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Conserved domains on  [gi|13111977|gb|AAH03161|]
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Twinfilin, actin-binding protein, homolog 2 (Drosophila) [Homo sapiens]

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 2.18e-64

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: 200.55  E-value: 2.18e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13111977   4 QTGIHATEELKEFFAKAR-AGSVRLIKVVIEDEQLVLGASQEPVGRWDQDYDRAVLPLLDAQQPCYLLYRLDSQNaQGFE 82
Cdd:cd11285   1 QSGITASEELLDAFKSAKsSGSVRAIKITIENEELVPDATIETTGSWEQDFDLLVLPLLEEKEPCYILYRLDSKS-AGYE 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 13111977  83 WLFLAWSPDNSPVRLKMLYAATRATVKKEFGGGHIKDELFGTVKDDLSFAGYQKHLSSCA 142
Cdd:cd11285  80 WVFISFVPDSAPVRQKMLYASTRATLKRELGSNHIKDELFATELEELTLEGYEKHLKHEA 139
ADF_Twf-C_like cd11284
C-terminal ADF domain of twinfilin and related proteins; Actin depolymerization factor ...
 176-311 3.60e-61

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: 192.06  E-value: 3.60e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13111977 176 QGLAFPLQPEAQRALQQLKQKMVNYIQMKLDLERETIELVHTEPTDV-AQLPSRVPRDAARYHFFLYKHThegdPLESVV 254
Cdd:cd11284   1 PGVAFPVSEEAKDALSELASGGVNLVQLSIDLENETIELVSSSSISIpDDLSSLIPSDHPRYHFYRYPHT----YLSSVV 76

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 13111977 255 FIYSMPGYkCSIKERMLYSSCKSRLLDSVEQDFHLEIAKKIEIGDGAELTAEFLYDE 311
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 2.18e-64

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: 200.55  E-value: 2.18e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13111977   4 QTGIHATEELKEFFAKAR-AGSVRLIKVVIEDEQLVLGASQEPVGRWDQDYDRAVLPLLDAQQPCYLLYRLDSQNaQGFE 82
Cdd:cd11285   1 QSGITASEELLDAFKSAKsSGSVRAIKITIENEELVPDATIETTGSWEQDFDLLVLPLLEEKEPCYILYRLDSKS-AGYE 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 13111977  83 WLFLAWSPDNSPVRLKMLYAATRATVKKEFGGGHIKDELFGTVKDDLSFAGYQKHLSSCA 142
Cdd:cd11285  80 WVFISFVPDSAPVRQKMLYASTRATLKRELGSNHIKDELFATELEELTLEGYEKHLKHEA 139
ADF_Twf-C_like cd11284
C-terminal ADF domain of twinfilin and related proteins; Actin depolymerization factor ...
 176-311 3.60e-61

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: 192.06  E-value: 3.60e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13111977 176 QGLAFPLQPEAQRALQQLKQKMVNYIQMKLDLERETIELVHTEPTDV-AQLPSRVPRDAARYHFFLYKHThegdPLESVV 254
Cdd:cd11284   1 PGVAFPVSEEAKDALSELASGGVNLVQLSIDLENETIELVSSSSISIpDDLSSLIPSDHPRYHFYRYPHT----YLSSVV 76

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 13111977 255 FIYSMPGYkCSIKERMLYSSCKSRLLDSVEQDFHLEIAKKIEIGDGAELTAEFLYDE 311
Cdd:cd11284  77 FIYSCPSG-SKVKERMLYASSKSGLLNHAEDEGKIEIDKKIEIGDPDELTESFLSDE 132
ADF smart00102
Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin ...
 185-313 6.76e-24

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


Pssm-ID: 214516  Cd Length: 127  Bit Score: 95.04  E-value: 6.76e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13111977    185 EAQRALQQLKQKmvNYIQMKLDLERETIELVHTEPT--DVAQLPSRVPRDAARYHFFLYKHTHEGDPLESVVFIYSMPGy 262
Cdd:smart00102   5 EAFNELKKKRKH--SAIIFKIDKDNEEIVVEEVGSTedSYDEFVEELPEDECRYALYDYKFTTEESKKSKIVFIFWSPD- 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 13111977    263 KCSIKERMLYSSCKSRLLDSVEQdfhleIAKKIEIGDGAELTAEFLYDEVH 313
Cdd:smart00102  82 GAPVKSKMLYASSKDTLKKELGG-----IQVEVQATDEDDLDEEALKEKLK 127
ADF smart00102
Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin ...
 11-130 1.03e-21

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


Pssm-ID: 214516  Cd Length: 127  Bit Score: 89.27  E-value: 1.03e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13111977     11 EELKEFFAKARAG---SVRLIKVVIEDEQLVLGASQEPVGRWDQDYDRavlplLDAQQPCYLLYRLDSQ--NAQGFEWLF 85
Cdd:smart00102   1 EDCKEAFNELKKKrkhSAIIFKIDKDNEEIVVEEVGSTEDSYDEFVEE-----LPEDECRYALYDYKFTteESKKSKIVF 75

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 13111977     86 LAWSPDNSPVRLKMLYAATRATVKKEFGGGHIKDElfGTVKDDLS 130
Cdd:smart00102  76 IFWSPDGAPVKSKMLYASSKDTLKKELGGIQVEVQ--ATDEDDLD 118
Cofilin_ADF pfam00241
Cofilin/tropomyosin-type actin-binding protein; Severs actin filaments and binds to actin ...
 186-310 5.29e-21

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


Pssm-ID: 459727  Cd Length: 123  Bit Score: 86.86  E-value: 5.29e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13111977   186 AQRALQQLKQ-KMVNYIQMKLDLERETIELVHT--EPTDVAQLPSRVPRDAARYHFFLYKHTHE-GDPLESVVFIYSMPG 261
Cdd:pfam00241   1 CKEAYQELRSdKKTNWIIFKIDDDKEEIVVEETgeGGLSYDEFLEELPDDEPRYAVYRFEYTHDdGSKRSKLVFITWCPD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 13111977   262 yKCSIKERMLYSSCKSRLLDSVeQDFHLEiakkIEIGDGAELTAEFLYD 310
Cdd:pfam00241  81 -GAPIKRKMLYASSKAALKREL-KGIHVE----IQATDPSELTEEEILE 123
Cofilin_ADF pfam00241
Cofilin/tropomyosin-type actin-binding protein; Severs actin filaments and binds to actin ...
 27-131 1.26e-17

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


Pssm-ID: 459727  Cd Length: 123  Bit Score: 78.00  E-value: 1.26e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13111977    27 LIKVVIEDEQLVLgasqEPVGRWDQDYDrAVLPLLDAQQPCYLLYRLDSQNAQG---FEWLFLAWSPDNSPVRLKMLYAA 103
Cdd:pfam00241  18 IFKIDDDKEEIVV----EETGEGGLSYD-EFLEELPDDEPRYAVYRFEYTHDDGskrSKLVFITWCPDGAPIKRKMLYAS 92

                          90       100
                  ....*....|....*....|....*...
gi 13111977   104 TRATVKKEFGGGHIkdELFGTVKDDLSF 131
Cdd:pfam00241  93 SKAALKRELKGIHV--EIQATDPSELTE 118
PLN03216 PLN03216
actin depolymerizing factor; Provisional
 5-116 2.96e-05

actin depolymerizing factor; Provisional


Pssm-ID: 178755  Cd Length: 141  Bit Score: 43.38  E-value: 2.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13111977    5 TGIHATEELKEFFAKARAGSV-RLIKVVIEDEQLVLgaSQEPVGRWDQDYDR--AVLPLLDAQqpcYLLYRLD---SQNA 78
Cdd:PLN03216   8 TGMWVTDECKNSFMEMKWKKVhRYIVFKIDEKSRKV--TVDKVGGPGESYDDlaASLPTDDCR---YAVFDFDfvtVDNC 82

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 13111977   79 QGFEWLFLAWSPDNSPVRLKMLYAATRATVKKEFGGGH 116
Cdd:PLN03216  83 RKSKIFFIAWSPEASRIRAKMLYATSKDGLRRVLDGVH 120
 
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 2.18e-64

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: 200.55  E-value: 2.18e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13111977   4 QTGIHATEELKEFFAKAR-AGSVRLIKVVIEDEQLVLGASQEPVGRWDQDYDRAVLPLLDAQQPCYLLYRLDSQNaQGFE 82
Cdd:cd11285   1 QSGITASEELLDAFKSAKsSGSVRAIKITIENEELVPDATIETTGSWEQDFDLLVLPLLEEKEPCYILYRLDSKS-AGYE 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 13111977  83 WLFLAWSPDNSPVRLKMLYAATRATVKKEFGGGHIKDELFGTVKDDLSFAGYQKHLSSCA 142
Cdd:cd11285  80 WVFISFVPDSAPVRQKMLYASTRATLKRELGSNHIKDELFATELEELTLEGYEKHLKHEA 139
ADF_Twf-C_like cd11284
C-terminal ADF domain of twinfilin and related proteins; Actin depolymerization factor ...
 176-311 3.60e-61

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: 192.06  E-value: 3.60e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13111977 176 QGLAFPLQPEAQRALQQLKQKMVNYIQMKLDLERETIELVHTEPTDV-AQLPSRVPRDAARYHFFLYKHThegdPLESVV 254
Cdd:cd11284   1 PGVAFPVSEEAKDALSELASGGVNLVQLSIDLENETIELVSSSSISIpDDLSSLIPSDHPRYHFYRYPHT----YLSSVV 76

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 13111977 255 FIYSMPGYkCSIKERMLYSSCKSRLLDSVEQDFHLEIAKKIEIGDGAELTAEFLYDE 311
Cdd:cd11284  77 FIYSCPSG-SKVKERMLYASSKSGLLNHAEDEGKIEIDKKIEIGDPDELTESFLSDE 132
ADF smart00102
Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin ...
 185-313 6.76e-24

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


Pssm-ID: 214516  Cd Length: 127  Bit Score: 95.04  E-value: 6.76e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13111977    185 EAQRALQQLKQKmvNYIQMKLDLERETIELVHTEPT--DVAQLPSRVPRDAARYHFFLYKHTHEGDPLESVVFIYSMPGy 262
Cdd:smart00102   5 EAFNELKKKRKH--SAIIFKIDKDNEEIVVEEVGSTedSYDEFVEELPEDECRYALYDYKFTTEESKKSKIVFIFWSPD- 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 13111977    263 KCSIKERMLYSSCKSRLLDSVEQdfhleIAKKIEIGDGAELTAEFLYDEVH 313
Cdd:smart00102  82 GAPVKSKMLYASSKDTLKKELGG-----IQVEVQATDEDDLDEEALKEKLK 127
ADF smart00102
Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin ...
 11-130 1.03e-21

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


Pssm-ID: 214516  Cd Length: 127  Bit Score: 89.27  E-value: 1.03e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13111977     11 EELKEFFAKARAG---SVRLIKVVIEDEQLVLGASQEPVGRWDQDYDRavlplLDAQQPCYLLYRLDSQ--NAQGFEWLF 85
Cdd:smart00102   1 EDCKEAFNELKKKrkhSAIIFKIDKDNEEIVVEEVGSTEDSYDEFVEE-----LPEDECRYALYDYKFTteESKKSKIVF 75

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 13111977     86 LAWSPDNSPVRLKMLYAATRATVKKEFGGGHIKDElfGTVKDDLS 130
Cdd:smart00102  76 IFWSPDGAPVKSKMLYASSKDTLKKELGGIQVEVQ--ATDEDDLD 118
Cofilin_ADF pfam00241
Cofilin/tropomyosin-type actin-binding protein; Severs actin filaments and binds to actin ...
 186-310 5.29e-21

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


Pssm-ID: 459727  Cd Length: 123  Bit Score: 86.86  E-value: 5.29e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13111977   186 AQRALQQLKQ-KMVNYIQMKLDLERETIELVHT--EPTDVAQLPSRVPRDAARYHFFLYKHTHE-GDPLESVVFIYSMPG 261
Cdd:pfam00241   1 CKEAYQELRSdKKTNWIIFKIDDDKEEIVVEETgeGGLSYDEFLEELPDDEPRYAVYRFEYTHDdGSKRSKLVFITWCPD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 13111977   262 yKCSIKERMLYSSCKSRLLDSVeQDFHLEiakkIEIGDGAELTAEFLYD 310
Cdd:pfam00241  81 -GAPIKRKMLYASSKAALKREL-KGIHVE----IQATDPSELTEEEILE 123
ADF_gelsolin cd00013
Actin depolymerization factor/cofilin- and gelsolin-like domains; Actin depolymerization ...
 199-300 9.35e-20

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: 82.90  E-value: 9.35e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13111977 199 NYIQMKLDLERETIELVHTEPTDVAQLPSRVPRDAARYHFFLYKHTHEGDPLESVVFIYSMPGYkCSIKERMLYSSCKSR 278
Cdd:cd00013   1 DWVLFKVDAKKEEIVVGSTGAGFLDEFLEELPEDDPRYAFYRFKYPHSDDKRSKFVFISWIPDG-VSIKQKMVYATNKQT 79

                        90       100
                ....*....|....*....|..
gi 13111977 279 LLDSVEqdfhlEIAKKIEIGDG 300
Cdd:cd00013  80 LKEALF-----GLAVPVQIRDG 96
ADF_gelsolin cd00013
Actin depolymerization factor/cofilin- and gelsolin-like domains; Actin depolymerization ...
 26-127 1.46e-18

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: 79.43  E-value: 1.46e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13111977  26 RLIKVVIEDEQLVLGASQEPvgrwdqdYDRAVLPLLDAQQPCYLLYRLDSQNAQGF--EWLFLAWSPDNSPVRLKMLYAA 103
Cdd:cd00013   3 VLFKVDAKKEEIVVGSTGAG-------FLDEFLEELPEDDPRYAFYRFKYPHSDDKrsKFVFISWIPDGVSIKQKMVYAT 75

                        90       100
                ....*....|....*....|....
gi 13111977 104 TRATVKKEFggGHIKDELFGTVKD 127
Cdd:cd00013  76 NKQTLKEAL--FGLAVPVQIRDGD 97
Cofilin_ADF pfam00241
Cofilin/tropomyosin-type actin-binding protein; Severs actin filaments and binds to actin ...
 27-131 1.26e-17

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


Pssm-ID: 459727  Cd Length: 123  Bit Score: 78.00  E-value: 1.26e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13111977    27 LIKVVIEDEQLVLgasqEPVGRWDQDYDrAVLPLLDAQQPCYLLYRLDSQNAQG---FEWLFLAWSPDNSPVRLKMLYAA 103
Cdd:pfam00241  18 IFKIDDDKEEIVV----EETGEGGLSYD-EFLEELPDDEPRYAVYRFEYTHDDGskrSKLVFITWCPDGAPIKRKMLYAS 92

                          90       100
                  ....*....|....*....|....*...
gi 13111977   104 TRATVKKEFGGGHIkdELFGTVKDDLSF 131
Cdd:pfam00241  93 SKAALKRELKGIHV--EIQATDPSELTE 118
ADF_cofilin_like cd11286
Cofilin, Destrin, and related actin depolymerizing factors; Actin depolymerization factor ...
 5-132 1.64e-14

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: 69.51  E-value: 1.64e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13111977   5 TGIHATEELKEFFAKARAGSV-RLI--KVVIEDEQLVLgasqEPVGRWDQDYDRaVLPLLDAQQPCYLLYRLDSQNAQGF 81
Cdd:cd11286   1 SGVKVSDECITAFNELKLKKKhKYIifKISDDKKEIVV----EKVGERDASYDD-FLEKLPENECRYAVYDFEYETKDGG 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 13111977  82 ---EWLFLAWSPDNSPVRLKMLYAATRATVKKEFGGGHIkdELFGTVKDDLSFA 132
Cdd:cd11286  76 krsKLVFISWCPDTAPIKSKMLYASSKDALKKKLNGIKK--EIQATDLSELSEE 127
ADF_GMF-beta_like cd11283
ADF-homology domain of glia maturation factor beta and related proteins; Actin ...
 184-304 1.63e-08

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: 52.24  E-value: 1.63e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13111977 184 PEAQRALQQL---KQKMVNYIQMKLDLERETI----ELVHTEPTDVAQ-LPSRVPRdaarYHFFLYKHTHeGD-----PL 250
Cdd:cd11283   4 DEVKEALKKFrfrKSKANAALILKIDKEKQEIvvdeELEDISIEELAEeLPEHSPR----FVLYSYKMKH-DDgrisyPL 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 13111977 251 esvVFIYSMPGyKCSIKERMLYSSCKSRLLDSveqdfhLEIAKKIEIGDGAELT 304
Cdd:cd11283  79 ---VLIYWSPQ-GCSPELQMLYAGAKELLVKE------AEVTKVFEIRDGEELT 122
ADF_cofilin_like cd11286
Cofilin, Destrin, and related actin depolymerizing factors; Actin depolymerization factor ...
 184-306 1.47e-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: 46.78  E-value: 1.47e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13111977 184 PEAQRALQQLK-QKMVNYIQMKLDLERETIELVHTEPTDVA--QLPSRVPRDAARYHFFLYKHTHEGD-PLESVVFIYSM 259
Cdd:cd11286   7 DECITAFNELKlKKKHKYIIFKISDDKKEIVVEKVGERDASydDFLEKLPENECRYAVYDFEYETKDGgKRSKLVFISWC 86

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 13111977 260 PGyKCSIKERMLYSSCKSRLLDSVEQdfhleIAKKIEIGDGAELTAE 306
Cdd:cd11286  87 PD-TAPIKSKMLYASSKDALKKKLNG-----IKKEIQATDLSELSEE 127
PLN03216 PLN03216
actin depolymerizing factor; Provisional
 5-116 2.96e-05

actin depolymerizing factor; Provisional


Pssm-ID: 178755  Cd Length: 141  Bit Score: 43.38  E-value: 2.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13111977    5 TGIHATEELKEFFAKARAGSV-RLIKVVIEDEQLVLgaSQEPVGRWDQDYDR--AVLPLLDAQqpcYLLYRLD---SQNA 78
Cdd:PLN03216   8 TGMWVTDECKNSFMEMKWKKVhRYIVFKIDEKSRKV--TVDKVGGPGESYDDlaASLPTDDCR---YAVFDFDfvtVDNC 82

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 13111977   79 QGFEWLFLAWSPDNSPVRLKMLYAATRATVKKEFGGGH 116
Cdd:PLN03216  83 RKSKIFFIAWSPEASRIRAKMLYATSKDGLRRVLDGVH 120
ADF_Twf-C_like cd11284
C-terminal ADF domain of twinfilin and related proteins; Actin depolymerization factor ...
 9-113 3.53e-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: 37.21  E-value: 3.53e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13111977   9 ATEELKEFfakaRAGSVRLI--KVVIEDEQLVLGASQE-PVGRWDQDydravlpLLDAQQPCYLLYRLDSQNAQGFewLF 85
Cdd:cd11284  11 AKDALSEL----ASGGVNLVqlSIDLENETIELVSSSSiSIPDDLSS-------LIPSDHPRYHFYRYPHTYLSSV--VF 77

                        90       100       110
                ....*....|....*....|....*....|..
gi 13111977  86 LAWSPDNSPVRLKMLYAATRA----TVKKEFG 113
Cdd:cd11284  78 IYSCPSGSKVKERMLYASSKSgllnHAEDEGK 109
 
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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