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Conserved domains on  [gi|18405794|ref|NP_565958|]
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villin 2 [Arabidopsis thaliana]

Protein Classification

gelsolin_S1_like and gelsolin_S6_like domain-containing protein( domain architecture ID 12972108)

protein containing domains gelsolin_S1_like, gelsolin_S2_like, gelsolin_S4_like, and gelsolin_S6_like

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; ...
 10-122 2.35e-65

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: 214.78  E-value: 2.35e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405794  10 FQGAGQKPGTEIWRIENFEAVPVPKSEHGKFYMGDTYIVLQTTQNKGGAYLFDIHFWIGKDTSQDEAGTAAVKTVELDAV 89
Cdd:cd11290   1 FEGVGQKPGLQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDPSGSLSYDIHYWLGKEASQDEAGAAAIKAVELDDY 80

                        90       100       110
                ....*....|....*....|....*....|...
gi 18405794  90 LGGRAVQHREIQGHESDKFLSYFKPCIIPLEGG 122
Cdd:cd11290  81 LGGRPVQHREVQGHESEEFLSYFKKGIIYIEGG 113
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 620-718 1.15e-42

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: 1.15e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405794 620 DPHLFSFAFNRGKFQVEEIYNFAQDDLLTEDIYFLDTHAEVFVWVGQCVEPKEKQTVFEIGQKYIDLAGSLEGLhPKVPI 699
Cdd:cd11291   1 KPRLFRCSNESGFFKVEEISDFSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYIETDPLGRSK-PRTPI 79

                        90       100
                ....*....|....*....|
gi 18405794 700 YKINEGNEPCFFTTYF-SWD 718
Cdd:cd11291  80 YLVKQGNEPPTFTGYFhAWD 99
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
 384-485 4.81e-41

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: 145.88  E-value: 4.81e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405794 384 PLLESGGKLEVWYVNGKVKTPLPKEDIGKLYSGDCYLVLYTYHSGeRKDEYFLSCWFGKKSIPEDQDTAIRLANTMSNSL 463
Cdd:cd11293   1 MYDDGSGKVEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQGG-GKEEHILYFWQGRHSSQDERAAAALLTVELDEEL 79

                        90       100
                ....*....|....*....|..
gi 18405794 464 KGRPVQGRIYEGKEPPQFVALF 485
Cdd:cd11293  80 KGRAVQVRVVQGKEPPHFLALF 101
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 136-230 3.24e-35

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: 128.89  E-value: 3.24e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405794 136 ETRLYTCKGKRAIRLKQVPFARSSLNHDDVFILDTEEKIYQFNGANSNIQERAKALEVVQYLKDKYHEGTCDVAIVDDGK 215
Cdd:cd11289   1 KPRLLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKVIVLDEGD 80

                        90
                ....*....|....*
gi 18405794 216 ldtESDSGAFWVLFG 230
Cdd:cd11289  81 ---TNESPEFWKVLG 92
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 252-341 9.38e-33

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: 121.97  E-value: 9.38e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405794 252 PKLYCITD--GKME--PI-DGDLSKSMLENTKCYLLDCGAEIYIWVGRVTQVDERKAASQSAEEFLASENRPKATHVTRV 326
Cdd:cd11292   4 KKLYKVSDasGKLKltEVaEGSLNQEMLDSEDCYILDCGSEIFVWVGKGASLDERKAALKNAEEFLRKKKRPPYTQVTRV 83

                        90
                ....*....|....*
gi 18405794 327 IQGYESHSFKSNFDS 341
Cdd:cd11292  84 TEGGESALFKSKFAN 98
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 517-607 1.48e-32

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: 121.18  E-value: 1.48e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405794 517 SIALVQVSGTGVHNNKAVQVETVATSLNSYECFLLQSGTSMFLWHGNQSTHEQLELATKVAEFLKPGITLKHAKEGTESS 596
Cdd:cd11288   2 PTRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVASFLKPKASLQEVAEGSEPD 81

                        90
                ....*....|.
gi 18405794 597 TFWFALGGKQN 607
Cdd:cd11288  82 EFWEALGGKSE 92
VHP pfam02209
Villin headpiece domain;
941-976 2.13e-13

Villin headpiece domain;


:

Pssm-ID: 460493  Cd Length: 36  Bit Score: 64.71  E-value: 2.13e-13
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 18405794   941 YLSEEEFQSVFGIEKEAFNNLPRWKQDLLKKKFDLF 976
Cdd:pfam02209   1 YLSDEDFEEVFGMSREEFYKLPKWKQNNLKKKAGLF 36
DUF4045 super family cl38397
Domain of unknown function (DUF4045); This presumed domain is functionally uncharacterized. ...
 843-952 3.87e-03

Domain of unknown function (DUF4045); This presumed domain is functionally uncharacterized. This domain family is found in bacteria and eukaryotes, and is typically between 384 and 430 amino acids in length.


The actual alignment was detected with superfamily member pfam13254:

Pssm-ID: 433066 [Multi-domain]  Cd Length: 415  Bit Score: 40.92  E-value: 3.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405794   843 NKKSPDTSPTRRSTSSNPADDIPLTEAKDEEEA---SEVAGLEAKEEEEVSPAADETEAKQ-----ETEEQGDSEIQPSG 914
Cdd:pfam13254 242 DTLSTDKEQSPAPTSASEPPPKTKELPKDSEEPaapSKSAEASTEKKEPDTESSPETSSEKsapslLSPVSKASIDKPLS 321

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 18405794   915 ATFTYEQL-RAKSENPVtgIDF----KRREAyLSEE------EFQSVFG 952
Cdd:pfam13254 322 SPDRDPLSpKPKPQSPP--KDFranlRSREV-PKDKskkdepEFKNVFG 367
 
Name Accession Description Interval E-value
gelsolin_S1_like cd11290
Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; ...
 10-122 2.35e-65

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: 214.78  E-value: 2.35e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405794  10 FQGAGQKPGTEIWRIENFEAVPVPKSEHGKFYMGDTYIVLQTTQNKGGAYLFDIHFWIGKDTSQDEAGTAAVKTVELDAV 89
Cdd:cd11290   1 FEGVGQKPGLQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDPSGSLSYDIHYWLGKEASQDEAGAAAIKAVELDDY 80

                        90       100       110
                ....*....|....*....|....*....|...
gi 18405794  90 LGGRAVQHREIQGHESDKFLSYFKPCIIPLEGG 122
Cdd:cd11290  81 LGGRPVQHREVQGHESEEFLSYFKKGIIYIEGG 113
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 620-718 1.15e-42

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: 1.15e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405794 620 DPHLFSFAFNRGKFQVEEIYNFAQDDLLTEDIYFLDTHAEVFVWVGQCVEPKEKQTVFEIGQKYIDLAGSLEGLhPKVPI 699
Cdd:cd11291   1 KPRLFRCSNESGFFKVEEISDFSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYIETDPLGRSK-PRTPI 79

                        90       100
                ....*....|....*....|
gi 18405794 700 YKINEGNEPCFFTTYF-SWD 718
Cdd:cd11291  80 YLVKQGNEPPTFTGYFhAWD 99
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
 384-485 4.81e-41

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: 145.88  E-value: 4.81e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405794 384 PLLESGGKLEVWYVNGKVKTPLPKEDIGKLYSGDCYLVLYTYHSGeRKDEYFLSCWFGKKSIPEDQDTAIRLANTMSNSL 463
Cdd:cd11293   1 MYDDGSGKVEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQGG-GKEEHILYFWQGRHSSQDERAAAALLTVELDEEL 79

                        90       100
                ....*....|....*....|..
gi 18405794 464 KGRPVQGRIYEGKEPPQFVALF 485
Cdd:cd11293  80 KGRAVQVRVVQGKEPPHFLALF 101
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 136-230 3.24e-35

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: 128.89  E-value: 3.24e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405794 136 ETRLYTCKGKRAIRLKQVPFARSSLNHDDVFILDTEEKIYQFNGANSNIQERAKALEVVQYLKDKYHEGTCDVAIVDDGK 215
Cdd:cd11289   1 KPRLLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKVIVLDEGD 80

                        90
                ....*....|....*
gi 18405794 216 ldtESDSGAFWVLFG 230
Cdd:cd11289  81 ---TNESPEFWKVLG 92
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 252-341 9.38e-33

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: 121.97  E-value: 9.38e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405794 252 PKLYCITD--GKME--PI-DGDLSKSMLENTKCYLLDCGAEIYIWVGRVTQVDERKAASQSAEEFLASENRPKATHVTRV 326
Cdd:cd11292   4 KKLYKVSDasGKLKltEVaEGSLNQEMLDSEDCYILDCGSEIFVWVGKGASLDERKAALKNAEEFLRKKKRPPYTQVTRV 83

                        90
                ....*....|....*
gi 18405794 327 IQGYESHSFKSNFDS 341
Cdd:cd11292  84 TEGGESALFKSKFAN 98
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 517-607 1.48e-32

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: 121.18  E-value: 1.48e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405794 517 SIALVQVSGTGVHNNKAVQVETVATSLNSYECFLLQSGTSMFLWHGNQSTHEQLELATKVAEFLKPGITLKHAKEGTESS 596
Cdd:cd11288   2 PTRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVASFLKPKASLQEVAEGSEPD 81

                        90
                ....*....|.
gi 18405794 597 TFWFALGGKQN 607
Cdd:cd11288  82 EFWEALGGKSE 92
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 138-231 1.81e-24

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 98.13  E-value: 1.81e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405794    138 RLYTCKGKRAIRLKQVPFARSSLNHDDVFILDTEEKIYQFNGANSNIQERAKALEVVQYLKDKYHEGTCDVAIVDDGKld 217
Cdd:smart00262   1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVRVVDEGK-- 78

                           90
                   ....*....|....
gi 18405794    218 tESDSgaFWVLFGG 231
Cdd:smart00262  79 -EPPE--FWSLFGG 89
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 20-115 4.97e-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: 85.42  E-value: 4.97e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405794     20 EIWRIENFEAVPVPKSE--HGKFYMGDTYIVLQTTqnkggaylfDIHFWIGKDTSQDEAGTAAVKTVELDAVLGGRAVQH 97
Cdd:smart00262   1 FLVRVKGKRNVRVPEVPfsQGSLNSGDCYILDTGS---------EIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQV 71

                           90
                   ....*....|....*....
gi 18405794     98 REI-QGHESDKFLSYFKPC 115
Cdd:smart00262  72 RVVdEGKEPPEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 259-342 3.95e-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: 83.11  E-value: 3.95e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405794    259 DGKMEPIDGDLSKSMLENTKCYLLDCGAEIYIWVGRVTQVDERKAASQSAEEFLASEnRPKATHVTRVIQGYESHSFKSN 338
Cdd:smart00262   8 KRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTL-GPGPVQVRVVDEGKEPPEFWSL 86


                   ....
gi 18405794    339 FDSW 342
Cdd:smart00262  87 FGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 631-715 2.49e-18

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 80.80  E-value: 2.49e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405794    631 GKFQVEEIY-NFAQDDLLTEDIYFLDTHAEVFVWVGQCVEPKEKQTVFEIGQKYIDLAGSleglhPKVPIYKINEGNEPC 709
Cdd:smart00262   7 GKRNVRVPEvPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGP-----GPVQVRVVDEGKEPP 81


                   ....*.
gi 18405794    710 FFTTYF 715
Cdd:smart00262  82 EFWSLF 87
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 393-486 4.70e-17

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 76.95  E-value: 4.70e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405794    393 EVWYVNGKVKTPLP--KEDIGKLYSGDCYLVLYTYHSgerkdeYFlscWFGKKSIPEDQDTAIRLANTMSNSLKGRPVQG 470
Cdd:smart00262   1 FLVRVKGKRNVRVPevPFSQGSLNSGDCYILDTGSEI------YV---WVGKKSSQDEKKKAAELAVELDDTLGPGPVQV 71

                           90
                   ....*....|....*..
gi 18405794    471 RIY-EGKEPPQFVALFQ 486
Cdd:smart00262  72 RVVdEGKEPPEFWSLFG 88
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 522-605 1.22e-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: 75.79  E-value: 1.22e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405794    522 QVSGTGVHNNKAVQVETVATSLNSYECFLLQSGTSMFLWHGNQSTHEQLELATKVAEFL----KPGITLKH-AKEGTESS 596
Cdd:smart00262   2 LVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELddtlGPGPVQVRvVDEGKEPP 81


                   ....*....
gi 18405794    597 TFWFALGGK 605
Cdd:smart00262  82 EFWSLFGGW 90
VHP pfam02209
Villin headpiece domain;
941-976 2.13e-13

Villin headpiece domain;


Pssm-ID: 460493  Cd Length: 36  Bit Score: 64.71  E-value: 2.13e-13
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 18405794   941 YLSEEEFQSVFGIEKEAFNNLPRWKQDLLKKKFDLF 976
Cdd:pfam02209   1 YLSDEDFEEVFGMSREEFYKLPKWKQNNLKKKAGLF 36
VHP smart00153
Villin headpiece domain;
941-976 2.99e-12

Villin headpiece domain;


Pssm-ID: 128458  Cd Length: 36  Bit Score: 61.57  E-value: 2.99e-12
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 18405794    941 YLSEEEFQSVFGIEKEAFNNLPRWKQDLLKKKFDLF 976
Cdd:smart00153   1 YLSDEDFEEVFGMTREEFYKLPLWKQNQLKKKKGLF 36
Gelsolin pfam00626
Gelsolin repeat;
262-336 5.65e-12

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 61.94  E-value: 5.65e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18405794   262 MEPIDGDLSKSMLENTKCYLLDCGAEIYIWVGRVTQVDERKAASQSAEEFLASENRPKATHVtRVIQGYESHSFK 336
Cdd:pfam00626   3 VLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDERFPLPEVI-RVPQGKEPARFL 76
Gelsolin pfam00626
Gelsolin repeat;
26-109 2.07e-11

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 60.40  E-value: 2.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405794    26 NFEAVPVPKSEHGKFYMGDTYIVLQTtqnkggaylFDIHFWIGKDTSQDEAGTAAVKTVELDAV-LGGRAVQHREIQGHE 104
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNG---------FTIFLWVGKGSSLLEKLFAALLAAQLDDDeRFPLPEVIRVPQGKE 71


                  ....*
gi 18405794   105 SDKFL 109
Cdd:pfam00626  72 PARFL 76
Gelsolin pfam00626
Gelsolin repeat;
146-215 2.62e-10

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 57.32  E-value: 2.62e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405794   146 RAIRLKQVPFARSSLNHDDVFILDTEEKIYQFNGANSNIQERAKALEVVQYLKDKYHEGTCDVAIVDDGK 215
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDERFPLPEVIRVPQGK 70
Gelsolin pfam00626
Gelsolin repeat;
402-482 2.79e-05

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 43.07  E-value: 2.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405794   402 KTPLPKE---DIGKLYSGDCYLVLYTYHSgerkdeyFLscWFGKKSIPEDQDTAIRLANTM-SNSLKGRPVQGRIYEGKE 477
Cdd:pfam00626   1 KFVLPPPvplSQESLNSGDCYLLDNGFTI-------FL--WVGKGSSLLEKLFAALLAAQLdDDERFPLPEVIRVPQGKE 71


                  ....*
gi 18405794   478 PPQFV 482
Cdd:pfam00626  72 PARFL 76
Gelsolin pfam00626
Gelsolin repeat;
632-711 4.93e-04

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 39.60  E-value: 4.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405794   632 KFQVEEIYNFAQDDLLTEDIYFLDTHAEVFVWVGQCVEPKEKQTVFEIGQKYIDlagslEGLHPKVPIYKINEGNEPCFF 711
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDD-----DERFPLPEVIRVPQGKEPARF 75
DUF4045 pfam13254
Domain of unknown function (DUF4045); This presumed domain is functionally uncharacterized. ...
 843-952 3.87e-03

Domain of unknown function (DUF4045); This presumed domain is functionally uncharacterized. This domain family is found in bacteria and eukaryotes, and is typically between 384 and 430 amino acids in length.


Pssm-ID: 433066 [Multi-domain]  Cd Length: 415  Bit Score: 40.92  E-value: 3.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405794   843 NKKSPDTSPTRRSTSSNPADDIPLTEAKDEEEA---SEVAGLEAKEEEEVSPAADETEAKQ-----ETEEQGDSEIQPSG 914
Cdd:pfam13254 242 DTLSTDKEQSPAPTSASEPPPKTKELPKDSEEPaapSKSAEASTEKKEPDTESSPETSSEKsapslLSPVSKASIDKPLS 321

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 18405794   915 ATFTYEQL-RAKSENPVtgIDF----KRREAyLSEE------EFQSVFG 952
Cdd:pfam13254 322 SPDRDPLSpKPKPQSPP--KDFranlRSREV-PKDKskkdepEFKNVFG 367
 
Name Accession Description Interval E-value
gelsolin_S1_like cd11290
Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; ...
 10-122 2.35e-65

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: 214.78  E-value: 2.35e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405794  10 FQGAGQKPGTEIWRIENFEAVPVPKSEHGKFYMGDTYIVLQTTQNKGGAYLFDIHFWIGKDTSQDEAGTAAVKTVELDAV 89
Cdd:cd11290   1 FEGVGQKPGLQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDPSGSLSYDIHYWLGKEASQDEAGAAAIKAVELDDY 80

                        90       100       110
                ....*....|....*....|....*....|...
gi 18405794  90 LGGRAVQHREIQGHESDKFLSYFKPCIIPLEGG 122
Cdd:cd11290  81 LGGRPVQHREVQGHESEEFLSYFKKGIIYIEGG 113
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 620-718 1.15e-42

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: 1.15e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405794 620 DPHLFSFAFNRGKFQVEEIYNFAQDDLLTEDIYFLDTHAEVFVWVGQCVEPKEKQTVFEIGQKYIDLAGSLEGLhPKVPI 699
Cdd:cd11291   1 KPRLFRCSNESGFFKVEEISDFSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYIETDPLGRSK-PRTPI 79

                        90       100
                ....*....|....*....|
gi 18405794 700 YKINEGNEPCFFTTYF-SWD 718
Cdd:cd11291  80 YLVKQGNEPPTFTGYFhAWD 99
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
 384-485 4.81e-41

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: 145.88  E-value: 4.81e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405794 384 PLLESGGKLEVWYVNGKVKTPLPKEDIGKLYSGDCYLVLYTYHSGeRKDEYFLSCWFGKKSIPEDQDTAIRLANTMSNSL 463
Cdd:cd11293   1 MYDDGSGKVEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQGG-GKEEHILYFWQGRHSSQDERAAAALLTVELDEEL 79

                        90       100
                ....*....|....*....|..
gi 18405794 464 KGRPVQGRIYEGKEPPQFVALF 485
Cdd:cd11293  80 KGRAVQVRVVQGKEPPHFLALF 101
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 136-230 3.24e-35

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: 128.89  E-value: 3.24e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405794 136 ETRLYTCKGKRAIRLKQVPFARSSLNHDDVFILDTEEKIYQFNGANSNIQERAKALEVVQYLKDKYHEGTCDVAIVDDGK 215
Cdd:cd11289   1 KPRLLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKVIVLDEGD 80

                        90
                ....*....|....*
gi 18405794 216 ldtESDSGAFWVLFG 230
Cdd:cd11289  81 ---TNESPEFWKVLG 92
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 252-341 9.38e-33

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: 121.97  E-value: 9.38e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405794 252 PKLYCITD--GKME--PI-DGDLSKSMLENTKCYLLDCGAEIYIWVGRVTQVDERKAASQSAEEFLASENRPKATHVTRV 326
Cdd:cd11292   4 KKLYKVSDasGKLKltEVaEGSLNQEMLDSEDCYILDCGSEIFVWVGKGASLDERKAALKNAEEFLRKKKRPPYTQVTRV 83

                        90
                ....*....|....*
gi 18405794 327 IQGYESHSFKSNFDS 341
Cdd:cd11292  84 TEGGESALFKSKFAN 98
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 517-607 1.48e-32

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: 121.18  E-value: 1.48e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405794 517 SIALVQVSGTGVHNNKAVQVETVATSLNSYECFLLQSGTSMFLWHGNQSTHEQLELATKVAEFLKPGITLKHAKEGTESS 596
Cdd:cd11288   2 PTRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVASFLKPKASLQEVAEGSEPD 81

                        90
                ....*....|.
gi 18405794 597 TFWFALGGKQN 607
Cdd:cd11288  82 EFWEALGGKSE 92
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
 19-112 3.43e-28

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: 109.28  E-value: 3.43e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405794  19 TEIWRIENFEAVPVPKSEHGKFYMGDTYIVLQTTQNKGGAYLFdIHFWIGKDTSQDEAGTAAVKTVELDAVLGGRAVQHR 98
Cdd:cd11293   9 VEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQGGGKEEHI-LYFWQGRHSSQDERAAAALLTVELDEELKGRAVQVR 87

                        90
                ....*....|....
gi 18405794  99 EIQGHESDKFLSYF 112
Cdd:cd11293  88 VVQGKEPPHFLALF 101
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 138-231 1.81e-24

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 98.13  E-value: 1.81e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405794    138 RLYTCKGKRAIRLKQVPFARSSLNHDDVFILDTEEKIYQFNGANSNIQERAKALEVVQYLKDKYHEGTCDVAIVDDGKld 217
Cdd:smart00262   1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVRVVDEGK-- 78

                           90
                   ....*....|....
gi 18405794    218 tESDSgaFWVLFGG 231
Cdd:smart00262  79 -EPPE--FWSLFGG 89
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 20-115 4.97e-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: 85.42  E-value: 4.97e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405794     20 EIWRIENFEAVPVPKSE--HGKFYMGDTYIVLQTTqnkggaylfDIHFWIGKDTSQDEAGTAAVKTVELDAVLGGRAVQH 97
Cdd:smart00262   1 FLVRVKGKRNVRVPEVPfsQGSLNSGDCYILDTGS---------EIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQV 71

                           90
                   ....*....|....*....
gi 18405794     98 REI-QGHESDKFLSYFKPC 115
Cdd:smart00262  72 RVVdEGKEPPEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 259-342 3.95e-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: 83.11  E-value: 3.95e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405794    259 DGKMEPIDGDLSKSMLENTKCYLLDCGAEIYIWVGRVTQVDERKAASQSAEEFLASEnRPKATHVTRVIQGYESHSFKSN 338
Cdd:smart00262   8 KRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTL-GPGPVQVRVVDEGKEPPEFWSL 86


                   ....
gi 18405794    339 FDSW 342
Cdd:smart00262  87 FGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 631-715 2.49e-18

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 80.80  E-value: 2.49e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405794    631 GKFQVEEIY-NFAQDDLLTEDIYFLDTHAEVFVWVGQCVEPKEKQTVFEIGQKYIDLAGSleglhPKVPIYKINEGNEPC 709
Cdd:smart00262   7 GKRNVRVPEvPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGP-----GPVQVRVVDEGKEPP 81


                   ....*.
gi 18405794    710 FFTTYF 715
Cdd:smart00262  82 EFWSLF 87
gelsolin_S1_like cd11290
Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; ...
 392-494 8.56e-18

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: 79.96  E-value: 8.56e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405794 392 LEVWYVNGKVKTPLPKEDIGKLYSGDCYLVLYTYHSGERKDEYFLSCWFGKKSIPEDQDTAIRLANTMSNSLKGRPVQGR 471
Cdd:cd11290  10 LQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDPSGSLSYDIHYWLGKEASQDEAGAAAIKAVELDDYLGGRPVQHR 89

                        90       100
                ....*....|....*....|...
gi 18405794 472 IYEGKEPPQFVALFQPMVVLKGG 494
Cdd:cd11290  90 EVQGHESEEFLSYFKKGIIYIEG 112
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 393-486 4.70e-17

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 76.95  E-value: 4.70e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405794    393 EVWYVNGKVKTPLP--KEDIGKLYSGDCYLVLYTYHSgerkdeYFlscWFGKKSIPEDQDTAIRLANTMSNSLKGRPVQG 470
Cdd:smart00262   1 FLVRVKGKRNVRVPevPFSQGSLNSGDCYILDTGSEI------YV---WVGKKSSQDEKKKAAELAVELDDTLGPGPVQV 71

                           90
                   ....*....|....*..
gi 18405794    471 RIY-EGKEPPQFVALFQ 486
Cdd:smart00262  72 RVVdEGKEPPEFWSLFG 88
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 522-605 1.22e-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: 75.79  E-value: 1.22e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405794    522 QVSGTGVHNNKAVQVETVATSLNSYECFLLQSGTSMFLWHGNQSTHEQLELATKVAEFL----KPGITLKH-AKEGTESS 596
Cdd:smart00262   2 LVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELddtlGPGPVQVRvVDEGKEPP 81


                   ....*....
gi 18405794    597 TFWFALGGK 605
Cdd:smart00262  82 EFWSLFGGW 90
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 630-716 5.80e-14

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: 68.43  E-value: 5.80e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405794 630 RGKFQVEEIY--NFAQDDLLTEDIYFLDTHAEVFVWVGQCVEPKEKQTVFEIGQKYIdlagSLEGLHPKVPIYKINEGNE 707
Cdd:cd11292  13 SGKLKLTEVAegSLNQEMLDSEDCYILDCGSEIFVWVGKGASLDERKAALKNAEEFL----RKKKRPPYTQVTRVTEGGE 88


                ....*....
gi 18405794 708 PCFFTTYFS 716
Cdd:cd11292  89 SALFKSKFA 97
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 251-339 6.78e-14

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


Pssm-ID: 200436  Cd Length: 88  Bit Score: 67.78  E-value: 6.78e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405794 251 PPKLYCI---TDGKMEPIDGDlSKSMLENtKCYLLDCGAEIYIWVGRVTQVDERKAASQSAEEFlaSENRPKATHVTRVI 327
Cdd:cd11280   1 PPRLYRVrgsKAIEIEEVPLA-SSSLDSD-DVFVLDTGSEIYIWQGRASSQAELAAAALLAKEL--DEERKGKPEIVRIR 76

                        90
                ....*....|..
gi 18405794 328 QGYESHSFKSNF 339
Cdd:cd11280  77 QGQEPREFWSLF 88
VHP pfam02209
Villin headpiece domain;
941-976 2.13e-13

Villin headpiece domain;


Pssm-ID: 460493  Cd Length: 36  Bit Score: 64.71  E-value: 2.13e-13
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 18405794   941 YLSEEEFQSVFGIEKEAFNNLPRWKQDLLKKKFDLF 976
Cdd:pfam02209   1 YLSDEDFEEVFGMSREEFYKLPKWKQNNLKKKAGLF 36
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 21-112 1.63e-12

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


Pssm-ID: 200436  Cd Length: 88  Bit Score: 63.93  E-value: 1.63e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405794  21 IWRIE---NFEAVPVPKSeHGKFYMGDTYiVLQTTqnkggaylFDIHFWIGKDTSQDEAGTAAVKTVELDAVLGGRAVQH 97
Cdd:cd11280   4 LYRVRgskAIEIEEVPLA-SSSLDSDDVF-VLDTG--------SEIYIWQGRASSQAELAAAALLAKELDEERKGKPEIV 73

                        90
                ....*....|....*
gi 18405794  98 REIQGHESDKFLSYF 112
Cdd:cd11280  74 RIRQGQEPREFWSLF 88
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 279-343 2.22e-12

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: 63.86  E-value: 2.22e-12
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18405794 279 CYLLDCGAEIYIWVGRVTQVDERKAASQSAEEFLASEN--RPK-ATHVTRVIQGYESHSFKSNFDSWP 343
Cdd:cd11291  32 IMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYIETDPlgRSKpRTPIYLVKQGNEPPTFTGYFHAWD 99
VHP smart00153
Villin headpiece domain;
941-976 2.99e-12

Villin headpiece domain;


Pssm-ID: 128458  Cd Length: 36  Bit Score: 61.57  E-value: 2.99e-12
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 18405794    941 YLSEEEFQSVFGIEKEAFNNLPRWKQDLLKKKFDLF 976
Cdd:smart00153   1 YLSDEDFEEVFGMTREEFYKLPLWKQNQLKKKKGLF 36
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 137-229 3.16e-12

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


Pssm-ID: 200436  Cd Length: 88  Bit Score: 63.16  E-value: 3.16e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405794 137 TRLYTCKGKRAIRLKQVPFARSSLNHDDVFILDTEEKIYQFNGANSNIQERAKALEVVQYLkDKYHEGTCDVAIVDDGKl 216
Cdd:cd11280   2 PRLYRVRGSKAIEIEEVPLASSSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKEL-DEERKGKPEIVRIRQGQ- 79

                        90
                ....*....|...
gi 18405794 217 dtESDSgaFWVLF 229
Cdd:cd11280  80 --EPRE--FWSLF 88
Gelsolin pfam00626
Gelsolin repeat;
262-336 5.65e-12

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 61.94  E-value: 5.65e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18405794   262 MEPIDGDLSKSMLENTKCYLLDCGAEIYIWVGRVTQVDERKAASQSAEEFLASENRPKATHVtRVIQGYESHSFK 336
Cdd:pfam00626   3 VLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDERFPLPEVI-RVPQGKEPARFL 76
Gelsolin pfam00626
Gelsolin repeat;
26-109 2.07e-11

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 60.40  E-value: 2.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405794    26 NFEAVPVPKSEHGKFYMGDTYIVLQTtqnkggaylFDIHFWIGKDTSQDEAGTAAVKTVELDAV-LGGRAVQHREIQGHE 104
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNG---------FTIFLWVGKGSSLLEKLFAALLAAQLDDDeRFPLPEVIRVPQGKE 71


                  ....*
gi 18405794   105 SDKFL 109
Cdd:pfam00626  72 PARFL 76
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 136-231 2.32e-10

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


Pssm-ID: 200444  Cd Length: 92  Bit Score: 58.01  E-value: 2.32e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405794 136 ETRLYTCKG--KRAIRLKQVPFARSSLNHDDVFILDTEEKIYQFNGANSNIQERAKALEVVQYLKDKyhegtCDVAIVDD 213
Cdd:cd11288   2 PTRLFQVRGngSGNTRAVEVDADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVASFLKPK-----ASLQEVAE 76

                        90
                ....*....|....*...
gi 18405794 214 GKldtESDSgaFWVLFGG 231
Cdd:cd11288  77 GS---EPDE--FWEALGG 89
Gelsolin pfam00626
Gelsolin repeat;
146-215 2.62e-10

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 57.32  E-value: 2.62e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405794   146 RAIRLKQVPFARSSLNHDDVFILDTEEKIYQFNGANSNIQERAKALEVVQYLKDKYHEGTCDVAIVDDGK 215
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDERFPLPEVIRVPQGK 70
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 136-215 1.00e-08

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: 53.46  E-value: 1.00e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405794 136 ETRLYTCKGKRAI-RLKQV-PFARSSLNHDDVFILDTEEKIYQFNGANSNIQERAKALEVVQ-YLK---DKYHEGTCDVA 209
Cdd:cd11291   1 KPRLFRCSNESGFfKVEEIsDFSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKkYIEtdpLGRSKPRTPIY 80


                ....*.
gi 18405794 210 IVDDGK 215
Cdd:cd11291  81 LVKQGN 86
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 520-603 4.44e-07

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


Pssm-ID: 200445  Cd Length: 92  Bit Score: 48.77  E-value: 4.44e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405794 520 LVQVSGTGvhNNKAVQVETVATSLNSYECFLLQSGTSMFLWHGNQSTHEQLELATKVAEFLKPGITLKHAK-------EG 592
Cdd:cd11289   4 LLHVKGRR--NVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKvivldegDT 81

                        90
                ....*....|.
gi 18405794 593 TESSTFWFALG 603
Cdd:cd11289  82 NESPEFWKVLG 92
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 528-599 4.30e-06

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: 45.82  E-value: 4.30e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405794 528 VHNNKAVQVETVA---TSLNSYECFLLQSGTSMFLWHGNQSTHEQLELATKVAE------FLKPGITLkhAKEGTESSTF 598
Cdd:cd11280   7 VRGSKAIEIEEVPlasSSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKeldeerKGKPEIVR--IRQGQEPREF 84


                .
gi 18405794 599 W 599
Cdd:cd11280  85 W 85
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 394-485 1.95e-05

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: 43.90  E-value: 1.95e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405794 394 VWYVNGKVKTPLPKED--IGKLYSGDCYLVLYTYHSgerkdeYFlscWFGKKSIPEDQDTAIRLANTMSNSLKGRPVQGR 471
Cdd:cd11280   4 LYRVRGSKAIEIEEVPlaSSSLDSDDVFVLDTGSEI------YI---WQGRASSQAELAAAALLAKELDEERKGKPEIVR 74

                        90
                ....*....|....
gi 18405794 472 IYEGKEPPQFVALF 485
Cdd:cd11280  75 IRQGQEPREFWSLF 88
Gelsolin pfam00626
Gelsolin repeat;
402-482 2.79e-05

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 43.07  E-value: 2.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405794   402 KTPLPKE---DIGKLYSGDCYLVLYTYHSgerkdeyFLscWFGKKSIPEDQDTAIRLANTM-SNSLKGRPVQGRIYEGKE 477
Cdd:pfam00626   1 KFVLPPPvplSQESLNSGDCYLLDNGFTI-------FL--WVGKGSSLLEKLFAALLAAQLdDDERFPLPEVIRVPQGKE 71


                  ....*
gi 18405794   478 PPQFV 482
Cdd:pfam00626  72 PARFL 76
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 268-335 2.87e-05

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: 43.38  E-value: 2.87e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18405794 268 DLSKSMLENTKCYLLDCGAEIYIWVGRVTQVDERKAASQSAEEFLASENRPKA-THVTRVIQGYESHSF 335
Cdd:cd11289  19 ELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAkVIVLDEGDTNESPEF 87
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 515-610 3.17e-05

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


Pssm-ID: 200448  Cd Length: 98  Bit Score: 43.78  E-value: 3.17e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405794 515 PESIALVQVS-GTGVHNNKAVQVETVATS-LNSYECFLLQSGTSMFLWHGNQSTHEQLELATKVA-EFLKPGITLKHAK- 590
Cdd:cd11292   1 AEQKKLYKVSdASGKLKLTEVAEGSLNQEmLDSEDCYILDCGSEIFVWVGKGASLDERKAALKNAeEFLRKKKRPPYTQv 80

                        90       100
                ....*....|....*....|....
gi 18405794 591 ----EGTESSTFwfalggKQNFTS 610
Cdd:cd11292  81 trvtEGGESALF------KSKFAN 98
Gelsolin pfam00626
Gelsolin repeat;
632-711 4.93e-04

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 39.60  E-value: 4.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405794   632 KFQVEEIYNFAQDDLLTEDIYFLDTHAEVFVWVGQCVEPKEKQTVFEIGQKYIDlagslEGLHPKVPIYKINEGNEPCFF 711
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDD-----DERFPLPEVIRVPQGKEPARF 75
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 635-715 3.80e-03

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: 37.35  E-value: 3.80e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405794 635 VEEIYNFAQDdLLTEDIYFLDTHAEVFVWVGQCVEPKEKQTVFEIgQKYIDlagslEGLHPKVPIYKINEGNEPCFFTTY 714
Cdd:cd11280  15 IEEVPLASSS-LDSDDVFVLDTGSEIYIWQGRASSQAELAAAALL-AKELD-----EERKGKPEIVRIRQGQEPREFWSL 87


                .
gi 18405794 715 F 715
Cdd:cd11280  88 F 88
DUF4045 pfam13254
Domain of unknown function (DUF4045); This presumed domain is functionally uncharacterized. ...
 843-952 3.87e-03

Domain of unknown function (DUF4045); This presumed domain is functionally uncharacterized. This domain family is found in bacteria and eukaryotes, and is typically between 384 and 430 amino acids in length.


Pssm-ID: 433066 [Multi-domain]  Cd Length: 415  Bit Score: 40.92  E-value: 3.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405794   843 NKKSPDTSPTRRSTSSNPADDIPLTEAKDEEEA---SEVAGLEAKEEEEVSPAADETEAKQ-----ETEEQGDSEIQPSG 914
Cdd:pfam13254 242 DTLSTDKEQSPAPTSASEPPPKTKELPKDSEEPaapSKSAEASTEKKEPDTESSPETSSEKsapslLSPVSKASIDKPLS 321

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 18405794   915 ATFTYEQL-RAKSENPVtgIDF----KRREAyLSEE------EFQSVFG 952
Cdd:pfam13254 322 SPDRDPLSpKPKPQSPP--KDFranlRSREV-PKDKskkdepEFKNVFG 367
 
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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