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Conserved domains on  [gi|1395232716|gb|AWP04329|]
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Scinderin-like protein [Scophthalmus maximus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MIG-14_Wnt-bd pfam06664
Wnt-binding factor required for Wnt secretion; MIG-14 is a Wnt-binding factor. Newly ...
 742-1060 3.99e-113

Wnt-binding factor required for Wnt secretion; MIG-14 is a Wnt-binding factor. Newly synthesized EGL-20/Wnt binds to MIG-14 in the Golgi, targetting the Wnt to the cell membrane for secretion. AP-2-mediated endocytosis and retromer retrieval at the sorting endosome would recycle MIG-14 to the Golgi, where it can bind to EGL-20/Wnt for next cycle of secretion.


:

Pssm-ID: 461980  Cd Length: 294  Bit Score: 352.71  E-value: 3.99e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395232716  742 ECDLLPFMEVGSVAHKYYLLNIRLPVNERKKVNVGIgeiKDIRLVSIHQNGGFTKVWFAMKTFLTPSILIIMIWY--WRR 819
Cdd:pfam06664    1 NCDPITLFELGSLDYSYYLINIRFPNLEEFHDNYDG---KELVFTFIHQNPGFTLFEIWFRTIFLIISFIVLIWFlfSLR 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395232716  820 iTLMSRPPVLLEKVILALGISMTFINIPVEWFSVGFNWTWMLLFGDIRQGIFYSMLLSFWIIFCgEHLMD-QTERNRFSV 898
Cdd:pfam06664   78 -KLLSRDWSLEQKWLFVLLILLILFNNPFFPLTLLFNSWFFLLLDDIFQGIFYSALLLFWLVFF-DHLRDeQNERKSLSF 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395232716  899 YWKQVGPIVFGSFCLFIFDMCERGVQLTNPFYSIWAsdvgTELAMAFIIVAGICACLYFLFLCFMVFQVFRNISGKRTSl 978
Cdd:pfam06664  156 YLPKLLLVGVLWLSLLILDIWERGVQLKDPFYSIWD----SELADGFKILAGILAVLYFLYLLYLIFRVFSEIRSKRMP- 230

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395232716  979 pamsrarrlhyEGLIfRFKFLMLVTLACAAMTVIFFIISQVNEGHWhwgehtVEVNSAFFTGIYGMWNLYVFAIMFLYAP 1058
Cdd:pfam06664  231 -----------EGDI-RFKFLMLLTLLCAAVTVIFIILGQFSFGQN------FNSTSAFFLGFYGMLNLYVYTLAYLYAP 292


                   ..
gi 1395232716 1059 SH 1060
Cdd:pfam06664  293 SH 294
gelsolin_S1_like cd11290
Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; ...
 25-133 3.62e-53

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: 181.27  E-value: 3.62e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395232716   25 FVGAGKTPGLQVWRIENLDLKPVPKALHGSFYTGDAYLLLFTT----SAPSYNIHMWLGDECSQDESGAVAIFATQLDDF 100
Cdd:cd11290      1 FEGVGQKPGLQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTldpsGSLSYDIHYWLGKEASQDEAGAAAIKAVELDDY 80

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1395232716  101 LGGGPVQYREVQNFESNTLVGYFRSGIKYQKGG 133
Cdd:cd11290     81 LGGRPVQHREVQGHESEEFLSYFKKGIIYIEGG 113
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
 400-500 4.49e-51

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: 174.77  E-value: 4.49e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395232716  400 MVDDGKGKVQIWRVENGAMAPVDPSAYGHFYGGDCYLILYSYRLGGREQHIIYTWQGLRCSQDELAASAFLTVKLDDSMG 479
Cdd:cd11293      1 MYDDGSGKVEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQGGGKEEHILYFWQGRHSSQDERAAAALLTVELDEELK 80

                           90       100
                   ....*....|....*....|.
gi 1395232716  480 GSPVQVRVTQGQEPPHLMSLF 500
Cdd:cd11293     81 GRAVQVRVVQGKEPPHFLALF 101
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 148-237 2.09e-42

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: 149.70  E-value: 2.09e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395232716  148 VKRLLHIKGRRAIRATEVDMSWSNFNKGDCFIIDLGKDVYQWCGSQCNRFERLKASQVAIDIRDNERNGRAKLHMVEEGE 227
Cdd:cd11289      1 KPRLLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKVIVLDEGD 80

                           90
                   ....*....|..
gi 1395232716  228 --EPAAVIEALG 237
Cdd:cd11289     81 tnESPEFWKVLG 92
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 261-354 4.13e-32

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


:

Pssm-ID: 200448  Cd Length: 98  Bit Score: 120.43  E-value: 4.13e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395232716  261 LYMISDASGAMKVSAVApSSPFKQAMLSAEECYILDNGVDrnIFVWKGPKANMSERKAAMSAGQQFIKDKGYSNKTQIQV 340
Cdd:cd11292      6 LYKVSDASGKLKLTEVA-EGSLNQEMLDSEDCYILDCGSE--IFVWVGKGASLDERKAALKNAEEFLRKKKRPPYTQVTR 82

                           90
                   ....*....|....
gi 1395232716  341 LPAGAETTLFKQFF 354
Cdd:cd11292     83 VTEGGESALFKSKF 96
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 522-600 1.30e-28

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: 110.01  E-value: 1.30e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395232716  522 SSTRLFHIRQSSSRATRAVEVEASASSLNTNDVFVLKSPKAVFVWRGMGASDEEMAAAKHVVGFLGGSAA--QVSERKEP 599
Cdd:cd11288      1 SPTRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVASFLKPKASlqEVAEGSEP 80


                   .
gi 1395232716  600 A 600
Cdd:cd11288     81 D 81
 
Name Accession Description Interval E-value
MIG-14_Wnt-bd pfam06664
Wnt-binding factor required for Wnt secretion; MIG-14 is a Wnt-binding factor. Newly ...
 742-1060 3.99e-113

Wnt-binding factor required for Wnt secretion; MIG-14 is a Wnt-binding factor. Newly synthesized EGL-20/Wnt binds to MIG-14 in the Golgi, targetting the Wnt to the cell membrane for secretion. AP-2-mediated endocytosis and retromer retrieval at the sorting endosome would recycle MIG-14 to the Golgi, where it can bind to EGL-20/Wnt for next cycle of secretion.


Pssm-ID: 461980  Cd Length: 294  Bit Score: 352.71  E-value: 3.99e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395232716  742 ECDLLPFMEVGSVAHKYYLLNIRLPVNERKKVNVGIgeiKDIRLVSIHQNGGFTKVWFAMKTFLTPSILIIMIWY--WRR 819
Cdd:pfam06664    1 NCDPITLFELGSLDYSYYLINIRFPNLEEFHDNYDG---KELVFTFIHQNPGFTLFEIWFRTIFLIISFIVLIWFlfSLR 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395232716  820 iTLMSRPPVLLEKVILALGISMTFINIPVEWFSVGFNWTWMLLFGDIRQGIFYSMLLSFWIIFCgEHLMD-QTERNRFSV 898
Cdd:pfam06664   78 -KLLSRDWSLEQKWLFVLLILLILFNNPFFPLTLLFNSWFFLLLDDIFQGIFYSALLLFWLVFF-DHLRDeQNERKSLSF 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395232716  899 YWKQVGPIVFGSFCLFIFDMCERGVQLTNPFYSIWAsdvgTELAMAFIIVAGICACLYFLFLCFMVFQVFRNISGKRTSl 978
Cdd:pfam06664  156 YLPKLLLVGVLWLSLLILDIWERGVQLKDPFYSIWD----SELADGFKILAGILAVLYFLYLLYLIFRVFSEIRSKRMP- 230

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395232716  979 pamsrarrlhyEGLIfRFKFLMLVTLACAAMTVIFFIISQVNEGHWhwgehtVEVNSAFFTGIYGMWNLYVFAIMFLYAP 1058
Cdd:pfam06664  231 -----------EGDI-RFKFLMLLTLLCAAVTVIFIILGQFSFGQN------FNSTSAFFLGFYGMLNLYVYTLAYLYAP 292


                   ..
gi 1395232716 1059 SH 1060
Cdd:pfam06664  293 SH 294
gelsolin_S1_like cd11290
Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; ...
 25-133 3.62e-53

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: 181.27  E-value: 3.62e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395232716   25 FVGAGKTPGLQVWRIENLDLKPVPKALHGSFYTGDAYLLLFTT----SAPSYNIHMWLGDECSQDESGAVAIFATQLDDF 100
Cdd:cd11290      1 FEGVGQKPGLQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTldpsGSLSYDIHYWLGKEASQDEAGAAAIKAVELDDY 80

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1395232716  101 LGGGPVQYREVQNFESNTLVGYFRSGIKYQKGG 133
Cdd:cd11290     81 LGGRPVQHREVQGHESEEFLSYFKKGIIYIEGG 113
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
 400-500 4.49e-51

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: 174.77  E-value: 4.49e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395232716  400 MVDDGKGKVQIWRVENGAMAPVDPSAYGHFYGGDCYLILYSYRLGGREQHIIYTWQGLRCSQDELAASAFLTVKLDDSMG 479
Cdd:cd11293      1 MYDDGSGKVEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQGGGKEEHILYFWQGRHSSQDERAAAALLTVELDEELK 80

                           90       100
                   ....*....|....*....|.
gi 1395232716  480 GSPVQVRVTQGQEPPHLMSLF 500
Cdd:cd11293     81 GRAVQVRVVQGKEPPHFLALF 101
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 148-237 2.09e-42

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: 149.70  E-value: 2.09e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395232716  148 VKRLLHIKGRRAIRATEVDMSWSNFNKGDCFIIDLGKDVYQWCGSQCNRFERLKASQVAIDIRDNERNGRAKLHMVEEGE 227
Cdd:cd11289      1 KPRLLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKVIVLDEGD 80

                           90
                   ....*....|..
gi 1395232716  228 --EPAAVIEALG 237
Cdd:cd11289     81 tnESPEFWKVLG 92
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 261-354 4.13e-32

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


Pssm-ID: 200448  Cd Length: 98  Bit Score: 120.43  E-value: 4.13e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395232716  261 LYMISDASGAMKVSAVApSSPFKQAMLSAEECYILDNGVDrnIFVWKGPKANMSERKAAMSAGQQFIKDKGYSNKTQIQV 340
Cdd:cd11292      6 LYKVSDASGKLKLTEVA-EGSLNQEMLDSEDCYILDCGSE--IFVWVGKGASLDERKAALKNAEEFLRKKKRPPYTQVTR 82

                           90
                   ....*....|....
gi 1395232716  341 LPAGAETTLFKQFF 354
Cdd:cd11292     83 VTEGGESALFKSKF 96
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 522-600 1.30e-28

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: 110.01  E-value: 1.30e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395232716  522 SSTRLFHIRQSSSRATRAVEVEASASSLNTNDVFVLKSPKAVFVWRGMGASDEEMAAAKHVVGFLGGSAA--QVSERKEP 599
Cdd:cd11288      1 SPTRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVASFLKPKASlqEVAEGSEP 80


                   .
gi 1395232716  600 A 600
Cdd:cd11288     81 D 81
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 150-239 1.44e-25

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 101.60  E-value: 1.44e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395232716   150 RLLHIKGRRAIRATEVDMSWSNFNKGDCFIIDLGKDVYQWCGSQCNRFERLKASQVAIDIRDNERNGRAKLHMVEEGEEP 229
Cdd:smart00262    1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVRVVDEGKEP 80

                            90
                    ....*....|
gi 1395232716   230 AAVIEALGPK 239
Cdd:smart00262   81 PEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 409-503 2.03e-22

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 92.36  E-value: 2.03e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395232716   409 QIWRVENGAMAPVD--PSAYGHFYGGDCYLILYsyrlggreQHIIYTWQGLRCSQDELAASAFLTVKLDDSMGGSPVQVR 486
Cdd:smart00262    1 FLVRVKGKRNVRVPevPFSQGSLNSGDCYILDT--------GSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVR 72

                            90
                    ....*....|....*...
gi 1395232716   487 -VTQGQEPPHLMSLFAGK 503
Cdd:smart00262   73 vVDEGKEPPEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 269-357 1.19e-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: 81.57  E-value: 1.19e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395232716   269 GAMKVSAVAPSSPFKQAMLSAEECYILDNGVDrnIFVWKGPKANMSERKAAMSAGQQFIKDKGySNKTQIQVLPAGAETT 348
Cdd:smart00262    5 VKGKRNVRVPEVPFSQGSLNSGDCYILDTGSE--IYVWVGKKSSQDEKKKAAELAVELDDTLG-PGPVQVRVVDEGKEPP 81


                    ....*....
gi 1395232716   349 LFKQFFIDW 357
Cdd:smart00262   82 EFWSLFGGW 90
Gelsolin pfam00626
Gelsolin repeat;
158-233 4.09e-17

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 76.96  E-value: 4.09e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1395232716  158 RAIRATEVDMSWSNFNKGDCFIIDLGKDVYQWCGSQCNRFERLKASQVAIDIRDNERNGRAKLHMVEEGEEPAAVI 233
Cdd:pfam00626    1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDERFPLPEVIRVPQGKEPARFL 76
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 35-126 1.98e-16

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 75.41  E-value: 1.98e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395232716    35 QVWRIENLDLKPVP--KALHGSFYTGDAYLLLFTtsapsYNIHMWLGDECSQDESGAVAIFATQLDDFLGGGPVQYREV- 111
Cdd:smart00262    1 FLVRVKGKRNVRVPevPFSQGSLNSGDCYILDTG-----SEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVRVVd 75

                            90
                    ....*....|....*
gi 1395232716   112 QNFESNTLVGYFRSG 126
Cdd:smart00262   76 EGKEPPEFWSLFGGW 90
Gelsolin pfam00626
Gelsolin repeat;
418-497 7.53e-13

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 64.64  E-value: 7.53e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395232716  418 MAPVDPSAYGHFYGGDCYLILYSYrlggreqhIIYTWQGLRCSQDELAASAFLTVKLDDSM-GGSPVQVRVTQGQEPPHL 496
Cdd:pfam00626    4 LPPPVPLSQESLNSGDCYLLDNGF--------TIFLWVGKGSSLLEKLFAALLAAQLDDDErFPLPEVIRVPQGKEPARF 75


                   .
gi 1395232716  497 M 497
Cdd:pfam00626   76 L 76
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 527-600 2.11e-12

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: 63.85  E-value: 2.11e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395232716   527 FHIRQSSSRATRAVEVEASASSLNTNDVFVLKSPKAVFVWRGMGASDEE-MAAAKHVVGF---LGGSAAQ---VSERKEP 599
Cdd:smart00262    1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEkKKAAELAVELddtLGPGPVQvrvVDEGKEP 80


                    .
gi 1395232716   600 A 600
Cdd:smart00262   81 P 81
Gelsolin pfam00626
Gelsolin repeat;
41-120 6.64e-12

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 61.94  E-value: 6.64e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395232716   41 NLDLKPVPKALHGSFYTGDAYLLLFTtsapsYNIHMWLGDECSQDESGAVAIFATQLDD-FLGGGPVQYREVQNFESNTL 119
Cdd:pfam00626    1 KFVLPPPVPLSQESLNSGDCYLLDNG-----FTIFLWVGKGSSLLEKLFAALLAAQLDDdERFPLPEVIRVPQGKEPARF 75


                   .
gi 1395232716  120 V 120
Cdd:pfam00626   76 L 76
Gelsolin pfam00626
Gelsolin repeat;
276-351 2.91e-10

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 57.32  E-value: 2.91e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1395232716  276 VAPSSPFKQAMLSAEECYILDNGVdrNIFVWKGPKANMSERKAAMSAGQQFIKDKgYSNKTQIQVLPAGAETTLFK 351
Cdd:pfam00626    4 LPPPVPLSQESLNSGDCYLLDNGF--TIFLWVGKGSSLLEKLFAALLAAQLDDDE-RFPLPEVIRVPQGKEPARFL 76
Gelsolin pfam00626
Gelsolin repeat;
535-585 2.59e-06

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 46.15  E-value: 2.59e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1395232716  535 RATRAVEVEASASSLNTNDVFVLKSPKAVFVWRGMGAS-DEEMAAAKHVVGF 585
Cdd:pfam00626    1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSlLEKLFAALLAAQL 52
 
Name Accession Description Interval E-value
MIG-14_Wnt-bd pfam06664
Wnt-binding factor required for Wnt secretion; MIG-14 is a Wnt-binding factor. Newly ...
 742-1060 3.99e-113

Wnt-binding factor required for Wnt secretion; MIG-14 is a Wnt-binding factor. Newly synthesized EGL-20/Wnt binds to MIG-14 in the Golgi, targetting the Wnt to the cell membrane for secretion. AP-2-mediated endocytosis and retromer retrieval at the sorting endosome would recycle MIG-14 to the Golgi, where it can bind to EGL-20/Wnt for next cycle of secretion.


Pssm-ID: 461980  Cd Length: 294  Bit Score: 352.71  E-value: 3.99e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395232716  742 ECDLLPFMEVGSVAHKYYLLNIRLPVNERKKVNVGIgeiKDIRLVSIHQNGGFTKVWFAMKTFLTPSILIIMIWY--WRR 819
Cdd:pfam06664    1 NCDPITLFELGSLDYSYYLINIRFPNLEEFHDNYDG---KELVFTFIHQNPGFTLFEIWFRTIFLIISFIVLIWFlfSLR 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395232716  820 iTLMSRPPVLLEKVILALGISMTFINIPVEWFSVGFNWTWMLLFGDIRQGIFYSMLLSFWIIFCgEHLMD-QTERNRFSV 898
Cdd:pfam06664   78 -KLLSRDWSLEQKWLFVLLILLILFNNPFFPLTLLFNSWFFLLLDDIFQGIFYSALLLFWLVFF-DHLRDeQNERKSLSF 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395232716  899 YWKQVGPIVFGSFCLFIFDMCERGVQLTNPFYSIWAsdvgTELAMAFIIVAGICACLYFLFLCFMVFQVFRNISGKRTSl 978
Cdd:pfam06664  156 YLPKLLLVGVLWLSLLILDIWERGVQLKDPFYSIWD----SELADGFKILAGILAVLYFLYLLYLIFRVFSEIRSKRMP- 230

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395232716  979 pamsrarrlhyEGLIfRFKFLMLVTLACAAMTVIFFIISQVNEGHWhwgehtVEVNSAFFTGIYGMWNLYVFAIMFLYAP 1058
Cdd:pfam06664  231 -----------EGDI-RFKFLMLLTLLCAAVTVIFIILGQFSFGQN------FNSTSAFFLGFYGMLNLYVYTLAYLYAP 292


                   ..
gi 1395232716 1059 SH 1060
Cdd:pfam06664  293 SH 294
gelsolin_S1_like cd11290
Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; ...
 25-133 3.62e-53

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: 181.27  E-value: 3.62e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395232716   25 FVGAGKTPGLQVWRIENLDLKPVPKALHGSFYTGDAYLLLFTT----SAPSYNIHMWLGDECSQDESGAVAIFATQLDDF 100
Cdd:cd11290      1 FEGVGQKPGLQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTldpsGSLSYDIHYWLGKEASQDEAGAAAIKAVELDDY 80

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1395232716  101 LGGGPVQYREVQNFESNTLVGYFRSGIKYQKGG 133
Cdd:cd11290     81 LGGRPVQHREVQGHESEEFLSYFKKGIIYIEGG 113
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
 400-500 4.49e-51

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: 174.77  E-value: 4.49e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395232716  400 MVDDGKGKVQIWRVENGAMAPVDPSAYGHFYGGDCYLILYSYRLGGREQHIIYTWQGLRCSQDELAASAFLTVKLDDSMG 479
Cdd:cd11293      1 MYDDGSGKVEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQGGGKEEHILYFWQGRHSSQDERAAAALLTVELDEELK 80

                           90       100
                   ....*....|....*....|.
gi 1395232716  480 GSPVQVRVTQGQEPPHLMSLF 500
Cdd:cd11293     81 GRAVQVRVVQGKEPPHFLALF 101
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 148-237 2.09e-42

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: 149.70  E-value: 2.09e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395232716  148 VKRLLHIKGRRAIRATEVDMSWSNFNKGDCFIIDLGKDVYQWCGSQCNRFERLKASQVAIDIRDNERNGRAKLHMVEEGE 227
Cdd:cd11289      1 KPRLLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKVIVLDEGD 80

                           90
                   ....*....|..
gi 1395232716  228 --EPAAVIEALG 237
Cdd:cd11289     81 tnESPEFWKVLG 92
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 261-354 4.13e-32

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


Pssm-ID: 200448  Cd Length: 98  Bit Score: 120.43  E-value: 4.13e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395232716  261 LYMISDASGAMKVSAVApSSPFKQAMLSAEECYILDNGVDrnIFVWKGPKANMSERKAAMSAGQQFIKDKGYSNKTQIQV 340
Cdd:cd11292      6 LYKVSDASGKLKLTEVA-EGSLNQEMLDSEDCYILDCGSE--IFVWVGKGASLDERKAALKNAEEFLRKKKRPPYTQVTR 82

                           90
                   ....*....|....
gi 1395232716  341 LPAGAETTLFKQFF 354
Cdd:cd11292     83 VTEGGESALFKSKF 96
gelsolin_S1_like cd11290
Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; ...
 408-511 1.96e-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: 113.47  E-value: 1.96e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395232716  408 VQIWRVENGAMAPVDPSAYGHFYGGDCYLILYSYRLG-GREQHIIYTWQGLRCSQDELAASAFLTVKLDDSMGGSPVQVR 486
Cdd:cd11290     10 LQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDPsGSLSYDIHYWLGKEASQDEAGAAAIKAVELDDYLGGRPVQHR 89

                           90       100
                   ....*....|....*....|....*
gi 1395232716  487 VTQGQEPPHLMSLFagKPMIIHSGG 511
Cdd:cd11290     90 EVQGHESEEFLSYF--KKGIIYIEG 112
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 522-600 1.30e-28

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: 110.01  E-value: 1.30e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395232716  522 SSTRLFHIRQSSSRATRAVEVEASASSLNTNDVFVLKSPKAVFVWRGMGASDEEMAAAKHVVGFLGGSAA--QVSERKEP 599
Cdd:cd11288      1 SPTRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVASFLKPKASlqEVAEGSEP 80


                   .
gi 1395232716  600 A 600
Cdd:cd11288     81 D 81
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 150-239 1.44e-25

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 101.60  E-value: 1.44e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395232716   150 RLLHIKGRRAIRATEVDMSWSNFNKGDCFIIDLGKDVYQWCGSQCNRFERLKASQVAIDIRDNERNGRAKLHMVEEGEEP 229
Cdd:smart00262    1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVRVVDEGKEP 80

                            90
                    ....*....|
gi 1395232716   230 AAVIEALGPK 239
Cdd:smart00262   81 PEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 409-503 2.03e-22

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 92.36  E-value: 2.03e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395232716   409 QIWRVENGAMAPVD--PSAYGHFYGGDCYLILYsyrlggreQHIIYTWQGLRCSQDELAASAFLTVKLDDSMGGSPVQVR 486
Cdd:smart00262    1 FLVRVKGKRNVRVPevPFSQGSLNSGDCYILDT--------GSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVR 72

                            90
                    ....*....|....*...
gi 1395232716   487 -VTQGQEPPHLMSLFAGK 503
Cdd:smart00262   73 vVDEGKEPPEFWSLFGGW 90
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
 27-123 2.85e-22

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: 92.33  E-value: 2.85e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395232716   27 GAGKtpgLQVWRIENLDLKPVPKALHGSFYTGDAYLLLFTTSA---PSYNIHMWLGDECSQDESGAVAIFATQLDDFLGG 103
Cdd:cd11293      5 GSGK---VEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQGggkEEHILYFWQGRHSSQDERAAAALLTVELDEELKG 81

                           90       100
                   ....*....|....*....|
gi 1395232716  104 GPVQYREVQNFESNTLVGYF 123
Cdd:cd11293     82 RAVQVRVVQGKEPPHFLALF 101
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 269-357 1.19e-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: 81.57  E-value: 1.19e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395232716   269 GAMKVSAVAPSSPFKQAMLSAEECYILDNGVDrnIFVWKGPKANMSERKAAMSAGQQFIKDKGySNKTQIQVLPAGAETT 348
Cdd:smart00262    5 VKGKRNVRVPEVPFSQGSLNSGDCYILDTGSE--IYVWVGKKSSQDEKKKAAELAVELDDTLG-PGPVQVRVVDEGKEPP 81


                    ....*....
gi 1395232716   349 LFKQFFIDW 357
Cdd:smart00262   82 EFWSLFGGW 90
Gelsolin pfam00626
Gelsolin repeat;
158-233 4.09e-17

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 76.96  E-value: 4.09e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1395232716  158 RAIRATEVDMSWSNFNKGDCFIIDLGKDVYQWCGSQCNRFERLKASQVAIDIRDNERNGRAKLHMVEEGEEPAAVI 233
Cdd:pfam00626    1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDERFPLPEVIRVPQGKEPARFL 76
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 35-126 1.98e-16

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 75.41  E-value: 1.98e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395232716    35 QVWRIENLDLKPVP--KALHGSFYTGDAYLLLFTtsapsYNIHMWLGDECSQDESGAVAIFATQLDDFLGGGPVQYREV- 111
Cdd:smart00262    1 FLVRVKGKRNVRVPevPFSQGSLNSGDCYILDTG-----SEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVRVVd 75

                            90
                    ....*....|....*
gi 1395232716   112 QNFESNTLVGYFRSG 126
Cdd:smart00262   76 EGKEPPEFWSLFGGW 90
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 407-500 1.61e-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: 70.09  E-value: 1.61e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395232716  407 KVQIWRVE---NGAMAPVDPSAYGhFYGGDCYLILYsyrlgGREqhiIYTWQGLRCSQDELAASAFLTVKLDDSMGGSPV 483
Cdd:cd11280      1 PPRLYRVRgskAIEIEEVPLASSS-LDSDDVFVLDT-----GSE---IYIWQGRASSQAELAAAALLAKELDEERKGKPE 71

                           90
                   ....*....|....*..
gi 1395232716  484 QVRVTQGQEPPHLMSLF 500
Cdd:cd11280     72 IVRIRQGQEPREFWSLF 88
Gelsolin pfam00626
Gelsolin repeat;
418-497 7.53e-13

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 64.64  E-value: 7.53e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395232716  418 MAPVDPSAYGHFYGGDCYLILYSYrlggreqhIIYTWQGLRCSQDELAASAFLTVKLDDSM-GGSPVQVRVTQGQEPPHL 496
Cdd:pfam00626    4 LPPPVPLSQESLNSGDCYLLDNGF--------TIFLWVGKGSSLLEKLFAALLAAQLDDDErFPLPEVIRVPQGKEPARF 75


                   .
gi 1395232716  497 M 497
Cdd:pfam00626   76 L 76
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 527-600 2.11e-12

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: 63.85  E-value: 2.11e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395232716   527 FHIRQSSSRATRAVEVEASASSLNTNDVFVLKSPKAVFVWRGMGASDEE-MAAAKHVVGF---LGGSAAQ---VSERKEP 599
Cdd:smart00262    1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEkKKAAELAVELddtLGPGPVQvrvVDEGKEP 80


                    .
gi 1395232716   600 A 600
Cdd:smart00262   81 P 81
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 150-240 4.14e-12

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: 63.02  E-value: 4.14e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395232716  150 RLLHIKG--RRAIRATEVDMSWSNFNKGDCFIIDLGKDVYQWCGSQCNRFERLKASQVAIDIRDnerngRAKLHMVEEGE 227
Cdd:cd11288      4 RLFQVRGngSGNTRAVEVDADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVASFLKP-----KASLQEVAEGS 78

                           90
                   ....*....|...
gi 1395232716  228 EPAAVIEALGPKS 240
Cdd:cd11288     79 EPDEFWEALGGKS 91
Gelsolin pfam00626
Gelsolin repeat;
41-120 6.64e-12

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 61.94  E-value: 6.64e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395232716   41 NLDLKPVPKALHGSFYTGDAYLLLFTtsapsYNIHMWLGDECSQDESGAVAIFATQLDD-FLGGGPVQYREVQNFESNTL 119
Cdd:pfam00626    1 KFVLPPPVPLSQESLNSGDCYLLDNG-----FTIFLWVGKGSSLLEKLFAALLAAQLDDdERFPLPEVIRVPQGKEPARF 75


                   .
gi 1395232716  120 V 120
Cdd:pfam00626   76 L 76
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 261-358 1.16e-11

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: 62.31  E-value: 1.16e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395232716  261 LYMISDASGAMKVSAVapsSPFKQAMLSAEECYILDNGvdRNIFVWKGPKANMSERKAAMSAGQQFIK---DKGYSNKTQ 337
Cdd:cd11291      4 LFRCSNESGFFKVEEI---SDFSQDDLDTDDIMLLDTG--DEVFVWVGSESSDEEKKEALTSAKKYIEtdpLGRSKPRTP 78

                           90       100
                   ....*....|....*....|.
gi 1395232716  338 IQVLPAGAETTLFKQFFIDWK 358
Cdd:cd11291     79 IYLVKQGNEPPTFTGYFHAWD 99
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 35-123 1.57e-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: 61.23  E-value: 1.57e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395232716   35 QVWRIE---NLDLKPVPKAlHGSFYTGDAYLLLFTTsapsyNIHMWLGDECSQDESGAVAIFATQLDDFLGGGPVQYREV 111
Cdd:cd11280      3 RLYRVRgskAIEIEEVPLA-SSSLDSDDVFVLDTGS-----EIYIWQGRASSQAELAAAALLAKELDEERKGKPEIVRIR 76

                           90
                   ....*....|..
gi 1395232716  112 QNFESNTLVGYF 123
Cdd:cd11280     77 QGQEPREFWSLF 88
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 150-230 6.35e-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: 59.69  E-value: 6.35e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395232716  150 RLLHIKGRRAIRATEVDMSWSNFNKGDCFIIDLGKDVYQWCGSQCNRFERLKASQVAIDIrDNERNGRAKLHMVEEGEEP 229
Cdd:cd11280      3 RLYRVRGSKAIEIEEVPLASSSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKEL-DEERKGKPEIVRIRQGQEP 81


                   .
gi 1395232716  230 A 230
Cdd:cd11280     82 R 82
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 523-601 1.10e-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: 58.92  E-value: 1.10e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395232716  523 STRLFHIRqsSSRATRAVEVEASASSLNTNDVFVLKSPKAVFVWRGMGASDEEMAA----AKHVVGFLGGSAAQVSERK- 597
Cdd:cd11280      1 PPRLYRVR--GSKAIEIEEVPLASSSLDSDDVFVLDTGSEIYIWQGRASSQAELAAaallAKELDEERKGKPEIVRIRQg 78


                   ....*
gi 1395232716  598 -EPAP 601
Cdd:cd11280     79 qEPRE 83
Gelsolin pfam00626
Gelsolin repeat;
276-351 2.91e-10

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 57.32  E-value: 2.91e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1395232716  276 VAPSSPFKQAMLSAEECYILDNGVdrNIFVWKGPKANMSERKAAMSAGQQFIKDKgYSNKTQIQVLPAGAETTLFK 351
Cdd:pfam00626    4 LPPPVPLSQESLNSGDCYLLDNGF--TIFLWVGKGSSLLEKLFAALLAAQLDDDE-RFPLPEVIRVPQGKEPARFL 76
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 261-354 1.57e-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: 55.84  E-value: 1.57e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395232716  261 LYMISdASGAMKVSAVAPSSPfkqaMLSAEECYILDNGvdRNIFVWKGPKANMSERKAAMSAGQQFikDKGYSNKTQIQV 340
Cdd:cd11280      4 LYRVR-GSKAIEIEEVPLASS----SLDSDDVFVLDTG--SEIYIWQGRASSQAELAAAALLAKEL--DEERKGKPEIVR 74

                           90
                   ....*....|....
gi 1395232716  341 LPAGAETTLFKQFF 354
Cdd:cd11280     75 IRQGQEPREFWSLF 88
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 524-604 1.40e-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: 53.01  E-value: 1.40e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395232716  524 TRLFHIRQSssRATRAVEVEASASSLNTNDVFVLKSPKAVFVWRGMGASDEEMAAAKHVVGFL------GGSAAQVSERK 597
Cdd:cd11289      2 PRLLHVKGR--RNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIrderrlGRAKVIVLDEG 79


                   ....*..
gi 1395232716  598 EPAPSPT 604
Cdd:cd11289     80 DTNESPE 86
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 172-231 1.27e-07

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: 50.71  E-value: 1.27e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1395232716  172 FNKGDCFIIDLGKDVYQWCGSQCNRFERLKASQVAID-IRDNERNGRAKLHMVEEGEEPAA 231
Cdd:cd11292     31 LDSEDCYILDCGSEIFVWVGKGASLDERKAALKNAEEfLRKKKRPPYTQVTRVTEGGESAL 91
Gelsolin pfam00626
Gelsolin repeat;
535-585 2.59e-06

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 46.15  E-value: 2.59e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1395232716  535 RATRAVEVEASASSLNTNDVFVLKSPKAVFVWRGMGAS-DEEMAAAKHVVGF 585
Cdd:pfam00626    1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSlLEKLFAALLAAQL 52
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 541-586 1.79e-05

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


Pssm-ID: 200448  Cd Length: 98  Bit Score: 44.55  E-value: 1.79e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1395232716  541 EVEASASSLNTNDVFVLKSPKAVFVWRGMGAS-DEEMAAAKHVVGFL 586
Cdd:cd11292     23 EGSLNQEMLDSEDCYILDCGSEIFVWVGKGASlDERKAALKNAEEFL 69
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 161-231 7.72e-04

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: 39.97  E-value: 7.72e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1395232716  161 RATEV-DMSWSNFNKGDCFIIDLGKDVYQWCGSQCNRFERLKASQVA---IDI-RDNERNGRAKLHMVEEGEEPAA 231
Cdd:cd11291     15 KVEEIsDFSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAkkyIETdPLGRSKPRTPIYLVKQGNEPPT 90
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 524-575 4.20e-03

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: 37.66  E-value: 4.20e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1395232716  524 TRLFHIRQSSSRATRAVEVEASASSLNTNDVFVLKSPKAVFVWRGMGASDEE 575
Cdd:cd11291      2 PRLFRCSNESGFFKVEEISDFSQDDLDTDDIMLLDTGDEVFVWVGSESSDEE 53
 
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.
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