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Conserved domains on  [gi|1063741799|ref|NP_001318818|]
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actin filament bundling protein P-115-ABP protein [Arabidopsis thaliana]

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; ...
 12-124 2.15e-65

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: 214.78  E-value: 2.15e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741799  12 LQGAGQKSGIEIWRIENFKPVTVPQESHGKFFTGDSYIVLKTTASRSGSLHHDIHYWLGKDSSQDEAGAVAVMTVELDSA 91
Cdd:cd11290     1 FEGVGQKPGLQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDPSGSLSYDIHYWLGKEASQDEAGAAAIKAVELDDY 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1063741799  92 LGGRAVQYREVQGHETEKFLSYFKPCIIPQEGG 124
Cdd:cd11290    81 LGGRPVQHREVQGHESEEFLSYFKKGIIYIEGG 113
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
 388-488 8.08e-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: 8.08e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741799 388 PYIDGTGNLQVWRINCEEKILLEAAEQSKFYSGDCYILQYSYPGEDREEHLVGTWFGKQSVEEDRASAISLANKMVESMK 467
Cdd:cd11293     1 MYDDGSGKVEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQGGGKEEHILYFWQGRHSSQDERAAAALLTVELDEELK 80

                          90       100
                  ....*....|....*....|.
gi 1063741799 468 FVPAQARINEGKEPIQFFVIM 488
Cdd:cd11293    81 GRAVQVRVVQGKEPPHFLALF 101
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 623-722 3.45e-38

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: 137.43  E-value: 3.45e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741799 623 DPHLFSCTYTNESLKATEIFNFTQDDLMTEDIFILDCHTEVFVWVGQQVDPKKKPQALDIGENFLKHDFLLENLaSETPI 702
Cdd:cd11291     1 KPRLFRCSNESGFFKVEEISDFSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYIETDPLGRSK-PRTPI 79

                          90       100
                  ....*....|....*....|
gi 1063741799 703 YIVTEGNEPPFFTRFFTWDS 722
Cdd:cd11291    80 YLVKQGNEPPTFTGYFHAWD 99
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 235-343 2.46e-32

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: 120.82  E-value: 2.46e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741799 235 APLPKKPAVNDDetaasdgiklfsVEKGQTDAVEAECLTKELLDTNKCYILDCGLELFVWKGRSTSIDQRKSATEAAEEF 314
Cdd:cd11292     1 AEQKKLYKVSDA------------SGKLKLTEVAEGSLNQEMLDSEDCYILDCGSEIFVWVGKGASLDERKAALKNAEEF 68

                          90       100       110
                  ....*....|....*....|....*....|
gi 1063741799 315 FRSS-EPPKSNLVSVMEGYETVMFRSKFDS 343
Cdd:cd11292    69 LRKKkRPPYTQVTRVTEGGESALFKSKFAN 98
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 138-232 1.01e-31

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: 118.88  E-value: 1.01e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741799 138 QTRLYICKGKHVVRVKEVPFVRSTLNHEDVFILDTESKIFQFSGSKSSIQERAKALEVVQYIKDTYHDGKCDIAAVEDGr 217
Cdd:cd11289     1 KPRLLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKVIVLDEG- 79

                          90
                  ....*....|....*
gi 1063741799 218 mmADAEAGEFWGLFG 232
Cdd:cd11289    80 --DTNESPEFWKVLG 92
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 520-610 2.14e-30

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


:

Pssm-ID: 200444  Cd Length: 92  Bit Score: 115.02  E-value: 2.14e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741799 520 GVALFRVQGSGPENMQAIQIEAASAGLNSSHCYILHGDSTVFTWCGNLTSSEDQELMERMLDLIKPNEPTKAQKEGSESE 599
Cdd:cd11288     2 PTRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVASFLKPKASLQEVAEGSEPD 81

                          90
                  ....*....|.
gi 1063741799 600 QFWELLGGKSE 610
Cdd:cd11288    82 EFWEALGGKSE 92
VHP pfam02209
Villin headpiece domain;
927-962 6.38e-14

Villin headpiece domain;


:

Pssm-ID: 460493  Cd Length: 36  Bit Score: 66.25  E-value: 6.38e-14
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1063741799 927 YLTSVEFKEKFEMTKNEFYKLPKWKQNKLKMSVNLF 962
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; ...
 12-124 2.15e-65

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: 214.78  E-value: 2.15e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741799  12 LQGAGQKSGIEIWRIENFKPVTVPQESHGKFFTGDSYIVLKTTASRSGSLHHDIHYWLGKDSSQDEAGAVAVMTVELDSA 91
Cdd:cd11290     1 FEGVGQKPGLQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDPSGSLSYDIHYWLGKEASQDEAGAAAIKAVELDDY 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1063741799  92 LGGRAVQYREVQGHETEKFLSYFKPCIIPQEGG 124
Cdd:cd11290    81 LGGRPVQHREVQGHESEEFLSYFKKGIIYIEGG 113
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
 388-488 8.08e-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: 8.08e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741799 388 PYIDGTGNLQVWRINCEEKILLEAAEQSKFYSGDCYILQYSYPGEDREEHLVGTWFGKQSVEEDRASAISLANKMVESMK 467
Cdd:cd11293     1 MYDDGSGKVEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQGGGKEEHILYFWQGRHSSQDERAAAALLTVELDEELK 80

                          90       100
                  ....*....|....*....|.
gi 1063741799 468 FVPAQARINEGKEPIQFFVIM 488
Cdd:cd11293    81 GRAVQVRVVQGKEPPHFLALF 101
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 623-722 3.45e-38

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: 137.43  E-value: 3.45e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741799 623 DPHLFSCTYTNESLKATEIFNFTQDDLMTEDIFILDCHTEVFVWVGQQVDPKKKPQALDIGENFLKHDFLLENLaSETPI 702
Cdd:cd11291     1 KPRLFRCSNESGFFKVEEISDFSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYIETDPLGRSK-PRTPI 79

                          90       100
                  ....*....|....*....|
gi 1063741799 703 YIVTEGNEPPFFTRFFTWDS 722
Cdd:cd11291    80 YLVKQGNEPPTFTGYFHAWD 99
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 235-343 2.46e-32

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: 120.82  E-value: 2.46e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741799 235 APLPKKPAVNDDetaasdgiklfsVEKGQTDAVEAECLTKELLDTNKCYILDCGLELFVWKGRSTSIDQRKSATEAAEEF 314
Cdd:cd11292     1 AEQKKLYKVSDA------------SGKLKLTEVAEGSLNQEMLDSEDCYILDCGSEIFVWVGKGASLDERKAALKNAEEF 68

                          90       100       110
                  ....*....|....*....|....*....|
gi 1063741799 315 FRSS-EPPKSNLVSVMEGYETVMFRSKFDS 343
Cdd:cd11292    69 LRKKkRPPYTQVTRVTEGGESALFKSKFAN 98
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 138-232 1.01e-31

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: 118.88  E-value: 1.01e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741799 138 QTRLYICKGKHVVRVKEVPFVRSTLNHEDVFILDTESKIFQFSGSKSSIQERAKALEVVQYIKDTYHDGKCDIAAVEDGr 217
Cdd:cd11289     1 KPRLLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKVIVLDEG- 79

                          90
                  ....*....|....*
gi 1063741799 218 mmADAEAGEFWGLFG 232
Cdd:cd11289    80 --DTNESPEFWKVLG 92
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 520-610 2.14e-30

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


Pssm-ID: 200444  Cd Length: 92  Bit Score: 115.02  E-value: 2.14e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741799 520 GVALFRVQGSGPENMQAIQIEAASAGLNSSHCYILHGDSTVFTWCGNLTSSEDQELMERMLDLIKPNEPTKAQKEGSESE 599
Cdd:cd11288     2 PTRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVASFLKPKASLQEVAEGSEPD 81

                          90
                  ....*....|.
gi 1063741799 600 QFWELLGGKSE 610
Cdd:cd11288    82 EFWEALGGKSE 92
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 144-233 8.11e-24

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 96.21  E-value: 8.11e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741799  144 CKGKHVVRVKEVPFVRSTLNHEDVFILDTESKIFQFSGSKSSIQERAKALEVVQYIKDTYHDGKCDIAAVEDGRmmadaE 223
Cdd:smart00262   5 VKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVRVVDEGK-----E 79

                           90
                   ....*....|
gi 1063741799  224 AGEFWGLFGG 233
Cdd:smart00262  80 PPEFWSLFGG 89
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 22-117 7.25e-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: 7.25e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741799   22 EIWRIENFKPVTVPQ--ESHGKFFTGDSYIVLKTtasrsgslhHDIHYWLGKDSSQDEAGAVAVMTVELDSALGGRAVQY 99
Cdd:smart00262   1 FLVRVKGKRNVRVPEvpFSQGSLNSGDCYILDTG---------SEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQV 71

                           90
                   ....*....|....*....
gi 1063741799  100 REV-QGHETEKFLSYFKPC 117
Cdd:smart00262  72 RVVdEGKEPPEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 261-344 5.94e-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: 79.64  E-value: 5.94e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741799  261 KGQTDAVEAEClTKELLDTNKCYILDCGLELFVWKGRSTSIDQRKSATEAAEEFFRSSEPPKSNLVSVMEGYETVMFRSK 340
Cdd:smart00262   8 KRNVRVPEVPF-SQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVRVVDEGKEPPEFWSL 86


                   ....
gi 1063741799  341 FDSW 344
Cdd:smart00262  87 FGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 643-718 2.50e-16

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: 75.02  E-value: 2.50e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063741799  643 NFTQDDLMTEDIFILDCHTEVFVWVGQQVDPKKKPQALDIGENFLKHDFllenlASETPIYIVTEGNEPPFFTRFF 718
Cdd:smart00262  17 PFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLG-----PGPVQVRVVDEGKEPPEFWSLF 87
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 397-490 1.31e-15

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: 72.71  E-value: 1.31e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741799  397 QVWRINCEEKILLE--AAEQSKFYSGDCYILQYsypgedreEHLVGTWFGKQSVEEDRASAISLANKMVESMKFVPAQAR 474
Cdd:smart00262   1 FLVRVKGKRNVRVPevPFSQGSLNSGDCYILDT--------GSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVR 72

                           90
                   ....*....|....*..
gi 1063741799  475 -INEGKEPIQFFVIMQS 490
Cdd:smart00262  73 vVDEGKEPPEFWSLFGG 89
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 524-608 5.72e-14

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 68.09  E-value: 5.72e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741799  524 FRVQGSGPENMQAIQIEAASAGLNSSHCYILHGDSTVFTWCGNLTSSEDQEL-MERMLDLIKPNEPTKAQ----KEGSES 598
Cdd:smart00262   1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKaAELAVELDDTLGPGPVQvrvvDEGKEP 80

                           90
                   ....*....|
gi 1063741799  599 EQFWELLGGK 608
Cdd:smart00262  81 PEFWSLFGGW 90
VHP pfam02209
Villin headpiece domain;
927-962 6.38e-14

Villin headpiece domain;


Pssm-ID: 460493  Cd Length: 36  Bit Score: 66.25  E-value: 6.38e-14
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1063741799 927 YLTSVEFKEKFEMTKNEFYKLPKWKQNKLKMSVNLF 962
Cdd:pfam02209   1 YLSDEDFEEVFGMSREEFYKLPKWKQNNLKKKAGLF 36
VHP smart00153
Villin headpiece domain;
927-962 9.60e-13

Villin headpiece domain;


Pssm-ID: 128458  Cd Length: 36  Bit Score: 63.11  E-value: 9.60e-13
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1063741799  927 YLTSVEFKEKFEMTKNEFYKLPKWKQNKLKMSVNLF 962
Cdd:smart00153   1 YLSDEDFEEVFGMTREEFYKLPLWKQNQLKKKKGLF 36
Gelsolin pfam00626
Gelsolin repeat;
28-111 1.37e-11

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 61.17  E-value: 1.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741799  28 NFKPVTVPQESHGKFFTGDSYIVLKTTasrsgslhhDIHYWLGKDSSQDEAGAVAVMTVELD-SALGGRAVQYREVQGHE 106
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNGF---------TIFLWVGKGSSLLEKLFAALLAAQLDdDERFPLPEVIRVPQGKE 71


                  ....*
gi 1063741799 107 TEKFL 111
Cdd:pfam00626  72 PARFL 76
Gelsolin pfam00626
Gelsolin repeat;
148-217 4.07e-09

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 53.85  E-value: 4.07e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741799 148 HVVRVKEVPFVRSTLNHEDVFILDTESKIFQFSGSKSSIQERAKALEVVQYIKDTYHDGKCDIAAVEDGR 217
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDERFPLPEVIRVPQGK 70
Gelsolin pfam00626
Gelsolin repeat;
272-338 1.94e-08

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 51.92  E-value: 1.94e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741799 272 LTKELLDTNKCYILDCGLELFVWKGRSTSIDQRKSATEAAEEF---FRSSEPPKSNLVsvmEGYETVMFR 338
Cdd:pfam00626  10 LSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLdddERFPLPEVIRVP---QGKEPARFL 76
Gelsolin pfam00626
Gelsolin repeat;
643-714 1.03e-06

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 47.30  E-value: 1.03e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063741799 643 NFTQDDLMTEDIFILDCHTEVFVWVGQQVDPKKKPQALDigenfLKHDFLLENLASETPIYIVTEGNEPPFF 714
Cdd:pfam00626   9 PLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAAL-----LAAQLDDDERFPLPEVIRVPQGKEPARF 75
 
Name Accession Description Interval E-value
gelsolin_S1_like cd11290
Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; ...
 12-124 2.15e-65

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: 214.78  E-value: 2.15e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741799  12 LQGAGQKSGIEIWRIENFKPVTVPQESHGKFFTGDSYIVLKTTASRSGSLHHDIHYWLGKDSSQDEAGAVAVMTVELDSA 91
Cdd:cd11290     1 FEGVGQKPGLQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDPSGSLSYDIHYWLGKEASQDEAGAAAIKAVELDDY 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1063741799  92 LGGRAVQYREVQGHETEKFLSYFKPCIIPQEGG 124
Cdd:cd11290    81 LGGRPVQHREVQGHESEEFLSYFKKGIIYIEGG 113
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
 388-488 8.08e-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: 8.08e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741799 388 PYIDGTGNLQVWRINCEEKILLEAAEQSKFYSGDCYILQYSYPGEDREEHLVGTWFGKQSVEEDRASAISLANKMVESMK 467
Cdd:cd11293     1 MYDDGSGKVEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQGGGKEEHILYFWQGRHSSQDERAAAALLTVELDEELK 80

                          90       100
                  ....*....|....*....|.
gi 1063741799 468 FVPAQARINEGKEPIQFFVIM 488
Cdd:cd11293    81 GRAVQVRVVQGKEPPHFLALF 101
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 623-722 3.45e-38

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: 137.43  E-value: 3.45e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741799 623 DPHLFSCTYTNESLKATEIFNFTQDDLMTEDIFILDCHTEVFVWVGQQVDPKKKPQALDIGENFLKHDFLLENLaSETPI 702
Cdd:cd11291     1 KPRLFRCSNESGFFKVEEISDFSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYIETDPLGRSK-PRTPI 79

                          90       100
                  ....*....|....*....|
gi 1063741799 703 YIVTEGNEPPFFTRFFTWDS 722
Cdd:cd11291    80 YLVKQGNEPPTFTGYFHAWD 99
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 235-343 2.46e-32

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: 120.82  E-value: 2.46e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741799 235 APLPKKPAVNDDetaasdgiklfsVEKGQTDAVEAECLTKELLDTNKCYILDCGLELFVWKGRSTSIDQRKSATEAAEEF 314
Cdd:cd11292     1 AEQKKLYKVSDA------------SGKLKLTEVAEGSLNQEMLDSEDCYILDCGSEIFVWVGKGASLDERKAALKNAEEF 68

                          90       100       110
                  ....*....|....*....|....*....|
gi 1063741799 315 FRSS-EPPKSNLVSVMEGYETVMFRSKFDS 343
Cdd:cd11292    69 LRKKkRPPYTQVTRVTEGGESALFKSKFAN 98
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 138-232 1.01e-31

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: 118.88  E-value: 1.01e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741799 138 QTRLYICKGKHVVRVKEVPFVRSTLNHEDVFILDTESKIFQFSGSKSSIQERAKALEVVQYIKDTYHDGKCDIAAVEDGr 217
Cdd:cd11289     1 KPRLLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKVIVLDEG- 79

                          90
                  ....*....|....*
gi 1063741799 218 mmADAEAGEFWGLFG 232
Cdd:cd11289    80 --DTNESPEFWKVLG 92
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 520-610 2.14e-30

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


Pssm-ID: 200444  Cd Length: 92  Bit Score: 115.02  E-value: 2.14e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741799 520 GVALFRVQGSGPENMQAIQIEAASAGLNSSHCYILHGDSTVFTWCGNLTSSEDQELMERMLDLIKPNEPTKAQKEGSESE 599
Cdd:cd11288     2 PTRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVASFLKPKASLQEVAEGSEPD 81

                          90
                  ....*....|.
gi 1063741799 600 QFWELLGGKSE 610
Cdd:cd11288    82 EFWEALGGKSE 92
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
 21-114 6.05e-30

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: 114.29  E-value: 6.05e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741799  21 IEIWRIENFKPVTVPQESHGKFFTGDSYIVLkTTASRSGSLHHDIHYWLGKDSSQDEAGAVAVMTVELDSALGGRAVQYR 100
Cdd:cd11293     9 VEVWRIENDEKVPVPKEEYGQFYGGDCYIVL-YTYQGGGKEEHILYFWQGRHSSQDERAAAALLTVELDEELKGRAVQVR 87

                          90
                  ....*....|....
gi 1063741799 101 EVQGHETEKFLSYF 114
Cdd:cd11293    88 VVQGKEPPHFLALF 101
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 144-233 8.11e-24

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 96.21  E-value: 8.11e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741799  144 CKGKHVVRVKEVPFVRSTLNHEDVFILDTESKIFQFSGSKSSIQERAKALEVVQYIKDTYHDGKCDIAAVEDGRmmadaE 223
Cdd:smart00262   5 VKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVRVVDEGK-----E 79

                           90
                   ....*....|
gi 1063741799  224 AGEFWGLFGG 233
Cdd:smart00262  80 PPEFWSLFGG 89
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 22-117 7.25e-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: 7.25e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741799   22 EIWRIENFKPVTVPQ--ESHGKFFTGDSYIVLKTtasrsgslhHDIHYWLGKDSSQDEAGAVAVMTVELDSALGGRAVQY 99
Cdd:smart00262   1 FLVRVKGKRNVRVPEvpFSQGSLNSGDCYILDTG---------SEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQV 71

                           90
                   ....*....|....*....
gi 1063741799  100 REV-QGHETEKFLSYFKPC 117
Cdd:smart00262  72 RVVdEGKEPPEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 261-344 5.94e-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: 79.64  E-value: 5.94e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741799  261 KGQTDAVEAEClTKELLDTNKCYILDCGLELFVWKGRSTSIDQRKSATEAAEEFFRSSEPPKSNLVSVMEGYETVMFRSK 340
Cdd:smart00262   8 KRNVRVPEVPF-SQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVRVVDEGKEPPEFWSL 86


                   ....
gi 1063741799  341 FDSW 344
Cdd:smart00262  87 FGGW 90
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 633-718 1.42e-17

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: 78.83  E-value: 1.42e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741799 633 NESLKATEIF--NFTQDDLMTEDIFILDCHTEVFVWVGQQVDPKKKPQALDIGENFLKHdfllENLASETPIYIVTEGNE 710
Cdd:cd11292    13 SGKLKLTEVAegSLNQEMLDSEDCYILDCGSEIFVWVGKGASLDERKAALKNAEEFLRK----KKRPPYTQVTRVTEGGE 88


                  ....*...
gi 1063741799 711 PPFFTRFF 718
Cdd:cd11292    89 SALFKSKF 96
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 643-718 2.50e-16

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: 75.02  E-value: 2.50e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063741799  643 NFTQDDLMTEDIFILDCHTEVFVWVGQQVDPKKKPQALDIGENFLKHDFllenlASETPIYIVTEGNEPPFFTRFF 718
Cdd:smart00262  17 PFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLG-----PGPVQVRVVDEGKEPPEFWSLF 87
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 397-490 1.31e-15

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: 72.71  E-value: 1.31e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741799  397 QVWRINCEEKILLE--AAEQSKFYSGDCYILQYsypgedreEHLVGTWFGKQSVEEDRASAISLANKMVESMKFVPAQAR 474
Cdd:smart00262   1 FLVRVKGKRNVRVPevPFSQGSLNSGDCYILDT--------GSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVR 72

                           90
                   ....*....|....*..
gi 1063741799  475 -INEGKEPIQFFVIMQS 490
Cdd:smart00262  73 vVDEGKEPPEFWSLFGG 89
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 524-608 5.72e-14

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 68.09  E-value: 5.72e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741799  524 FRVQGSGPENMQAIQIEAASAGLNSSHCYILHGDSTVFTWCGNLTSSEDQEL-MERMLDLIKPNEPTKAQ----KEGSES 598
Cdd:smart00262   1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKaAELAVELDDTLGPGPVQvrvvDEGKEP 80

                           90
                   ....*....|
gi 1063741799  599 EQFWELLGGK 608
Cdd:smart00262  81 PEFWSLFGGW 90
VHP pfam02209
Villin headpiece domain;
927-962 6.38e-14

Villin headpiece domain;


Pssm-ID: 460493  Cd Length: 36  Bit Score: 66.25  E-value: 6.38e-14
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1063741799 927 YLTSVEFKEKFEMTKNEFYKLPKWKQNKLKMSVNLF 962
Cdd:pfam02209   1 YLSDEDFEEVFGMSREEFYKLPKWKQNNLKKKAGLF 36
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 23-114 2.75e-13

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: 66.24  E-value: 2.75e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741799  23 IWRIE---NFKPVTVPQEShGKFFTGDSYiVLKTtasrsGSlhhDIHYWLGKDSSQDEAGAVAVMTVELDSALGGRAVQY 99
Cdd:cd11280     4 LYRVRgskAIEIEEVPLAS-SSLDSDDVF-VLDT-----GS---EIYIWQGRASSQAELAAAALLAKELDEERKGKPEIV 73

                          90
                  ....*....|....*
gi 1063741799 100 REVQGHETEKFLSYF 114
Cdd:cd11280    74 RIRQGQEPREFWSLF 88
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 138-231 4.83e-13

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: 65.47  E-value: 4.83e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741799 138 QTRLYICKGKHVVRVKEVPFVRSTLNHEDVFILDTESKIFQFSGSKSSIQERAKALEVVQYIKDTYhDGKCDIAAVEDGR 217
Cdd:cd11280     1 PPRLYRVRGSKAIEIEEVPLASSSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKELDEER-KGKPEIVRIRQGQ 79

                          90
                  ....*....|....
gi 1063741799 218 mmadaEAGEFWGLF 231
Cdd:cd11280    80 -----EPREFWSLF 88
VHP smart00153
Villin headpiece domain;
927-962 9.60e-13

Villin headpiece domain;


Pssm-ID: 128458  Cd Length: 36  Bit Score: 63.11  E-value: 9.60e-13
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1063741799  927 YLTSVEFKEKFEMTKNEFYKLPKWKQNKLKMSVNLF 962
Cdd:smart00153   1 YLSDEDFEEVFGMTREEFYKLPLWKQNQLKKKKGLF 36
Gelsolin pfam00626
Gelsolin repeat;
28-111 1.37e-11

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 61.17  E-value: 1.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741799  28 NFKPVTVPQESHGKFFTGDSYIVLKTTasrsgslhhDIHYWLGKDSSQDEAGAVAVMTVELD-SALGGRAVQYREVQGHE 106
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNGF---------TIFLWVGKGSSLLEKLFAALLAAQLDdDERFPLPEVIRVPQGKE 71


                  ....*
gi 1063741799 107 TEKFL 111
Cdd:pfam00626  72 PARFL 76
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 256-341 3.02e-10

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


Pssm-ID: 200436  Cd Length: 88  Bit Score: 57.76  E-value: 3.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741799 256 LFSVEKGQTDAVEAECLTKELLDTNKCYILDCGLELFVWKGRSTSIDQRKSATEAAEEfFRSSEPPKSNLVSVMEGYETV 335
Cdd:cd11280     4 LYRVRGSKAIEIEEVPLASSSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKE-LDEERKGKPEIVRIRQGQEPR 82


                  ....*.
gi 1063741799 336 MFRSKF 341
Cdd:cd11280    83 EFWSLF 88
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 138-233 2.18e-09

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: 55.32  E-value: 2.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741799 138 QTRLY-ICK-GKHVVRVKEVPFVRSTLNHEDVFILDTESKIFQFSGSKSSIQERAKALEVVQYIKDtyhdgKCDIAAVED 215
Cdd:cd11288     2 PTRLFqVRGnGSGNTRAVEVDADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVASFLKP-----KASLQEVAE 76

                          90
                  ....*....|....*...
gi 1063741799 216 GrmmadAEAGEFWGLFGG 233
Cdd:cd11288    77 G-----SEPDEFWEALGG 89
Gelsolin pfam00626
Gelsolin repeat;
148-217 4.07e-09

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 53.85  E-value: 4.07e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741799 148 HVVRVKEVPFVRSTLNHEDVFILDTESKIFQFSGSKSSIQERAKALEVVQYIKDTYHDGKCDIAAVEDGR 217
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDERFPLPEVIRVPQGK 70
Gelsolin pfam00626
Gelsolin repeat;
272-338 1.94e-08

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 51.92  E-value: 1.94e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741799 272 LTKELLDTNKCYILDCGLELFVWKGRSTSIDQRKSATEAAEEF---FRSSEPPKSNLVsvmEGYETVMFR 338
Cdd:pfam00626  10 LSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLdddERFPLPEVIRVP---QGKEPARFL 76
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 254-345 4.30e-08

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: 51.91  E-value: 4.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741799 254 IKLF--SVEKGQTDAVEAECLTKELLDTNKCYILDCGLELFVWKGRSTSIDQRKSATEAAEEFF---RSSEP-PKSNLVS 327
Cdd:cd11291     2 PRLFrcSNESGFFKVEEISDFSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYIetdPLGRSkPRTPIYL 81

                          90
                  ....*....|....*...
gi 1063741799 328 VMEGYETVMFRSKFDSWP 345
Cdd:cd11291    82 VKQGNEPPTFTGYFHAWD 99
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 138-200 8.58e-08

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: 50.76  E-value: 8.58e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063741799 138 QTRLYIC---KGkhVVRVKEV-PFVRSTLNHEDVFILDTESKIFQFSGSKSSIQERAKALEVVQ-YIK 200
Cdd:cd11291     1 KPRLFRCsneSG--FFKVEEIsDFSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKkYIE 66
Gelsolin pfam00626
Gelsolin repeat;
643-714 1.03e-06

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 47.30  E-value: 1.03e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063741799 643 NFTQDDLMTEDIFILDCHTEVFVWVGQQVDPKKKPQALDigenfLKHDFLLENLASETPIYIVTEGNEPPFF 714
Cdd:pfam00626   9 PLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAAL-----LAAQLDDDERFPLPEVIRVPQGKEPARF 75
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 623-718 1.34e-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: 47.36  E-value: 1.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741799 623 DPHLFSCTYtNESLKATEIFNFTQDdLMTEDIFILDCHTEVFVWVGQQVDPKKKPQALDIGENFLKHDFllenlaSETPI 702
Cdd:cd11280     1 PPRLYRVRG-SKAIEIEEVPLASSS-LDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKELDEERK------GKPEI 72

                          90
                  ....*....|....*.
gi 1063741799 703 YIVTEGNEPPFFTRFF 718
Cdd:cd11280    73 VRIRQGQEPREFWSLF 88
gelsolin_S1_like cd11290
Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; ...
 396-464 2.64e-06

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: 47.22  E-value: 2.64e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741799 396 LQVWRINCEEKILLEAAEQSKFYSGDCYI-LQYSYPGEDREEHLVGTWFGKQSVEEDRASAislANKMVE 464
Cdd:cd11290    10 LQIWRIENFELVPVPESFYGKFYEGDSYIvLKTTLDPSGSLSYDIHYWLGKEASQDEAGAA---AIKAVE 76
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 419-485 1.28e-05

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


Pssm-ID: 200444  Cd Length: 92  Bit Score: 44.53  E-value: 1.28e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741799 419 SGDCYILQ---YSYpgedreehlvgTWFGKQSVEEDRASAISLANKMVESMKFVpaqaRINEGKEPIQFF 485
Cdd:cd11288    30 SNDVFVLKtpsSVY-----------LWVGKGSSEDERELAKDVASFLKPKASLQ----EVAEGSEPDEFW 84
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 252-337 8.64e-05

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


Pssm-ID: 200444  Cd Length: 92  Bit Score: 42.22  E-value: 8.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741799 252 DGIKLFSV---EKGQTDAVEAECLTKeLLDTNKCYILDCGLELFVWKGRSTSIDQRKSATEAAEEFFrssepPKSNLVSV 328
Cdd:cd11288     1 SPTRLFQVrgnGSGNTRAVEVDADAS-SLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVASFLK-----PKASLQEV 74


                  ....*....
gi 1063741799 329 MEGYETVMF 337
Cdd:cd11288    75 AEGSEPDEF 83
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 523-606 2.75e-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: 2.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741799 523 LFRVqgSGPENMQAIQIEAASAGLNSSHCYILHGDSTVFTWCGNLTSSedqelMER-----MLDLIKPNEPTKAQK---- 593
Cdd:cd11289     4 LLHV--KGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNR-----FEKakamqLAQGIRDERRLGRAKvivl 76

                          90
                  ....*....|....*.
gi 1063741799 594 ---EGSESEQFWELLG 606
Cdd:cd11289    77 degDTNESPEFWKVLG 92
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 405-484 2.80e-04

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: 40.81  E-value: 2.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741799 405 EKILLEAaeqSKFYSGDCYILQYsypgeDREEHLvgtWFGKQSVEEDRASAISLANKMVESMKFVPAQARINEGKEPIQF 484
Cdd:cd11280    16 EEVPLAS---SSLDSDDVFVLDT-----GSEIYI---WQGRASSQAELAAAALLAKELDEERKGKPEIVRIRQGQEPREF 84
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 272-311 3.76e-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: 40.30  E-value: 3.76e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1063741799 272 LTKELLDTNKCYILDCGLELFVWKGRSTSIDQRKSATEAA 311
Cdd:cd11289    20 LSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLA 59
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 523-605 2.06e-03

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: 38.12  E-value: 2.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741799 523 LFRVQGSGPENMQaiQIEAASAGLNSSHCYILHGDSTVFTWCGNLTS----SEDQELMERMLDLIKPNEPTKAQKEGSES 598
Cdd:cd11280     4 LYRVRGSKAIEIE--EVPLASSSLDSDDVFVLDTGSEIYIWQGRASSqaelAAAALLAKELDEERKGKPEIVRIRQGQEP 81


                  ....*..
gi 1063741799 599 EQFWELL 605
Cdd:cd11280    82 REFWSLF 88
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 518-601 2.90e-03

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


Pssm-ID: 200448  Cd Length: 98  Bit Score: 38.00  E-value: 2.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741799 518 AEGVALFRVQ-GSGPENMQAIQIEAASAG-LNSSHCYILHGDSTVFTWCGNLTSSED-QELMERMLDLIKP-NEPTKAQ- 592
Cdd:cd11292     1 AEQKKLYKVSdASGKLKLTEVAEGSLNQEmLDSEDCYILDCGSEIFVWVGKGASLDErKAALKNAEEFLRKkKRPPYTQv 80

                          90
                  ....*....|..
gi 1063741799 593 ---KEGSESEQF 601
Cdd:cd11292    81 trvTEGGESALF 92
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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