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Conserved domains on  [gi|706114291|ref|XP_010193982|]
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gelsolin isoform X1 [Colius striatus]

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_S1_like cd11290
Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; ...
 55-167 1.06e-64

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: 210.93  E-value: 1.06e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 706114291  55 FAKAGKEPGLQIWRIEKFDLVPVPKNLYGDFFTGDSYLVLNTIRQRSGNLQYDLHFWLGDESSQDERGAAAIFTVQMDDY 134
Cdd:cd11290    1 FEGVGQKPGLQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDPSGSLSYDIHYWLGKEASQDEAGAAAIKAVELDDY 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 706114291 135 LHGKAVQHREVQGHESSTFLGYFKSGIKYKAGG 167
Cdd:cd11290   81 LGGRPVQHREVQGHESEEFLSYFKKGIIYIEGG 113
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
 435-535 3.76e-56

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: 187.09  E-value: 3.76e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 706114291 435 MEDDGSGKKQIWRIEGSEKVPVSPSTYGQFYGGDSYIILYNYQHAGKQGQIIYTWQGADSTQDEIATSAFLTVQLDEELG 514
Cdd:cd11293    1 MYDDGSGKVEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQGGGKEEHILYFWQGRHSSQDERAAAALLTVELDEELK 80

                         90       100
                 ....*....|....*....|.
gi 706114291 515 GSPVQKRVVQGKEPPHLMSMF 535
Cdd:cd11293   81 GRAVQVRVVQGKEPPHFLALF 101
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 662-760 2.58e-52

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: 176.72  E-value: 2.58e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 706114291 662 PPRLFACSNKSGRFTIEEVPgDLTQEDLATDDVMLLDTWDQVFVWIGKDAQEEEKTEALKSAKRYIETDPASRDK-RTPV 740
Cdd:cd11291    1 KPRLFRCSNESGFFKVEEIS-DFSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYIETDPLGRSKpRTPI 79

                         90       100
                 ....*....|....*....|
gi 706114291 741 TVVKQGFEPPTFSGWFLGWD 760
Cdd:cd11291   80 YLVKQGNEPPTFTGYFHAWD 99
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 182-271 4.21e-44

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: 153.55  E-value: 4.21e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 706114291 182 VQRLLQVKGRRTVRATEVPVTWESFNTGDCFILDLGSNIFQWCGSNSNRHERLKATVLAKGIRDNERNGRARVYVSEEG- 260
Cdd:cd11289    1 KPRLLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKVIVLDEGd 80

                         90
                 ....*....|..
gi 706114291 261 -SEREEMLQVLG 271
Cdd:cd11289   81 tNESPEFWKVLG 92
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 294-391 1.15e-40

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: 144.31  E-value: 1.15e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 706114291 294 AKLYKVSNGAGNMAVSLVADEnPFSQAALNTDDCFILDHGTdgKIFVWKGKTANSDEKAAALKTASEFIDKMGYPKHTQV 373
Cdd:cd11292    4 KKLYKVSDASGKLKLTEVAEG-SLNQEMLDSEDCYILDCGS--EIFVWVGKGASLDERKAALKNAEEFLRKKKRPPYTQV 80

                         90
                 ....*....|....*...
gi 706114291 374 QVLPESGETPLFKQFFKN 391
Cdd:cd11292   81 TRVTEGGESALFKSKFAN 98
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 557-646 5.60e-40

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: 141.99  E-value: 5.60e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 706114291 557 AATRLFQVRSSTSGATRAVELDATASQLNSNDAFVLKTPSAAYLWVGQGASDAEKSGAQELLKILG--ARPVQVSEGREP 634
Cdd:cd11288    1 SPTRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVASFLKpkASLQEVAEGSEP 80

                         90
                 ....*....|..
gi 706114291 635 DNFWAALGGKAP 646
Cdd:cd11288   81 DEFWEALGGKSE 92
 
Name Accession Description Interval E-value
gelsolin_S1_like cd11290
Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; ...
 55-167 1.06e-64

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: 210.93  E-value: 1.06e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 706114291  55 FAKAGKEPGLQIWRIEKFDLVPVPKNLYGDFFTGDSYLVLNTIRQRSGNLQYDLHFWLGDESSQDERGAAAIFTVQMDDY 134
Cdd:cd11290    1 FEGVGQKPGLQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDPSGSLSYDIHYWLGKEASQDEAGAAAIKAVELDDY 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 706114291 135 LHGKAVQHREVQGHESSTFLGYFKSGIKYKAGG 167
Cdd:cd11290   81 LGGRPVQHREVQGHESEEFLSYFKKGIIYIEGG 113
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
 435-535 3.76e-56

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: 187.09  E-value: 3.76e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 706114291 435 MEDDGSGKKQIWRIEGSEKVPVSPSTYGQFYGGDSYIILYNYQHAGKQGQIIYTWQGADSTQDEIATSAFLTVQLDEELG 514
Cdd:cd11293    1 MYDDGSGKVEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQGGGKEEHILYFWQGRHSSQDERAAAALLTVELDEELK 80

                         90       100
                 ....*....|....*....|.
gi 706114291 515 GSPVQKRVVQGKEPPHLMSMF 535
Cdd:cd11293   81 GRAVQVRVVQGKEPPHFLALF 101
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 662-760 2.58e-52

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: 176.72  E-value: 2.58e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 706114291 662 PPRLFACSNKSGRFTIEEVPgDLTQEDLATDDVMLLDTWDQVFVWIGKDAQEEEKTEALKSAKRYIETDPASRDK-RTPV 740
Cdd:cd11291    1 KPRLFRCSNESGFFKVEEIS-DFSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYIETDPLGRSKpRTPI 79

                         90       100
                 ....*....|....*....|
gi 706114291 741 TVVKQGFEPPTFSGWFLGWD 760
Cdd:cd11291   80 YLVKQGNEPPTFTGYFHAWD 99
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 182-271 4.21e-44

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: 153.55  E-value: 4.21e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 706114291 182 VQRLLQVKGRRTVRATEVPVTWESFNTGDCFILDLGSNIFQWCGSNSNRHERLKATVLAKGIRDNERNGRARVYVSEEG- 260
Cdd:cd11289    1 KPRLLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKVIVLDEGd 80

                         90
                 ....*....|..
gi 706114291 261 -SEREEMLQVLG 271
Cdd:cd11289   81 tNESPEFWKVLG 92
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 294-391 1.15e-40

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: 144.31  E-value: 1.15e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 706114291 294 AKLYKVSNGAGNMAVSLVADEnPFSQAALNTDDCFILDHGTdgKIFVWKGKTANSDEKAAALKTASEFIDKMGYPKHTQV 373
Cdd:cd11292    4 KKLYKVSDASGKLKLTEVAEG-SLNQEMLDSEDCYILDCGS--EIFVWVGKGASLDERKAALKNAEEFLRKKKRPPYTQV 80

                         90
                 ....*....|....*...
gi 706114291 374 QVLPESGETPLFKQFFKN 391
Cdd:cd11292   81 TRVTEGGESALFKSKFAN 98
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 557-646 5.60e-40

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: 141.99  E-value: 5.60e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 706114291 557 AATRLFQVRSSTSGATRAVELDATASQLNSNDAFVLKTPSAAYLWVGQGASDAEKSGAQELLKILG--ARPVQVSEGREP 634
Cdd:cd11288    1 SPTRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVASFLKpkASLQEVAEGSEP 80

                         90
                 ....*....|..
gi 706114291 635 DNFWAALGGKAP 646
Cdd:cd11288   81 DEFWEALGGKSE 92
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 184-273 3.34e-28

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 108.53  E-value: 3.34e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 706114291   184 RLLQVKGRRTVRATEVPVTWESFNTGDCFILDLGSNIFQWCGSNSNRHERLKATVLAKGIRDNERNGRARVYVSEEGSER 263
Cdd:smart00262   1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVRVVDEGKEP 80

                           90
                   ....*....|
gi 706114291   264 EEMLQVLGPK 273
Cdd:smart00262  81 PEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 668-759 4.83e-27

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: 105.07  E-value: 4.83e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 706114291   668 CSNKSGRFTIEEVPGDLTQEDLATDDVMLLDTWDQVFVWIGKDAQEEEKTEALKSAKRYIETDpasRDKRTPVTVVKQGF 747
Cdd:smart00262   2 LVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTL---GPGPVQVRVVDEGK 78

                           90
                   ....*....|..
gi 706114291   748 EPPTFSGWFLGW 759
Cdd:smart00262  79 EPPEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 304-392 6.87e-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: 6.87e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 706114291   304 GNMAVSLVADENPFSQAALNTDDCFILDHGTDgkIFVWKGKTANSDEKAAALKTASEFIDKMGyPKHTQVQVLPESGETP 383
Cdd:smart00262   5 VKGKRNVRVPEVPFSQGSLNSGDCYILDTGSE--IYVWVGKKSSQDEKKKAAELAVELDDTLG-PGPVQVRVVDEGKEPP 81


                   ....*....
gi 706114291   384 LFKQFFKNW 392
Cdd:smart00262  82 EFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 444-538 1.91e-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: 100.44  E-value: 1.91e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 706114291   444 QIWRIEGSEKVPV--SPSTYGQFYGGDSYIILYnyqhagkqGQIIYTWQGADSTQDEIATSAFLTVQLDEELGGSPVQKR 521
Cdd:smart00262   1 FLVRVKGKRNVRVpeVPFSQGSLNSGDCYILDT--------GSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVR 72

                           90
                   ....*....|....*...
gi 706114291   522 VV-QGKEPPHLMSMFGGK 538
Cdd:smart00262  73 VVdEGKEPPEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 65-160 3.89e-23

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 93.90  E-value: 3.89e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 706114291    65 QIWRIEKFDLVPVP--KNLYGDFFTGDSYLVLNTirqrsgnlqYDLHFWLGDESSQDERGAAAIFTVQMDDYLHGKAVQH 142
Cdd:smart00262   1 FLVRVKGKRNVRVPevPFSQGSLNSGDCYILDTG---------SEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQV 71

                           90
                   ....*....|....*....
gi 706114291   143 REV-QGHESSTFLGYFKSG 160
Cdd:smart00262  72 RVVdEGKEPPEFWSLFGGW 90
Gelsolin pfam00626
Gelsolin repeat;
192-267 4.52e-21

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 87.75  E-value: 4.52e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 706114291  192 RTVRATEVPVTWESFNTGDCFILDLGSNIFQWCGSNSNRHERLKATVLAKGIRDNERNGRARVYVSEEGSEREEML 267
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDERFPLPEVIRVPQGKEPARFL 76
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 562-644 3.49e-20

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 85.81  E-value: 3.49e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 706114291   562 FQVRSSTSGATRAVELDATASQLNSNDAFVLKTPSAAYLWVGQGASDAEKSGA----QELLKILGARPVQ---VSEGREP 634
Cdd:smart00262   1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAaelaVELDDTLGPGPVQvrvVDEGKEP 80

                           90
                   ....*....|
gi 706114291   635 DNFWAALGGK 644
Cdd:smart00262  81 PEFWSLFGGW 90
Gelsolin pfam00626
Gelsolin repeat;
675-752 7.93e-18

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 78.50  E-value: 7.93e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 706114291  675 FTIEEVPGDLTQEDLATDDVMLLDTWDQVFVWIGKDAQEEEKTEALKSAKRYIETDpasRDKRTPVTVVKQGFEPPTF 752
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDE---RFPLPEVIRVPQGKEPARF 75
Gelsolin pfam00626
Gelsolin repeat;
450-532 1.26e-14

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 69.26  E-value: 1.26e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 706114291  450 GSEKVPVSPSTYGQFYGGDSYIILynyqhagkQGQIIYTWQGADSTQDEIATSAFLTVQLD-EELGGSPVQKRVVQGKEP 528
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLD--------NGFTIFLWVGKGSSLLEKLFAALLAAQLDdDERFPLPEVIRVPQGKEP 72


                  ....
gi 706114291  529 PHLM 532
Cdd:pfam00626  73 ARFL 76
Gelsolin pfam00626
Gelsolin repeat;
71-154 2.05e-14

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 68.87  E-value: 2.05e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 706114291   71 KFDLVPVPKNLYGDFFTGDSYLVLNTirqrsgnlqYDLHFWLGDESSQDERGAAAIFTVQMDD-YLHGKAVQHREVQGHE 149
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNG---------FTIFLWVGKGSSLLEKLFAALLAAQLDDdERFPLPEVIRVPQGKE 71


                  ....*
gi 706114291  150 SSTFL 154
Cdd:pfam00626  72 PARFL 76
Gelsolin pfam00626
Gelsolin repeat;
308-386 3.15e-14

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 68.10  E-value: 3.15e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 706114291  308 VSLVADENPFSQAALNTDDCFILDHGTdgKIFVWKGKTANSDEKAAALKTASEFIDKMGYPKhTQVQVLPESGETPLFK 386
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNGF--TIFLWVGKGSSLLEKLFAALLAAQLDDDERFPL-PEVIRVPQGKEPARFL 76
Gelsolin pfam00626
Gelsolin repeat;
570-638 3.64e-09

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 53.85  E-value: 3.64e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 706114291  570 GATRAVELDATASQLNSNDAFVLKTPSAAYLWVGQGASDAEKSGAQELLKIL-----GARPVQ--VSEGREPDNFW 638
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLddderFPLPEVirVPQGKEPARFL 76
 
Name Accession Description Interval E-value
gelsolin_S1_like cd11290
Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; ...
 55-167 1.06e-64

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: 210.93  E-value: 1.06e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 706114291  55 FAKAGKEPGLQIWRIEKFDLVPVPKNLYGDFFTGDSYLVLNTIRQRSGNLQYDLHFWLGDESSQDERGAAAIFTVQMDDY 134
Cdd:cd11290    1 FEGVGQKPGLQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDPSGSLSYDIHYWLGKEASQDEAGAAAIKAVELDDY 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 706114291 135 LHGKAVQHREVQGHESSTFLGYFKSGIKYKAGG 167
Cdd:cd11290   81 LGGRPVQHREVQGHESEEFLSYFKKGIIYIEGG 113
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
 435-535 3.76e-56

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: 187.09  E-value: 3.76e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 706114291 435 MEDDGSGKKQIWRIEGSEKVPVSPSTYGQFYGGDSYIILYNYQHAGKQGQIIYTWQGADSTQDEIATSAFLTVQLDEELG 514
Cdd:cd11293    1 MYDDGSGKVEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQGGGKEEHILYFWQGRHSSQDERAAAALLTVELDEELK 80

                         90       100
                 ....*....|....*....|.
gi 706114291 515 GSPVQKRVVQGKEPPHLMSMF 535
Cdd:cd11293   81 GRAVQVRVVQGKEPPHFLALF 101
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 662-760 2.58e-52

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: 176.72  E-value: 2.58e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 706114291 662 PPRLFACSNKSGRFTIEEVPgDLTQEDLATDDVMLLDTWDQVFVWIGKDAQEEEKTEALKSAKRYIETDPASRDK-RTPV 740
Cdd:cd11291    1 KPRLFRCSNESGFFKVEEIS-DFSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYIETDPLGRSKpRTPI 79

                         90       100
                 ....*....|....*....|
gi 706114291 741 TVVKQGFEPPTFSGWFLGWD 760
Cdd:cd11291   80 YLVKQGNEPPTFTGYFHAWD 99
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 182-271 4.21e-44

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: 153.55  E-value: 4.21e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 706114291 182 VQRLLQVKGRRTVRATEVPVTWESFNTGDCFILDLGSNIFQWCGSNSNRHERLKATVLAKGIRDNERNGRARVYVSEEG- 260
Cdd:cd11289    1 KPRLLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKVIVLDEGd 80

                         90
                 ....*....|..
gi 706114291 261 -SEREEMLQVLG 271
Cdd:cd11289   81 tNESPEFWKVLG 92
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 294-391 1.15e-40

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: 144.31  E-value: 1.15e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 706114291 294 AKLYKVSNGAGNMAVSLVADEnPFSQAALNTDDCFILDHGTdgKIFVWKGKTANSDEKAAALKTASEFIDKMGYPKHTQV 373
Cdd:cd11292    4 KKLYKVSDASGKLKLTEVAEG-SLNQEMLDSEDCYILDCGS--EIFVWVGKGASLDERKAALKNAEEFLRKKKRPPYTQV 80

                         90
                 ....*....|....*...
gi 706114291 374 QVLPESGETPLFKQFFKN 391
Cdd:cd11292   81 TRVTEGGESALFKSKFAN 98
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 557-646 5.60e-40

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: 141.99  E-value: 5.60e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 706114291 557 AATRLFQVRSSTSGATRAVELDATASQLNSNDAFVLKTPSAAYLWVGQGASDAEKSGAQELLKILG--ARPVQVSEGREP 634
Cdd:cd11288    1 SPTRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVASFLKpkASLQEVAEGSEP 80

                         90
                 ....*....|..
gi 706114291 635 DNFWAALGGKAP 646
Cdd:cd11288   81 DEFWEALGGKSE 92
gelsolin_S1_like cd11290
Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; ...
 438-546 8.57e-32

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: 119.64  E-value: 8.57e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 706114291 438 DGSGKK---QIWRIEGSEKVPVSPSTYGQFYGGDSYIILYNYQHA-GKQGQIIYTWQGADSTQDEIATSAFLTVQLDEEL 513
Cdd:cd11290    2 EGVGQKpglQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDPsGSLSYDIHYWLGKEASQDEAGAAAIKAVELDDYL 81

                         90       100       110
                 ....*....|....*....|....*....|...
gi 706114291 514 GGSPVQKRVVQGKEPPHLMSMFggKPLIVYKGG 546
Cdd:cd11290   82 GGRPVQHREVQGHESEEFLSYF--KKGIIYIEG 112
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
 64-157 1.26e-29

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: 113.13  E-value: 1.26e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 706114291  64 LQIWRIEKFDLVPVPKNLYGDFFTGDSYLVLNTIrQRSGNLQYDLHFWLGDESSQDERGAAAIFTVQMDDYLHGKAVQHR 143
Cdd:cd11293    9 VEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTY-QGGGKEEHILYFWQGRHSSQDERAAAALLTVELDEELKGRAVQVR 87

                         90
                 ....*....|....
gi 706114291 144 EVQGHESSTFLGYF 157
Cdd:cd11293   88 VVQGKEPPHFLALF 101
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 184-273 3.34e-28

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 108.53  E-value: 3.34e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 706114291   184 RLLQVKGRRTVRATEVPVTWESFNTGDCFILDLGSNIFQWCGSNSNRHERLKATVLAKGIRDNERNGRARVYVSEEGSER 263
Cdd:smart00262   1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVRVVDEGKEP 80

                           90
                   ....*....|
gi 706114291   264 EEMLQVLGPK 273
Cdd:smart00262  81 PEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 668-759 4.83e-27

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: 105.07  E-value: 4.83e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 706114291   668 CSNKSGRFTIEEVPGDLTQEDLATDDVMLLDTWDQVFVWIGKDAQEEEKTEALKSAKRYIETDpasRDKRTPVTVVKQGF 747
Cdd:smart00262   2 LVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTL---GPGPVQVRVVDEGK 78

                           90
                   ....*....|..
gi 706114291   748 EPPTFSGWFLGW 759
Cdd:smart00262  79 EPPEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 304-392 6.87e-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: 6.87e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 706114291   304 GNMAVSLVADENPFSQAALNTDDCFILDHGTDgkIFVWKGKTANSDEKAAALKTASEFIDKMGyPKHTQVQVLPESGETP 383
Cdd:smart00262   5 VKGKRNVRVPEVPFSQGSLNSGDCYILDTGSE--IYVWVGKKSSQDEKKKAAELAVELDDTLG-PGPVQVRVVDEGKEPP 81


                   ....*....
gi 706114291   384 LFKQFFKNW 392
Cdd:smart00262  82 EFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 444-538 1.91e-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: 100.44  E-value: 1.91e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 706114291   444 QIWRIEGSEKVPV--SPSTYGQFYGGDSYIILYnyqhagkqGQIIYTWQGADSTQDEIATSAFLTVQLDEELGGSPVQKR 521
Cdd:smart00262   1 FLVRVKGKRNVRVpeVPFSQGSLNSGDCYILDT--------GSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVR 72

                           90
                   ....*....|....*...
gi 706114291   522 VV-QGKEPPHLMSMFGGK 538
Cdd:smart00262  73 VVdEGKEPPEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 65-160 3.89e-23

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 93.90  E-value: 3.89e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 706114291    65 QIWRIEKFDLVPVP--KNLYGDFFTGDSYLVLNTirqrsgnlqYDLHFWLGDESSQDERGAAAIFTVQMDDYLHGKAVQH 142
Cdd:smart00262   1 FLVRVKGKRNVRVPevPFSQGSLNSGDCYILDTG---------SEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQV 71

                           90
                   ....*....|....*....
gi 706114291   143 REV-QGHESSTFLGYFKSG 160
Cdd:smart00262  72 RVVdEGKEPPEFWSLFGGW 90
Gelsolin pfam00626
Gelsolin repeat;
192-267 4.52e-21

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 87.75  E-value: 4.52e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 706114291  192 RTVRATEVPVTWESFNTGDCFILDLGSNIFQWCGSNSNRHERLKATVLAKGIRDNERNGRARVYVSEEGSEREEML 267
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDERFPLPEVIRVPQGKEPARFL 76
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 562-644 3.49e-20

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 85.81  E-value: 3.49e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 706114291   562 FQVRSSTSGATRAVELDATASQLNSNDAFVLKTPSAAYLWVGQGASDAEKSGA----QELLKILGARPVQ---VSEGREP 634
Cdd:smart00262   1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAaelaVELDDTLGPGPVQvrvVDEGKEP 80

                           90
                   ....*....|
gi 706114291   635 DNFWAALGGK 644
Cdd:smart00262  81 PEFWSLFGGW 90
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 663-756 5.39e-20

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


Pssm-ID: 200448  Cd Length: 98  Bit Score: 85.38  E-value: 5.39e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 706114291 663 PRLFACSNKSGRFTIEEVP-GDLTQEDLATDDVMLLDTWDQVFVWIGKDAQEEEKTEALKSAKRYIETDpaSRDKRTPVT 741
Cdd:cd11292    4 KKLYKVSDASGKLKLTEVAeGSLNQEMLDSEDCYILDCGSEIFVWVGKGASLDERKAALKNAEEFLRKK--KRPPYTQVT 81

                         90
                 ....*....|....*
gi 706114291 742 VVKQGFEPPTFSGWF 756
Cdd:cd11292   82 RVTEGGESALFKSKF 96
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 662-756 6.58e-19

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: 82.03  E-value: 6.58e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 706114291 662 PPRLFACSNKSgRFTIEEVPGDltQEDLATDDVMLLDTWDQVFVWIGKDAQEEEKTEALKSAKRYIEtdpaSRDKRTPVT 741
Cdd:cd11280    1 PPRLYRVRGSK-AIEIEEVPLA--SSSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKELDE----ERKGKPEIV 73

                         90
                 ....*....|....*
gi 706114291 742 VVKQGFEPPTFSGWF 756
Cdd:cd11280   74 RIRQGQEPREFWSLF 88
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 295-392 4.66e-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: 80.03  E-value: 4.66e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 706114291 295 KLYKVSNGAGNmavsLVADE-NPFSQAALNTDDCFILDHGTdgKIFVWKGKTANSDEKAAALKTASEFIDKMG---YPKH 370
Cdd:cd11291    3 RLFRCSNESGF----FKVEEiSDFSQDDLDTDDIMLLDTGD--EVFVWVGSESSDEEKKEALTSAKKYIETDPlgrSKPR 76

                         90       100
                 ....*....|....*....|..
gi 706114291 371 TQVQVLPESGETPLFKQFFKNW 392
Cdd:cd11291   77 TPIYLVKQGNEPPTFTGYFHAW 98
Gelsolin pfam00626
Gelsolin repeat;
675-752 7.93e-18

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 78.50  E-value: 7.93e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 706114291  675 FTIEEVPGDLTQEDLATDDVMLLDTWDQVFVWIGKDAQEEEKTEALKSAKRYIETDpasRDKRTPVTVVKQGFEPPTF 752
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDE---RFPLPEVIRVPQGKEPARF 75
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 184-270 3.55e-16

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: 74.33  E-value: 3.55e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 706114291 184 RLLQVKGRRTVRATEVPVTWESFNTGDCFILDLGSNIFQWCGSNSNRHERLKATVLAKGIrDNERNGRARVYVSEEGSER 263
Cdd:cd11280    3 RLYRVRGSKAIEIEEVPLASSSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKEL-DEERKGKPEIVRIRQGQEP 81


                 ....*..
gi 706114291 264 EEMLQVL 270
Cdd:cd11280   82 REFWSLF 88
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 558-641 7.88e-16

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: 73.17  E-value: 7.88e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 706114291 558 ATRLFQVRSSTsgATRAVELDATASQLNSNDAFVLKTPSAAYLWVGQGASDAEKSGAQELLKILGARP------VQVSEG 631
Cdd:cd11280    1 PPRLYRVRGSK--AIEIEEVPLASSSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKELDEERkgkpeiVRIRQG 78

                         90
                 ....*....|
gi 706114291 632 REPDNFWAAL 641
Cdd:cd11280   79 QEPREFWSLF 88
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 442-535 1.74e-15

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: 72.02  E-value: 1.74e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 706114291 442 KKQIWRIEGS---EKVPVSPSTYgQFYGGDSYIILYnyqhagkqGQIIYTWQGADSTQDEIATSAFLTVQLDEELGGSPV 518
Cdd:cd11280    1 PPRLYRVRGSkaiEIEEVPLASS-SLDSDDVFVLDT--------GSEIYIWQGRASSQAELAAAALLAKELDEERKGKPE 71

                         90
                 ....*....|....*..
gi 706114291 519 QKRVVQGKEPPHLMSMF 535
Cdd:cd11280   72 IVRIRQGQEPREFWSLF 88
Gelsolin pfam00626
Gelsolin repeat;
450-532 1.26e-14

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 69.26  E-value: 1.26e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 706114291  450 GSEKVPVSPSTYGQFYGGDSYIILynyqhagkQGQIIYTWQGADSTQDEIATSAFLTVQLD-EELGGSPVQKRVVQGKEP 528
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLD--------NGFTIFLWVGKGSSLLEKLFAALLAAQLDdDERFPLPEVIRVPQGKEP 72


                  ....
gi 706114291  529 PHLM 532
Cdd:pfam00626  73 ARFL 76
Gelsolin pfam00626
Gelsolin repeat;
71-154 2.05e-14

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 68.87  E-value: 2.05e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 706114291   71 KFDLVPVPKNLYGDFFTGDSYLVLNTirqrsgnlqYDLHFWLGDESSQDERGAAAIFTVQMDD-YLHGKAVQHREVQGHE 149
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNG---------FTIFLWVGKGSSLLEKLFAALLAAQLDDdERFPLPEVIRVPQGKE 71


                  ....*
gi 706114291  150 SSTFL 154
Cdd:pfam00626  72 PARFL 76
Gelsolin pfam00626
Gelsolin repeat;
308-386 3.15e-14

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 68.10  E-value: 3.15e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 706114291  308 VSLVADENPFSQAALNTDDCFILDHGTdgKIFVWKGKTANSDEKAAALKTASEFIDKMGYPKhTQVQVLPESGETPLFK 386
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNGF--TIFLWVGKGSSLLEKLFAALLAAQLDDDERFPL-PEVIRVPQGKEPARFL 76
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 65-157 7.61e-14

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


Pssm-ID: 200436  Cd Length: 88  Bit Score: 67.39  E-value: 7.61e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 706114291  65 QIWRIEK---FDLVPVPKNLYgDFFTGDSYLVLntirqrsgnLQYDLHFWLGDESSQDERGAAAIFTVQMDDYLHGKAVQ 141
Cdd:cd11280    3 RLYRVRGskaIEIEEVPLASS-SLDSDDVFVLD---------TGSEIYIWQGRASSQAELAAAALLAKELDEERKGKPEI 72

                         90
                 ....*....|....*.
gi 706114291 142 HREVQGHESSTFLGYF 157
Cdd:cd11280   73 VRIRQGQEPREFWSLF 88
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 296-389 8.11e-12

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


Pssm-ID: 200436  Cd Length: 88  Bit Score: 61.61  E-value: 8.11e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 706114291 296 LYKVS-NGAGNMAVSLVADEnpfsqaALNTDDCFILDHGTDgkIFVWKGKTANSDEKAAALKTASEFiDKMGYPKhTQVQ 374
Cdd:cd11280    4 LYRVRgSKAIEIEEVPLASS------SLDSDDVFVLDTGSE--IYIWQGRASSQAELAAAALLAKEL-DEERKGK-PEIV 73

                         90
                 ....*....|....*
gi 706114291 375 VLPESGETPLFKQFF 389
Cdd:cd11280   74 RIRQGQEPREFWSLF 88
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 184-273 6.45e-10

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: 56.47  E-value: 6.45e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 706114291 184 RLLQVKGRRTV--RATEVPVTWESFNTGDCFILDLGSNIFQWCGSNSNRHERLkatvLAKGIRDNERNGRARVYVsEEGS 261
Cdd:cd11288    4 RLFQVRGNGSGntRAVEVDADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERE----LAKDVASFLKPKASLQEV-AEGS 78

                         90
                 ....*....|..
gi 706114291 262 EREEMLQVLGPK 273
Cdd:cd11288   79 EPDEFWEALGGK 90
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 294-390 2.13e-09

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: 54.94  E-value: 2.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 706114291 294 AKLYKVSnGAGNMAVSLVadenPFSQAALNTDDCFILDHGTdgKIFVWKGKTANSDEKAAALKTASEFIDKMGYPKhTQV 373
Cdd:cd11289    2 PRLLHVK-GRRNVRAREV----ELSWSSLNSGDVFILDLGS--TIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGR-AKV 73

                         90
                 ....*....|....*..
gi 706114291 374 QVLpESGETPLFKQFFK 390
Cdd:cd11289   74 IVL-DEGDTNESPEFWK 89
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 558-642 3.06e-09

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: 54.55  E-value: 3.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 706114291 558 ATRLFQVRSSTSGATRAVELdaTASQLNSNDAFVLKTPSAAYLWVGQGASDAEKSGAQELLKIL------GARPVQV--- 628
Cdd:cd11289    1 KPRLLHVKGRRNVRAREVEL--SWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIrderrlGRAKVIVlde 78

                         90
                 ....*....|....
gi 706114291 629 SEGREPDNFWAALG 642
Cdd:cd11289   79 GDTNESPEFWKVLG 92
Gelsolin pfam00626
Gelsolin repeat;
570-638 3.64e-09

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 53.85  E-value: 3.64e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 706114291  570 GATRAVELDATASQLNSNDAFVLKTPSAAYLWVGQGASDAEKSGAQELLKIL-----GARPVQ--VSEGREPDNFW 638
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLddderFPLPEVirVPQGKEPARFL 76
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 294-385 5.20e-08

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: 51.08  E-value: 5.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 706114291 294 AKLYKV-SNGAGNM-AVslvadENPFSQAALNTDDCFILDHGTdgKIFVWKGKTANSDEKAAALKTASEFIDKmgypkhT 371
Cdd:cd11288    3 TRLFQVrGNGSGNTrAV-----EVDADASSLNSNDVFVLKTPS--SVYLWVGKGSSEDERELAKDVASFLKPK------A 69

                         90
                 ....*....|....
gi 706114291 372 QVQVLPESGETPLF 385
Cdd:cd11288   70 SLQEVAEGSEPDEF 83
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 556-637 1.44e-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: 44.16  E-value: 1.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 706114291 556 PAATRLFQVR-SSTSGATRAVELD-ATASQLNSNDAFVLKTPSAAYLWVGQGASDAEK----SGAQELLKILGARP---- 625
Cdd:cd11292    1 AEQKKLYKVSdASGKLKLTEVAEGsLNQEMLDSEDCYILDCGSEIFVWVGKGASLDERkaalKNAEEFLRKKKRPPytqv 80

                         90
                 ....*....|..
gi 706114291 626 VQVSEGREPDNF 637
Cdd:cd11292   81 TRVTEGGESALF 92
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 194-262 6.80e-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: 42.28  E-value: 6.80e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 706114291 194 VRATEV-PVTWESFNTGDCFILDLGSNIFQWCGSNSNRHERLKATVLAKGI----RDNERNGRARVYVSEEGSE 262
Cdd:cd11291   14 FKVEEIsDFSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYietdPLGRSKPRTPIYLVKQGNE 87
ADF_gelsolin cd00013
Actin depolymerization factor/cofilin- and gelsolin-like domains; Actin depolymerization ...
 558-631 2.01e-04

Actin depolymerization factor/cofilin- and gelsolin-like domains; Actin depolymerization factor/cofilin-like domains are present in a family of essential eukaryotic actin regulatory proteins; these proteins enhance the turnover rate of actin and interact with actin monomers as well as actin filaments.


Pssm-ID: 200435  Cd Length: 97  Bit Score: 40.91  E-value: 2.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 706114291 558 ATRLFQVRSSTS----GATRAVELDATASQLNSNDAFVLKTPS------------AAYLWVGQGASD----AEKSGAQEL 617
Cdd:cd00013    1 DWVLFKVDAKKEeivvGSTGAGFLDEFLEELPEDDPRYAFYRFkyphsddkrskfVFISWIPDGVSIkqkmVYATNKQTL 80

                         90
                 ....*....|....*.
gi 706114291 618 LKILG--ARPVQVSEG 631
Cdd:cd00013   81 KEALFglAVPVQIRDG 96
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 662-752 8.56e-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: 39.14  E-value: 8.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 706114291 662 PPRLFACSnksGRFTIE--EVPgdLTQEDLATDDVMLLDTWDQVFVWIGKDAQEEEKTEALKSAKRyIETDpaSRDKRTP 739
Cdd:cd11289    1 KPRLLHVK---GRRNVRarEVE--LSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQG-IRDE--RRLGRAK 72

                         90
                 ....*....|....*
gi 706114291 740 VTVVKQGF--EPPTF 752
Cdd:cd11289   73 VIVLDEGDtnESPEF 87
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
 301-389 5.62e-03

Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200449  Cd Length: 101  Bit Score: 36.87  E-value: 5.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 706114291 301 NGAGNMAVSLVADEN-----PFSQAALNTDDCFILDHGTDGK------IFVWKGKTANSDEKAAALKTASEFIDKMGYpK 369
Cdd:cd11293    4 DGSGKVEVWRIENDEkvpvpKEEYGQFYGGDCYIVLYTYQGGgkeehiLYFWQGRHSSQDERAAAALLTVELDEELKG-R 82

                         90       100
                 ....*....|....*....|
gi 706114291 370 HTQVQVLpESGETPLFKQFF 389
Cdd:cd11293   83 AVQVRVV-QGKEPPHFLALF 101
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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