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Conserved domains on  [gi|327263631|ref|XP_003216622|]
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PREDICTED: cofilin-2 [Anolis carolinensis]

Protein Classification

ADF_cofilin_like domain-containing protein (domain architecture ID 10181692)

ADF_cofilin_like domain-containing protein

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 ...
3-153 1.35e-50

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: 161.57  E-value: 1.35e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327263631   3 SGVTVNDEVIKVFNDMKVRKSstpeeikkrKKAVLFCLSDDKKQIIVEEakqilVGEVGDTVEDpytsFVKLLPLNDCRY 82
Cdd:cd11286    1 SGVKVSDECITAFNELKLKKK---------HKYIIFKISDDKKEIVVEK-----VGERDASYDD----FLEKLPENECRY 62
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 327263631  83 ALYDATYETK-ESKKEDLVFIFWAPESAPLKSKMIYASSKDAIKKKFTGIKHEWQVNGLDDIkDRCTLGEKL 153
Cdd:cd11286   63 AVYDFEYETKdGGKRSKLVFISWCPDTAPIKSKMLYASSKDALKKKLNGIKKEIQATDLSEL-SEEEILEKL 133
 
Name Accession Description Interval E-value
ADF_cofilin_like cd11286
Cofilin, Destrin, and related actin depolymerizing factors; Actin depolymerization factor ...
3-153 1.35e-50

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: 161.57  E-value: 1.35e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327263631   3 SGVTVNDEVIKVFNDMKVRKSstpeeikkrKKAVLFCLSDDKKQIIVEEakqilVGEVGDTVEDpytsFVKLLPLNDCRY 82
Cdd:cd11286    1 SGVKVSDECITAFNELKLKKK---------HKYIIFKISDDKKEIVVEK-----VGERDASYDD----FLEKLPENECRY 62
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 327263631  83 ALYDATYETK-ESKKEDLVFIFWAPESAPLKSKMIYASSKDAIKKKFTGIKHEWQVNGLDDIkDRCTLGEKL 153
Cdd:cd11286   63 AVYDFEYETKdGGKRSKLVFISWCPDTAPIKSKMLYASSKDALKKKLNGIKKEIQATDLSEL-SEEEILEKL 133
ADF smart00102
Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin ...
19-154 1.71e-41

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


Pssm-ID: 214516  Cd Length: 127  Bit Score: 138.19  E-value: 1.71e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327263631    19 KVRKSSTPEEIKKRK-KAVLFCLSDDKKQIIVEEAKQilvgevgdtVEDPYTSFVKLLPLNDCRYALYDATYETKESKKE 97
Cdd:smart00102   1 EDCKEAFNELKKKRKhSAIIFKIDKDNEEIVVEEVGS---------TEDSYDEFVEELPEDECRYALYDYKFTTEESKKS 71
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 327263631    98 DLVFIFWAPESAPLKSKMIYASSKDAIKKKFTGIKHEWQVNGLDDIkDRCTLGEKLG 154
Cdd:smart00102  72 KIVFIFWSPDGAPVKSKMLYASSKDTLKKELGGIQVEVQATDEDDL-DEEALKEKLK 127
Cofilin_ADF pfam00241
Cofilin/tropomyosin-type actin-binding protein; Severs actin filaments and binds to actin ...
27-143 3.55e-27

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


Pssm-ID: 306703  Cd Length: 119  Bit Score: 100.73  E-value: 3.55e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327263631   27 EEIKKRKK-AVLFCLSDDKKQIIVEEAkqilvgevgdtvEDPYTSFVKLLPLNDCRYALYDATYETKESKKEDLVFIFWA 105
Cdd:pfam00241   6 QEVRSDKSnWIIFKIDDEKNEIVVEAG------------EGGLEELAEELPDKVPRYAVYRVKYTHDDGRVSKLVFIYWC 73
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 327263631  106 PESAPLKSKMIYASSKDAIKKKF-TGIKHEWQVNGLDDI 143
Cdd:pfam00241  74 PGGAPIKRKMLYASSKGALKRELlKGIHVEIQARDLSEL 112
PLN03216 PLN03216
actin depolymerizing factor; Provisional
3-146 9.80e-19

actin depolymerizing factor; Provisional


Pssm-ID: 178755  Cd Length: 141  Bit Score: 79.20  E-value: 9.80e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327263631   3 SGVTVNDEVIKVFNDMKvrksstpeeIKKRKKAVLFCLSDDKKQIIVEEakqilVGEVGDTVEDPYTSfvklLPLNDCRY 82
Cdd:PLN03216   8 TGMWVTDECKNSFMEMK---------WKKVHRYIVFKIDEKSRKVTVDK-----VGGPGESYDDLAAS----LPTDDCRY 69
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327263631  83 ALYDATYETKES-KKEDLVFIFWAPESAPLKSKMIYASSKDAIKKKFTGIKHEWQVN-----GLDDIKDR 146
Cdd:PLN03216  70 AVFDFDFVTVDNcRKSKIFFIAWSPEASRIRAKMLYATSKDGLRRVLDGVHYELQATdptemGFDVIRDR 139
 
Name Accession Description Interval E-value
ADF_cofilin_like cd11286
Cofilin, Destrin, and related actin depolymerizing factors; Actin depolymerization factor ...
3-153 1.35e-50

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: 161.57  E-value: 1.35e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327263631   3 SGVTVNDEVIKVFNDMKVRKSstpeeikkrKKAVLFCLSDDKKQIIVEEakqilVGEVGDTVEDpytsFVKLLPLNDCRY 82
Cdd:cd11286    1 SGVKVSDECITAFNELKLKKK---------HKYIIFKISDDKKEIVVEK-----VGERDASYDD----FLEKLPENECRY 62
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 327263631  83 ALYDATYETK-ESKKEDLVFIFWAPESAPLKSKMIYASSKDAIKKKFTGIKHEWQVNGLDDIkDRCTLGEKL 153
Cdd:cd11286   63 AVYDFEYETKdGGKRSKLVFISWCPDTAPIKSKMLYASSKDALKKKLNGIKKEIQATDLSEL-SEEEILEKL 133
ADF smart00102
Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin ...
19-154 1.71e-41

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


Pssm-ID: 214516  Cd Length: 127  Bit Score: 138.19  E-value: 1.71e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327263631    19 KVRKSSTPEEIKKRK-KAVLFCLSDDKKQIIVEEAKQilvgevgdtVEDPYTSFVKLLPLNDCRYALYDATYETKESKKE 97
Cdd:smart00102   1 EDCKEAFNELKKKRKhSAIIFKIDKDNEEIVVEEVGS---------TEDSYDEFVEELPEDECRYALYDYKFTTEESKKS 71
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 327263631    98 DLVFIFWAPESAPLKSKMIYASSKDAIKKKFTGIKHEWQVNGLDDIkDRCTLGEKLG 154
Cdd:smart00102  72 KIVFIFWSPDGAPVKSKMLYASSKDTLKKELGGIQVEVQATDEDDL-DEEALKEKLK 127
Cofilin_ADF pfam00241
Cofilin/tropomyosin-type actin-binding protein; Severs actin filaments and binds to actin ...
27-143 3.55e-27

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


Pssm-ID: 306703  Cd Length: 119  Bit Score: 100.73  E-value: 3.55e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327263631   27 EEIKKRKK-AVLFCLSDDKKQIIVEEAkqilvgevgdtvEDPYTSFVKLLPLNDCRYALYDATYETKESKKEDLVFIFWA 105
Cdd:pfam00241   6 QEVRSDKSnWIIFKIDDEKNEIVVEAG------------EGGLEELAEELPDKVPRYAVYRVKYTHDDGRVSKLVFIYWC 73
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 327263631  106 PESAPLKSKMIYASSKDAIKKKF-TGIKHEWQVNGLDDI 143
Cdd:pfam00241  74 PGGAPIKRKMLYASSKGALKRELlKGIHVEIQARDLSEL 112
PLN03216 PLN03216
actin depolymerizing factor; Provisional
3-146 9.80e-19

actin depolymerizing factor; Provisional


Pssm-ID: 178755  Cd Length: 141  Bit Score: 79.20  E-value: 9.80e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327263631   3 SGVTVNDEVIKVFNDMKvrksstpeeIKKRKKAVLFCLSDDKKQIIVEEakqilVGEVGDTVEDPYTSfvklLPLNDCRY 82
Cdd:PLN03216   8 TGMWVTDECKNSFMEMK---------WKKVHRYIVFKIDEKSRKVTVDK-----VGGPGESYDDLAAS----LPTDDCRY 69
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327263631  83 ALYDATYETKES-KKEDLVFIFWAPESAPLKSKMIYASSKDAIKKKFTGIKHEWQVN-----GLDDIKDR 146
Cdd:PLN03216  70 AVFDFDFVTVDNcRKSKIFFIAWSPEASRIRAKMLYATSKDGLRRVLDGVHYELQATdptemGFDVIRDR 139
ADF_gelsolin cd00013
Actin depolymerization factor/cofilin- and gelsolin-like domains; Actin depolymerization ...
34-141 4.22e-17

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: 73.65  E-value: 4.22e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327263631  34 KAVLFCLSDDKKQIIVeeakqilvgevGDTVEDPYTSFVKLLPLNDCRYALYDATYETKESKKEDLVFIFWAPESAPLKS 113
Cdd:cd00013    1 DWVLFKVDAKKEEIVV-----------GSTGAGFLDEFLEELPEDDPRYAFYRFKYPHSDDKRSKFVFISWIPDGVSIKQ 69
                         90       100
                 ....*....|....*....|....*...
gi 327263631 114 KMIYASSKDAIKKKFTGIKHEWQVNGLD 141
Cdd:cd00013   70 KMVYATNKQTLKEALFGLAVPVQIRDGD 97
PTZ00152 PTZ00152
cofilin/actin-depolymerizing factor 1-like protein; Provisional
1-131 5.04e-15

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


Pssm-ID: 173441  Cd Length: 122  Bit Score: 68.44  E-value: 5.04e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327263631   1 MASGVTVNDEVIKVFNDMKVRKSStpeeikkrkKAVLFCLSDDKkqIIVEEakqilvgevgDTVEDPYTSFVKLLPLND- 79
Cdd:PTZ00152   1 MISGIRVNDNCVTEFNNMKIRKTC---------RWIIFVIENCE--IIIHS----------KGATTTLTELVGSIDKNDk 59
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 327263631  80 --CRYALYDATYETKeskkedlvFIFWAPESAPLKSKMIYASSKDAIKKKFTGI 131
Cdd:PTZ00152  60 iqCAYVVFDAVNKIH--------FFMYARESSNSRDRMTYASSKQALLKKIEGV 105
ADF_Twf-N_like cd11285
N-terminal ADF domain of twinfilin and related proteins; Actin depolymerization factor ...
3-145 4.47e-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: 63.42  E-value: 4.47e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327263631   3 SGVTVNDEVIKVFNDMKVRKSstpeeikkrkkAVLFCLSDDKKQIIVEEAKqilvgEVGDTVEDPYTSFVKLLPLND--C 80
Cdd:cd11285    2 SGITASEELLDAFKSAKSSGS-----------VRAIKITIENEELVPDATI-----ETTGSWEQDFDLLVLPLLEEKepC 65
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 327263631  81 rYALYDATYETKESkkeDLVFIFWAPESAPLKSKMIYASSKDAIKKKFTG--IKHEWQVNGLDDIKD 145
Cdd:cd11285   66 -YILYRLDSKSAGY---EWVFISFVPDSAPVRQKMLYASTRATLKRELGSnhIKDELFATELEELTL 128
ADF_GMF-beta_like cd11283
ADF-homology domain of glia maturation factor beta and related proteins; Actin ...
6-128 3.26e-06

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  Cd Length: 122  Bit Score: 43.76  E-value: 3.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327263631   6 TVNDEVIKVFNDMKVRKSSTPeeikkrkKAVLFCLSDDKKQIIV-EEAKQILVGEVGDTvedpytsfvklLPLNDCRYAL 84
Cdd:cd11283    1 DISDEVKEALKKFRFRKSKAN-------AALILKIDKEKQEIVVdEELEDISIEELAEE-----------LPEHSPRFVL 62
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 327263631  85 YDATYETKESKKE-DLVFIFWAPESAPLKSKMIYASSKDAIKKKF 128
Cdd:cd11283   63 YSYKMKHDDGRISyPLVLIYWSPQGCSPELQMLYAGAKELLVKEA 107
ADF_Twf-C_like cd11284
C-terminal ADF domain of twinfilin and related proteins; Actin depolymerization factor ...
31-121 7.43e-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: 37.60  E-value: 7.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327263631  31 KRKKAVLFCLSDDKKQIIVEEAKQIlvgevgdtveDPYTSFVKLLPLNDCRYALYdaTYetKESKKEDLVFIFWAPESAP 110
Cdd:cd11284   21 GGVNLVQLSIDLENETIELVSSSSI----------SIPDDLSSLIPSDHPRYHFY--RY--PHTYLSSVVFIYSCPSGSK 86
                         90
                 ....*....|.
gi 327263631 111 LKSKMIYASSK 121
Cdd:cd11284   87 VKERMLYASSK 97
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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