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Conserved domains on  [gi|1886442444|gb|KAF6268258|]
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villin 1 [Pipistrellus kuhlii]

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; ...
 17-121 5.92e-52

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: 176.64  E-value: 5.92e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886442444  17 PGVKIWRIEAMQMVPVPPSSFGSFFDGDCYVLLAIHKTGSN-LSYDIHYWIGQASSQDEQGAAAIYTTQMDDFLKGRAVQ 95
Cdd:cd11290     8 PGLQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDPSGsLSYDIHYWLGKEASQDEAGAAAIKAVELDDYLGGRPVQ 87

                          90       100
                  ....*....|....*....|....*.
gi 1886442444  96 HREVQGNESEAFRGYFKKGLVIRKGG 121
Cdd:cd11290    88 HREVQGHESEEFLSYFKKGIIYIEGG 113
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 619-715 6.57e-49

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: 167.47  E-value: 6.57e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886442444 619 PRLFECSNQTGRFLATEIPDFTQDDLEEDDVFLLDVWDQVFFWIGKHANEDEKKAAATTVQEYLKTHPSGRD-PETPIVV 697
Cdd:cd11291     2 PRLFRCSNESGFFKVEEISDFSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYIETDPLGRSkPRTPIYL 81

                          90
                  ....*....|....*...
gi 1886442444 698 VKQGHEPPTFTGWFLAWD 715
Cdd:cd11291    82 VKQGNEPPTFTGYFHAWD 99
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
 392-492 6.22e-46

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: 159.36  E-value: 6.22e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886442444 392 LVDDGSGEVQVWRIENLELVPVEPKWLGHFYGGDCYLLLYTYLIGEKPHYLLYIWQGSQASPDEITASAYQAVILDQQYN 471
Cdd:cd11293     1 MYDDGSGKVEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQGGGKEEHILYFWQGRHSSQDERAAAALLTVELDEELK 80

                          90       100
                  ....*....|....*....|.
gi 1886442444 472 NEPVQIRVPMGKEPLHLMSIF 492
Cdd:cd11293    81 GRAVQVRVVQGKEPPHFLALF 101
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 513-603 6.71e-46

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: 158.93  E-value: 6.71e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886442444 513 PATRLFQVRGTSANNTKAFEVPARASSLNSNDVFILKTPSCCYLWCGKGCSGDEREMAKMVADTIS-RTEKQVVVEGQEP 591
Cdd:cd11288     1 SPTRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVASFLKpKASLQEVAEGSEP 80

                          90
                  ....*....|..
gi 1886442444 592 ANFWMALGGKAP 603
Cdd:cd11288    81 DEFWEALGGKSE 92
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 250-348 3.61e-39

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: 140.08  E-value: 3.61e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886442444 250 KAALKLYHVSDSAGKLVVREVATRPLTQDLLKHEDCYILDQGGlKIYVWKGKKANTEERKGAMSQALNFIKAKQYPPSTQ 329
Cdd:cd11292     1 AEQKKLYKVSDASGKLKLTEVAEGSLNQEMLDSEDCYILDCGS-EIFVWVGKGASLDERKAALKNAEEFLRKKKRPPYTQ 79

                          90
                  ....*....|....*....
gi 1886442444 330 VEVQNDGAESAVFQQLFQK 348
Cdd:cd11292    80 VTRVTEGGESALFKSKFAN 98
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 138-231 4.88e-37

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: 133.90  E-value: 4.88e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886442444 138 RLLHVKGKRNVVAGEVEMSWKSFNRGDVFLLDLGKLIIQWNGPESNHMERLRGTTLAKEIRDQERGGRTYVAVVDGENEK 217
Cdd:cd11289     3 RLLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKVIVLDEGDTN 82

                          90
                  ....*....|....
gi 1886442444 218 ASPQlmevMEHVLG 231
Cdd:cd11289    83 ESPE----FWKVLG 92
VHP pfam02209
Villin headpiece domain;
792-827 3.83e-14

Villin headpiece domain;


:

Pssm-ID: 460493  Cd Length: 36  Bit Score: 66.63  E-value: 3.83e-14
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1886442444 792 HLSPEDFTKALGMTPAAFSALPQWKQQNLKKANGLF 827
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; ...
 17-121 5.92e-52

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: 176.64  E-value: 5.92e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886442444  17 PGVKIWRIEAMQMVPVPPSSFGSFFDGDCYVLLAIHKTGSN-LSYDIHYWIGQASSQDEQGAAAIYTTQMDDFLKGRAVQ 95
Cdd:cd11290     8 PGLQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDPSGsLSYDIHYWLGKEASQDEAGAAAIKAVELDDYLGGRPVQ 87

                          90       100
                  ....*....|....*....|....*.
gi 1886442444  96 HREVQGNESEAFRGYFKKGLVIRKGG 121
Cdd:cd11290    88 HREVQGHESEEFLSYFKKGIIYIEGG 113
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 619-715 6.57e-49

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: 167.47  E-value: 6.57e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886442444 619 PRLFECSNQTGRFLATEIPDFTQDDLEEDDVFLLDVWDQVFFWIGKHANEDEKKAAATTVQEYLKTHPSGRD-PETPIVV 697
Cdd:cd11291     2 PRLFRCSNESGFFKVEEISDFSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYIETDPLGRSkPRTPIYL 81

                          90
                  ....*....|....*...
gi 1886442444 698 VKQGHEPPTFTGWFLAWD 715
Cdd:cd11291    82 VKQGNEPPTFTGYFHAWD 99
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
 392-492 6.22e-46

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: 159.36  E-value: 6.22e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886442444 392 LVDDGSGEVQVWRIENLELVPVEPKWLGHFYGGDCYLLLYTYLIGEKPHYLLYIWQGSQASPDEITASAYQAVILDQQYN 471
Cdd:cd11293     1 MYDDGSGKVEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQGGGKEEHILYFWQGRHSSQDERAAAALLTVELDEELK 80

                          90       100
                  ....*....|....*....|.
gi 1886442444 472 NEPVQIRVPMGKEPLHLMSIF 492
Cdd:cd11293    81 GRAVQVRVVQGKEPPHFLALF 101
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 513-603 6.71e-46

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: 158.93  E-value: 6.71e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886442444 513 PATRLFQVRGTSANNTKAFEVPARASSLNSNDVFILKTPSCCYLWCGKGCSGDEREMAKMVADTIS-RTEKQVVVEGQEP 591
Cdd:cd11288     1 SPTRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVASFLKpKASLQEVAEGSEP 80

                          90
                  ....*....|..
gi 1886442444 592 ANFWMALGGKAP 603
Cdd:cd11288    81 DEFWEALGGKSE 92
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 250-348 3.61e-39

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: 140.08  E-value: 3.61e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886442444 250 KAALKLYHVSDSAGKLVVREVATRPLTQDLLKHEDCYILDQGGlKIYVWKGKKANTEERKGAMSQALNFIKAKQYPPSTQ 329
Cdd:cd11292     1 AEQKKLYKVSDASGKLKLTEVAEGSLNQEMLDSEDCYILDCGS-EIFVWVGKGASLDERKAALKNAEEFLRKKKRPPYTQ 79

                          90
                  ....*....|....*....
gi 1886442444 330 VEVQNDGAESAVFQQLFQK 348
Cdd:cd11292    80 VTRVTEGGESALFKSKFAN 98
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 138-231 4.88e-37

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: 133.90  E-value: 4.88e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886442444 138 RLLHVKGKRNVVAGEVEMSWKSFNRGDVFLLDLGKLIIQWNGPESNHMERLRGTTLAKEIRDQERGGRTYVAVVDGENEK 217
Cdd:cd11289     3 RLLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKVIVLDEGDTN 82

                          90
                  ....*....|....
gi 1886442444 218 ASPQlmevMEHVLG 231
Cdd:cd11289    83 ESPE----FWKVLG 92
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 518-601 4.77e-28

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: 108.15  E-value: 4.77e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886442444  518 FQVRGTSANNTKAFEVPARASSLNSNDVFILKTPSCCYLWCGKGCSGDEREMAKMVADTISRTEK------QVVVEGQEP 591
Cdd:smart00262   1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGpgpvqvRVVDEGKEP 80

                           90
                   ....*....|
gi 1886442444  592 ANFWMALGGK 601
Cdd:smart00262  81 PEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 623-714 6.92e-25

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: 99.29  E-value: 6.92e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886442444  623 ECSNQTGRFLATEIP-DFTQDDLEEDDVFLLDVWDQVFFWIGKHANEDEKKAAATTVQEYLKTHPSGRdpeTPIVVVKQG 701
Cdd:smart00262   1 FLVRVKGKRNVRVPEvPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGP---VQVRVVDEG 77

                           90
                   ....*....|...
gi 1886442444  702 HEPPTFTGWFLAW 714
Cdd:smart00262  78 KEPPEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 401-494 1.00e-22

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: 1.00e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886442444  401 QVWRIENLELVPVE--PKWLGHFYGGDCYLLLYTYLIgekphyllYIWQGSQASPDEITASAYQAVILDQQYNNEPVQIR 478
Cdd:smart00262   1 FLVRVKGKRNVRVPevPFSQGSLNSGDCYILDTGSEI--------YVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVR 72

                           90
                   ....*....|....*..
gi 1886442444  479 -VPMGKEPLHLMSIFKG 494
Cdd:smart00262  73 vVDEGKEPPEFWSLFGG 89
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 20-114 5.15e-22

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: 90.81  E-value: 5.15e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886442444   20 KIWRIEAMQMVPVPPSSF--GSFFDGDCYVLLAihktgsnlSYDIHYWIGQASSQDEQGAAAIYTTQMDDFLKGRAVQHR 97
Cdd:smart00262   1 FLVRVKGKRNVRVPEVPFsqGSLNSGDCYILDT--------GSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVR 72

                           90
                   ....*....|....*...
gi 1886442444   98 EV-QGNESEAFRGYFKKG 114
Cdd:smart00262  73 VVdEGKEPPEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 254-349 7.38e-22

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: 90.43  E-value: 7.38e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886442444  254 KLYHVSdsaGKLVVREVaTRPLTQDLLKHEDCYILDQGGlKIYVWKGKKANTEERKGAMSQALNFIKAKQyPPSTQVEVQ 333
Cdd:smart00262   1 FLVRVK---GKRNVRVP-EVPFSQGSLNSGDCYILDTGS-EIYVWVGKKSSQDEKKKAAELAVELDDTLG-PGPVQVRVV 74

                           90
                   ....*....|....*.
gi 1886442444  334 NDGAESAVFQQLFQKW 349
Cdd:smart00262  75 DEGKEPPEFWSLFGGW 90
Gelsolin pfam00626
Gelsolin repeat;
630-707 1.58e-18

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 80.43  E-value: 1.58e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1886442444 630 RFLATEIPDFTQDDLEEDDVFLLDVWDQVFFWIGKHANEDEKKAAATTVQEYLKTHpsgRDPETPIVVVKQGHEPPTF 707
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDE---RFPLPEVIRVPQGKEPARF 75
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 138-212 3.21e-18

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: 80.03  E-value: 3.21e-18
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1886442444  138 RLLHVKGKRNVVAGEVEMSWKSFNRGDVFLLDLGKLIIQWNGPESNHMERLRGTTLAKEIRDQERGGRTYVAVVD 212
Cdd:smart00262   1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVRVVD 75
Gelsolin pfam00626
Gelsolin repeat;
27-108 1.11e-16

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 75.42  E-value: 1.11e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886442444  27 MQMVPVPPSSFGSFFDGDCYVLLAihktgsnlSYDIHYWIGQASSQDEQGAAAIYTTQMDD-FLKGRAVQHREVQGNESE 105
Cdd:pfam00626   2 FVLPPPVPLSQESLNSGDCYLLDN--------GFTIFLWVGKGSSLLEKLFAALLAAQLDDdERFPLPEVIRVPQGKEPA 73


                  ...
gi 1886442444 106 AFR 108
Cdd:pfam00626  74 RFL 76
Gelsolin pfam00626
Gelsolin repeat;
269-342 6.46e-16

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 73.11  E-value: 6.46e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1886442444 269 EVATRPLTQDLLKHEDCYILDQGgLKIYVWKGKKANTEERKGAMSQALNFIKaKQYPPSTQVEVQNDGAESAVF 342
Cdd:pfam00626   4 LPPPVPLSQESLNSGDCYLLDNG-FTIFLWVGKGSSLLEKLFAALLAAQLDD-DERFPLPEVIRVPQGKEPARF 75
Gelsolin pfam00626
Gelsolin repeat;
407-489 1.19e-15

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 72.34  E-value: 1.19e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886442444 407 NLELVPVEPKWLGHFYGGDCYLLLYTYLIgekphyllYIWQGSQASPDEITASAYQAV-ILDQQYNNEPVQIRVPMGKEP 485
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNGFTI--------FLWVGKGSSLLEKLFAALLAAqLDDDERFPLPEVIRVPQGKEP 72


                  ....
gi 1886442444 486 LHLM 489
Cdd:pfam00626  73 ARFL 76
Gelsolin pfam00626
Gelsolin repeat;
146-216 1.04e-14

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 69.64  E-value: 1.04e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1886442444 146 RNVVAGEVEMSWKSFNRGDVFLLDLGKLIIQWNGPESNHMERLRGTTLAKEIRDQERGGRTYVAVVDGENE 216
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDERFPLPEVIRVPQGKE 71
VHP pfam02209
Villin headpiece domain;
792-827 3.83e-14

Villin headpiece domain;


Pssm-ID: 460493  Cd Length: 36  Bit Score: 66.63  E-value: 3.83e-14
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1886442444 792 HLSPEDFTKALGMTPAAFSALPQWKQQNLKKANGLF 827
Cdd:pfam02209   1 YLSDEDFEEVFGMSREEFYKLPKWKQNNLKKKAGLF 36
VHP smart00153
Villin headpiece domain;
792-827 1.94e-11

Villin headpiece domain;


Pssm-ID: 128458  Cd Length: 36  Bit Score: 59.25  E-value: 1.94e-11
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1886442444  792 HLSPEDFTKALGMTPAAFSALPQWKQQNLKKANGLF 827
Cdd:smart00153   1 YLSDEDFEEVFGMTREEFYKLPLWKQNQLKKKKGLF 36
Gelsolin pfam00626
Gelsolin repeat;
532-595 4.91e-07

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 47.69  E-value: 4.91e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886442444 532 EVPARASSLNSNDVFILKTPSCCYLWCGKGCSGDEREMAKMVA------DTISRTEKQVVVEGQEPANFW 595
Cdd:pfam00626   7 PVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAaqldddERFPLPEVIRVPQGKEPARFL 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; ...
 17-121 5.92e-52

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: 176.64  E-value: 5.92e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886442444  17 PGVKIWRIEAMQMVPVPPSSFGSFFDGDCYVLLAIHKTGSN-LSYDIHYWIGQASSQDEQGAAAIYTTQMDDFLKGRAVQ 95
Cdd:cd11290     8 PGLQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDPSGsLSYDIHYWLGKEASQDEAGAAAIKAVELDDYLGGRPVQ 87

                          90       100
                  ....*....|....*....|....*.
gi 1886442444  96 HREVQGNESEAFRGYFKKGLVIRKGG 121
Cdd:cd11290    88 HREVQGHESEEFLSYFKKGIIYIEGG 113
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 619-715 6.57e-49

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: 167.47  E-value: 6.57e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886442444 619 PRLFECSNQTGRFLATEIPDFTQDDLEEDDVFLLDVWDQVFFWIGKHANEDEKKAAATTVQEYLKTHPSGRD-PETPIVV 697
Cdd:cd11291     2 PRLFRCSNESGFFKVEEISDFSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYIETDPLGRSkPRTPIYL 81

                          90
                  ....*....|....*...
gi 1886442444 698 VKQGHEPPTFTGWFLAWD 715
Cdd:cd11291    82 VKQGNEPPTFTGYFHAWD 99
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
 392-492 6.22e-46

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: 159.36  E-value: 6.22e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886442444 392 LVDDGSGEVQVWRIENLELVPVEPKWLGHFYGGDCYLLLYTYLIGEKPHYLLYIWQGSQASPDEITASAYQAVILDQQYN 471
Cdd:cd11293     1 MYDDGSGKVEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQGGGKEEHILYFWQGRHSSQDERAAAALLTVELDEELK 80

                          90       100
                  ....*....|....*....|.
gi 1886442444 472 NEPVQIRVPMGKEPLHLMSIF 492
Cdd:cd11293    81 GRAVQVRVVQGKEPPHFLALF 101
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 513-603 6.71e-46

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: 158.93  E-value: 6.71e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886442444 513 PATRLFQVRGTSANNTKAFEVPARASSLNSNDVFILKTPSCCYLWCGKGCSGDEREMAKMVADTIS-RTEKQVVVEGQEP 591
Cdd:cd11288     1 SPTRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVASFLKpKASLQEVAEGSEP 80

                          90
                  ....*....|..
gi 1886442444 592 ANFWMALGGKAP 603
Cdd:cd11288    81 DEFWEALGGKSE 92
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 250-348 3.61e-39

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: 140.08  E-value: 3.61e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886442444 250 KAALKLYHVSDSAGKLVVREVATRPLTQDLLKHEDCYILDQGGlKIYVWKGKKANTEERKGAMSQALNFIKAKQYPPSTQ 329
Cdd:cd11292     1 AEQKKLYKVSDASGKLKLTEVAEGSLNQEMLDSEDCYILDCGS-EIFVWVGKGASLDERKAALKNAEEFLRKKKRPPYTQ 79

                          90
                  ....*....|....*....
gi 1886442444 330 VEVQNDGAESAVFQQLFQK 348
Cdd:cd11292    80 VTRVTEGGESALFKSKFAN 98
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 138-231 4.88e-37

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: 133.90  E-value: 4.88e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886442444 138 RLLHVKGKRNVVAGEVEMSWKSFNRGDVFLLDLGKLIIQWNGPESNHMERLRGTTLAKEIRDQERGGRTYVAVVDGENEK 217
Cdd:cd11289     3 RLLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKVIVLDEGDTN 82

                          90
                  ....*....|....
gi 1886442444 218 ASPQlmevMEHVLG 231
Cdd:cd11289    83 ESPE----FWKVLG 92
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 518-601 4.77e-28

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: 108.15  E-value: 4.77e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886442444  518 FQVRGTSANNTKAFEVPARASSLNSNDVFILKTPSCCYLWCGKGCSGDEREMAKMVADTISRTEK------QVVVEGQEP 591
Cdd:smart00262   1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGpgpvqvRVVDEGKEP 80

                           90
                   ....*....|
gi 1886442444  592 ANFWMALGGK 601
Cdd:smart00262  81 PEFWSLFGGW 90
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
 19-111 1.56e-25

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: 101.19  E-value: 1.56e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886442444  19 VKIWRIEAMQMVPVPPSSFGSFFDGDCYVLLAIHKTGSNLSYDIHYWIGQASSQDEQGAAAIYTTQMDDFLKGRAVQHRE 98
Cdd:cd11293     9 VEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQGGGKEEHILYFWQGRHSSQDERAAAALLTVELDEELKGRAVQVRV 88

                          90
                  ....*....|...
gi 1886442444  99 VQGNESEAFRGYF 111
Cdd:cd11293    89 VQGKEPPHFLALF 101
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 623-714 6.92e-25

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: 99.29  E-value: 6.92e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886442444  623 ECSNQTGRFLATEIP-DFTQDDLEEDDVFLLDVWDQVFFWIGKHANEDEKKAAATTVQEYLKTHPSGRdpeTPIVVVKQG 701
Cdd:smart00262   1 FLVRVKGKRNVRVPEvPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGP---VQVRVVDEG 77

                           90
                   ....*....|...
gi 1886442444  702 HEPPTFTGWFLAW 714
Cdd:smart00262  78 KEPPEFWSLFGGW 90
gelsolin_S1_like cd11290
Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; ...
 400-502 6.67e-24

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: 97.29  E-value: 6.67e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886442444 400 VQVWRIENLELVPVEPKWLGHFYGGDCYLLLYTYLIG-EKPHYLLYIWQGSQASPDEITASAYQAVILDQQYNNEPVQIR 478
Cdd:cd11290    10 LQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDPsGSLSYDIHYWLGKEASQDEAGAAAIKAVELDDYLGGRPVQHR 89

                          90       100
                  ....*....|....*....|....
gi 1886442444 479 VPMGKEPLHLMSIFKgQMVVYQGG 502
Cdd:cd11290    90 EVQGHESEEFLSYFK-KGIIYIEG 112
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 401-494 1.00e-22

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: 1.00e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886442444  401 QVWRIENLELVPVE--PKWLGHFYGGDCYLLLYTYLIgekphyllYIWQGSQASPDEITASAYQAVILDQQYNNEPVQIR 478
Cdd:smart00262   1 FLVRVKGKRNVRVPevPFSQGSLNSGDCYILDTGSEI--------YVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVR 72

                           90
                   ....*....|....*..
gi 1886442444  479 -VPMGKEPLHLMSIFKG 494
Cdd:smart00262  73 vVDEGKEPPEFWSLFGG 89
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 20-114 5.15e-22

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: 90.81  E-value: 5.15e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886442444   20 KIWRIEAMQMVPVPPSSF--GSFFDGDCYVLLAihktgsnlSYDIHYWIGQASSQDEQGAAAIYTTQMDDFLKGRAVQHR 97
Cdd:smart00262   1 FLVRVKGKRNVRVPEVPFsqGSLNSGDCYILDT--------GSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVR 72

                           90
                   ....*....|....*...
gi 1886442444   98 EV-QGNESEAFRGYFKKG 114
Cdd:smart00262  73 VVdEGKEPPEFWSLFGGW 90
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 618-711 6.19e-22

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: 91.16  E-value: 6.19e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886442444 618 TPRLFECSNQTGRFLATEIPD--FTQDDLEEDDVFLLDVWDQVFFWIGKHANEDEKKAAATTVQEYLKTHpsGRDPETPI 695
Cdd:cd11292     3 QKKLYKVSDASGKLKLTEVAEgsLNQEMLDSEDCYILDCGSEIFVWVGKGASLDERKAALKNAEEFLRKK--KRPPYTQV 80

                          90
                  ....*....|....*.
gi 1886442444 696 VVVKQGHEPPTFTGWF 711
Cdd:cd11292    81 TRVTEGGESALFKSKF 96
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 254-349 7.38e-22

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: 90.43  E-value: 7.38e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886442444  254 KLYHVSdsaGKLVVREVaTRPLTQDLLKHEDCYILDQGGlKIYVWKGKKANTEERKGAMSQALNFIKAKQyPPSTQVEVQ 333
Cdd:smart00262   1 FLVRVK---GKRNVRVP-EVPFSQGSLNSGDCYILDTGS-EIYVWVGKKSSQDEKKKAAELAVELDDTLG-PGPVQVRVV 74

                           90
                   ....*....|....*.
gi 1886442444  334 NDGAESAVFQQLFQKW 349
Cdd:smart00262  75 DEGKEPPEFWSLFGGW 90
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 21-111 1.56e-18

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: 80.87  E-value: 1.56e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886442444  21 IWRIEA---MQMVPVPPSSfGSFFDGDCYVLlaihKTGSnlsyDIHYWIGQASSQDEQGAAAIYTTQMDDFLKGRAVQHR 97
Cdd:cd11280     4 LYRVRGskaIEIEEVPLAS-SSLDSDDVFVL----DTGS----EIYIWQGRASSQAELAAAALLAKELDEERKGKPEIVR 74

                          90
                  ....*....|....
gi 1886442444  98 EVQGNESEAFRGYF 111
Cdd:cd11280    75 IRQGQEPREFWSLF 88
Gelsolin pfam00626
Gelsolin repeat;
630-707 1.58e-18

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 80.43  E-value: 1.58e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1886442444 630 RFLATEIPDFTQDDLEEDDVFLLDVWDQVFFWIGKHANEDEKKAAATTVQEYLKTHpsgRDPETPIVVVKQGHEPPTF 707
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDE---RFPLPEVIRVPQGKEPARF 75
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 138-212 3.21e-18

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: 80.03  E-value: 3.21e-18
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1886442444  138 RLLHVKGKRNVVAGEVEMSWKSFNRGDVFLLDLGKLIIQWNGPESNHMERLRGTTLAKEIRDQERGGRTYVAVVD 212
Cdd:smart00262   1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVRVVD 75
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 619-711 4.73e-18

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: 79.72  E-value: 4.73e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886442444 619 PRLFECSNQT-GRFlaTEIPDFTQDdLEEDDVFLLDVWDQVFFWIGKHANEDEKKAAATTVQEYLKThpsgRDPETPIVV 697
Cdd:cd11280     2 PRLYRVRGSKaIEI--EEVPLASSS-LDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKELDEE----RKGKPEIVR 74

                          90
                  ....*....|....
gi 1886442444 698 VKQGHEPPTFTGWF 711
Cdd:cd11280    75 IRQGQEPREFWSLF 88
Gelsolin pfam00626
Gelsolin repeat;
27-108 1.11e-16

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 75.42  E-value: 1.11e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886442444  27 MQMVPVPPSSFGSFFDGDCYVLLAihktgsnlSYDIHYWIGQASSQDEQGAAAIYTTQMDD-FLKGRAVQHREVQGNESE 105
Cdd:pfam00626   2 FVLPPPVPLSQESLNSGDCYLLDN--------GFTIFLWVGKGSSLLEKLFAALLAAQLDDdERFPLPEVIRVPQGKEPA 73


                  ...
gi 1886442444 106 AFR 108
Cdd:pfam00626  74 RFL 76
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 254-349 3.84e-16

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: 74.64  E-value: 3.84e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886442444 254 KLYHVSDSAGKLVVREVAtrPLTQDLLKHEDCYILDQGGlKIYVWKGKKANTEERKGAMSQALNFIK---AKQYPPSTQV 330
Cdd:cd11291     3 RLFRCSNESGFFKVEEIS--DFSQDDLDTDDIMLLDTGD-EVFVWVGSESSDEEKKEALTSAKKYIEtdpLGRSKPRTPI 79

                          90
                  ....*....|....*....
gi 1886442444 331 EVQNDGAESAVFQQLFQKW 349
Cdd:cd11291    80 YLVKQGNEPPTFTGYFHAW 98
Gelsolin pfam00626
Gelsolin repeat;
269-342 6.46e-16

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 73.11  E-value: 6.46e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1886442444 269 EVATRPLTQDLLKHEDCYILDQGgLKIYVWKGKKANTEERKGAMSQALNFIKaKQYPPSTQVEVQNDGAESAVF 342
Cdd:pfam00626   4 LPPPVPLSQESLNSGDCYLLDNG-FTIFLWVGKGSSLLEKLFAALLAAQLDD-DERFPLPEVIRVPQGKEPARF 75
Gelsolin pfam00626
Gelsolin repeat;
407-489 1.19e-15

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 72.34  E-value: 1.19e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886442444 407 NLELVPVEPKWLGHFYGGDCYLLLYTYLIgekphyllYIWQGSQASPDEITASAYQAV-ILDQQYNNEPVQIRVPMGKEP 485
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNGFTI--------FLWVGKGSSLLEKLFAALLAAqLDDDERFPLPEVIRVPQGKEP 72


                  ....
gi 1886442444 486 LHLM 489
Cdd:pfam00626  73 ARFL 76
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 514-599 3.31e-15

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: 71.50  E-value: 3.31e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886442444 514 ATRLFQVRGTsaNNTKAFEVPARASSLNSNDVFILKTPSCCYLWCGKGCSGDEREMAKMVADTI------SRTEKQVVVE 587
Cdd:cd11289     1 KPRLLHVKGR--RNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIrderrlGRAKVIVLDE 78

                          90
                  ....*....|....
gi 1886442444 588 G--QEPANFWMALG 599
Cdd:cd11289    79 GdtNESPEFWKVLG 92
Gelsolin pfam00626
Gelsolin repeat;
146-216 1.04e-14

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 69.64  E-value: 1.04e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1886442444 146 RNVVAGEVEMSWKSFNRGDVFLLDLGKLIIQWNGPESNHMERLRGTTLAKEIRDQERGGRTYVAVVDGENE 216
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDERFPLPEVIRVPQGKE 71
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 401-492 1.47e-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: 1.47e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886442444 401 QVWRIENLELVPVEPKWLGH--FYGGDCYLLLYTYLIgekphyllYIWQGSQASPDEITASAYQAVILDQQYNNEPVQIR 478
Cdd:cd11280     3 RLYRVRGSKAIEIEEVPLASssLDSDDVFVLDTGSEI--------YIWQGRASSQAELAAAALLAKELDEERKGKPEIVR 74

                          90
                  ....*....|....
gi 1886442444 479 VPMGKEPLHLMSIF 492
Cdd:cd11280    75 IRQGQEPREFWSLF 88
VHP pfam02209
Villin headpiece domain;
792-827 3.83e-14

Villin headpiece domain;


Pssm-ID: 460493  Cd Length: 36  Bit Score: 66.63  E-value: 3.83e-14
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1886442444 792 HLSPEDFTKALGMTPAAFSALPQWKQQNLKKANGLF 827
Cdd:pfam02209   1 YLSDEDFEEVFGMSREEFYKLPKWKQNNLKKKAGLF 36
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 514-595 3.14e-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: 3.14e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886442444 514 ATRLFQVRGTSAnnTKAFEVPARASSLNSNDVFILKTPSCCYLWCGKGCSGDE----REMAKMVADTI-SRTEKQVVVEG 588
Cdd:cd11280     1 PPRLYRVRGSKA--IEIEEVPLASSSLDSDDVFVLDTGSEIYIWQGRASSQAElaaaALLAKELDEERkGKPEIVRIRQG 78


                  ....*..
gi 1886442444 589 QEPANFW 595
Cdd:cd11280    79 QEPREFW 85
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 254-346 1.39e-11

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: 61.48  E-value: 1.39e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886442444 254 KLYHVSdsaGKLVVReVATRPLTQDLLKHEDCYILDQGgLKIYVWKGKKANTEERKGAMsQALNFIKAKQYPPSTQVEVQ 333
Cdd:cd11289     3 RLLHVK---GRRNVR-AREVELSWSSLNSGDVFILDLG-STIYQWNGSKSNRFEKAKAM-QLAQGIRDERRLGRAKVIVL 76

                          90
                  ....*....|....*
gi 1886442444 334 NDGA--ESAVFQQLF 346
Cdd:cd11289    77 DEGDtnESPEFWKVL 91
VHP smart00153
Villin headpiece domain;
792-827 1.94e-11

Villin headpiece domain;


Pssm-ID: 128458  Cd Length: 36  Bit Score: 59.25  E-value: 1.94e-11
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1886442444  792 HLSPEDFTKALGMTPAAFSALPQWKQQNLKKANGLF 827
Cdd:smart00153   1 YLSDEDFEEVFGMTREEFYKLPLWKQNQLKKKKGLF 36
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 512-594 1.05e-09

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: 56.10  E-value: 1.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886442444 512 APATRLFQVrGTSANNTKAFEV---PARASSLNSNDVFILKTPSCCYLWCGKGCSGDEREMAKMVADTISRTEK------ 582
Cdd:cd11292     1 AEQKKLYKV-SDASGKLKLTEVaegSLNQEMLDSEDCYILDCGSEIFVWVGKGASLDERKAALKNAEEFLRKKKrppytq 79

                          90
                  ....*....|...
gi 1886442444 583 -QVVVEGQEPANF 594
Cdd:cd11292    80 vTRVTEGGESALF 92
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 255-346 6.15e-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: 6.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886442444 255 LYHVSDS-AGKLVvrEVATRPltqDLLKHEDCYILDQGgLKIYVWKGKKANTEERKGAMSQALNFIkaKQYPPSTQVEVQ 333
Cdd:cd11280     4 LYRVRGSkAIEIE--EVPLAS---SSLDSDDVFVLDTG-SEIYIWQGRASSQAELAAAALLAKELD--EERKGKPEIVRI 75

                          90
                  ....*....|...
gi 1886442444 334 NDGAESAVFQQLF 346
Cdd:cd11280    76 RQGQEPREFWSLF 88
Gelsolin pfam00626
Gelsolin repeat;
532-595 4.91e-07

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 47.69  E-value: 4.91e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886442444 532 EVPARASSLNSNDVFILKTPSCCYLWCGKGCSGDEREMAKMVA------DTISRTEKQVVVEGQEPANFW 595
Cdd:pfam00626   7 PVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAaqldddERFPLPEVIRVPQGKEPARFL 76
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 254-342 6.29e-07

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: 48.00  E-value: 6.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886442444 254 KLYHV---SDSAGKLV-VREVATrpltqdLLKHEDCYILdQGGLKIYVWKGKKANTEERKGAMSQAlNFIKakqypPSTQ 329
Cdd:cd11288     4 RLFQVrgnGSGNTRAVeVDADAS------SLNSNDVFVL-KTPSSVYLWVGKGSSEDERELAKDVA-SFLK-----PKAS 70

                          90
                  ....*....|...
gi 1886442444 330 VEVQNDGAESAVF 342
Cdd:cd11288    71 LQEVAEGSEPDEF 83
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 137-214 1.59e-06

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


Pssm-ID: 200436  Cd Length: 88  Bit Score: 46.98  E-value: 1.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886442444 137 RRLLHVKGKRNVVAGEVEMSWKSFNRGDVFLLDLGKLIIQWNGPESNhMERLRGT-TLAKEIrDQERGGRT-YVAVVDGE 214
Cdd:cd11280     2 PRLYRVRGSKAIEIEEVPLASSSLDSDDVFVLDTGSEIYIWQGRASS-QAELAAAaLLAKEL-DEERKGKPeIVRIRQGQ 79
gelsolin_S1_like cd11290
Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; ...
 655-711 8.64e-04

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: 39.90  E-value: 8.64e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1886442444 655 WDqVFFWIGKHANEDEKKAAAT-TVQ--EYLkthpsGRDP----ETpivvvkQGHEPPTFTGWF 711
Cdd:cd11290    52 YD-IHYWLGKEASQDEAGAAAIkAVEldDYL-----GGRPvqhrEV------QGHESEEFLSYF 103
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
 658-711 1.25e-03

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: 38.79  E-value: 1.25e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1886442444 658 VFFWIGKHANEDEKKAAAT-TVQ--EYLKTHPSgrdpetpIVVVKQGHEPPTFTGWF 711
Cdd:cd11293    52 LYFWQGRHSSQDERAAAALlTVEldEELKGRAV-------QVRVVQGKEPPHFLALF 101
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 43-113 1.32e-03

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


Pssm-ID: 200448  Cd Length: 98  Bit Score: 38.77  E-value: 1.32e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1886442444  43 GDCYVLLAIHKtgsnlsydIHYWIGQASSQDEQGAAAIYTTQmddFL--KGRAVQ---HREVQGNESEAFRGYFKK 113
Cdd:cd11292    34 EDCYILDCGSE--------IFVWVGKGASLDERKAALKNAEE---FLrkKKRPPYtqvTRVTEGGESALFKSKFAN 98
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 138-214 4.46e-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: 37.21  E-value: 4.46e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1886442444 138 RLLHVKG--KRNVVAGEVEMSWKSFNRGDVFLLDLGKLIIQWNGPESNHMERlrgtTLAKEIRDQERGGRTYVAVVDGE 214
Cdd:cd11288     4 RLFQVRGngSGNTRAVEVDADASSLNSNDVFVLKTPSSVYLWVGKGSSEDER----ELAKDVASFLKPKASLQEVAEGS 78
 
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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