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Conserved domains on  [gi|41053868|ref|NP_956532|]
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villin-1 [Danio rerio]

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; ...
18-122 1.36e-55

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: 186.66  E-value: 1.36e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053868  18 PGLQIWRVENMELVPCPSKTFGQFFEGDSYVILYTHKT-SNNFSYDIHYWLGKSTSQDEMGAAAIYTTQMDDHLGGVAVQ 96
Cdd:cd11290   8 PGLQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDpSGSLSYDIHYWLGKEASQDEAGAAAIKAVELDDYLGGRPVQ 87
                        90       100
                ....*....|....*....|....*.
gi 41053868  97 HRETQGHESATFQGYFKQGIIYKKGG 122
Cdd:cd11290  88 HREVQGHESEEFLSYFKKGIIYIEGG 113
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
621-717 5.97e-50

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: 170.56  E-value: 5.97e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053868 621 PRLFECSNQTGRFIATEITNFNQDDLDEDDVMLLDIWDQVYLWIGKGANDTEKREAVVTAQEYLKSHPAGRDL-DTPVLV 699
Cdd:cd11291   2 PRLFRCSNESGFFKVEEISDFSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYIETDPLGRSKpRTPIYL 81
                        90
                ....*....|....*...
gi 41053868 700 VKQGFEPPTFTGWFHAWD 717
Cdd:cd11291  82 VKQGNEPPTFTGYFHAWD 99
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
394-494 3.25e-44

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: 154.35  E-value: 3.25e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053868 394 MVDDGSGEAEVWRIEDNELAPVDRKWLGHFYGGDCYLILYKYEVSSKFHYILYMWQGRHASTAELTACAYQAVILDQKYN 473
Cdd:cd11293   1 MYDDGSGKVEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQGGGKEEHILYFWQGRHSSQDERAAAALLTVELDEELK 80
                        90       100
                ....*....|....*....|.
gi 41053868 474 GEPVQVRVPMGKEPMHLMAIF 494
Cdd:cd11293  81 GRAVQVRVVQGKEPPHFLALF 101
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
515-605 9.21e-43

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: 150.07  E-value: 9.21e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053868 515 PSVRLFHVHGTNEFNTRATEVPPRSSSLNSNDVFVLSTDKCCYLWYGKGCSGDEREMAKSLADIIS-EREKQVIAEGQEP 593
Cdd:cd11288   1 SPTRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVASFLKpKASLQEVAEGSEP 80
                        90
                ....*....|..
gi 41053868 594 ADFWVNLGGKSQ 605
Cdd:cd11288  81 DEFWEALGGKSE 92
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
139-225 7.84e-39

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: 138.91  E-value: 7.84e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053868 139 RLLHVKGNKHVVAGEVEMSWNSFNKGDVFLLDLGSLIIQWNGPKSNRMERLRGMNLAKDIRDRERGGRAQVAVVEGDDEQ 218
Cdd:cd11289   3 RLLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKVIVLDEGDTN 82

                ....*..
gi 41053868 219 SSEEAMK 225
Cdd:cd11289  83 ESPEFWK 89
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
252-350 6.26e-35

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: 128.14  E-value: 6.26e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053868 252 KTAIKLYHISDAQGSLVVQEVAVKPLTQDLLKTEDCYLLDQGGiKIFIWKGKKASKAERTESLKMAEAYVKAKGYPVSTY 331
Cdd:cd11292   1 AEQKKLYKVSDASGKLKLTEVAEGSLNQEMLDSEDCYILDCGS-EIFVWVGKGASLDERKAALKNAEEFLRKKKRPPYTQ 79
                        90
                ....*....|....*....
gi 41053868 332 IETVSEGAESSVFKQLFQK 350
Cdd:cd11292  80 VTRVTEGGESALFKSKFAN 98
VHP pfam02209
Villin headpiece domain;
799-834 8.94e-13

Villin headpiece domain;


:

Pssm-ID: 460493  Cd Length: 36  Bit Score: 62.78  E-value: 8.94e-13
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 41053868   799 YLSDDDFALAMGISRMNFYAMPSWKQLNLKKEKGLF 834
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; ...
18-122 1.36e-55

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: 186.66  E-value: 1.36e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053868  18 PGLQIWRVENMELVPCPSKTFGQFFEGDSYVILYTHKT-SNNFSYDIHYWLGKSTSQDEMGAAAIYTTQMDDHLGGVAVQ 96
Cdd:cd11290   8 PGLQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDpSGSLSYDIHYWLGKEASQDEAGAAAIKAVELDDYLGGRPVQ 87
                        90       100
                ....*....|....*....|....*.
gi 41053868  97 HRETQGHESATFQGYFKQGIIYKKGG 122
Cdd:cd11290  88 HREVQGHESEEFLSYFKKGIIYIEGG 113
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
621-717 5.97e-50

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: 170.56  E-value: 5.97e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053868 621 PRLFECSNQTGRFIATEITNFNQDDLDEDDVMLLDIWDQVYLWIGKGANDTEKREAVVTAQEYLKSHPAGRDL-DTPVLV 699
Cdd:cd11291   2 PRLFRCSNESGFFKVEEISDFSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYIETDPLGRSKpRTPIYL 81
                        90
                ....*....|....*...
gi 41053868 700 VKQGFEPPTFTGWFHAWD 717
Cdd:cd11291  82 VKQGNEPPTFTGYFHAWD 99
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
394-494 3.25e-44

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: 154.35  E-value: 3.25e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053868 394 MVDDGSGEAEVWRIEDNELAPVDRKWLGHFYGGDCYLILYKYEVSSKFHYILYMWQGRHASTAELTACAYQAVILDQKYN 473
Cdd:cd11293   1 MYDDGSGKVEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQGGGKEEHILYFWQGRHSSQDERAAAALLTVELDEELK 80
                        90       100
                ....*....|....*....|.
gi 41053868 474 GEPVQVRVPMGKEPMHLMAIF 494
Cdd:cd11293  81 GRAVQVRVVQGKEPPHFLALF 101
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
515-605 9.21e-43

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: 150.07  E-value: 9.21e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053868 515 PSVRLFHVHGTNEFNTRATEVPPRSSSLNSNDVFVLSTDKCCYLWYGKGCSGDEREMAKSLADIIS-EREKQVIAEGQEP 593
Cdd:cd11288   1 SPTRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVASFLKpKASLQEVAEGSEP 80
                        90
                ....*....|..
gi 41053868 594 ADFWVNLGGKSQ 605
Cdd:cd11288  81 DEFWEALGGKSE 92
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
139-225 7.84e-39

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: 138.91  E-value: 7.84e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053868 139 RLLHVKGNKHVVAGEVEMSWNSFNKGDVFLLDLGSLIIQWNGPKSNRMERLRGMNLAKDIRDRERGGRAQVAVVEGDDEQ 218
Cdd:cd11289   3 RLLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKVIVLDEGDTN 82

                ....*..
gi 41053868 219 SSEEAMK 225
Cdd:cd11289  83 ESPEFWK 89
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
252-350 6.26e-35

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: 128.14  E-value: 6.26e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053868 252 KTAIKLYHISDAQGSLVVQEVAVKPLTQDLLKTEDCYLLDQGGiKIFIWKGKKASKAERTESLKMAEAYVKAKGYPVSTY 331
Cdd:cd11292   1 AEQKKLYKVSDASGKLKLTEVAEGSLNQEMLDSEDCYILDCGS-EIFVWVGKGASLDERKAALKNAEEFLRKKKRPPYTQ 79
                        90
                ....*....|....*....
gi 41053868 332 IETVSEGAESSVFKQLFQK 350
Cdd:cd11292  80 VTRVTEGGESALFKSKFAN 98
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
520-603 3.27e-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: 3.27e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053868    520 FHVHGTNEFNTRATEVPPRSSSLNSNDVFVLSTDKCCYLWYGKGCSGDEREMAKSLADIISEREK------QVIAEGQEP 593
Cdd:smart00262   1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGpgpvqvRVVDEGKEP 80
                           90
                   ....*....|
gi 41053868    594 ADFWVNLGGK 603
Cdd:smart00262  81 PEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
625-716 9.38e-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: 93.13  E-value: 9.38e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053868    625 ECSNQTGRFIATEIT-NFNQDDLDEDDVMLLDIWDQVYLWIGKGANDTEKREAVVTAQEYLKSHPAGRdldTPVLVVKQG 703
Cdd:smart00262   1 FLVRVKGKRNVRVPEvPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGP---VQVRVVDEG 77
                           90
                   ....*....|...
gi 41053868    704 FEPPTFTGWFHAW 716
Cdd:smart00262  78 KEPPEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
259-351 2.11e-20

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: 86.19  E-value: 2.11e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053868    259 HISDAQGSLVVQEVAVkPLTQDLLKTEDCYLLDQGGIkIFIWKGKKASKAERTESLKMAEAYVKAKGyPVSTYIETVSEG 338
Cdd:smart00262   1 FLVRVKGKRNVRVPEV-PFSQGSLNSGDCYILDTGSE-IYVWVGKKSSQDEKKKAAELAVELDDTLG-PGPVQVRVVDEG 77
                           90
                   ....*....|...
gi 41053868    339 AESSVFKQLFQKW 351
Cdd:smart00262  78 KEPPEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
139-215 7.86e-20

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: 84.65  E-value: 7.86e-20
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41053868    139 RLLHVKGNKHVVAGEVEMSWNSFNKGDVFLLDLGSLIIQWNGPKSNRMERLRGMNLAKDIRDRERGGRAQVAVV-EGD 215
Cdd:smart00262   1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVRVVdEGK 78
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
21-113 4.28e-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: 4.28e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053868     21 QIWRVENMELVPCPSKTF--GQFFEGDSYVILYTHktsnnfsyDIHYWLGKSTSQDEMGAAAIYTTQMDDHLGGVAVQHR 98
Cdd:smart00262   1 FLVRVKGKRNVRVPEVPFsqGSLNSGDCYILDTGS--------EIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVR 72
                           90
                   ....*....|....*.
gi 41053868     99 E-TQGHESATFQGYFK 113
Cdd:smart00262  73 VvDEGKEPPEFWSLFG 88
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
403-497 9.40e-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: 81.57  E-value: 9.40e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053868    403 EVWRIEDNELAPVDR--KWLGHFYGGDCYLILYKYEVsskfhyilYMWQGRHASTAELTACAYQAVILDQKYNGEPVQVR 480
Cdd:smart00262   1 FLVRVKGKRNVRVPEvpFSQGSLNSGDCYILDTGSEI--------YVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVR 72
                           90
                   ....*....|....*...
gi 41053868    481 -VPMGKEPMHLMAIFKGK 497
Cdd:smart00262  73 vVDEGKEPPEFWSLFGGW 90
Gelsolin pfam00626
Gelsolin repeat;
410-491 1.01e-14

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 69.64  E-value: 1.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053868   410 NELAPVDRKWLGHFYGGDCYLILYkyevsskfHYILYMWQGRHASTAELTACAYQAV-ILDQKYNGEPVQVRVPMGKEPM 488
Cdd:pfam00626   2 FVLPPPVPLSQESLNSGDCYLLDN--------GFTIFLWVGKGSSLLEKLFAALLAAqLDDDERFPLPEVIRVPQGKEPA 73

                  ...
gi 41053868   489 HLM 491
Cdd:pfam00626  74 RFL 76
Gelsolin pfam00626
Gelsolin repeat;
147-218 1.69e-14

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 68.87  E-value: 1.69e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41053868   147 KHVVAGEVEMSWNSFNKGDVFLLDLGSLIIQWNGPKSNRMERLRGMNLAKDIRDRERGGRAQVAVVEGDDEQ 218
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDERFPLPEVIRVPQGKEP 72
Gelsolin pfam00626
Gelsolin repeat;
632-709 4.35e-14

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 67.72  E-value: 4.35e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41053868   632 RFIATEITNFNQDDLDEDDVMLLDIWDQVYLWIGKGANDTEKREAVVTAQEYLKSHpagRDLDTPVLVVKQGFEPPTF 709
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDE---RFPLPEVIRVPQGKEPARF 75
Gelsolin pfam00626
Gelsolin repeat;
27-108 5.19e-13

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 65.02  E-value: 5.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053868    27 NMELVPCPSKTFGQFFEGDSYVILYThktsnnfsYDIHYWLGKSTSQDEMGAAAIYTTQMDD-HLGGVAVQHRETQGHES 105
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNG--------FTIFLWVGKGSSLLEKLFAALLAAQLDDdERFPLPEVIRVPQGKEP 72

                  ...
gi 41053868   106 ATF 108
Cdd:pfam00626  73 ARF 75
VHP pfam02209
Villin headpiece domain;
799-834 8.94e-13

Villin headpiece domain;


Pssm-ID: 460493  Cd Length: 36  Bit Score: 62.78  E-value: 8.94e-13
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 41053868   799 YLSDDDFALAMGISRMNFYAMPSWKQLNLKKEKGLF 834
Cdd:pfam02209   1 YLSDEDFEEVFGMSREEFYKLPKWKQNNLKKKAGLF 36
Gelsolin pfam00626
Gelsolin repeat;
268-345 7.69e-11

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 58.86  E-value: 7.69e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41053868   268 VVQEVAVKPLTQDLLKTEDCYLLDQGGiKIFIWKGKKASKAERTESLKMAEAYVKAKgYPVSTYIETVSEGAESSVFK 345
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNGF-TIFLWVGKGSSLLEKLFAALLAAQLDDDE-RFPLPEVIRVPQGKEPARFL 76
VHP smart00153
Villin headpiece domain;
799-834 1.15e-10

Villin headpiece domain;


Pssm-ID: 128458  Cd Length: 36  Bit Score: 56.94  E-value: 1.15e-10
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 41053868    799 YLSDDDFALAMGISRMNFYAMPSWKQLNLKKEKGLF 834
Cdd:smart00153   1 YLSDEDFEEVFGMTREEFYKLPLWKQNQLKKKKGLF 36
Gelsolin pfam00626
Gelsolin repeat;
528-597 8.32e-05

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 41.52  E-value: 8.32e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41053868   528 FNTRATEVPPRSSSLNSNDVFVLSTDKCCYLWYGKGCSGDEREMAKSLA-DIISER-----EKQVIAEGQEPADFW 597
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAaQLDDDErfplpEVIRVPQGKEPARFL 76
 
Name Accession Description Interval E-value
gelsolin_S1_like cd11290
Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; ...
18-122 1.36e-55

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: 186.66  E-value: 1.36e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053868  18 PGLQIWRVENMELVPCPSKTFGQFFEGDSYVILYTHKT-SNNFSYDIHYWLGKSTSQDEMGAAAIYTTQMDDHLGGVAVQ 96
Cdd:cd11290   8 PGLQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDpSGSLSYDIHYWLGKEASQDEAGAAAIKAVELDDYLGGRPVQ 87
                        90       100
                ....*....|....*....|....*.
gi 41053868  97 HRETQGHESATFQGYFKQGIIYKKGG 122
Cdd:cd11290  88 HREVQGHESEEFLSYFKKGIIYIEGG 113
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
621-717 5.97e-50

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: 170.56  E-value: 5.97e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053868 621 PRLFECSNQTGRFIATEITNFNQDDLDEDDVMLLDIWDQVYLWIGKGANDTEKREAVVTAQEYLKSHPAGRDL-DTPVLV 699
Cdd:cd11291   2 PRLFRCSNESGFFKVEEISDFSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYIETDPLGRSKpRTPIYL 81
                        90
                ....*....|....*...
gi 41053868 700 VKQGFEPPTFTGWFHAWD 717
Cdd:cd11291  82 VKQGNEPPTFTGYFHAWD 99
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
394-494 3.25e-44

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: 154.35  E-value: 3.25e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053868 394 MVDDGSGEAEVWRIEDNELAPVDRKWLGHFYGGDCYLILYKYEVSSKFHYILYMWQGRHASTAELTACAYQAVILDQKYN 473
Cdd:cd11293   1 MYDDGSGKVEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQGGGKEEHILYFWQGRHSSQDERAAAALLTVELDEELK 80
                        90       100
                ....*....|....*....|.
gi 41053868 474 GEPVQVRVPMGKEPMHLMAIF 494
Cdd:cd11293  81 GRAVQVRVVQGKEPPHFLALF 101
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
515-605 9.21e-43

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: 150.07  E-value: 9.21e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053868 515 PSVRLFHVHGTNEFNTRATEVPPRSSSLNSNDVFVLSTDKCCYLWYGKGCSGDEREMAKSLADIIS-EREKQVIAEGQEP 593
Cdd:cd11288   1 SPTRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVASFLKpKASLQEVAEGSEP 80
                        90
                ....*....|..
gi 41053868 594 ADFWVNLGGKSQ 605
Cdd:cd11288  81 DEFWEALGGKSE 92
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
139-225 7.84e-39

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: 138.91  E-value: 7.84e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053868 139 RLLHVKGNKHVVAGEVEMSWNSFNKGDVFLLDLGSLIIQWNGPKSNRMERLRGMNLAKDIRDRERGGRAQVAVVEGDDEQ 218
Cdd:cd11289   3 RLLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKVIVLDEGDTN 82

                ....*..
gi 41053868 219 SSEEAMK 225
Cdd:cd11289  83 ESPEFWK 89
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
252-350 6.26e-35

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: 128.14  E-value: 6.26e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053868 252 KTAIKLYHISDAQGSLVVQEVAVKPLTQDLLKTEDCYLLDQGGiKIFIWKGKKASKAERTESLKMAEAYVKAKGYPVSTY 331
Cdd:cd11292   1 AEQKKLYKVSDASGKLKLTEVAEGSLNQEMLDSEDCYILDCGS-EIFVWVGKGASLDERKAALKNAEEFLRKKKRPPYTQ 79
                        90
                ....*....|....*....
gi 41053868 332 IETVSEGAESSVFKQLFQK 350
Cdd:cd11292  80 VTRVTEGGESALFKSKFAN 98
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
20-112 3.56e-28

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: 108.90  E-value: 3.56e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053868  20 LQIWRVENMELVPCPSKTFGQFFEGDSYVILYTHKTSNNFSYDIHYWLGKSTSQDEMGAAAIYTTQMDDHLGGVAVQHRE 99
Cdd:cd11293   9 VEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQGGGKEEHILYFWQGRHSSQDERAAAALLTVELDEELKGRAVQVRV 88
                        90
                ....*....|...
gi 41053868 100 TQGHESATFQGYF 112
Cdd:cd11293  89 VQGKEPPHFLALF 101
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
520-603 3.27e-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: 3.27e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053868    520 FHVHGTNEFNTRATEVPPRSSSLNSNDVFVLSTDKCCYLWYGKGCSGDEREMAKSLADIISEREK------QVIAEGQEP 593
Cdd:smart00262   1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGpgpvqvRVVDEGKEP 80
                           90
                   ....*....|
gi 41053868    594 ADFWVNLGGK 603
Cdd:smart00262  81 PEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
625-716 9.38e-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: 93.13  E-value: 9.38e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053868    625 ECSNQTGRFIATEIT-NFNQDDLDEDDVMLLDIWDQVYLWIGKGANDTEKREAVVTAQEYLKSHPAGRdldTPVLVVKQG 703
Cdd:smart00262   1 FLVRVKGKRNVRVPEvPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGP---VQVRVVDEG 77
                           90
                   ....*....|...
gi 41053868    704 FEPPTFTGWFHAW 716
Cdd:smart00262  78 KEPPEFWSLFGGW 90
gelsolin_S1_like cd11290
Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; ...
403-504 1.38e-20

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: 87.66  E-value: 1.38e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053868 403 EVWRIEDNELAPVDRKWLGHFYGGDCYLILYKYEV-SSKFHYILYMWQGRHASTAELTACAYQAVILDQKYNGEPVQVRV 481
Cdd:cd11290  11 QIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDpSGSLSYDIHYWLGKEASQDEAGAAAIKAVELDDYLGGRPVQHRE 90
                        90       100
                ....*....|....*....|...
gi 41053868 482 PMGKEPMHLMAIFKgKMIVYEEG 504
Cdd:cd11290  91 VQGHESEEFLSYFK-KGIIYIEG 112
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
259-351 2.11e-20

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: 86.19  E-value: 2.11e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053868    259 HISDAQGSLVVQEVAVkPLTQDLLKTEDCYLLDQGGIkIFIWKGKKASKAERTESLKMAEAYVKAKGyPVSTYIETVSEG 338
Cdd:smart00262   1 FLVRVKGKRNVRVPEV-PFSQGSLNSGDCYILDTGSE-IYVWVGKKSSQDEKKKAAELAVELDDTLG-PGPVQVRVVDEG 77
                           90
                   ....*....|...
gi 41053868    339 AESSVFKQLFQKW 351
Cdd:smart00262  78 KEPPEFWSLFGGW 90
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
618-713 3.30e-20

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: 86.15  E-value: 3.30e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053868 618 SITPRLFECSNQTGRFIATEIT--NFNQDDLDEDDVMLLDIWDQVYLWIGKGANDTEKREAVVTAQEYLKSHpaGRDLDT 695
Cdd:cd11292   1 AEQKKLYKVSDASGKLKLTEVAegSLNQEMLDSEDCYILDCGSEIFVWVGKGASLDERKAALKNAEEFLRKK--KRPPYT 78
                        90
                ....*....|....*...
gi 41053868 696 PVLVVKQGFEPPTFTGWF 713
Cdd:cd11292  79 QVTRVTEGGESALFKSKF 96
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
139-215 7.86e-20

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: 84.65  E-value: 7.86e-20
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41053868    139 RLLHVKGNKHVVAGEVEMSWNSFNKGDVFLLDLGSLIIQWNGPKSNRMERLRGMNLAKDIRDRERGGRAQVAVV-EGD 215
Cdd:smart00262   1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVRVVdEGK 78
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
21-113 4.28e-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: 4.28e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053868     21 QIWRVENMELVPCPSKTF--GQFFEGDSYVILYTHktsnnfsyDIHYWLGKSTSQDEMGAAAIYTTQMDDHLGGVAVQHR 98
Cdd:smart00262   1 FLVRVKGKRNVRVPEVPFsqGSLNSGDCYILDTGS--------EIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVR 72
                           90
                   ....*....|....*.
gi 41053868     99 E-TQGHESATFQGYFK 113
Cdd:smart00262  73 VvDEGKEPPEFWSLFG 88
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
403-497 9.40e-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: 81.57  E-value: 9.40e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053868    403 EVWRIEDNELAPVDR--KWLGHFYGGDCYLILYKYEVsskfhyilYMWQGRHASTAELTACAYQAVILDQKYNGEPVQVR 480
Cdd:smart00262   1 FLVRVKGKRNVRVPEvpFSQGSLNSGDCYILDTGSEI--------YVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVR 72
                           90
                   ....*....|....*...
gi 41053868    481 -VPMGKEPMHLMAIFKGK 497
Cdd:smart00262  73 vVDEGKEPPEFWSLFGGW 90
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
518-601 3.77e-18

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: 79.97  E-value: 3.77e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053868 518 RLFHVHGtnEFNTRATEVPPRSSSLNSNDVFVLSTDKCCYLWYGKGCSGDEREMAKSLADIISEREK------QVIAEG- 590
Cdd:cd11289   3 RLLHVKG--RRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRlgrakvIVLDEGd 80
                        90
                ....*....|..
gi 41053868 591 -QEPADFWVNLG 601
Cdd:cd11289  81 tNESPEFWKVLG 92
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
255-351 1.97e-15

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: 72.33  E-value: 1.97e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053868 255 IKLYHISDAQGSLVVQEVAvkPLTQDLLKTEDCYLLDQGGiKIFIWKGKKASKAERTESLKMAEAYVK---AKGYPVSTY 331
Cdd:cd11291   2 PRLFRCSNESGFFKVEEIS--DFSQDDLDTDDIMLLDTGD-EVFVWVGSESSDEEKKEALTSAKKYIEtdpLGRSKPRTP 78
                        90       100
                ....*....|....*....|
gi 41053868 332 IETVSEGAESSVFKQLFQKW 351
Cdd:cd11291  79 IYLVKQGNEPPTFTGYFHAW 98
Gelsolin pfam00626
Gelsolin repeat;
410-491 1.01e-14

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 69.64  E-value: 1.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053868   410 NELAPVDRKWLGHFYGGDCYLILYkyevsskfHYILYMWQGRHASTAELTACAYQAV-ILDQKYNGEPVQVRVPMGKEPM 488
Cdd:pfam00626   2 FVLPPPVPLSQESLNSGDCYLLDN--------GFTIFLWVGKGSSLLEKLFAALLAAqLDDDERFPLPEVIRVPQGKEPA 73

                  ...
gi 41053868   489 HLM 491
Cdd:pfam00626  74 RFL 76
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
21-112 1.18e-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: 1.18e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053868  21 QIWRVE---NMELVPCPSKTfGQFFEGDSYVILythktsnnFSYDIHYWLGKSTSQDEMGAAAIYTTQMDDHLGGVAVQH 97
Cdd:cd11280   3 RLYRVRgskAIEIEEVPLAS-SSLDSDDVFVLD--------TGSEIYIWQGRASSQAELAAAALLAKELDEERKGKPEIV 73
                        90
                ....*....|....*
gi 41053868  98 RETQGHESATFQGYF 112
Cdd:cd11280  74 RIRQGQEPREFWSLF 88
Gelsolin pfam00626
Gelsolin repeat;
147-218 1.69e-14

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 68.87  E-value: 1.69e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41053868   147 KHVVAGEVEMSWNSFNKGDVFLLDLGSLIIQWNGPKSNRMERLRGMNLAKDIRDRERGGRAQVAVVEGDDEQ 218
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDERFPLPEVIRVPQGKEP 72
Gelsolin pfam00626
Gelsolin repeat;
632-709 4.35e-14

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 67.72  E-value: 4.35e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41053868   632 RFIATEITNFNQDDLDEDDVMLLDIWDQVYLWIGKGANDTEKREAVVTAQEYLKSHpagRDLDTPVLVVKQGFEPPTF 709
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDE---RFPLPEVIRVPQGKEPARF 75
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
621-713 5.17e-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: 68.16  E-value: 5.17e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053868 621 PRLFECSNQTgrfiATEITNFNQDD--LDEDDVMLLDIWDQVYLWIGKGANDTEKREAVVTAQEYLKShpagRDLDTPVL 698
Cdd:cd11280   2 PRLYRVRGSK----AIEIEEVPLASssLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKELDEE----RKGKPEIV 73
                        90
                ....*....|....*
gi 41053868 699 VVKQGFEPPTFTGWF 713
Cdd:cd11280  74 RIRQGQEPREFWSLF 88
Gelsolin pfam00626
Gelsolin repeat;
27-108 5.19e-13

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 65.02  E-value: 5.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053868    27 NMELVPCPSKTFGQFFEGDSYVILYThktsnnfsYDIHYWLGKSTSQDEMGAAAIYTTQMDD-HLGGVAVQHRETQGHES 105
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNG--------FTIFLWVGKGSSLLEKLFAALLAAQLDDdERFPLPEVIRVPQGKEP 72

                  ...
gi 41053868   106 ATF 108
Cdd:pfam00626  73 ARF 75
VHP pfam02209
Villin headpiece domain;
799-834 8.94e-13

Villin headpiece domain;


Pssm-ID: 460493  Cd Length: 36  Bit Score: 62.78  E-value: 8.94e-13
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 41053868   799 YLSDDDFALAMGISRMNFYAMPSWKQLNLKKEKGLF 834
Cdd:pfam02209   1 YLSDEDFEEVFGMSREEFYKLPKWKQNNLKKKAGLF 36
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
404-494 2.76e-12

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: 63.16  E-value: 2.76e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053868 404 VWRIEDN---ELAPVDRKwLGHFYGGDCYLILYKYEVsskfhyilYMWQGRHASTAELTACAYQAVILDQKYNGEPVQVR 480
Cdd:cd11280   4 LYRVRGSkaiEIEEVPLA-SSSLDSDDVFVLDTGSEI--------YIWQGRASSQAELAAAALLAKELDEERKGKPEIVR 74
                        90
                ....*....|....
gi 41053868 481 VPMGKEPMHLMAIF 494
Cdd:cd11280  75 IRQGQEPREFWSLF 88
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
518-597 3.56e-12

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: 62.77  E-value: 3.56e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053868 518 RLFHVHGTNefNTRATEVPPRSSSLNSNDVFVLSTDKCCYLWYGKGCSGDEREMAKSLADIISEREK-----QVIAEGQE 592
Cdd:cd11280   3 RLYRVRGSK--AIEIEEVPLASSSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKELDEERKgkpeiVRIRQGQE 80

                ....*
gi 41053868 593 PADFW 597
Cdd:cd11280  81 PREFW 85
Gelsolin pfam00626
Gelsolin repeat;
268-345 7.69e-11

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 58.86  E-value: 7.69e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41053868   268 VVQEVAVKPLTQDLLKTEDCYLLDQGGiKIFIWKGKKASKAERTESLKMAEAYVKAKgYPVSTYIETVSEGAESSVFK 345
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNGF-TIFLWVGKGSSLLEKLFAALLAAQLDDDE-RFPLPEVIRVPQGKEPARFL 76
VHP smart00153
Villin headpiece domain;
799-834 1.15e-10

Villin headpiece domain;


Pssm-ID: 128458  Cd Length: 36  Bit Score: 56.94  E-value: 1.15e-10
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 41053868    799 YLSDDDFALAMGISRMNFYAMPSWKQLNLKKEKGLF 834
Cdd:smart00153   1 YLSDEDFEEVFGMTREEFYKLPLWKQNQLKKKKGLF 36
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
257-348 2.06e-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: 2.06e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053868 257 LYHISdAQGSLVVQEVAVKPltqDLLKTEDCYLLDQGGIkIFIWKGKKASKAERTESLKMAEAYVKA-KGYPVstyIETV 335
Cdd:cd11280   4 LYRVR-GSKAIEIEEVPLAS---SSLDSDDVFVLDTGSE-IYIWQGRASSQAELAAAALLAKELDEErKGKPE---IVRI 75
                        90
                ....*....|...
gi 41053868 336 SEGAESSVFKQLF 348
Cdd:cd11280  76 RQGQEPREFWSLF 88
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
138-213 6.98e-08

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: 50.83  E-value: 6.98e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41053868 138 RRLLHVKGNKHVVAGEVEMSWNSFNKGDVFLLDLGSLIIQWNGPKSNRMERLRGMNLAKDIrDRERGGRAQVAVVE 213
Cdd:cd11280   2 PRLYRVRGSKAIEIEEVPLASSSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKEL-DEERKGKPEIVRIR 76
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
514-596 2.54e-07

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: 49.56  E-value: 2.54e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053868 514 RPSVRLFHVH-GTNEFNTRATEVPPRSSS-LNSNDVFVLSTDKCCYLWYGKGCSGDEREMAKSLADIISEREK------- 584
Cdd:cd11292   1 AEQKKLYKVSdASGKLKLTEVAEGSLNQEmLDSEDCYILDCGSEIFVWVGKGASLDERKAALKNAEEFLRKKKrppytqv 80
                        90
                ....*....|..
gi 41053868 585 QVIAEGQEPADF 596
Cdd:cd11292  81 TRVTEGGESALF 92
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
255-344 1.35e-05

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: 44.14  E-value: 1.35e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053868 255 IKLYHISdAQGSLVVQEVAVkPLTQDLLKTEDCYLLdQGGIKIFIWKGKKASKAERteslKMAEaYVkAKGYPVSTYIET 334
Cdd:cd11288   3 TRLFQVR-GNGSGNTRAVEV-DADASSLNSNDVFVL-KTPSSVYLWVGKGSSEDER----ELAK-DV-ASFLKPKASLQE 73
                        90
                ....*....|
gi 41053868 335 VSEGAESSVF 344
Cdd:cd11288  74 VAEGSEPDEF 83
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
256-317 6.86e-05

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: 42.22  E-value: 6.86e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41053868 256 KLYHISdAQGSLVVQEVavkPLTQDLLKTEDCYLLDQGGiKIFIWKGKKASKAERTESLKMA 317
Cdd:cd11289   3 RLLHVK-GRRNVRAREV---ELSWSSLNSGDVFILDLGS-TIYQWNGSKSNRFEKAKAMQLA 59
Gelsolin pfam00626
Gelsolin repeat;
528-597 8.32e-05

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 41.52  E-value: 8.32e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41053868   528 FNTRATEVPPRSSSLNSNDVFVLSTDKCCYLWYGKGCSGDEREMAKSLA-DIISER-----EKQVIAEGQEPADFW 597
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAaQLDDDErfplpEVIRVPQGKEPARFL 76
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
139-216 1.59e-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: 41.06  E-value: 1.59e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41053868 139 RLLHVKGNKHVV--AGEVEMSWNSFNKGDVFLLDLGSLIIQWNGPKSNRMERlrgmNLAKDIRDRERGGRAQVAVVEGDD 216
Cdd:cd11288   4 RLFQVRGNGSGNtrAVEVDADASSLNSNDVFVLKTPSSVYLWVGKGSSEDER----ELAKDVASFLKPKASLQEVAEGSE 79
 
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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