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Conserved domains on  [gi|568966412|ref|XP_006513161|]
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advillin isoform X1 [Mus musculus]

Protein Classification

villin/gelsolin family protein( domain architecture ID 10181771)

villin/gelsolin family protein which is an actin regulatory protein; similar to human actin-binding proteins advillin and villin-1; contains a villin headpiece domain and six gelsolin-like repeats

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
gelsolin_S1_like cd11290
Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; ...
 36-147 7.56e-57

Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin_like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


:

Pssm-ID: 200446  Cd Length: 113  Bit Score: 190.51  E-value: 7.56e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966412  36 FRAVSNDPRIITWRIEKMELALVPLSAHGNFYEGDCYIVLSTRRVGS-LLSQNIHFWIGKDSSQDEQSCAAIYTTQLDDY 114
Cdd:cd11290    1 FEGVGQKPGLQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDPSgSLSYDIHYWLGKEASQDEAGAAAIKAVELDDY 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 568966412 115 LGGSPVQHREVQYHESDTFRGYFKQGIIYKKGG 147
Cdd:cd11290   81 LGGRPVQHREVQGHESEEFLSYFKKGIIYIEGG 113
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
 448-548 3.97e-52

Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


:

Pssm-ID: 200449  Cd Length: 101  Bit Score: 177.08  E-value: 3.97e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966412 448 MVDDGKGQVEVWRIENLELVPVEYQWHGFFYGGDCYLVLYTYDVNGKPHYILYIWQGRHASRDELAASAYRAVEVDQQFD 527
Cdd:cd11293    1 MYDDGSGKVEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQGGGKEEHILYFWQGRHSSQDERAAAALLTVELDEELK 80

                         90       100
                 ....*....|....*....|.
gi 568966412 528 GAPVQVRVSMGKEPRHFMAIF 548
Cdd:cd11293   81 GRAVQVRVVQGKEPPHFLALF 101
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 676-771 3.51e-47

Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


:

Pssm-ID: 200447 [Multi-domain]  Cd Length: 99  Bit Score: 162.85  E-value: 3.51e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966412 676 RLFECSNKTGRFLVTEVTDFTQEDLSPGDVMLLDTWDQVFLWIGAEANATEKKGALSTAQEYLVTHPSGRD-PDTPILII 754
Cdd:cd11291    3 RLFRCSNESGFFKVEEISDFSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYIETDPLGRSkPRTPIYLV 82

                         90
                 ....*....|....*..
gi 568966412 755 KQGFEPPTFTGWFLAWD 771
Cdd:cd11291   83 KQGNEPPTFTGYFHAWD 99
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 306-404 2.62e-41

Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


:

Pssm-ID: 200448  Cd Length: 98  Bit Score: 146.24  E-value: 2.62e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966412 306 KSSIMLYHVSDTAGQLSVTEVATRPLVQDLLNHDDCYILDQsGTKIYVWKGKGATKVEKQAAMSKALDFIKMKGYPSSTN 385
Cdd:cd11292    1 AEQKKLYKVSDASGKLKLTEVAEGSLNQEMLDSEDCYILDC-GSEIFVWVGKGASLDERKAALKNAEEFLRKKKRPPYTQ 79

                         90
                 ....*....|....*....
gi 568966412 386 VETVNDGAESAMFKQLFQK 404
Cdd:cd11292   80 VTRVTEGGESALFKSKFAN 98
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 162-282 5.65e-35

Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


:

Pssm-ID: 200445  Cd Length: 92  Bit Score: 128.12  E-value: 5.65e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966412 162 VKRLLHVKGKRNIQATEVsltrecpgcpvlppwhlrlprtaltahtqvEMSWDSFNRGDVFLLDLGMVIIQWNGPESNSG 241
Cdd:cd11289    1 KPRLLHVKGRRNVRAREV------------------------------ELSWSSLNSGDVFILDLGSTIYQWNGSKSNRF 50

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 568966412 242 ERLKAMLLAKDIRDRERGGRAEIGVIEGDKEAASPGLMTVL 282
Cdd:cd11289   51 EKAKAMQLAQGIRDERRLGRAKVIVLDEGDTNESPEFWKVL 91
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 569-658 2.99e-30

Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


:

Pssm-ID: 200444  Cd Length: 92  Bit Score: 114.64  E-value: 2.99e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966412 569 PPVRLFQIHGNDKSNTKAVEVSASASSLNSNDVFLLRTQAEHYLWYGKGSSGDERAMAKELVDLLCDG-NADTVAEGQEP 647
Cdd:cd11288    1 SPTRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVASFLKPKaSLQEVAEGSEP 80

                         90
                 ....*....|.
gi 568966412 648 PEFWDLLGGKT 658
Cdd:cd11288   81 DEFWEALGGKS 91
VHP pfam02209
Villin headpiece domain;
843-878 4.98e-14

Villin headpiece domain;


:

Pssm-ID: 460493  Cd Length: 36  Bit Score: 66.63  E-value: 4.98e-14
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 568966412  843 YLSEQDFVSVFGITRGQFTALPGWKQLQLKKERGLF 878
Cdd:pfam02209   1 YLSDEDFEEVFGMSREEFYKLPKWKQNNLKKKAGLF 36
 
Name Accession Description Interval E-value
gelsolin_S1_like cd11290
Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; ...
 36-147 7.56e-57

Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin_like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200446  Cd Length: 113  Bit Score: 190.51  E-value: 7.56e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966412  36 FRAVSNDPRIITWRIEKMELALVPLSAHGNFYEGDCYIVLSTRRVGS-LLSQNIHFWIGKDSSQDEQSCAAIYTTQLDDY 114
Cdd:cd11290    1 FEGVGQKPGLQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDPSgSLSYDIHYWLGKEASQDEAGAAAIKAVELDDY 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 568966412 115 LGGSPVQHREVQYHESDTFRGYFKQGIIYKKGG 147
Cdd:cd11290   81 LGGRPVQHREVQGHESEEFLSYFKKGIIYIEGG 113
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
 448-548 3.97e-52

Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200449  Cd Length: 101  Bit Score: 177.08  E-value: 3.97e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966412 448 MVDDGKGQVEVWRIENLELVPVEYQWHGFFYGGDCYLVLYTYDVNGKPHYILYIWQGRHASRDELAASAYRAVEVDQQFD 527
Cdd:cd11293    1 MYDDGSGKVEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQGGGKEEHILYFWQGRHSSQDERAAAALLTVELDEELK 80

                         90       100
                 ....*....|....*....|.
gi 568966412 528 GAPVQVRVSMGKEPRHFMAIF 548
Cdd:cd11293   81 GRAVQVRVVQGKEPPHFLALF 101
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 676-771 3.51e-47

Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200447 [Multi-domain]  Cd Length: 99  Bit Score: 162.85  E-value: 3.51e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966412 676 RLFECSNKTGRFLVTEVTDFTQEDLSPGDVMLLDTWDQVFLWIGAEANATEKKGALSTAQEYLVTHPSGRD-PDTPILII 754
Cdd:cd11291    3 RLFRCSNESGFFKVEEISDFSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYIETDPLGRSkPRTPIYLV 82

                         90
                 ....*....|....*..
gi 568966412 755 KQGFEPPTFTGWFLAWD 771
Cdd:cd11291   83 KQGNEPPTFTGYFHAWD 99
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 306-404 2.62e-41

Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200448  Cd Length: 98  Bit Score: 146.24  E-value: 2.62e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966412 306 KSSIMLYHVSDTAGQLSVTEVATRPLVQDLLNHDDCYILDQsGTKIYVWKGKGATKVEKQAAMSKALDFIKMKGYPSSTN 385
Cdd:cd11292    1 AEQKKLYKVSDASGKLKLTEVAEGSLNQEMLDSEDCYILDC-GSEIFVWVGKGASLDERKAALKNAEEFLRKKKRPPYTQ 79

                         90
                 ....*....|....*....
gi 568966412 386 VETVNDGAESAMFKQLFQK 404
Cdd:cd11292   80 VTRVTEGGESALFKSKFAN 98
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 162-282 5.65e-35

Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200445  Cd Length: 92  Bit Score: 128.12  E-value: 5.65e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966412 162 VKRLLHVKGKRNIQATEVsltrecpgcpvlppwhlrlprtaltahtqvEMSWDSFNRGDVFLLDLGMVIIQWNGPESNSG 241
Cdd:cd11289    1 KPRLLHVKGRRNVRAREV------------------------------ELSWSSLNSGDVFILDLGSTIYQWNGSKSNRF 50

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 568966412 242 ERLKAMLLAKDIRDRERGGRAEIGVIEGDKEAASPGLMTVL 282
Cdd:cd11289   51 EKAKAMQLAQGIRDERRLGRAKVIVLDEGDTNESPEFWKVL 91
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 569-658 2.99e-30

Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200444  Cd Length: 92  Bit Score: 114.64  E-value: 2.99e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966412 569 PPVRLFQIHGNDKSNTKAVEVSASASSLNSNDVFLLRTQAEHYLWYGKGSSGDERAMAKELVDLLCDG-NADTVAEGQEP 647
Cdd:cd11288    1 SPTRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVASFLKPKaSLQEVAEGSEP 80

                         90
                 ....*....|.
gi 568966412 648 PEFWDLLGGKT 658
Cdd:cd11288   81 DEFWEALGGKS 91
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 323-405 1.78e-24

Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and actin-binding. Both intra- and extracellular domains.


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 98.13  E-value: 1.78e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966412   323 VTEVATRPLVQDLLNHDDCYILDqSGTKIYVWKGKGATKVEKQAAMSKALDFIKMKGyPSSTNVETVNDGAESAMFKQLF 402
Cdd:smart00262  10 NVRVPEVPFSQGSLNSGDCYILD-TGSEIYVWVGKKSSQDEKKKAAELAVELDDTLG-PGPVQVRVVDEGKEPPEFWSLF 87


                   ...
gi 568966412   403 QKW 405
Cdd:smart00262  88 GGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 679-770 4.45e-24

Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and actin-binding. Both intra- and extracellular domains.


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 96.98  E-value: 4.45e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966412   679 ECSNKTGRFLVTEVT-DFTQEDLSPGDVMLLDTWDQVFLWIGAEANATEKKGALSTAQEYLVTHPSGRdpdTPILIIKQG 757
Cdd:smart00262   1 FLVRVKGKRNVRVPEvPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGP---VQVRVVDEG 77

                           90
                   ....*....|...
gi 568966412   758 FEPPTFTGWFLAW 770
Cdd:smart00262  78 KEPPEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 457-551 1.09e-23

Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and actin-binding. Both intra- and extracellular domains.


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 95.82  E-value: 1.09e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966412   457 EVWRIENLELVPVEYQ--WHGFFYGGDCYLVLYTYDVngkphyilYIWQGRHASRDELAASAYRAVEVDQQFDGAPVQVR 534
Cdd:smart00262   1 FLVRVKGKRNVRVPEVpfSQGSLNSGDCYILDTGSEI--------YVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVR 72

                           90
                   ....*....|....*...
gi 568966412   535 -VSMGKEPRHFMAIFKGK 551
Cdd:smart00262  73 vVDEGKEPPEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 48-138 3.12e-19

Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and actin-binding. Both intra- and extracellular domains.


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 83.11  E-value: 3.12e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966412    48 WRIE---KMELALVPLSaHGNFYEGDCYIVLSTrrvgsllsQNIHFWIGKDSSQDEQSCAAIYTTQLDDYLGGSPVQHRE 124
Cdd:smart00262   3 VRVKgkrNVRVPEVPFS-QGSLNSGDCYILDTG--------SEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVRV 73

                           90
                   ....*....|....*
gi 568966412   125 V-QYHESDTFRGYFK 138
Cdd:smart00262  74 VdEGKEPPEFWSLFG 88
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 574-657 1.23e-17

Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and actin-binding. Both intra- and extracellular domains.


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 78.49  E-value: 1.23e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966412   574 FQIHGNDKSNTKAVEVSASASSLNSNDVFLLRTQAEHYLWYGKGSSGDERAMAKELVDLLCDGNAD------TVAEGQEP 647
Cdd:smart00262   1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPgpvqvrVVDEGKEP 80

                           90
                   ....*....|
gi 568966412   648 PEFWDLLGGK 657
Cdd:smart00262  81 PEFWSLFGGW 90
Gelsolin pfam00626
Gelsolin repeat;
209-275 2.61e-15

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 71.57  E-value: 2.61e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568966412  209 VEMSWDSFNRGDVFLLDLGMVIIQWNGPESNSGERLKAMLLAKDIRDRERGGRAEIGVIEGDKEAAS 275
Cdd:pfam00626   8 VPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDERFPLPEVIRVPQGKEPAR 74
Gelsolin pfam00626
Gelsolin repeat;
52-134 2.99e-15

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 71.18  E-value: 2.99e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966412   52 KMELALVPLSAHGNFYEGDCYIVLSTrrvgsllsQNIHFWIGKDSSQDEQSCAAIYTTQLDD-YLGGSPVQHREVQYHES 130
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNG--------FTIFLWVGKGSSLLEKLFAALLAAQLDDdERFPLPEVIRVPQGKEP 72


                  ....
gi 568966412  131 DTFR 134
Cdd:pfam00626  73 ARFL 76
Gelsolin pfam00626
Gelsolin repeat;
322-399 1.34e-14

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 69.26  E-value: 1.34e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568966412  322 SVTEVATRPLVQDLLNHDDCYILDQsGTKIYVWKGKGATKVEKQAAMSKALDFIKMKgYPSSTNVETVNDGAESAMFK 399
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDN-GFTIFLWVGKGSSLLEKLFAALLAAQLDDDE-RFPLPEVIRVPQGKEPARFL 76
Gelsolin pfam00626
Gelsolin repeat;
686-763 1.34e-14

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 69.26  E-value: 1.34e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568966412  686 RFLVTEVTDFTQEDLSPGDVMLLDTWDQVFLWIGAEANATEKKGALSTAQEYLVTHpsgRDPDTPILIIKQGFEPPTF 763
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDE---RFPLPEVIRVPQGKEPARF 75
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 208-274 4.37e-14

Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and actin-binding. Both intra- and extracellular domains.


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 68.47  E-value: 4.37e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568966412   208 QVEMSWDSFNRGDVFLLDLGMVIIQWNGPESNSGERLKAMLLAKDIRDRERGGRAEIGVIEGDKEAA 274
Cdd:smart00262  15 EVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVRVVDEGKEPP 81
VHP pfam02209
Villin headpiece domain;
843-878 4.98e-14

Villin headpiece domain;


Pssm-ID: 460493  Cd Length: 36  Bit Score: 66.63  E-value: 4.98e-14
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 568966412  843 YLSEQDFVSVFGITRGQFTALPGWKQLQLKKERGLF 878
Cdd:pfam02209   1 YLSDEDFEEVFGMSREEFYKLPKWKQNNLKKKAGLF 36
Gelsolin pfam00626
Gelsolin repeat;
463-545 8.16e-14

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 67.33  E-value: 8.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966412  463 NLELVPVEYQWHGFFYGGDCYLVLYTYDvngkphyiLYIWQGRHASRDELAASAYRAVEVDQQF-DGAPVQVRVSMGKEP 541
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNGFT--------IFLWVGKGSSLLEKLFAALLAAQLDDDErFPLPEVIRVPQGKEP 72


                  ....
gi 568966412  542 RHFM 545
Cdd:pfam00626  73 ARFL 76
VHP smart00153
Villin headpiece domain;
843-878 2.30e-13

Villin headpiece domain;


Pssm-ID: 128458  Cd Length: 36  Bit Score: 64.65  E-value: 2.30e-13
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 568966412   843 YLSEQDFVSVFGITRGQFTALPGWKQLQLKKERGLF 878
Cdd:smart00153   1 YLSDEDFEEVFGMTREEFYKLPLWKQNQLKKKKGLF 36
 
Name Accession Description Interval E-value
gelsolin_S1_like cd11290
Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; ...
 36-147 7.56e-57

Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin_like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200446  Cd Length: 113  Bit Score: 190.51  E-value: 7.56e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966412  36 FRAVSNDPRIITWRIEKMELALVPLSAHGNFYEGDCYIVLSTRRVGS-LLSQNIHFWIGKDSSQDEQSCAAIYTTQLDDY 114
Cdd:cd11290    1 FEGVGQKPGLQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDPSgSLSYDIHYWLGKEASQDEAGAAAIKAVELDDY 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 568966412 115 LGGSPVQHREVQYHESDTFRGYFKQGIIYKKGG 147
Cdd:cd11290   81 LGGRPVQHREVQGHESEEFLSYFKKGIIYIEGG 113
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
 448-548 3.97e-52

Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200449  Cd Length: 101  Bit Score: 177.08  E-value: 3.97e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966412 448 MVDDGKGQVEVWRIENLELVPVEYQWHGFFYGGDCYLVLYTYDVNGKPHYILYIWQGRHASRDELAASAYRAVEVDQQFD 527
Cdd:cd11293    1 MYDDGSGKVEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQGGGKEEHILYFWQGRHSSQDERAAAALLTVELDEELK 80

                         90       100
                 ....*....|....*....|.
gi 568966412 528 GAPVQVRVSMGKEPRHFMAIF 548
Cdd:cd11293   81 GRAVQVRVVQGKEPPHFLALF 101
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 676-771 3.51e-47

Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200447 [Multi-domain]  Cd Length: 99  Bit Score: 162.85  E-value: 3.51e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966412 676 RLFECSNKTGRFLVTEVTDFTQEDLSPGDVMLLDTWDQVFLWIGAEANATEKKGALSTAQEYLVTHPSGRD-PDTPILII 754
Cdd:cd11291    3 RLFRCSNESGFFKVEEISDFSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYIETDPLGRSkPRTPIYLV 82

                         90
                 ....*....|....*..
gi 568966412 755 KQGFEPPTFTGWFLAWD 771
Cdd:cd11291   83 KQGNEPPTFTGYFHAWD 99
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 306-404 2.62e-41

Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200448  Cd Length: 98  Bit Score: 146.24  E-value: 2.62e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966412 306 KSSIMLYHVSDTAGQLSVTEVATRPLVQDLLNHDDCYILDQsGTKIYVWKGKGATKVEKQAAMSKALDFIKMKGYPSSTN 385
Cdd:cd11292    1 AEQKKLYKVSDASGKLKLTEVAEGSLNQEMLDSEDCYILDC-GSEIFVWVGKGASLDERKAALKNAEEFLRKKKRPPYTQ 79

                         90
                 ....*....|....*....
gi 568966412 386 VETVNDGAESAMFKQLFQK 404
Cdd:cd11292   80 VTRVTEGGESALFKSKFAN 98
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 162-282 5.65e-35

Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200445  Cd Length: 92  Bit Score: 128.12  E-value: 5.65e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966412 162 VKRLLHVKGKRNIQATEVsltrecpgcpvlppwhlrlprtaltahtqvEMSWDSFNRGDVFLLDLGMVIIQWNGPESNSG 241
Cdd:cd11289    1 KPRLLHVKGRRNVRAREV------------------------------ELSWSSLNSGDVFILDLGSTIYQWNGSKSNRF 50

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 568966412 242 ERLKAMLLAKDIRDRERGGRAEIGVIEGDKEAASPGLMTVL 282
Cdd:cd11289   51 EKAKAMQLAQGIRDERRLGRAKVIVLDEGDTNESPEFWKVL 91
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 569-658 2.99e-30

Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200444  Cd Length: 92  Bit Score: 114.64  E-value: 2.99e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966412 569 PPVRLFQIHGNDKSNTKAVEVSASASSLNSNDVFLLRTQAEHYLWYGKGSSGDERAMAKELVDLLCDG-NADTVAEGQEP 647
Cdd:cd11288    1 SPTRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVASFLKPKaSLQEVAEGSEP 80

                         90
                 ....*....|.
gi 568966412 648 PEFWDLLGGKT 658
Cdd:cd11288   81 DEFWEALGGKS 91
gelsolin_S1_like cd11290
Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; ...
 456-558 9.69e-29

Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin_like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200446  Cd Length: 113  Bit Score: 111.16  E-value: 9.69e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966412 456 VEVWRIENLELVPVEYQWHGFFYGGDCYLVLYTY-DVNGKPHYILYIWQGRHASRDELAASAYRAVEVDQQFDGAPVQVR 534
Cdd:cd11290   10 LQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTlDPSGSLSYDIHYWLGKEASQDEAGAAAIKAVELDDYLGGRPVQHR 89

                         90       100
                 ....*....|....*....|....
gi 568966412 535 VSMGKEPRHFMAIFKgKLVIYEGG 558
Cdd:cd11290   90 EVQGHESEEFLSYFK-KGIIYIEG 112
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 323-405 1.78e-24

Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and actin-binding. Both intra- and extracellular domains.


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 98.13  E-value: 1.78e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966412   323 VTEVATRPLVQDLLNHDDCYILDqSGTKIYVWKGKGATKVEKQAAMSKALDFIKMKGyPSSTNVETVNDGAESAMFKQLF 402
Cdd:smart00262  10 NVRVPEVPFSQGSLNSGDCYILD-TGSEIYVWVGKKSSQDEKKKAAELAVELDDTLG-PGPVQVRVVDEGKEPPEFWSLF 87


                   ...
gi 568966412   403 QKW 405
Cdd:smart00262  88 GGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 679-770 4.45e-24

Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and actin-binding. Both intra- and extracellular domains.


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 96.98  E-value: 4.45e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966412   679 ECSNKTGRFLVTEVT-DFTQEDLSPGDVMLLDTWDQVFLWIGAEANATEKKGALSTAQEYLVTHPSGRdpdTPILIIKQG 757
Cdd:smart00262   1 FLVRVKGKRNVRVPEvPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGP---VQVRVVDEG 77

                           90
                   ....*....|...
gi 568966412   758 FEPPTFTGWFLAW 770
Cdd:smart00262  78 KEPPEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 457-551 1.09e-23

Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and actin-binding. Both intra- and extracellular domains.


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 95.82  E-value: 1.09e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966412   457 EVWRIENLELVPVEYQ--WHGFFYGGDCYLVLYTYDVngkphyilYIWQGRHASRDELAASAYRAVEVDQQFDGAPVQVR 534
Cdd:smart00262   1 FLVRVKGKRNVRVPEVpfSQGSLNSGDCYILDTGSEI--------YVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVR 72

                           90
                   ....*....|....*...
gi 568966412   535 -VSMGKEPRHFMAIFKGK 551
Cdd:smart00262  73 vVDEGKEPPEFWSLFGGW 90
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
 48-137 4.07e-22

Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200449  Cd Length: 101  Bit Score: 91.56  E-value: 4.07e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966412  48 WRIEKMELALVPLSAHGNFYEGDCYIVLSTRRVGSLLSQNIHFWIGKDSSQDEQSCAAIYTTQLDDYLGGSPVQHREVQY 127
Cdd:cd11293   12 WRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQGGGKEEHILYFWQGRHSSQDERAAAALLTVELDEELKGRAVQVRVVQG 91

                         90
                 ....*....|
gi 568966412 128 HESDTFRGYF 137
Cdd:cd11293   92 KEPPHFLALF 101
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 673-767 1.14e-21

Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200448  Cd Length: 98  Bit Score: 90.39  E-value: 1.14e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966412 673 VQVRLFECSNKTGRFLVTEVTD--FTQEDLSPGDVMLLDTWDQVFLWIGAEANATEKKGALSTAQEYLvtHPSGRDPDTP 750
Cdd:cd11292    2 EQKKLYKVSDASGKLKLTEVAEgsLNQEMLDSEDCYILDCGSEIFVWVGKGASLDERKAALKNAEEFL--RKKKRPPYTQ 79

                         90
                 ....*....|....*..
gi 568966412 751 ILIIKQGFEPPTFTGWF 767
Cdd:cd11292   80 VTRVTEGGESALFKSKF 96
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 48-138 3.12e-19

Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and actin-binding. Both intra- and extracellular domains.


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 83.11  E-value: 3.12e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966412    48 WRIE---KMELALVPLSaHGNFYEGDCYIVLSTrrvgsllsQNIHFWIGKDSSQDEQSCAAIYTTQLDDYLGGSPVQHRE 124
Cdd:smart00262   3 VRVKgkrNVRVPEVPFS-QGSLNSGDCYILDTG--------SEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVRV 73

                           90
                   ....*....|....*
gi 568966412   125 V-QYHESDTFRGYFK 138
Cdd:smart00262  74 VdEGKEPPEFWSLFG 88
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 574-657 1.23e-17

Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and actin-binding. Both intra- and extracellular domains.


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 78.49  E-value: 1.23e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966412   574 FQIHGNDKSNTKAVEVSASASSLNSNDVFLLRTQAEHYLWYGKGSSGDERAMAKELVDLLCDGNAD------TVAEGQEP 647
Cdd:smart00262   1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPgpvqvrVVDEGKEP 80

                           90
                   ....*....|
gi 568966412   648 PEFWDLLGGK 657
Cdd:smart00262  81 PEFWSLFGGW 90
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 311-406 3.14e-17

Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200447 [Multi-domain]  Cd Length: 99  Bit Score: 77.72  E-value: 3.14e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966412 311 LYHVSDTAGQLSVTEVAtrPLVQDLLNHDDCYILDqSGTKIYVWKGKGATKVEKQAAMSKALDFIKMKGYPSS---TNVE 387
Cdd:cd11291    4 LFRCSNESGFFKVEEIS--DFSQDDLDTDDIMLLD-TGDEVFVWVGSESSDEEKKEALTSAKKYIETDPLGRSkprTPIY 80

                         90
                 ....*....|....*....
gi 568966412 388 TVNDGAESAMFKQLFQKWS 406
Cdd:cd11291   81 LVKQGNEPPTFTGYFHAWD 99
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 458-548 5.47e-17

Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200436  Cd Length: 88  Bit Score: 76.64  E-value: 5.47e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966412 458 VWRIENLELVPVEYQW--HGFFYGGDCYLVLYTYDVngkphyilYIWQGRHASRDELAASAYRAVEVDQQFDGAPVQVRV 535
Cdd:cd11280    4 LYRVRGSKAIEIEEVPlaSSSLDSDDVFVLDTGSEI--------YIWQGRASSQAELAAAALLAKELDEERKGKPEIVRI 75

                         90
                 ....*....|...
gi 568966412 536 SMGKEPRHFMAIF 548
Cdd:cd11280   76 RQGQEPREFWSLF 88
Gelsolin pfam00626
Gelsolin repeat;
209-275 2.61e-15

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 71.57  E-value: 2.61e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568966412  209 VEMSWDSFNRGDVFLLDLGMVIIQWNGPESNSGERLKAMLLAKDIRDRERGGRAEIGVIEGDKEAAS 275
Cdd:pfam00626   8 VPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDERFPLPEVIRVPQGKEPAR 74
Gelsolin pfam00626
Gelsolin repeat;
52-134 2.99e-15

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 71.18  E-value: 2.99e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966412   52 KMELALVPLSAHGNFYEGDCYIVLSTrrvgsllsQNIHFWIGKDSSQDEQSCAAIYTTQLDD-YLGGSPVQHREVQYHES 130
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNG--------FTIFLWVGKGSSLLEKLFAALLAAQLDDdERFPLPEVIRVPQGKEP 72


                  ....
gi 568966412  131 DTFR 134
Cdd:pfam00626  73 ARFL 76
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 674-767 1.22e-14

Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200436  Cd Length: 88  Bit Score: 70.09  E-value: 1.22e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966412 674 QVRLFECSNKTgRFLVTEVTDFTqEDLSPGDVMLLDTWDQVFLWIGAEANATEKKGALSTAQEYLvthpSGRDPDTPILI 753
Cdd:cd11280    1 PPRLYRVRGSK-AIEIEEVPLAS-SSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKELD----EERKGKPEIVR 74

                         90
                 ....*....|....
gi 568966412 754 IKQGFEPPTFTGWF 767
Cdd:cd11280   75 IRQGQEPREFWSLF 88
Gelsolin pfam00626
Gelsolin repeat;
322-399 1.34e-14

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 69.26  E-value: 1.34e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568966412  322 SVTEVATRPLVQDLLNHDDCYILDQsGTKIYVWKGKGATKVEKQAAMSKALDFIKMKgYPSSTNVETVNDGAESAMFK 399
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDN-GFTIFLWVGKGSSLLEKLFAALLAAQLDDDE-RFPLPEVIRVPQGKEPARFL 76
Gelsolin pfam00626
Gelsolin repeat;
686-763 1.34e-14

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 69.26  E-value: 1.34e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568966412  686 RFLVTEVTDFTQEDLSPGDVMLLDTWDQVFLWIGAEANATEKKGALSTAQEYLVTHpsgRDPDTPILIIKQGFEPPTF 763
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDE---RFPLPEVIRVPQGKEPARF 75
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 42-137 3.10e-14

Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200436  Cd Length: 88  Bit Score: 68.93  E-value: 3.10e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966412  42 DPRIitWRIEK---MELALVPLsAHGNFYEGDCYIVLSTRrvgsllsqNIHFWIGKDSSQDEQSCAAIYTTQLDDYLGGS 118
Cdd:cd11280    1 PPRL--YRVRGskaIEIEEVPL-ASSSLDSDDVFVLDTGS--------EIYIWQGRASSQAELAAAALLAKELDEERKGK 69

                         90
                 ....*....|....*....
gi 568966412 119 PVQHREVQYHESDTFRGYF 137
Cdd:cd11280   70 PEIVRIRQGQEPREFWSLF 88
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 208-274 4.37e-14

Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and actin-binding. Both intra- and extracellular domains.


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 68.47  E-value: 4.37e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568966412   208 QVEMSWDSFNRGDVFLLDLGMVIIQWNGPESNSGERLKAMLLAKDIRDRERGGRAEIGVIEGDKEAA 274
Cdd:smart00262  15 EVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVRVVDEGKEPP 81
VHP pfam02209
Villin headpiece domain;
843-878 4.98e-14

Villin headpiece domain;


Pssm-ID: 460493  Cd Length: 36  Bit Score: 66.63  E-value: 4.98e-14
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 568966412  843 YLSEQDFVSVFGITRGQFTALPGWKQLQLKKERGLF 878
Cdd:pfam02209   1 YLSDEDFEEVFGMSREEFYKLPKWKQNNLKKKAGLF 36
Gelsolin pfam00626
Gelsolin repeat;
463-545 8.16e-14

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 67.33  E-value: 8.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966412  463 NLELVPVEYQWHGFFYGGDCYLVLYTYDvngkphyiLYIWQGRHASRDELAASAYRAVEVDQQF-DGAPVQVRVSMGKEP 541
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNGFT--------IFLWVGKGSSLLEKLFAALLAAQLDDDErFPLPEVIRVPQGKEP 72


                  ....
gi 568966412  542 RHFM 545
Cdd:pfam00626  73 ARFL 76
VHP smart00153
Villin headpiece domain;
843-878 2.30e-13

Villin headpiece domain;


Pssm-ID: 128458  Cd Length: 36  Bit Score: 64.65  E-value: 2.30e-13
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 568966412   843 YLSEQDFVSVFGITRGQFTALPGWKQLQLKKERGLF 878
Cdd:smart00153   1 YLSDEDFEEVFGMTREEFYKLPLWKQNQLKKKKGLF 36
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 310-405 2.97e-10

Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200445  Cd Length: 92  Bit Score: 57.63  E-value: 2.97e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966412 310 MLYHVSdtaG--QLSVTEVatrPLVQDLLNHDDCYILDqSGTKIYVWKGKGATKVEKqaamSKALDF---IKMKGYPSST 384
Cdd:cd11289    3 RLLHVK---GrrNVRAREV---ELSWSSLNSGDVFILD-LGSTIYQWNGSKSNRFEK----AKAMQLaqgIRDERRLGRA 71

                         90       100
                 ....*....|....*....|.
gi 568966412 385 NVETVNDGAESAMFKQLFQKW 405
Cdd:cd11289   72 KVIVLDEGDTNESPEFWKVLG 92
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 570-654 3.37e-10

Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200436  Cd Length: 88  Bit Score: 57.38  E-value: 3.37e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966412 570 PVRLFQIHGndKSNTKAVEVSASASSLNSNDVFLLRTQAEHYLWYGKGSSGDERA----MAKELVDLLcDGNADTV--AE 643
Cdd:cd11280    1 PPRLYRVRG--SKAIEIEEVPLASSSLDSDDVFVLDTGSEIYIWQGRASSQAELAaaalLAKELDEER-KGKPEIVriRQ 77

                         90
                 ....*....|.
gi 568966412 644 GQEPPEFWDLL 654
Cdd:cd11280   78 GQEPREFWSLF 88
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 307-398 4.86e-10

Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200444  Cd Length: 92  Bit Score: 56.86  E-value: 4.86e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966412 307 SSIMLYHVSDTagqlsvTEVATRpLVQD-----LLNHDDCYILdQSGTKIYVWKGKGATKVEKQAAmSKALDFIKmkgyp 381
Cdd:cd11288    1 SPTRLFQVRGN------GSGNTR-AVEVdadasSLNSNDVFVL-KTPSSVYLWVGKGSSEDERELA-KDVASFLK----- 66

                         90
                 ....*....|....*..
gi 568966412 382 SSTNVETVNDGAESAMF 398
Cdd:cd11288   67 PKASLQEVAEGSEPDEF 83
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 311-402 2.61e-09

Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200436  Cd Length: 88  Bit Score: 54.68  E-value: 2.61e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966412 311 LYHVSDtAGQLSVTEVATRPlvqDLLNHDDCYILDqSGTKIYVWKGKGATKVEKQAA--MSKALDfikmKGYPSSTNVET 388
Cdd:cd11280    4 LYRVRG-SKAIEIEEVPLAS---SSLDSDDVFVLD-TGSEIYIWQGRASSQAELAAAalLAKELD----EERKGKPEIVR 74

                         90
                 ....*....|....
gi 568966412 389 VNDGAESAMFKQLF 402
Cdd:cd11280   75 IRQGQEPREFWSLF 88
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 570-655 1.03e-07

Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200445  Cd Length: 92  Bit Score: 50.31  E-value: 1.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966412 570 PVRLFQIHGndKSNTKAVEVSASASSLNSNDVFLLRTQAEHYLWYGKGSSGDERAMAKELVDLLCD----GNADT----V 641
Cdd:cd11289    1 KPRLLHVKG--RRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDerrlGRAKVivldE 78

                         90
                 ....*....|....
gi 568966412 642 AEGQEPPEFWDLLG 655
Cdd:cd11289   79 GDTNESPEFWKVLG 92
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 215-274 4.41e-06

Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200436  Cd Length: 88  Bit Score: 45.82  E-value: 4.41e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966412 215 SFNRGDVFLLDLGMVIIQWNGPESNSGERLKAMLLAKDIrDRERGGRAEIGVIEGDKEAA 274
Cdd:cd11280   24 SLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKEL-DEERKGKPEIVRIRQGQEPR 82
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 674-763 7.18e-04

Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200445  Cd Length: 92  Bit Score: 39.53  E-value: 7.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966412 674 QVRLFECSNKTgRFLVTEVtDFTQEDLSPGDVMLLDTWDQVFLWIGAEANATEKKGALSTAQeYLVTHPSGRDPDTPILI 753
Cdd:cd11289    1 KPRLLHVKGRR-NVRAREV-ELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQ-GIRDERRLGRAKVIVLD 77

                         90
                 ....*....|
gi 568966412 754 IKQGFEPPTF 763
Cdd:cd11289   78 EGDTNESPEF 87
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 704-763 9.03e-04

Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200444  Cd Length: 92  Bit Score: 39.14  E-value: 9.03e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568966412 704 DVMLLDTWDQVFLWIGAEANATEKKGALSTAQEYlvthpsgrDPDTPILIIKQGFEPPTF 763
Cdd:cd11288   32 DVFVLKTPSSVYLWVGKGSSEDERELAKDVASFL--------KPKASLQEVAEGSEPDEF 83
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 600-650 2.32e-03

Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200448  Cd Length: 98  Bit Score: 38.00  E-value: 2.32e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568966412 600 DVFLLRTQAEHYLWYGKGSSGDERAMAKEL-VDLL--CDGNADT----VAEGQEPPEF 650
Cdd:cd11292   35 DCYILDCGSEIFVWVGKGASLDERKAALKNaEEFLrkKKRPPYTqvtrVTEGGESALF 92
 
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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