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Conserved domains on  [gi|19482160|ref|NP_082347|]
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coactosin-like protein [Mus musculus]

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 ...
 9-120 7.80e-44

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: 139.69  E-value: 7.80e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19482160   9 ACRAAYNLVRDDGSAVIWVTFRYDGA-TIVPGDQGADY-QHFIQQCTDDVRLFAFVRFTTGDAMSKRSKFALITWIGEDV 86
Cdd:cd11282   1 EIREAYNDVRSDVSDTNWVLLGYESSnTLVLRGSGSGGiDELKAQLPDDEVLFGYVRITLGDGESKRSKFVFITWIGENV 80

                        90       100       110
                ....*....|....*....|....*....|....
gi 19482160  87 SGLQRAKTGTDKTLVKEVVQNFAKEFVISDRKEL 120
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 ...
 9-120 7.80e-44

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: 139.69  E-value: 7.80e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19482160   9 ACRAAYNLVRDDGSAVIWVTFRYDGA-TIVPGDQGADY-QHFIQQCTDDVRLFAFVRFTTGDAMSKRSKFALITWIGEDV 86
Cdd:cd11282   1 EIREAYNDVRSDVSDTNWVLLGYESSnTLVLRGSGSGGiDELKAQLPDDEVLFGYVRITLGDGESKRSKFVFITWIGENV 80

                        90       100       110
                ....*....|....*....|....*....|....
gi 19482160  87 SGLQRAKTGTDKTLVKEVVQNFAKEFVISDRKEL 120
Cdd:cd11282  81 SVLRRAKVSVHKGDVKEVLSPFHVELTASSKDEL 114
ADF smart00102
Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin ...
 8-130 3.04e-28

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


Pssm-ID: 214516  Cd Length: 127  Bit Score: 100.44  E-value: 3.04e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19482160      8 EACRAAYNLVRDD--GSAVIWVTFRYDgATIVPGDQG---ADYQHFIQQCTDDVRLFAFVRFTTGDAMSKRSKFALITWI 82
Cdd:smart00102   1 EDCKEAFNELKKKrkHSAIIFKIDKDN-EEIVVEEVGsteDSYDEFVEELPEDECRYALYDYKFTTEESKKSKIVFIFWS 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 19482160     83 GEDVSGLQRAKTGTDKTLVKEVVQNFAKEFVISDRKELEEDFIRSELK 130
Cdd:smart00102  80 PDGAPVKSKMLYASSKDTLKKELGGIQVEVQATDEDDLDEEALKEKLK 127
Cofilin_ADF pfam00241
Cofilin/tropomyosin-type actin-binding protein; Severs actin filaments and binds to actin ...
 10-127 2.64e-25

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


Pssm-ID: 459727  Cd Length: 123  Bit Score: 93.02  E-value: 2.64e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19482160    10 CRAAYNLVRDDGSaVIWVTFRYDGA--TIVP---GDQGADYQHFIQQCTDDVRLFAFVRFT-TGDAMSKRSKFALITWIG 83
Cdd:pfam00241   1 CKEAYQELRSDKK-TNWIIFKIDDDkeEIVVeetGEGGLSYDEFLEELPDDEPRYAVYRFEyTHDDGSKRSKLVFITWCP 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 19482160    84 EDVSGLQRAKTGTDKTLVKEVVQNFAKEFVISDRKELEEDFIRS 127
Cdd:pfam00241  80 DGAPIKRKMLYASSKAALKRELKGIHVEIQATDPSELTEEEILE 123
 
Name Accession Description Interval E-value
ADF_coactosin_like cd11282
Coactosin-like members of the ADF homology domain family; Actin depolymerization factor ...
 9-120 7.80e-44

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: 139.69  E-value: 7.80e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19482160   9 ACRAAYNLVRDDGSAVIWVTFRYDGA-TIVPGDQGADY-QHFIQQCTDDVRLFAFVRFTTGDAMSKRSKFALITWIGEDV 86
Cdd:cd11282   1 EIREAYNDVRSDVSDTNWVLLGYESSnTLVLRGSGSGGiDELKAQLPDDEVLFGYVRITLGDGESKRSKFVFITWIGENV 80

                        90       100       110
                ....*....|....*....|....*....|....
gi 19482160  87 SGLQRAKTGTDKTLVKEVVQNFAKEFVISDRKEL 120
Cdd:cd11282  81 SVLRRAKVSVHKGDVKEVLSPFHVELTASSKDEL 114
ADF_gelsolin cd00013
Actin depolymerization factor/cofilin- and gelsolin-like domains; Actin depolymerization ...
 25-118 1.06e-28

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: 101.00  E-value: 1.06e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19482160  25 IWVTFRYDGA--TIVPGDQGADYQH-FIQQCTDDVRLFAFVRFTTGDAMSKRSKFALITWIGEDVSGLQRAKTGTDKTLV 101
Cdd:cd00013   1 DWVLFKVDAKkeEIVVGSTGAGFLDeFLEELPEDDPRYAFYRFKYPHSDDKRSKFVFISWIPDGVSIKQKMVYATNKQTL 80

                        90
                ....*....|....*..
gi 19482160 102 KEVVQNFAKEFVISDRK 118
Cdd:cd00013  81 KEALFGLAVPVQIRDGD 97
ADF smart00102
Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin ...
 8-130 3.04e-28

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


Pssm-ID: 214516  Cd Length: 127  Bit Score: 100.44  E-value: 3.04e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19482160      8 EACRAAYNLVRDD--GSAVIWVTFRYDgATIVPGDQG---ADYQHFIQQCTDDVRLFAFVRFTTGDAMSKRSKFALITWI 82
Cdd:smart00102   1 EDCKEAFNELKKKrkHSAIIFKIDKDN-EEIVVEEVGsteDSYDEFVEELPEDECRYALYDYKFTTEESKKSKIVFIFWS 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 19482160     83 GEDVSGLQRAKTGTDKTLVKEVVQNFAKEFVISDRKELEEDFIRSELK 130
Cdd:smart00102  80 PDGAPVKSKMLYASSKDTLKKELGGIQVEVQATDEDDLDEEALKEKLK 127
Cofilin_ADF pfam00241
Cofilin/tropomyosin-type actin-binding protein; Severs actin filaments and binds to actin ...
 10-127 2.64e-25

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


Pssm-ID: 459727  Cd Length: 123  Bit Score: 93.02  E-value: 2.64e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19482160    10 CRAAYNLVRDDGSaVIWVTFRYDGA--TIVP---GDQGADYQHFIQQCTDDVRLFAFVRFT-TGDAMSKRSKFALITWIG 83
Cdd:pfam00241   1 CKEAYQELRSDKK-TNWIIFKIDDDkeEIVVeetGEGGLSYDEFLEELPDDEPRYAVYRFEyTHDDGSKRSKLVFITWCP 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 19482160    84 EDVSGLQRAKTGTDKTLVKEVVQNFAKEFVISDRKELEEDFIRS 127
Cdd:pfam00241  80 DGAPIKRKMLYASSKAALKRELKGIHVEIQATDPSELTEEEILE 123
ADF_drebrin_like cd11281
ADF homology domain of drebrin and actin-binding protein 1 (abp1); Actin depolymerization ...
 11-135 3.61e-12

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: 59.57  E-value: 3.61e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19482160  11 RAAYNLVRDDGSAVIWVTFRYDG--ATIVPGDQGA-DYQHFIQQCTDDVRLFAFVRFTtgDAMSKRSKFALITWIGEDVS 87
Cdd:cd11281  11 LAAYEDVVDGKSSTDWALFTYEGksNDLKVADTGDgGLEELVEEFSDGKVQYGFARVK--DPNSGLPKFVLINWCGEGVP 88

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 19482160  88 GLQRAKTGTDktlVKEvVQNFAKEF--VISDRKE--LEEDFIRSELKKAGGA 135
Cdd:cd11281  89 DARKGSFASH---VAA-VANFLKGAhvQINARSEddLDEDAILKKVSKASGA 136
ADF_cofilin_like cd11286
Cofilin, Destrin, and related actin depolymerizing factors; Actin depolymerization factor ...
 4-129 6.32e-05

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: 40.23  E-value: 6.32e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19482160   4 KIDKEaCRAAYNLVRDdGSAVIWVTFRY--DGATIVP---GDQGADYQHFIQQC-TDDVRLFAF-VRFTTGDAmSKRSKF 76
Cdd:cd11286   4 KVSDE-CITAFNELKL-KKKHKYIIFKIsdDKKEIVVekvGERDASYDDFLEKLpENECRYAVYdFEYETKDG-GKRSKL 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 19482160  77 ALITWIGEDVSglQRAKT--GTDKTLVKEVVQNFAKEFVISDRKELEEDFIRSEL 129
Cdd:cd11286  81 VFISWCPDTAP--IKSKMlyASSKDALKKKLNGIKKEIQATDLSELSEEEILEKL 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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