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Conserved domains on  [gi|1063705238|ref|NP_001324174|]
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villin-like 1 [Arabidopsis thaliana]

Protein Classification

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; ...
 12-123 2.24e-50

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: 172.41  E-value: 2.24e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705238  12 FQGVGTKSGLEIWCVYNKQLISIPKSSFGKFHSGNAYLVLRTFLRKIESPQYDIHYWLGIDANEVDSILASDKALDLDAA 91
Cdd:cd11290     1 FEGVGQKPGLQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDPSGSLSYDIHYWLGKEASQDEAGAAAIKAVELDDY 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1063705238  92 LGCCTVQYREVQGQETEKFLSYFKPCIIPVEG 123
Cdd:cd11290    81 LGGRPVQHREVQGHESEEFLSYFKKGIIYIEG 112
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 601-698 1.60e-44

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: 155.53  E-value: 1.60e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705238 601 EPHLFTCSCSSDVLKVKEIYNFVQDDLTTEDVFLLDCQSEVYVWIGSNSNIKSKEEALTLGLKFLEMDILEEGLtMRTPV 680
Cdd:cd11291     1 KPRLFRCSNESGFFKVEEISDFSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYIETDPLGRSK-PRTPI 79

                          90
                  ....*....|....*...
gi 1063705238 681 YVVTEGHEPPFFTRFFEW 698
Cdd:cd11291    80 YLVKQGNEPPTFTGYFHA 97
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 497-588 1.89e-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: 120.80  E-value: 1.89e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705238 497 NKASLFRVVGTSPRNMQAIQVNLVATSLNSSYSYILQYGASAFTWIGKLSSDSDHEVLDRMLYFLDTSCQPIYIREGNET 576
Cdd:cd11288     1 SPTRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVASFLKPKASLQEVAEGSEP 80

                          90
                  ....*....|..
gi 1063705238 577 DTFWNLLGGKSE 588
Cdd:cd11288    81 DEFWEALGGKSE 92
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 245-344 5.30e-32

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


:

Pssm-ID: 200448  Cd Length: 98  Bit Score: 119.66  E-value: 5.30e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705238 245 QEQTQTPCAELFWidTKGNLHPTGTSSLDKDMLEKNKCYMLDCHSEVFVWMGRNTSLTERKTSISSSEEFLRKEGRSTTT 324
Cdd:cd11292     1 AEQKKLYKVSDAS--GKLKLTEVAEGSLNQEMLDSEDCYILDCGSEIFVWVGKGASLDERKAALKNAEEFLRKKKRPPYT 78

                          90       100
                  ....*....|....*....|
gi 1063705238 325 SLVLLTEGLENARFRSFFNK 344
Cdd:cd11292    79 QVTRVTEGGESALFKSKFAN 98
ADF_gelsolin super family cl15697
Actin depolymerization factor/cofilin- and gelsolin-like domains; Actin depolymerization ...
 393-466 4.73e-28

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 cd11293:

Pssm-ID: 472830  Cd Length: 101  Bit Score: 108.51  E-value: 4.73e-28
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063705238 393 TKLFTGDCYLVQYKYTYKERTEHLLYVWIGCESIQQDRADAITNASAIVGTTKGESVLCHIYQGNEPSRFFPMF 466
Cdd:cd11293    28 GQFYGGDCYIVLYTYQGGGKEEHILYFWQGRHSSQDERAAAALLTVELDEELKGRAVQVRVVQGKEPPHFLALF 101
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 140-231 6.03e-28

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: 108.09  E-value: 6.03e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705238 140 LLRCKGDHVVRVKEVPFLRSSLNHDDVFILDTASKVFLFAGCNSSTQEKAKAMEVVEYIKDNKHDGRCEVATIEDGKfsg 219
Cdd:cd11289     4 LLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKVIVLDEGD--- 80

                          90
                  ....*....|..
gi 1063705238 220 DSDAGEFWSFFG 231
Cdd:cd11289    81 TNESPEFWKVLG 92
VHP smart00153
Villin headpiece domain;
857-892 2.87e-14

Villin headpiece domain;


:

Pssm-ID: 128458  Cd Length: 36  Bit Score: 67.34  E-value: 2.87e-14
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1063705238  857 YLTEKEFEERFGMAKSEFYALPKWKQNKLKISLHLF 892
Cdd:smart00153   1 YLSDEDFEEVFGMTREEFYKLPLWKQNQLKKKKGLF 36
 
Name Accession Description Interval E-value
gelsolin_S1_like cd11290
Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; ...
 12-123 2.24e-50

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: 172.41  E-value: 2.24e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705238  12 FQGVGTKSGLEIWCVYNKQLISIPKSSFGKFHSGNAYLVLRTFLRKIESPQYDIHYWLGIDANEVDSILASDKALDLDAA 91
Cdd:cd11290     1 FEGVGQKPGLQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDPSGSLSYDIHYWLGKEASQDEAGAAAIKAVELDDY 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1063705238  92 LGCCTVQYREVQGQETEKFLSYFKPCIIPVEG 123
Cdd:cd11290    81 LGGRPVQHREVQGHESEEFLSYFKKGIIYIEG 112
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 601-698 1.60e-44

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: 155.53  E-value: 1.60e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705238 601 EPHLFTCSCSSDVLKVKEIYNFVQDDLTTEDVFLLDCQSEVYVWIGSNSNIKSKEEALTLGLKFLEMDILEEGLtMRTPV 680
Cdd:cd11291     1 KPRLFRCSNESGFFKVEEISDFSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYIETDPLGRSK-PRTPI 79

                          90
                  ....*....|....*...
gi 1063705238 681 YVVTEGHEPPFFTRFFEW 698
Cdd:cd11291    80 YLVKQGNEPPTFTGYFHA 97
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 497-588 1.89e-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: 120.80  E-value: 1.89e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705238 497 NKASLFRVVGTSPRNMQAIQVNLVATSLNSSYSYILQYGASAFTWIGKLSSDSDHEVLDRMLYFLDTSCQPIYIREGNET 576
Cdd:cd11288     1 SPTRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVASFLKPKASLQEVAEGSEP 80

                          90
                  ....*....|..
gi 1063705238 577 DTFWNLLGGKSE 588
Cdd:cd11288    81 DEFWEALGGKSE 92
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 245-344 5.30e-32

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


Pssm-ID: 200448  Cd Length: 98  Bit Score: 119.66  E-value: 5.30e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705238 245 QEQTQTPCAELFWidTKGNLHPTGTSSLDKDMLEKNKCYMLDCHSEVFVWMGRNTSLTERKTSISSSEEFLRKEGRSTTT 324
Cdd:cd11292     1 AEQKKLYKVSDAS--GKLKLTEVAEGSLNQEMLDSEDCYILDCGSEIFVWVGKGASLDERKAALKNAEEFLRKKKRPPYT 78

                          90       100
                  ....*....|....*....|
gi 1063705238 325 SLVLLTEGLENARFRSFFNK 344
Cdd:cd11292    79 QVTRVTEGGESALFKSKFAN 98
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
 393-466 4.73e-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: 108.51  E-value: 4.73e-28
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063705238 393 TKLFTGDCYLVQYKYTYKERTEHLLYVWIGCESIQQDRADAITNASAIVGTTKGESVLCHIYQGNEPSRFFPMF 466
Cdd:cd11293    28 GQFYGGDCYIVLYTYQGGGKEEHILYFWQGRHSSQDERAAAALLTVELDEELKGRAVQVRVVQGKEPPHFLALF 101
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 140-231 6.03e-28

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: 108.09  E-value: 6.03e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705238 140 LLRCKGDHVVRVKEVPFLRSSLNHDDVFILDTASKVFLFAGCNSSTQEKAKAMEVVEYIKDNKHDGRCEVATIEDGKfsg 219
Cdd:cd11289     4 LLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKVIVLDEGD--- 80

                          90
                  ....*....|..
gi 1063705238 220 DSDAGEFWSFFG 231
Cdd:cd11289    81 TNESPEFWKVLG 92
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 140-232 3.51e-25

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 100.06  E-value: 3.51e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705238  140 LLRCKGDHVVRVKEVPFLRSSLNHDDVFILDTASKVFLFAGCNSSTQEKAKAMEVVEYIKDNKHDGRCEVATIEDGKfsg 219
Cdd:smart00262   2 LVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVRVVDEGK--- 78

                           90
                   ....*....|...
gi 1063705238  220 dsDAGEFWSFFGG 232
Cdd:smart00262  79 --EPPEFWSLFGG 89
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 607-696 2.52e-21

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 88.89  E-value: 2.52e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705238  607 CSCSSDVLKVKEIY-NFVQDDLTTEDVFLLDCQSEVYVWIGSNSNIKSKEEALTLGLKFLEMDILEegltmRTPVYVVTE 685
Cdd:smart00262   2 LVRVKGKRNVRVPEvPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPG-----PVQVRVVDE 76

                           90
                   ....*....|.
gi 1063705238  686 GHEPPFFTRFF 696
Cdd:smart00262  77 GKEPPEFWSLF 87
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 502-586 6.38e-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: 76.56  E-value: 6.38e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705238  502 FRVVGTSPRNMQAIQVNLVATSLNSSYSYILQYGASAFTWIGKLSSDSDHEVLDRMLYFLDTSCQPIY-----IREGNET 576
Cdd:smart00262   1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPvqvrvVDEGKEP 80

                           90
                   ....*....|
gi 1063705238  577 DTFWNLLGGK 586
Cdd:smart00262  81 PEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 270-345 7.00e-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: 73.48  E-value: 7.00e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063705238  270 SSLDKDMLEKNKCYMLDCHSEVFVWMGRNTSLTERKTSISSSEEFLRKEgRSTTTSLVLLTEGLENARFRSFFNKW 345
Cdd:smart00262  16 VPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTL-GPGPVQVRVVDEGKEPPEFWSLFGGW 90
VHP smart00153
Villin headpiece domain;
857-892 2.87e-14

Villin headpiece domain;


Pssm-ID: 128458  Cd Length: 36  Bit Score: 67.34  E-value: 2.87e-14
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1063705238  857 YLTEKEFEERFGMAKSEFYALPKWKQNKLKISLHLF 892
Cdd:smart00153   1 YLSDEDFEEVFGMTREEFYKLPLWKQNQLKKKKGLF 36
VHP pfam02209
Villin headpiece domain;
857-892 8.16e-14

Villin headpiece domain;


Pssm-ID: 460493  Cd Length: 36  Bit Score: 65.86  E-value: 8.16e-14
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1063705238 857 YLTEKEFEERFGMAKSEFYALPKWKQNKLKISLHLF 892
Cdd:pfam02209   1 YLSDEDFEEVFGMSREEFYKLPKWKQNNLKKKAGLF 36
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 22-117 3.37e-13

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: 65.78  E-value: 3.37e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705238   22 EIWCVYNKQLISIPKSSF--GKFHSGNAYLVLRTflrkiespqYDIHYWLGIDANEVDSILASDKALDLDAALGCCTVQY 99
Cdd:smart00262   1 FLVRVKGKRNVRVPEVPFsqGSLNSGDCYILDTG---------SEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQV 71

                           90
                   ....*....|....*....
gi 1063705238  100 REV-QGQETEKFLSYFKPC 117
Cdd:smart00262  72 RVVdEGKEPPEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 389-468 4.20e-12

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 62.70  E-value: 4.20e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705238  389 DNLKTKLFTGDCYLVQYKytykerteHLLYVWIGCESIQQDRADAITNASAIVGTTKGESVLCHIY-QGNEPSRFFPMFQ 467
Cdd:smart00262  17 PFSQGSLNSGDCYILDTG--------SEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVRVVdEGKEPPEFWSLFG 88


                   .
gi 1063705238  468 S 468
Cdd:smart00262  89 G 89
Gelsolin pfam00626
Gelsolin repeat;
147-216 8.49e-11

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 58.47  E-value: 8.49e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705238 147 HVVRVKEVPFLRSSLNHDDVFILDTASKVFLFAGCNSSTQEKAKAMEVVEYIKDNKHDGRCEVATIEDGK 216
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDERFPLPEVIRVPQGK 70
Gelsolin pfam00626
Gelsolin repeat;
624-692 9.86e-10

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 55.78  E-value: 9.86e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063705238 624 QDDLTTEDVFLLDCQSEVYVWIGSNSNIKSKEEALTlglkfLEMDILEEGLTMRTPVYVVTEGHEPPFF 692
Cdd:pfam00626  12 QESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAAL-----LAAQLDDDERFPLPEVIRVPQGKEPARF 75
Gelsolin pfam00626
Gelsolin repeat;
272-339 3.74e-08

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 51.15  E-value: 3.74e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063705238 272 LDKDMLEKNKCYMLDCHSEVFVWMGRNTSLTERKTSISSSEEfLRKEGRSTTTSLVLLTEGLENARFR 339
Cdd:pfam00626  10 LSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQ-LDDDERFPLPEVIRVPQGKEPARFL 76
Gelsolin pfam00626
Gelsolin repeat;
34-111 2.42e-05

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 43.07  E-value: 2.42e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063705238  34 IPKSSFGKFHSGNAYLVLRTFlrkiespqyDIHYWLGIDANEVDSILASDKALDLDA-ALGCCTVQYREVQGQETEKFL 111
Cdd:pfam00626   7 PVPLSQESLNSGDCYLLDNGF---------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; ...
 12-123 2.24e-50

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: 172.41  E-value: 2.24e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705238  12 FQGVGTKSGLEIWCVYNKQLISIPKSSFGKFHSGNAYLVLRTFLRKIESPQYDIHYWLGIDANEVDSILASDKALDLDAA 91
Cdd:cd11290     1 FEGVGQKPGLQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDPSGSLSYDIHYWLGKEASQDEAGAAAIKAVELDDY 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1063705238  92 LGCCTVQYREVQGQETEKFLSYFKPCIIPVEG 123
Cdd:cd11290    81 LGGRPVQHREVQGHESEEFLSYFKKGIIYIEG 112
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 601-698 1.60e-44

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: 155.53  E-value: 1.60e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705238 601 EPHLFTCSCSSDVLKVKEIYNFVQDDLTTEDVFLLDCQSEVYVWIGSNSNIKSKEEALTLGLKFLEMDILEEGLtMRTPV 680
Cdd:cd11291     1 KPRLFRCSNESGFFKVEEISDFSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYIETDPLGRSK-PRTPI 79

                          90
                  ....*....|....*...
gi 1063705238 681 YVVTEGHEPPFFTRFFEW 698
Cdd:cd11291    80 YLVKQGNEPPTFTGYFHA 97
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 497-588 1.89e-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: 120.80  E-value: 1.89e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705238 497 NKASLFRVVGTSPRNMQAIQVNLVATSLNSSYSYILQYGASAFTWIGKLSSDSDHEVLDRMLYFLDTSCQPIYIREGNET 576
Cdd:cd11288     1 SPTRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVASFLKPKASLQEVAEGSEP 80

                          90
                  ....*....|..
gi 1063705238 577 DTFWNLLGGKSE 588
Cdd:cd11288    81 DEFWEALGGKSE 92
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 245-344 5.30e-32

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


Pssm-ID: 200448  Cd Length: 98  Bit Score: 119.66  E-value: 5.30e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705238 245 QEQTQTPCAELFWidTKGNLHPTGTSSLDKDMLEKNKCYMLDCHSEVFVWMGRNTSLTERKTSISSSEEFLRKEGRSTTT 324
Cdd:cd11292     1 AEQKKLYKVSDAS--GKLKLTEVAEGSLNQEMLDSEDCYILDCGSEIFVWVGKGASLDERKAALKNAEEFLRKKKRPPYT 78

                          90       100
                  ....*....|....*....|
gi 1063705238 325 SLVLLTEGLENARFRSFFNK 344
Cdd:cd11292    79 QVTRVTEGGESALFKSKFAN 98
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
 393-466 4.73e-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: 108.51  E-value: 4.73e-28
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063705238 393 TKLFTGDCYLVQYKYTYKERTEHLLYVWIGCESIQQDRADAITNASAIVGTTKGESVLCHIYQGNEPSRFFPMF 466
Cdd:cd11293    28 GQFYGGDCYIVLYTYQGGGKEEHILYFWQGRHSSQDERAAAALLTVELDEELKGRAVQVRVVQGKEPPHFLALF 101
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 140-231 6.03e-28

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: 108.09  E-value: 6.03e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705238 140 LLRCKGDHVVRVKEVPFLRSSLNHDDVFILDTASKVFLFAGCNSSTQEKAKAMEVVEYIKDNKHDGRCEVATIEDGKfsg 219
Cdd:cd11289     4 LLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKVIVLDEGD--- 80

                          90
                  ....*....|..
gi 1063705238 220 DSDAGEFWSFFG 231
Cdd:cd11289    81 TNESPEFWKVLG 92
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 140-232 3.51e-25

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 100.06  E-value: 3.51e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705238  140 LLRCKGDHVVRVKEVPFLRSSLNHDDVFILDTASKVFLFAGCNSSTQEKAKAMEVVEYIKDNKHDGRCEVATIEDGKfsg 219
Cdd:smart00262   2 LVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVRVVDEGK--- 78

                           90
                   ....*....|...
gi 1063705238  220 dsDAGEFWSFFGG 232
Cdd:smart00262  79 --EPPEFWSLFGG 89
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 607-696 2.52e-21

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 88.89  E-value: 2.52e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705238  607 CSCSSDVLKVKEIY-NFVQDDLTTEDVFLLDCQSEVYVWIGSNSNIKSKEEALTLGLKFLEMDILEegltmRTPVYVVTE 685
Cdd:smart00262   2 LVRVKGKRNVRVPEvPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPG-----PVQVRVVDE 76

                           90
                   ....*....|.
gi 1063705238  686 GHEPPFFTRFF 696
Cdd:smart00262  77 GKEPPEFWSLF 87
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 600-696 5.20e-18

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


Pssm-ID: 200448  Cd Length: 98  Bit Score: 79.99  E-value: 5.20e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705238 600 EEPHLFTCSCSSDVLKVKEIY--NFVQDDLTTEDVFLLDCQSEVYVWIGSNSNIKSKEEALTLGLKFLEMdileEGLTMR 677
Cdd:cd11292     2 EQKKLYKVSDASGKLKLTEVAegSLNQEMLDSEDCYILDCGSEIFVWVGKGASLDERKAALKNAEEFLRK----KKRPPY 77

                          90
                  ....*....|....*....
gi 1063705238 678 TPVYVVTEGHEPPFFTRFF 696
Cdd:cd11292    78 TQVTRVTEGGESALFKSKF 96
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 502-586 6.38e-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: 76.56  E-value: 6.38e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705238  502 FRVVGTSPRNMQAIQVNLVATSLNSSYSYILQYGASAFTWIGKLSSDSDHEVLDRMLYFLDTSCQPIY-----IREGNET 576
Cdd:smart00262   1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPvqvrvVDEGKEP 80

                           90
                   ....*....|
gi 1063705238  577 DTFWNLLGGK 586
Cdd:smart00262  81 PEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 270-345 7.00e-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: 73.48  E-value: 7.00e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063705238  270 SSLDKDMLEKNKCYMLDCHSEVFVWMGRNTSLTERKTSISSSEEFLRKEgRSTTTSLVLLTEGLENARFRSFFNKW 345
Cdd:smart00262  16 VPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTL-GPGPVQVRVVDEGKEPPEFWSLFGGW 90
VHP smart00153
Villin headpiece domain;
857-892 2.87e-14

Villin headpiece domain;


Pssm-ID: 128458  Cd Length: 36  Bit Score: 67.34  E-value: 2.87e-14
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1063705238  857 YLTEKEFEERFGMAKSEFYALPKWKQNKLKISLHLF 892
Cdd:smart00153   1 YLSDEDFEEVFGMTREEFYKLPLWKQNQLKKKKGLF 36
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
 21-114 4.65e-14

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: 68.84  E-value: 4.65e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705238  21 LEIWCVYNKQLISIPKSSFGKFHSGNAYLVLRTFLRKiESPQYDIHYWLGIDANEVDSILASDKALDLDAALGCCTVQYR 100
Cdd:cd11293     9 VEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQGG-GKEEHILYFWQGRHSSQDERAAAALLTVELDEELKGRAVQVR 87

                          90
                  ....*....|....
gi 1063705238 101 EVQGQETEKFLSYF 114
Cdd:cd11293    88 VVQGKEPPHFLALF 101
VHP pfam02209
Villin headpiece domain;
857-892 8.16e-14

Villin headpiece domain;


Pssm-ID: 460493  Cd Length: 36  Bit Score: 65.86  E-value: 8.16e-14
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1063705238 857 YLTEKEFEERFGMAKSEFYALPKWKQNKLKISLHLF 892
Cdd:pfam02209   1 YLSDEDFEEVFGMSREEFYKLPKWKQNNLKKKAGLF 36
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 22-117 3.37e-13

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: 65.78  E-value: 3.37e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705238   22 EIWCVYNKQLISIPKSSF--GKFHSGNAYLVLRTflrkiespqYDIHYWLGIDANEVDSILASDKALDLDAALGCCTVQY 99
Cdd:smart00262   1 FLVRVKGKRNVRVPEVPFsqGSLNSGDCYILDTG---------SEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQV 71

                           90
                   ....*....|....*....
gi 1063705238  100 REV-QGQETEKFLSYFKPC 117
Cdd:smart00262  72 RVVdEGKEPPEFWSLFGGW 90
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 259-346 4.03e-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: 63.09  E-value: 4.03e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705238 259 DTKGNLHPTGTSSLDKDMLEKNKCYMLDCHSEVFVWMGRNTSLTERKTSISSSEEFLRKEG---RSTTTSLVLLTEGLEN 335
Cdd:cd11291     9 NESGFFKVEEISDFSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYIETDPlgrSKPRTPIYLVKQGNEP 88

                          90
                  ....*....|.
gi 1063705238 336 ARFRSFFNKWP 346
Cdd:cd11291    89 PTFTGYFHAWD 99
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 389-468 4.20e-12

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 62.70  E-value: 4.20e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705238  389 DNLKTKLFTGDCYLVQYKytykerteHLLYVWIGCESIQQDRADAITNASAIVGTTKGESVLCHIY-QGNEPSRFFPMFQ 467
Cdd:smart00262  17 PFSQGSLNSGDCYILDTG--------SEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVRVVdEGKEPPEFWSLFG 88


                   .
gi 1063705238  468 S 468
Cdd:smart00262  89 G 89
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 602-696 2.08e-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: 2.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705238 602 PHLFTCScSSDVLKVKEIYNFVQDdLTTEDVFLLDCQSEVYVWIGSNSNIKSKEEALTLGLKFLEMDileeglTMRTPVY 681
Cdd:cd11280     2 PRLYRVR-GSKAIEIEEVPLASSS-LDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKELDEER------KGKPEIV 73

                          90
                  ....*....|....*
gi 1063705238 682 VVTEGHEPPFFTRFF 696
Cdd:cd11280    74 RIRQGQEPREFWSLF 88
Gelsolin pfam00626
Gelsolin repeat;
147-216 8.49e-11

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 58.47  E-value: 8.49e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705238 147 HVVRVKEVPFLRSSLNHDDVFILDTASKVFLFAGCNSSTQEKAKAMEVVEYIKDNKHDGRCEVATIEDGK 216
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDERFPLPEVIRVPQGK 70
Gelsolin pfam00626
Gelsolin repeat;
624-692 9.86e-10

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 55.78  E-value: 9.86e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063705238 624 QDDLTTEDVFLLDCQSEVYVWIGSNSNIKSKEEALTlglkfLEMDILEEGLTMRTPVYVVTEGHEPPFF 692
Cdd:pfam00626  12 QESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAAL-----LAAQLDDDERFPLPEVIRVPQGKEPARF 75
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 140-230 1.00e-09

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


Pssm-ID: 200436  Cd Length: 88  Bit Score: 55.84  E-value: 1.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705238 140 LLRCKGDHVVRVKEVPFLRSSLNHDDVFILDTASKVFLFAGCNSSTQEKAKAMEVVEYIkDNKHDGRCEVATIEDGkfsg 219
Cdd:cd11280     4 LYRVRGSKAIEIEEVPLASSSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKEL-DEERKGKPEIVRIRQG---- 78

                          90
                  ....*....|.
gi 1063705238 220 dSDAGEFWSFF 230
Cdd:cd11280    79 -QEPREFWSLF 88
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 136-232 1.52e-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: 55.70  E-value: 1.52e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705238 136 YQVtllRCKGDHVVRVKEVPFLRSSLNHDDVFILDTASKVFLFAGCNSSTQEKAKAMEVVEYIKDnkhdgRCEVATIEDG 215
Cdd:cd11288     6 FQV---RGNGSGNTRAVEVDADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVASFLKP-----KASLQEVAEG 77

                          90
                  ....*....|....*..
gi 1063705238 216 KfsgDSDagEFWSFFGG 232
Cdd:cd11288    78 S---EPD--EFWEALGG 89
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 148-216 2.59e-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: 52.30  E-value: 2.59e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063705238 148 VVRVKEV-PFLRSSLNHDDVFILDTASKVFLFAGCNSSTQEKAKAMEVVE-YIK---DNKHDGRCEVATIEDGK 216
Cdd:cd11291    13 FFKVEEIsDFSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKkYIEtdpLGRSKPRTPIYLVKQGN 86
Gelsolin pfam00626
Gelsolin repeat;
272-339 3.74e-08

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 51.15  E-value: 3.74e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063705238 272 LDKDMLEKNKCYMLDCHSEVFVWMGRNTSLTERKTSISSSEEfLRKEGRSTTTSLVLLTEGLENARFR 339
Cdd:pfam00626  10 LSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQ-LDDDERFPLPEVIRVPQGKEPARFL 76
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 627-696 1.05e-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: 44.54  E-value: 1.05e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063705238 627 LTTEDVFLLDCQSEVYVWIGSNSNI--KSKEEALTLGLKflemDILEEGltmRTPVYVVTEGHEPP---FFTRFF 696
Cdd:cd11289    25 LNSGDVFILDLGSTIYQWNGSKSNRfeKAKAMQLAQGIR----DERRLG---RAKVIVLDEGDTNEspeFWKVLG 92
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 266-342 2.08e-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: 2.08e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063705238 266 PTGTSSLDKDmleknKCYMLDCHSEVFVWMGRNTSLTERKTSISSSEEFLRKEGrsTTTSLVLLTEGLENARFRSFF 342
Cdd:cd11280    19 PLASSSLDSD-----DVFVLDTGSEIYIWQGRASSQAELAAAALLAKELDEERK--GKPEIVRIRQGQEPREFWSLF 88
Gelsolin pfam00626
Gelsolin repeat;
34-111 2.42e-05

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 43.07  E-value: 2.42e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063705238  34 IPKSSFGKFHSGNAYLVLRTFlrkiespqyDIHYWLGIDANEVDSILASDKALDLDA-ALGCCTVQYREVQGQETEKFL 111
Cdd:pfam00626   7 PVPLSQESLNSGDCYLLDNGF---------TIFLWVGKGSSLLEKLFAALLAAQLDDdERFPLPEVIRVPQGKEPARFL 76
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 501-583 4.50e-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: 42.74  E-value: 4.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705238 501 LFRVVGTSPRNMQaiQVNLVATSLNSSYSYILQYGASAFTWIGKLSSDSDH----EVLDRMLYFLDTSCQPIYIREGNET 576
Cdd:cd11280     4 LYRVRGSKAIEIE--EVPLASSSLDSDDVFVLDTGSEIYIWQGRASSQAELaaaaLLAKELDEERKGKPEIVRIRQGQEP 81


                  ....*..
gi 1063705238 577 DTFWNLL 583
Cdd:cd11280    82 REFWSLF 88
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 498-584 1.25e-04

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: 41.45  E-value: 1.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705238 498 KASLFRVVGTspRNMQAIQVNLVATSLNSSYSYILQYGASAFTWIGKLSSdsdheVLDR-----MLYFLDTS-----CQP 567
Cdd:cd11289     1 KPRLLHVKGR--RNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSN-----RFEKakamqLAQGIRDErrlgrAKV 73

                          90
                  ....*....|....*....
gi 1063705238 568 IYIREG--NETDTFWNLLG 584
Cdd:cd11289    74 IVLDEGdtNESPEFWKVLG 92
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 62-114 4.94e-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: 39.66  E-value: 4.94e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1063705238  62 QYDIHYWLGIDANEVDSILASDKALDLDAALGCCTVQYREVQGQETEKFLSYF 114
Cdd:cd11280    36 GSEIYIWQGRASSQAELAAAALLAKELDEERKGKPEIVRIRQGQEPREFWSLF 88
gelsolin_S1_like cd11290
Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; ...
 394-475 2.54e-03

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: 38.36  E-value: 2.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705238 394 KLFTGDCYLVQykYTYKERTEHL---LYVWIGCESIQQDRAdaitnASAIVgTTK------GESVLCHIYQGNEPSRFFP 464
Cdd:cd11290    30 KFYEGDSYIVL--KTTLDPSGSLsydIHYWLGKEASQDEAG-----AAAIK-AVElddylgGRPVQHREVQGHESEEFLS 101

                          90
                  ....*....|.
gi 1063705238 465 MFQSLVVFKGG 475
Cdd:cd11290   102 YFKKGIIYIEG 112
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 393-466 3.67e-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: 3.67e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063705238 393 TKLFTGDCYLVQYKYTykertehlLYVWIGCESIQQDRADAITNASAIVGTTKGESVLCHIYQGNEPSRFFPMF 466
Cdd:cd11280    23 SSLDSDDVFVLDTGSE--------IYIWQGRASSQAELAAAALLAKELDEERKGKPEIVRIRQGQEPREFWSLF 88
 
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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