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Conserved domains on  [gi|149018686|gb|EDL77327|]
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protein tyrosine kinase 9-like (A6-related protein) (predicted), isoform CRA_a [Rattus norvegicus]

Protein Classification

twinfilin-like domain-containing protein( domain architecture ID 10336924)

twinfilin-like domain-containing protein, similar to Trypanosoma cruzi G-actin binding protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ADF_Twf-C_like cd11284
C-terminal ADF domain of twinfilin and related proteins; Actin depolymerization factor ...
 78-213 5.59e-62

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: 190.52  E-value: 5.59e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149018686  78 QGLAFPLQPEAQRALQQLKQKTVNYIQLKLDLERETIELVHTEPT-NVAQLPSRVPRDAARYHFFLYKHTHegdsLESVV 156
Cdd:cd11284    1 PGVAFPVSEEAKDALSELASGGVNLVQLSIDLENETIELVSSSSIsIPDDLSSLIPSDHPRYHFYRYPHTY----LSSVV 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 149018686 157 FIYSMPGYkCSIKERMLYSSCKSRLLDSVEQDFQLEIAKKIEIGDGAELTAEFLYDE 213
Cdd:cd11284   77 FIYSCPSG-SKVKERMLYASSKSGLLNHAEDEGKIEIDKKIEIGDPDELTESFLSDE 132
ADF_gelsolin super family cl15697
Actin depolymerization factor/cofilin- and gelsolin-like domains; Actin depolymerization ...
 1-44 1.34e-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.


The actual alignment was detected with superfamily member cd11285:

Pssm-ID: 472830  Cd Length: 139  Bit Score: 79.21  E-value: 1.34e-18
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 149018686   1 MLYAATRATVKKEFGGGHIKDELFGTVKDDLSLAGYQKHLSSCA 44
Cdd:cd11285   96 MLYASTRATLKRELGSNHIKDELFATELEELTLEGYEKHLKHEA 139
 
Name Accession Description Interval E-value
ADF_Twf-C_like cd11284
C-terminal ADF domain of twinfilin and related proteins; Actin depolymerization factor ...
 78-213 5.59e-62

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: 190.52  E-value: 5.59e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149018686  78 QGLAFPLQPEAQRALQQLKQKTVNYIQLKLDLERETIELVHTEPT-NVAQLPSRVPRDAARYHFFLYKHTHegdsLESVV 156
Cdd:cd11284    1 PGVAFPVSEEAKDALSELASGGVNLVQLSIDLENETIELVSSSSIsIPDDLSSLIPSDHPRYHFYRYPHTY----LSSVV 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 149018686 157 FIYSMPGYkCSIKERMLYSSCKSRLLDSVEQDFQLEIAKKIEIGDGAELTAEFLYDE 213
Cdd:cd11284   77 FIYSCPSG-SKVKERMLYASSKSGLLNHAEDEGKIEIDKKIEIGDPDELTESFLSDE 132
ADF smart00102
Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin ...
 87-215 2.31e-25

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


Pssm-ID: 214516  Cd Length: 127  Bit Score: 96.58  E-value: 2.31e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149018686    87 EAQRALqqLKQKTVNYIQLKLDLERETIELVHTEPTN--VAQLPSRVPRDAARYHFFLYKHTHEGDSLESVVFIYSMPGy 164
Cdd:smart00102   5 EAFNEL--KKKRKHSAIIFKIDKDNEEIVVEEVGSTEdsYDEFVEELPEDECRYALYDYKFTTEESKKSKIVFIFWSPD- 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 149018686   165 KCSIKERMLYSSCKSRLLDSVEQdfqleIAKKIEIGDGAELTAEFLYDEVH 215
Cdd:smart00102  82 GAPVKSKMLYASSKDTLKKELGG-----IQVEVQATDEDDLDEEALKEKLK 127
Cofilin_ADF pfam00241
Cofilin/tropomyosin-type actin-binding protein; Severs actin filaments and binds to actin ...
 88-212 2.12e-22

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


Pssm-ID: 459727  Cd Length: 123  Bit Score: 88.79  E-value: 2.12e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149018686   88 AQRALQQLKQ-KTVNYIQLKLDLERETIELVHT--EPTNVAQLPSRVPRDAARYHFFLYKHTHEGDS-LESVVFIYSMPG 163
Cdd:pfam00241   1 CKEAYQELRSdKKTNWIIFKIDDDKEEIVVEETgeGGLSYDEFLEELPDDEPRYAVYRFEYTHDDGSkRSKLVFITWCPD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 149018686  164 yKCSIKERMLYSSCKSRLLDSVEqdfqlEIAKKIEIGDGAELTAEFLYD 212
Cdd:pfam00241  81 -GAPIKRKMLYASSKAALKRELK-----GIHVEIQATDPSELTEEEILE 123
ADF_Twf-N_like cd11285
N-terminal ADF domain of twinfilin and related proteins; Actin depolymerization factor ...
 1-44 1.34e-18

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: 79.21  E-value: 1.34e-18
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 149018686   1 MLYAATRATVKKEFGGGHIKDELFGTVKDDLSLAGYQKHLSSCA 44
Cdd:cd11285   96 MLYASTRATLKRELGSNHIKDELFATELEELTLEGYEKHLKHEA 139
ADF smart00102
Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin ...
 1-33 1.08e-03

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


Pssm-ID: 214516  Cd Length: 127  Bit Score: 38.03  E-value: 1.08e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 149018686     1 MLYAATRATVKKEFGGGHIKDElfGTVKDDLSL 33
Cdd:smart00102  89 MLYASSKDTLKKELGGIQVEVQ--ATDEDDLDE 119
PLN03216 PLN03216
actin depolymerizing factor; Provisional
 87-190 2.77e-03

actin depolymerizing factor; Provisional


Pssm-ID: 178755  Cd Length: 141  Bit Score: 37.21  E-value: 2.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149018686  87 EAQRALQQLKQKTVN-YIQLKLDlERE---TIELVHTEPTNVAQLPSRVPRDAARYHFFLYKHTHEGDSLESVVFIYSMP 162
Cdd:PLN03216  15 ECKNSFMEMKWKKVHrYIVFKID-EKSrkvTVDKVGGPGESYDDLAASLPTDDCRYAVFDFDFVTVDNCRKSKIFFIAWS 93

                         90       100       110
                 ....*....|....*....|....*....|.
gi 149018686 163 GYKCSIKERMLYSSCKS---RLLDSVEQDFQ 190
Cdd:PLN03216  94 PEASRIRAKMLYATSKDglrRVLDGVHYELQ 124
Cofilin_ADF pfam00241
Cofilin/tropomyosin-type actin-binding protein; Severs actin filaments and binds to actin ...
 1-32 3.38e-03

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


Pssm-ID: 459727  Cd Length: 123  Bit Score: 36.40  E-value: 3.38e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 149018686    1 MLYAATRATVKKEFGGGHIkdELFGTVKDDLS 32
Cdd:pfam00241  88 MLYASSKAALKRELKGIHV--EIQATDPSELT 117
 
Name Accession Description Interval E-value
ADF_Twf-C_like cd11284
C-terminal ADF domain of twinfilin and related proteins; Actin depolymerization factor ...
 78-213 5.59e-62

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: 190.52  E-value: 5.59e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149018686  78 QGLAFPLQPEAQRALQQLKQKTVNYIQLKLDLERETIELVHTEPT-NVAQLPSRVPRDAARYHFFLYKHTHegdsLESVV 156
Cdd:cd11284    1 PGVAFPVSEEAKDALSELASGGVNLVQLSIDLENETIELVSSSSIsIPDDLSSLIPSDHPRYHFYRYPHTY----LSSVV 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 149018686 157 FIYSMPGYkCSIKERMLYSSCKSRLLDSVEQDFQLEIAKKIEIGDGAELTAEFLYDE 213
Cdd:cd11284   77 FIYSCPSG-SKVKERMLYASSKSGLLNHAEDEGKIEIDKKIEIGDPDELTESFLSDE 132
ADF smart00102
Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin ...
 87-215 2.31e-25

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


Pssm-ID: 214516  Cd Length: 127  Bit Score: 96.58  E-value: 2.31e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149018686    87 EAQRALqqLKQKTVNYIQLKLDLERETIELVHTEPTN--VAQLPSRVPRDAARYHFFLYKHTHEGDSLESVVFIYSMPGy 164
Cdd:smart00102   5 EAFNEL--KKKRKHSAIIFKIDKDNEEIVVEEVGSTEdsYDEFVEELPEDECRYALYDYKFTTEESKKSKIVFIFWSPD- 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 149018686   165 KCSIKERMLYSSCKSRLLDSVEQdfqleIAKKIEIGDGAELTAEFLYDEVH 215
Cdd:smart00102  82 GAPVKSKMLYASSKDTLKKELGG-----IQVEVQATDEDDLDEEALKEKLK 127
Cofilin_ADF pfam00241
Cofilin/tropomyosin-type actin-binding protein; Severs actin filaments and binds to actin ...
 88-212 2.12e-22

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


Pssm-ID: 459727  Cd Length: 123  Bit Score: 88.79  E-value: 2.12e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149018686   88 AQRALQQLKQ-KTVNYIQLKLDLERETIELVHT--EPTNVAQLPSRVPRDAARYHFFLYKHTHEGDS-LESVVFIYSMPG 163
Cdd:pfam00241   1 CKEAYQELRSdKKTNWIIFKIDDDKEEIVVEETgeGGLSYDEFLEELPDDEPRYAVYRFEYTHDDGSkRSKLVFITWCPD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 149018686  164 yKCSIKERMLYSSCKSRLLDSVEqdfqlEIAKKIEIGDGAELTAEFLYD 212
Cdd:pfam00241  81 -GAPIKRKMLYASSKAALKRELK-----GIHVEIQATDPSELTEEEILE 123
ADF_gelsolin cd00013
Actin depolymerization factor/cofilin- and gelsolin-like domains; Actin depolymerization ...
 101-202 2.40e-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: 82.51  E-value: 2.40e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149018686 101 NYIQLKLDLERETIELVHTEPTNVAQLPSRVPRDAARYHFFLYKHTHEGDSLESVVFIYSMPGYkCSIKERMLYSSCKSR 180
Cdd:cd00013    1 DWVLFKVDAKKEEIVVGSTGAGFLDEFLEELPEDDPRYAFYRFKYPHSDDKRSKFVFISWIPDG-VSIKQKMVYATNKQT 79

                         90       100
                 ....*....|....*....|..
gi 149018686 181 LLDSVEqdfqlEIAKKIEIGDG 202
Cdd:cd00013   80 LKEALF-----GLAVPVQIRDG 96
ADF_Twf-N_like cd11285
N-terminal ADF domain of twinfilin and related proteins; Actin depolymerization factor ...
 1-44 1.34e-18

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: 79.21  E-value: 1.34e-18
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 149018686   1 MLYAATRATVKKEFGGGHIKDELFGTVKDDLSLAGYQKHLSSCA 44
Cdd:cd11285   96 MLYASTRATLKRELGSNHIKDELFATELEELTLEGYEKHLKHEA 139
ADF_GMF-beta_like cd11283
ADF-homology domain of glia maturation factor beta and related proteins; Actin ...
 86-206 2.78e-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: 51.08  E-value: 2.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149018686  86 PEAQRALQQL---KQKTVNYIQLKLDLERETI----ELVHTEPTNVAQ-LPSRVPRdaarYHFFLYKHTHeGDSLESV-- 155
Cdd:cd11283    4 DEVKEALKKFrfrKSKANAALILKIDKEKQEIvvdeELEDISIEELAEeLPEHSPR----FVLYSYKMKH-DDGRISYpl 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 149018686 156 VFIYSMPGyKCSIKERMLYSSCKSRLLDSveqdfqLEIAKKIEIGDGAELT 206
Cdd:cd11283   79 VLIYWSPQ-GCSPELQMLYAGAKELLVKE------AEVTKVFEIRDGEELT 122
ADF_cofilin_like cd11286
Cofilin, Destrin, and related actin depolymerizing factors; Actin depolymerization factor ...
 86-208 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: 46.40  E-value: 1.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149018686  86 PEAQRALQQLK-QKTVNYIQLKLDLERETIELVHTEPTNVA--QLPSRVPRDAARYHFFLYKHTHEGDSLES-VVFIYSM 161
Cdd:cd11286    7 DECITAFNELKlKKKHKYIIFKISDDKKEIVVEKVGERDASydDFLEKLPENECRYAVYDFEYETKDGGKRSkLVFISWC 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 149018686 162 PGyKCSIKERMLYSSCKSRLLDSVEQdfqleIAKKIEIGDGAELTAE 208
Cdd:cd11286   87 PD-TAPIKSKMLYASSKDALKKKLNG-----IKKEIQATDLSELSEE 127
ADF smart00102
Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin ...
 1-33 1.08e-03

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


Pssm-ID: 214516  Cd Length: 127  Bit Score: 38.03  E-value: 1.08e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 149018686     1 MLYAATRATVKKEFGGGHIKDElfGTVKDDLSL 33
Cdd:smart00102  89 MLYASSKDTLKKELGGIQVEVQ--ATDEDDLDE 119
PLN03216 PLN03216
actin depolymerizing factor; Provisional
 87-190 2.77e-03

actin depolymerizing factor; Provisional


Pssm-ID: 178755  Cd Length: 141  Bit Score: 37.21  E-value: 2.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149018686  87 EAQRALQQLKQKTVN-YIQLKLDlERE---TIELVHTEPTNVAQLPSRVPRDAARYHFFLYKHTHEGDSLESVVFIYSMP 162
Cdd:PLN03216  15 ECKNSFMEMKWKKVHrYIVFKID-EKSrkvTVDKVGGPGESYDDLAASLPTDDCRYAVFDFDFVTVDNCRKSKIFFIAWS 93

                         90       100       110
                 ....*....|....*....|....*....|.
gi 149018686 163 GYKCSIKERMLYSSCKS---RLLDSVEQDFQ 190
Cdd:PLN03216  94 PEASRIRAKMLYATSKDglrRVLDGVHYELQ 124
Cofilin_ADF pfam00241
Cofilin/tropomyosin-type actin-binding protein; Severs actin filaments and binds to actin ...
 1-32 3.38e-03

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


Pssm-ID: 459727  Cd Length: 123  Bit Score: 36.40  E-value: 3.38e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 149018686    1 MLYAATRATVKKEFGGGHIkdELFGTVKDDLS 32
Cdd:pfam00241  88 MLYASSKAALKRELKGIHV--EIQATDPSELT 117
 
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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