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Conserved domains on  [gi|57015325|sp|Q9Y6U3|]
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RecName: Full=Scinderin; AltName: Full=Adseverin

Protein Classification

villin/gelsolin family protein( domain architecture ID 10181758)

villin/gelsolin family protein which is an actin regulatory protein; similar to human actin-binding proteins gelsolin and adseverin; contains six gelsolin-like repeats

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 613-711 4.27e-53

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: 178.26  E-value: 4.27e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57015325 613 PPRLYGCSNKTGRFVIEEIPGeFTQDDLAEDDVMLLDAWEQIFIWIGKDANEVEKKESLKSAKMYLETDPSGRDK-RTPI 691
Cdd:cd11291   1 KPRLFRCSNESGFFKVEEISD-FSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYIETDPLGRSKpRTPI 79

                        90       100
                ....*....|....*....|
gi 57015325 692 VIIKQGHEPPTFTGWFLGWD 711
Cdd:cd11291  80 YLVKQGNEPPTFTGYFHAWD 99
gelsolin_S1_like cd11290
Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; ...
 10-121 2.04e-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: 2.04e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57015325  10 FARAGKQAGLQVWRIEKLELVPVPQSAHGDFYVGDAYLVLHTAKT-SRGFTYHLHFWLGKECSQDESTAAAIFTVQMDDY 88
Cdd:cd11290   1 FEGVGQKPGLQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDpSGSLSYDIHYWLGKEASQDEAGAAAIKAVELDDY 80

                        90       100       110
                ....*....|....*....|....*....|...
gi 57015325  89 LGGKPVQNRELQGYESNDFVSYFKGGLKYKAGG 121
Cdd:cd11290  81 LGGRPVQHREVQGHESEEFLSYFKKGIIYIEGG 113
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
 390-486 3.71e-45

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: 156.28  E-value: 3.71e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57015325 390 MVDDGSGKVEIWRVENNGRIQVDQNSYGEFYGGDCYIILYTYPRG----QIIYTWQGANATRDELTTSAFLTVQLDRSLG 465
Cdd:cd11293   1 MYDDGSGKVEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQGGgkeeHILYFWQGRHSSQDERAAAALLTVELDEELK 80

                        90       100
                ....*....|....*....|.
gi 57015325 466 GQAVQIRVSQGKEPVHLLSLF 486
Cdd:cd11293  81 GRAVQVRVVQGKEPPHFLALF 101
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 136-225 1.45e-43

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: 151.62  E-value: 1.45e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57015325 136 AKRLLHVKGRRVVRATEVPLSWDSFNKGDCFIIDLGTEIYQWCGSSCNKYERLKANQVATGIRYNERKGRSELIVVEEG- 214
Cdd:cd11289   1 KPRLLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKVIVLDEGd 80

                        90
                ....*....|..
gi 57015325 215 -SEPSELIKVLG 225
Cdd:cd11289  81 tNESPEFWKVLG 92
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 246-346 4.45e-42

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: 147.78  E-value: 4.45e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57015325 246 RKMAKLYMVSDASGSMRVTVVAEEnPFSMAMLLSEECFILDHGAakQIFVWKGKDANPQERKAAMKTAEEFLQQMNYSKN 325
Cdd:cd11292   1 AEQKKLYKVSDASGKLKLTEVAEG-SLNQEMLDSEDCYILDCGS--EIFVWVGKGASLDERKAALKNAEEFLRKKKRPPY 77

                        90       100
                ....*....|....*....|.
gi 57015325 326 TQIQVLPEGGETPIFKQFFKD 346
Cdd:cd11292  78 TQVTRVTEGGESALFKSKFAN 98
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 508-598 7.15e-41

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: 144.30  E-value: 7.15e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57015325 508 PPTRLFQVRRNLASITRIVEVDVDANSLNSNDVFVLKLPqNSGYIWVGKGASQEEEKGAEYVASVLK--CKTLRIQEGEE 585
Cdd:cd11288   1 SPTRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKTP-SSVYLWVGKGSSEDERELAKDVASFLKpkASLQEVAEGSE 79

                        90
                ....*....|...
gi 57015325 586 PEEFWNSLGGKKD 598
Cdd:cd11288  80 PDEFWEALGGKSE 92
 
Name Accession Description Interval E-value
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 613-711 4.27e-53

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: 178.26  E-value: 4.27e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57015325 613 PPRLYGCSNKTGRFVIEEIPGeFTQDDLAEDDVMLLDAWEQIFIWIGKDANEVEKKESLKSAKMYLETDPSGRDK-RTPI 691
Cdd:cd11291   1 KPRLFRCSNESGFFKVEEISD-FSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYIETDPLGRSKpRTPI 79

                        90       100
                ....*....|....*....|
gi 57015325 692 VIIKQGHEPPTFTGWFLGWD 711
Cdd:cd11291  80 YLVKQGNEPPTFTGYFHAWD 99
gelsolin_S1_like cd11290
Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; ...
 10-121 2.04e-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: 2.04e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57015325  10 FARAGKQAGLQVWRIEKLELVPVPQSAHGDFYVGDAYLVLHTAKT-SRGFTYHLHFWLGKECSQDESTAAAIFTVQMDDY 88
Cdd:cd11290   1 FEGVGQKPGLQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDpSGSLSYDIHYWLGKEASQDEAGAAAIKAVELDDY 80

                        90       100       110
                ....*....|....*....|....*....|...
gi 57015325  89 LGGKPVQNRELQGYESNDFVSYFKGGLKYKAGG 121
Cdd:cd11290  81 LGGRPVQHREVQGHESEEFLSYFKKGIIYIEGG 113
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
 390-486 3.71e-45

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: 156.28  E-value: 3.71e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57015325 390 MVDDGSGKVEIWRVENNGRIQVDQNSYGEFYGGDCYIILYTYPRG----QIIYTWQGANATRDELTTSAFLTVQLDRSLG 465
Cdd:cd11293   1 MYDDGSGKVEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQGGgkeeHILYFWQGRHSSQDERAAAALLTVELDEELK 80

                        90       100
                ....*....|....*....|.
gi 57015325 466 GQAVQIRVSQGKEPVHLLSLF 486
Cdd:cd11293  81 GRAVQVRVVQGKEPPHFLALF 101
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 136-225 1.45e-43

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: 151.62  E-value: 1.45e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57015325 136 AKRLLHVKGRRVVRATEVPLSWDSFNKGDCFIIDLGTEIYQWCGSSCNKYERLKANQVATGIRYNERKGRSELIVVEEG- 214
Cdd:cd11289   1 KPRLLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKVIVLDEGd 80

                        90
                ....*....|..
gi 57015325 215 -SEPSELIKVLG 225
Cdd:cd11289  81 tNESPEFWKVLG 92
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 246-346 4.45e-42

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: 147.78  E-value: 4.45e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57015325 246 RKMAKLYMVSDASGSMRVTVVAEEnPFSMAMLLSEECFILDHGAakQIFVWKGKDANPQERKAAMKTAEEFLQQMNYSKN 325
Cdd:cd11292   1 AEQKKLYKVSDASGKLKLTEVAEG-SLNQEMLDSEDCYILDCGS--EIFVWVGKGASLDERKAALKNAEEFLRKKKRPPY 77

                        90       100
                ....*....|....*....|.
gi 57015325 326 TQIQVLPEGGETPIFKQFFKD 346
Cdd:cd11292  78 TQVTRVTEGGESALFKSKFAN 98
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 508-598 7.15e-41

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: 144.30  E-value: 7.15e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57015325 508 PPTRLFQVRRNLASITRIVEVDVDANSLNSNDVFVLKLPqNSGYIWVGKGASQEEEKGAEYVASVLK--CKTLRIQEGEE 585
Cdd:cd11288   1 SPTRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKTP-SSVYLWVGKGSSEDERELAKDVASFLKpkASLQEVAEGSE 79

                        90
                ....*....|...
gi 57015325 586 PEEFWNSLGGKKD 598
Cdd:cd11288  80 PDEFWEALGGKSE 92
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 619-710 6.15e-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: 101.99  E-value: 6.15e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57015325    619 CSNKTGRFVIEEIPGEFTQDDLAEDDVMLLDAWEQIFIWIGKDANEVEKKESLKSAKMYLETDPSGrdkRTPIVIIKQGH 698
Cdd:smart00262   2 LVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPG---PVQVRVVDEGK 78

                           90
                   ....*....|..
gi 57015325    699 EPPTFTGWFLGW 710
Cdd:smart00262  79 EPPEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 138-225 1.16e-25

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 101.22  E-value: 1.16e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57015325    138 RLLHVKGRRVVRATEVPLSWDSFNKGDCFIIDLGTEIYQWCGSSCNKYERLKANQVATGIRYNERKGRSELIVVEEGSEP 217
Cdd:smart00262   1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVRVVDEGKEP 80


                   ....*...
gi 57015325    218 SELIKVLG 225
Cdd:smart00262  81 PEFWSLFG 88
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 259-347 6.93e-25

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 98.90  E-value: 6.93e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57015325    259 GSMRVTVVAEENPFSMAMLLSEECFILDHGAakQIFVWKGKDANPQERKAAMKTAEEFLQQMNySKNTQIQVLPEGGETP 338
Cdd:smart00262   5 VKGKRNVRVPEVPFSQGSLNSGDCYILDTGS--EIYVWVGKKSSQDEKKKAAELAVELDDTLG-PGPVQVRVVDEGKEPP 81


                   ....*....
gi 57015325    339 IFKQFFKDW 347
Cdd:smart00262  82 EFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 399-489 4.29e-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: 4.29e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57015325    399 EIWRVENNGRIQVDQ--NSYGEFYGGDCYIILYtyprGQIIYTWQGANATRDELTTSAFLTVQLDRSLGGQAVQIR-VSQ 475
Cdd:smart00262   1 FLVRVKGKRNVRVPEvpFSQGSLNSGDCYILDT----GSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVRvVDE 76

                           90
                   ....*....|....
gi 57015325    476 GKEPVHLLSLFKDK 489
Cdd:smart00262  77 GKEPPEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 20-114 1.39e-21

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: 89.66  E-value: 1.39e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57015325     20 QVWRIEKLELVPVPQS--AHGDFYVGDAYLVLHTaktsrgftYHLHFWLGKECSQDESTAAAIFTVQMDDYLGGKPVQNR 97
Cdd:smart00262   1 FLVRVKGKRNVRVPEVpfSQGSLNSGDCYILDTG--------SEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVR 72

                           90
                   ....*....|....*...
gi 57015325     98 EL-QGYESNDFVSYFKGG 114
Cdd:smart00262  73 VVdEGKEPPEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 513-596 6.29e-21

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: 87.73  E-value: 6.29e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57015325    513 FQVRRNLASITRIVEVDVDANSLNSNDVFVLKLPQNSgYIWVGKGASQEEEKGAEYVASVL-------KCKTLRIQEGEE 585
Cdd:smart00262   1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEI-YVWVGKKSSQDEKKKAAELAVELddtlgpgPVQVRVVDEGKE 79

                           90
                   ....*....|.
gi 57015325    586 PEEFWNSLGGK 596
Cdd:smart00262  80 PPEFWSLFGGW 90
Gelsolin pfam00626
Gelsolin repeat;
146-221 2.16e-19

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 82.74  E-value: 2.16e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 57015325   146 RVVRATEVPLSWDSFNKGDCFIIDLGTEIYQWCGSSCNKYERLKANQVATGIRYNERKGRSELIVVEEGSEPSELI 221
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDERFPLPEVIRVPQGKEPARFL 76
Gelsolin pfam00626
Gelsolin repeat;
626-703 4.39e-15

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 70.41  E-value: 4.39e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 57015325   626 FVIEEIPGEFTQDDLAEDDVMLLDAWEQIFIWIGKDANEVEKKESLKSAKMYLETDpsgRDKRTPIVIIKQGHEPPTF 703
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDE---RFPLPEVIRVPQGKEPARF 75
Gelsolin pfam00626
Gelsolin repeat;
263-341 2.72e-14

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 68.10  E-value: 2.72e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 57015325   263 VTVVAEENPFSMAMLLSEECFILDHGaaKQIFVWKGKDANPQERKAAMKTAEEFLQQMnYSKNTQIQVLPEGGETPIFK 341
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNG--FTIFLWVGKGSSLLEKLFAALLAAQLDDDE-RFPLPEVIRVPQGKEPARFL 76
Gelsolin pfam00626
Gelsolin repeat;
26-108 4.02e-14

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 67.72  E-value: 4.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57015325    26 KLELVPVPQSAHGDFYVGDAYLVLHTaktsrgftYHLHFWLGKECSQDESTAAAIFTVQMDD-YLGGKPVQNRELQGYES 104
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNG--------FTIFLWVGKGSSLLEKLFAALLAAQLDDdERFPLPEVIRVPQGKEP 72


                  ....
gi 57015325   105 NDFV 108
Cdd:pfam00626  73 ARFL 76
Gelsolin pfam00626
Gelsolin repeat;
410-483 2.33e-11

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 60.01  E-value: 2.33e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 57015325   410 QVDQNSYGEFYGGDCYIILYtyprGQIIYTWQGANATRDELTTSAFLTVQLDRS-LGGQAVQIRVSQGKEPVHLL 483
Cdd:pfam00626   6 PPVPLSQESLNSGDCYLLDN----GFTIFLWVGKGSSLLEKLFAALLAAQLDDDeRFPLPEVIRVPQGKEPARFL 76
Gelsolin pfam00626
Gelsolin repeat;
526-590 3.87e-07

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 48.07  E-value: 3.87e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 57015325   526 VEVDVDANSLNSNDVFVLKLPQNSgYIWVGKGASQEEEKGAEYVASVL-------KCKTLRIQEGEEPEEFW 590
Cdd:pfam00626   6 PPVPLSQESLNSGDCYLLDNGFTI-FLWVGKGSSLLEKLFAALLAAQLddderfpLPEVIRVPQGKEPARFL 76
 
Name Accession Description Interval E-value
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 613-711 4.27e-53

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: 178.26  E-value: 4.27e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57015325 613 PPRLYGCSNKTGRFVIEEIPGeFTQDDLAEDDVMLLDAWEQIFIWIGKDANEVEKKESLKSAKMYLETDPSGRDK-RTPI 691
Cdd:cd11291   1 KPRLFRCSNESGFFKVEEISD-FSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYIETDPLGRSKpRTPI 79

                        90       100
                ....*....|....*....|
gi 57015325 692 VIIKQGHEPPTFTGWFLGWD 711
Cdd:cd11291  80 YLVKQGNEPPTFTGYFHAWD 99
gelsolin_S1_like cd11290
Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; ...
 10-121 2.04e-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: 2.04e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57015325  10 FARAGKQAGLQVWRIEKLELVPVPQSAHGDFYVGDAYLVLHTAKT-SRGFTYHLHFWLGKECSQDESTAAAIFTVQMDDY 88
Cdd:cd11290   1 FEGVGQKPGLQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDpSGSLSYDIHYWLGKEASQDEAGAAAIKAVELDDY 80

                        90       100       110
                ....*....|....*....|....*....|...
gi 57015325  89 LGGKPVQNRELQGYESNDFVSYFKGGLKYKAGG 121
Cdd:cd11290  81 LGGRPVQHREVQGHESEEFLSYFKKGIIYIEGG 113
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
 390-486 3.71e-45

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: 156.28  E-value: 3.71e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57015325 390 MVDDGSGKVEIWRVENNGRIQVDQNSYGEFYGGDCYIILYTYPRG----QIIYTWQGANATRDELTTSAFLTVQLDRSLG 465
Cdd:cd11293   1 MYDDGSGKVEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQGGgkeeHILYFWQGRHSSQDERAAAALLTVELDEELK 80

                        90       100
                ....*....|....*....|.
gi 57015325 466 GQAVQIRVSQGKEPVHLLSLF 486
Cdd:cd11293  81 GRAVQVRVVQGKEPPHFLALF 101
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 136-225 1.45e-43

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: 151.62  E-value: 1.45e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57015325 136 AKRLLHVKGRRVVRATEVPLSWDSFNKGDCFIIDLGTEIYQWCGSSCNKYERLKANQVATGIRYNERKGRSELIVVEEG- 214
Cdd:cd11289   1 KPRLLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKVIVLDEGd 80

                        90
                ....*....|..
gi 57015325 215 -SEPSELIKVLG 225
Cdd:cd11289  81 tNESPEFWKVLG 92
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 246-346 4.45e-42

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: 147.78  E-value: 4.45e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57015325 246 RKMAKLYMVSDASGSMRVTVVAEEnPFSMAMLLSEECFILDHGAakQIFVWKGKDANPQERKAAMKTAEEFLQQMNYSKN 325
Cdd:cd11292   1 AEQKKLYKVSDASGKLKLTEVAEG-SLNQEMLDSEDCYILDCGS--EIFVWVGKGASLDERKAALKNAEEFLRKKKRPPY 77

                        90       100
                ....*....|....*....|.
gi 57015325 326 TQIQVLPEGGETPIFKQFFKD 346
Cdd:cd11292  78 TQVTRVTEGGESALFKSKFAN 98
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 508-598 7.15e-41

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: 144.30  E-value: 7.15e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57015325 508 PPTRLFQVRRNLASITRIVEVDVDANSLNSNDVFVLKLPqNSGYIWVGKGASQEEEKGAEYVASVLK--CKTLRIQEGEE 585
Cdd:cd11288   1 SPTRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKTP-SSVYLWVGKGSSEDERELAKDVASFLKpkASLQEVAEGSE 79

                        90
                ....*....|...
gi 57015325 586 PEEFWNSLGGKKD 598
Cdd:cd11288  80 PDEFWEALGGKSE 92
gelsolin_S1_like cd11290
Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; ...
 398-497 2.45e-27

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: 106.92  E-value: 2.45e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57015325 398 VEIWRVENNGRIQVDQNSYGEFYGGDCYIILYTYPRGQI-----IYTWQGANATRDELTTSAFLTVQLDRSLGGQAVQIR 472
Cdd:cd11290  10 LQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDPSGslsydIHYWLGKEASQDEAGAAAIKAVELDDYLGGRPVQHR 89

                        90       100
                ....*....|....*....|....*
gi 57015325 473 VSQGKEPVHLLSLFkdKPLIIYKNG 497
Cdd:cd11290  90 EVQGHESEEFLSYF--KKGIIYIEG 112
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
 19-111 9.47e-27

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: 104.66  E-value: 9.47e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57015325  19 LQVWRIEKLELVPVPQSAHGDFYVGDAYLVLHTAKTSRGFTYHLHFWLGKECSQDESTAAAIFTVQMDDYLGGKPVQNRE 98
Cdd:cd11293   9 VEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQGGGKEEHILYFWQGRHSSQDERAAAALLTVELDEELKGRAVQVRV 88

                        90
                ....*....|...
gi 57015325  99 LQGYESNDFVSYF 111
Cdd:cd11293  89 VQGKEPPHFLALF 101
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 619-710 6.15e-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: 101.99  E-value: 6.15e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57015325    619 CSNKTGRFVIEEIPGEFTQDDLAEDDVMLLDAWEQIFIWIGKDANEVEKKESLKSAKMYLETDPSGrdkRTPIVIIKQGH 698
Cdd:smart00262   2 LVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPG---PVQVRVVDEGK 78

                           90
                   ....*....|..
gi 57015325    699 EPPTFTGWFLGW 710
Cdd:smart00262  79 EPPEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 138-225 1.16e-25

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 101.22  E-value: 1.16e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57015325    138 RLLHVKGRRVVRATEVPLSWDSFNKGDCFIIDLGTEIYQWCGSSCNKYERLKANQVATGIRYNERKGRSELIVVEEGSEP 217
Cdd:smart00262   1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVRVVDEGKEP 80


                   ....*...
gi 57015325    218 SELIKVLG 225
Cdd:smart00262  81 PEFWSLFG 88
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 259-347 6.93e-25

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 98.90  E-value: 6.93e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57015325    259 GSMRVTVVAEENPFSMAMLLSEECFILDHGAakQIFVWKGKDANPQERKAAMKTAEEFLQQMNySKNTQIQVLPEGGETP 338
Cdd:smart00262   5 VKGKRNVRVPEVPFSQGSLNSGDCYILDTGS--EIYVWVGKKSSQDEKKKAAELAVELDDTLG-PGPVQVRVVDEGKEPP 81


                   ....*....
gi 57015325    339 IFKQFFKDW 347
Cdd:smart00262  82 EFWSLFGGW 90
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 613-707 1.15e-22

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: 92.43  E-value: 1.15e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57015325 613 PPRLYGCSNKTgRFVIEEIPGEFTqdDLAEDDVMLLDAWEQIFIWIGKDANEVEKKESLKSAKMYLETdpsgRDKRTPIV 692
Cdd:cd11280   1 PPRLYRVRGSK-AIEIEEVPLASS--SLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKELDEE----RKGKPEIV 73

                        90
                ....*....|....*
gi 57015325 693 IIKQGHEPPTFTGWF 707
Cdd:cd11280  74 RIRQGQEPREFWSLF 88
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 399-489 4.29e-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: 4.29e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57015325    399 EIWRVENNGRIQVDQ--NSYGEFYGGDCYIILYtyprGQIIYTWQGANATRDELTTSAFLTVQLDRSLGGQAVQIR-VSQ 475
Cdd:smart00262   1 FLVRVKGKRNVRVPEvpFSQGSLNSGDCYILDT----GSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVRvVDE 76

                           90
                   ....*....|....
gi 57015325    476 GKEPVHLLSLFKDK 489
Cdd:smart00262  77 GKEPPEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 20-114 1.39e-21

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: 89.66  E-value: 1.39e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57015325     20 QVWRIEKLELVPVPQS--AHGDFYVGDAYLVLHTaktsrgftYHLHFWLGKECSQDESTAAAIFTVQMDDYLGGKPVQNR 97
Cdd:smart00262   1 FLVRVKGKRNVRVPEVpfSQGSLNSGDCYILDTG--------SEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVR 72

                           90
                   ....*....|....*...
gi 57015325     98 EL-QGYESNDFVSYFKGG 114
Cdd:smart00262  73 VVdEGKEPPEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 513-596 6.29e-21

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: 87.73  E-value: 6.29e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57015325    513 FQVRRNLASITRIVEVDVDANSLNSNDVFVLKLPQNSgYIWVGKGASQEEEKGAEYVASVL-------KCKTLRIQEGEE 585
Cdd:smart00262   1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEI-YVWVGKKSSQDEKKKAAELAVELddtlgpgPVQVRVVDEGKE 79

                           90
                   ....*....|.
gi 57015325    586 PEEFWNSLGGK 596
Cdd:smart00262  80 PPEFWSLFGGW 90
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 509-593 6.49e-20

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: 84.73  E-value: 6.49e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57015325 509 PTRLFQVRRNlaSITRIVEVDVDANSLNSNDVFVLKLpQNSGYIWVGKGASQEEEKGAEYVASVL------KCKTLRIQE 582
Cdd:cd11280   1 PPRLYRVRGS--KAIEIEEVPLASSSLDSDDVFVLDT-GSEIYIWQGRASSQAELAAAALLAKELdeerkgKPEIVRIRQ 77

                        90
                ....*....|.
gi 57015325 583 GEEPEEFWNSL 593
Cdd:cd11280  78 GQEPREFWSLF 88
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 614-707 2.10e-19

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: 83.45  E-value: 2.10e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57015325 614 PRLYGCSNKTGRFVIEEIP-GEFTQDDLAEDDVMLLDAWEQIFIWIGKDANEVEKKESLKSAKMYLETdpSGRDKRTPIV 692
Cdd:cd11292   4 KKLYKVSDASGKLKLTEVAeGSLNQEMLDSEDCYILDCGSEIFVWVGKGASLDERKAALKNAEEFLRK--KKRPPYTQVT 81

                        90
                ....*....|....*
gi 57015325 693 IIKQGHEPPTFTGWF 707
Cdd:cd11292  82 RVTEGGESALFKSKF 96
Gelsolin pfam00626
Gelsolin repeat;
146-221 2.16e-19

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 82.74  E-value: 2.16e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 57015325   146 RVVRATEVPLSWDSFNKGDCFIIDLGTEIYQWCGSSCNKYERLKANQVATGIRYNERKGRSELIVVEEGSEPSELI 221
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDERFPLPEVIRVPQGKEPARFL 76
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 250-347 1.83e-18

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: 80.80  E-value: 1.83e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57015325 250 KLYMVSDASGsmrVTVVAEENPFSMAMLLSEECFILDHGaaKQIFVWKGKDANPQERKAAMKTAEEFLQQMNYSKN---T 326
Cdd:cd11291   3 RLFRCSNESG---FFKVEEISDFSQDDLDTDDIMLLDTG--DEVFVWVGSESSDEEKKEALTSAKKYIETDPLGRSkprT 77

                        90       100
                ....*....|....*....|.
gi 57015325 327 QIQVLPEGGETPIFKQFFKDW 347
Cdd:cd11291  78 PIYLVKQGNEPPTFTGYFHAW 98
Gelsolin pfam00626
Gelsolin repeat;
626-703 4.39e-15

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 70.41  E-value: 4.39e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 57015325   626 FVIEEIPGEFTQDDLAEDDVMLLDAWEQIFIWIGKDANEVEKKESLKSAKMYLETDpsgRDKRTPIVIIKQGHEPPTF 703
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDE---RFPLPEVIRVPQGKEPARF 75
Gelsolin pfam00626
Gelsolin repeat;
263-341 2.72e-14

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 68.10  E-value: 2.72e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 57015325   263 VTVVAEENPFSMAMLLSEECFILDHGaaKQIFVWKGKDANPQERKAAMKTAEEFLQQMnYSKNTQIQVLPEGGETPIFK 341
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNG--FTIFLWVGKGSSLLEKLFAALLAAQLDDDE-RFPLPEVIRVPQGKEPARFL 76
Gelsolin pfam00626
Gelsolin repeat;
26-108 4.02e-14

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 67.72  E-value: 4.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57015325    26 KLELVPVPQSAHGDFYVGDAYLVLHTaktsrgftYHLHFWLGKECSQDESTAAAIFTVQMDD-YLGGKPVQNRELQGYES 104
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNG--------FTIFLWVGKGSSLLEKLFAALLAAQLDDdERFPLPEVIRVPQGKEP 72


                  ....
gi 57015325   105 NDFV 108
Cdd:pfam00626  73 ARFL 76
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 138-220 1.59e-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: 66.62  E-value: 1.59e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57015325 138 RLLHVKGRRVVRATEVPLSWDSFNKGDCFIIDLGTEIYQWCGSSCNKYERLKANQVATGIRyNERKGRSELIVVEEGSEP 217
Cdd:cd11280   3 RLYRVRGSKAIEIEEVPLASSSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKELD-EERKGKPEIVRIRQGQEP 81


                ...
gi 57015325 218 SEL 220
Cdd:cd11280  82 REF 84
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 20-111 2.54e-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: 65.85  E-value: 2.54e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57015325  20 QVWRIEK---LELVPVPQsAHGDFYVGDAYLVLhtaktsrgFTYHLHFWLGKECSQDESTAAAIFTVQMDDYLGGKPVQN 96
Cdd:cd11280   3 RLYRVRGskaIEIEEVPL-ASSSLDSDDVFVLD--------TGSEIYIWQGRASSQAELAAAALLAKELDEERKGKPEIV 73

                        90
                ....*....|....*
gi 57015325  97 RELQGYESNDFVSYF 111
Cdd:cd11280  74 RIRQGQEPREFWSLF 88
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 400-486 1.61e-12

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


Pssm-ID: 200436  Cd Length: 88  Bit Score: 63.54  E-value: 1.61e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57015325 400 IWRVENNGRI---QVDQNSYgEFYGGDCYIILYtyprGQIIYTWQGANATRDELTTSAFLTVQLDRSLGGQAVQIRVSQG 476
Cdd:cd11280   4 LYRVRGSKAIeieEVPLASS-SLDSDDVFVLDT----GSEIYIWQGRASSQAELAAAALLAKELDEERKGKPEIVRIRQG 78

                        90
                ....*....|
gi 57015325 477 KEPVHLLSLF 486
Cdd:cd11280  79 QEPREFWSLF 88
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 509-594 1.26e-11

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


Pssm-ID: 200445  Cd Length: 92  Bit Score: 61.10  E-value: 1.26e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57015325 509 PTRLFQV--RRNlasiTRIVEVDVDANSLNSNDVFVLKLPQNSgYIWVGKGASQEEE-KGAEYVASVL------KCKTLR 579
Cdd:cd11289   1 KPRLLHVkgRRN----VRAREVELSWSSLNSGDVFILDLGSTI-YQWNGSKSNRFEKaKAMQLAQGIRderrlgRAKVIV 75

                        90
                ....*....|....*..
gi 57015325 580 IQEGE--EPEEFWNSLG 594
Cdd:cd11289  76 LDEGDtnESPEFWKVLG 92
Gelsolin pfam00626
Gelsolin repeat;
410-483 2.33e-11

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 60.01  E-value: 2.33e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 57015325   410 QVDQNSYGEFYGGDCYIILYtyprGQIIYTWQGANATRDELTTSAFLTVQLDRS-LGGQAVQIRVSQGKEPVHLL 483
Cdd:pfam00626   6 PPVPLSQESLNSGDCYLLDN----GFTIFLWVGKGSSLLEKLFAALLAAQLDDDeRFPLPEVIRVPQGKEPARFL 76
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 251-344 2.51e-11

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: 60.07  E-value: 2.51e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57015325 251 LYMVSdASGSMRVtvvaEENPFSMAMLLSEECFILDHGAakQIFVWKGKDANPQERKAAMKTAEEFLQQmnYSKNTQIQV 330
Cdd:cd11280   4 LYRVR-GSKAIEI----EEVPLASSSLDSDDVFVLDTGS--EIYIWQGRASSQAELAAAALLAKELDEE--RKGKPEIVR 74

                        90
                ....*....|....
gi 57015325 331 LPEGGETPIFKQFF 344
Cdd:cd11280  75 IRQGQEPREFWSLF 88
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 138-227 5.90e-11

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: 59.17  E-value: 5.90e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57015325 138 RLLHVKGRRVV--RATEVPLSWDSFNKGDCFIIDLGTEIYQWCGSSCNKYERLKANQVATGIrynerKGRSELIVVEEGS 215
Cdd:cd11288   4 RLFQVRGNGSGntRAVEVDADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVASFL-----KPKASLQEVAEGS 78

                        90
                ....*....|..
gi 57015325 216 EPSELIKVLGEK 227
Cdd:cd11288  79 EPDEFWEALGGK 90
Gelsolin pfam00626
Gelsolin repeat;
526-590 3.87e-07

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 48.07  E-value: 3.87e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 57015325   526 VEVDVDANSLNSNDVFVLKLPQNSgYIWVGKGASQEEEKGAEYVASVL-------KCKTLRIQEGEEPEEFW 590
Cdd:pfam00626   6 PPVPLSQESLNSGDCYLLDNGFTI-FLWVGKGSSLLEKLFAALLAAQLddderfpLPEVIRVPQGKEPARFL 76
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 269-340 1.43e-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: 46.84  E-value: 1.43e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 57015325 269 ENPFSMAMLLSEECFILDHGaaKQIFVWKGKDANPQERKAAMKTAEeflqqmNYSKNTQIQVLPEGGETPIF 340
Cdd:cd11288  20 EVDADASSLNSNDVFVLKTP--SSVYLWVGKGSSEDERELAKDVAS------FLKPKASLQEVAEGSEPDEF 83
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 147-222 1.99e-05

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: 43.83  E-value: 1.99e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57015325 147 VVRATEV-PLSWDSFNKGDCFIIDLGTEIYQWCGSSCNKYERLKANQVATgiRY------NERKGRSELIVVEEGSEPSE 219
Cdd:cd11291  13 FFKVEEIsDFSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAK--KYietdplGRSKPRTPIYLVKQGNEPPT 90


                ...
gi 57015325 220 LIK 222
Cdd:cd11291  91 FTG 93
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 535-589 6.72e-05

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: 42.24  E-value: 6.72e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 57015325 535 LNSNDVFVLKlpQNSG-YIWVGKGASQEEEKGA-----EYVASVLKCKTL---RIQEGEEPEEF 589
Cdd:cd11292  31 LDSEDCYILD--CGSEiFVWVGKGASLDERKAAlknaeEFLRKKKRPPYTqvtRVTEGGESALF 92
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 613-703 2.98e-03

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: 37.60  E-value: 2.98e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57015325 613 PPRLYGCSnktGRFVIEEIPGEFTQDDLAEDDVMLLDAWEQIFIWIGKDANEVEKKESLKSAKMYLETDPSGRDKrTPIV 692
Cdd:cd11289   1 KPRLLHVK---GRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAK-VIVL 76

                        90
                ....*....|.
gi 57015325 693 IIKQGHEPPTF 703
Cdd:cd11289  77 DEGDTNESPEF 87
 
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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