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Conserved domains on  [gi|136255943|ref|NP_835232|]
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scinderin like a [Danio rerio]

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; ...
 7-115 2.00e-56

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: 187.82  E-value: 2.00e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 136255943   7 FQNAGKEPGLQIWRIEKMDLKLVPKQLHGNFFTGDAYVVLFTSP----APSYNVHMWLGNECSQDESGAAAIFAMQLDDH 82
Cdd:cd11290    1 FEGVGQKPGLQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLdpsgSLSYDIHYWLGKEASQDEAGAAAIKAVELDDY 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 136255943  83 LGGAPVQYREVQNNESVTFLGYFKTGIKYKQGG 115
Cdd:cd11290   81 LGGRPVQHREVQGHESEEFLSYFKKGIIYIEGG 113
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
 383-483 1.65e-54

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: 182.09  E-value: 1.65e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 136255943 383 MVDDGSGKVQVWRVEGNDRVPVDPSSFGQFFGGDCYLILYTYLNGGREQHIIYTWQGLKCTQDELTASAFLTVKLDDSMG 462
Cdd:cd11293    1 MYDDGSGKVEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQGGGKEEHILYFWQGRHSSQDERAAAALLTVELDEELK 80

                         90       100
                 ....*....|....*....|.
gi 136255943 463 GAPVQVRVTQGQEPAHLMSLF 483
Cdd:cd11293   81 GRAVQVRVVQGKEPPHFLALF 101
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 608-704 1.30e-41

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: 146.67  E-value: 1.30e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 136255943 608 PRLFGCSNKTGRLIAEEVPgDLTQSDLATDDVMLLDTWDQIFLWIGNDANVEEKIGSAKIAKDYVDSDPSKR--QGIPII 685
Cdd:cd11291    2 PRLFRCSNESGFFKVEEIS-DFSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYIETDPLGRskPRTPIY 80

                         90
                 ....*....|....*....
gi 136255943 686 TIKQGFEPPSFTGWFQAWD 704
Cdd:cd11291   81 LVKQGNEPPTFTGYFHAWD 99
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 131-212 3.72e-41

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: 145.07  E-value: 3.72e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 136255943 131 KRVLHIKGRRAIRATEVNMSWASFNHGDCFILDLGKDIYQWCGSKCNRFERLKASEVSIGIRDNERNGRATLHIVEDGSE 210
Cdd:cd11289    2 PRLLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKVIVLDEGDT 81


                 ..
gi 136255943 211 PD 212
Cdd:cd11289   82 NE 83
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 239-339 1.53e-37

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: 135.07  E-value: 1.53e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 136255943 239 QKKASLHMVSDAAGSMKTSEVKQnSPFKQELLNPSDCYILDNGldSKIFVWKGPRANTEERKSAMKVAEQFIKEKNYPKN 318
Cdd:cd11292    1 AEQKKLYKVSDASGKLKLTEVAE-GSLNQEMLDSEDCYILDCG--SEIFVWVGKGASLDERKAALKNAEEFLRKKKRPPY 77

                         90       100
                 ....*....|....*....|.
gi 136255943 319 TQIQVMPGGGETTLFKQFFSN 339
Cdd:cd11292   78 TQVTRVTEGGESALFKSKFAN 98
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 506-594 4.87e-37

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: 133.51  E-value: 4.87e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 136255943 506 TTRLFHIRQSSTRATRAVEVEPCASKLNTNDVFVLKFPEGMFLWKGVGASEEEIAAAKYVCSILGGSA--TEISEGKEPA 583
Cdd:cd11288    2 PTRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVASFLKPKAslQEVAEGSEPD 81

                         90
                 ....*....|.
gi 136255943 584 AFWSSLGGKKD 594
Cdd:cd11288   82 EFWEALGGKSE 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; ...
 7-115 2.00e-56

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: 187.82  E-value: 2.00e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 136255943   7 FQNAGKEPGLQIWRIEKMDLKLVPKQLHGNFFTGDAYVVLFTSP----APSYNVHMWLGNECSQDESGAAAIFAMQLDDH 82
Cdd:cd11290    1 FEGVGQKPGLQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLdpsgSLSYDIHYWLGKEASQDEAGAAAIKAVELDDY 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 136255943  83 LGGAPVQYREVQNNESVTFLGYFKTGIKYKQGG 115
Cdd:cd11290   81 LGGRPVQHREVQGHESEEFLSYFKKGIIYIEGG 113
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
 383-483 1.65e-54

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: 182.09  E-value: 1.65e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 136255943 383 MVDDGSGKVQVWRVEGNDRVPVDPSSFGQFFGGDCYLILYTYLNGGREQHIIYTWQGLKCTQDELTASAFLTVKLDDSMG 462
Cdd:cd11293    1 MYDDGSGKVEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQGGGKEEHILYFWQGRHSSQDERAAAALLTVELDEELK 80

                         90       100
                 ....*....|....*....|.
gi 136255943 463 GAPVQVRVTQGQEPAHLMSLF 483
Cdd:cd11293   81 GRAVQVRVVQGKEPPHFLALF 101
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 608-704 1.30e-41

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: 146.67  E-value: 1.30e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 136255943 608 PRLFGCSNKTGRLIAEEVPgDLTQSDLATDDVMLLDTWDQIFLWIGNDANVEEKIGSAKIAKDYVDSDPSKR--QGIPII 685
Cdd:cd11291    2 PRLFRCSNESGFFKVEEIS-DFSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYIETDPLGRskPRTPIY 80

                         90
                 ....*....|....*....
gi 136255943 686 TIKQGFEPPSFTGWFQAWD 704
Cdd:cd11291   81 LVKQGNEPPTFTGYFHAWD 99
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 131-212 3.72e-41

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: 145.07  E-value: 3.72e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 136255943 131 KRVLHIKGRRAIRATEVNMSWASFNHGDCFILDLGKDIYQWCGSKCNRFERLKASEVSIGIRDNERNGRATLHIVEDGSE 210
Cdd:cd11289    2 PRLLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKVIVLDEGDT 81


                 ..
gi 136255943 211 PD 212
Cdd:cd11289   82 NE 83
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 239-339 1.53e-37

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: 135.07  E-value: 1.53e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 136255943 239 QKKASLHMVSDAAGSMKTSEVKQnSPFKQELLNPSDCYILDNGldSKIFVWKGPRANTEERKSAMKVAEQFIKEKNYPKN 318
Cdd:cd11292    1 AEQKKLYKVSDASGKLKLTEVAE-GSLNQEMLDSEDCYILDCG--SEIFVWVGKGASLDERKAALKNAEEFLRKKKRPPY 77

                         90       100
                 ....*....|....*....|.
gi 136255943 319 TQIQVMPGGGETTLFKQFFSN 339
Cdd:cd11292   78 TQVTRVTEGGESALFKSKFAN 98
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 506-594 4.87e-37

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: 133.51  E-value: 4.87e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 136255943 506 TTRLFHIRQSSTRATRAVEVEPCASKLNTNDVFVLKFPEGMFLWKGVGASEEEIAAAKYVCSILGGSA--TEISEGKEPA 583
Cdd:cd11288    2 PTRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVASFLKPKAslQEVAEGSEPD 81

                         90
                 ....*....|.
gi 136255943 584 AFWSSLGGKKD 594
Cdd:cd11288   82 EFWEALGGKSE 92
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 132-221 1.84e-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: 103.53  E-value: 1.84e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 136255943   132 RVLHIKGRRAIRATEVNMSWASFNHGDCFILDLGKDIYQWCGSKCNRFERLKASEVSIGIRDNERNGRATLHIVEDGSEP 211
Cdd:smart00262   1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVRVVDEGKEP 80

                           90
                   ....*....|
gi 136255943   212 DVFSNTLGPK 221
Cdd:smart00262  81 PEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 392-486 5.38e-24

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 96.21  E-value: 5.38e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 136255943   392 QVWRVEGNDRVPVDPSSF--GQFFGGDCYLILYTylnggreqHIIYTWQGLKCTQDELTASAFLTVKLDDSMGGAPVQVR 469
Cdd:smart00262   1 FLVRVKGKRNVRVPEVPFsqGSLNSGDCYILDTG--------SEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVR 72

                           90
                   ....*....|....*...
gi 136255943   470 -VTQGQEPAHLMSLFKGK 486
Cdd:smart00262  73 vVDEGKEPPEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 613-703 5.71e-24

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 96.21  E-value: 5.71e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 136255943   613 CSNKTGRLIAEEVPGDLTQSDLATDDVMLLDTWDQIFLWIGNDANVEEKIGSAKIAKDYVDSDPSKRQgiPIITIKQGFE 692
Cdd:smart00262   2 LVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPV--QVRVVDEGKE 79

                           90
                   ....*....|.
gi 136255943   693 PPSFTGWFQAW 703
Cdd:smart00262  80 PPEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 263-340 1.38e-21

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 89.66  E-value: 1.38e-21
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 136255943   263 SPFKQELLNPSDCYILDNGldSKIFVWKGPRANTEERKSAMKVAEQFIKEKNyPKNTQIQVMPGGGETTLFKQFFSNW 340
Cdd:smart00262  16 VPFSQGSLNSGDCYILDTG--SEIYVWVGKKSSQDEKKKAAELAVELDDTLG-PGPVQVRVVDEGKEPPEFWSLFGGW 90
Gelsolin pfam00626
Gelsolin repeat;
140-214 2.71e-18

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 79.66  E-value: 2.71e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 136255943  140 RAIRATEVNMSWASFNHGDCFILDLGKDIYQWCGSKCNRFERLKASEVSIGIRDNERNGRATLHIVEDGSEPDVF 214
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDERFPLPEVIRVPQGKEPARF 75
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 510-592 5.76e-18

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 79.26  E-value: 5.76e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 136255943   510 FHIRQSSTRATRAVEVEPCASKLNTNDVFVLKFPEGMFLWKGVGASEEEIAAAKYVCSIL----GGSAT---EISEGKEP 582
Cdd:smart00262   1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELddtlGPGPVqvrVVDEGKEP 80

                           90
                   ....*....|
gi 136255943   583 AAFWSSLGGK 592
Cdd:smart00262  81 PEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 17-108 3.19e-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: 76.95  E-value: 3.19e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 136255943    17 QIWRIEKMDLKLVP--KQLHGNFFTGDAYVVLFTSpapsyNVHMWLGNECSQDESGAAAIFAMQLDDHLGGAPVQYREV- 93
Cdd:smart00262   1 FLVRVKGKRNVRVPevPFSQGSLNSGDCYILDTGS-----EIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVRVVd 75

                           90
                   ....*....|....*
gi 136255943    94 QNNESVTFLGYFKTG 108
Cdd:smart00262  76 EGKEPPEFWSLFGGW 90
Gelsolin pfam00626
Gelsolin repeat;
623-696 1.93e-15

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 71.57  E-value: 1.93e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 136255943  623 EEVPGDLTQSDLATDDVMLLDTWDQIFLWIGNDANVEEKIGSAKIAKDYvdsDPSKRQGIP-IITIKQGFEPPSF 696
Cdd:pfam00626   4 LPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQL---DDDERFPLPeVIRVPQGKEPARF 75
Gelsolin pfam00626
Gelsolin repeat;
398-480 1.60e-13

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 66.18  E-value: 1.60e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 136255943  398 GNDRVPVDPSSFGQFFGGDCYLILYTYlnggreqhIIYTWQGLKCTQDELTASAFLTVKLDDSM-GGAPVQVRVTQGQEP 476
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNGF--------TIFLWVGKGSSLLEKLFAALLAAQLDDDErFPLPEVIRVPQGKEP 72


                  ....
gi 136255943  477 AHLM 480
Cdd:pfam00626  73 ARFL 76
Gelsolin pfam00626
Gelsolin repeat;
264-334 2.14e-13

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 65.79  E-value: 2.14e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 136255943  264 PFKQELLNPSDCYILDNGldSKIFVWKGPRANTEERKSAMKVAEQFIKEKNYPKnTQIQVMPGGGETTLFK 334
Cdd:pfam00626   9 PLSQESLNSGDCYLLDNG--FTIFLWVGKGSSLLEKLFAALLAAQLDDDERFPL-PEVIRVPQGKEPARFL 76
Gelsolin pfam00626
Gelsolin repeat;
34-102 1.75e-10

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 57.32  E-value: 1.75e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 136255943   34 HGNFFTGDAYVVLFTspapsYNVHMWLGNECSQDESGAAAIFAMQLDD-HLGGAPVQYREVQNNESVTFL 102
Cdd:pfam00626  12 QESLNSGDCYLLDNG-----FTIFLWVGKGSSLLEKLFAALLAAQLDDdERFPLPEVIRVPQGKEPARFL 76
Gelsolin pfam00626
Gelsolin repeat;
518-586 1.32e-04

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 40.75  E-value: 1.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 136255943  518 RATRAVEVEPCASKLNTNDVFVLKFPEGMFLWKGVGASEEEIAAAKYvcsilggSATEIS--------------EGKEPA 583
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAAL-------LAAQLDdderfplpevirvpQGKEPA 73


                  ...
gi 136255943  584 AFW 586
Cdd:pfam00626  74 RFL 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; ...
 7-115 2.00e-56

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: 187.82  E-value: 2.00e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 136255943   7 FQNAGKEPGLQIWRIEKMDLKLVPKQLHGNFFTGDAYVVLFTSP----APSYNVHMWLGNECSQDESGAAAIFAMQLDDH 82
Cdd:cd11290    1 FEGVGQKPGLQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLdpsgSLSYDIHYWLGKEASQDEAGAAAIKAVELDDY 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 136255943  83 LGGAPVQYREVQNNESVTFLGYFKTGIKYKQGG 115
Cdd:cd11290   81 LGGRPVQHREVQGHESEEFLSYFKKGIIYIEGG 113
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
 383-483 1.65e-54

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: 182.09  E-value: 1.65e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 136255943 383 MVDDGSGKVQVWRVEGNDRVPVDPSSFGQFFGGDCYLILYTYLNGGREQHIIYTWQGLKCTQDELTASAFLTVKLDDSMG 462
Cdd:cd11293    1 MYDDGSGKVEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQGGGKEEHILYFWQGRHSSQDERAAAALLTVELDEELK 80

                         90       100
                 ....*....|....*....|.
gi 136255943 463 GAPVQVRVTQGQEPAHLMSLF 483
Cdd:cd11293   81 GRAVQVRVVQGKEPPHFLALF 101
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 608-704 1.30e-41

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: 146.67  E-value: 1.30e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 136255943 608 PRLFGCSNKTGRLIAEEVPgDLTQSDLATDDVMLLDTWDQIFLWIGNDANVEEKIGSAKIAKDYVDSDPSKR--QGIPII 685
Cdd:cd11291    2 PRLFRCSNESGFFKVEEIS-DFSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYIETDPLGRskPRTPIY 80

                         90
                 ....*....|....*....
gi 136255943 686 TIKQGFEPPSFTGWFQAWD 704
Cdd:cd11291   81 LVKQGNEPPTFTGYFHAWD 99
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 131-212 3.72e-41

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: 145.07  E-value: 3.72e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 136255943 131 KRVLHIKGRRAIRATEVNMSWASFNHGDCFILDLGKDIYQWCGSKCNRFERLKASEVSIGIRDNERNGRATLHIVEDGSE 210
Cdd:cd11289    2 PRLLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKVIVLDEGDT 81


                 ..
gi 136255943 211 PD 212
Cdd:cd11289   82 NE 83
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 239-339 1.53e-37

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: 135.07  E-value: 1.53e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 136255943 239 QKKASLHMVSDAAGSMKTSEVKQnSPFKQELLNPSDCYILDNGldSKIFVWKGPRANTEERKSAMKVAEQFIKEKNYPKN 318
Cdd:cd11292    1 AEQKKLYKVSDASGKLKLTEVAE-GSLNQEMLDSEDCYILDCG--SEIFVWVGKGASLDERKAALKNAEEFLRKKKRPPY 77

                         90       100
                 ....*....|....*....|.
gi 136255943 319 TQIQVMPGGGETTLFKQFFSN 339
Cdd:cd11292   78 TQVTRVTEGGESALFKSKFAN 98
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 506-594 4.87e-37

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: 133.51  E-value: 4.87e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 136255943 506 TTRLFHIRQSSTRATRAVEVEPCASKLNTNDVFVLKFPEGMFLWKGVGASEEEIAAAKYVCSILGGSA--TEISEGKEPA 583
Cdd:cd11288    2 PTRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVASFLKPKAslQEVAEGSEPD 81

                         90
                 ....*....|.
gi 136255943 584 AFWSSLGGKKD 594
Cdd:cd11288   82 EFWEALGGKSE 92
gelsolin_S1_like cd11290
Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; ...
 391-494 5.84e-29

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: 111.55  E-value: 5.84e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 136255943 391 VQVWRVEGNDRVPVDPSSFGQFFGGDCYLILYTYLNG-GREQHIIYTWQGLKCTQDELTASAFLTVKLDDSMGGAPVQVR 469
Cdd:cd11290   10 LQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDPsGSLSYDIHYWLGKEASQDEAGAAAIKAVELDDYLGGRPVQHR 89

                         90       100
                 ....*....|....*....|....*
gi 136255943 470 VTQGQEPAHLMSLFkgKPMIIHLGG 494
Cdd:cd11290   90 EVQGHESEEFLSYF--KKGIIYIEG 112
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 132-221 1.84e-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: 103.53  E-value: 1.84e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 136255943   132 RVLHIKGRRAIRATEVNMSWASFNHGDCFILDLGKDIYQWCGSKCNRFERLKASEVSIGIRDNERNGRATLHIVEDGSEP 211
Cdd:smart00262   1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVRVVDEGKEP 80

                           90
                   ....*....|
gi 136255943   212 DVFSNTLGPK 221
Cdd:smart00262  81 PEFWSLFGGW 90
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
 16-105 1.48e-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: 98.50  E-value: 1.48e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 136255943  16 LQIWRIEKMDLKLVPKQLHGNFFTGDAYVVLFT---SPAPSYNVHMWLGNECSQDESGAAAIFAMQLDDHLGGAPVQYRE 92
Cdd:cd11293    9 VEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTyqgGGKEEHILYFWQGRHSSQDERAAAALLTVELDEELKGRAVQVRV 88

                         90
                 ....*....|...
gi 136255943  93 VQNNESVTFLGYF 105
Cdd:cd11293   89 VQGKEPPHFLALF 101
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 392-486 5.38e-24

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 96.21  E-value: 5.38e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 136255943   392 QVWRVEGNDRVPVDPSSF--GQFFGGDCYLILYTylnggreqHIIYTWQGLKCTQDELTASAFLTVKLDDSMGGAPVQVR 469
Cdd:smart00262   1 FLVRVKGKRNVRVPEVPFsqGSLNSGDCYILDTG--------SEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVR 72

                           90
                   ....*....|....*...
gi 136255943   470 -VTQGQEPAHLMSLFKGK 486
Cdd:smart00262  73 vVDEGKEPPEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 613-703 5.71e-24

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 96.21  E-value: 5.71e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 136255943   613 CSNKTGRLIAEEVPGDLTQSDLATDDVMLLDTWDQIFLWIGNDANVEEKIGSAKIAKDYVDSDPSKRQgiPIITIKQGFE 692
Cdd:smart00262   2 LVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPV--QVRVVDEGKE 79

                           90
                   ....*....|.
gi 136255943   693 PPSFTGWFQAW 703
Cdd:smart00262  80 PPEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 263-340 1.38e-21

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 89.66  E-value: 1.38e-21
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 136255943   263 SPFKQELLNPSDCYILDNGldSKIFVWKGPRANTEERKSAMKVAEQFIKEKNyPKNTQIQVMPGGGETTLFKQFFSNW 340
Cdd:smart00262  16 VPFSQGSLNSGDCYILDTG--SEIYVWVGKKSSQDEKKKAAELAVELDDTLG-PGPVQVRVVDEGKEPPEFWSLFGGW 90
Gelsolin pfam00626
Gelsolin repeat;
140-214 2.71e-18

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 79.66  E-value: 2.71e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 136255943  140 RAIRATEVNMSWASFNHGDCFILDLGKDIYQWCGSKCNRFERLKASEVSIGIRDNERNGRATLHIVEDGSEPDVF 214
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDERFPLPEVIRVPQGKEPARF 75
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 510-592 5.76e-18

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 79.26  E-value: 5.76e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 136255943   510 FHIRQSSTRATRAVEVEPCASKLNTNDVFVLKFPEGMFLWKGVGASEEEIAAAKYVCSIL----GGSAT---EISEGKEP 582
Cdd:smart00262   1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELddtlGPGPVqvrVVDEGKEP 80

                           90
                   ....*....|
gi 136255943   583 AAFWSSLGGK 592
Cdd:smart00262  81 PEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 17-108 3.19e-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: 76.95  E-value: 3.19e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 136255943    17 QIWRIEKMDLKLVP--KQLHGNFFTGDAYVVLFTSpapsyNVHMWLGNECSQDESGAAAIFAMQLDDHLGGAPVQYREV- 93
Cdd:smart00262   1 FLVRVKGKRNVRVPevPFSQGSLNSGDCYILDTGS-----EIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVRVVd 75

                           90
                   ....*....|....*
gi 136255943    94 QNNESVTFLGYFKTG 108
Cdd:smart00262  76 EGKEPPEFWSLFGGW 90
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 390-483 3.71e-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: 73.94  E-value: 3.71e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 136255943 390 KVQVWRVEGNDR---VPVDPSSfGQFFGGDCYLILYTYlnggreqhIIYTWQGLKCTQDELTASAFLTVKLDDSMGGAPV 466
Cdd:cd11280    1 PPRLYRVRGSKAieiEEVPLAS-SSLDSDDVFVLDTGS--------EIYIWQGRASSQAELAAAALLAKELDEERKGKPE 71

                         90
                 ....*....|....*..
gi 136255943 467 QVRVTQGQEPAHLMSLF 483
Cdd:cd11280   72 IVRIRQGQEPREFWSLF 88
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 248-341 5.61e-16

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: 73.87  E-value: 5.61e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 136255943 248 SDAAGSMKTSEVkqnSPFKQELLNPSDCYILDNGldSKIFVWKGPRANTEERKSAMKVAEQFIKE---KNYPKNTQIQVM 324
Cdd:cd11291    8 SNESGFFKVEEI---SDFSQDDLDTDDIMLLDTG--DEVFVWVGSESSDEEKKEALTSAKKYIETdplGRSKPRTPIYLV 82

                         90
                 ....*....|....*..
gi 136255943 325 PGGGETTLFKQFFSNWK 341
Cdd:cd11291   83 KQGNEPPTFTGYFHAWD 99
Gelsolin pfam00626
Gelsolin repeat;
623-696 1.93e-15

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 71.57  E-value: 1.93e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 136255943  623 EEVPGDLTQSDLATDDVMLLDTWDQIFLWIGNDANVEEKIGSAKIAKDYvdsDPSKRQGIP-IITIKQGFEPPSF 696
Cdd:pfam00626   4 LPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQL---DDDERFPLPeVIRVPQGKEPARF 75
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 605-702 2.12e-15

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: 72.28  E-value: 2.12e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 136255943 605 VKLPRLFGCSNKTGRLIAEEVP-GDLTQSDLATDDVMLLDTWDQIFLWIGNDANVEEKIGSAKIAKDYVDSDPSKRQgIP 683
Cdd:cd11292    1 AEQKKLYKVSDASGKLKLTEVAeGSLNQEMLDSEDCYILDCGSEIFVWVGKGASLDERKAALKNAEEFLRKKKRPPY-TQ 79

                         90
                 ....*....|....*....
gi 136255943 684 IITIKQGFEPPSFTGWFQA 702
Cdd:cd11292   80 VTRVTEGGESALFKSKFAN 98
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 608-700 8.61e-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: 8.61e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 136255943 608 PRLFGCSNKTgRLIAEEVPGDltQSDLATDDVMLLDTWDQIFLWIGNDANVEEKIGSAKIAKDYVDSDPSKrqgIPIITI 687
Cdd:cd11280    2 PRLYRVRGSK-AIEIEEVPLA--SSSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKELDEERKGK---PEIVRI 75

                         90
                 ....*....|...
gi 136255943 688 KQGFEPPSFTGWF 700
Cdd:cd11280   76 RQGQEPREFWSLF 88
Gelsolin pfam00626
Gelsolin repeat;
398-480 1.60e-13

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 66.18  E-value: 1.60e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 136255943  398 GNDRVPVDPSSFGQFFGGDCYLILYTYlnggreqhIIYTWQGLKCTQDELTASAFLTVKLDDSM-GGAPVQVRVTQGQEP 476
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNGF--------TIFLWVGKGSSLLEKLFAALLAAQLDDDErFPLPEVIRVPQGKEP 72


                  ....
gi 136255943  477 AHLM 480
Cdd:pfam00626  73 ARFL 76
Gelsolin pfam00626
Gelsolin repeat;
264-334 2.14e-13

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 65.79  E-value: 2.14e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 136255943  264 PFKQELLNPSDCYILDNGldSKIFVWKGPRANTEERKSAMKVAEQFIKEKNYPKnTQIQVMPGGGETTLFK 334
Cdd:pfam00626   9 PLSQESLNSGDCYLLDNG--FTIFLWVGKGSSLLEKLFAALLAAQLDDDERFPL-PEVIRVPQGKEPARFL 76
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 17-105 1.13e-12

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


Pssm-ID: 200436  Cd Length: 88  Bit Score: 63.93  E-value: 1.13e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 136255943  17 QIWRIE-KMDLKLVPKQL-HGNFFTGDAYVVLFTSpapsyNVHMWLGNECSQDESGAAAIFAMQLDDHLGGAPVQYREVQ 94
Cdd:cd11280    3 RLYRVRgSKAIEIEEVPLaSSSLDSDDVFVLDTGS-----EIYIWQGRASSQAELAAAALLAKELDEERKGKPEIVRIRQ 77

                         90
                 ....*....|.
gi 136255943  95 NNESVTFLGYF 105
Cdd:cd11280   78 GQEPREFWSLF 88
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 507-589 2.30e-12

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


Pssm-ID: 200436  Cd Length: 88  Bit Score: 63.16  E-value: 2.30e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 136255943 507 TRLFHIRQSStrATRAVEVEPCASKLNTNDVFVLKFPEGMFLWKGVGASEEEIAAAKYV---CSILGGSATEIS---EGK 580
Cdd:cd11280    2 PRLYRVRGSK--AIEIEEVPLASSSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLakeLDEERKGKPEIVrirQGQ 79


                 ....*....
gi 136255943 581 EPAAFWSSL 589
Cdd:cd11280   80 EPREFWSLF 88
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 507-590 2.44e-11

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


Pssm-ID: 200445  Cd Length: 92  Bit Score: 60.33  E-value: 2.44e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 136255943 507 TRLFHIRQSstRATRAVEVEPCASKLNTNDVFVLKFPEGMFLWKGVGASEEEIAAAKYVCSIL-----GGSAT----EIS 577
Cdd:cd11289    2 PRLLHVKGR--RNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIrderrLGRAKvivlDEG 79

                         90
                 ....*....|...
gi 136255943 578 EGKEPAAFWSSLG 590
Cdd:cd11289   80 DTNESPEFWKVLG 92
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 250-337 3.02e-11

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


Pssm-ID: 200436  Cd Length: 88  Bit Score: 60.07  E-value: 3.02e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 136255943 250 AAGSMKTSEVkqnsPFKQELLNPSDCYILDNGldSKIFVWKGPRANTEERKSAMKVAEQFIKEknYPKNTQIQVMPGGGE 329
Cdd:cd11280    9 GSKAIEIEEV----PLASSSLDSDDVFVLDTG--SEIYIWQGRASSQAELAAAALLAKELDEE--RKGKPEIVRIRQGQE 80


                 ....*...
gi 136255943 330 TTLFKQFF 337
Cdd:cd11280   81 PREFWSLF 88
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 132-221 1.20e-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: 58.40  E-value: 1.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 136255943 132 RVLHIKG--RRAIRATEVNMSWASFNHGDCFILDLGKDIYQWCGSKCNRFERLKASEVSigirdNERNGRATLHIVEDGS 209
Cdd:cd11288    4 RLFQVRGngSGNTRAVEVDADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVA-----SFLKPKASLQEVAEGS 78

                         90
                 ....*....|..
gi 136255943 210 EPDVFSNTLGPK 221
Cdd:cd11288   79 EPDEFWEALGGK 90
Gelsolin pfam00626
Gelsolin repeat;
34-102 1.75e-10

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 57.32  E-value: 1.75e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 136255943   34 HGNFFTGDAYVVLFTspapsYNVHMWLGNECSQDESGAAAIFAMQLDD-HLGGAPVQYREVQNNESVTFL 102
Cdd:pfam00626  12 QESLNSGDCYLLDNG-----FTIFLWVGKGSSLLEKLFAALLAAQLDDdERFPLPEVIRVPQGKEPARFL 76
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 132-218 4.33e-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: 56.61  E-value: 4.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 136255943 132 RVLHIKGRRAIRATEVNMSWASFNHGDCFILDLGKDIYQWCGSKCNRFERLKASEVSIGIrDNERNGRATLHIVEDGSEP 211
Cdd:cd11280    3 RLYRVRGSKAIEIEEVPLASSSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKEL-DEERKGKPEIVRIRQGQEP 81


                 ....*..
gi 136255943 212 DVFSNTL 218
Cdd:cd11280   82 REFWSLF 88
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 608-703 4.54e-07

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: 48.39  E-value: 4.54e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 136255943 608 PRLFGCSNKtgRLI-AEEVPgdLTQSDLATDDVMLLDTWDQIFLWIGNDANVEEKIGSAKIAKDYVDsdpSKRQGIP-II 685
Cdd:cd11289    2 PRLLHVKGR--RNVrAREVE--LSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRD---ERRLGRAkVI 74

                         90
                 ....*....|....*...
gi 136255943 686 TIKQGFEPPSFTGWFQAW 703
Cdd:cd11289   75 VLDEGDTNESPEFWKVLG 92
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 251-333 1.40e-05

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


Pssm-ID: 200444  Cd Length: 92  Bit Score: 44.14  E-value: 1.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 136255943 251 AGSMKTSEVkqnsPFKQELLNPSDCYILDNGldSKIFVWKGPRANTEERKSAMKVAEqFIKEKnypknTQIQVMPGGGET 330
Cdd:cd11288   13 SGNTRAVEV----DADASSLNSNDVFVLKTP--SSVYLWVGKGSSEDERELAKDVAS-FLKPK-----ASLQEVAEGSEP 80


                 ...
gi 136255943 331 TLF 333
Cdd:cd11288   81 DEF 83
Gelsolin pfam00626
Gelsolin repeat;
518-586 1.32e-04

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 40.75  E-value: 1.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 136255943  518 RATRAVEVEPCASKLNTNDVFVLKFPEGMFLWKGVGASEEEIAAAKYvcsilggSATEIS--------------EGKEPA 583
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAAL-------LAAQLDdderfplpevirvpQGKEPA 73


                  ...
gi 136255943  584 AFW 586
Cdd:pfam00626  74 RFL 76
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 506-562 4.57e-04

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: 39.93  E-value: 4.57e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 136255943 506 TTRLFHIRQSSTR-ATRAVEVEP-CASKLNTNDVFVLKFPEGMFLWKGVGASEEEIAAA 562
Cdd:cd11292    3 QKKLYKVSDASGKlKLTEVAEGSlNQEMLDSEDCYILDCGSEIFVWVGKGASLDERKAA 61
 
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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