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Conserved domains on  [gi|1931045936|dbj|GHP01738|]
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actin-depolymerizing factor [Pycnococcus provasolii]

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 ...
 96-214 8.21e-35

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: 120.35  E-value: 8.21e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931045936  96 DLLKKKVYKWVMFRIDKHLiraQQVGMKKSG---ASYSDFVSMLPCDEARFGVVDVDLINSDGCKLSRIVFVHWAPDTAP 172
Cdd:cd11286    15 ELKLKKKHKYIIFKISDDK---KEIVVEKVGerdASYDDFLEKLPENECRYAVYDFEYETKDGGKRSKLVFISWCPDTAP 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1931045936 173 AMHKMKSASSAQHFKNLLQGVSVELQASDLDEMGEEGLMSRI 214
Cdd:cd11286    92 IKSKMLYASSKDALKKKLNGIKKEIQATDLSELSEEEILEKL 133
 
Name Accession Description Interval E-value
ADF_cofilin_like cd11286
Cofilin, Destrin, and related actin depolymerizing factors; Actin depolymerization factor ...
 96-214 8.21e-35

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: 120.35  E-value: 8.21e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931045936  96 DLLKKKVYKWVMFRIDKHLiraQQVGMKKSG---ASYSDFVSMLPCDEARFGVVDVDLINSDGCKLSRIVFVHWAPDTAP 172
Cdd:cd11286    15 ELKLKKKHKYIIFKISDDK---KEIVVEKVGerdASYDDFLEKLPENECRYAVYDFEYETKDGGKRSKLVFISWCPDTAP 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1931045936 173 AMHKMKSASSAQHFKNLLQGVSVELQASDLDEMGEEGLMSRI 214
Cdd:cd11286    92 IKSKMLYASSKDALKKKLNGIKKEIQATDLSELSEEEILEKL 133
Cofilin_ADF pfam00241
Cofilin/tropomyosin-type actin-binding protein; Severs actin filaments and binds to actin ...
 95-212 1.04e-33

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


Pssm-ID: 459727  Cd Length: 123  Bit Score: 117.29  E-value: 1.04e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931045936  95 KDLLKKKVYKWVMFRIDKHL--IRAQQVGmkKSGASYSDFVSMLPCDEARFGVVDVDLINSDGCKLSRIVFVHWAPDTAP 172
Cdd:pfam00241   6 QELRSDKKTNWIIFKIDDDKeeIVVEETG--EGGLSYDEFLEELPDDEPRYAVYRFEYTHDDGSKRSKLVFITWCPDGAP 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1931045936 173 AMHKMKSASSAQHFKNLLQGVSVELQASDLDEMGEEGLMS 212
Cdd:pfam00241  84 IKRKMLYASSKAALKRELKGIHVEIQATDPSELTEEEILE 123
ADF smart00102
Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin ...
 96-215 3.76e-27

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


Pssm-ID: 214516  Cd Length: 127  Bit Score: 100.44  E-value: 3.76e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931045936   96 DLLKKKVYKWVMFRIDKHlirAQQVGMKKSG---ASYSDFVSMLPCDEARFGVVDVDLiNSDGCKLSRIVFVHWAPDTAP 172
Cdd:smart00102   9 ELKKKRKHSAIIFKIDKD---NEEIVVEEVGsteDSYDEFVEELPEDECRYALYDYKF-TTEESKKSKIVFIFWSPDGAP 84

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1931045936  173 AMHKMKSASSAQHFKNLLQGVSVELQASDLDEMGEEGLMSRIR 215
Cdd:smart00102  85 VKSKMLYASSKDTLKKELGGIQVEVQATDEDDLDEEALKEKLK 127
PLN03216 PLN03216
actin depolymerizing factor; Provisional
 100-216 3.63e-22

actin depolymerizing factor; Provisional


Pssm-ID: 178755  Cd Length: 141  Bit Score: 88.06  E-value: 3.63e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931045936 100 KKVYKWVMFRIDKhliRAQQVGMKKSGA---SYSDFVSMLPCDEARFGVVDVDLINSDGCKLSRIVFVHWAPDTAPAMHK 176
Cdd:PLN03216   26 KKVHRYIVFKIDE---KSRKVTVDKVGGpgeSYDDLAASLPTDDCRYAVFDFDFVTVDNCRKSKIFFIAWSPEASRIRAK 102

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1931045936 177 MKSASSAQHFKNLLQGVSVELQASDLDEMGeeglMSRIRD 216
Cdd:PLN03216  103 MLYATSKDGLRRVLDGVHYELQATDPTEMG----FDVIRD 138
 
Name Accession Description Interval E-value
ADF_cofilin_like cd11286
Cofilin, Destrin, and related actin depolymerizing factors; Actin depolymerization factor ...
 96-214 8.21e-35

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: 120.35  E-value: 8.21e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931045936  96 DLLKKKVYKWVMFRIDKHLiraQQVGMKKSG---ASYSDFVSMLPCDEARFGVVDVDLINSDGCKLSRIVFVHWAPDTAP 172
Cdd:cd11286    15 ELKLKKKHKYIIFKISDDK---KEIVVEKVGerdASYDDFLEKLPENECRYAVYDFEYETKDGGKRSKLVFISWCPDTAP 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1931045936 173 AMHKMKSASSAQHFKNLLQGVSVELQASDLDEMGEEGLMSRI 214
Cdd:cd11286    92 IKSKMLYASSKDALKKKLNGIKKEIQATDLSELSEEEILEKL 133
Cofilin_ADF pfam00241
Cofilin/tropomyosin-type actin-binding protein; Severs actin filaments and binds to actin ...
 95-212 1.04e-33

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


Pssm-ID: 459727  Cd Length: 123  Bit Score: 117.29  E-value: 1.04e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931045936  95 KDLLKKKVYKWVMFRIDKHL--IRAQQVGmkKSGASYSDFVSMLPCDEARFGVVDVDLINSDGCKLSRIVFVHWAPDTAP 172
Cdd:pfam00241   6 QELRSDKKTNWIIFKIDDDKeeIVVEETG--EGGLSYDEFLEELPDDEPRYAVYRFEYTHDDGSKRSKLVFITWCPDGAP 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1931045936 173 AMHKMKSASSAQHFKNLLQGVSVELQASDLDEMGEEGLMS 212
Cdd:pfam00241  84 IKRKMLYASSKAALKRELKGIHVEIQATDPSELTEEEILE 123
ADF smart00102
Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin ...
 96-215 3.76e-27

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


Pssm-ID: 214516  Cd Length: 127  Bit Score: 100.44  E-value: 3.76e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931045936   96 DLLKKKVYKWVMFRIDKHlirAQQVGMKKSG---ASYSDFVSMLPCDEARFGVVDVDLiNSDGCKLSRIVFVHWAPDTAP 172
Cdd:smart00102   9 ELKKKRKHSAIIFKIDKD---NEEIVVEEVGsteDSYDEFVEELPEDECRYALYDYKF-TTEESKKSKIVFIFWSPDGAP 84

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1931045936  173 AMHKMKSASSAQHFKNLLQGVSVELQASDLDEMGEEGLMSRIR 215
Cdd:smart00102  85 VKSKMLYASSKDTLKKELGGIQVEVQATDEDDLDEEALKEKLK 127
PLN03216 PLN03216
actin depolymerizing factor; Provisional
 100-216 3.63e-22

actin depolymerizing factor; Provisional


Pssm-ID: 178755  Cd Length: 141  Bit Score: 88.06  E-value: 3.63e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931045936 100 KKVYKWVMFRIDKhliRAQQVGMKKSGA---SYSDFVSMLPCDEARFGVVDVDLINSDGCKLSRIVFVHWAPDTAPAMHK 176
Cdd:PLN03216   26 KKVHRYIVFKIDE---KSRKVTVDKVGGpgeSYDDLAASLPTDDCRYAVFDFDFVTVDNCRKSKIFFIAWSPEASRIRAK 102

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1931045936 177 MKSASSAQHFKNLLQGVSVELQASDLDEMGeeglMSRIRD 216
Cdd:PLN03216  103 MLYATSKDGLRRVLDGVHYELQATDPTEMG----FDVIRD 138
ADF_gelsolin cd00013
Actin depolymerization factor/cofilin- and gelsolin-like domains; Actin depolymerization ...
 104-203 4.14e-14

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: 65.56  E-value: 4.14e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931045936 104 KWVMFRIDKhliRAQQVGMKKSGASYSD-FVSMLPCDEARFGVVDVDLINSDGcKLSRIVFVHWAPDTAPAMHKMKSASS 182
Cdd:cd00013     1 DWVLFKVDA---KKEEIVVGSTGAGFLDeFLEELPEDDPRYAFYRFKYPHSDD-KRSKFVFISWIPDGVSIKQKMVYATN 76

                          90       100
                  ....*....|....*....|.
gi 1931045936 183 AQHFKNLLQGVSVELQASDLD 203
Cdd:cd00013    77 KQTLKEALFGLAVPVQIRDGD 97
ADF_drebrin_like cd11281
ADF homology domain of drebrin and actin-binding protein 1 (abp1); Actin depolymerization ...
 100-217 1.23e-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: 54.57  E-value: 1.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931045936 100 KKVYKWVMFRIDK--HLIRAQQVGmkksGASYSDFVSMLPCDEARFGVVDVDLINSDgckLSRIVFVHWAPDTAPAMHKM 177
Cdd:cd11281    21 KSSTDWALFTYEGksNDLKVADTG----DGGLEELVEEFSDGKVQYGFARVKDPNSG---LPKFVLINWCGEGVPDARKG 93

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1931045936 178 KSASSAQHFKNLLQGVSVELQASDLDEMGEEGLMSRIRDS 217
Cdd:cd11281    94 SFASHVAAVANFLKGAHVQINARSEDDLDEDAILKKVSKA 133
ADF_coactosin_like cd11282
Coactosin-like members of the ADF homology domain family; Actin depolymerization factor ...
 105-205 1.60e-07

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: 48.40  E-value: 1.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931045936 105 WVMFRIDKHLiraqQVGMKKSGASYSD-FVSMLPCDEARFGVVDVDLINsDGCKLSRIVFVHWAPDTAPAMHKMKSASSA 183
Cdd:cd11282    18 WVLLGYESSN----TLVLRGSGSGGIDeLKAQLPDDEVLFGYVRITLGD-GESKRSKFVFITWIGENVSVLRRAKVSVHK 92

                          90       100
                  ....*....|....*....|..
gi 1931045936 184 QHFKNLLQGVSVELQASDLDEM 205
Cdd:cd11282    93 GDVKEVLSPFHVELTASSKDEL 114
PTZ00152 PTZ00152
cofilin/actin-depolymerizing factor 1-like protein; Provisional
 81-207 4.09e-07

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


Pssm-ID: 173441  Cd Length: 122  Bit Score: 47.25  E-value: 4.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931045936  81 VAGIGTSQLSLQMHKDLLKKKVYKWVMFRIDKHLIRAQQVGmkkSGASYSDFVSMLPCD---EARFGVVDVdlinsdgck 157
Cdd:PTZ00152    2 ISGIRVNDNCVTEFNNMKIRKTCRWIIFVIENCEIIIHSKG---ATTTLTELVGSIDKNdkiQCAYVVFDA--------- 69

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1931045936 158 LSRIVFVHWAPDTAPAMHKMKSASSAQHFKNLLQGVSVelQASDLDEMGE 207
Cdd:PTZ00152   70 VNKIHFFMYARESSNSRDRMTYASSKQALLKKIEGVNV--LTSVIESAQD 117
ADF_Twf-C_like cd11284
C-terminal ADF domain of twinfilin and related proteins; Actin depolymerization factor ...
 98-212 9.77e-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: 35.28  E-value: 9.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931045936  98 LKKKVYKWVMFRIDkhlIRAQQVGM--KKSGASYSDFVSMLPCDEARFGvvdvdLINSDGCKLSRIVFVHWAPDTAPAMH 175
Cdd:cd11284    18 LASGGVNLVQLSID---LENETIELvsSSSISIPDDLSSLIPSDHPRYH-----FYRYPHTYLSSVVFIYSCPSGSKVKE 89

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1931045936 176 KMKSASSAQHFKNLLQ---GVSVE--LQASDLDEMGEEGLMS 212
Cdd:cd11284    90 RMLYASSKSGLLNHAEdegKIEIDkkIEIGDPDELTESFLSD 131
 
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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