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Conserved domains on  [gi|334848198|ref|NP_001229326|]
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twinfilin-1 isoform 1 [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 1.74e-66

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: 206.33  E-value: 1.74e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334848198   4 QTGIQASEDVKEIFARAR-NGKYRLLKISIENEQLVIGSYSQPSDSWDKDYDSFVLPLLEDKQPCYILFRLDSQNaQGYE 82
Cdd:cd11285    1 QSGITASEELLDAFKSAKsSGSVRAIKITIENEELVPDATIETTGSWEQDFDLLVLPLLEEKEPCYILYRLDSKS-AGYE 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 334848198  83 WIFIAWSPDHSHVRQKMLYAATRATLKKEFGGGHIKDEVFGTVKEDVSLHGYKKYLLSQS 142
Cdd:cd11285   80 WVFISFVPDSAPVRQKMLYASTRATLKRELGSNHIKDELFATELEELTLEGYEKHLKHEA 139
ADF_Twf-C_like cd11284
C-terminal ADF domain of twinfilin and related proteins; Actin depolymerization factor ...
 183-318 4.03e-57

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: 182.05  E-value: 4.03e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334848198 183 QGVAFPISREAFQALEKLNNRQLNYVQLEIDIKNEIIILANTTNT-ELKDLPKRIPKDSARYHFFLYKHshegDYLESIV 261
Cdd:cd11284    1 PGVAFPVSEEAKDALSELASGGVNLVQLSIDLENETIELVSSSSIsIPDDLSSLIPSDHPRYHFYRYPH----TYLSSVV 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 334848198 262 FIYSMPGYtCSIRERMLYSSCKSRLLEIVERQLQMDVIRKIEIDNGDELTADFLYEE 318
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 1.74e-66

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: 206.33  E-value: 1.74e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334848198   4 QTGIQASEDVKEIFARAR-NGKYRLLKISIENEQLVIGSYSQPSDSWDKDYDSFVLPLLEDKQPCYILFRLDSQNaQGYE 82
Cdd:cd11285    1 QSGITASEELLDAFKSAKsSGSVRAIKITIENEELVPDATIETTGSWEQDFDLLVLPLLEEKEPCYILYRLDSKS-AGYE 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 334848198  83 WIFIAWSPDHSHVRQKMLYAATRATLKKEFGGGHIKDEVFGTVKEDVSLHGYKKYLLSQS 142
Cdd:cd11285   80 WVFISFVPDSAPVRQKMLYASTRATLKRELGSNHIKDELFATELEELTLEGYEKHLKHEA 139
ADF_Twf-C_like cd11284
C-terminal ADF domain of twinfilin and related proteins; Actin depolymerization factor ...
 183-318 4.03e-57

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: 182.05  E-value: 4.03e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334848198 183 QGVAFPISREAFQALEKLNNRQLNYVQLEIDIKNEIIILANTTNT-ELKDLPKRIPKDSARYHFFLYKHshegDYLESIV 261
Cdd:cd11284    1 PGVAFPVSEEAKDALSELASGGVNLVQLSIDLENETIELVSSSSIsIPDDLSSLIPSDHPRYHFYRYPH----TYLSSVV 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 334848198 262 FIYSMPGYtCSIRERMLYSSCKSRLLEIVERQLQMDVIRKIEIDNGDELTADFLYEE 318
Cdd:cd11284   77 FIYSCPSG-SKVKERMLYASSKSGLLNHAEDEGKIEIDKKIEIGDPDELTESFLSDE 132
ADF smart00102
Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin ...
 188-320 3.01e-34

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


Pssm-ID: 214516  Cd Length: 127  Bit Score: 122.39  E-value: 3.01e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334848198   188 PISREAFQALEKlnNRQLNYVQLEIDIKNEIIILANTTNTE--LKDLPKRIPKDSARYHFFLYKHSHEGDYLESIVFIYS 265
Cdd:smart00102   1 EDCKEAFNELKK--KRKHSAIIFKIDKDNEEIVVEEVGSTEdsYDEFVEELPEDECRYALYDYKFTTEESKKSKIVFIFW 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 334848198   266 MPGyTCSIRERMLYSSCKSRLLEIVErQLQMDVirkiEIDNGDELTADFLYEEVH 320
Cdd:smart00102  79 SPD-GAPVKSKMLYASSKDTLKKELG-GIQVEV----QATDEDDLDEEALKEKLK 127
ADF smart00102
Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin ...
 11-138 7.70e-32

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


Pssm-ID: 214516  Cd Length: 127  Bit Score: 116.23  E-value: 7.70e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334848198    11 EDVKEIFARARNGK---YRLLKISIENEQLVIGSYSQPSDSWDKDYDSfvlplLEDKQPCYILFRLDSQ--NAQGYEWIF 85
Cdd:smart00102   1 EDCKEAFNELKKKRkhsAIIFKIDKDNEEIVVEEVGSTEDSYDEFVEE-----LPEDECRYALYDYKFTteESKKSKIVF 75

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 334848198    86 IAWSPDHSHVRQKMLYAATRATLKKEFGGGHIKDEVfgTVKEDVSLHGYKKYL 138
Cdd:smart00102  76 IFWSPDGAPVKSKMLYASSKDTLKKELGGIQVEVQA--TDEDDLDEEALKEKL 126
Cofilin_ADF pfam00241
Cofilin/tropomyosin-type actin-binding protein; Severs actin filaments and binds to actin ...
 13-130 2.47e-22

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


Pssm-ID: 459727  Cd Length: 123  Bit Score: 90.71  E-value: 2.47e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334848198   13 VKEIFARARNGK---YRLLKISIENEQLVIGSysqpSDSWDKDYDSFVlPLLEDKQPCYILFRLDSQNAQG---YEWIFI 86
Cdd:pfam00241   1 CKEAYQELRSDKktnWIIFKIDDDKEEIVVEE----TGEGGLSYDEFL-EELPDDEPRYAVYRFEYTHDDGskrSKLVFI 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 334848198   87 AWSPDHSHVRQKMLYAATRATLKKEFGGGHIkdEVFGTVKEDVS 130
Cdd:pfam00241  76 TWCPDGAPIKRKMLYASSKAALKRELKGIHV--EIQATDPSELT 117
Cofilin_ADF pfam00241
Cofilin/tropomyosin-type actin-binding protein; Severs actin filaments and binds to actin ...
 191-317 5.59e-20

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


Pssm-ID: 459727  Cd Length: 123  Bit Score: 84.55  E-value: 5.59e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334848198  191 REAFQALekLNNRQLNYVQLEIDIKNEIIILANTTNTELK--DLPKRIPKDSARYHFFLYKHSHE-GDYLESIVFIYSMP 267
Cdd:pfam00241   2 KEAYQEL--RSDKKTNWIIFKIDDDKEEIVVEETGEGGLSydEFLEELPDDEPRYAVYRFEYTHDdGSKRSKLVFITWCP 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 334848198  268 GyTCSIRERMLYSSCKSRLLeiveRQLQmDVIRKIEIDNGDELTADFLYE 317
Cdd:pfam00241  80 D-GAPIKRKMLYASSKAALK----RELK-GIHVEIQATDPSELTEEEILE 123
PLN03216 PLN03216
actin depolymerizing factor; Provisional
 5-116 6.74e-07

actin depolymerizing factor; Provisional


Pssm-ID: 178755  Cd Length: 141  Bit Score: 48.00  E-value: 6.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334848198   5 TGIQASEDVKEIFARARNGK---YRLLKISIENEQLVIGSYSQPSDSwdkdYDSFVLPLLEDKqpC-YILFRLD---SQN 77
Cdd:PLN03216   8 TGMWVTDECKNSFMEMKWKKvhrYIVFKIDEKSRKVTVDKVGGPGES----YDDLAASLPTDD--CrYAVFDFDfvtVDN 81

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 334848198  78 AQGYEWIFIAWSPDHSHVRQKMLYAATRATLKKEFGGGH 116
Cdd:PLN03216  82 CRKSKIFFIAWSPEASRIRAKMLYATSKDGLRRVLDGVH 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 1.74e-66

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: 206.33  E-value: 1.74e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334848198   4 QTGIQASEDVKEIFARAR-NGKYRLLKISIENEQLVIGSYSQPSDSWDKDYDSFVLPLLEDKQPCYILFRLDSQNaQGYE 82
Cdd:cd11285    1 QSGITASEELLDAFKSAKsSGSVRAIKITIENEELVPDATIETTGSWEQDFDLLVLPLLEEKEPCYILYRLDSKS-AGYE 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 334848198  83 WIFIAWSPDHSHVRQKMLYAATRATLKKEFGGGHIKDEVFGTVKEDVSLHGYKKYLLSQS 142
Cdd:cd11285   80 WVFISFVPDSAPVRQKMLYASTRATLKRELGSNHIKDELFATELEELTLEGYEKHLKHEA 139
ADF_Twf-C_like cd11284
C-terminal ADF domain of twinfilin and related proteins; Actin depolymerization factor ...
 183-318 4.03e-57

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: 182.05  E-value: 4.03e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334848198 183 QGVAFPISREAFQALEKLNNRQLNYVQLEIDIKNEIIILANTTNT-ELKDLPKRIPKDSARYHFFLYKHshegDYLESIV 261
Cdd:cd11284    1 PGVAFPVSEEAKDALSELASGGVNLVQLSIDLENETIELVSSSSIsIPDDLSSLIPSDHPRYHFYRYPH----TYLSSVV 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 334848198 262 FIYSMPGYtCSIRERMLYSSCKSRLLEIVERQLQMDVIRKIEIDNGDELTADFLYEE 318
Cdd:cd11284   77 FIYSCPSG-SKVKERMLYASSKSGLLNHAEDEGKIEIDKKIEIGDPDELTESFLSDE 132
ADF smart00102
Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin ...
 188-320 3.01e-34

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


Pssm-ID: 214516  Cd Length: 127  Bit Score: 122.39  E-value: 3.01e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334848198   188 PISREAFQALEKlnNRQLNYVQLEIDIKNEIIILANTTNTE--LKDLPKRIPKDSARYHFFLYKHSHEGDYLESIVFIYS 265
Cdd:smart00102   1 EDCKEAFNELKK--KRKHSAIIFKIDKDNEEIVVEEVGSTEdsYDEFVEELPEDECRYALYDYKFTTEESKKSKIVFIFW 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 334848198   266 MPGyTCSIRERMLYSSCKSRLLEIVErQLQMDVirkiEIDNGDELTADFLYEEVH 320
Cdd:smart00102  79 SPD-GAPVKSKMLYASSKDTLKKELG-GIQVEV----QATDEDDLDEEALKEKLK 127
ADF smart00102
Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin ...
 11-138 7.70e-32

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


Pssm-ID: 214516  Cd Length: 127  Bit Score: 116.23  E-value: 7.70e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334848198    11 EDVKEIFARARNGK---YRLLKISIENEQLVIGSYSQPSDSWDKDYDSfvlplLEDKQPCYILFRLDSQ--NAQGYEWIF 85
Cdd:smart00102   1 EDCKEAFNELKKKRkhsAIIFKIDKDNEEIVVEEVGSTEDSYDEFVEE-----LPEDECRYALYDYKFTteESKKSKIVF 75

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 334848198    86 IAWSPDHSHVRQKMLYAATRATLKKEFGGGHIKDEVfgTVKEDVSLHGYKKYL 138
Cdd:smart00102  76 IFWSPDGAPVKSKMLYASSKDTLKKELGGIQVEVQA--TDEDDLDEEALKEKL 126
ADF_gelsolin cd00013
Actin depolymerization factor/cofilin- and gelsolin-like domains; Actin depolymerization ...
 206-308 2.04e-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: 106.39  E-value: 2.04e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334848198 206 NYVQLEIDIKNEIIILANTTNTELKDLPKRIPKDSARYHFFLYKHSHEGDYLESIVFIYSMPGYtCSIRERMLYSSCKSR 285
Cdd:cd00013    1 DWVLFKVDAKKEEIVVGSTGAGFLDEFLEELPEDDPRYAFYRFKYPHSDDKRSKFVFISWIPDG-VSIKQKMVYATNKQT 79

                         90       100
                 ....*....|....*....|...
gi 334848198 286 LLEIVErqlqmDVIRKIEIDNGD 308
Cdd:cd00013   80 LKEALF-----GLAVPVQIRDGD 97
ADF_gelsolin cd00013
Actin depolymerization factor/cofilin- and gelsolin-like domains; Actin depolymerization ...
 24-127 1.41e-24

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: 95.99  E-value: 1.41e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334848198  24 KYRLLKISIENEQLVIGSYSQPsdswdkdYDSFVLPLLEDKQPCYILFRLDSQNA--QGYEWIFIAWSPDHSHVRQKMLY 101
Cdd:cd00013    1 DWVLFKVDAKKEEIVVGSTGAG-------FLDEFLEELPEDDPRYAFYRFKYPHSddKRSKFVFISWIPDGVSIKQKMVY 73

                         90       100
                 ....*....|....*....|....*.
gi 334848198 102 AATRATLKKEFggGHIKDEVFGTVKE 127
Cdd:cd00013   74 ATNKQTLKEAL--FGLAVPVQIRDGD 97
Cofilin_ADF pfam00241
Cofilin/tropomyosin-type actin-binding protein; Severs actin filaments and binds to actin ...
 13-130 2.47e-22

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


Pssm-ID: 459727  Cd Length: 123  Bit Score: 90.71  E-value: 2.47e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334848198   13 VKEIFARARNGK---YRLLKISIENEQLVIGSysqpSDSWDKDYDSFVlPLLEDKQPCYILFRLDSQNAQG---YEWIFI 86
Cdd:pfam00241   1 CKEAYQELRSDKktnWIIFKIDDDKEEIVVEE----TGEGGLSYDEFL-EELPDDEPRYAVYRFEYTHDDGskrSKLVFI 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 334848198   87 AWSPDHSHVRQKMLYAATRATLKKEFGGGHIkdEVFGTVKEDVS 130
Cdd:pfam00241  76 TWCPDGAPIKRKMLYASSKAALKRELKGIHV--EIQATDPSELT 117
Cofilin_ADF pfam00241
Cofilin/tropomyosin-type actin-binding protein; Severs actin filaments and binds to actin ...
 191-317 5.59e-20

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


Pssm-ID: 459727  Cd Length: 123  Bit Score: 84.55  E-value: 5.59e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334848198  191 REAFQALekLNNRQLNYVQLEIDIKNEIIILANTTNTELK--DLPKRIPKDSARYHFFLYKHSHE-GDYLESIVFIYSMP 267
Cdd:pfam00241   2 KEAYQEL--RSDKKTNWIIFKIDDDKEEIVVEETGEGGLSydEFLEELPDDEPRYAVYRFEYTHDdGSKRSKLVFITWCP 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 334848198  268 GyTCSIRERMLYSSCKSRLLeiveRQLQmDVIRKIEIDNGDELTADFLYE 317
Cdd:pfam00241  80 D-GAPIKRKMLYASSKAALK----RELK-GIHVEIQATDPSELTEEEILE 123
ADF_cofilin_like cd11286
Cofilin, Destrin, and related actin depolymerizing factors; Actin depolymerization factor ...
 5-131 1.59e-19

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: 83.38  E-value: 1.59e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334848198   5 TGIQASEDVKEIFARARNG---KYRLLKISIENEQLVIGSYSQPsdswDKDYDSFVlPLLEDKQPCYILFRLDSQNAQGY 81
Cdd:cd11286    1 SGVKVSDECITAFNELKLKkkhKYIIFKISDDKKEIVVEKVGER----DASYDDFL-EKLPENECRYAVYDFEYETKDGG 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 334848198  82 ---EWIFIAWSPDHSHVRQKMLYAATRATLKKEFGGGHIkdEVFGTVKEDVSL 131
Cdd:cd11286   76 krsKLVFISWCPDTAPIKSKMLYASSKDALKKKLNGIKK--EIQATDLSELSE 126
ADF_GMF-beta_like cd11283
ADF-homology domain of glia maturation factor beta and related proteins; Actin ...
 189-311 5.65e-09

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: 53.78  E-value: 5.65e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334848198 189 ISREAFQALEKL---NNRQLNYVQLEIDIKN-EIIILANTTNTELKDLPKRIPKDSARYHFFLYKHSH-EGDYLESIVFI 263
Cdd:cd11283    2 ISDEVKEALKKFrfrKSKANAALILKIDKEKqEIVVDEELEDISIEELAEELPEHSPRFVLYSYKMKHdDGRISYPLVLI 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 334848198 264 YSMPGyTCSIRERMLYSSCKSRLleiverQLQMDVIRKIEIDNGDELT 311
Cdd:cd11283   82 YWSPQ-GCSPELQMLYAGAKELL------VKEAEVTKVFEIRDGEELT 122
ADF_Twf-C_like cd11284
C-terminal ADF domain of twinfilin and related proteins; Actin depolymerization factor ...
 10-113 2.29e-07

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: 49.15  E-value: 2.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334848198  10 SEDVKEIFARARNGKYRL--LKISIENEQLVI-GSYSQPSDSWDKDydsfvlpLLEDKQPCYILFRLDSQNAQGYewIFI 86
Cdd:cd11284    8 SEEAKDALSELASGGVNLvqLSIDLENETIELvSSSSISIPDDLSS-------LIPSDHPRYHFYRYPHTYLSSV--VFI 78

                         90       100       110
                 ....*....|....*....|....*....|.
gi 334848198  87 AWSPDHSHVRQKMLYAATRA----TLKKEFG 113
Cdd:cd11284   79 YSCPSGSKVKERMLYASSKSgllnHAEDEGK 109
PLN03216 PLN03216
actin depolymerizing factor; Provisional
 5-116 6.74e-07

actin depolymerizing factor; Provisional


Pssm-ID: 178755  Cd Length: 141  Bit Score: 48.00  E-value: 6.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334848198   5 TGIQASEDVKEIFARARNGK---YRLLKISIENEQLVIGSYSQPSDSwdkdYDSFVLPLLEDKqpC-YILFRLD---SQN 77
Cdd:PLN03216   8 TGMWVTDECKNSFMEMKWKKvhrYIVFKIDEKSRKVTVDKVGGPGES----YDDLAASLPTDD--CrYAVFDFDfvtVDN 81

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 334848198  78 AQGYEWIFIAWSPDHSHVRQKMLYAATRATLKKEFGGGH 116
Cdd:PLN03216  82 CRKSKIFFIAWSPEASRIRAKMLYATSKDGLRRVLDGVH 120
ADF_cofilin_like cd11286
Cofilin, Destrin, and related actin depolymerizing factors; Actin depolymerization factor ...
 184-313 3.99e-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: 45.63  E-value: 3.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334848198 184 GVAfpISREAFQALEKLN-NRQLNYVQLEI-DIKNEIIILANTTNTEL-KDLPKRIPKDSARYHF--FLYKHSHEGDyLE 258
Cdd:cd11286    2 GVK--VSDECITAFNELKlKKKHKYIIFKIsDDKKEIVVEKVGERDASyDDFLEKLPENECRYAVydFEYETKDGGK-RS 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 334848198 259 SIVFIYSMPGyTCSIRERMLYSSCKSRLleivERQLQmDVIRKIEIDNGDELTAD 313
Cdd:cd11286   79 KLVFISWCPD-TAPIKSKMLYASSKDAL----KKKLN-GIKKEIQATDLSELSEE 127
 
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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