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Conserved domains on  [gi|24643098|ref|NP_573321|]
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uncharacterized protein Dmel_CG6873 [Drosophila melanogaster]

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 ...
 3-142 1.95e-54

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: 167.35  E-value: 1.95e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643098   3 SGINLSRECQHVFEQIRKLKQHRYAVFVIQDE-REIKVEVLGVREANYDDFLADLqraGSNQCRFAVYDYEYQHQcqgtl 81
Cdd:cd11286   1 SGVKVSDECITAFNELKLKKKHKYIIFKISDDkKEIVVEKVGERDASYDDFLEKL---PENECRYAVYDFEYETK----- 72

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24643098  82 STCLKEKLILMLWCPTLARIKDKMLYSSTFAVLKREFPGVQKCIQATEPEEACRNAVEEQL 142
Cdd:cd11286  73 DGGKRSKLVFISWCPDTAPIKSKMLYASSKDALKKKLNGIKKEIQATDLSELSEEEILEKL 133
 
Name Accession Description Interval E-value
ADF_cofilin_like cd11286
Cofilin, Destrin, and related actin depolymerizing factors; Actin depolymerization factor ...
 3-142 1.95e-54

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: 167.35  E-value: 1.95e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643098   3 SGINLSRECQHVFEQIRKLKQHRYAVFVIQDE-REIKVEVLGVREANYDDFLADLqraGSNQCRFAVYDYEYQHQcqgtl 81
Cdd:cd11286   1 SGVKVSDECITAFNELKLKKKHKYIIFKISDDkKEIVVEKVGERDASYDDFLEKL---PENECRYAVYDFEYETK----- 72

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24643098  82 STCLKEKLILMLWCPTLARIKDKMLYSSTFAVLKREFPGVQKCIQATEPEEACRNAVEEQL 142
Cdd:cd11286  73 DGGKRSKLVFISWCPDTAPIKSKMLYASSKDALKKKLNGIKKEIQATDLSELSEEEILEKL 133
ADF smart00102
Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin ...
 9-143 3.85e-35

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


Pssm-ID: 214516  Cd Length: 127  Bit Score: 118.54  E-value: 3.85e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643098      9 RECQHVFEQIRKLKQHRYAVFVI-QDEREIKVEVLGVREANYDDFLADLQRagsNQCRFAVYDYEYQHQcqgtlsTCLKE 87
Cdd:smart00102   1 EDCKEAFNELKKKRKHSAIIFKIdKDNEEIVVEEVGSTEDSYDEFVEELPE---DECRYALYDYKFTTE------ESKKS 71

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 24643098     88 KLILMLWCPTLARIKDKMLYSSTFAVLKREFPGVQKCIQATEPEEACRNAVEEQLR 143
Cdd:smart00102  72 KIVFIFWSPDGAPVKSKMLYASSKDTLKKELGGIQVEVQATDEDDLDEEALKEKLK 127
Cofilin_ADF pfam00241
Cofilin/tropomyosin-type actin-binding protein; Severs actin filaments and binds to actin ...
 11-140 5.35e-35

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


Pssm-ID: 459727  Cd Length: 123  Bit Score: 117.67  E-value: 5.35e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643098    11 CQHVFEQIRKLKQHRYAVFVIQDE-REIKVEVLGVREANYDDFLADLQragSNQCRFAVYDYEYQHQCQGTLStclkeKL 89
Cdd:pfam00241   1 CKEAYQELRSDKKTNWIIFKIDDDkEEIVVEETGEGGLSYDEFLEELP---DDEPRYAVYRFEYTHDDGSKRS-----KL 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 24643098    90 ILMLWCPTLARIKDKMLYSSTFAVLKREFPGVQKCIQATEPEEACRNAVEE 140
Cdd:pfam00241  73 VFITWCPDGAPIKRKMLYASSKAALKRELKGIHVEIQATDPSELTEEEILE 123
PLN03216 PLN03216
actin depolymerizing factor; Provisional
 3-132 5.50e-24

actin depolymerizing factor; Provisional


Pssm-ID: 178755  Cd Length: 141  Bit Score: 90.37  E-value: 5.50e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643098    3 SGINLSRECQHVFEQIRKLKQHRYAVFVIQDE-REIKVEVLGVREANYDDFLADLQragSNQCRFAVYDYEYQhqcqgTL 81
Cdd:PLN03216   8 TGMWVTDECKNSFMEMKWKKVHRYIVFKIDEKsRKVTVDKVGGPGESYDDLAASLP---TDDCRYAVFDFDFV-----TV 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 24643098   82 STCLKEKLILMLWCPTLARIKDKMLYSSTFAVLKREFPGVQKCIQATEPEE 132
Cdd:PLN03216  80 DNCRKSKIFFIAWSPEASRIRAKMLYATSKDGLRRVLDGVHYELQATDPTE 130
 
Name Accession Description Interval E-value
ADF_cofilin_like cd11286
Cofilin, Destrin, and related actin depolymerizing factors; Actin depolymerization factor ...
 3-142 1.95e-54

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: 167.35  E-value: 1.95e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643098   3 SGINLSRECQHVFEQIRKLKQHRYAVFVIQDE-REIKVEVLGVREANYDDFLADLqraGSNQCRFAVYDYEYQHQcqgtl 81
Cdd:cd11286   1 SGVKVSDECITAFNELKLKKKHKYIIFKISDDkKEIVVEKVGERDASYDDFLEKL---PENECRYAVYDFEYETK----- 72

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24643098  82 STCLKEKLILMLWCPTLARIKDKMLYSSTFAVLKREFPGVQKCIQATEPEEACRNAVEEQL 142
Cdd:cd11286  73 DGGKRSKLVFISWCPDTAPIKSKMLYASSKDALKKKLNGIKKEIQATDLSELSEEEILEKL 133
ADF smart00102
Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin ...
 9-143 3.85e-35

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


Pssm-ID: 214516  Cd Length: 127  Bit Score: 118.54  E-value: 3.85e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643098      9 RECQHVFEQIRKLKQHRYAVFVI-QDEREIKVEVLGVREANYDDFLADLQRagsNQCRFAVYDYEYQHQcqgtlsTCLKE 87
Cdd:smart00102   1 EDCKEAFNELKKKRKHSAIIFKIdKDNEEIVVEEVGSTEDSYDEFVEELPE---DECRYALYDYKFTTE------ESKKS 71

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 24643098     88 KLILMLWCPTLARIKDKMLYSSTFAVLKREFPGVQKCIQATEPEEACRNAVEEQLR 143
Cdd:smart00102  72 KIVFIFWSPDGAPVKSKMLYASSKDTLKKELGGIQVEVQATDEDDLDEEALKEKLK 127
Cofilin_ADF pfam00241
Cofilin/tropomyosin-type actin-binding protein; Severs actin filaments and binds to actin ...
 11-140 5.35e-35

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


Pssm-ID: 459727  Cd Length: 123  Bit Score: 117.67  E-value: 5.35e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643098    11 CQHVFEQIRKLKQHRYAVFVIQDE-REIKVEVLGVREANYDDFLADLQragSNQCRFAVYDYEYQHQCQGTLStclkeKL 89
Cdd:pfam00241   1 CKEAYQELRSDKKTNWIIFKIDDDkEEIVVEETGEGGLSYDEFLEELP---DDEPRYAVYRFEYTHDDGSKRS-----KL 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 24643098    90 ILMLWCPTLARIKDKMLYSSTFAVLKREFPGVQKCIQATEPEEACRNAVEE 140
Cdd:pfam00241  73 VFITWCPDGAPIKRKMLYASSKAALKRELKGIHVEIQATDPSELTEEEILE 123
PLN03216 PLN03216
actin depolymerizing factor; Provisional
 3-132 5.50e-24

actin depolymerizing factor; Provisional


Pssm-ID: 178755  Cd Length: 141  Bit Score: 90.37  E-value: 5.50e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643098    3 SGINLSRECQHVFEQIRKLKQHRYAVFVIQDE-REIKVEVLGVREANYDDFLADLQragSNQCRFAVYDYEYQhqcqgTL 81
Cdd:PLN03216   8 TGMWVTDECKNSFMEMKWKKVHRYIVFKIDEKsRKVTVDKVGGPGESYDDLAASLP---TDDCRYAVFDFDFV-----TV 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 24643098   82 STCLKEKLILMLWCPTLARIKDKMLYSSTFAVLKREFPGVQKCIQATEPEE 132
Cdd:PLN03216  80 DNCRKSKIFFIAWSPEASRIRAKMLYATSKDGLRRVLDGVHYELQATDPTE 130
ADF_gelsolin cd00013
Actin depolymerization factor/cofilin- and gelsolin-like domains; Actin depolymerization ...
 33-131 1.74e-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: 64.79  E-value: 1.74e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643098  33 DEREIkveVLGVREANYDDFLadLQRAGSNQCRFAVYDYEYQHqcqgtlSTCLKEKLILMLWCPTLARIKDKMLYSSTFA 112
Cdd:cd00013  10 KKEEI---VVGSTGAGFLDEF--LEELPEDDPRYAFYRFKYPH------SDDKRSKFVFISWIPDGVSIKQKMVYATNKQ 78

                        90
                ....*....|....*....
gi 24643098 113 VLKREFPGVQKCIQATEPE 131
Cdd:cd00013  79 TLKEALFGLAVPVQIRDGD 97
PTZ00152 PTZ00152
cofilin/actin-depolymerizing factor 1-like protein; Provisional
 1-121 7.42e-09

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


Pssm-ID: 173441  Cd Length: 122  Bit Score: 50.72  E-value: 7.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643098    1 MASGINLSRECQHVFEQIRKLKQHRYAVFVIQDErEIKVEVLGVREAnYDDFLADLQRAGSNQCRFAVYDyeyqhqcqgt 80
Cdd:PTZ00152   1 MISGIRVNDNCVTEFNNMKIRKTCRWIIFVIENC-EIIIHSKGATTT-LTELVGSIDKNDKIQCAYVVFD---------- 68

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 24643098   81 lstcLKEKLILMLWCPTLARIKDKMLYSSTFAVLKREFPGV 121
Cdd:PTZ00152  69 ----AVNKIHFFMYARESSNSRDRMTYASSKQALLKKIEGV 105
ADF_Twf-N_like cd11285
N-terminal ADF domain of twinfilin and related proteins; Actin depolymerization factor ...
 3-146 1.79e-06

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: 44.55  E-value: 1.79e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24643098   3 SGINLSRECQHVFEQIRKLKQHRYAVFVIQDEREIKVEVLGVREANYDDFLADLQRAGS-NQCRFAVYDYEYQHQcqgtl 81
Cdd:cd11285   2 SGITASEELLDAFKSAKSSGSVRAIKITIENEELVPDATIETTGSWEQDFDLLVLPLLEeKEPCYILYRLDSKSA----- 76

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24643098  82 stclKEKLILMLWCPTLARIKDKMLYSSTFAVLKREFPG--VQKCIQATEPEEACRNAVEEQLRSLD 146
Cdd:cd11285  77 ----GYEWVFISFVPDSAPVRQKMLYASTRATLKRELGSnhIKDELFATELEELTLEGYEKHLKHEA 139
ADF_GMF-beta_like cd11283
ADF-homology domain of glia maturation factor beta and related proteins; Actin ...
 61-132 1.48e-04

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: 39.14  E-value: 1.48e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24643098  61 SNQCRFAVYDYEYQHQcQGTLSTclkeKLILMLWCPTLARIKDKMLYSSTFAVLKREFpGVQKCIQATEPEE 132
Cdd:cd11283  55 EHSPRFVLYSYKMKHD-DGRISY----PLVLIYWSPQGCSPELQMLYAGAKELLVKEA-EVTKVFEIRDGEE 120
 
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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