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Conserved domains on  [gi|56606100|ref|NP_001008521|]
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twinfilin-1 [Rattus norvegicus]

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 1.35e-67

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: 208.64  E-value: 1.35e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56606100   4 QTGIQASEDVKEIFARAR-NGKYRLLKISIENEQLVVGSCSPPSDSWEQDYDPFVLPLLEDKQPCYVLFRLDSQNaQGYE 82
Cdd:cd11285   1 QSGITASEELLDAFKSAKsSGSVRAIKITIENEELVPDATIETTGSWEQDFDLLVLPLLEEKEPCYILYRLDSKS-AGYE 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 56606100  83 WIFIAWSPDHSHVRQKMLYAATRATLKKEFGGGHIKDEVFGTVKEDVSLHGYRKYLLSQS 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 1.10e-58

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: 185.90  E-value: 1.10e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56606100 176 QGVAFPISRDAFQALEKLSKRQLNYVQLEIDIKNETIILANTENT-ELKDLPKRIPKDSARYHFFLYKHshegDYLESIV 254
Cdd:cd11284   1 PGVAFPVSEEAKDALSELASGGVNLVQLSIDLENETIELVSSSSIsIPDDLSSLIPSDHPRYHFYRYPH----TYLSSVV 76

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 56606100 255 FIYSMPGYtCSIRERMLYSSCKSPLLDIVERQLQMDVIRKIEIDNGDELTADFLYDE 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 1.35e-67

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: 208.64  E-value: 1.35e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56606100   4 QTGIQASEDVKEIFARAR-NGKYRLLKISIENEQLVVGSCSPPSDSWEQDYDPFVLPLLEDKQPCYVLFRLDSQNaQGYE 82
Cdd:cd11285   1 QSGITASEELLDAFKSAKsSGSVRAIKITIENEELVPDATIETTGSWEQDFDLLVLPLLEEKEPCYILYRLDSKS-AGYE 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 56606100  83 WIFIAWSPDHSHVRQKMLYAATRATLKKEFGGGHIKDEVFGTVKEDVSLHGYRKYLLSQS 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 1.10e-58

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: 185.90  E-value: 1.10e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56606100 176 QGVAFPISRDAFQALEKLSKRQLNYVQLEIDIKNETIILANTENT-ELKDLPKRIPKDSARYHFFLYKHshegDYLESIV 254
Cdd:cd11284   1 PGVAFPVSEEAKDALSELASGGVNLVQLSIDLENETIELVSSSSIsIPDDLSSLIPSDHPRYHFYRYPH----TYLSSVV 76

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 56606100 255 FIYSMPGYtCSIRERMLYSSCKSPLLDIVERQLQMDVIRKIEIDNGDELTADFLYDE 311
Cdd:cd11284  77 FIYSCPSG-SKVKERMLYASSKSGLLNHAEDEGKIEIDKKIEIGDPDELTESFLSDE 132
ADF smart00102
Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin ...
 181-313 8.60e-34

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


Pssm-ID: 214516  Cd Length: 127  Bit Score: 121.24  E-value: 8.60e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56606100    181 PISRDAFQALEKlsKRQLNYVQLEIDIKNETIILANTENTE--LKDLPKRIPKDSARYHFFLYKHSHEGDYLESIVFIYS 258
Cdd:smart00102   1 EDCKEAFNELKK--KRKHSAIIFKIDKDNEEIVVEEVGSTEdsYDEFVEELPEDECRYALYDYKFTTEESKKSKIVFIFW 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 56606100    259 MPGyTCSIRERMLYSSCKSPLLDIVErQLQMDVirkiEIDNGDELTADFLYDEVH 313
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 9.52e-30

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


Pssm-ID: 214516  Cd Length: 127  Bit Score: 110.45  E-value: 9.52e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56606100     11 EDVKEIFARARNGK---YRLLKISIENEQLVVGSCSPPSDSWEQDYDpfvlpLLEDKQPCYVLFRLDSQ--NAQGYEWIF 85
Cdd:smart00102   1 EDCKEAFNELKKKRkhsAIIFKIDKDNEEIVVEEVGSTEDSYDEFVE-----ELPEDECRYALYDYKFTteESKKSKIVF 75

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 56606100     86 IAWSPDHSHVRQKMLYAATRATLKKEFGGGHIKDEVfgTVKEDVSLHGYRKYL 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 9.29e-22

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


Pssm-ID: 459727  Cd Length: 123  Bit Score: 89.17  E-value: 9.29e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56606100    13 VKEIFARARNGK---YRLLKISIENEQLVVGScsppSDSWEQDYDPFVlPLLEDKQPCYVLFRLDSQNAQG---YEWIFI 86
Cdd:pfam00241   1 CKEAYQELRSDKktnWIIFKIDDDKEEIVVEE----TGEGGLSYDEFL-EELPDDEPRYAVYRFEYTHDDGskrSKLVFI 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 56606100    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 ...
 184-310 4.19e-21

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


Pssm-ID: 459727  Cd Length: 123  Bit Score: 87.24  E-value: 4.19e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56606100   184 RDAFQALekLSKRQLNYVQLEIDIKNETIILANTENTELK--DLPKRIPKDSARYHFFLYKHSHE-GDYLESIVFIYSMP 260
Cdd:pfam00241   2 KEAYQEL--RSDKKTNWIIFKIDDDKEEIVVEETGEGGLSydEFLEELPDDEPRYAVYRFEYTHDdGSKRSKLVFITWCP 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 56606100   261 GyTCSIRERMLYSSCKSPLLdiveRQLQmDVIRKIEIDNGDELTADFLYD 310
Cdd:pfam00241  80 D-GAPIKRKMLYASSKAALK----RELK-GIHVEIQATDPSELTEEEILE 123
PLN03216 PLN03216
actin depolymerizing factor; Provisional
 5-116 3.51e-07

actin depolymerizing factor; Provisional


Pssm-ID: 178755  Cd Length: 141  Bit Score: 49.15  E-value: 3.51e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56606100    5 TGIQASEDVKEIFARARNGK---YRLLKISIENEQLVVGSCSPPSDSweqdYDPFVLPLLEDKqpC-YVLFRLD---SQN 77
Cdd:PLN03216   8 TGMWVTDECKNSFMEMKWKKvhrYIVFKIDEKSRKVTVDKVGGPGES----YDDLAASLPTDD--CrYAVFDFDfvtVDN 81

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 56606100   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 1.35e-67

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: 208.64  E-value: 1.35e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56606100   4 QTGIQASEDVKEIFARAR-NGKYRLLKISIENEQLVVGSCSPPSDSWEQDYDPFVLPLLEDKQPCYVLFRLDSQNaQGYE 82
Cdd:cd11285   1 QSGITASEELLDAFKSAKsSGSVRAIKITIENEELVPDATIETTGSWEQDFDLLVLPLLEEKEPCYILYRLDSKS-AGYE 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 56606100  83 WIFIAWSPDHSHVRQKMLYAATRATLKKEFGGGHIKDEVFGTVKEDVSLHGYRKYLLSQS 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 1.10e-58

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: 185.90  E-value: 1.10e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56606100 176 QGVAFPISRDAFQALEKLSKRQLNYVQLEIDIKNETIILANTENT-ELKDLPKRIPKDSARYHFFLYKHshegDYLESIV 254
Cdd:cd11284   1 PGVAFPVSEEAKDALSELASGGVNLVQLSIDLENETIELVSSSSIsIPDDLSSLIPSDHPRYHFYRYPH----TYLSSVV 76

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 56606100 255 FIYSMPGYtCSIRERMLYSSCKSPLLDIVERQLQMDVIRKIEIDNGDELTADFLYDE 311
Cdd:cd11284  77 FIYSCPSG-SKVKERMLYASSKSGLLNHAEDEGKIEIDKKIEIGDPDELTESFLSDE 132
ADF smart00102
Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin ...
 181-313 8.60e-34

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


Pssm-ID: 214516  Cd Length: 127  Bit Score: 121.24  E-value: 8.60e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56606100    181 PISRDAFQALEKlsKRQLNYVQLEIDIKNETIILANTENTE--LKDLPKRIPKDSARYHFFLYKHSHEGDYLESIVFIYS 258
Cdd:smart00102   1 EDCKEAFNELKK--KRKHSAIIFKIDKDNEEIVVEEVGSTEdsYDEFVEELPEDECRYALYDYKFTTEESKKSKIVFIFW 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 56606100    259 MPGyTCSIRERMLYSSCKSPLLDIVErQLQMDVirkiEIDNGDELTADFLYDEVH 313
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 9.52e-30

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


Pssm-ID: 214516  Cd Length: 127  Bit Score: 110.45  E-value: 9.52e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56606100     11 EDVKEIFARARNGK---YRLLKISIENEQLVVGSCSPPSDSWEQDYDpfvlpLLEDKQPCYVLFRLDSQ--NAQGYEWIF 85
Cdd:smart00102   1 EDCKEAFNELKKKRkhsAIIFKIDKDNEEIVVEEVGSTEDSYDEFVE-----ELPEDECRYALYDYKFTteESKKSKIVF 75

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 56606100     86 IAWSPDHSHVRQKMLYAATRATLKKEFGGGHIKDEVfgTVKEDVSLHGYRKYL 138
Cdd:smart00102  76 IFWSPDGAPVKSKMLYASSKDTLKKELGGIQVEVQA--TDEDDLDEEALKEKL 126
ADF_gelsolin cd00013
Actin depolymerization factor/cofilin- and gelsolin-like domains; Actin depolymerization ...
 199-301 3.46e-29

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: 107.94  E-value: 3.46e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56606100 199 NYVQLEIDIKNETIILANTENTELKDLPKRIPKDSARYHFFLYKHSHEGDYLESIVFIYSMPGYtCSIRERMLYSSCKSP 278
Cdd:cd00013   1 DWVLFKVDAKKEEIVVGSTGAGFLDEFLEELPEDDPRYAFYRFKYPHSDDKRSKFVFISWIPDG-VSIKQKMVYATNKQT 79

                        90       100
                ....*....|....*....|...
gi 56606100 279 LLDIVErqlqmDVIRKIEIDNGD 301
Cdd:cd00013  80 LKEALF-----GLAVPVQIRDGD 97
ADF_gelsolin cd00013
Actin depolymerization factor/cofilin- and gelsolin-like domains; Actin depolymerization ...
 24-127 6.97e-27

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: 102.16  E-value: 6.97e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56606100  24 KYRLLKISIENEQLVVGSCSPPsdsweqdYDPFVLPLLEDKQPCYVLFRLDSQNA--QGYEWIFIAWSPDHSHVRQKMLY 101
Cdd:cd00013   1 DWVLFKVDAKKEEIVVGSTGAG-------FLDEFLEELPEDDPRYAFYRFKYPHSddKRSKFVFISWIPDGVSIKQKMVY 73

                        90       100
                ....*....|....*....|....*.
gi 56606100 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 9.29e-22

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


Pssm-ID: 459727  Cd Length: 123  Bit Score: 89.17  E-value: 9.29e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56606100    13 VKEIFARARNGK---YRLLKISIENEQLVVGScsppSDSWEQDYDPFVlPLLEDKQPCYVLFRLDSQNAQG---YEWIFI 86
Cdd:pfam00241   1 CKEAYQELRSDKktnWIIFKIDDDKEEIVVEE----TGEGGLSYDEFL-EELPDDEPRYAVYRFEYTHDDGskrSKLVFI 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 56606100    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 ...
 184-310 4.19e-21

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


Pssm-ID: 459727  Cd Length: 123  Bit Score: 87.24  E-value: 4.19e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56606100   184 RDAFQALekLSKRQLNYVQLEIDIKNETIILANTENTELK--DLPKRIPKDSARYHFFLYKHSHE-GDYLESIVFIYSMP 260
Cdd:pfam00241   2 KEAYQEL--RSDKKTNWIIFKIDDDKEEIVVEETGEGGLSydEFLEELPDDEPRYAVYRFEYTHDdGSKRSKLVFITWCP 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 56606100   261 GyTCSIRERMLYSSCKSPLLdiveRQLQmDVIRKIEIDNGDELTADFLYD 310
Cdd:pfam00241  80 D-GAPIKRKMLYASSKAALK----RELK-GIHVEIQATDPSELTEEEILE 123
ADF_cofilin_like cd11286
Cofilin, Destrin, and related actin depolymerizing factors; Actin depolymerization factor ...
 5-131 1.81e-20

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: 86.07  E-value: 1.81e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56606100   5 TGIQASEDVKEIFARARNG---KYRLLKISIENEQLVVGSCSPPSDSWEQdydpfVLPLLEDKQPCYVLFRLDSQNAQGY 81
Cdd:cd11286   1 SGVKVSDECITAFNELKLKkkhKYIIFKISDDKKEIVVEKVGERDASYDD-----FLEKLPENECRYAVYDFEYETKDGG 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 56606100  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 ...
 182-304 4.48e-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: 4.48e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56606100 182 ISRDAFQALEK--LSKRQLNY-VQLEIDIKNETIILANT-ENTELKDLPKRIPKDSARYHFFLYKHSH-EGDYLESIVFI 256
Cdd:cd11283   2 ISDEVKEALKKfrFRKSKANAaLILKIDKEKQEIVVDEElEDISIEELAEELPEHSPRFVLYSYKMKHdDGRISYPLVLI 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 56606100 257 YSMPGyTCSIRERMLYSSCKSPLLDiverqlQMDVIRKIEIDNGDELT 304
Cdd:cd11283  82 YWSPQ-GCSPELQMLYAGAKELLVK------EAEVTKVFEIRDGEELT 122
ADF_Twf-C_like cd11284
C-terminal ADF domain of twinfilin and related proteins; Actin depolymerization factor ...
 10-113 2.48e-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: 2.48e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56606100  10 SEDVKEIFARARNGKYRL--LKISIENEQLVVG---SCSPPSDsweqdydpfvLP-LLEDKQPCYVLFRLDSQNAQGYew 83
Cdd:cd11284   8 SEEAKDALSELASGGVNLvqLSIDLENETIELVsssSISIPDD----------LSsLIPSDHPRYHFYRYPHTYLSSV-- 75

                        90       100       110
                ....*....|....*....|....*....|....
gi 56606100  84 IFIAWSPDHSHVRQKMLYAATRA----TLKKEFG 113
Cdd:cd11284  76 VFIYSCPSGSKVKERMLYASSKSgllnHAEDEGK 109
PLN03216 PLN03216
actin depolymerizing factor; Provisional
 5-116 3.51e-07

actin depolymerizing factor; Provisional


Pssm-ID: 178755  Cd Length: 141  Bit Score: 49.15  E-value: 3.51e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56606100    5 TGIQASEDVKEIFARARNGK---YRLLKISIENEQLVVGSCSPPSDSweqdYDPFVLPLLEDKqpC-YVLFRLD---SQN 77
Cdd:PLN03216   8 TGMWVTDECKNSFMEMKWKKvhrYIVFKIDEKSRKVTVDKVGGPGES----YDDLAASLPTDD--CrYAVFDFDfvtVDN 81

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 56606100   78 AQGYEWIFIAWSPDHSHVRQKMLYAATRATLKKEFGGGH 116
Cdd:PLN03216  82 CRKSKIFFIAWSPEASRIRAKMLYATSKDGLRRVLDGVH 120
ADF_cofilin_like cd11286
Cofilin, Destrin, and related actin depolymerizing factors; Actin depolymerization factor ...
 177-306 7.08e-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: 7.08e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56606100 177 GVAfpISRDAFQALEKLS-KRQLNYVQLEIDIKNETIILANTE--NTELKDLPKRIPKDSARYHF--FLYKHSHEGDyLE 251
Cdd:cd11286   2 GVK--VSDECITAFNELKlKKKHKYIIFKISDDKKEIVVEKVGerDASYDDFLEKLPENECRYAVydFEYETKDGGK-RS 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 56606100 252 SIVFIYSMPGyTCSIRERMLYSSCKspllDIVERQLQmDVIRKIEIDNGDELTAD 306
Cdd:cd11286  79 KLVFISWCPD-TAPIKSKMLYASSK----DALKKKLN-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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