-ESKKEDLVFIF 86
Cdd:cd11286   14 NELKLKKkhKYIIFKISDDKKEIVVEK-----VGERDASYDD----FLEKLPENECRYAVYDFEYETKdGGKRSKLVFIS 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 343887344  87 WAPESAPLKSKMIYASSKDAIKKKFTGIKHEWQVNGLDDIkDRSTLGEKL 136
Cdd:cd11286   85 WCPDTAPIKSKMLYASSKDALKKKLNGIKKEIQATDLSEL-SEEEILEKL 133
ADF smart00102
Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin ...
 2-137 2.31e-42

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


Pssm-ID: 214516  Cd Length: 127  Bit Score: 136.64  E-value: 2.31e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887344     2 KVRKSSTQEEIKKRK-KAVLFCLSDDKRQIIVEEAKQilvgdigdtVEDPYTSFVKLLPLNDCRYALYDATYETKESKKE 80
Cdd:smart00102   1 EDCKEAFNELKKKRKhSAIIFKIDKDNEEIVVEEVGS---------TEDSYDEFVEELPEDECRYALYDYKFTTEESKKS 71

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 343887344    81 DLVFIFWAPESAPLKSKMIYASSKDAIKKKFTGIKHEWQVNGLDDIkDRSTLGEKLG 137
Cdd:smart00102  72 KIVFIFWSPDGAPVKSKMLYASSKDTLKKELGGIQVEVQATDEDDL-DEEALKEKLK 127
Cofilin_ADF pfam00241
Cofilin/tropomyosin-type actin-binding protein; Severs actin filaments and binds to actin ...
 10-126 4.94e-31

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


Pssm-ID: 459727  Cd Length: 123  Bit Score: 107.66  E-value: 4.94e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887344   10 EEIKKRKK--AVLFCLSDDKRQIIVEEakqilVGDIGDTVEDpytsFVKLLPLNDCRYALYDATYETK-ESKKEDLVFIF 86
Cdd:pfam00241   6 QELRSDKKtnWIIFKIDDDKEEIVVEE-----TGEGGLSYDE----FLEELPDDEPRYAVYRFEYTHDdGSKRSKLVFIT 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 343887344   87 WAPESAPLKSKMIYASSKDAIKKKFTGIKHEWQVNGLDDI 126
Cdd:pfam00241  77 WCPDGAPIKRKMLYASSKAALKRELKGIHVEIQATDPSEL 116
PLN03216 PLN03216
actin depolymerizing factor; Provisional
 13-130 1.35e-17

actin depolymerizing factor; Provisional


Pssm-ID: 178755  Cd Length: 141  Bit Score: 74.19  E-value: 1.35e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887344  13 KKRKKAVLFCLSDDKRQIIVEEakqilVGDIGDTVEDPYTSfvklLPLNDCRYALYDATYETKES-KKEDLVFIFWAPES 91
Cdd:PLN03216  26 KKVHRYIVFKIDEKSRKVTVDK-----VGGPGESYDDLAAS----LPTDDCRYAVFDFDFVTVDNcRKSKIFFIAWSPEA 96

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 343887344  92 APLKSKMIYASSKDAIKKKFTGIKHEWQVN-----GLDDIKDRS 130
Cdd:PLN03216  97 SRIRAKMLYATSKDGLRRVLDGVHYELQATdptemGFDVIRDRA 140
 
Name Accession Description Interval E-value
ADF_cofilin_like cd11286
Cofilin, Destrin, and related actin depolymerizing factors; Actin depolymerization factor ...
 10-136 5.87e-44

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: 141.16  E-value: 5.87e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887344  10 EEIKKRK--KAVLFCLSDDKRQIIVEEakqilVGDIGDTVEDpytsFVKLLPLNDCRYALYDATYETK-ESKKEDLVFIF 86
Cdd:cd11286   14 NELKLKKkhKYIIFKISDDKKEIVVEK-----VGERDASYDD----FLEKLPENECRYAVYDFEYETKdGGKRSKLVFIS 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 343887344  87 WAPESAPLKSKMIYASSKDAIKKKFTGIKHEWQVNGLDDIkDRSTLGEKL 136
Cdd:cd11286   85 WCPDTAPIKSKMLYASSKDALKKKLNGIKKEIQATDLSEL-SEEEILEKL 133
ADF smart00102
Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin ...
 2-137 2.31e-42

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


Pssm-ID: 214516  Cd Length: 127  Bit Score: 136.64  E-value: 2.31e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887344     2 KVRKSSTQEEIKKRK-KAVLFCLSDDKRQIIVEEAKQilvgdigdtVEDPYTSFVKLLPLNDCRYALYDATYETKESKKE 80
Cdd:smart00102   1 EDCKEAFNELKKKRKhSAIIFKIDKDNEEIVVEEVGS---------TEDSYDEFVEELPEDECRYALYDYKFTTEESKKS 71

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 343887344    81 DLVFIFWAPESAPLKSKMIYASSKDAIKKKFTGIKHEWQVNGLDDIkDRSTLGEKLG 137
Cdd:smart00102  72 KIVFIFWSPDGAPVKSKMLYASSKDTLKKELGGIQVEVQATDEDDL-DEEALKEKLK 127
Cofilin_ADF pfam00241
Cofilin/tropomyosin-type actin-binding protein; Severs actin filaments and binds to actin ...
 10-126 4.94e-31

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


Pssm-ID: 459727  Cd Length: 123  Bit Score: 107.66  E-value: 4.94e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887344   10 EEIKKRKK--AVLFCLSDDKRQIIVEEakqilVGDIGDTVEDpytsFVKLLPLNDCRYALYDATYETK-ESKKEDLVFIF 86
Cdd:pfam00241   6 QELRSDKKtnWIIFKIDDDKEEIVVEE-----TGEGGLSYDE----FLEELPDDEPRYAVYRFEYTHDdGSKRSKLVFIT 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 343887344   87 WAPESAPLKSKMIYASSKDAIKKKFTGIKHEWQVNGLDDI 126
Cdd:pfam00241  77 WCPDGAPIKRKMLYASSKAALKRELKGIHVEIQATDPSEL 116
ADF_gelsolin cd00013
Actin depolymerization factor/cofilin- and gelsolin-like domains; Actin depolymerization ...
 17-124 5.01e-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: 74.04  E-value: 5.01e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887344  17 KAVLFCLSDDKRQIIVeeakqilvgdiGDTVEDPYTSFVKLLPLNDCRYALYDATYETKESKKEDLVFIFWAPESAPLKS 96
Cdd:cd00013    1 DWVLFKVDAKKEEIVV-----------GSTGAGFLDEFLEELPEDDPRYAFYRFKYPHSDDKRSKFVFISWIPDGVSIKQ 69

                         90       100
                 ....*....|....*....|....*...
gi 343887344  97 KMIYASSKDAIKKKFTGIKHEWQVNGLD 124
Cdd:cd00013   70 KMVYATNKQTLKEALFGLAVPVQIRDGD 97
PLN03216 PLN03216
actin depolymerizing factor; Provisional
 13-130 1.35e-17

actin depolymerizing factor; Provisional


Pssm-ID: 178755  Cd Length: 141  Bit Score: 74.19  E-value: 1.35e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887344  13 KKRKKAVLFCLSDDKRQIIVEEakqilVGDIGDTVEDPYTSfvklLPLNDCRYALYDATYETKES-KKEDLVFIFWAPES 91
Cdd:PLN03216  26 KKVHRYIVFKIDEKSRKVTVDK-----VGGPGESYDDLAAS----LPTDDCRYAVFDFDFVTVDNcRKSKIFFIAWSPEA 96

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 343887344  92 APLKSKMIYASSKDAIKKKFTGIKHEWQVN-----GLDDIKDRS 130
Cdd:PLN03216  97 SRIRAKMLYATSKDGLRRVLDGVHYELQATdptemGFDVIRDRA 140
PTZ00152 PTZ00152
cofilin/actin-depolymerizing factor 1-like protein; Provisional
 30-114 6.79e-10

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


Pssm-ID: 173441  Cd Length: 122  Bit Score: 53.42  E-value: 6.79e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887344  30 IIVEEAKQILVGDIGDTveDPYTSFVKLLPLND---CRYALYDATYETKeskkedlvFIFWAPESAPLKSKMIYASSKDA 106
Cdd:PTZ00152  28 IFVIENCEIIIHSKGAT--TTLTELVGSIDKNDkiqCAYVVFDAVNKIH--------FFMYARESSNSRDRMTYASSKQA 97


                 ....*...
gi 343887344 107 IKKKFTGI 114
Cdd:PTZ00152  98 LLKKIEGV 105
ADF_Twf-N_like cd11285
N-terminal ADF domain of twinfilin and related proteins; Actin depolymerization factor ...
 75-128 1.81e-09

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: 52.64  E-value: 1.81e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 343887344  75 KESKKEDLVFIFWAPESAPLKSKMIYASSKDAIKKKFTG--IKHEWQVNGLDDIKD 128
Cdd:cd11285   73 SKSAGYEWVFISFVPDSAPVRQKMLYASTRATLKRELGSnhIKDELFATELEELTL 128
ADF_GMF-beta_like cd11283
ADF-homology domain of glia maturation factor beta and related proteins; Actin ...
 6-111 1.11e-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: 42.22  E-value: 1.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887344   6 SSTQEEIKK---RKK----AVLFCLSDDKRQIIVEEakQILVGDIGDTVEDpytsfvklLPLNDCRYALYDATYETKESK 78
Cdd:cd11283    4 DEVKEALKKfrfRKSkanaALILKIDKEKQEIVVDE--ELEDISIEELAEE--------LPEHSPRFVLYSYKMKHDDGR 73

                         90       100       110
                 ....*....|....*....|....*....|....
gi 343887344  79 KE-DLVFIFWAPESAPLKSKMIYASSKDAIKKKF 111
Cdd:cd11283   74 ISyPLVLIYWSPQGCSPELQMLYAGAKELLVKEA 107
ADF_Twf-C_like cd11284
C-terminal ADF domain of twinfilin and related proteins; Actin depolymerization factor ...
 9-104 4.87e-04

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: 37.98  E-value: 4.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343887344   9 QEEIKKRKKAVLFCLSDDKRQIIVEEAKQILVGDigdtvedpytSFVKLLPLNDCRYALYdaTYetKESKKEDLVFIFWA 88
Cdd:cd11284   16 SELASGGVNLVQLSIDLENETIELVSSSSISIPD----------DLSSLIPSDHPRYHFY--RY--PHTYLSSVVFIYSC 81

                         90
                 ....*....|....*.
gi 343887344  89 PESAPLKSKMIYASSK 104
Cdd:cd11284   82 PSGSKVKERMLYASSK 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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