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Conserved domains on  [gi|1039021966|gb|ANM70922|]
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actin depolymerizing factor 4 [Arabidopsis thaliana]

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 ...
 1-131 2.29e-63

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: 189.30  E-value: 2.29e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039021966   1 MAVHDDCKLRFLELKAKRTHRFIVYKIEEKQKQVIVEKVGEPILTYEDFAASLPADECRYAIYDFDFVTAENCQKSKIFF 80
Cdd:cd11286     3 VKVSDECITAFNELKLKKKHKYIIFKISDDKKEIVVEKVGERDASYDDFLEKLPENECRYAVYDFEYETKDGGKRSKLVF 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1039021966  81 IAWCPDVAKVRSKMIYASSKDRFKRELDGIQVELQATDPTEMDLDVLKSRV 131
Cdd:cd11286    83 ISWCPDTAPIKSKMLYASSKDALKKKLNGIKKEIQATDLSELSEEEILEKL 133
 
Name Accession Description Interval E-value
ADF_cofilin_like cd11286
Cofilin, Destrin, and related actin depolymerizing factors; Actin depolymerization factor ...
 1-131 2.29e-63

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: 189.30  E-value: 2.29e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039021966   1 MAVHDDCKLRFLELKAKRTHRFIVYKIEEKQKQVIVEKVGEPILTYEDFAASLPADECRYAIYDFDFVTAENCQKSKIFF 80
Cdd:cd11286     3 VKVSDECITAFNELKLKKKHKYIIFKISDDKKEIVVEKVGERDASYDDFLEKLPENECRYAVYDFEYETKDGGKRSKLVF 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1039021966  81 IAWCPDVAKVRSKMIYASSKDRFKRELDGIQVELQATDPTEMDLDVLKSRV 131
Cdd:cd11286    83 ISWCPDTAPIKSKMLYASSKDALKKKLNGIKKEIQATDLSELSEEEILEKL 133
PLN03216 PLN03216
actin depolymerizing factor; Provisional
 1-130 3.11e-62

actin depolymerizing factor; Provisional


Pssm-ID: 178755  Cd Length: 141  Bit Score: 187.06  E-value: 3.11e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039021966   1 MAVHDDCKLRFLELKAKRTHRFIVYKIEEKQKQVIVEKVGEPILTYEDFAASLPADECRYAIYDFDFVTAENCQKSKIFF 80
Cdd:PLN03216   10 MWVTDECKNSFMEMKWKKVHRYIVFKIDEKSRKVTVDKVGGPGESYDDLAASLPTDDCRYAVFDFDFVTVDNCRKSKIFF 89

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039021966  81 IAWCPDVAKVRSKMIYASSKDRFKRELDGIQVELQATDPTEMDLDVLKSR 130
Cdd:PLN03216   90 IAWSPEASRIRAKMLYATSKDGLRRVLDGVHYELQATDPTEMGFDVIRDR 139
ADF smart00102
Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin ...
 5-132 8.66e-56

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


Pssm-ID: 214516  Cd Length: 127  Bit Score: 170.16  E-value: 8.66e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039021966    5 DDCKLRFLELKAKRTHRFIVYKIEEKQKQVIVEKVGEPILTYEDFAASLPADECRYAIYDFDFVTaENCQKSKIFFIAWC 84
Cdd:smart00102   1 EDCKEAFNELKKKRKHSAIIFKIDKDNEEIVVEEVGSTEDSYDEFVEELPEDECRYALYDYKFTT-EESKKSKIVFIFWS 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1039021966   85 PDVAKVRSKMIYASSKDRFKRELDGIQVELQATDPTEMDLDVLKSRVN 132
Cdd:smart00102  80 PDGAPVKSKMLYASSKDTLKKELGGIQVEVQATDEDDLDEEALKEKLK 127
Cofilin_ADF pfam00241
Cofilin/tropomyosin-type actin-binding protein; Severs actin filaments and binds to actin ...
 7-129 1.78e-48

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


Pssm-ID: 459727  Cd Length: 123  Bit Score: 151.57  E-value: 1.78e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039021966   7 CKLRFLELKAKRTHRFIVYKIEEKQKQVIVEKVGEPILTYEDFAASLPADECRYAIYDFDFVTAENCQKSKIFFIAWCPD 86
Cdd:pfam00241   1 CKEAYQELRSDKKTNWIIFKIDDDKEEIVVEETGEGGLSYDEFLEELPDDEPRYAVYRFEYTHDDGSKRSKLVFITWCPD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1039021966  87 VAKVRSKMIYASSKDRFKRELDGIQVELQATDPTEMDLDVLKS 129
Cdd:pfam00241  81 GAPIKRKMLYASSKAALKRELKGIHVEIQATDPSELTEEEILE 123
 
Name Accession Description Interval E-value
ADF_cofilin_like cd11286
Cofilin, Destrin, and related actin depolymerizing factors; Actin depolymerization factor ...
 1-131 2.29e-63

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: 189.30  E-value: 2.29e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039021966   1 MAVHDDCKLRFLELKAKRTHRFIVYKIEEKQKQVIVEKVGEPILTYEDFAASLPADECRYAIYDFDFVTAENCQKSKIFF 80
Cdd:cd11286     3 VKVSDECITAFNELKLKKKHKYIIFKISDDKKEIVVEKVGERDASYDDFLEKLPENECRYAVYDFEYETKDGGKRSKLVF 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1039021966  81 IAWCPDVAKVRSKMIYASSKDRFKRELDGIQVELQATDPTEMDLDVLKSRV 131
Cdd:cd11286    83 ISWCPDTAPIKSKMLYASSKDALKKKLNGIKKEIQATDLSELSEEEILEKL 133
PLN03216 PLN03216
actin depolymerizing factor; Provisional
 1-130 3.11e-62

actin depolymerizing factor; Provisional


Pssm-ID: 178755  Cd Length: 141  Bit Score: 187.06  E-value: 3.11e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039021966   1 MAVHDDCKLRFLELKAKRTHRFIVYKIEEKQKQVIVEKVGEPILTYEDFAASLPADECRYAIYDFDFVTAENCQKSKIFF 80
Cdd:PLN03216   10 MWVTDECKNSFMEMKWKKVHRYIVFKIDEKSRKVTVDKVGGPGESYDDLAASLPTDDCRYAVFDFDFVTVDNCRKSKIFF 89

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039021966  81 IAWCPDVAKVRSKMIYASSKDRFKRELDGIQVELQATDPTEMDLDVLKSR 130
Cdd:PLN03216   90 IAWSPEASRIRAKMLYATSKDGLRRVLDGVHYELQATDPTEMGFDVIRDR 139
ADF smart00102
Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin ...
 5-132 8.66e-56

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


Pssm-ID: 214516  Cd Length: 127  Bit Score: 170.16  E-value: 8.66e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039021966    5 DDCKLRFLELKAKRTHRFIVYKIEEKQKQVIVEKVGEPILTYEDFAASLPADECRYAIYDFDFVTaENCQKSKIFFIAWC 84
Cdd:smart00102   1 EDCKEAFNELKKKRKHSAIIFKIDKDNEEIVVEEVGSTEDSYDEFVEELPEDECRYALYDYKFTT-EESKKSKIVFIFWS 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1039021966   85 PDVAKVRSKMIYASSKDRFKRELDGIQVELQATDPTEMDLDVLKSRVN 132
Cdd:smart00102  80 PDGAPVKSKMLYASSKDTLKKELGGIQVEVQATDEDDLDEEALKEKLK 127
Cofilin_ADF pfam00241
Cofilin/tropomyosin-type actin-binding protein; Severs actin filaments and binds to actin ...
 7-129 1.78e-48

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


Pssm-ID: 459727  Cd Length: 123  Bit Score: 151.57  E-value: 1.78e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039021966   7 CKLRFLELKAKRTHRFIVYKIEEKQKQVIVEKVGEPILTYEDFAASLPADECRYAIYDFDFVTAENCQKSKIFFIAWCPD 86
Cdd:pfam00241   1 CKEAYQELRSDKKTNWIIFKIDDDKEEIVVEETGEGGLSYDEFLEELPDDEPRYAVYRFEYTHDDGSKRSKLVFITWCPD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1039021966  87 VAKVRSKMIYASSKDRFKRELDGIQVELQATDPTEMDLDVLKS 129
Cdd:pfam00241  81 GAPIKRKMLYASSKAALKRELKGIHVEIQATDPSELTEEEILE 123
ADF_gelsolin cd00013
Actin depolymerization factor/cofilin- and gelsolin-like domains; Actin depolymerization ...
 21-118 3.02e-20

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: 79.05  E-value: 3.02e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039021966  21 RFIVYKIEEKQKQVIVEKVGEPILtyEDFAASLPADECRYAIYDFDFVTAENcQKSKIFFIAWCPDVAKVRSKMIYASSK 100
Cdd:cd00013     1 DWVLFKVDAKKEEIVVGSTGAGFL--DEFLEELPEDDPRYAFYRFKYPHSDD-KRSKFVFISWIPDGVSIKQKMVYATNK 77

                          90
                  ....*....|....*...
gi 1039021966 101 DRFKRELDGIQVELQATD 118
Cdd:cd00013    78 QTLKEALFGLAVPVQIRD 95
PTZ00152 PTZ00152
cofilin/actin-depolymerizing factor 1-like protein; Provisional
 1-112 1.33e-17

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


Pssm-ID: 173441  Cd Length: 122  Bit Score: 73.06  E-value: 1.33e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039021966   1 MAVHDDCKLRFLELKAKRTHRFIVYKIEekQKQVIVEKVGEPIlTYEDFAASLPAD---ECRYAIYDfdfvtaencQKSK 77
Cdd:PTZ00152    5 IRVNDNCVTEFNNMKIRKTCRWIIFVIE--NCEIIIHSKGATT-TLTELVGSIDKNdkiQCAYVVFD---------AVNK 72

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1039021966  78 IFFIAWCPDVAKVRSKMIYASSKDRFKRELDGIQV 112
Cdd:PTZ00152   73 IHFFMYARESSNSRDRMTYASSKQALLKKIEGVNV 107
ADF_Twf-N_like cd11285
N-terminal ADF domain of twinfilin and related proteins; Actin depolymerization factor ...
 3-125 4.02e-13

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: 61.88  E-value: 4.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039021966   3 VHDDCKLRFLELKAKRTHRFIVYKIEEKQKQVivekvGEPILTYEDFAA--------SLPADECRYAIYDFDfvtaENCQ 74
Cdd:cd11285     6 ASEELLDAFKSAKSSGSVRAIKITIENEELVP-----DATIETTGSWEQdfdllvlpLLEEKEPCYILYRLD----SKSA 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039021966  75 KSKIFFIAWCPDVAKVRSKMIYASSKDRFKRELDG--IQVELQATDPTEMDLD 125
Cdd:cd11285    77 GYEWVFISFVPDSAPVRQKMLYASTRATLKRELGSnhIKDELFATELEELTLE 129
ADF_Twf-C_like cd11284
C-terminal ADF domain of twinfilin and related proteins; Actin depolymerization factor ...
 22-129 1.27e-12

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: 60.32  E-value: 1.27e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039021966  22 FIVYKIEEKQKQVIVEKVgEPILTYEDFAASLPADECRYAIYDFDfvtaeNCQKSKIFFIAWCPDVAKVRSKMIYASSKD 101
Cdd:cd11284    25 LVQLSIDLENETIELVSS-SSISIPDDLSSLIPSDHPRYHFYRYP-----HTYLSSVVFIYSCPSGSKVKERMLYASSKS 98

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1039021966 102 RFKREL---DGIQVE--LQATDPTEMDLDVLKS 129
Cdd:cd11284    99 GLLNHAedeGKIEIDkkIEIGDPDELTESFLSD 131
ADF_GMF-beta_like cd11283
ADF-homology domain of glia maturation factor beta and related proteins; Actin ...
 8-108 2.48e-11

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: 56.48  E-value: 2.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039021966   8 KLRFLELKAKRTHRFIVYKIEEKQKQVIVEKVGEPIlTYEDFAASLPADECRYAIYDFDFVTAENCQKSKIFFIAWCPDV 87
Cdd:cd11283     9 ALKKFRFRKSKANAALILKIDKEKQEIVVDEELEDI-SIEELAEELPEHSPRFVLYSYKMKHDDGRISYPLVLIYWSPQG 87

                          90       100
                  ....*....|....*....|.
gi 1039021966  88 AKVRSKMIYASSKDRFKRELD 108
Cdd:cd11283    88 CSPELQMLYAGAKELLVKEAE 108
ADF_drebrin_like cd11281
ADF homology domain of drebrin and actin-binding protein 1 (abp1); Actin depolymerization ...
 21-132 4.11e-03

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: 34.92  E-value: 4.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039021966  21 RFIVYKIEEKQKQVIVEKVGEPILtyEDFAASLPADECRYAiydFDFVTAENCQKSKIFFIAWCPDVAKVRSKMIYASSK 100
Cdd:cd11281    25 DWALFTYEGKSNDLKVADTGDGGL--EELVEEFSDGKVQYG---FARVKDPNSGLPKFVLINWCGEGVPDARKGSFASHV 99

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1039021966 101 DRFKRELDGIQVELQATDPTEMDLDVLKSRVN 132
Cdd:cd11281   100 AAVANFLKGAHVQINARSEDDLDEDAILKKVS 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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