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Conserved domains on  [gi|79487032|ref|NP_194289|]
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actin depolymerizing factor 7 [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

 Zoom to residue level

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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 ...
 6-136 1.43e-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: 190.08  E-value: 1.43e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487032   6 SGMAVEDECKLKFLELKSKRNYRFIIFRI--DGQQVVVEKLGNPDETYDDFTASLPANECRYAVFDFDFITDENCQKSKI 83
Cdd:cd11286   1 SGVKVSDECITAFNELKLKKKHKYIIFKIsdDKKEIVVEKVGERDASYDDFLEKLPENECRYAVYDFEYETKDGGKRSKL 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 79487032  84 FFIAWSPDSSRVRMKMVYASSKDRFKRELDGIQVELQATDPSEMSFDIIKSRA 136
Cdd:cd11286  81 VFISWCPDTAPIKSKMLYASSKDALKKKLNGIKKEIQATDLSELSEEEILEKL 133
 
Name Accession Description Interval E-value
ADF_cofilin_like cd11286
Cofilin, Destrin, and related actin depolymerizing factors; Actin depolymerization factor ...
 6-136 1.43e-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: 190.08  E-value: 1.43e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487032   6 SGMAVEDECKLKFLELKSKRNYRFIIFRI--DGQQVVVEKLGNPDETYDDFTASLPANECRYAVFDFDFITDENCQKSKI 83
Cdd:cd11286   1 SGVKVSDECITAFNELKLKKKHKYIIFKIsdDKKEIVVEKVGERDASYDDFLEKLPENECRYAVYDFEYETKDGGKRSKL 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 79487032  84 FFIAWSPDSSRVRMKMVYASSKDRFKRELDGIQVELQATDPSEMSFDIIKSRA 136
Cdd:cd11286  81 VFISWCPDTAPIKSKMLYASSKDALKKKLNGIKKEIQATDLSELSEEEILEKL 133
PLN03216 PLN03216
actin depolymerizing factor; Provisional
 4-136 3.37e-63

actin depolymerizing factor; Provisional


Pssm-ID: 178755  Cd Length: 141  Bit Score: 189.75  E-value: 3.37e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487032    4 AASGMAVEDECKLKFLELKSKRNYRFIIFRID--GQQVVVEKLGNPDETYDDFTASLPANECRYAVFDFDFITDENCQKS 81
Cdd:PLN03216   6 ATTGMWVTDECKNSFMEMKWKKVHRYIVFKIDekSRKVTVDKVGGPGESYDDLAASLPTDDCRYAVFDFDFVTVDNCRKS 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 79487032   82 KIFFIAWSPDSSRVRMKMVYASSKDRFKRELDGIQVELQATDPSEMSFDIIKSRA 136
Cdd:PLN03216  86 KIFFIAWSPEASRIRAKMLYATSKDGLRRVLDGVHYELQATDPTEMGFDVIRDRA 140
ADF smart00102
Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin ...
 12-136 4.71e-54

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


Pssm-ID: 214516  Cd Length: 127  Bit Score: 165.92  E-value: 4.71e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487032     12 DECKLKFLELKSKRNYRFIIFRID--GQQVVVEKLGNPDETYDDFTASLPANECRYAVFDFDFiTDENCQKSKIFFIAWS 89
Cdd:smart00102   1 EDCKEAFNELKKKRKHSAIIFKIDkdNEEIVVEEVGSTEDSYDEFVEELPEDECRYALYDYKF-TTEESKKSKIVFIFWS 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 79487032     90 PDSSRVRMKMVYASSKDRFKRELDGIQVELQATDPSEMSFDIIKSRA 136
Cdd:smart00102  80 PDGAPVKSKMLYASSKDTLKKELGGIQVEVQATDEDDLDEEALKEKL 126
Cofilin_ADF pfam00241
Cofilin/tropomyosin-type actin-binding protein; Severs actin filaments and binds to actin ...
 14-134 3.51e-49

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


Pssm-ID: 459727  Cd Length: 123  Bit Score: 153.50  E-value: 3.51e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487032    14 CKLKFLELKSKRNYRFIIFRIDG--QQVVVEKLGNPDETYDDFTASLPANECRYAVFDFDFITDENCQKSKIFFIAWSPD 91
Cdd:pfam00241   1 CKEAYQELRSDKKTNWIIFKIDDdkEEIVVEETGEGGLSYDEFLEELPDDEPRYAVYRFEYTHDDGSKRSKLVFITWCPD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 79487032    92 SSRVRMKMVYASSKDRFKRELDGIQVELQATDPSEMSFDIIKS 134
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 ...
 6-136 1.43e-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: 190.08  E-value: 1.43e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487032   6 SGMAVEDECKLKFLELKSKRNYRFIIFRI--DGQQVVVEKLGNPDETYDDFTASLPANECRYAVFDFDFITDENCQKSKI 83
Cdd:cd11286   1 SGVKVSDECITAFNELKLKKKHKYIIFKIsdDKKEIVVEKVGERDASYDDFLEKLPENECRYAVYDFEYETKDGGKRSKL 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 79487032  84 FFIAWSPDSSRVRMKMVYASSKDRFKRELDGIQVELQATDPSEMSFDIIKSRA 136
Cdd:cd11286  81 VFISWCPDTAPIKSKMLYASSKDALKKKLNGIKKEIQATDLSELSEEEILEKL 133
PLN03216 PLN03216
actin depolymerizing factor; Provisional
 4-136 3.37e-63

actin depolymerizing factor; Provisional


Pssm-ID: 178755  Cd Length: 141  Bit Score: 189.75  E-value: 3.37e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487032    4 AASGMAVEDECKLKFLELKSKRNYRFIIFRID--GQQVVVEKLGNPDETYDDFTASLPANECRYAVFDFDFITDENCQKS 81
Cdd:PLN03216   6 ATTGMWVTDECKNSFMEMKWKKVHRYIVFKIDekSRKVTVDKVGGPGESYDDLAASLPTDDCRYAVFDFDFVTVDNCRKS 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 79487032   82 KIFFIAWSPDSSRVRMKMVYASSKDRFKRELDGIQVELQATDPSEMSFDIIKSRA 136
Cdd:PLN03216  86 KIFFIAWSPEASRIRAKMLYATSKDGLRRVLDGVHYELQATDPTEMGFDVIRDRA 140
ADF smart00102
Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin ...
 12-136 4.71e-54

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


Pssm-ID: 214516  Cd Length: 127  Bit Score: 165.92  E-value: 4.71e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487032     12 DECKLKFLELKSKRNYRFIIFRID--GQQVVVEKLGNPDETYDDFTASLPANECRYAVFDFDFiTDENCQKSKIFFIAWS 89
Cdd:smart00102   1 EDCKEAFNELKKKRKHSAIIFKIDkdNEEIVVEEVGSTEDSYDEFVEELPEDECRYALYDYKF-TTEESKKSKIVFIFWS 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 79487032     90 PDSSRVRMKMVYASSKDRFKRELDGIQVELQATDPSEMSFDIIKSRA 136
Cdd:smart00102  80 PDGAPVKSKMLYASSKDTLKKELGGIQVEVQATDEDDLDEEALKEKL 126
Cofilin_ADF pfam00241
Cofilin/tropomyosin-type actin-binding protein; Severs actin filaments and binds to actin ...
 14-134 3.51e-49

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


Pssm-ID: 459727  Cd Length: 123  Bit Score: 153.50  E-value: 3.51e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487032    14 CKLKFLELKSKRNYRFIIFRIDG--QQVVVEKLGNPDETYDDFTASLPANECRYAVFDFDFITDENCQKSKIFFIAWSPD 91
Cdd:pfam00241   1 CKEAYQELRSDKKTNWIIFKIDDdkEEIVVEETGEGGLSYDEFLEELPDDEPRYAVYRFEYTHDDGSKRSKLVFITWCPD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 79487032    92 SSRVRMKMVYASSKDRFKRELDGIQVELQATDPSEMSFDIIKS 134
Cdd:pfam00241  81 GAPIKRKMLYASSKAALKRELKGIHVEIQATDPSELTEEEILE 123
PTZ00152 PTZ00152
cofilin/actin-depolymerizing factor 1-like protein; Provisional
 5-117 3.59e-21

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


Pssm-ID: 173441  Cd Length: 122  Bit Score: 82.31  E-value: 3.59e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487032    5 ASGMAVEDECKLKFLELKSKRNYRFIIFRIDGQQVVVEKLGNPDeTYDDFTASLPAN---ECRYAVFDfdfitdencQKS 81
Cdd:PTZ00152   2 ISGIRVNDNCVTEFNNMKIRKTCRWIIFVIENCEIIIHSKGATT-TLTELVGSIDKNdkiQCAYVVFD---------AVN 71

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 79487032   82 KIFFIAWSPDSSRVRMKMVYASSKDRFKRELDGIQV 117
Cdd:PTZ00152  72 KIHFFMYARESSNSRDRMTYASSKQALLKKIEGVNV 107
ADF_gelsolin cd00013
Actin depolymerization factor/cofilin- and gelsolin-like domains; Actin depolymerization ...
 28-123 3.54e-19

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: 76.35  E-value: 3.54e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487032  28 RFIIFRIDG--QQVVVEKLGNPDEtyDDFTASLPANECRYAVFDFDFiTDENCQKSKIFFIAWSPDSSRVRMKMVYASSK 105
Cdd:cd00013   1 DWVLFKVDAkkEEIVVGSTGAGFL--DEFLEELPEDDPRYAFYRFKY-PHSDDKRSKFVFISWIPDGVSIKQKMVYATNK 77

                        90
                ....*....|....*...
gi 79487032 106 DRFKRELDGIQVELQATD 123
Cdd:cd00013  78 QTLKEALFGLAVPVQIRD 95
ADF_Twf-N_like cd11285
N-terminal ADF domain of twinfilin and related proteins; Actin depolymerization factor ...
 6-130 4.55e-16

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: 69.58  E-value: 4.55e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487032   6 SGMAVEDECKLKFLELKSKRNYRFIIFRIDGQQVVVEKLGNPDETYDDF-----TASLPANECRYAVFdfdfITDENCQK 80
Cdd:cd11285   2 SGITASEELLDAFKSAKSSGSVRAIKITIENEELVPDATIETTGSWEQDfdllvLPLLEEKEPCYILY----RLDSKSAG 77

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 79487032  81 SKIFFIAWSPDSSRVRMKMVYASSKDRFKRELDG--IQVELQATDPSEMSFD 130
Cdd:cd11285  78 YEWVFISFVPDSAPVRQKMLYASTRATLKRELGSnhIKDELFATELEELTLE 129
ADF_GMF-beta_like cd11283
ADF-homology domain of glia maturation factor beta and related proteins; Actin ...
 10-113 9.20e-10

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: 52.62  E-value: 9.20e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487032  10 VEDECK--LKFLELKSKRNYRFIIFRID--GQQVVVEKLGNpDETYDDFTASLPANECRYAVFDFDFITDENCQKSKIFF 85
Cdd:cd11283   2 ISDEVKeaLKKFRFRKSKANAALILKIDkeKQEIVVDEELE-DISIEELAEELPEHSPRFVLYSYKMKHDDGRISYPLVL 80

                        90       100
                ....*....|....*....|....*...
gi 79487032  86 IAWSPDSSRVRMKMVYASSKDRFKRELD 113
Cdd:cd11283  81 IYWSPQGCSPELQMLYAGAKELLVKEAE 108
ADF_Twf-C_like cd11284
C-terminal ADF domain of twinfilin and related proteins; Actin depolymerization factor ...
 7-134 9.49e-10

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: 53.00  E-value: 9.49e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79487032   7 GMAVEDECKLKFLELKSKrNYRFIIFRIDGQQVVVEkLGNPDET--YDDFTASLPANECRYAVFDFDfitdeNCQKSKIF 84
Cdd:cd11284   4 AFPVSEEAKDALSELASG-GVNLVQLSIDLENETIE-LVSSSSIsiPDDLSSLIPSDHPRYHFYRYP-----HTYLSSVV 76

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 79487032  85 FIAWSPDSSRVRMKMVYASSKDRFKREL---DGIQVE--LQATDPSEMSFDIIKS 134
Cdd:cd11284  77 FIYSCPSGSKVKERMLYASSKSGLLNHAedeGKIEIDkkIEIGDPDELTESFLSD 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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