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Conserved domains on  [gi|386765046|ref|NP_996149|]
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gelsolin, isoform J [Drosophila melanogaster]

Protein Classification

gelsolin/scinderin family protein; gelsolin family protein( domain architecture ID 10181791)

villin/gelsolin family protein similar to Homo sapiens gelsolin, a calcium-regulated, actin-modulating protein that binds to the plus (or barbed) ends of actin monomers or filaments, preventing monomer exchange (end-blocking or capping), and to Homo sapiens scinderin, a Ca(2+)-dependent actin filament-severing protein that has a regulatory function in exocytosis by affecting the organization of the microfilament network underneath the plasma membrane| gelsolin family protein, similar to Columba livia scinderin

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; ...
 63-176 3.39e-61

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: 201.68  E-value: 3.39e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765046  63 FANAGRTPGLEIWRIENFEPVIYPKTNYGKFYTGDSFIVLNTIENKKDKkLSWDVHFWLGLETSTDEAGAAAILTVQLDD 142
Cdd:cd11290    1 FEGVGQKPGLQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDPSGS-LSYDIHYWLGKEASQDEAGAAAIKAVELDD 79

                         90       100       110
                 ....*....|....*....|....*....|....
gi 386765046 143 LLNGGPVQHREVQDHESQLFLSYFKNGIRYEQGG 176
Cdd:cd11290   80 YLGGRPVQHREVQGHESEEFLSYFKKGIIYIEGG 113
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 307-404 2.03e-45

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: 157.80  E-value: 2.03e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765046 307 AAAVSLYKVSDASGKLKVDIIGQKPLTQAMLDTRECFILDTGSGIFVWVGKGATQKEKTDAMAKAQEFLRTKKYPAWTQI 386
Cdd:cd11292    1 AEQKKLYKVSDASGKLKLTEVAEGSLNQEMLDSEDCYILDCGSEIFVWVGKGASLDERKAALKNAEEFLRKKKRPPYTQV 80

                         90
                 ....*....|....*...
gi 386765046 387 HRIVEGSESAPFKQYFDT 404
Cdd:cd11292   81 TRVTEGGESALFKSKFAN 98
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 675-774 7.75e-43

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: 150.53  E-value: 7.75e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765046 675 ESRLFHCHLSSGgFLKVEEVAQYEQEDLDSDDIMLLDAGDEIYLWVGYGVSEEENGKLLDTAKLYFNLEPTARSFDTVSI 754
Cdd:cd11291    1 KPRLFRCSNESG-FFKVEEISDFSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYIETDPLGRSKPRTPI 79

                         90       100
                 ....*....|....*....|
gi 386765046 755 IRVPQGKEPRVFKRMFPNWD 774
Cdd:cd11291   80 YLVKQGNEPPTFTGYFHAWD 99
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 191-283 1.86e-40

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


:

Pssm-ID: 200445  Cd Length: 92  Bit Score: 143.53  E-value: 1.86e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765046 191 ETRLFQVKGKRNVRVRQVNLSVSSMNTGDCFILDAGSDIYVYVGSQAKRVEKLKAISAANQIRDQDHNGRARVQIVDDFS 270
Cdd:cd11289    1 KPRLLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKVIVLDEGD 80

                         90
                 ....*....|...
gi 386765046 271 TDaDKQHFFDVLG 283
Cdd:cd11289   81 TN-ESPEFWKVLG 92
ADF_gelsolin super family cl15697
Actin depolymerization factor/cofilin- and gelsolin-like domains; Actin depolymerization ...
 569-661 6.41e-22

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


The actual alignment was detected with superfamily member cd11288:

Pssm-ID: 472830  Cd Length: 92  Bit Score: 90.75  E-value: 6.41e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765046 569 TAQLFRIRGTVESDVHASEVAADSSSLASSDAFVLHSGKShkIYIWNGLGASAFEKQAAVDRFSDYWDDVELEQVEEGAE 648
Cdd:cd11288    2 PTRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKTPSS--VYLWVGKGSSEDERELAKDVASFLKPKASLQEVAEGSE 79

                         90
                 ....*....|...
gi 386765046 649 PDEFWEELNGEGQ 661
Cdd:cd11288   80 PDEFWEALGGKSE 92
ADF_gelsolin super family cl15697
Actin depolymerization factor/cofilin- and gelsolin-like domains; Actin depolymerization ...
 470-558 1.39e-04

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


The actual alignment was detected with superfamily member smart00262:

Pssm-ID: 472830 [Multi-domain]  Cd Length: 90  Bit Score: 41.12  E-value: 1.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765046   470 GSDEIVVSTVPFDEKLpLLGFASYVLtynyeanngDTGSLTYVWHGVKASAAARKRAFE--EGLVGSKDGLLVQT---NQ 544
Cdd:smart00262   7 GKRNVRVPEVPFSQGS-LNSGDCYIL---------DTGSEIYVWVGKKSSQDEKKKAAElaVELDDTLGPGPVQVrvvDE 76

                           90
                   ....*....|....
gi 386765046   545 GHEPRHFYKIFKGK 558
Cdd:smart00262  77 GKEPPEFWSLFGGW 90
 
Name Accession Description Interval E-value
gelsolin_S1_like cd11290
Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; ...
 63-176 3.39e-61

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: 201.68  E-value: 3.39e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765046  63 FANAGRTPGLEIWRIENFEPVIYPKTNYGKFYTGDSFIVLNTIENKKDKkLSWDVHFWLGLETSTDEAGAAAILTVQLDD 142
Cdd:cd11290    1 FEGVGQKPGLQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDPSGS-LSYDIHYWLGKEASQDEAGAAAIKAVELDD 79

                         90       100       110
                 ....*....|....*....|....*....|....
gi 386765046 143 LLNGGPVQHREVQDHESQLFLSYFKNGIRYEQGG 176
Cdd:cd11290   80 YLGGRPVQHREVQGHESEEFLSYFKKGIIYIEGG 113
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 307-404 2.03e-45

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: 157.80  E-value: 2.03e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765046 307 AAAVSLYKVSDASGKLKVDIIGQKPLTQAMLDTRECFILDTGSGIFVWVGKGATQKEKTDAMAKAQEFLRTKKYPAWTQI 386
Cdd:cd11292    1 AEQKKLYKVSDASGKLKLTEVAEGSLNQEMLDSEDCYILDCGSEIFVWVGKGASLDERKAALKNAEEFLRKKKRPPYTQV 80

                         90
                 ....*....|....*...
gi 386765046 387 HRIVEGSESAPFKQYFDT 404
Cdd:cd11292   81 TRVTEGGESALFKSKFAN 98
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 675-774 7.75e-43

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: 150.53  E-value: 7.75e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765046 675 ESRLFHCHLSSGgFLKVEEVAQYEQEDLDSDDIMLLDAGDEIYLWVGYGVSEEENGKLLDTAKLYFNLEPTARSFDTVSI 754
Cdd:cd11291    1 KPRLFRCSNESG-FFKVEEISDFSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYIETDPLGRSKPRTPI 79

                         90       100
                 ....*....|....*....|
gi 386765046 755 IRVPQGKEPRVFKRMFPNWD 774
Cdd:cd11291   80 YLVKQGNEPPTFTGYFHAWD 99
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 191-283 1.86e-40

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


Pssm-ID: 200445  Cd Length: 92  Bit Score: 143.53  E-value: 1.86e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765046 191 ETRLFQVKGKRNVRVRQVNLSVSSMNTGDCFILDAGSDIYVYVGSQAKRVEKLKAISAANQIRDQDHNGRARVQIVDDFS 270
Cdd:cd11289    1 KPRLLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKVIVLDEGD 80

                         90
                 ....*....|...
gi 386765046 271 TDaDKQHFFDVLG 283
Cdd:cd11289   81 TN-ESPEFWKVLG 92
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 314-405 9.34e-27

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 104.30  E-value: 9.34e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765046   314 KVSDASGKLKVDIIgQKPLTQAMLDTRECFILDTGSGIFVWVGKGATQKEKTDAMAKAQEFLRTKKyPAWTQIHRIVEGS 393
Cdd:smart00262   1 FLVRVKGKRNVRVP-EVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLG-PGPVQVRVVDEGK 78

                           90
                   ....*....|..
gi 386765046   394 ESAPFKQYFDTW 405
Cdd:smart00262  79 EPPEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 193-285 3.24e-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: 102.76  E-value: 3.24e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765046   193 RLFQVKGKRNVRVRQVNLSVSSMNTGDCFILDAGSDIYVYVGSQAKRVEKLKAISAANQIRDQDHNGRARVQIVDDFSTD 272
Cdd:smart00262   1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVRVVDEGKEP 80

                           90
                   ....*....|...
gi 386765046   273 AdkqHFFDVLGSG 285
Cdd:smart00262  81 P---EFWSLFGGW 90
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 569-661 6.41e-22

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: 90.75  E-value: 6.41e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765046 569 TAQLFRIRGTVESDVHASEVAADSSSLASSDAFVLHSGKShkIYIWNGLGASAFEKQAAVDRFSDYWDDVELEQVEEGAE 648
Cdd:cd11288    2 PTRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKTPSS--VYLWVGKGSSEDERELAKDVASFLKPKASLQEVAEGSE 79

                         90
                 ....*....|...
gi 386765046 649 PDEFWEELNGEGQ 661
Cdd:cd11288   80 PDEFWEALGGKSE 92
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 679-773 3.62e-20

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 85.81  E-value: 3.62e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765046   679 FHCHLSSGGFLKVEEVAqYEQEDLDSDDIMLLDAGDEIYLWVGYGVSEEENGKLLDTAKLYFNLEPtarsFDTVSIIRVP 758
Cdd:smart00262   1 FLVRVKGKRNVRVPEVP-FSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLG----PGPVQVRVVD 75

                           90
                   ....*....|....*
gi 386765046   759 QGKEPRVFKRMFPNW 773
Cdd:smart00262  76 EGKEPPEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 73-169 1.32e-19

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: 83.88  E-value: 1.32e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765046    73 EIWRIENFE--PVIYPKTNYGKFYTGDSFIVLNTienkkdkklsWDVHFWLGLETSTDEAGAAAILTVQLDDLLNGGPVQ 150
Cdd:smart00262   1 FLVRVKGKRnvRVPEVPFSQGSLNSGDCYILDTG----------SEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQ 70

                           90       100
                   ....*....|....*....|
gi 386765046   151 HREV-QDHESQLFLSYFKNG 169
Cdd:smart00262  71 VRVVdEGKEPPEFWSLFGGW 90
Gelsolin pfam00626
Gelsolin repeat;
331-399 1.04e-13

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 66.95  E-value: 1.04e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386765046  331 PLTQAMLDTRECFILDTGSGIFVWVGKGATQKEKTDAMAKAQEfLRTKKYPAWTQIHRIVEGSESAPFK 399
Cdd:pfam00626   9 PLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQ-LDDDERFPLPEVIRVPQGKEPARFL 76
Gelsolin pfam00626
Gelsolin repeat;
201-268 1.70e-13

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 66.18  E-value: 1.70e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386765046  201 RNVRVRQVNLSVSSMNTGDCFILDAGSDIYVYVGSQAKRVEKLKAISAANQIRDQDHNGRARVQIVDD 268
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDERFPLPEVIRVPQ 68
Gelsolin pfam00626
Gelsolin repeat;
690-767 1.10e-11

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 61.17  E-value: 1.10e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386765046  690 KVEEVAQYEQEDLDSDDIMLLDAGDEIYLWVGYGVSEEENGKLLDTAKLYfnlePTARSFDTVSIIRVPQGKEPRVFK 767
Cdd:pfam00626   3 VLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQL----DDDERFPLPEVIRVPQGKEPARFL 76
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 573-658 2.20e-09

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: 54.99  E-value: 2.20e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765046   573 FRIRGTVESDVHASEVAADSSSLASSDAFVLHSGksHKIYIWNGLGASAFEKQAAVDRFSDYWDD-----VELEQVEEGA 647
Cdd:smart00262   1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTG--SEIYVWVGKKSSQDEKKKAAELAVELDDTlgpgpVQVRVVDEGK 78

                           90
                   ....*....|.
gi 386765046   648 EPDEFWEELNG 658
Cdd:smart00262  79 EPPEFWSLFGG 89
Gelsolin pfam00626
Gelsolin repeat;
79-163 5.68e-09

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 53.47  E-value: 5.68e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765046   79 NFEPVIYPKTNYGKFYTGDSFIVLNTIenkkdkklswDVHFWLGLETSTDEAGAAAILTVQLDDL-LNGGPVQHREVQDH 157
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNGF----------TIFLWVGKGSSLLEKLFAALLAAQLDDDeRFPLPEVIRVPQGK 70


                  ....*.
gi 386765046  158 ESQLFL 163
Cdd:pfam00626  71 EPARFL 76
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 470-558 1.39e-04

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: 41.12  E-value: 1.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765046   470 GSDEIVVSTVPFDEKLpLLGFASYVLtynyeanngDTGSLTYVWHGVKASAAARKRAFE--EGLVGSKDGLLVQT---NQ 544
Cdd:smart00262   7 GKRNVRVPEVPFSQGS-LNSGDCYIL---------DTGSEIYVWVGKKSSQDEKKKAAElaVELDDTLGPGPVQVrvvDE 76

                           90
                   ....*....|....
gi 386765046   545 GHEPRHFYKIFKGK 558
Cdd:smart00262  77 GKEPPEFWSLFGGW 90
Gelsolin pfam00626
Gelsolin repeat;
601-653 9.46e-03

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 35.75  E-value: 9.46e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 386765046  601 FVLHSGKshKIYIWNGLGASAFEKQAAVDRFSDYWDD-----VELEQVEEGAEPDEFW 653
Cdd:pfam00626  21 YLLDNGF--TIFLWVGKGSSLLEKLFAALLAAQLDDDerfplPEVIRVPQGKEPARFL 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; ...
 63-176 3.39e-61

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: 201.68  E-value: 3.39e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765046  63 FANAGRTPGLEIWRIENFEPVIYPKTNYGKFYTGDSFIVLNTIENKKDKkLSWDVHFWLGLETSTDEAGAAAILTVQLDD 142
Cdd:cd11290    1 FEGVGQKPGLQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDPSGS-LSYDIHYWLGKEASQDEAGAAAIKAVELDD 79

                         90       100       110
                 ....*....|....*....|....*....|....
gi 386765046 143 LLNGGPVQHREVQDHESQLFLSYFKNGIRYEQGG 176
Cdd:cd11290   80 YLGGRPVQHREVQGHESEEFLSYFKKGIIYIEGG 113
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 307-404 2.03e-45

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: 157.80  E-value: 2.03e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765046 307 AAAVSLYKVSDASGKLKVDIIGQKPLTQAMLDTRECFILDTGSGIFVWVGKGATQKEKTDAMAKAQEFLRTKKYPAWTQI 386
Cdd:cd11292    1 AEQKKLYKVSDASGKLKLTEVAEGSLNQEMLDSEDCYILDCGSEIFVWVGKGASLDERKAALKNAEEFLRKKKRPPYTQV 80

                         90
                 ....*....|....*...
gi 386765046 387 HRIVEGSESAPFKQYFDT 404
Cdd:cd11292   81 TRVTEGGESALFKSKFAN 98
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 675-774 7.75e-43

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: 150.53  E-value: 7.75e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765046 675 ESRLFHCHLSSGgFLKVEEVAQYEQEDLDSDDIMLLDAGDEIYLWVGYGVSEEENGKLLDTAKLYFNLEPTARSFDTVSI 754
Cdd:cd11291    1 KPRLFRCSNESG-FFKVEEISDFSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYIETDPLGRSKPRTPI 79

                         90       100
                 ....*....|....*....|
gi 386765046 755 IRVPQGKEPRVFKRMFPNWD 774
Cdd:cd11291   80 YLVKQGNEPPTFTGYFHAWD 99
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 191-283 1.86e-40

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


Pssm-ID: 200445  Cd Length: 92  Bit Score: 143.53  E-value: 1.86e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765046 191 ETRLFQVKGKRNVRVRQVNLSVSSMNTGDCFILDAGSDIYVYVGSQAKRVEKLKAISAANQIRDQDHNGRARVQIVDDFS 270
Cdd:cd11289    1 KPRLLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKVIVLDEGD 80

                         90
                 ....*....|...
gi 386765046 271 TDaDKQHFFDVLG 283
Cdd:cd11289   81 TN-ESPEFWKVLG 92
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 314-405 9.34e-27

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 104.30  E-value: 9.34e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765046   314 KVSDASGKLKVDIIgQKPLTQAMLDTRECFILDTGSGIFVWVGKGATQKEKTDAMAKAQEFLRTKKyPAWTQIHRIVEGS 393
Cdd:smart00262   1 FLVRVKGKRNVRVP-EVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLG-PGPVQVRVVDEGK 78

                           90
                   ....*....|..
gi 386765046   394 ESAPFKQYFDTW 405
Cdd:smart00262  79 EPPEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 193-285 3.24e-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: 102.76  E-value: 3.24e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765046   193 RLFQVKGKRNVRVRQVNLSVSSMNTGDCFILDAGSDIYVYVGSQAKRVEKLKAISAANQIRDQDHNGRARVQIVDDFSTD 272
Cdd:smart00262   1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVRVVDEGKEP 80

                           90
                   ....*....|...
gi 386765046   273 AdkqHFFDVLGSG 285
Cdd:smart00262  81 P---EFWSLFGGW 90
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
 72-166 9.99e-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: 96.19  E-value: 9.99e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765046  72 LEIWRIENFEPVIYPKTNYGKFYTGDSFIVLNT-IENKKDKKLswdVHFWLGLETSTDEAGAAAILTVQLDDLLNGGPVQ 150
Cdd:cd11293    9 VEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTyQGGGKEEHI---LYFWQGRHSSQDERAAAALLTVELDEELKGRAVQ 85

                         90
                 ....*....|....*.
gi 386765046 151 HREVQDHESQLFLSYF 166
Cdd:cd11293   86 VRVVQGKEPPHFLALF 101
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 569-661 6.41e-22

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: 90.75  E-value: 6.41e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765046 569 TAQLFRIRGTVESDVHASEVAADSSSLASSDAFVLHSGKShkIYIWNGLGASAFEKQAAVDRFSDYWDDVELEQVEEGAE 648
Cdd:cd11288    2 PTRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKTPSS--VYLWVGKGSSEDERELAKDVASFLKPKASLQEVAEGSE 79

                         90
                 ....*....|...
gi 386765046 649 PDEFWEELNGEGQ 661
Cdd:cd11288   80 PDEFWEALGGKSE 92
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 679-773 3.62e-20

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 85.81  E-value: 3.62e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765046   679 FHCHLSSGGFLKVEEVAqYEQEDLDSDDIMLLDAGDEIYLWVGYGVSEEENGKLLDTAKLYFNLEPtarsFDTVSIIRVP 758
Cdd:smart00262   1 FLVRVKGKRNVRVPEVP-FSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLG----PGPVQVRVVD 75

                           90
                   ....*....|....*
gi 386765046   759 QGKEPRVFKRMFPNW 773
Cdd:smart00262  76 EGKEPPEFWSLFGGW 90
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 312-405 1.19e-19

Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200447 [Multi-domain]  Cd Length: 99  Bit Score: 84.66  E-value: 1.19e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765046 312 LYKVSDASGKLKVDIIGqkPLTQAMLDTRECFILDTGSGIFVWVGKGATQKEKTDAMAKAQEFL---RTKKYPAWTQIHR 388
Cdd:cd11291    4 LFRCSNESGFFKVEEIS--DFSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYIetdPLGRSKPRTPIYL 81

                         90
                 ....*....|....*..
gi 386765046 389 IVEGSESAPFKQYFDTW 405
Cdd:cd11291   82 VKQGNEPPTFTGYFHAW 98
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 73-169 1.32e-19

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: 83.88  E-value: 1.32e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765046    73 EIWRIENFE--PVIYPKTNYGKFYTGDSFIVLNTienkkdkklsWDVHFWLGLETSTDEAGAAAILTVQLDDLLNGGPVQ 150
Cdd:smart00262   1 FLVRVKGKRnvRVPEVPFSQGSLNSGDCYILDTG----------SEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQ 70

                           90       100
                   ....*....|....*....|
gi 386765046   151 HREV-QDHESQLFLSYFKNG 169
Cdd:smart00262  71 VRVVdEGKEPPEFWSLFGGW 90
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 336-402 1.81e-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: 69.32  E-value: 1.81e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386765046 336 MLDTRECFILDTGSGIFVWVGKGATQKEKTdAMAKAQEFLRTKKYPAwTQIHRIVEGSESAPFKQYF 402
Cdd:cd11280   24 SLDSDDVFVLDTGSEIYIWQGRASSQAELA-AAALLAKELDEERKGK-PEIVRIRQGQEPREFWSLF 88
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 677-770 4.27e-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: 68.16  E-value: 4.27e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765046 677 RLFHCHLSSGGflKVEEVAQYEqEDLDSDDIMLLDAGDEIYLWVGYGVSEEENGKLLDTAKlyfnlEPTARSFDTVSIIR 756
Cdd:cd11280    3 RLYRVRGSKAI--EIEEVPLAS-SSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAK-----ELDEERKGKPEIVR 74

                         90
                 ....*....|....
gi 386765046 757 VPQGKEPRVFKRMF 770
Cdd:cd11280   75 IRQGQEPREFWSLF 88
Gelsolin pfam00626
Gelsolin repeat;
331-399 1.04e-13

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 66.95  E-value: 1.04e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386765046  331 PLTQAMLDTRECFILDTGSGIFVWVGKGATQKEKTDAMAKAQEfLRTKKYPAWTQIHRIVEGSESAPFK 399
Cdd:pfam00626   9 PLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQ-LDDDERFPLPEVIRVPQGKEPARFL 76
Gelsolin pfam00626
Gelsolin repeat;
201-268 1.70e-13

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 66.18  E-value: 1.70e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386765046  201 RNVRVRQVNLSVSSMNTGDCFILDAGSDIYVYVGSQAKRVEKLKAISAANQIRDQDHNGRARVQIVDD 268
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDERFPLPEVIRVPQ 68
Gelsolin pfam00626
Gelsolin repeat;
690-767 1.10e-11

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 61.17  E-value: 1.10e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386765046  690 KVEEVAQYEQEDLDSDDIMLLDAGDEIYLWVGYGVSEEENGKLLDTAKLYfnlePTARSFDTVSIIRVPQGKEPRVFK 767
Cdd:pfam00626   3 VLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQL----DDDERFPLPEVIRVPQGKEPARFL 76
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 192-266 1.80e-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: 60.84  E-value: 1.80e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386765046 192 TRLFQVKGKRNVRVRQVNLSVSSMNTGDCFILDAGSDIYVYVGSQAKRVEKLKAISAANQIRDQDhNGRARVQIV 266
Cdd:cd11280    2 PRLYRVRGSKAIEIEEVPLASSSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKELDEER-KGKPEIVRI 75
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 191-286 3.92e-11

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


Pssm-ID: 200444  Cd Length: 92  Bit Score: 59.94  E-value: 3.92e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765046 191 ETRLFQVKG--KRNVRVRQVNLSVSSMNTGDCFILDAGSDIYVYVGSQAKRVEKLKAISAANQIRDqdhngRARVQIVDD 268
Cdd:cd11288    2 PTRLFQVRGngSGNTRAVEVDADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVASFLKP-----KASLQEVAE 76

                         90
                 ....*....|....*...
gi 386765046 269 FSTDAdkqHFFDVLGSGS 286
Cdd:cd11288   77 GSEPD---EFWEALGGKS 91
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 685-772 6.97e-11

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: 59.57  E-value: 6.97e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765046 685 SGGFLKVEEVAQYE--QEDLDSDDIMLLDAGDEIYLWVGYGVSEEENGKLLDTAKLYFNlePTARSfDTVSIIRVPQGKE 762
Cdd:cd11292   12 ASGKLKLTEVAEGSlnQEMLDSEDCYILDCGSEIFVWVGKGASLDERKAALKNAEEFLR--KKKRP-PYTQVTRVTEGGE 88

                         90
                 ....*....|
gi 386765046 763 PRVFKRMFPN 772
Cdd:cd11292   89 SALFKSKFAN 98
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 573-658 2.20e-09

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: 54.99  E-value: 2.20e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765046   573 FRIRGTVESDVHASEVAADSSSLASSDAFVLHSGksHKIYIWNGLGASAFEKQAAVDRFSDYWDD-----VELEQVEEGA 647
Cdd:smart00262   1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTG--SEIYVWVGKKSSQDEKKKAAELAVELDDTlgpgpVQVRVVDEGK 78

                           90
                   ....*....|.
gi 386765046   648 EPDEFWEELNG 658
Cdd:smart00262  79 EPPEFWSLFGG 89
Gelsolin pfam00626
Gelsolin repeat;
79-163 5.68e-09

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 53.47  E-value: 5.68e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765046   79 NFEPVIYPKTNYGKFYTGDSFIVLNTIenkkdkklswDVHFWLGLETSTDEAGAAAILTVQLDDL-LNGGPVQHREVQDH 157
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNGF----------TIFLWVGKGSSLLEKLFAALLAAQLDDDeRFPLPEVIRVPQGK 70


                  ....*.
gi 386765046  158 ESQLFL 163
Cdd:pfam00626  71 EPARFL 76
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 336-398 7.29e-09

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: 53.39  E-value: 7.29e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386765046 336 MLDTRECFILDTGSGIFVWVGKGATQKEKtdAMAKAQ-EFLRTKkypawTQIHRIVEGSESAPF 398
Cdd:cd11288   27 SLNSNDVFVLKTPSSVYLWVGKGSSEDER--ELAKDVaSFLKPK-----ASLQEVAEGSEPDEF 83
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 74-166 1.15e-08

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: 52.76  E-value: 1.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765046  74 IWRIE-----NFEPVIyPKTNygKFYTGDSFIVLNTIEnkkdkklswdVHFWLGLETSTDEAGAAAILTVQLDDLLNGGP 148
Cdd:cd11280    4 LYRVRgskaiEIEEVP-LASS--SLDSDDVFVLDTGSE----------IYIWQGRASSQAELAAAALLAKELDEERKGKP 70

                         90
                 ....*....|....*...
gi 386765046 149 VQHREVQDHESQLFLSYF 166
Cdd:cd11280   71 EIVRIRQGQEPREFWSLF 88
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 191-249 3.22e-07

Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200447 [Multi-domain]  Cd Length: 99  Bit Score: 49.22  E-value: 3.22e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386765046 191 ETRLFQVKGKR-NVRVRQV-NLSVSSMNTGDCFILDAGSDIYVYVGSQAKRVEKLKAISAA 249
Cdd:cd11291    1 KPRLFRCSNESgFFKVEEIsDFSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSA 61
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 677-766 7.53e-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: 42.22  E-value: 7.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765046 677 RLFHCHLSSGGFLK---VEEVAqyeqEDLDSDDIMLLDAGDEIYLWVGYGVSEEENGKLLDTAKLYfnleptarsFDTVS 753
Cdd:cd11288    4 RLFQVRGNGSGNTRaveVDADA----SSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVASFL---------KPKAS 70

                         90
                 ....*....|...
gi 386765046 754 IIRVPQGKEPRVF 766
Cdd:cd11288   71 LQEVAEGSEPDEF 83
gelsolin_S1_like cd11290
Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; ...
 351-404 1.05e-04

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: 42.21  E-value: 1.05e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 386765046 351 IFVWVGKGATQKEKTDAMAKAQE---FLRTKkypawTQIHRIVEGSESAPFKQYFDT 404
Cdd:cd11290   54 IHYWLGKEASQDEAGAAAIKAVElddYLGGR-----PVQHREVQGHESEEFLSYFKK 105
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 470-558 1.39e-04

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: 41.12  E-value: 1.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765046   470 GSDEIVVSTVPFDEKLpLLGFASYVLtynyeanngDTGSLTYVWHGVKASAAARKRAFE--EGLVGSKDGLLVQT---NQ 544
Cdd:smart00262   7 GKRNVRVPEVPFSQGS-LNSGDCYIL---------DTGSEIYVWVGKKSSQDEKKKAAElaVELDDTLGPGPVQVrvvDE 76

                           90
                   ....*....|....
gi 386765046   545 GHEPRHFYKIFKGK 558
Cdd:smart00262  77 GKEPPEFWSLFGGW 90
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 571-654 8.15e-04

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: 39.27  E-value: 8.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765046 571 QLFRIRGtvESDVHASEVAADSSSLASSDAFVLHSGKshKIYIWNGLGASAFEKQAAVD---RFSDYWDDV-ELEQVEEG 646
Cdd:cd11280    3 RLYRVRG--SKAIEIEEVPLASSSLDSDDVFVLDTGS--EIYIWQGRASSQAELAAAALlakELDEERKGKpEIVRIRQG 78


                 ....*...
gi 386765046 647 AEPDEFWE 654
Cdd:cd11280   79 QEPREFWS 86
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 677-737 1.41e-03

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


Pssm-ID: 200445  Cd Length: 92  Bit Score: 38.37  E-value: 1.41e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386765046 677 RLFHCHlsSGGFLKVEEVAqYEQEDLDSDDIMLLDAGDEIYLWVGYGVSEEENGKLLDTAK 737
Cdd:cd11289    3 RLLHVK--GRRNVRAREVE-LSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQ 60
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 572-656 2.84e-03

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


Pssm-ID: 200445  Cd Length: 92  Bit Score: 37.60  E-value: 2.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386765046 572 LFRIRGtvESDVHASEVAADSSSLASSDAFVLHSGksHKIYIWNGLGASAFEKQAAVDrFSDYWDDVE------LEQVEE 645
Cdd:cd11289    4 LLHVKG--RRNVRAREVELSWSSLNSGDVFILDLG--STIYQWNGSKSNRFEKAKAMQ-LAQGIRDERrlgrakVIVLDE 78

                         90
                 ....*....|...
gi 386765046 646 GA--EPDEFWEEL 656
Cdd:cd11289   79 GDtnESPEFWKVL 91
Gelsolin pfam00626
Gelsolin repeat;
601-653 9.46e-03

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 35.75  E-value: 9.46e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 386765046  601 FVLHSGKshKIYIWNGLGASAFEKQAAVDRFSDYWDD-----VELEQVEEGAEPDEFW 653
Cdd:pfam00626  21 YLLDNGF--TIFLWVGKGSSLLEKLFAALLAAQLDDDerfplPEVIRVPQGKEPARFL 76
 
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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