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Conserved domains on  [gi|755560683|ref|XP_011245178|]
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supervillin isoform X2 [Mus musculus]

Protein Classification

supervillin family protein( domain architecture ID 10181714)

supervillin family protein, a villin/gelsolin superfamily member, directly binds and cross-links F-actin; also regulates myosin II contractility subjacent to plasma membranes

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
1718-1831 3.20e-44

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: 155.89  E-value: 3.20e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755560683 1718 QFEIATVSVDVWHILEFDYSRLPRQSIGQFHEGDAYVVKWKYMastavgsrqkgehlvrVAGKEKCVYFFWQGRHSTVSE 1797
Cdd:cd11293     1 MYDDGSGKVEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQ----------------GGGKEEHILYFWQGRHSSQDE 64
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 755560683 1798 KGTSALMTVELDEE---RGAQVQVLQGKEPPCFLQCF 1831
Cdd:cd11293    65 RAAAALLTVELDEElkgRAVQVRVVQGKEPPHFLALF 101
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
1414-1510 2.77e-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: 130.05  E-value: 2.77e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755560683 1414 KLMLLQIKGRRHVQTRLVEPRASSLNSGDCFLLLSPQYCFLWVGEFSNVIEKAKASELATLIQTKRELGCRATYIQTIEE 1493
Cdd:cd11289     1 KPRLLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKVIVLDEGD 80
                          90
                  ....*....|....*..
gi 755560683 1494 GiNTHTHaakdFWKLLG 1510
Cdd:cd11289    81 T-NESPE----FWKVLG 92
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
1851-1956 1.64e-26

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: 105.01  E-value: 1.64e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755560683 1851 SEWRLYCVRGEVPMEGNLLEVACHCSSLRSRTSMVVLNINKalIYLWHGCKAQGHTKEVGRTAANKIKEECpleaglhss 1930
Cdd:cd11288     1 SPTRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKTPSS--VYLWVGKGSSEDERELAKDVASFLKPKA--------- 69
                          90       100
                  ....*....|....*....|....*.
gi 755560683 1931 snvTIHECDEGSEPLGFWDALGRRDR 1956
Cdd:cd11288    70 ---SLQEVAEGSEPDEFWEALGGKSE 92
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
1535-1635 6.25e-18

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: 80.49  E-value: 6.25e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755560683 1535 NCVYRLTDDKlvpdDDYWGKIPKCS-LLQSKEVLVFDFGSEVYVWHGKEVTLAQRKIAFQLAKHLWNGtfdyencdinpl 1613
Cdd:cd11280     2 PRLYRVRGSK----AIEIEEVPLASsSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKELDEE------------ 65
                          90       100
                  ....*....|....*....|...
gi 755560683 1614 DPGECNPLIPRKGQG-RPDWAIF 1635
Cdd:cd11280    66 RKGKPEIVRIRQGQEpREFWSLF 88
VHP pfam02209
Villin headpiece domain;
2151-2186 7.42e-15

Villin headpiece domain;


:

Pssm-ID: 460493  Cd Length: 36  Bit Score: 70.10  E-value: 7.42e-15
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 755560683  2151 YLTDEDFEFALDMSRDEFNALPTWKQVNLKKSKGLF 2186
Cdd:pfam02209    1 YLSDEDFEEVFGMSREEFYKLPKWKQNNLKKKAGLF 36
ADF_gelsolin super family cl15697
Actin depolymerization factor/cofilin- and gelsolin-like domains; Actin depolymerization ...
1973-2095 2.73e-13

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 cd11291:

Pssm-ID: 472830 [Multi-domain]  Cd Length: 99  Bit Score: 67.71  E-value: 2.73e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755560683 1973 PRLFILSSSSGDFSATEFVypaqapsavssmPFLQEDLYSApqpALFLVDNHHEVYLWQGWWPTENKItgsarirwasdr 2052
Cdd:cd11291     2 PRLFRCSNESGFFKVEEIS------------DFSQDDLDTD---DIMLLDTGDEVFVWVGSESSDEEK------------ 54
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 755560683 2053 KSAMETVLQYCRGKNLKRPPPKS--YLIHAGLEPLTFTNMFPSWE 2095
Cdd:cd11291    55 KEALTSAKKYIETDPLGRSKPRTpiYLVKQGNEPPTFTGYFHAWD 99
 
Name Accession Description Interval E-value
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
1718-1831 3.20e-44

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: 155.89  E-value: 3.20e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755560683 1718 QFEIATVSVDVWHILEFDYSRLPRQSIGQFHEGDAYVVKWKYMastavgsrqkgehlvrVAGKEKCVYFFWQGRHSTVSE 1797
Cdd:cd11293     1 MYDDGSGKVEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQ----------------GGGKEEHILYFWQGRHSSQDE 64
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 755560683 1798 KGTSALMTVELDEE---RGAQVQVLQGKEPPCFLQCF 1831
Cdd:cd11293    65 RAAAALLTVELDEElkgRAVQVRVVQGKEPPHFLALF 101
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
1414-1510 2.77e-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: 130.05  E-value: 2.77e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755560683 1414 KLMLLQIKGRRHVQTRLVEPRASSLNSGDCFLLLSPQYCFLWVGEFSNVIEKAKASELATLIQTKRELGCRATYIQTIEE 1493
Cdd:cd11289     1 KPRLLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKVIVLDEGD 80
                          90
                  ....*....|....*..
gi 755560683 1494 GiNTHTHaakdFWKLLG 1510
Cdd:cd11289    81 T-NESPE----FWKVLG 92
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
1851-1956 1.64e-26

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: 105.01  E-value: 1.64e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755560683 1851 SEWRLYCVRGEVPMEGNLLEVACHCSSLRSRTSMVVLNINKalIYLWHGCKAQGHTKEVGRTAANKIKEECpleaglhss 1930
Cdd:cd11288     1 SPTRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKTPSS--VYLWVGKGSSEDERELAKDVASFLKPKA--------- 69
                          90       100
                  ....*....|....*....|....*.
gi 755560683 1931 snvTIHECDEGSEPLGFWDALGRRDR 1956
Cdd:cd11288    70 ---SLQEVAEGSEPDEFWEALGGKSE 92
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
1417-1511 5.89e-22

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 91.97  E-value: 5.89e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755560683   1417 LLQIKGRRHVQTRLVEPRASSLNSGDCFLLLSPQYCFLWVGEFSNVIEKAKASELATLIqtKRELGCRATYIQTIEEGIN 1496
Cdd:smart00262    2 LVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVEL--DDTLGPGPVQVRVVDEGKE 79
                            90
                    ....*....|....*
gi 755560683   1497 THThaakdFWKLLGG 1511
Cdd:smart00262   80 PPE-----FWSLFGG 89
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
1535-1635 6.25e-18

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: 80.49  E-value: 6.25e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755560683 1535 NCVYRLTDDKlvpdDDYWGKIPKCS-LLQSKEVLVFDFGSEVYVWHGKEVTLAQRKIAFQLAKHLWNGtfdyencdinpl 1613
Cdd:cd11280     2 PRLYRVRGSK----AIEIEEVPLASsSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKELDEE------------ 65
                          90       100
                  ....*....|....*....|...
gi 755560683 1614 DPGECNPLIPRKGQG-RPDWAIF 1635
Cdd:cd11280    66 RKGKPEIVRIRQGQEpREFWSLF 88
VHP pfam02209
Villin headpiece domain;
2151-2186 7.42e-15

Villin headpiece domain;


Pssm-ID: 460493  Cd Length: 36  Bit Score: 70.10  E-value: 7.42e-15
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 755560683  2151 YLTDEDFEFALDMSRDEFNALPTWKQVNLKKSKGLF 2186
Cdd:pfam02209    1 YLSDEDFEEVFGMSREEFYKLPKWKQNNLKKKAGLF 36
VHP smart00153
Villin headpiece domain;
2151-2186 1.23e-14

Villin headpiece domain;


Pssm-ID: 128458  Cd Length: 36  Bit Score: 69.27  E-value: 1.23e-14
                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 755560683   2151 YLTDEDFEFALDMSRDEFNALPTWKQVNLKKSKGLF 2186
Cdd:smart00153    1 YLSDEDFEEVFGMTREEFYKLPLWKQNQLKKKKGLF 36
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
1973-2095 2.73e-13

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: 67.71  E-value: 2.73e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755560683 1973 PRLFILSSSSGDFSATEFVypaqapsavssmPFLQEDLYSApqpALFLVDNHHEVYLWQGWWPTENKItgsarirwasdr 2052
Cdd:cd11291     2 PRLFRCSNESGFFKVEEIS------------DFSQDDLDTD---DIMLLDTGDEVFVWVGSESSDEEK------------ 54
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 755560683 2053 KSAMETVLQYCRGKNLKRPPPKS--YLIHAGLEPLTFTNMFPSWE 2095
Cdd:cd11291    55 KEALTSAKKYIETDPLGRSKPRTpiYLVKQGNEPPTFTGYFHAWD 99
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
1728-1834 1.01e-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: 65.78  E-value: 1.01e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755560683   1728 VWHILEFDYSRLPRQ--SIGQFHEGDAYVVKWkymastavgsrqkGEHLvrvagkekcvyFFWQGRHSTVSEKGTSALMT 1805
Cdd:smart00262    2 LVRVKGKRNVRVPEVpfSQGSLNSGDCYILDT-------------GSEI-----------YVWVGKKSSQDEKKKAAELA 57
                            90       100       110
                    ....*....|....*....|....*....|...
gi 755560683   1806 VELDEERG---AQVQ-VLQGKEPPCFLQCFQGG 1834
Cdd:smart00262   58 VELDDTLGpgpVQVRvVDEGKEPPEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
1856-1952 1.21e-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: 65.39  E-value: 1.21e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755560683   1856 YCVRGEVPMEGNLLEVACHCSSLRSRTSMVVLNinKALIYLWHGCKAQGHTKEVGRTAANKIKEECPleaglhsSSNVTI 1935
Cdd:smart00262    1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDT--GSEIYVWVGKKSSQDEKKKAAELAVELDDTLG-------PGPVQV 71
                            90
                    ....*....|....*..
gi 755560683   1936 HECDEGSEPLGFWDALG 1952
Cdd:smart00262   72 RVVDEGKEPPEFWSLFG 88
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
2000-2094 1.08e-06

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: 48.44  E-value: 1.08e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755560683   2000 VSSMPFLQEDLYSApqpALFLVDNHHEVYLWQGwwptenkiTGSARirwaSDRKSAMETVLQYCrgKNLKRPPPKSYLIH 2079
Cdd:smart00262   13 VPEVPFSQGSLNSG---DCYILDTGSEIYVWVG--------KKSSQ----DEKKKAAELAVELD--DTLGPGPVQVRVVD 75
                            90
                    ....*....|....*
gi 755560683   2080 AGLEPLTFTNMFPSW 2094
Cdd:smart00262   76 EGKEPPEFWSLFGGW 90
Gelsolin pfam00626
Gelsolin repeat;
1435-1494 5.76e-06

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 46.15  E-value: 5.76e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755560683  1435 ASSLNSGDCFLLLSPQYCFLWVGEFSNVIEKAKASELAT-LIQTKRelgCRATYIQTIEEG 1494
Cdd:pfam00626   12 QESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAqLDDDER---FPLPEVIRVPQG 69
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
1556-1654 7.90e-06

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: 46.13  E-value: 7.90e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755560683   1556 PKCSLLQSKEVLVFDFGSEVYVWHGKEVTLAQRKIAFQLAKHLwngtFDYENcdinpldpgecnpliPRKGQGRpdwaif 1635
Cdd:smart00262   18 FSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVEL----DDTLG---------------PGPVQVR------ 72
                            90
                    ....*....|....*....
gi 755560683   1636 gRVTEHNETILFKEKFLDW 1654
Cdd:smart00262   73 -VVDEGKEPPEFWSLFGGW 90
Gelsolin pfam00626
Gelsolin repeat;
1786-1828 9.45e-03

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 36.90  E-value: 9.45e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 755560683  1786 FFWQGRHSTVSEKGTSALMTVELD-EERGA---QVQVLQGKEPPCFL 1828
Cdd:pfam00626   30 FLWVGKGSSLLEKLFAALLAAQLDdDERFPlpeVIRVPQGKEPARFL 76
 
Name Accession Description Interval E-value
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
1718-1831 3.20e-44

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: 155.89  E-value: 3.20e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755560683 1718 QFEIATVSVDVWHILEFDYSRLPRQSIGQFHEGDAYVVKWKYMastavgsrqkgehlvrVAGKEKCVYFFWQGRHSTVSE 1797
Cdd:cd11293     1 MYDDGSGKVEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQ----------------GGGKEEHILYFWQGRHSSQDE 64
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 755560683 1798 KGTSALMTVELDEE---RGAQVQVLQGKEPPCFLQCF 1831
Cdd:cd11293    65 RAAAALLTVELDEElkgRAVQVRVVQGKEPPHFLALF 101
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
1414-1510 2.77e-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: 130.05  E-value: 2.77e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755560683 1414 KLMLLQIKGRRHVQTRLVEPRASSLNSGDCFLLLSPQYCFLWVGEFSNVIEKAKASELATLIQTKRELGCRATYIQTIEE 1493
Cdd:cd11289     1 KPRLLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKVIVLDEGD 80
                          90
                  ....*....|....*..
gi 755560683 1494 GiNTHTHaakdFWKLLG 1510
Cdd:cd11289    81 T-NESPE----FWKVLG 92
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
1851-1956 1.64e-26

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: 105.01  E-value: 1.64e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755560683 1851 SEWRLYCVRGEVPMEGNLLEVACHCSSLRSRTSMVVLNINKalIYLWHGCKAQGHTKEVGRTAANKIKEECpleaglhss 1930
Cdd:cd11288     1 SPTRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKTPSS--VYLWVGKGSSEDERELAKDVASFLKPKA--------- 69
                          90       100
                  ....*....|....*....|....*.
gi 755560683 1931 snvTIHECDEGSEPLGFWDALGRRDR 1956
Cdd:cd11288    70 ---SLQEVAEGSEPDEFWEALGGKSE 92
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
1417-1511 5.89e-22

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 91.97  E-value: 5.89e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755560683   1417 LLQIKGRRHVQTRLVEPRASSLNSGDCFLLLSPQYCFLWVGEFSNVIEKAKASELATLIqtKRELGCRATYIQTIEEGIN 1496
Cdd:smart00262    2 LVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVEL--DDTLGPGPVQVRVVDEGKE 79
                            90
                    ....*....|....*
gi 755560683   1497 THThaakdFWKLLGG 1511
Cdd:smart00262   80 PPE-----FWSLFGG 89
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
1535-1635 6.25e-18

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: 80.49  E-value: 6.25e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755560683 1535 NCVYRLTDDKlvpdDDYWGKIPKCS-LLQSKEVLVFDFGSEVYVWHGKEVTLAQRKIAFQLAKHLWNGtfdyencdinpl 1613
Cdd:cd11280     2 PRLYRVRGSK----AIEIEEVPLASsSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKELDEE------------ 65
                          90       100
                  ....*....|....*....|...
gi 755560683 1614 DPGECNPLIPRKGQG-RPDWAIF 1635
Cdd:cd11280    66 RKGKPEIVRIRQGQEpREFWSLF 88
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
1416-1514 6.56e-17

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: 77.66  E-value: 6.56e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755560683 1416 MLLQIKGRRHVQTRLVE--PRASSLNSGDCFLLLSPQYCFLWVGEFSNVIEKAKASELATLIQTKRElgcratyIQTIEE 1493
Cdd:cd11288     4 RLFQVRGNGSGNTRAVEvdADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVASFLKPKAS-------LQEVAE 76
                          90       100
                  ....*....|....*....|.
gi 755560683 1494 GINThthaaKDFWKLLGGQTS 1514
Cdd:cd11288    77 GSEP-----DEFWEALGGKSE 92
VHP pfam02209
Villin headpiece domain;
2151-2186 7.42e-15

Villin headpiece domain;


Pssm-ID: 460493  Cd Length: 36  Bit Score: 70.10  E-value: 7.42e-15
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 755560683  2151 YLTDEDFEFALDMSRDEFNALPTWKQVNLKKSKGLF 2186
Cdd:pfam02209    1 YLSDEDFEEVFGMSREEFYKLPKWKQNNLKKKAGLF 36
VHP smart00153
Villin headpiece domain;
2151-2186 1.23e-14

Villin headpiece domain;


Pssm-ID: 128458  Cd Length: 36  Bit Score: 69.27  E-value: 1.23e-14
                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 755560683   2151 YLTDEDFEFALDMSRDEFNALPTWKQVNLKKSKGLF 2186
Cdd:smart00153    1 YLSDEDFEEVFGMTREEFYKLPLWKQNQLKKKKGLF 36
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
1973-2095 2.73e-13

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: 67.71  E-value: 2.73e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755560683 1973 PRLFILSSSSGDFSATEFVypaqapsavssmPFLQEDLYSApqpALFLVDNHHEVYLWQGWWPTENKItgsarirwasdr 2052
Cdd:cd11291     2 PRLFRCSNESGFFKVEEIS------------DFSQDDLDTD---DIMLLDTGDEVFVWVGSESSDEEK------------ 54
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 755560683 2053 KSAMETVLQYCRGKNLKRPPPKS--YLIHAGLEPLTFTNMFPSWE 2095
Cdd:cd11291    55 KEALTSAKKYIETDPLGRSKPRTpiYLVKQGNEPPTFTGYFHAWD 99
gelsolin_S1_like cd11290
Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; ...
1726-1840 2.93e-13

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: 68.02  E-value: 2.93e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755560683 1726 VDVWHILEFDYSRLPRQSIGQFHEGDAYVVkwkyMASTAVGSrqkgehlvrvaGKEKCVYFFWQGRHSTVSEKGTSALMT 1805
Cdd:cd11290    10 LQIWRIENFELVPVPESFYGKFYEGDSYIV----LKTTLDPS-----------GSLSYDIHYWLGKEASQDEAGAAAIKA 74
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 755560683 1806 VELDEERGAQ-VQV--LQGKEPPCFLQCFQGGMVVHSG 1840
Cdd:cd11290    75 VELDDYLGGRpVQHreVQGHESEEFLSYFKKGIIYIEG 112
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
1728-1834 1.01e-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: 65.78  E-value: 1.01e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755560683   1728 VWHILEFDYSRLPRQ--SIGQFHEGDAYVVKWkymastavgsrqkGEHLvrvagkekcvyFFWQGRHSTVSEKGTSALMT 1805
Cdd:smart00262    2 LVRVKGKRNVRVPEVpfSQGSLNSGDCYILDT-------------GSEI-----------YVWVGKKSSQDEKKKAAELA 57
                            90       100       110
                    ....*....|....*....|....*....|...
gi 755560683   1806 VELDEERG---AQVQ-VLQGKEPPCFLQCFQGG 1834
Cdd:smart00262   58 VELDDTLGpgpVQVRvVDEGKEPPEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
1856-1952 1.21e-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: 65.39  E-value: 1.21e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755560683   1856 YCVRGEVPMEGNLLEVACHCSSLRSRTSMVVLNinKALIYLWHGCKAQGHTKEVGRTAANKIKEECPleaglhsSSNVTI 1935
Cdd:smart00262    1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDT--GSEIYVWVGKKSSQDEKKKAAELAVELDDTLG-------PGPVQV 71
                            90
                    ....*....|....*..
gi 755560683   1936 HECDEGSEPLGFWDALG 1952
Cdd:smart00262   72 RVVDEGKEPPEFWSLFG 88
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
1972-2091 7.08e-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: 60.46  E-value: 7.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755560683 1972 APRLFILSSSSgdfsATEFVYPAQAPSAVSSMPFLQEDLYSapqpalflvdnhhEVYLWQGWwptenkitGSARIRWASD 2051
Cdd:cd11280     1 PPRLYRVRGSK----AIEIEEVPLASSSLDSDDVFVLDTGS-------------EIYIWQGR--------ASSQAELAAA 55
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 755560683 2052 RKSAMETVLQYcrgknlkRPPPKSYLIHAGLEPLTFTNMF 2091
Cdd:cd11280    56 ALLAKELDEER-------KGKPEIVRIRQGQEPREFWSLF 88
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
1559-1651 8.51e-09

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: 54.95  E-value: 8.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755560683 1559 SLLQSKEVLVFDFGSEVYVWHGKEVTLAQRKIAFQLA-KHLwngtfdyencdinpldpgecnpliprKGQGRPDWAIFGR 1637
Cdd:cd11292    29 EMLDSEDCYILDCGSEIFVWVGKGASLDERKAALKNAeEFL--------------------------RKKKRPPYTQVTR 82
                          90
                  ....*....|....
gi 755560683 1638 VTEHNETILFKEKF 1651
Cdd:cd11292    83 VTEGGESALFKSKF 96
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
2000-2094 1.08e-06

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: 48.44  E-value: 1.08e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755560683   2000 VSSMPFLQEDLYSApqpALFLVDNHHEVYLWQGwwptenkiTGSARirwaSDRKSAMETVLQYCrgKNLKRPPPKSYLIH 2079
Cdd:smart00262   13 VPEVPFSQGSLNSG---DCYILDTGSEIYVWVG--------KKSSQ----DEKKKAAELAVELD--DTLGPGPVQVRVVD 75
                            90
                    ....*....|....*
gi 755560683   2080 AGLEPLTFTNMFPSW 2094
Cdd:smart00262   76 EGKEPPEFWSLFGGW 90
Gelsolin pfam00626
Gelsolin repeat;
1435-1494 5.76e-06

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 46.15  E-value: 5.76e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755560683  1435 ASSLNSGDCFLLLSPQYCFLWVGEFSNVIEKAKASELAT-LIQTKRelgCRATYIQTIEEG 1494
Cdd:pfam00626   12 QESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAqLDDDER---FPLPEVIRVPQG 69
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
1556-1654 7.90e-06

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: 46.13  E-value: 7.90e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755560683   1556 PKCSLLQSKEVLVFDFGSEVYVWHGKEVTLAQRKIAFQLAKHLwngtFDYENcdinpldpgecnpliPRKGQGRpdwaif 1635
Cdd:smart00262   18 FSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVEL----DDTLG---------------PGPVQVR------ 72
                            90
                    ....*....|....*....
gi 755560683   1636 gRVTEHNETILFKEKFLDW 1654
Cdd:smart00262   73 -VVDEGKEPPEFWSLFGGW 90
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
1783-1831 3.72e-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: 44.28  E-value: 3.72e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 755560683 1783 CVYFFWQGRHSTVSEKGTSALMTVELDEERG---AQVQVLQGKEPPCFLQCF 1831
Cdd:cd11280    37 SEIYIWQGRASSQAELAAAALLAKELDEERKgkpEIVRIRQGQEPREFWSLF 88
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
1436-1507 4.10e-05

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


Pssm-ID: 200448  Cd Length: 98  Bit Score: 44.16  E-value: 4.10e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755560683 1436 SSLNSGDCFLLLSPQYCFLWVGEFSNVIEKAKASELAT-LIQTKRElgCRATYIQTIEEGinTHTHAAKDFWK 1507
Cdd:cd11292    29 EMLDSEDCYILDCGSEIFVWVGKGASLDERKAALKNAEeFLRKKKR--PPYTQVTRVTEG--GESALFKSKFA 97
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
1431-1509 6.61e-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: 43.51  E-value: 6.61e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755560683 1431 VEPRASSLNSGDCFLLLSPQYCFLWVGEFSNVIEKAKASELATliQTKRELGCRATYIQtIEEGinthtHAAKDFWKLL 1509
Cdd:cd11280    18 VPLASSSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAK--ELDEERKGKPEIVR-IRQG-----QEPREFWSLF 88
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
1556-1602 1.32e-04

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


Pssm-ID: 200444  Cd Length: 92  Bit Score: 42.60  E-value: 1.32e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 755560683 1556 PKCSLLQSKEVLVFDFGSEVYVWHGKEVTLAQRKIAFQLAKHLWNGT 1602
Cdd:cd11288    23 ADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVASFLKPKA 69
Gelsolin pfam00626
Gelsolin repeat;
1786-1828 9.45e-03

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 36.90  E-value: 9.45e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 755560683  1786 FFWQGRHSTVSEKGTSALMTVELD-EERGA---QVQVLQGKEPPCFL 1828
Cdd:pfam00626   30 FLWVGKGSSLLEKLFAALLAAQLDdDERFPlpeVIRVPQGKEPARFL 76
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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