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Conserved domains on  [gi|157951655|ref|NP_033765|]
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advillin [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; ...
 7-118 1.34e-56

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: 189.36  E-value: 1.34e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951655   7 FRAVSNDPRIITWRIEKMELALVPLSAHGNFYEGDCYIVLSTRRVGS-LLSQNIHFWIGKDSSQDEQSCAAIYTTQLDDY 85
Cdd:cd11290    1 FEGVGQKPGLQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDPSgSLSYDIHYWLGKEASQDEAGAAAIKAVELDDY 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 157951655  86 LGGSPVQHREVQYHESDTFRGYFKQGIIYKKGG 118
Cdd:cd11290   81 LGGRPVQHREVQGHESEEFLSYFKKGIIYIEGG 113
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
 389-489 5.85e-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: 175.92  E-value: 5.85e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951655 389 MVDDGKGQVEVWRIENLELVPVEYQWHGFFYGGDCYLVLYTYDVNGKPHYILYIWQGRHASRDELAASAYRAVEVDQQFD 468
Cdd:cd11293    1 MYDDGSGKVEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQGGGKEEHILYFWQGRHSSQDERAAAALLTVELDEELK 80

                         90       100
                 ....*....|....*....|.
gi 157951655 469 GAPVQVRVSMGKEPRHFMAIF 489
Cdd:cd11293   81 GRAVQVRVVQGKEPPHFLALF 101
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 617-712 4.64e-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: 162.47  E-value: 4.64e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951655 617 RLFECSNKTGRFLVTEVTDFTQEDLSPGDVMLLDTWDQVFLWIGAEANATEKKGALSTAQEYLVTHPSGRD-PDTPILII 695
Cdd:cd11291    3 RLFRCSNESGFFKVEEISDFSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYIETDPLGRSkPRTPIYLV 82

                         90
                 ....*....|....*..
gi 157951655 696 KQGFEPPTFTGWFLAWD 712
Cdd:cd11291   83 KQGNEPPTFTGYFHAWD 99
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 247-345 4.02e-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: 145.47  E-value: 4.02e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951655 247 KSSIMLYHVSDTAGQLSVTEVATRPLVQDLLNHDDCYILDQsGTKIYVWKGKGATKVEKQAAMSKALDFIKMKGYPSSTN 326
Cdd:cd11292    1 AEQKKLYKVSDASGKLKLTEVAEGSLNQEMLDSEDCYILDC-GSEIFVWVGKGASLDERKAALKNAEEFLRKKKRPPYTQ 79

                         90
                 ....*....|....*....
gi 157951655 327 VETVNDGAESAMFKQLFQK 345
Cdd:cd11292   80 VTRVTEGGESALFKSKFAN 98
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 133-223 2.13e-40

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: 143.53  E-value: 2.13e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951655 133 VKRLLHVKGKRNIQATEVEMSWDSFNRGDVFLLDLGMVIIQWNGPESNSGERLKAMLLAKDIRDRERGGRAEIGVIEGDK 212
Cdd:cd11289    1 KPRLLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKVIVLDEGD 80

                         90
                 ....*....|.
gi 157951655 213 EAASPGLMTVL 223
Cdd:cd11289   81 TNESPEFWKVL 91
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 510-599 3.47e-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: 114.25  E-value: 3.47e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951655 510 PPVRLFQIHGNDKSNTKAVEVSASASSLNSNDVFLLRTQAEHYLWYGKGSSGDERAMAKELVDLLCDG-NADTVAEGQEP 588
Cdd:cd11288    1 SPTRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVASFLKPKaSLQEVAEGSEP 80

                         90
                 ....*....|.
gi 157951655 589 PEFWDLLGGKT 599
Cdd:cd11288   81 DEFWEALGGKS 91
VHP pfam02209
Villin headpiece domain;
784-819 7.01e-14

Villin headpiece domain;


:

Pssm-ID: 460493  Cd Length: 36  Bit Score: 65.86  E-value: 7.01e-14
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 157951655  784 YLSEQDFVSVFGITRGQFTALPGWKQLQLKKERGLF 819
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; ...
 7-118 1.34e-56

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: 189.36  E-value: 1.34e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951655   7 FRAVSNDPRIITWRIEKMELALVPLSAHGNFYEGDCYIVLSTRRVGS-LLSQNIHFWIGKDSSQDEQSCAAIYTTQLDDY 85
Cdd:cd11290    1 FEGVGQKPGLQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDPSgSLSYDIHYWLGKEASQDEAGAAAIKAVELDDY 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 157951655  86 LGGSPVQHREVQYHESDTFRGYFKQGIIYKKGG 118
Cdd:cd11290   81 LGGRPVQHREVQGHESEEFLSYFKKGIIYIEGG 113
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
 389-489 5.85e-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: 175.92  E-value: 5.85e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951655 389 MVDDGKGQVEVWRIENLELVPVEYQWHGFFYGGDCYLVLYTYDVNGKPHYILYIWQGRHASRDELAASAYRAVEVDQQFD 468
Cdd:cd11293    1 MYDDGSGKVEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQGGGKEEHILYFWQGRHSSQDERAAAALLTVELDEELK 80

                         90       100
                 ....*....|....*....|.
gi 157951655 469 GAPVQVRVSMGKEPRHFMAIF 489
Cdd:cd11293   81 GRAVQVRVVQGKEPPHFLALF 101
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 617-712 4.64e-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: 162.47  E-value: 4.64e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951655 617 RLFECSNKTGRFLVTEVTDFTQEDLSPGDVMLLDTWDQVFLWIGAEANATEKKGALSTAQEYLVTHPSGRD-PDTPILII 695
Cdd:cd11291    3 RLFRCSNESGFFKVEEISDFSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYIETDPLGRSkPRTPIYLV 82

                         90
                 ....*....|....*..
gi 157951655 696 KQGFEPPTFTGWFLAWD 712
Cdd:cd11291   83 KQGNEPPTFTGYFHAWD 99
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 247-345 4.02e-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: 145.47  E-value: 4.02e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951655 247 KSSIMLYHVSDTAGQLSVTEVATRPLVQDLLNHDDCYILDQsGTKIYVWKGKGATKVEKQAAMSKALDFIKMKGYPSSTN 326
Cdd:cd11292    1 AEQKKLYKVSDASGKLKLTEVAEGSLNQEMLDSEDCYILDC-GSEIFVWVGKGASLDERKAALKNAEEFLRKKKRPPYTQ 79

                         90
                 ....*....|....*....
gi 157951655 327 VETVNDGAESAMFKQLFQK 345
Cdd:cd11292   80 VTRVTEGGESALFKSKFAN 98
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 133-223 2.13e-40

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: 143.53  E-value: 2.13e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951655 133 VKRLLHVKGKRNIQATEVEMSWDSFNRGDVFLLDLGMVIIQWNGPESNSGERLKAMLLAKDIRDRERGGRAEIGVIEGDK 212
Cdd:cd11289    1 KPRLLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKVIVLDEGD 80

                         90
                 ....*....|.
gi 157951655 213 EAASPGLMTVL 223
Cdd:cd11289   81 TNESPEFWKVL 91
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 510-599 3.47e-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: 114.25  E-value: 3.47e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951655 510 PPVRLFQIHGNDKSNTKAVEVSASASSLNSNDVFLLRTQAEHYLWYGKGSSGDERAMAKELVDLLCDG-NADTVAEGQEP 588
Cdd:cd11288    1 SPTRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVASFLKPKaSLQEVAEGSEP 80

                         90
                 ....*....|.
gi 157951655 589 PEFWDLLGGKT 599
Cdd:cd11288   81 DEFWEALGGKS 91
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 264-346 2.67e-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: 97.36  E-value: 2.67e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951655   264 VTEVATRPLVQDLLNHDDCYILDqSGTKIYVWKGKGATKVEKQAAMSKALDFIKMKGyPSSTNVETVNDGAESAMFKQLF 343
Cdd:smart00262  10 NVRVPEVPFSQGSLNSGDCYILD-TGSEIYVWVGKKSSQDEKKKAAELAVELDDTLG-PGPVQVRVVDEGKEPPEFWSLF 87


                   ...
gi 157951655   344 QKW 346
Cdd:smart00262  88 GGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 620-711 6.22e-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: 96.21  E-value: 6.22e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951655   620 ECSNKTGRFLVTEVT-DFTQEDLSPGDVMLLDTWDQVFLWIGAEANATEKKGALSTAQEYLVTHPSGRdpdTPILIIKQG 698
Cdd:smart00262   1 FLVRVKGKRNVRVPEvPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGP---VQVRVVDEG 77

                           90
                   ....*....|...
gi 157951655   699 FEPPTFTGWFLAW 711
Cdd:smart00262  78 KEPPEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 398-492 1.81e-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: 95.05  E-value: 1.81e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951655   398 EVWRIENLELVPVEYQ--WHGFFYGGDCYLVLYTYDVngkphyilYIWQGRHASRDELAASAYRAVEVDQQFDGAPVQVR 475
Cdd:smart00262   1 FLVRVKGKRNVRVPEVpfSQGSLNSGDCYILDTGSEI--------YVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVR 72

                           90
                   ....*....|....*...
gi 157951655   476 -VSMGKEPRHFMAIFKGK 492
Cdd:smart00262  73 vVDEGKEPPEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 135-215 4.07e-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: 82.73  E-value: 4.07e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951655   135 RLLHVKGKRNIQATEVEMSWDSFNRGDVFLLDLGMVIIQWNGPESNSGERLKAMLLAKDIRDRERGGRAEIGVIEGDKEA 214
Cdd:smart00262   1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVRVVDEGKEP 80


                   .
gi 157951655   215 A 215
Cdd:smart00262  81 P 81
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 19-109 4.90e-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: 82.34  E-value: 4.90e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951655    19 WRIE---KMELALVPLSaHGNFYEGDCYIVLSTrrvgsllsQNIHFWIGKDSSQDEQSCAAIYTTQLDDYLGGSPVQHRE 95
Cdd:smart00262   3 VRVKgkrNVRVPEVPFS-QGSLNSGDCYILDTG--------SEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVRV 73

                           90
                   ....*....|....*
gi 157951655    96 V-QYHESDTFRGYFK 109
Cdd:smart00262  74 VdEGKEPPEFWSLFG 88
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 515-598 1.61e-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: 78.10  E-value: 1.61e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951655   515 FQIHGNDKSNTKAVEVSASASSLNSNDVFLLRTQAEHYLWYGKGSSGDERAMAKELVDLLCDGNAD------TVAEGQEP 588
Cdd:smart00262   1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPgpvqvrVVDEGKEP 80

                           90
                   ....*....|
gi 157951655   589 PEFWDLLGGK 598
Cdd:smart00262  81 PEFWSLFGGW 90
Gelsolin pfam00626
Gelsolin repeat;
143-216 2.53e-16

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 74.27  E-value: 2.53e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157951655  143 RNIQATEVEMSWDSFNRGDVFLLDLGMVIIQWNGPESNSGERLKAMLLAKDIRDRERGGRAEIGVIEGDKEAAS 216
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDERFPLPEVIRVPQGKEPAR 74
Gelsolin pfam00626
Gelsolin repeat;
23-105 3.59e-15

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 70.80  E-value: 3.59e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951655   23 KMELALVPLSAHGNFYEGDCYIVLSTrrvgsllsQNIHFWIGKDSSQDEQSCAAIYTTQLDD-YLGGSPVQHREVQYHES 101
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNG--------FTIFLWVGKGSSLLEKLFAALLAAQLDDdERFPLPEVIRVPQGKEP 72


                  ....
gi 157951655  102 DTFR 105
Cdd:pfam00626  73 ARFL 76
Gelsolin pfam00626
Gelsolin repeat;
627-704 1.61e-14

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 69.26  E-value: 1.61e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157951655  627 RFLVTEVTDFTQEDLSPGDVMLLDTWDQVFLWIGAEANATEKKGALSTAQEYLVTHpsgRDPDTPILIIKQGFEPPTF 704
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDE---RFPLPEVIRVPQGKEPARF 75
Gelsolin pfam00626
Gelsolin repeat;
263-340 1.66e-14

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 68.87  E-value: 1.66e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157951655  263 SVTEVATRPLVQDLLNHDDCYILDQsGTKIYVWKGKGATKVEKQAAMSKALDFIKMKgYPSSTNVETVNDGAESAMFK 340
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDN-GFTIFLWVGKGSSLLEKLFAALLAAQLDDDE-RFPLPEVIRVPQGKEPARFL 76
VHP pfam02209
Villin headpiece domain;
784-819 7.01e-14

Villin headpiece domain;


Pssm-ID: 460493  Cd Length: 36  Bit Score: 65.86  E-value: 7.01e-14
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 157951655  784 YLSEQDFVSVFGITRGQFTALPGWKQLQLKKERGLF 819
Cdd:pfam02209   1 YLSDEDFEEVFGMSREEFYKLPKWKQNNLKKKAGLF 36
Gelsolin pfam00626
Gelsolin repeat;
404-486 1.05e-13

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 66.95  E-value: 1.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951655  404 NLELVPVEYQWHGFFYGGDCYLVLYTYDvngkphyiLYIWQGRHASRDELAASAYRAVEVDQQF-DGAPVQVRVSMGKEP 482
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNGFT--------IFLWVGKGSSLLEKLFAALLAAQLDDDErFPLPEVIRVPQGKEP 72


                  ....
gi 157951655  483 RHFM 486
Cdd:pfam00626  73 ARFL 76
VHP smart00153
Villin headpiece domain;
784-819 3.64e-13

Villin headpiece domain;


Pssm-ID: 128458  Cd Length: 36  Bit Score: 63.88  E-value: 3.64e-13
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 157951655   784 YLSEQDFVSVFGITRGQFTALPGWKQLQLKKERGLF 819
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; ...
 7-118 1.34e-56

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: 189.36  E-value: 1.34e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951655   7 FRAVSNDPRIITWRIEKMELALVPLSAHGNFYEGDCYIVLSTRRVGS-LLSQNIHFWIGKDSSQDEQSCAAIYTTQLDDY 85
Cdd:cd11290    1 FEGVGQKPGLQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDPSgSLSYDIHYWLGKEASQDEAGAAAIKAVELDDY 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 157951655  86 LGGSPVQHREVQYHESDTFRGYFKQGIIYKKGG 118
Cdd:cd11290   81 LGGRPVQHREVQGHESEEFLSYFKKGIIYIEGG 113
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
 389-489 5.85e-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: 175.92  E-value: 5.85e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951655 389 MVDDGKGQVEVWRIENLELVPVEYQWHGFFYGGDCYLVLYTYDVNGKPHYILYIWQGRHASRDELAASAYRAVEVDQQFD 468
Cdd:cd11293    1 MYDDGSGKVEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQGGGKEEHILYFWQGRHSSQDERAAAALLTVELDEELK 80

                         90       100
                 ....*....|....*....|.
gi 157951655 469 GAPVQVRVSMGKEPRHFMAIF 489
Cdd:cd11293   81 GRAVQVRVVQGKEPPHFLALF 101
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 617-712 4.64e-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: 162.47  E-value: 4.64e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951655 617 RLFECSNKTGRFLVTEVTDFTQEDLSPGDVMLLDTWDQVFLWIGAEANATEKKGALSTAQEYLVTHPSGRD-PDTPILII 695
Cdd:cd11291    3 RLFRCSNESGFFKVEEISDFSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYIETDPLGRSkPRTPIYLV 82

                         90
                 ....*....|....*..
gi 157951655 696 KQGFEPPTFTGWFLAWD 712
Cdd:cd11291   83 KQGNEPPTFTGYFHAWD 99
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 247-345 4.02e-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: 145.47  E-value: 4.02e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951655 247 KSSIMLYHVSDTAGQLSVTEVATRPLVQDLLNHDDCYILDQsGTKIYVWKGKGATKVEKQAAMSKALDFIKMKGYPSSTN 326
Cdd:cd11292    1 AEQKKLYKVSDASGKLKLTEVAEGSLNQEMLDSEDCYILDC-GSEIFVWVGKGASLDERKAALKNAEEFLRKKKRPPYTQ 79

                         90
                 ....*....|....*....
gi 157951655 327 VETVNDGAESAMFKQLFQK 345
Cdd:cd11292   80 VTRVTEGGESALFKSKFAN 98
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 133-223 2.13e-40

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: 143.53  E-value: 2.13e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951655 133 VKRLLHVKGKRNIQATEVEMSWDSFNRGDVFLLDLGMVIIQWNGPESNSGERLKAMLLAKDIRDRERGGRAEIGVIEGDK 212
Cdd:cd11289    1 KPRLLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKVIVLDEGD 80

                         90
                 ....*....|.
gi 157951655 213 EAASPGLMTVL 223
Cdd:cd11289   81 TNESPEFWKVL 91
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 510-599 3.47e-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: 114.25  E-value: 3.47e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951655 510 PPVRLFQIHGNDKSNTKAVEVSASASSLNSNDVFLLRTQAEHYLWYGKGSSGDERAMAKELVDLLCDG-NADTVAEGQEP 588
Cdd:cd11288    1 SPTRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVASFLKPKaSLQEVAEGSEP 80

                         90
                 ....*....|.
gi 157951655 589 PEFWDLLGGKT 599
Cdd:cd11288   81 DEFWEALGGKS 91
gelsolin_S1_like cd11290
Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; ...
 397-499 1.61e-28

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: 110.39  E-value: 1.61e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951655 397 VEVWRIENLELVPVEYQWHGFFYGGDCYLVLYTY-DVNGKPHYILYIWQGRHASRDELAASAYRAVEVDQQFDGAPVQVR 475
Cdd:cd11290   10 LQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTlDPSGSLSYDIHYWLGKEASQDEAGAAAIKAVELDDYLGGRPVQHR 89

                         90       100
                 ....*....|....*....|....
gi 157951655 476 VSMGKEPRHFMAIFKgKLVIYEGG 499
Cdd:cd11290   90 EVQGHESEEFLSYFK-KGIIYIEG 112
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 264-346 2.67e-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: 97.36  E-value: 2.67e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951655   264 VTEVATRPLVQDLLNHDDCYILDqSGTKIYVWKGKGATKVEKQAAMSKALDFIKMKGyPSSTNVETVNDGAESAMFKQLF 343
Cdd:smart00262  10 NVRVPEVPFSQGSLNSGDCYILD-TGSEIYVWVGKKSSQDEKKKAAELAVELDDTLG-PGPVQVRVVDEGKEPPEFWSLF 87


                   ...
gi 157951655   344 QKW 346
Cdd:smart00262  88 GGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 620-711 6.22e-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: 96.21  E-value: 6.22e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951655   620 ECSNKTGRFLVTEVT-DFTQEDLSPGDVMLLDTWDQVFLWIGAEANATEKKGALSTAQEYLVTHPSGRdpdTPILIIKQG 698
Cdd:smart00262   1 FLVRVKGKRNVRVPEvPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGP---VQVRVVDEG 77

                           90
                   ....*....|...
gi 157951655   699 FEPPTFTGWFLAW 711
Cdd:smart00262  78 KEPPEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 398-492 1.81e-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: 95.05  E-value: 1.81e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951655   398 EVWRIENLELVPVEYQ--WHGFFYGGDCYLVLYTYDVngkphyilYIWQGRHASRDELAASAYRAVEVDQQFDGAPVQVR 475
Cdd:smart00262   1 FLVRVKGKRNVRVPEVpfSQGSLNSGDCYILDTGSEI--------YVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVR 72

                           90
                   ....*....|....*...
gi 157951655   476 -VSMGKEPRHFMAIFKGK 492
Cdd:smart00262  73 vVDEGKEPPEFWSLFGGW 90
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
 19-108 5.37e-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: 91.18  E-value: 5.37e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951655  19 WRIEKMELALVPLSAHGNFYEGDCYIVLSTRRVGSLLSQNIHFWIGKDSSQDEQSCAAIYTTQLDDYLGGSPVQHREVQY 98
Cdd:cd11293   12 WRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQGGGKEEHILYFWQGRHSSQDERAAAALLTVELDEELKGRAVQVRVVQG 91

                         90
                 ....*....|
gi 157951655  99 HESDTFRGYF 108
Cdd:cd11293   92 KEPPHFLALF 101
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 614-708 1.50e-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: 90.00  E-value: 1.50e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951655 614 VQVRLFECSNKTGRFLVTEVTD--FTQEDLSPGDVMLLDTWDQVFLWIGAEANATEKKGALSTAQEYLvtHPSGRDPDTP 691
Cdd:cd11292    2 EQKKLYKVSDASGKLKLTEVAEgsLNQEMLDSEDCYILDCGSEIFVWVGKGASLDERKAALKNAEEFL--RKKKRPPYTQ 79

                         90
                 ....*....|....*..
gi 157951655 692 ILIIKQGFEPPTFTGWF 708
Cdd:cd11292   80 VTRVTEGGESALFKSKF 96
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 135-215 4.07e-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: 82.73  E-value: 4.07e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951655   135 RLLHVKGKRNIQATEVEMSWDSFNRGDVFLLDLGMVIIQWNGPESNSGERLKAMLLAKDIRDRERGGRAEIGVIEGDKEA 214
Cdd:smart00262   1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVRVVDEGKEP 80


                   .
gi 157951655   215 A 215
Cdd:smart00262  81 P 81
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 19-109 4.90e-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: 82.34  E-value: 4.90e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951655    19 WRIE---KMELALVPLSaHGNFYEGDCYIVLSTrrvgsllsQNIHFWIGKDSSQDEQSCAAIYTTQLDDYLGGSPVQHRE 95
Cdd:smart00262   3 VRVKgkrNVRVPEVPFS-QGSLNSGDCYILDTG--------SEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVRV 73

                           90
                   ....*....|....*
gi 157951655    96 V-QYHESDTFRGYFK 109
Cdd:smart00262  74 VdEGKEPPEFWSLFG 88
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 515-598 1.61e-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: 78.10  E-value: 1.61e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951655   515 FQIHGNDKSNTKAVEVSASASSLNSNDVFLLRTQAEHYLWYGKGSSGDERAMAKELVDLLCDGNAD------TVAEGQEP 588
Cdd:smart00262   1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPgpvqvrVVDEGKEP 80

                           90
                   ....*....|
gi 157951655   589 PEFWDLLGGK 598
Cdd:smart00262  81 PEFWSLFGGW 90
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 252-347 3.72e-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: 77.34  E-value: 3.72e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951655 252 LYHVSDTAGQLSVTEVAtrPLVQDLLNHDDCYILDqSGTKIYVWKGKGATKVEKQAAMSKALDFIKMKGYPSS---TNVE 328
Cdd:cd11291    4 LFRCSNESGFFKVEEIS--DFSQDDLDTDDIMLLD-TGDEVFVWVGSESSDEEKKEALTSAKKYIETDPLGRSkprTPIY 80

                         90
                 ....*....|....*....
gi 157951655 329 TVNDGAESAMFKQLFQKWS 347
Cdd:cd11291   81 LVKQGNEPPTFTGYFHAWD 99
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 399-489 6.18e-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: 76.25  E-value: 6.18e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951655 399 VWRIENLELVPVEYQW--HGFFYGGDCYLVLYTYDVngkphyilYIWQGRHASRDELAASAYRAVEVDQQFDGAPVQVRV 476
Cdd:cd11280    4 LYRVRGSKAIEIEEVPlaSSSLDSDDVFVLDTGSEI--------YIWQGRASSQAELAAAALLAKELDEERKGKPEIVRI 75

                         90
                 ....*....|...
gi 157951655 477 SMGKEPRHFMAIF 489
Cdd:cd11280   76 RQGQEPREFWSLF 88
Gelsolin pfam00626
Gelsolin repeat;
143-216 2.53e-16

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 74.27  E-value: 2.53e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157951655  143 RNIQATEVEMSWDSFNRGDVFLLDLGMVIIQWNGPESNSGERLKAMLLAKDIRDRERGGRAEIGVIEGDKEAAS 216
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDERFPLPEVIRVPQGKEPAR 74
Gelsolin pfam00626
Gelsolin repeat;
23-105 3.59e-15

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 70.80  E-value: 3.59e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951655   23 KMELALVPLSAHGNFYEGDCYIVLSTrrvgsllsQNIHFWIGKDSSQDEQSCAAIYTTQLDD-YLGGSPVQHREVQYHES 101
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNG--------FTIFLWVGKGSSLLEKLFAALLAAQLDDdERFPLPEVIRVPQGKEP 72


                  ....
gi 157951655  102 DTFR 105
Cdd:pfam00626  73 ARFL 76
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 615-708 1.24e-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: 69.70  E-value: 1.24e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951655 615 QVRLFECSNKTgRFLVTEVTDFTqEDLSPGDVMLLDTWDQVFLWIGAEANATEKKGALSTAQEYLvthpSGRDPDTPILI 694
Cdd:cd11280    1 PPRLYRVRGSK-AIEIEEVPLAS-SSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKELD----EERKGKPEIVR 74

                         90
                 ....*....|....
gi 157951655 695 IKQGFEPPTFTGWF 708
Cdd:cd11280   75 IRQGQEPREFWSLF 88
Gelsolin pfam00626
Gelsolin repeat;
627-704 1.61e-14

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 69.26  E-value: 1.61e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157951655  627 RFLVTEVTDFTQEDLSPGDVMLLDTWDQVFLWIGAEANATEKKGALSTAQEYLVTHpsgRDPDTPILIIKQGFEPPTF 704
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDE---RFPLPEVIRVPQGKEPARF 75
Gelsolin pfam00626
Gelsolin repeat;
263-340 1.66e-14

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 68.87  E-value: 1.66e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157951655  263 SVTEVATRPLVQDLLNHDDCYILDQsGTKIYVWKGKGATKVEKQAAMSKALDFIKMKgYPSSTNVETVNDGAESAMFK 340
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDN-GFTIFLWVGKGSSLLEKLFAALLAAQLDDDE-RFPLPEVIRVPQGKEPARFL 76
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 13-108 3.34e-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: 68.55  E-value: 3.34e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951655  13 DPRIitWRIEK---MELALVPLsAHGNFYEGDCYIVLSTRrvgsllsqNIHFWIGKDSSQDEQSCAAIYTTQLDDYLGGS 89
Cdd:cd11280    1 PPRL--YRVRGskaIEIEEVPL-ASSSLDSDDVFVLDTGS--------EIYIWQGRASSQAELAAAALLAKELDEERKGK 69

                         90
                 ....*....|....*....
gi 157951655  90 PVQHREVQYHESDTFRGYF 108
Cdd:cd11280   70 PEIVRIRQGQEPREFWSLF 88
VHP pfam02209
Villin headpiece domain;
784-819 7.01e-14

Villin headpiece domain;


Pssm-ID: 460493  Cd Length: 36  Bit Score: 65.86  E-value: 7.01e-14
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 157951655  784 YLSEQDFVSVFGITRGQFTALPGWKQLQLKKERGLF 819
Cdd:pfam02209   1 YLSDEDFEEVFGMSREEFYKLPKWKQNNLKKKAGLF 36
Gelsolin pfam00626
Gelsolin repeat;
404-486 1.05e-13

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 66.95  E-value: 1.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951655  404 NLELVPVEYQWHGFFYGGDCYLVLYTYDvngkphyiLYIWQGRHASRDELAASAYRAVEVDQQF-DGAPVQVRVSMGKEP 482
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNGFT--------IFLWVGKGSSLLEKLFAALLAAQLDDDErFPLPEVIRVPQGKEP 72


                  ....
gi 157951655  483 RHFM 486
Cdd:pfam00626  73 ARFL 76
VHP smart00153
Villin headpiece domain;
784-819 3.64e-13

Villin headpiece domain;


Pssm-ID: 128458  Cd Length: 36  Bit Score: 63.88  E-value: 3.64e-13
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 157951655   784 YLSEQDFVSVFGITRGQFTALPGWKQLQLKKERGLF 819
Cdd:smart00153   1 YLSDEDFEEVFGMTREEFYKLPLWKQNQLKKKKGLF 36
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 511-595 3.52e-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: 56.99  E-value: 3.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951655 511 PVRLFQIHGndKSNTKAVEVSASASSLNSNDVFLLRTQAEHYLWYGKGSSGDERA----MAKELVDLLcDGNADTV--AE 584
Cdd:cd11280    1 PPRLYRVRG--SKAIEIEEVPLASSSLDSDDVFVLDTGSEIYIWQGRASSQAELAaaalLAKELDEER-KGKPEIVriRQ 77

                         90
                 ....*....|.
gi 157951655 585 GQEPPEFWDLL 595
Cdd:cd11280   78 GQEPREFWSLF 88
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 251-346 3.53e-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: 57.25  E-value: 3.53e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951655 251 MLYHVSdtaG--QLSVTEVatrPLVQDLLNHDDCYILDqSGTKIYVWKGKGATKVEKqaamSKALDF---IKMKGYPSST 325
Cdd:cd11289    3 RLLHVK---GrrNVRAREV---ELSWSSLNSGDVFILD-LGSTIYQWNGSKSNRFEK----AKAMQLaqgIRDERRLGRA 71

                         90       100
                 ....*....|....*....|.
gi 157951655 326 NVETVNDGAESAMFKQLFQKW 346
Cdd:cd11289   72 KVIVLDEGDTNESPEFWKVLG 92
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 248-339 5.28e-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: 5.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951655 248 SSIMLYHVSDTagqlsvTEVATRpLVQD-----LLNHDDCYILdQSGTKIYVWKGKGATKVEKQAAmSKALDFIKmkgyp 322
Cdd:cd11288    1 SPTRLFQVRGN------GSGNTR-AVEVdadasSLNSNDVFVL-KTPSSVYLWVGKGSSEDERELA-KDVASFLK----- 66

                         90
                 ....*....|....*..
gi 157951655 323 SSTNVETVNDGAESAMF 339
Cdd:cd11288   67 PKASLQEVAEGSEPDEF 83
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 135-215 2.00e-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: 55.07  E-value: 2.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951655 135 RLLHVKGKRNIQATEVEMSWDSFNRGDVFLLDLGMVIIQWNGPESNSGERLKAMLLAKDIrDRERGGRAEIGVIEGDKEA 214
Cdd:cd11280    3 RLYRVRGSKAIEIEEVPLASSSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKEL-DEERKGKPEIVRIRQGQEP 81


                 .
gi 157951655 215 A 215
Cdd:cd11280   82 R 82
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 252-343 2.71e-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: 2.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951655 252 LYHVSDtAGQLSVTEVATRPlvqDLLNHDDCYILDqSGTKIYVWKGKGATKVEKQAA--MSKALDfikmKGYPSSTNVET 329
Cdd:cd11280    4 LYRVRG-SKAIEIEEVPLAS---SSLDSDDVFVLD-TGSEIYIWQGRASSQAELAAAalLAKELD----EERKGKPEIVR 74

                         90
                 ....*....|....
gi 157951655 330 VNDGAESAMFKQLF 343
Cdd:cd11280   75 IRQGQEPREFWSLF 88
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 511-596 1.15e-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: 1.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951655 511 PVRLFQIHGndKSNTKAVEVSASASSLNSNDVFLLRTQAEHYLWYGKGSSGDERAMAKELVDLLCD----GNADT----V 582
Cdd:cd11289    1 KPRLLHVKG--RRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDerrlGRAKVivldE 78

                         90
                 ....*....|....
gi 157951655 583 AEGQEPPEFWDLLG 596
Cdd:cd11289   79 GDTNESPEFWKVLG 92
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 615-704 7.58e-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: 39.14  E-value: 7.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951655 615 QVRLFECSNKTgRFLVTEVtDFTQEDLSPGDVMLLDTWDQVFLWIGAEANATEKKGALSTAQeYLVTHPSGRDPDTPILI 694
Cdd:cd11289    1 KPRLLHVKGRR-NVRAREV-ELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQ-GIRDERRLGRAKVIVLD 77

                         90
                 ....*....|
gi 157951655 695 IKQGFEPPTF 704
Cdd:cd11289   78 EGDTNESPEF 87
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 645-704 9.25e-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: 9.25e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 157951655 645 DVMLLDTWDQVFLWIGAEANATEKKGALSTAQEYlvthpsgrDPDTPILIIKQGFEPPTF 704
Cdd:cd11288   32 DVFVLKTPSSVYLWVGKGSSEDERELAKDVASFL--------KPKASLQEVAEGSEPDEF 83
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 541-591 2.64e-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: 2.64e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 157951655 541 DVFLLRTQAEHYLWYGKGSSGDERAMAKEL-VDLL--CDGNADT----VAEGQEPPEF 591
Cdd:cd11292   35 DCYILDCGSEIFVWVGKGASLDERKAALKNaEEFLrkKKRPPYTqvtrVTEGGESALF 92
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 135-197 2.68e-03

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: 37.60  E-value: 2.68e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157951655 135 RLLHVKG--KRNIQATEVEMSWDSFNRGDVFLLDLGMVIIQWNGPESNSGERLKAMLLAKDIRDR 197
Cdd:cd11288    4 RLFQVRGngSGNTRAVEVDADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVASFLKPK 68
 
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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