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Conserved domains on  [gi|1694576778|ref|XP_029466979|]
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gelsolin isoform X2 [Rhinatrema bivittatum]

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; ...
 8-120 5.44e-59

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: 194.75  E-value: 5.44e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694576778   8 FQKAGKEPGLQIWRVEKMDLVAVPKNLYGDFFTGDAYLVLNTIKQRSGNLQYDLHFWLGDYCTQDESGAAAIFTVQMDDY 87
Cdd:cd11290     1 FEGVGQKPGLQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDPSGSLSYDIHYWLGKEASQDEAGAAAIKAVELDDY 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1694576778  88 LCGKPIQNREVQGYESSTFLGYFKSGIKYKAGG 120
Cdd:cd11290    81 LGGRPVQHREVQGHESEEFLSYFKKGIIYIEGG 113
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 623-721 1.97e-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: 179.42  E-value: 1.97e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694576778 623 PPRLFACSNKTGRFIIEEVPGEnTQDDLATDDVMLLDTWDQVFVWIGTEAQDEEKKEALASASKYIETDPANRDK-RTPI 701
Cdd:cd11291     1 KPRLFRCSNESGFFKVEEISDF-SQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYIETDPLGRSKpRTPI 79

                          90       100
                  ....*....|....*....|
gi 1694576778 702 AIVKQGFEPPTFTGWFLGWD 721
Cdd:cd11291    80 YLVKQGNEPPTFTGYFHAWD 99
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
 388-497 1.59e-48

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: 165.91  E-value: 1.59e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694576778 388 MVDDGSGKKEIWRIEGSAKVPVDIAHYGQFYGGDSYIILYNFKHGGKQGQIIYTWQGADSTPDEITTSAFLSAQLDETLG 467
Cdd:cd11293     1 MYDDGSGKVEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQGGGKEEHILYFWQGRHSSQDERAAAALLTVELDEELK 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 1694576778 468 GGPVqslgslsrsQVRVVQGKEPAHLMSMF 497
Cdd:cd11293    81 GRAV---------QVRVVQGKEPPHFLALF 101
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 244-344 1.97e-41

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: 146.24  E-value: 1.97e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694576778 244 RKLAKLYRVSNGSGAMSVSLVADEnPFTQSALNSGDCFILDHGSdgKIFVWKGKGANTEEKKVALKTATEFISKMGYPKQ 323
Cdd:cd11292     1 AEQKKLYKVSDASGKLKLTEVAEG-SLNQEMLDSEDCYILDCGS--EIFVWVGKGASLDERKAALKNAEEFLRKKKRPPY 77

                          90       100
                  ....*....|....*....|.
gi 1694576778 324 TQIQVLPESGETPLFKQFFKN 344
Cdd:cd11292    78 TQVTRVTEGGESALFKSKFAN 98
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 137-224 4.38e-40

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: 141.99  E-value: 4.38e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694576778 137 RLLQVKGRRLARAIEVPVTWESFNKGDCFILDLGDEIYQWCGSKSNRFEKLKATNISKGIRDNERSGRAKVYVMEEG--M 214
Cdd:cd11289     3 RLLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKVIVLDEGdtN 82

                          90
                  ....*....|
gi 1694576778 215 EREKMLEVMG 224
Cdd:cd11289    83 ESPEFWKVLG 92
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 519-607 1.22e-35

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: 129.66  E-value: 1.22e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694576778 519 AETRLFQVRASSSGCTRAIELEATASNLNSNDVFVLKTSAAAYVWVGQGSSAAEKRGAQALLSILGVQASS--IAEGRET 596
Cdd:cd11288     1 SPTRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVASFLKPKASLqeVAEGSEP 80

                          90
                  ....*....|.
gi 1694576778 597 DDFWAALGGKA 607
Cdd:cd11288    81 DEFWEALGGKS 91
 
Name Accession Description Interval E-value
gelsolin_S1_like cd11290
Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; ...
 8-120 5.44e-59

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: 194.75  E-value: 5.44e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694576778   8 FQKAGKEPGLQIWRVEKMDLVAVPKNLYGDFFTGDAYLVLNTIKQRSGNLQYDLHFWLGDYCTQDESGAAAIFTVQMDDY 87
Cdd:cd11290     1 FEGVGQKPGLQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDPSGSLSYDIHYWLGKEASQDEAGAAAIKAVELDDY 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1694576778  88 LCGKPIQNREVQGYESSTFLGYFKSGIKYKAGG 120
Cdd:cd11290    81 LGGRPVQHREVQGHESEEFLSYFKKGIIYIEGG 113
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 623-721 1.97e-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: 179.42  E-value: 1.97e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694576778 623 PPRLFACSNKTGRFIIEEVPGEnTQDDLATDDVMLLDTWDQVFVWIGTEAQDEEKKEALASASKYIETDPANRDK-RTPI 701
Cdd:cd11291     1 KPRLFRCSNESGFFKVEEISDF-SQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYIETDPLGRSKpRTPI 79

                          90       100
                  ....*....|....*....|
gi 1694576778 702 AIVKQGFEPPTFTGWFLGWD 721
Cdd:cd11291    80 YLVKQGNEPPTFTGYFHAWD 99
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
 388-497 1.59e-48

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: 165.91  E-value: 1.59e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694576778 388 MVDDGSGKKEIWRIEGSAKVPVDIAHYGQFYGGDSYIILYNFKHGGKQGQIIYTWQGADSTPDEITTSAFLSAQLDETLG 467
Cdd:cd11293     1 MYDDGSGKVEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQGGGKEEHILYFWQGRHSSQDERAAAALLTVELDEELK 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 1694576778 468 GGPVqslgslsrsQVRVVQGKEPAHLMSMF 497
Cdd:cd11293    81 GRAV---------QVRVVQGKEPPHFLALF 101
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 244-344 1.97e-41

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: 146.24  E-value: 1.97e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694576778 244 RKLAKLYRVSNGSGAMSVSLVADEnPFTQSALNSGDCFILDHGSdgKIFVWKGKGANTEEKKVALKTATEFISKMGYPKQ 323
Cdd:cd11292     1 AEQKKLYKVSDASGKLKLTEVAEG-SLNQEMLDSEDCYILDCGS--EIFVWVGKGASLDERKAALKNAEEFLRKKKRPPY 77

                          90       100
                  ....*....|....*....|.
gi 1694576778 324 TQIQVLPESGETPLFKQFFKN 344
Cdd:cd11292    78 TQVTRVTEGGESALFKSKFAN 98
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 137-224 4.38e-40

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: 141.99  E-value: 4.38e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694576778 137 RLLQVKGRRLARAIEVPVTWESFNKGDCFILDLGDEIYQWCGSKSNRFEKLKATNISKGIRDNERSGRAKVYVMEEG--M 214
Cdd:cd11289     3 RLLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKVIVLDEGdtN 82

                          90
                  ....*....|
gi 1694576778 215 EREKMLEVMG 224
Cdd:cd11289    83 ESPEFWKVLG 92
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 519-607 1.22e-35

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: 129.66  E-value: 1.22e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694576778 519 AETRLFQVRASSSGCTRAIELEATASNLNSNDVFVLKTSAAAYVWVGQGSSAAEKRGAQALLSILGVQASS--IAEGRET 596
Cdd:cd11288     1 SPTRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVASFLKPKASLqeVAEGSEP 80

                          90
                  ....*....|.
gi 1694576778 597 DDFWAALGGKA 607
Cdd:cd11288    81 DEFWEALGGKS 91
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 251-345 8.54e-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: 101.60  E-value: 8.54e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694576778  251 RVSNGSGamSVSLVADENPFTQSALNSGDCFILDHGSDgkIFVWKGKGANTEEKKVALKTATEFISKMGyPKQTQIQVLP 330
Cdd:smart00262   1 FLVRVKG--KRNVRVPEVPFSQGSLNSGDCYILDTGSE--IYVWVGKKSSQDEKKKAAELAVELDDTLG-PGPVQVRVVD 75

                           90
                   ....*....|....*
gi 1694576778  331 ESGETPLFKQFFKNW 345
Cdd:smart00262  76 EGKEPPEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 629-720 9.69e-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: 101.22  E-value: 9.69e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694576778  629 CSNKTGRFIIEEVPGENTQDDLATDDVMLLDTWDQVFVWIGTEAQDEEKKEALASASKYIETDpanRDKRTPIAIVKQGF 708
Cdd:smart00262   2 LVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTL---GPGPVQVRVVDEGK 78

                           90
                   ....*....|..
gi 1694576778  709 EPPTFTGWFLGW 720
Cdd:smart00262  79 EPPEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 137-226 1.25e-24

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 98.13  E-value: 1.25e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694576778  137 RLLQVKGRRLARAIEVPVTWESFNKGDCFILDLGDEIYQWCGSKSNRFEKLKATNISKGIRDNERSGRAKVYVMEEGMER 216
Cdd:smart00262   1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVRVVDEGKEP 80

                           90
                   ....*....|
gi 1694576778  217 EKMLEVMGDK 226
Cdd:smart00262  81 PEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 397-500 1.09e-20

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 86.96  E-value: 1.09e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694576778  397 EIWRIEGSAKVPVDI--AHYGQFYGGDSYIILYnfkhggkqGQIIYTWQGADSTPDEITTSAFLSAQLDETLGGGPVQsl 474
Cdd:smart00262   1 FLVRVKGKRNVRVPEvpFSQGSLNSGDCYILDT--------GSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQ-- 70

                           90       100
                   ....*....|....*....|....*.
gi 1694576778  475 gslsrsQVRVVQGKEPAHLMSMFDGK 500
Cdd:smart00262  71 ------VRVVDEGKEPPEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 524-606 3.05e-18

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 80.03  E-value: 3.05e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694576778  524 FQVRASSSGCTRAIELEATASNLNSNDVFVLKTSAAAYVWVGQGSSAAEKRGAQALLSIL-------GVQASSIAEGRET 596
Cdd:smart00262   1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELddtlgpgPVQVRVVDEGKEP 80

                           90
                   ....*....|
gi 1694576778  597 DDFWAALGGK 606
Cdd:smart00262  81 PEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 18-113 2.57e-17

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: 77.33  E-value: 2.57e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694576778   18 QIWRVEKMDLVAVP--KNLYGDFFTGDAYLVLNTikqrsgnlqYDLHFWLGDYCTQDESGAAAIFTVQMDDYLCGKPIQN 95
Cdd:smart00262   1 FLVRVKGKRNVRVPevPFSQGSLNSGDCYILDTG---------SEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQV 71

                           90
                   ....*....|....*....
gi 1694576778   96 REV-QGYESSTFLGYFKSG 113
Cdd:smart00262  72 RVVdEGKEPPEFWSLFGGW 90
Gelsolin pfam00626
Gelsolin repeat;
148-215 9.29e-17

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 75.42  E-value: 9.29e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1694576778 148 RAIEVPVTWESFNKGDCFILDLGDEIYQWCGSKSNRFEKLKATNISKGIRDNERSGRAKVYVMEEGME 215
Cdd:pfam00626   4 LPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDERFPLPEVIRVPQGKE 71
Gelsolin pfam00626
Gelsolin repeat;
261-339 5.80e-15

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 70.41  E-value: 5.80e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1694576778 261 VSLVADENPFTQSALNSGDCFILDHGSdgKIFVWKGKGANTEEKKVALKTATEFISKMGYPKqTQIQVLPESGETPLFK 339
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNGF--TIFLWVGKGSSLLEKLFAALLAAQLDDDERFPL-PEVIRVPQGKEPARFL 76
Gelsolin pfam00626
Gelsolin repeat;
636-713 3.70e-14

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 68.10  E-value: 3.70e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1694576778 636 FIIEEVPGENTQDDLATDDVMLLDTWDQVFVWIGTEAQDEEKKEALASASKYIETDpanRDKRTPIAIVKQGFEPPTF 713
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDE---RFPLPEVIRVPQGKEPARF 75
Gelsolin pfam00626
Gelsolin repeat;
24-107 4.92e-11

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 59.24  E-value: 4.92e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694576778  24 KMDLVAVPKNLYGDFFTGDAYLVLNTikqrsgnlqYDLHFWLGDYCTQDESGAAAIFTVQMDD-YLCGKPIQNREVQGYE 102
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNG---------FTIFLWVGKGSSLLEKLFAALLAAQLDDdERFPLPEVIRVPQGKE 71


                  ....*
gi 1694576778 103 SSTFL 107
Cdd:pfam00626  72 PARFL 76
Gelsolin pfam00626
Gelsolin repeat;
406-494 2.03e-10

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 57.32  E-value: 2.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694576778 406 KVPVDIAHYGQFYGGDSYIILynfkhggkQGQIIYTWQGADSTPDEITTSAFLSAQLDEtlgggpvQSLGSLSRsQVRVV 485
Cdd:pfam00626   4 LPPPVPLSQESLNSGDCYLLD--------NGFTIFLWVGKGSSLLEKLFAALLAAQLDD-------DERFPLPE-VIRVP 67


                  ....*....
gi 1694576778 486 QGKEPAHLM 494
Cdd:pfam00626  68 QGKEPARFL 76
Gelsolin pfam00626
Gelsolin repeat;
534-600 2.18e-04

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 40.37  E-value: 2.18e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1694576778 534 TRAIELEATASNLNSNDVFVLKTSAAAYVWVGQGSSAAEK-RGAQALLSILGVQASSIAE------GRETDDFW 600
Cdd:pfam00626   3 VLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKlFAALLAAQLDDDERFPLPEvirvpqGKEPARFL 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; ...
 8-120 5.44e-59

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: 194.75  E-value: 5.44e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694576778   8 FQKAGKEPGLQIWRVEKMDLVAVPKNLYGDFFTGDAYLVLNTIKQRSGNLQYDLHFWLGDYCTQDESGAAAIFTVQMDDY 87
Cdd:cd11290     1 FEGVGQKPGLQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDPSGSLSYDIHYWLGKEASQDEAGAAAIKAVELDDY 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1694576778  88 LCGKPIQNREVQGYESSTFLGYFKSGIKYKAGG 120
Cdd:cd11290    81 LGGRPVQHREVQGHESEEFLSYFKKGIIYIEGG 113
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 623-721 1.97e-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: 179.42  E-value: 1.97e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694576778 623 PPRLFACSNKTGRFIIEEVPGEnTQDDLATDDVMLLDTWDQVFVWIGTEAQDEEKKEALASASKYIETDPANRDK-RTPI 701
Cdd:cd11291     1 KPRLFRCSNESGFFKVEEISDF-SQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYIETDPLGRSKpRTPI 79

                          90       100
                  ....*....|....*....|
gi 1694576778 702 AIVKQGFEPPTFTGWFLGWD 721
Cdd:cd11291    80 YLVKQGNEPPTFTGYFHAWD 99
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
 388-497 1.59e-48

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: 165.91  E-value: 1.59e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694576778 388 MVDDGSGKKEIWRIEGSAKVPVDIAHYGQFYGGDSYIILYNFKHGGKQGQIIYTWQGADSTPDEITTSAFLSAQLDETLG 467
Cdd:cd11293     1 MYDDGSGKVEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQGGGKEEHILYFWQGRHSSQDERAAAALLTVELDEELK 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 1694576778 468 GGPVqslgslsrsQVRVVQGKEPAHLMSMF 497
Cdd:cd11293    81 GRAV---------QVRVVQGKEPPHFLALF 101
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 244-344 1.97e-41

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: 146.24  E-value: 1.97e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694576778 244 RKLAKLYRVSNGSGAMSVSLVADEnPFTQSALNSGDCFILDHGSdgKIFVWKGKGANTEEKKVALKTATEFISKMGYPKQ 323
Cdd:cd11292     1 AEQKKLYKVSDASGKLKLTEVAEG-SLNQEMLDSEDCYILDCGS--EIFVWVGKGASLDERKAALKNAEEFLRKKKRPPY 77

                          90       100
                  ....*....|....*....|.
gi 1694576778 324 TQIQVLPESGETPLFKQFFKN 344
Cdd:cd11292    78 TQVTRVTEGGESALFKSKFAN 98
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 137-224 4.38e-40

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: 141.99  E-value: 4.38e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694576778 137 RLLQVKGRRLARAIEVPVTWESFNKGDCFILDLGDEIYQWCGSKSNRFEKLKATNISKGIRDNERSGRAKVYVMEEG--M 214
Cdd:cd11289     3 RLLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKVIVLDEGdtN 82

                          90
                  ....*....|
gi 1694576778 215 EREKMLEVMG 224
Cdd:cd11289    83 ESPEFWKVLG 92
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 519-607 1.22e-35

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: 129.66  E-value: 1.22e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694576778 519 AETRLFQVRASSSGCTRAIELEATASNLNSNDVFVLKTSAAAYVWVGQGSSAAEKRGAQALLSILGVQASS--IAEGRET 596
Cdd:cd11288     1 SPTRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVASFLKPKASLqeVAEGSEP 80

                          90
                  ....*....|.
gi 1694576778 597 DDFWAALGGKA 607
Cdd:cd11288    81 DEFWEALGGKS 91
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 251-345 8.54e-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: 101.60  E-value: 8.54e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694576778  251 RVSNGSGamSVSLVADENPFTQSALNSGDCFILDHGSDgkIFVWKGKGANTEEKKVALKTATEFISKMGyPKQTQIQVLP 330
Cdd:smart00262   1 FLVRVKG--KRNVRVPEVPFSQGSLNSGDCYILDTGSE--IYVWVGKKSSQDEKKKAAELAVELDDTLG-PGPVQVRVVD 75

                           90
                   ....*....|....*
gi 1694576778  331 ESGETPLFKQFFKNW 345
Cdd:smart00262  76 EGKEPPEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 629-720 9.69e-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: 101.22  E-value: 9.69e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694576778  629 CSNKTGRFIIEEVPGENTQDDLATDDVMLLDTWDQVFVWIGTEAQDEEKKEALASASKYIETDpanRDKRTPIAIVKQGF 708
Cdd:smart00262   2 LVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTL---GPGPVQVRVVDEGK 78

                           90
                   ....*....|..
gi 1694576778  709 EPPTFTGWFLGW 720
Cdd:smart00262  79 EPPEFWSLFGGW 90
gelsolin_S1_like cd11290
Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; ...
 391-508 9.99e-25

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: 99.22  E-value: 9.99e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694576778 391 DGSGKKE---IWRIEGSAKVPVDIAHYGQFYGGDSYIILYNFKHG-GKQGQIIYTWQGADSTPDEITTSAFLSAQLDETL 466
Cdd:cd11290     2 EGVGQKPglqIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDPsGSLSYDIHYWLGKEASQDEAGAAAIKAVELDDYL 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1694576778 467 GGGPVqslgslsrsQVRVVQGKEPAHLMSMFdgKPLVVYRGG 508
Cdd:cd11290    82 GGRPV---------QHREVQGHESEEFLSYF--KKGIIYIEG 112
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 137-226 1.25e-24

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 98.13  E-value: 1.25e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694576778  137 RLLQVKGRRLARAIEVPVTWESFNKGDCFILDLGDEIYQWCGSKSNRFEKLKATNISKGIRDNERSGRAKVYVMEEGMER 216
Cdd:smart00262   1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVRVVDEGKEP 80

                           90
                   ....*....|
gi 1694576778  217 EKMLEVMGDK 226
Cdd:smart00262  81 PEFWSLFGGW 90
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
 17-110 3.69e-24

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: 97.34  E-value: 3.69e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694576778  17 LQIWRVEKMDLVAVPKNLYGDFFTGDAYLVLNTIkQRSGNLQYDLHFWLGDYCTQDESGAAAIFTVQMDDYLCGKPIQNR 96
Cdd:cd11293     9 VEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTY-QGGGKEEHILYFWQGRHSSQDERAAAALLTVELDEELKGRAVQVR 87

                          90
                  ....*....|....
gi 1694576778  97 EVQGYESSTFLGYF 110
Cdd:cd11293    88 VVQGKEPPHFLALF 101
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 397-500 1.09e-20

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 86.96  E-value: 1.09e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694576778  397 EIWRIEGSAKVPVDI--AHYGQFYGGDSYIILYnfkhggkqGQIIYTWQGADSTPDEITTSAFLSAQLDETLGGGPVQsl 474
Cdd:smart00262   1 FLVRVKGKRNVRVPEvpFSQGSLNSGDCYILDT--------GSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQ-- 70

                           90       100
                   ....*....|....*....|....*.
gi 1694576778  475 gslsrsQVRVVQGKEPAHLMSMFDGK 500
Cdd:smart00262  71 ------VRVVDEGKEPPEFWSLFGGW 90
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 248-345 1.87e-19

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: 83.89  E-value: 1.87e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694576778 248 KLYRVSNGSGAmsvsLVADE-NPFTQSALNSGDCFILDHGSdgKIFVWKGKGANTEEKKVALKTATEFISKMG---YPKQ 323
Cdd:cd11291     3 RLFRCSNESGF----FKVEEiSDFSQDDLDTDDIMLLDTGD--EVFVWVGSESSDEEKKEALTSAKKYIETDPlgrSKPR 76

                          90       100
                  ....*....|....*....|..
gi 1694576778 324 TQIQVLPESGETPLFKQFFKNW 345
Cdd:cd11291    77 TPIYLVKQGNEPPTFTGYFHAW 98
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 524-606 3.05e-18

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 80.03  E-value: 3.05e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694576778  524 FQVRASSSGCTRAIELEATASNLNSNDVFVLKTSAAAYVWVGQGSSAAEKRGAQALLSIL-------GVQASSIAEGRET 596
Cdd:smart00262   1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELddtlgpgPVQVRVVDEGKEP 80

                           90
                   ....*....|
gi 1694576778  597 DDFWAALGGK 606
Cdd:smart00262  81 PEFWSLFGGW 90
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 624-717 5.18e-18

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: 79.60  E-value: 5.18e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694576778 624 PRLFACSNKTGRFIIEEVPGEN-TQDDLATDDVMLLDTWDQVFVWIGTEAQDEEKKEALASASKYIETDpaNRDKRTPIA 702
Cdd:cd11292     4 KKLYKVSDASGKLKLTEVAEGSlNQEMLDSEDCYILDCGSEIFVWVGKGASLDERKAALKNAEEFLRKK--KRPPYTQVT 81

                          90
                  ....*....|....*
gi 1694576778 703 IVKQGFEPPTFTGWF 717
Cdd:cd11292    82 RVTEGGESALFKSKF 96
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 18-113 2.57e-17

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: 77.33  E-value: 2.57e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694576778   18 QIWRVEKMDLVAVP--KNLYGDFFTGDAYLVLNTikqrsgnlqYDLHFWLGDYCTQDESGAAAIFTVQMDDYLCGKPIQN 95
Cdd:smart00262   1 FLVRVKGKRNVRVPevPFSQGSLNSGDCYILDTG---------SEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQV 71

                           90
                   ....*....|....*....
gi 1694576778   96 REV-QGYESSTFLGYFKSG 113
Cdd:smart00262  72 RVVdEGKEPPEFWSLFGGW 90
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 623-717 5.13e-17

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


Pssm-ID: 200436  Cd Length: 88  Bit Score: 76.64  E-value: 5.13e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694576778 623 PPRLFACSNKTgRFIIEEVPGENTqdDLATDDVMLLDTWDQVFVWIGTEAQDEEKKEALASASKYIETdpanRDKRTPIA 702
Cdd:cd11280     1 PPRLYRVRGSK-AIEIEEVPLASS--SLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKELDEE----RKGKPEIV 73

                          90
                  ....*....|....*
gi 1694576778 703 IVKQGFEPPTFTGWF 717
Cdd:cd11280    74 RIRQGQEPREFWSLF 88
Gelsolin pfam00626
Gelsolin repeat;
148-215 9.29e-17

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 75.42  E-value: 9.29e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1694576778 148 RAIEVPVTWESFNKGDCFILDLGDEIYQWCGSKSNRFEKLKATNISKGIRDNERSGRAKVYVMEEGME 215
Cdd:pfam00626   4 LPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDERFPLPEVIRVPQGKE 71
Gelsolin pfam00626
Gelsolin repeat;
261-339 5.80e-15

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 70.41  E-value: 5.80e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1694576778 261 VSLVADENPFTQSALNSGDCFILDHGSdgKIFVWKGKGANTEEKKVALKTATEFISKMGYPKqTQIQVLPESGETPLFK 339
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNGF--TIFLWVGKGSSLLEKLFAALLAAQLDDDERFPL-PEVIRVPQGKEPARFL 76
Gelsolin pfam00626
Gelsolin repeat;
636-713 3.70e-14

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 68.10  E-value: 3.70e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1694576778 636 FIIEEVPGENTQDDLATDDVMLLDTWDQVFVWIGTEAQDEEKKEALASASKYIETDpanRDKRTPIAIVKQGFEPPTF 713
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDE---RFPLPEVIRVPQGKEPARF 75
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 249-342 5.85e-12

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


Pssm-ID: 200436  Cd Length: 88  Bit Score: 62.00  E-value: 5.85e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694576778 249 LYRVSnGSGAMSVSLVADENpftqSALNSGDCFILDHGSDgkIFVWKGKGANTEEKKVALKTATEFiSKMGYPKqTQIQV 328
Cdd:cd11280     4 LYRVR-GSKAIEIEEVPLAS----SSLDSDDVFVLDTGSE--IYIWQGRASSQAELAAAALLAKEL-DEERKGK-PEIVR 74

                          90
                  ....*....|....
gi 1694576778 329 LPESGETPLFKQFF 342
Cdd:cd11280    75 IRQGQEPREFWSLF 88
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 398-497 2.04e-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: 60.46  E-value: 2.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694576778 398 IWRIEGSA---KVPVDIAHYgQFYGGDSYIILYnfkhggkqGQIIYTWQGADSTPDEITTSAFLSAQLDETLGGGPVqsl 474
Cdd:cd11280     4 LYRVRGSKaieIEEVPLASS-SLDSDDVFVLDT--------GSEIYIWQGRASSQAELAAAALLAKELDEERKGKPE--- 71

                          90       100
                  ....*....|....*....|...
gi 1694576778 475 gslsrsQVRVVQGKEPAHLMSMF 497
Cdd:cd11280    72 ------IVRIRQGQEPREFWSLF 88
Gelsolin pfam00626
Gelsolin repeat;
24-107 4.92e-11

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 59.24  E-value: 4.92e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694576778  24 KMDLVAVPKNLYGDFFTGDAYLVLNTikqrsgnlqYDLHFWLGDYCTQDESGAAAIFTVQMDD-YLCGKPIQNREVQGYE 102
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNG---------FTIFLWVGKGSSLLEKLFAALLAAQLDDdERFPLPEVIRVPQGKE 71


                  ....*
gi 1694576778 103 SSTFL 107
Cdd:pfam00626  72 PARFL 76
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 136-223 5.15e-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: 59.30  E-value: 5.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694576778 136 RRLLQVKGRRLARAIEVPVTWESFNKGDCFILDLGDEIYQWCGSKSNRFEKLKATNISKGIrDNERSGRAKVYVMEEGME 215
Cdd:cd11280     2 PRLYRVRGSKAIEIEEVPLASSSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKEL-DEERKGKPEIVRIRQGQE 80


                  ....*...
gi 1694576778 216 REKMLEVM 223
Cdd:cd11280    81 PREFWSLF 88
Gelsolin pfam00626
Gelsolin repeat;
406-494 2.03e-10

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 57.32  E-value: 2.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694576778 406 KVPVDIAHYGQFYGGDSYIILynfkhggkQGQIIYTWQGADSTPDEITTSAFLSAQLDEtlgggpvQSLGSLSRsQVRVV 485
Cdd:pfam00626   4 LPPPVPLSQESLNSGDCYLLD--------NGFTIFLWVGKGSSLLEKLFAALLAAQLDD-------DERFPLPE-VIRVP 67


                  ....*....
gi 1694576778 486 QGKEPAHLM 494
Cdd:pfam00626  68 QGKEPARFL 76
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 247-338 2.37e-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: 57.63  E-value: 2.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694576778 247 AKLYRV-SNGSG---AMSVSLVAdenpftqSALNSGDCFILDHGSdgKIFVWKGKGANTEEKKVALKTATEFISKmgypk 322
Cdd:cd11288     3 TRLFQVrGNGSGntrAVEVDADA-------SSLNSNDVFVLKTPS--SVYLWVGKGSSEDERELAKDVASFLKPK----- 68

                          90
                  ....*....|....*.
gi 1694576778 323 qTQIQVLPESGETPLF 338
Cdd:cd11288    69 -ASLQEVAEGSEPDEF 83
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 247-343 7.61e-10

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: 56.09  E-value: 7.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694576778 247 AKLYRVSnGSGAMSVSLVadenPFTQSALNSGDCFILDHGSdgKIFVWKGKGANTEEKKVALKTATEFISKMGYPKqTQI 326
Cdd:cd11289     2 PRLLHVK-GRRNVRAREV----ELSWSSLNSGDVFILDLGS--TIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGR-AKV 73

                          90
                  ....*....|....*..
gi 1694576778 327 QVLpESGETPLFKQFFK 343
Cdd:cd11289    74 IVL-DEGDTNESPEFWK 89
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 521-603 8.72e-10

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


Pssm-ID: 200436  Cd Length: 88  Bit Score: 55.84  E-value: 8.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694576778 521 TRLFQVRASSSgcTRAIELEATASNLNSNDVFVLKTSAAAYVWVGQGSSAAEKRGAQALLSILGVQASS------IAEGR 594
Cdd:cd11280     2 PRLYRVRGSKA--IEIEEVPLASSSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKELDEERKGkpeivrIRQGQ 79


                  ....*....
gi 1694576778 595 ETDDFWAAL 603
Cdd:cd11280    80 EPREFWSLF 88
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 18-110 5.79e-09

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: 53.53  E-value: 5.79e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694576778  18 QIWRVEK---MDLVAVPKNLYgDFFTGDAYLVLntikqrsgnLQYDLHFWLGDYCTQDESGAAAIFTVQMDDYLCGKPIQ 94
Cdd:cd11280     3 RLYRVRGskaIEIEEVPLASS-SLDSDDVFVLD---------TGSEIYIWQGRASSQAELAAAALLAKELDEERKGKPEI 72

                          90
                  ....*....|....*.
gi 1694576778  95 NREVQGYESSTFLGYF 110
Cdd:cd11280    73 VRIRQGQEPREFWSLF 88
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 520-604 2.57e-08

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: 51.85  E-value: 2.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694576778 520 ETRLFQVRASSSgcTRAIELEATASNLNSNDVFVLKTSAAAYVWVGQGSSAAEK-RGAQALLSI-----LG---VQASSI 590
Cdd:cd11289     1 KPRLLHVKGRRN--VRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKaKAMQLAQGIrderrLGrakVIVLDE 78

                          90
                  ....*....|....
gi 1694576778 591 AEGRETDDFWAALG 604
Cdd:cd11289    79 GDTNESPEFWKVLG 92
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 160-215 7.94e-07

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: 47.68  E-value: 7.94e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694576778 160 NKGDCFILDLGDEIYQWCGSKSNRFEKLKATNISKGIRDNERSGR----AKVYVMEEGME 215
Cdd:cd11291    28 DTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYIETDPLGRskprTPIYLVKQGNE 87
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 137-226 3.75e-06

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


Pssm-ID: 200444  Cd Length: 92  Bit Score: 45.69  E-value: 3.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694576778 137 RLLQVKG--RRLARAIEVPVTWESFNKGDCFILDLGDEIYQWCGSKSNRFEKLKATNISKGIRDnersgRAKVYVMEEGM 214
Cdd:cd11288     4 RLFQVRGngSGNTRAVEVDADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVASFLKP-----KASLQEVAEGS 78

                          90
                  ....*....|..
gi 1694576778 215 EREKMLEVMGDK 226
Cdd:cd11288    79 EPDEFWEALGGK 90
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 518-579 4.03e-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: 43.01  E-value: 4.03e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1694576778 518 PAETRLFQVR-ASSSGCTRAIEL-EATASNLNSNDVFVLKTSAAAYVWVGQGSSAAEKRGAQAL 579
Cdd:cd11292     1 AEQKKLYKVSdASGKLKLTEVAEgSLNQEMLDSEDCYILDCGSEIFVWVGKGASLDERKAALKN 64
Gelsolin pfam00626
Gelsolin repeat;
534-600 2.18e-04

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 40.37  E-value: 2.18e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1694576778 534 TRAIELEATASNLNSNDVFVLKTSAAAYVWVGQGSSAAEK-RGAQALLSILGVQASSIAE------GRETDDFW 600
Cdd:pfam00626   3 VLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKlFAALLAAQLDDDERFPLPEvirvpqGKEPARFL 76
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 623-720 9.14e-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: 36.06  E-value: 9.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694576778 623 PPRLFACSNKtgRFI-IEEVPgeNTQDDLATDDVMLLDTWDQVFVWIGTEAQDEEKKEALASAsKYIETDpaNRDKRTPI 701
Cdd:cd11289     1 KPRLLHVKGR--RNVrAREVE--LSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLA-QGIRDE--RRLGRAKV 73

                          90
                  ....*....|....*....
gi 1694576778 702 AIVKQGFEPPTFTGWFLGW 720
Cdd:cd11289    74 IVLDEGDTNESPEFWKVLG 92
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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