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Conserved domains on  [gi|195345531|ref|XP_002039322|]
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coactosin-like protein [Drosophila sechellia]

Protein Classification

coactosin family protein( domain architecture ID 10181668)

coactosin family protein such as Dictyostelium discoideum coactosin, which binds to F-actin in a calcium independent manner; belongs to the actin depolymerization factor/cofilin-like (ADF) domain family

Gene Ontology:  GO:0051015
PubMed:  19768801|9693358

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ADF_coactosin_like cd11282
Coactosin-like members of the ADF homology domain family; Actin depolymerization factor ...
 28-139 1.84e-46

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: 147.40  E-value: 1.84e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195345531  28 SIREAYEDVRSDLTDTEWAVFKFDGA-QIIVHARGQCF-EEFRQQFGDSERAFGYIRIQMGDEMSKRKKFIFLTWIGQEV 105
Cdd:cd11282    1 EIREAYNDVRSDVSDTNWVLLGYESSnTLVLRGSGSGGiDELKAQLPDDEVLFGYVRITLGDGESKRSKFVFITWIGENV 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 195345531 106 GVIQRAKMSTDKALIKDVLNNFAVELQAGVEAEL 139
Cdd:cd11282   81 SVLRRAKVSVHKGDVKEVLSPFHVELTASSKDEL 114
 
Name Accession Description Interval E-value
ADF_coactosin_like cd11282
Coactosin-like members of the ADF homology domain family; Actin depolymerization factor ...
 28-139 1.84e-46

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: 147.40  E-value: 1.84e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195345531  28 SIREAYEDVRSDLTDTEWAVFKFDGA-QIIVHARGQCF-EEFRQQFGDSERAFGYIRIQMGDEMSKRKKFIFLTWIGQEV 105
Cdd:cd11282    1 EIREAYNDVRSDVSDTNWVLLGYESSnTLVLRGSGSGGiDELKAQLPDDEVLFGYVRITLGDGESKRSKFVFITWIGENV 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 195345531 106 GVIQRAKMSTDKALIKDVLNNFAVELQAGVEAEL 139
Cdd:cd11282   81 SVLRRAKVSVHKGDVKEVLSPFHVELTASSKDEL 114
Cofilin_ADF pfam00241
Cofilin/tropomyosin-type actin-binding protein; Severs actin filaments and binds to actin ...
 29-146 6.22e-27

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


Pssm-ID: 459727  Cd Length: 123  Bit Score: 98.03  E-value: 6.22e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195345531   29 IREAYEDVRSDlTDTEWAVFKFDGA--QIIVHARGQC---FEEFRQQFGDSERAFGYIRIQM-GDEMSKRKKFIFLTWIG 102
Cdd:pfam00241   1 CKEAYQELRSD-KKTNWIIFKIDDDkeEIVVEETGEGglsYDEFLEELPDDEPRYAVYRFEYtHDDGSKRSKLVFITWCP 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 195345531  103 QEVGVIQRAKMSTDKALIKDVLNNFAVELQAGVEAELDIELFRE 146
Cdd:pfam00241  80 DGAPIKRKMLYASSKAALKRELKGIHVEIQATDPSELTEEEILE 123
ADF smart00102
Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin ...
 30-149 4.09e-16

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


Pssm-ID: 214516  Cd Length: 127  Bit Score: 70.01  E-value: 4.09e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195345531    30 REAYEDVRSDLT--DTEWAVFKfDGAQIIVHARGQC---FEEFRQQFGDSERAFGYIRIQMGDEMSKRKKFIFLTWIGQE 104
Cdd:smart00102   4 KEAFNELKKKRKhsAIIFKIDK-DNEEIVVEEVGSTedsYDEFVEELPEDECRYALYDYKFTTEESKKSKIVFIFWSPDG 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 195345531   105 VGVIQRAKMSTDKALIKDVLNNFAVELQAGVEAELDIELFREALN 149
Cdd:smart00102  83 APVKSKMLYASSKDTLKKELGGIQVEVQATDEDDLDEEALKEKLK 127
 
Name Accession Description Interval E-value
ADF_coactosin_like cd11282
Coactosin-like members of the ADF homology domain family; Actin depolymerization factor ...
 28-139 1.84e-46

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: 147.40  E-value: 1.84e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195345531  28 SIREAYEDVRSDLTDTEWAVFKFDGA-QIIVHARGQCF-EEFRQQFGDSERAFGYIRIQMGDEMSKRKKFIFLTWIGQEV 105
Cdd:cd11282    1 EIREAYNDVRSDVSDTNWVLLGYESSnTLVLRGSGSGGiDELKAQLPDDEVLFGYVRITLGDGESKRSKFVFITWIGENV 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 195345531 106 GVIQRAKMSTDKALIKDVLNNFAVELQAGVEAEL 139
Cdd:cd11282   81 SVLRRAKVSVHKGDVKEVLSPFHVELTASSKDEL 114
Cofilin_ADF pfam00241
Cofilin/tropomyosin-type actin-binding protein; Severs actin filaments and binds to actin ...
 29-146 6.22e-27

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


Pssm-ID: 459727  Cd Length: 123  Bit Score: 98.03  E-value: 6.22e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195345531   29 IREAYEDVRSDlTDTEWAVFKFDGA--QIIVHARGQC---FEEFRQQFGDSERAFGYIRIQM-GDEMSKRKKFIFLTWIG 102
Cdd:pfam00241   1 CKEAYQELRSD-KKTNWIIFKIDDDkeEIVVEETGEGglsYDEFLEELPDDEPRYAVYRFEYtHDDGSKRSKLVFITWCP 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 195345531  103 QEVGVIQRAKMSTDKALIKDVLNNFAVELQAGVEAELDIELFRE 146
Cdd:pfam00241  80 DGAPIKRKMLYASSKAALKRELKGIHVEIQATDPSELTEEEILE 123
ADF smart00102
Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin ...
 30-149 4.09e-16

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


Pssm-ID: 214516  Cd Length: 127  Bit Score: 70.01  E-value: 4.09e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195345531    30 REAYEDVRSDLT--DTEWAVFKfDGAQIIVHARGQC---FEEFRQQFGDSERAFGYIRIQMGDEMSKRKKFIFLTWIGQE 104
Cdd:smart00102   4 KEAFNELKKKRKhsAIIFKIDK-DNEEIVVEEVGSTedsYDEFVEELPEDECRYALYDYKFTTEESKKSKIVFIFWSPDG 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 195345531   105 VGVIQRAKMSTDKALIKDVLNNFAVELQAGVEAELDIELFREALN 149
Cdd:smart00102  83 APVKSKMLYASSKDTLKKELGGIQVEVQATDEDDLDEEALKEKLK 127
ADF_drebrin_like cd11281
ADF homology domain of drebrin and actin-binding protein 1 (abp1); Actin depolymerization ...
 28-154 4.26e-14

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: 64.97  E-value: 4.26e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195345531  28 SIREAYEDVRSDLTDTEWAVFKFDG--AQIIVHARGQC-FEEFRQQFGDSERAFGYIRIqmGDEMSKRKKFIFLTWIGQE 104
Cdd:cd11281    9 EILAAYEDVVDGKSSTDWALFTYEGksNDLKVADTGDGgLEELVEEFSDGKVQYGFARV--KDPNSGLPKFVLINWCGEG 86

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 195345531 105 VGVIQRAKMSTDKALIKDVLNNFAVELQAGVEAELDIELFREALNRAGGA 154
Cdd:cd11281   87 VPDARKGSFASHVAAVANFLKGAHVQINARSEDDLDEDAILKKVSKASGA 136
ADF_gelsolin cd00013
Actin depolymerization factor/cofilin- and gelsolin-like domains; Actin depolymerization ...
 45-133 3.91e-11

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: 56.32  E-value: 3.91e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195345531  45 WAVFKFDGA--QIIVHARGQCFE-EFRQQFGDSERAFGYIRIQMGDEMSKRKKFIFLTWIGQEVGVIQRAKMSTDKALIK 121
Cdd:cd00013    2 WVLFKVDAKkeEIVVGSTGAGFLdEFLEELPEDDPRYAFYRFKYPHSDDKRSKFVFISWIPDGVSIKQKMVYATNKQTLK 81

                         90
                 ....*....|..
gi 195345531 122 DVLNNFAVELQA 133
Cdd:cd00013   82 EALFGLAVPVQI 93
ADF_cofilin_like cd11286
Cofilin, Destrin, and related actin depolymerizing factors; Actin depolymerization factor ...
 27-148 5.18e-07

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: 46.40  E-value: 5.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195345531  27 DSIREAYEDVRSDlTDTEWAVFKF--DGAQIIV---HARGQCFEEFRQQFGDSE-RafgYIRIQM---GDEMSKRKKFIF 97
Cdd:cd11286    7 DECITAFNELKLK-KKHKYIIFKIsdDKKEIVVekvGERDASYDDFLEKLPENEcR---YAVYDFeyeTKDGGKRSKLVF 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 195345531  98 LTWiGQEVGVIqRAKM--STDKALIKDVLNNFAVELQAGVEAELDIELFREAL 148
Cdd:cd11286   83 ISW-CPDTAPI-KSKMlyASSKDALKKKLNGIKKEIQATDLSELSEEEILEKL 133
 
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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