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Conserved domains on  [gi|1123971199|ref|XP_019597412|]
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PREDICTED: villin-1 [Rhinolophus sinicus]

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 6.55e-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: 6.55e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123971199  17 PGIQIWRIEAMQMVPVPSSTFGSFFDGDCYIVLAIHKTGSR-LSYDIHYWIGRASSQDEQGAAAIYTTQMDDFLKGQAVQ 95
Cdd:cd11290     8 PGLQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDPSGsLSYDIHYWLGKEASQDEAGAAAIKAVELDDYLGGRPVQ 87

                          90       100
                  ....*....|....*....|....*.
gi 1123971199  96 HREVQGNESDAFRGYFKQGLVIRKGG 121
Cdd:cd11290    88 HREVQGHESEEFLSYFKKGIIYIEGG 113
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 620-715 9.32e-47

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


:

Pssm-ID: 200447 [Multi-domain]  Cd Length: 99  Bit Score: 161.70  E-value: 9.32e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123971199 620 RLFECSNQTGCFRATEIPDFTQDDLEEDDVFLLDVWDQVFFWIGKHANEDEKKAAAITVQEYLKTHPSGRD-PETPIIVV 698
Cdd:cd11291     3 RLFRCSNESGFFKVEEISDFSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYIETDPLGRSkPRTPIYLV 82

                          90
                  ....*....|....*..
gi 1123971199 699 KQGHEPATFTGWFLAWD 715
Cdd:cd11291    83 KQGNEPPTFTGYFHAWD 99
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
 392-492 3.15e-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: 160.13  E-value: 3.15e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123971199 392 MVDDGSGEVQVWRIENLELVPVDSKWLGHFFGGDCYLLLYTYLIGEKQHYLLYIWQGSQASPDEITASAYQAVILDQQYN 471
Cdd:cd11293     1 MYDDGSGKVEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQGGGKEEHILYFWQGRHSSQDERAAAALLTVELDEELK 80

                          90       100
                  ....*....|....*....|.
gi 1123971199 472 NEPVQIRVPMGKEPSHLMSIF 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 8.93e-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: 158.55  E-value: 8.93e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123971199 513 PSTRLFQVRGTSSNNTKAFEVSARASSLNSNDVFILKTPSCCYLWYGKGCSGDEREMAKMVANTIS-RTEKQVVVEGQEP 591
Cdd:cd11288     1 SPTRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVASFLKpKASLQEVAEGSEP 80

                          90
                  ....*....|..
gi 1123971199 592 ANFWVALGGKAP 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 6.11e-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: 139.31  E-value: 6.11e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123971199 250 KAALKLYHVSDSEGKLVVREVATRPLTQDLLSHEDCYILDQGGlKIYVWKGKNANAQERKGAMSQALNFIKAKQYPPSTQ 329
Cdd:cd11292     1 AEQKKLYKVSDASGKLKLTEVAEGSLNQEMLDSEDCYILDCGS-EIFVWVGKGASLDERKAALKNAEEFLRKKKRPPYTQ 79

                          90
                  ....*....|....*....
gi 1123971199 330 IEVQNDGAESAVFQQLFQK 348
Cdd:cd11292    80 VTRVTEGGESALFKSKFAN 98
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 136-225 1.32e-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: 135.44  E-value: 1.32e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123971199 136 VQRLLHVKGKRNVVAGEVEMSWRSFNRGDVFLLDLGKLIIQWNGPESNRMERLRGMTLAKEIRDQERGGRTYVAVVEGEN 215
Cdd:cd11289     1 KPRLLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKVIVLDEGD 80

                          90
                  ....*....|
gi 1123971199 216 EKASPQLMEV 225
Cdd:cd11289    81 TNESPEFWKV 90
VHP pfam02209
Villin headpiece domain;
792-827 8.78e-13

Villin headpiece domain;


:

Pssm-ID: 460493  Cd Length: 36  Bit Score: 62.78  E-value: 8.78e-13
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1123971199 792 HLSVEDFTKALGMTPDAFSVLPRWKQQNLKKAKGLF 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 6.55e-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: 6.55e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123971199  17 PGIQIWRIEAMQMVPVPSSTFGSFFDGDCYIVLAIHKTGSR-LSYDIHYWIGRASSQDEQGAAAIYTTQMDDFLKGQAVQ 95
Cdd:cd11290     8 PGLQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDPSGsLSYDIHYWLGKEASQDEAGAAAIKAVELDDYLGGRPVQ 87

                          90       100
                  ....*....|....*....|....*.
gi 1123971199  96 HREVQGNESDAFRGYFKQGLVIRKGG 121
Cdd:cd11290    88 HREVQGHESEEFLSYFKKGIIYIEGG 113
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 620-715 9.32e-47

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


Pssm-ID: 200447 [Multi-domain]  Cd Length: 99  Bit Score: 161.70  E-value: 9.32e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123971199 620 RLFECSNQTGCFRATEIPDFTQDDLEEDDVFLLDVWDQVFFWIGKHANEDEKKAAAITVQEYLKTHPSGRD-PETPIIVV 698
Cdd:cd11291     3 RLFRCSNESGFFKVEEISDFSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYIETDPLGRSkPRTPIYLV 82

                          90
                  ....*....|....*..
gi 1123971199 699 KQGHEPATFTGWFLAWD 715
Cdd:cd11291    83 KQGNEPPTFTGYFHAWD 99
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
 392-492 3.15e-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: 160.13  E-value: 3.15e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123971199 392 MVDDGSGEVQVWRIENLELVPVDSKWLGHFFGGDCYLLLYTYLIGEKQHYLLYIWQGSQASPDEITASAYQAVILDQQYN 471
Cdd:cd11293     1 MYDDGSGKVEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQGGGKEEHILYFWQGRHSSQDERAAAALLTVELDEELK 80

                          90       100
                  ....*....|....*....|.
gi 1123971199 472 NEPVQIRVPMGKEPSHLMSIF 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 8.93e-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: 158.55  E-value: 8.93e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123971199 513 PSTRLFQVRGTSSNNTKAFEVSARASSLNSNDVFILKTPSCCYLWYGKGCSGDEREMAKMVANTIS-RTEKQVVVEGQEP 591
Cdd:cd11288     1 SPTRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVASFLKpKASLQEVAEGSEP 80

                          90
                  ....*....|..
gi 1123971199 592 ANFWVALGGKAP 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 6.11e-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: 139.31  E-value: 6.11e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123971199 250 KAALKLYHVSDSEGKLVVREVATRPLTQDLLSHEDCYILDQGGlKIYVWKGKNANAQERKGAMSQALNFIKAKQYPPSTQ 329
Cdd:cd11292     1 AEQKKLYKVSDASGKLKLTEVAEGSLNQEMLDSEDCYILDCGS-EIFVWVGKGASLDERKAALKNAEEFLRKKKRPPYTQ 79

                          90
                  ....*....|....*....
gi 1123971199 330 IEVQNDGAESAVFQQLFQK 348
Cdd:cd11292    80 VTRVTEGGESALFKSKFAN 98
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 136-225 1.32e-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: 135.44  E-value: 1.32e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123971199 136 VQRLLHVKGKRNVVAGEVEMSWRSFNRGDVFLLDLGKLIIQWNGPESNRMERLRGMTLAKEIRDQERGGRTYVAVVEGEN 215
Cdd:cd11289     1 KPRLLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKVIVLDEGD 80

                          90
                  ....*....|
gi 1123971199 216 EKASPQLMEV 225
Cdd:cd11289    81 TNESPEFWKV 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 518-601 4.05e-26

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: 102.76  E-value: 4.05e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123971199  518 FQVRGTSSNNTKAFEVSARASSLNSNDVFILKTPSCCYLWYGKGCSGDEREMAKMVANTISRTEK------QVVVEGQEP 591
Cdd:smart00262   1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGpgpvqvRVVDEGKEP 80

                           90
                   ....*....|
gi 1123971199  592 ANFWVALGGK 601
Cdd:smart00262  81 PEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 623-714 2.92e-24

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 97.36  E-value: 2.92e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123971199  623 ECSNQTGCFRATEIP-DFTQDDLEEDDVFLLDVWDQVFFWIGKHANEDEKKAAAITVQEYLKTHPSGRdpeTPIIVVKQG 701
Cdd:smart00262   1 FLVRVKGKRNVRVPEvPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGP---VQVRVVDEG 77

                           90
                   ....*....|...
gi 1123971199  702 HEPATFTGWFLAW 714
Cdd:smart00262  78 KEPPEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 257-349 1.63e-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: 92.36  E-value: 1.63e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123971199  257 HVSDSEGKLVVREVaTRPLTQDLLSHEDCYILDQGGlKIYVWKGKNANAQERKGAMSQALNFIKAKQyPPSTQIEVQNDG 336
Cdd:smart00262   1 FLVRVKGKRNVRVP-EVPFSQGSLNSGDCYILDTGS-EIYVWVGKKSSQDEKKKAAELAVELDDTLG-PGPVQVRVVDEG 77

                           90
                   ....*....|...
gi 1123971199  337 AESAVFQQLFQKW 349
Cdd:smart00262  78 KEPPEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 401-494 9.98e-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: 90.04  E-value: 9.98e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123971199  401 QVWRIENLELVPVD--SKWLGHFFGGDCYLLLYTYLIgekqhyllYIWQGSQASPDEITASAYQAVILDQQYNNEPVQIR 478
Cdd:smart00262   1 FLVRVKGKRNVRVPevPFSQGSLNSGDCYILDTGSEI--------YVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVR 72

                           90
                   ....*....|....*..
gi 1123971199  479 -VPMGKEPSHLMSIFKG 494
Cdd:smart00262  73 vVDEGKEPPEFWSLFGG 89
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 20-112 1.26e-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: 86.96  E-value: 1.26e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123971199   20 QIWRIEAMQMVPVPSSTF--GSFFDGDCYIVLAihktgsrlSYDIHYWIGRASSQDEQGAAAIYTTQMDDFLKGQAVQHR 97
Cdd:smart00262   1 FLVRVKGKRNVRVPEVPFsqGSLNSGDCYILDT--------GSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVR 72

                           90
                   ....*....|....*.
gi 1123971199   98 EV-QGNESDAFRGYFK 112
Cdd:smart00262  73 VVdEGKEPPEFWSLFG 88
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 138-214 1.25e-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: 81.18  E-value: 1.25e-18
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1123971199  138 RLLHVKGKRNVVAGEVEMSWRSFNRGDVFLLDLGKLIIQWNGPESNRMERLRGMTLAKEIRDQERGGRTYVAVV-EGE 214
Cdd:smart00262   1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVRVVdEGK 78
Gelsolin pfam00626
Gelsolin repeat;
635-707 1.81e-18

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 80.43  E-value: 1.81e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1123971199 635 EIPDFTQDDLEEDDVFLLDVWDQVFFWIGKHANEDEKKAAAITVQEYLKTHpsgRDPETPIIVVKQGHEPATF 707
Cdd:pfam00626   6 PPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDE---RFPLPEVIRVPQGKEPARF 75
Gelsolin pfam00626
Gelsolin repeat;
146-216 1.52e-15

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 71.96  E-value: 1.52e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1123971199 146 RNVVAGEVEMSWRSFNRGDVFLLDLGKLIIQWNGPESNRMERLRGMTLAKEIRDQERGGRTYVAVVEGENE 216
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDERFPLPEVIRVPQGKE 71
Gelsolin pfam00626
Gelsolin repeat;
407-489 2.53e-15

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 71.57  E-value: 2.53e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123971199 407 NLELVPVDSKWLGHFFGGDCYLLLYTYLIgekqhyllYIWQGSQASPDEITASAYQAV-ILDQQYNNEPVQIRVPMGKEP 485
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNGFTI--------FLWVGKGSSLLEKLFAALLAAqLDDDERFPLPEVIRVPQGKEP 72


                  ....
gi 1123971199 486 SHLM 489
Cdd:pfam00626  73 ARFL 76
Gelsolin pfam00626
Gelsolin repeat;
269-342 3.29e-15

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 71.18  E-value: 3.29e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1123971199 269 EVATRPLTQDLLSHEDCYILDQGgLKIYVWKGKNANAQERKGAMSQALNFIKaKQYPPSTQIEVQNDGAESAVF 342
Cdd:pfam00626   4 LPPPVPLSQESLNSGDCYLLDNG-FTIFLWVGKGSSLLEKLFAALLAAQLDD-DERFPLPEVIRVPQGKEPARF 75
Gelsolin pfam00626
Gelsolin repeat;
27-108 6.38e-15

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 70.41  E-value: 6.38e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123971199  27 MQMVPVPSSTFGSFFDGDCYIVLAihktgsrlSYDIHYWIGRASSQDEQGAAAIYTTQMDD-FLKGQAVQHREVQGNESD 105
Cdd:pfam00626   2 FVLPPPVPLSQESLNSGDCYLLDN--------GFTIFLWVGKGSSLLEKLFAALLAAQLDDdERFPLPEVIRVPQGKEPA 73


                  ...
gi 1123971199 106 AFR 108
Cdd:pfam00626  74 RFL 76
VHP pfam02209
Villin headpiece domain;
792-827 8.78e-13

Villin headpiece domain;


Pssm-ID: 460493  Cd Length: 36  Bit Score: 62.78  E-value: 8.78e-13
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1123971199 792 HLSVEDFTKALGMTPDAFSVLPRWKQQNLKKAKGLF 827
Cdd:pfam02209   1 YLSDEDFEEVFGMSREEFYKLPKWKQNNLKKKAGLF 36
VHP smart00153
Villin headpiece domain;
792-827 1.30e-10

Villin headpiece domain;


Pssm-ID: 128458  Cd Length: 36  Bit Score: 56.94  E-value: 1.30e-10
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1123971199  792 HLSVEDFTKALGMTPDAFSVLPRWKQQNLKKAKGLF 827
Cdd:smart00153   1 YLSDEDFEEVFGMTREEFYKLPLWKQNQLKKKKGLF 36
Gelsolin pfam00626
Gelsolin repeat;
532-595 1.70e-05

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 43.45  E-value: 1.70e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123971199 532 EVSARASSLNSNDVFILKTPSCCYLWYGKGCSGDEREMAKMVANTIS------RTEKQVVVEGQEPANFW 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 6.55e-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: 6.55e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123971199  17 PGIQIWRIEAMQMVPVPSSTFGSFFDGDCYIVLAIHKTGSR-LSYDIHYWIGRASSQDEQGAAAIYTTQMDDFLKGQAVQ 95
Cdd:cd11290     8 PGLQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDPSGsLSYDIHYWLGKEASQDEAGAAAIKAVELDDYLGGRPVQ 87

                          90       100
                  ....*....|....*....|....*.
gi 1123971199  96 HREVQGNESDAFRGYFKQGLVIRKGG 121
Cdd:cd11290    88 HREVQGHESEEFLSYFKKGIIYIEGG 113
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 620-715 9.32e-47

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


Pssm-ID: 200447 [Multi-domain]  Cd Length: 99  Bit Score: 161.70  E-value: 9.32e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123971199 620 RLFECSNQTGCFRATEIPDFTQDDLEEDDVFLLDVWDQVFFWIGKHANEDEKKAAAITVQEYLKTHPSGRD-PETPIIVV 698
Cdd:cd11291     3 RLFRCSNESGFFKVEEISDFSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYIETDPLGRSkPRTPIYLV 82

                          90
                  ....*....|....*..
gi 1123971199 699 KQGHEPATFTGWFLAWD 715
Cdd:cd11291    83 KQGNEPPTFTGYFHAWD 99
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
 392-492 3.15e-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: 160.13  E-value: 3.15e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123971199 392 MVDDGSGEVQVWRIENLELVPVDSKWLGHFFGGDCYLLLYTYLIGEKQHYLLYIWQGSQASPDEITASAYQAVILDQQYN 471
Cdd:cd11293     1 MYDDGSGKVEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQGGGKEEHILYFWQGRHSSQDERAAAALLTVELDEELK 80

                          90       100
                  ....*....|....*....|.
gi 1123971199 472 NEPVQIRVPMGKEPSHLMSIF 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 8.93e-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: 158.55  E-value: 8.93e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123971199 513 PSTRLFQVRGTSSNNTKAFEVSARASSLNSNDVFILKTPSCCYLWYGKGCSGDEREMAKMVANTIS-RTEKQVVVEGQEP 591
Cdd:cd11288     1 SPTRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVASFLKpKASLQEVAEGSEP 80

                          90
                  ....*....|..
gi 1123971199 592 ANFWVALGGKAP 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 6.11e-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: 139.31  E-value: 6.11e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123971199 250 KAALKLYHVSDSEGKLVVREVATRPLTQDLLSHEDCYILDQGGlKIYVWKGKNANAQERKGAMSQALNFIKAKQYPPSTQ 329
Cdd:cd11292     1 AEQKKLYKVSDASGKLKLTEVAEGSLNQEMLDSEDCYILDCGS-EIFVWVGKGASLDERKAALKNAEEFLRKKKRPPYTQ 79

                          90
                  ....*....|....*....
gi 1123971199 330 IEVQNDGAESAVFQQLFQK 348
Cdd:cd11292    80 VTRVTEGGESALFKSKFAN 98
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 136-225 1.32e-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: 135.44  E-value: 1.32e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123971199 136 VQRLLHVKGKRNVVAGEVEMSWRSFNRGDVFLLDLGKLIIQWNGPESNRMERLRGMTLAKEIRDQERGGRTYVAVVEGEN 215
Cdd:cd11289     1 KPRLLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKVIVLDEGD 80

                          90
                  ....*....|
gi 1123971199 216 EKASPQLMEV 225
Cdd:cd11289    81 TNESPEFWKV 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 518-601 4.05e-26

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: 102.76  E-value: 4.05e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123971199  518 FQVRGTSSNNTKAFEVSARASSLNSNDVFILKTPSCCYLWYGKGCSGDEREMAKMVANTISRTEK------QVVVEGQEP 591
Cdd:smart00262   1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGpgpvqvRVVDEGKEP 80

                           90
                   ....*....|
gi 1123971199  592 ANFWVALGGK 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 7.60e-26

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: 102.35  E-value: 7.60e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123971199  19 IQIWRIEAMQMVPVPSSTFGSFFDGDCYIVLAIHKTGSRLSYDIHYWIGRASSQDEQGAAAIYTTQMDDFLKGQAVQHRE 98
Cdd:cd11293     9 VEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQGGGKEEHILYFWQGRHSSQDERAAAALLTVELDEELKGRAVQVRV 88

                          90
                  ....*....|...
gi 1123971199  99 VQGNESDAFRGYF 111
Cdd:cd11293    89 VQGKEPPHFLALF 101
gelsolin_S1_like cd11290
Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; ...
 400-502 2.84e-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: 98.06  E-value: 2.84e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123971199 400 VQVWRIENLELVPVDSKWLGHFFGGDCYLLLYTYLIG-EKQHYLLYIWQGSQASPDEITASAYQAVILDQQYNNEPVQIR 478
Cdd:cd11290    10 LQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDPsGSLSYDIHYWLGKEASQDEAGAAAIKAVELDDYLGGRPVQHR 89

                          90       100
                  ....*....|....*....|....
gi 1123971199 479 VPMGKEPSHLMSIFKgRMVVYQGG 502
Cdd:cd11290    90 EVQGHESEEFLSYFK-KGIIYIEG 112
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 623-714 2.92e-24

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 97.36  E-value: 2.92e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123971199  623 ECSNQTGCFRATEIP-DFTQDDLEEDDVFLLDVWDQVFFWIGKHANEDEKKAAAITVQEYLKTHPSGRdpeTPIIVVKQG 701
Cdd:smart00262   1 FLVRVKGKRNVRVPEvPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGP---VQVRVVDEG 77

                           90
                   ....*....|...
gi 1123971199  702 HEPATFTGWFLAW 714
Cdd:smart00262  78 KEPPEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 257-349 1.63e-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: 92.36  E-value: 1.63e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123971199  257 HVSDSEGKLVVREVaTRPLTQDLLSHEDCYILDQGGlKIYVWKGKNANAQERKGAMSQALNFIKAKQyPPSTQIEVQNDG 336
Cdd:smart00262   1 FLVRVKGKRNVRVP-EVPFSQGSLNSGDCYILDTGS-EIYVWVGKKSSQDEKKKAAELAVELDDTLG-PGPVQVRVVDEG 77

                           90
                   ....*....|...
gi 1123971199  337 AESAVFQQLFQKW 349
Cdd:smart00262  78 KEPPEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 401-494 9.98e-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: 90.04  E-value: 9.98e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123971199  401 QVWRIENLELVPVD--SKWLGHFFGGDCYLLLYTYLIgekqhyllYIWQGSQASPDEITASAYQAVILDQQYNNEPVQIR 478
Cdd:smart00262   1 FLVRVKGKRNVRVPevPFSQGSLNSGDCYILDTGSEI--------YVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVR 72

                           90
                   ....*....|....*..
gi 1123971199  479 -VPMGKEPSHLMSIFKG 494
Cdd:smart00262  73 vVDEGKEPPEFWSLFGG 89
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 616-711 1.06e-21

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


Pssm-ID: 200448  Cd Length: 98  Bit Score: 90.39  E-value: 1.06e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123971199 616 VVTARLFECSNQTGCFRATEIPD--FTQDDLEEDDVFLLDVWDQVFFWIGKHANEDEKKAAAITVQEYLKTHpsGRDPET 693
Cdd:cd11292     1 AEQKKLYKVSDASGKLKLTEVAEgsLNQEMLDSEDCYILDCGSEIFVWVGKGASLDERKAALKNAEEFLRKK--KRPPYT 78

                          90
                  ....*....|....*...
gi 1123971199 694 PIIVVKQGHEPATFTGWF 711
Cdd:cd11292    79 QVTRVTEGGESALFKSKF 96
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 20-112 1.26e-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: 86.96  E-value: 1.26e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123971199   20 QIWRIEAMQMVPVPSSTF--GSFFDGDCYIVLAihktgsrlSYDIHYWIGRASSQDEQGAAAIYTTQMDDFLKGQAVQHR 97
Cdd:smart00262   1 FLVRVKGKRNVRVPEVPFsqGSLNSGDCYILDT--------GSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVR 72

                           90
                   ....*....|....*.
gi 1123971199   98 EV-QGNESDAFRGYFK 112
Cdd:smart00262  73 VVdEGKEPPEFWSLFG 88
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 138-214 1.25e-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: 81.18  E-value: 1.25e-18
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1123971199  138 RLLHVKGKRNVVAGEVEMSWRSFNRGDVFLLDLGKLIIQWNGPESNRMERLRGMTLAKEIRDQERGGRTYVAVV-EGE 214
Cdd:smart00262   1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVRVVdEGK 78
Gelsolin pfam00626
Gelsolin repeat;
635-707 1.81e-18

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 80.43  E-value: 1.81e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1123971199 635 EIPDFTQDDLEEDDVFLLDVWDQVFFWIGKHANEDEKKAAAITVQEYLKTHpsgRDPETPIIVVKQGHEPATF 707
Cdd:pfam00626   6 PPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDE---RFPLPEVIRVPQGKEPARF 75
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 620-711 6.21e-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: 79.33  E-value: 6.21e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123971199 620 RLFECSNQTGcFRATEIPDFTQDdLEEDDVFLLDVWDQVFFWIGKHANEDEKKAAAITVQEYLKThpsgRDPETPIIVVK 699
Cdd:cd11280     3 RLYRVRGSKA-IEIEEVPLASSS-LDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKELDEE----RKGKPEIVRIR 76

                          90
                  ....*....|..
gi 1123971199 700 QGHEPATFTGWF 711
Cdd:cd11280    77 QGQEPREFWSLF 88
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 18-111 1.83e-17

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


Pssm-ID: 200436  Cd Length: 88  Bit Score: 77.79  E-value: 1.83e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123971199  18 GIQIWRIEA---MQMVPVPSSTfGSFFDGDCYIVlaihKTGSrlsyDIHYWIGRASSQDEQGAAAIYTTQMDDFLKGQAV 94
Cdd:cd11280     1 PPRLYRVRGskaIEIEEVPLAS-SSLDSDDVFVL----DTGS----EIYIWQGRASSQAELAAAALLAKELDEERKGKPE 71

                          90
                  ....*....|....*..
gi 1123971199  95 QHREVQGNESDAFRGYF 111
Cdd:cd11280    72 IVRIRQGQEPREFWSLF 88
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 254-349 5.76e-17

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


Pssm-ID: 200447 [Multi-domain]  Cd Length: 99  Bit Score: 76.95  E-value: 5.76e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123971199 254 KLYHVSDSEGKLVVREVAtrPLTQDLLSHEDCYILDQGGlKIYVWKGKNANAQERKGAMSQALNFIK---AKQYPPSTQI 330
Cdd:cd11291     3 RLFRCSNESGFFKVEEIS--DFSQDDLDTDDIMLLDTGD-EVFVWVGSESSDEEKKEALTSAKKYIEtdpLGRSKPRTPI 79

                          90
                  ....*....|....*....
gi 1123971199 331 EVQNDGAESAVFQQLFQKW 349
Cdd:cd11291    80 YLVKQGNEPPTFTGYFHAW 98
Gelsolin pfam00626
Gelsolin repeat;
146-216 1.52e-15

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 71.96  E-value: 1.52e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1123971199 146 RNVVAGEVEMSWRSFNRGDVFLLDLGKLIIQWNGPESNRMERLRGMTLAKEIRDQERGGRTYVAVVEGENE 216
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDERFPLPEVIRVPQGKE 71
Gelsolin pfam00626
Gelsolin repeat;
407-489 2.53e-15

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 71.57  E-value: 2.53e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123971199 407 NLELVPVDSKWLGHFFGGDCYLLLYTYLIgekqhyllYIWQGSQASPDEITASAYQAV-ILDQQYNNEPVQIRVPMGKEP 485
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNGFTI--------FLWVGKGSSLLEKLFAALLAAqLDDDERFPLPEVIRVPQGKEP 72


                  ....
gi 1123971199 486 SHLM 489
Cdd:pfam00626  73 ARFL 76
Gelsolin pfam00626
Gelsolin repeat;
269-342 3.29e-15

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 71.18  E-value: 3.29e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1123971199 269 EVATRPLTQDLLSHEDCYILDQGgLKIYVWKGKNANAQERKGAMSQALNFIKaKQYPPSTQIEVQNDGAESAVF 342
Cdd:pfam00626   4 LPPPVPLSQESLNSGDCYLLDNG-FTIFLWVGKGSSLLEKLFAALLAAQLDD-DERFPLPEVIRVPQGKEPARF 75
Gelsolin pfam00626
Gelsolin repeat;
27-108 6.38e-15

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 70.41  E-value: 6.38e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123971199  27 MQMVPVPSSTFGSFFDGDCYIVLAihktgsrlSYDIHYWIGRASSQDEQGAAAIYTTQMDD-FLKGQAVQHREVQGNESD 105
Cdd:pfam00626   2 FVLPPPVPLSQESLNSGDCYLLDN--------GFTIFLWVGKGSSLLEKLFAALLAAQLDDdERFPLPEVIRVPQGKEPA 73


                  ...
gi 1123971199 106 AFR 108
Cdd:pfam00626  74 RFL 76
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 515-599 3.19e-13

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: 66.11  E-value: 3.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123971199 515 TRLFQVRGtsSNNTKAFEVSARASSLNSNDVFILKTPSCCYLWYGKGCSGDEREMAKMVANTI------SRTEKQVVVEG 588
Cdd:cd11289     2 PRLLHVKG--RRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIrderrlGRAKVIVLDEG 79

                          90
                  ....*....|...
gi 1123971199 589 --QEPANFWVALG 599
Cdd:cd11289    80 dtNESPEFWKVLG 92
VHP pfam02209
Villin headpiece domain;
792-827 8.78e-13

Villin headpiece domain;


Pssm-ID: 460493  Cd Length: 36  Bit Score: 62.78  E-value: 8.78e-13
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1123971199 792 HLSVEDFTKALGMTPDAFSVLPRWKQQNLKKAKGLF 827
Cdd:pfam02209   1 YLSDEDFEEVFGMSREEFYKLPKWKQNNLKKKAGLF 36
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 401-492 3.60e-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: 3.60e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123971199 401 QVWRIE---NLELVPVDSKwLGHFFGGDCYLLLYTYLIgekqhyllYIWQGSQASPDEITASAYQAVILDQQYNNEPVQI 477
Cdd:cd11280     3 RLYRVRgskAIEIEEVPLA-SSSLDSDDVFVLDTGSEI--------YIWQGRASSQAELAAAALLAKELDEERKGKPEIV 73

                          90
                  ....*....|....*
gi 1123971199 478 RVPMGKEPSHLMSIF 492
Cdd:cd11280    74 RIRQGQEPREFWSLF 88
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 514-595 8.99e-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: 61.61  E-value: 8.99e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123971199 514 STRLFQVRGtsSNNTKAFEVSARASSLNSNDVFILKTPSCCYLWYGKGCSGDE----REMAK-MVANTISRTEKQVVVEG 588
Cdd:cd11280     1 PPRLYRVRG--SKAIEIEEVPLASSSLDSDDVFVLDTGSEIYIWQGRASSQAElaaaALLAKeLDEERKGKPEIVRIRQG 78


                  ....*..
gi 1123971199 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 5.37e-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: 59.56  E-value: 5.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123971199 254 KLYHVSdseGKLVVReVATRPLTQDLLSHEDCYILDQGgLKIYVWKGKNANAQERKGAMsQALNFIKAKQYPPSTQIEVQ 333
Cdd:cd11289     3 RLLHVK---GRRNVR-AREVELSWSSLNSGDVFILDLG-STIYQWNGSKSNRFEKAKAM-QLAQGIRDERRLGRAKVIVL 76

                          90
                  ....*....|....*
gi 1123971199 334 NDGA--ESAVFQQLF 346
Cdd:cd11289    77 DEGDtnESPEFWKVL 91
VHP smart00153
Villin headpiece domain;
792-827 1.30e-10

Villin headpiece domain;


Pssm-ID: 128458  Cd Length: 36  Bit Score: 56.94  E-value: 1.30e-10
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1123971199  792 HLSVEDFTKALGMTPDAFSVLPRWKQQNLKKAKGLF 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 1.44e-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: 55.72  E-value: 1.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123971199 512 VPSTRLFQVrGTSSNNTKAFEV---SARASSLNSNDVFILKTPSCCYLWYGKGCSGDEREMAKMVANTISRTEK------ 582
Cdd:cd11292     1 AEQKKLYKV-SDASGKLKLTEVaegSLNQEMLDSEDCYILDCGSEIFVWVGKGASLDERKAALKNAEEFLRKKKrppytq 79

                          90
                  ....*....|...
gi 1123971199 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 1.06e-07

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: 50.06  E-value: 1.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123971199 255 LYHVSDSeGKLVVREVATRPltqDLLSHEDCYILDQGgLKIYVWKGKNANAQERKGAMSQALNFIkaKQYPPSTQIEVQN 334
Cdd:cd11280     4 LYRVRGS-KAIEIEEVPLAS---SSLDSDDVFVLDTG-SEIYIWQGRASSQAELAAAALLAKELD--EERKGKPEIVRIR 76

                          90
                  ....*....|..
gi 1123971199 335 DGAESAVFQQLF 346
Cdd:cd11280    77 QGQEPREFWSLF 88
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 138-214 4.13e-07

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: 48.52  E-value: 4.13e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1123971199 138 RLLHVKGKRNVVAGEVEMSWRSFNRGDVFLLDLGKLIIQWNGPESNRMERLRGMTLAKEIrDQERGGRT-YVAVVEGE 214
Cdd:cd11280     3 RLYRVRGSKAIEIEEVPLASSSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKEL-DEERKGKPeIVRIRQGQ 79
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 254-342 3.76e-06

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: 45.69  E-value: 3.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123971199 254 KLYHV---SDSEGKLV-VREVATrpltqdLLSHEDCYILdQGGLKIYVWKGKNANAQERKGAMSQAlNFIKakqypPSTQ 329
Cdd:cd11288     4 RLFQVrgnGSGNTRAVeVDADAS------SLNSNDVFVL-KTPSSVYLWVGKGSSEDERELAKDVA-SFLK-----PKAS 70

                          90
                  ....*....|...
gi 1123971199 330 IEVQNDGAESAVF 342
Cdd:cd11288    71 LQEVAEGSEPDEF 83
Gelsolin pfam00626
Gelsolin repeat;
532-595 1.70e-05

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 43.45  E-value: 1.70e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123971199 532 EVSARASSLNSNDVFILKTPSCCYLWYGKGCSGDEREMAKMVANTIS------RTEKQVVVEGQEPANFW 595
Cdd:pfam00626   7 PVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDdderfpLPEVIRVPQGKEPARFL 76
gelsolin_S1_like cd11290
Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; ...
 655-711 7.74e-05

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: 42.60  E-value: 7.74e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1123971199 655 WDqVFFWIGKHANEDEKKAAAI-TVQeyLKTHPSGRdpetPIIVVK-QGHEPATFTGWF 711
Cdd:cd11290    52 YD-IHYWLGKEASQDEAGAAAIkAVE--LDDYLGGR----PVQHREvQGHESEEFLSYF 103
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 619-714 2.77e-04

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


Pssm-ID: 200445  Cd Length: 92  Bit Score: 40.68  E-value: 2.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123971199 619 ARLFECSNQTGCfRATEIPdFTQDDLEEDDVFLLDVWDQVFFWIGKHANEDEkKAAAITVQEYLKThpSGRDPETPIIVV 698
Cdd:cd11289     2 PRLLHVKGRRNV-RAREVE-LSWSSLNSGDVFILDLGSTIYQWNGSKSNRFE-KAKAMQLAQGIRD--ERRLGRAKVIVL 76

                          90
                  ....*....|....*.
gi 1123971199 699 KQGHEPATFTGWFLAW 714
Cdd:cd11289    77 DEGDTNESPEFWKVLG 92
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 43-112 1.96e-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: 38.38  E-value: 1.96e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1123971199  43 GDCYIVLAIHKtgsrlsydIHYWIGRASSQDEQGAAAIYTT---QMDDFLKgQAVQHREVQGNESDAFRGYFK 112
Cdd:cd11292    34 EDCYILDCGSE--------IFVWVGKGASLDERKAALKNAEeflRKKKRPP-YTQVTRVTEGGESALFKSKFA 97
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 138-214 5.27e-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: 36.83  E-value: 5.27e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1123971199 138 RLLHVKG--KRNVVAGEVEMSWRSFNRGDVFLLDLGKLIIQWNGPESNRMERlrgmTLAKEIRDQERGGRTYVAVVEGE 214
Cdd:cd11288     4 RLFQVRGngSGNTRAVEVDADASSLNSNDVFVLKTPSSVYLWVGKGSSEDER----ELAKDVASFLKPKASLQEVAEGS 78
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
 658-711 6.00e-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: 36.87  E-value: 6.00e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1123971199 658 VFFWIGKHANEDEKKAAAI-TVQ--EYLKTHPS-GRdpetpiivVKQGHEPATFTGWF 711
Cdd:cd11293    52 LYFWQGRHSSQDERAAAALlTVEldEELKGRAVqVR--------VVQGKEPPHFLALF 101
 
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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