NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|32566130|ref|NP_503427|]
View 

Actin-depolymerizing factor 2, isoform c [Caenorhabditis elegans]

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 ...
 3-146 6.04e-46

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: 146.16  E-value: 6.04e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566130   3 SGVKVDPSCKNAYDLLHNKHQHSYIIFKIDKNDTAIVVEKVGEKNAPYAEFVEEMKKlvedgKECRYAAVDVEVTVQrqg 82
Cdd:cd11286   1 SGVKVSDECITAFNELKLKKKHKYIIFKISDDKKEIVVEKVGERDASYDDFLEKLPE-----NECRYAVYDFEYETK--- 72

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32566130  83 aeGTSTLNKVIFVQYCPDNAPVRRRMLYASSVRALKASL-GLEslFQVQASEMSDLDEKSVKSDL 146
Cdd:cd11286  73 --DGGKRSKLVFISWCPDTAPIKSKMLYASSKDALKKKLnGIK--KEIQATDLSELSEEEILEKL 133
 
Name Accession Description Interval E-value
ADF_cofilin_like cd11286
Cofilin, Destrin, and related actin depolymerizing factors; Actin depolymerization factor ...
 3-146 6.04e-46

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: 146.16  E-value: 6.04e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566130   3 SGVKVDPSCKNAYDLLHNKHQHSYIIFKIDKNDTAIVVEKVGEKNAPYAEFVEEMKKlvedgKECRYAAVDVEVTVQrqg 82
Cdd:cd11286   1 SGVKVSDECITAFNELKLKKKHKYIIFKISDDKKEIVVEKVGERDASYDDFLEKLPE-----NECRYAVYDFEYETK--- 72

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32566130  83 aeGTSTLNKVIFVQYCPDNAPVRRRMLYASSVRALKASL-GLEslFQVQASEMSDLDEKSVKSDL 146
Cdd:cd11286  73 --DGGKRSKLVFISWCPDTAPIKSKMLYASSKDALKKKLnGIK--KEIQATDLSELSEEEILEKL 133
ADF smart00102
Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin ...
 9-147 6.12e-40

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


Pssm-ID: 214516  Cd Length: 127  Bit Score: 130.87  E-value: 6.12e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566130      9 PSCKNAYDLLHNKHQHSYIIFKIDKNDTAIVVEKVGEKNAPYAEFVEEMKKlvedgKECRYAAVDVEVTVQrqgaegTST 88
Cdd:smart00102   1 EDCKEAFNELKKKRKHSAIIFKIDKDNEEIVVEEVGSTEDSYDEFVEELPE-----DECRYALYDYKFTTE------ESK 69

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 32566130     89 LNKVIFVQYCPDNAPVRRRMLYASSVRALKASLGLeSLFQVQASEMSDLDEKSVKSDLM 147
Cdd:smart00102  70 KSKIVFIFWSPDGAPVKSKMLYASSKDTLKKELGG-IQVEVQATDEDDLDEEALKEKLK 127
Cofilin_ADF pfam00241
Cofilin/tropomyosin-type actin-binding protein; Severs actin filaments and binds to actin ...
 11-144 1.28e-35

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


Pssm-ID: 459727  Cd Length: 123  Bit Score: 119.60  E-value: 1.28e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566130    11 CKNAYDLLHNKHQHSYIIFKIDKNDTAIVVEKVGEKNAPYAEFVEEMKKlvedgKECRYAAVDVEVTVqrqgaEGTSTLN 90
Cdd:pfam00241   1 CKEAYQELRSDKKTNWIIFKIDDDKEEIVVEETGEGGLSYDEFLEELPD-----DEPRYAVYRFEYTH-----DDGSKRS 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 32566130    91 KVIFVQYCPDNAPVRRRMLYASSVRALKASL-GLESlfQVQASEMSDLDEKSVKS 144
Cdd:pfam00241  71 KLVFITWCPDGAPIKRKMLYASSKAALKRELkGIHV--EIQATDPSELTEEEILE 123
PTZ00152 PTZ00152
cofilin/actin-depolymerizing factor 1-like protein; Provisional
 1-137 5.75e-16

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


Pssm-ID: 173441  Cd Length: 122  Bit Score: 69.21  E-value: 5.75e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566130    1 MASGVKVDPSCKNAYDLLHNKHQHSYIIFKIDknDTAIVVEKVGEKNApYAEFVEEMKKlvEDGKECRYAAVDvevtvqr 80
Cdd:PTZ00152   1 MISGIRVNDNCVTEFNNMKIRKTCRWIIFVIE--NCEIIIHSKGATTT-LTELVGSIDK--NDKIQCAYVVFD------- 68

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 32566130   81 qgaegtsTLNKVIFVQYCPDNAPVRRRMLYASSVRALKASLGLESLFQVQASEMSDL 137
Cdd:PTZ00152  69 -------AVNKIHFFMYARESSNSRDRMTYASSKQALLKKIEGVNVLTSVIESAQDV 118
 
Name Accession Description Interval E-value
ADF_cofilin_like cd11286
Cofilin, Destrin, and related actin depolymerizing factors; Actin depolymerization factor ...
 3-146 6.04e-46

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: 146.16  E-value: 6.04e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566130   3 SGVKVDPSCKNAYDLLHNKHQHSYIIFKIDKNDTAIVVEKVGEKNAPYAEFVEEMKKlvedgKECRYAAVDVEVTVQrqg 82
Cdd:cd11286   1 SGVKVSDECITAFNELKLKKKHKYIIFKISDDKKEIVVEKVGERDASYDDFLEKLPE-----NECRYAVYDFEYETK--- 72

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32566130  83 aeGTSTLNKVIFVQYCPDNAPVRRRMLYASSVRALKASL-GLEslFQVQASEMSDLDEKSVKSDL 146
Cdd:cd11286  73 --DGGKRSKLVFISWCPDTAPIKSKMLYASSKDALKKKLnGIK--KEIQATDLSELSEEEILEKL 133
ADF smart00102
Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin ...
 9-147 6.12e-40

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


Pssm-ID: 214516  Cd Length: 127  Bit Score: 130.87  E-value: 6.12e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566130      9 PSCKNAYDLLHNKHQHSYIIFKIDKNDTAIVVEKVGEKNAPYAEFVEEMKKlvedgKECRYAAVDVEVTVQrqgaegTST 88
Cdd:smart00102   1 EDCKEAFNELKKKRKHSAIIFKIDKDNEEIVVEEVGSTEDSYDEFVEELPE-----DECRYALYDYKFTTE------ESK 69

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 32566130     89 LNKVIFVQYCPDNAPVRRRMLYASSVRALKASLGLeSLFQVQASEMSDLDEKSVKSDLM 147
Cdd:smart00102  70 KSKIVFIFWSPDGAPVKSKMLYASSKDTLKKELGG-IQVEVQATDEDDLDEEALKEKLK 127
Cofilin_ADF pfam00241
Cofilin/tropomyosin-type actin-binding protein; Severs actin filaments and binds to actin ...
 11-144 1.28e-35

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


Pssm-ID: 459727  Cd Length: 123  Bit Score: 119.60  E-value: 1.28e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566130    11 CKNAYDLLHNKHQHSYIIFKIDKNDTAIVVEKVGEKNAPYAEFVEEMKKlvedgKECRYAAVDVEVTVqrqgaEGTSTLN 90
Cdd:pfam00241   1 CKEAYQELRSDKKTNWIIFKIDDDKEEIVVEETGEGGLSYDEFLEELPD-----DEPRYAVYRFEYTH-----DDGSKRS 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 32566130    91 KVIFVQYCPDNAPVRRRMLYASSVRALKASL-GLESlfQVQASEMSDLDEKSVKS 144
Cdd:pfam00241  71 KLVFITWCPDGAPIKRKMLYASSKAALKRELkGIHV--EIQATDPSELTEEEILE 123
PTZ00152 PTZ00152
cofilin/actin-depolymerizing factor 1-like protein; Provisional
 1-137 5.75e-16

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


Pssm-ID: 173441  Cd Length: 122  Bit Score: 69.21  E-value: 5.75e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566130    1 MASGVKVDPSCKNAYDLLHNKHQHSYIIFKIDknDTAIVVEKVGEKNApYAEFVEEMKKlvEDGKECRYAAVDvevtvqr 80
Cdd:PTZ00152   1 MISGIRVNDNCVTEFNNMKIRKTCRWIIFVIE--NCEIIIHSKGATTT-LTELVGSIDK--NDKIQCAYVVFD------- 68

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 32566130   81 qgaegtsTLNKVIFVQYCPDNAPVRRRMLYASSVRALKASLGLESLFQVQASEMSDL 137
Cdd:PTZ00152  69 -------AVNKIHFFMYARESSNSRDRMTYASSKQALLKKIEGVNVLTSVIESAQDV 118
PLN03216 PLN03216
actin depolymerizing factor; Provisional
 3-137 1.98e-14

actin depolymerizing factor; Provisional


Pssm-ID: 178755  Cd Length: 141  Bit Score: 65.72  E-value: 1.98e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566130    3 SGVKVDPSCKNAYDLLHNKHQHSYIIFKIDKNDTAIVVEKVGEKNAPYAEFVEEmkkLVEDgkECRYAAVDVE-VTVQrq 81
Cdd:PLN03216   8 TGMWVTDECKNSFMEMKWKKVHRYIVFKIDEKSRKVTVDKVGGPGESYDDLAAS---LPTD--DCRYAVFDFDfVTVD-- 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 32566130   82 gaegTSTLNKVIFVQYCPDNAPVRRRMLYASSVRALKASL-GLEslFQVQASEMSDL 137
Cdd:PLN03216  81 ----NCRKSKIFFIAWSPEASRIRAKMLYATSKDGLRRVLdGVH--YELQATDPTEM 131
ADF_gelsolin cd00013
Actin depolymerization factor/cofilin- and gelsolin-like domains; Actin depolymerization ...
 25-133 7.47e-13

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: 60.56  E-value: 7.47e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566130  25 SYIIFKIDKNDTAIVVEkvGEKNAPYAEFVEEMKKlvedgKECRYAAVDVEVTVQRQGaegtstLNKVIFVQYCPDNAPV 104
Cdd:cd00013   1 DWVLFKVDAKKEEIVVG--STGAGFLDEFLEELPE-----DDPRYAFYRFKYPHSDDK------RSKFVFISWIPDGVSI 67

                        90       100
                ....*....|....*....|....*....
gi 32566130 105 RRRMLYASSVRALKASLGlESLFQVQASE 133
Cdd:cd00013  68 KQKMVYATNKQTLKEALF-GLAVPVQIRD 95
ADF_Twf-N_like cd11285
N-terminal ADF domain of twinfilin and related proteins; Actin depolymerization factor ...
 3-145 2.77e-12

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: 59.95  E-value: 2.77e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566130   3 SGVKVDPSCKNAY-DLLHNKhqhSYIIFKIDKNDTAIVVEKVGEKNAPYAEFVEEMKKLVEDGKECRYAAVDVEVTvqrq 81
Cdd:cd11285   2 SGITASEELLDAFkSAKSSG---SVRAIKITIENEELVPDATIETTGSWEQDFDLLVLPLLEEKEPCYILYRLDSK---- 74

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32566130  82 gaegtSTLNKVIFVQYCPDNAPVRRRMLYASSVRALKASLGLESLF-QVQASEMSDLD----EKSVKSD 145
Cdd:cd11285  75 -----SAGYEWVFISFVPDSAPVRQKMLYASTRATLKRELGSNHIKdELFATELEELTlegyEKHLKHE 138
ADF_Twf-C_like cd11284
C-terminal ADF domain of twinfilin and related proteins; Actin depolymerization factor ...
 4-144 1.54e-09

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: 52.62  E-value: 1.54e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566130   4 GVKVDPSCKNAYDLLHNKHqHSYIIFKID-KNDTaIVVEKVGEKNAPyaefvEEMKKLVEDgKECRYaavdvevTVQRQG 82
Cdd:cd11284   4 AFPVSEEAKDALSELASGG-VNLVQLSIDlENET-IELVSSSSISIP-----DDLSSLIPS-DHPRY-------HFYRYP 68

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32566130  83 aegTSTLNKVIFVQYCPDNAPVRRRMLYASSVRAL----KASLGLESLFQVQASEMSDLDEKSVKS 144
Cdd:cd11284  69 ---HTYLSSVVFIYSCPSGSKVKERMLYASSKSGLlnhaEDEGKIEIDKKIEIGDPDELTESFLSD 131
ADF_drebrin_like cd11281
ADF homology domain of drebrin and actin-binding protein 1 (abp1); Actin depolymerization ...
 8-142 4.78e-09

ADF homology domain of drebrin and actin-binding protein 1 (abp1); 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. Abp1 and drebrin (developmentally regulated brain protein) are multidomain proteins with an N-terminal ADF homology domain and one or more C-terminal SH3 domains. They have been shown to interact with polymeric F-actin, but not with monomeric G-actin, and do not appear to promote the disassembly of actin filaments. Drebrin rather stabilizes actin filaments by inducing changes in the helical twist and may promote or interfere with the interactions of other proteins with actin filaments.


Pssm-ID: 200437  Cd Length: 136  Bit Score: 51.48  E-value: 4.78e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566130   8 DPSCKNAY-DLLHNKHQHSYIIFKIDKNDTAIVVEKVGEKNapYAEFVEEMkklvEDGKeCRYAAVDVEVTvqrqgaegT 86
Cdd:cd11281   7 SPEILAAYeDVVDGKSSTDWALFTYEGKSNDLKVADTGDGG--LEELVEEF----SDGK-VQYGFARVKDP--------N 71

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32566130  87 STLNKVIFVQYCPDNAPVRRRMLYASSVRALKaslgleSLF-----QVQASEMSDLDEKSV 142
Cdd:cd11281  72 SGLPKFVLINWCGEGVPDARKGSFASHVAAVA------NFLkgahvQINARSEDDLDEDAI 126
 
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