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Conserved domains on  [gi|21358413|ref|NP_650338|]
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twinfilin [Drosophila melanogaster]

Protein Classification

twinfilin( domain architecture ID 10181682)

twinfilin is an actin-binding protein involved in motile and morphological processes; it inhibits actin polymerization, likely by sequestering G-actin

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ADF_Twf-N_like cd11285
N-terminal ADF domain of twinfilin and related proteins; Actin depolymerization factor ...
 4-142 1.82e-62

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: 195.54  E-value: 1.82e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358413   4 QTGIRANEQLAKVFGKAK-NGKFRVIKVSIENEQLSCGATAETKKDWERDYDKLIGPLLEKDVPCYILYRLDAKiPLGYS 82
Cdd:cd11285   1 QSGITASEELLDAFKSAKsSGSVRAIKITIENEELVPDATIETTGSWEQDFDLLVLPLLEEKEPCYILYRLDSK-SAGYE 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358413  83 WLLISWTPDTASIRQKMVYASTKATLKTEFGSAYITEELHATTLDECTLEGYRRHKQDFA 142
Cdd:cd11285  80 WVFISFVPDSAPVRQKMLYASTRATLKRELGSNHIKDELFATELEELTLEGYEKHLKHEA 139
ADF_Twf-C_like cd11284
C-terminal ADF domain of twinfilin and related proteins; Actin depolymerization factor ...
 176-310 3.74e-47

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: 155.85  E-value: 3.74e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358413 176 GGINCPLSEATVAAVQDLVRGKHDYLQFRIDLEEEQIH-VSRAAKVELADLPKQVPEDHARYHLFLFRHTHEgdyfESYV 254
Cdd:cd11284   1 PGVAFPVSEEAKDALSELASGGVNLVQLSIDLENETIElVSSSSISIPDDLSSLIPSDHPRYHFYRYPHTYL----SSVV 76

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 21358413 255 FVYSMPGYsCSVRERMMYSSCKAPFLDEL-AALGVEVVKKLEIDSGSELTEAFLQDE 310
Cdd:cd11284  77 FIYSCPSG-SKVKERMLYASSKSGLLNHAeDEGKIEIDKKIEIGDPDELTESFLSDE 132
 
Name Accession Description Interval E-value
ADF_Twf-N_like cd11285
N-terminal ADF domain of twinfilin and related proteins; Actin depolymerization factor ...
 4-142 1.82e-62

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: 195.54  E-value: 1.82e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358413   4 QTGIRANEQLAKVFGKAK-NGKFRVIKVSIENEQLSCGATAETKKDWERDYDKLIGPLLEKDVPCYILYRLDAKiPLGYS 82
Cdd:cd11285   1 QSGITASEELLDAFKSAKsSGSVRAIKITIENEELVPDATIETTGSWEQDFDLLVLPLLEEKEPCYILYRLDSK-SAGYE 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358413  83 WLLISWTPDTASIRQKMVYASTKATLKTEFGSAYITEELHATTLDECTLEGYRRHKQDFA 142
Cdd:cd11285  80 WVFISFVPDSAPVRQKMLYASTRATLKRELGSNHIKDELFATELEELTLEGYEKHLKHEA 139
ADF_Twf-C_like cd11284
C-terminal ADF domain of twinfilin and related proteins; Actin depolymerization factor ...
 176-310 3.74e-47

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: 155.85  E-value: 3.74e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358413 176 GGINCPLSEATVAAVQDLVRGKHDYLQFRIDLEEEQIH-VSRAAKVELADLPKQVPEDHARYHLFLFRHTHEgdyfESYV 254
Cdd:cd11284   1 PGVAFPVSEEAKDALSELASGGVNLVQLSIDLENETIElVSSSSISIPDDLSSLIPSDHPRYHFYRYPHTYL----SSVV 76

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 21358413 255 FVYSMPGYsCSVRERMMYSSCKAPFLDEL-AALGVEVVKKLEIDSGSELTEAFLQDE 310
Cdd:cd11284  77 FIYSCPSG-SKVKERMLYASSKSGLLNHAeDEGKIEIDKKIEIGDPDELTESFLSDE 132
ADF smart00102
Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin ...
 184-312 6.26e-23

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


Pssm-ID: 214516  Cd Length: 127  Bit Score: 92.35  E-value: 6.26e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358413    184 EATVAAVQDLVRG-KHDYLQFRIDLEEEQIHVSRAAKVE--LADLPKQVPEDHARYHLFLFRHTHEGDYFESYVFVYSMP 260
Cdd:smart00102   1 EDCKEAFNELKKKrKHSAIIFKIDKDNEEIVVEEVGSTEdsYDEFVEELPEDECRYALYDYKFTTEESKKSKIVFIFWSP 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 21358413    261 GySCSVRERMMYSSCKAPFLDELAALGVEVvkklEIDSGSELTEAFLQDELH 312
Cdd:smart00102  81 D-GAPVKSKMLYASSKDTLKKELGGIQVEV----QATDEDDLDEEALKEKLK 127
Cofilin_ADF pfam00241
Cofilin/tropomyosin-type actin-binding protein; Severs actin filaments and binds to actin ...
 187-309 8.26e-23

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


Pssm-ID: 459727  Cd Length: 123  Bit Score: 91.87  E-value: 8.26e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358413   187 VAAVQDLVRGK-HDYLQFRIDLEEEQIHV--SRAAKVELADLPKQVPEDHARYHLFLFRHTHE-GDYFESYVFVYSMPGy 262
Cdd:pfam00241   2 KEAYQELRSDKkTNWIIFKIDDDKEEIVVeeTGEGGLSYDEFLEELPDDEPRYAVYRFEYTHDdGSKRSKLVFITWCPD- 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 21358413   263 SCSVRERMMYSSCKAPFLDELAALGVEVvkklEIDSGSELTEAFLQD 309
Cdd:pfam00241  81 GAPIKRKMLYASSKAALKRELKGIHVEI----QATDPSELTEEEILE 123
Cofilin_ADF pfam00241
Cofilin/tropomyosin-type actin-binding protein; Severs actin filaments and binds to actin ...
 21-132 1.21e-20

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


Pssm-ID: 459727  Cd Length: 123  Bit Score: 86.09  E-value: 1.21e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358413    21 KNGKFRVIKVSIENEQLSCGATAETKKDwerdYDKLIGpLLEKDVPCYILYRLDAKIPLG---YSWLLISWTPDTASIRQ 97
Cdd:pfam00241  12 KKTNWIIFKIDDDKEEIVVEETGEGGLS----YDEFLE-ELPDDEPRYAVYRFEYTHDDGskrSKLVFITWCPDGAPIKR 86

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 21358413    98 KMVYASTKATLKTEFGSayITEELHATTLDECTLE 132
Cdd:pfam00241  87 KMLYASSKAALKRELKG--IHVEIQATDPSELTEE 119
ADF smart00102
Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin ...
 19-135 4.47e-20

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


Pssm-ID: 214516  Cd Length: 127  Bit Score: 84.64  E-value: 4.47e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358413     19 KAKNGKFRVIKVSIENEQLSCGATAETkkdwERDYDKLIGpLLEKDVPCYILYRLDAKIPLGY--SWLLISWTPDTASIR 96
Cdd:smart00102  12 KKRKHSAIIFKIDKDNEEIVVEEVGST----EDSYDEFVE-ELPEDECRYALYDYKFTTEESKksKIVFIFWSPDGAPVK 86

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 21358413     97 QKMVYASTKATLKTEFGSAYIteELHATTLDECTLEGYR 135
Cdd:smart00102  87 SKMLYASSKDTLKKELGGIQV--EVQATDEDDLDEEALK 123
 
Name Accession Description Interval E-value
ADF_Twf-N_like cd11285
N-terminal ADF domain of twinfilin and related proteins; Actin depolymerization factor ...
 4-142 1.82e-62

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: 195.54  E-value: 1.82e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358413   4 QTGIRANEQLAKVFGKAK-NGKFRVIKVSIENEQLSCGATAETKKDWERDYDKLIGPLLEKDVPCYILYRLDAKiPLGYS 82
Cdd:cd11285   1 QSGITASEELLDAFKSAKsSGSVRAIKITIENEELVPDATIETTGSWEQDFDLLVLPLLEEKEPCYILYRLDSK-SAGYE 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358413  83 WLLISWTPDTASIRQKMVYASTKATLKTEFGSAYITEELHATTLDECTLEGYRRHKQDFA 142
Cdd:cd11285  80 WVFISFVPDSAPVRQKMLYASTRATLKRELGSNHIKDELFATELEELTLEGYEKHLKHEA 139
ADF_Twf-C_like cd11284
C-terminal ADF domain of twinfilin and related proteins; Actin depolymerization factor ...
 176-310 3.74e-47

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: 155.85  E-value: 3.74e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358413 176 GGINCPLSEATVAAVQDLVRGKHDYLQFRIDLEEEQIH-VSRAAKVELADLPKQVPEDHARYHLFLFRHTHEgdyfESYV 254
Cdd:cd11284   1 PGVAFPVSEEAKDALSELASGGVNLVQLSIDLENETIElVSSSSISIPDDLSSLIPSDHPRYHFYRYPHTYL----SSVV 76

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 21358413 255 FVYSMPGYsCSVRERMMYSSCKAPFLDEL-AALGVEVVKKLEIDSGSELTEAFLQDE 310
Cdd:cd11284  77 FIYSCPSG-SKVKERMLYASSKSGLLNHAeDEGKIEIDKKIEIGDPDELTESFLSDE 132
ADF smart00102
Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin ...
 184-312 6.26e-23

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


Pssm-ID: 214516  Cd Length: 127  Bit Score: 92.35  E-value: 6.26e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358413    184 EATVAAVQDLVRG-KHDYLQFRIDLEEEQIHVSRAAKVE--LADLPKQVPEDHARYHLFLFRHTHEGDYFESYVFVYSMP 260
Cdd:smart00102   1 EDCKEAFNELKKKrKHSAIIFKIDKDNEEIVVEEVGSTEdsYDEFVEELPEDECRYALYDYKFTTEESKKSKIVFIFWSP 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 21358413    261 GySCSVRERMMYSSCKAPFLDELAALGVEVvkklEIDSGSELTEAFLQDELH 312
Cdd:smart00102  81 D-GAPVKSKMLYASSKDTLKKELGGIQVEV----QATDEDDLDEEALKEKLK 127
Cofilin_ADF pfam00241
Cofilin/tropomyosin-type actin-binding protein; Severs actin filaments and binds to actin ...
 187-309 8.26e-23

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


Pssm-ID: 459727  Cd Length: 123  Bit Score: 91.87  E-value: 8.26e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358413   187 VAAVQDLVRGK-HDYLQFRIDLEEEQIHV--SRAAKVELADLPKQVPEDHARYHLFLFRHTHE-GDYFESYVFVYSMPGy 262
Cdd:pfam00241   2 KEAYQELRSDKkTNWIIFKIDDDKEEIVVeeTGEGGLSYDEFLEELPDDEPRYAVYRFEYTHDdGSKRSKLVFITWCPD- 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 21358413   263 SCSVRERMMYSSCKAPFLDELAALGVEVvkklEIDSGSELTEAFLQD 309
Cdd:pfam00241  81 GAPIKRKMLYASSKAALKRELKGIHVEI----QATDPSELTEEEILE 123
Cofilin_ADF pfam00241
Cofilin/tropomyosin-type actin-binding protein; Severs actin filaments and binds to actin ...
 21-132 1.21e-20

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


Pssm-ID: 459727  Cd Length: 123  Bit Score: 86.09  E-value: 1.21e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358413    21 KNGKFRVIKVSIENEQLSCGATAETKKDwerdYDKLIGpLLEKDVPCYILYRLDAKIPLG---YSWLLISWTPDTASIRQ 97
Cdd:pfam00241  12 KKTNWIIFKIDDDKEEIVVEETGEGGLS----YDEFLE-ELPDDEPRYAVYRFEYTHDDGskrSKLVFITWCPDGAPIKR 86

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 21358413    98 KMVYASTKATLKTEFGSayITEELHATTLDECTLE 132
Cdd:pfam00241  87 KMLYASSKAALKRELKG--IHVEIQATDPSELTEE 119
ADF smart00102
Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin ...
 19-135 4.47e-20

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


Pssm-ID: 214516  Cd Length: 127  Bit Score: 84.64  E-value: 4.47e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358413     19 KAKNGKFRVIKVSIENEQLSCGATAETkkdwERDYDKLIGpLLEKDVPCYILYRLDAKIPLGY--SWLLISWTPDTASIR 96
Cdd:smart00102  12 KKRKHSAIIFKIDKDNEEIVVEEVGST----EDSYDEFVE-ELPEDECRYALYDYKFTTEESKksKIVFIFWSPDGAPVK 86

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 21358413     97 QKMVYASTKATLKTEFGSAYIteELHATTLDECTLEGYR 135
Cdd:smart00102  87 SKMLYASSKDTLKKELGGIQV--EVQATDEDDLDEEALK 123
ADF_gelsolin cd00013
Actin depolymerization factor/cofilin- and gelsolin-like domains; Actin depolymerization ...
 199-291 7.74e-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: 74.81  E-value: 7.74e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358413 199 DYLQFRIDLEEEQIHVSRAAKVELADLPKQVPEDHARYHLFLFRHTHEGDYFESYVFVYSMPGYsCSVRERMMYSSCKAP 278
Cdd:cd00013   1 DWVLFKVDAKKEEIVVGSTGAGFLDEFLEELPEDDPRYAFYRFKYPHSDDKRSKFVFISWIPDG-VSIKQKMVYATNKQT 79

                        90
                ....*....|...
gi 21358413 279 FLDELAALGVEVV 291
Cdd:cd00013  80 LKEALFGLAVPVQ 92
ADF_cofilin_like cd11286
Cofilin, Destrin, and related actin depolymerizing factors; Actin depolymerization factor ...
 5-132 1.35e-15

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: 72.59  E-value: 1.35e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358413   5 TGIRANEQLAKVFGKAKNG---KFRVIKVSIENEQLscgaTAETKKDWERDYDKLIGPLLEKDvPCYILYRLDAKIPLGy 81
Cdd:cd11286   1 SGVKVSDECITAFNELKLKkkhKYIIFKISDDKKEI----VVEKVGERDASYDDFLEKLPENE-CRYAVYDFEYETKDG- 74

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 21358413  82 SWL----LISWTPDTASIRQKMVYASTKATLKTEFGSAYIteELHATTLDECTLE 132
Cdd:cd11286  75 GKRsklvFISWCPDTAPIKSKMLYASSKDALKKKLNGIKK--EIQATDLSELSEE 127
ADF_gelsolin cd00013
Actin depolymerization factor/cofilin- and gelsolin-like domains; Actin depolymerization ...
 24-127 3.43e-15

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: 70.19  E-value: 3.43e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358413  24 KFRVIKVSIENEQLSCGATAETkkdweRDYDKLigPLLEKDVPCYILYRLDA--KIPLGYSWLLISWTPDTASIRQKMVY 101
Cdd:cd00013   1 DWVLFKVDAKKEEIVVGSTGAG-----FLDEFL--EELPEDDPRYAFYRFKYphSDDKRSKFVFISWIPDGVSIKQKMVY 73

                        90       100
                ....*....|....*....|....*.
gi 21358413 102 ASTKATLKTEFGSayITEELHATTLD 127
Cdd:cd00013  74 ATNKQTLKEALFG--LAVPVQIRDGD 97
ADF_GMF-beta_like cd11283
ADF-homology domain of glia maturation factor beta and related proteins; Actin ...
 201-303 2.63e-07

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: 48.77  E-value: 2.63e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358413 201 LQFRIDLEEEQIhvsraakvELADLPKQVPEDHARYHLFLFRHTHeGDYFESY--VFVYSMPGySCSVRERMMYSSCKAP 278
Cdd:cd11283  33 QEIVVDEELEDI--------SIEELAEELPEHSPRFVLYSYKMKH-DDGRISYplVLIYWSPQ-GCSPELQMLYAGAKEL 102

                        90       100
                ....*....|....*....|....*
gi 21358413 279 FLDELaalgvEVVKKLEIDSGSELT 303
Cdd:cd11283 103 LVKEA-----EVTKVFEIRDGEELT 122
ADF_cofilin_like cd11286
Cofilin, Destrin, and related actin depolymerizing factors; Actin depolymerization factor ...
 182-311 8.61e-06

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: 44.86  E-value: 8.61e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358413 182 LSEATVAAVQDL-VRGKHDYLQFRIDLEEEQIHVSRAAKVELA--DLPKQVPEDHARYHLFLFRHTHEGDYFES-YVFVY 257
Cdd:cd11286   5 VSDECITAFNELkLKKKHKYIIFKISDDKKEIVVEKVGERDASydDFLEKLPENECRYAVYDFEYETKDGGKRSkLVFIS 84

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 21358413 258 SMPGySCSVRERMMYSSCKAPFLDELaalgVEVVKKLEIDSGSELTEAFLQDEL 311
Cdd:cd11286  85 WCPD-TAPIKSKMLYASSKDALKKKL----NGIKKEIQATDLSELSEEEILEKL 133
ADF_Twf-C_like cd11284
C-terminal ADF domain of twinfilin and related proteins; Actin depolymerization factor ...
 19-108 1.45e-03

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: 38.37  E-value: 1.45e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358413  19 KAKNGKFRVIKVSIENEQLSCGATAETkkdwerDYDKLIGPLLEKDVPCYILYRLD----AKIPLGYSwlliswTPDTAS 94
Cdd:cd11284  19 ASGGVNLVQLSIDLENETIELVSSSSI------SIPDDLSSLIPSDHPRYHFYRYPhtylSSVVFIYS------CPSGSK 86

                        90
                ....*....|....
gi 21358413  95 IRQKMVYASTKATL 108
Cdd:cd11284  87 VKERMLYASSKSGL 100
ADF_GMF-beta_like cd11283
ADF-homology domain of glia maturation factor beta and related proteins; Actin ...
 81-119 7.76e-03

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: 36.06  E-value: 7.76e-03
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 21358413  81 YSWLLISWTPDTASIRQKMVYASTKATLKTEFGSAYITE 119
Cdd:cd11283  76 YPLVLIYWSPQGCSPELQMLYAGAKELLVKEAEVTKVFE 114
 
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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