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Conserved domains on  [gi|2228568390|ref|NP_001392209|]
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supervillin isoform d [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; ...
 1703-1816 3.18e-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: 3.18e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568390 1703 QFEIATVSVDVWHILEFDYSRLPRQSIGQFHEGDAYVVKWKYMastavgsrqkgehlvrVAGKEKCVYFFWQGRHSTVSE 1782
Cdd:cd11293      1 MYDDGSGKVEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQ----------------GGGKEEHILYFWQGRHSSQDE 64

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2228568390 1783 KGTSALMTVELDEE---RGAQVQVLQGKEPPCFLQCF 1816
Cdd:cd11293     65 RAAAALLTVELDEElkgRAVQVRVVQGKEPPHFLALF 101
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 1399-1495 2.75e-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: 2.75e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568390 1399 KLMLLQIKGRRHVQTRLVEPRASSLNSGDCFLLLSPQYCFLWVGEFSNVIEKAKASELATLIQTKRELGCRATYIQTIEE 1478
Cdd:cd11289      1 KPRLLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKVIVLDEGD 80

                           90
                   ....*....|....*..
gi 2228568390 1479 GiNTHTHaakdFWKLLG 1495
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; ...
 1836-1941 1.54e-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: 1.54e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568390 1836 SEWRLYCVRGEVPMEGNLLEVACHCSSLRSRTSMVVLNINKalIYLWHGCKAQGHTKEVGRTAANKIKEECpleaglhss 1915
Cdd:cd11288      1 SPTRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKTPSS--VYLWVGKGSSEDERELAKDVASFLKPKA--------- 69

                           90       100
                   ....*....|....*....|....*.
gi 2228568390 1916 snvTIHECDEGSEPLGFWDALGRRDR 1941
Cdd:cd11288     70 ---SLQEVAEGSEPDEFWEALGGKSE 92
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 1520-1620 6.32e-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: 6.32e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568390 1520 NCVYRLTDDKlvpdDDYWGKIPKCS-LLQSKEVLVFDFGSEVYVWHGKEVTLAQRKIAFQLAKHLWNGtfdyencdinpl 1598
Cdd:cd11280      2 PRLYRVRGSK----AIEIEEVPLASsSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKELDEE------------ 65

                           90       100
                   ....*....|....*....|...
gi 2228568390 1599 DPGECNPLIPRKGQG-RPDWAIF 1620
Cdd:cd11280     66 RKGKPEIVRIRQGQEpREFWSLF 88
VHP pfam02209
Villin headpiece domain;
2136-2171 7.73e-15

Villin headpiece domain;


:

Pssm-ID: 460493  Cd Length: 36  Bit Score: 70.10  E-value: 7.73e-15
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 2228568390 2136 YLTDEDFEFALDMSRDEFNALPTWKQVNLKKSKGLF 2171
Cdd:pfam02209    1 YLSDEDFEEVFGMSREEFYKLPKWKQNNLKKKAGLF 36
ADF_gelsolin super family cl15697
Actin depolymerization factor/cofilin- and gelsolin-like domains; Actin depolymerization ...
 1958-2080 2.55e-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: 2.55e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568390 1958 PRLFILSSSSGDFSATEFVypaqapsavssmPFLQEDLYSApqpALFLVDNHHEVYLWQGWWPTENKItgsarirwasdr 2037
Cdd:cd11291      2 PRLFRCSNESGFFKVEEIS------------DFSQDDLDTD---DIMLLDTGDEVFVWVGSESSDEEK------------ 54

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 2228568390 2038 KSAMETVLQYCRGKNLKRPPPKS--YLIHAGLEPLTFTNMFPSWE 2080
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; ...
 1703-1816 3.18e-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: 3.18e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568390 1703 QFEIATVSVDVWHILEFDYSRLPRQSIGQFHEGDAYVVKWKYMastavgsrqkgehlvrVAGKEKCVYFFWQGRHSTVSE 1782
Cdd:cd11293      1 MYDDGSGKVEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQ----------------GGGKEEHILYFWQGRHSSQDE 64

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2228568390 1783 KGTSALMTVELDEE---RGAQVQVLQGKEPPCFLQCF 1816
Cdd:cd11293     65 RAAAALLTVELDEElkgRAVQVRVVQGKEPPHFLALF 101
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 1399-1495 2.75e-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: 2.75e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568390 1399 KLMLLQIKGRRHVQTRLVEPRASSLNSGDCFLLLSPQYCFLWVGEFSNVIEKAKASELATLIQTKRELGCRATYIQTIEE 1478
Cdd:cd11289      1 KPRLLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKVIVLDEGD 80

                           90
                   ....*....|....*..
gi 2228568390 1479 GiNTHTHaakdFWKLLG 1495
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; ...
 1836-1941 1.54e-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: 1.54e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568390 1836 SEWRLYCVRGEVPMEGNLLEVACHCSSLRSRTSMVVLNINKalIYLWHGCKAQGHTKEVGRTAANKIKEECpleaglhss 1915
Cdd:cd11288      1 SPTRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKTPSS--VYLWVGKGSSEDERELAKDVASFLKPKA--------- 69

                           90       100
                   ....*....|....*....|....*.
gi 2228568390 1916 snvTIHECDEGSEPLGFWDALGRRDR 1941
Cdd:cd11288     70 ---SLQEVAEGSEPDEFWEALGGKSE 92
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1402-1496 5.84e-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: 5.84e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568390  1402 LLQIKGRRHVQTRLVEPRASSLNSGDCFLLLSPQYCFLWVGEFSNVIEKAKASELATLIqtKRELGCRATYIQTIEEGIN 1481
Cdd:smart00262    2 LVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVEL--DDTLGPGPVQVRVVDEGKE 79

                            90
                    ....*....|....*
gi 2228568390  1482 THThaakdFWKLLGG 1496
Cdd:smart00262   80 PPE-----FWSLFGG 89
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 1520-1620 6.32e-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: 6.32e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568390 1520 NCVYRLTDDKlvpdDDYWGKIPKCS-LLQSKEVLVFDFGSEVYVWHGKEVTLAQRKIAFQLAKHLWNGtfdyencdinpl 1598
Cdd:cd11280      2 PRLYRVRGSK----AIEIEEVPLASsSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKELDEE------------ 65

                           90       100
                   ....*....|....*....|...
gi 2228568390 1599 DPGECNPLIPRKGQG-RPDWAIF 1620
Cdd:cd11280     66 RKGKPEIVRIRQGQEpREFWSLF 88
VHP pfam02209
Villin headpiece domain;
2136-2171 7.73e-15

Villin headpiece domain;


Pssm-ID: 460493  Cd Length: 36  Bit Score: 70.10  E-value: 7.73e-15
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 2228568390 2136 YLTDEDFEFALDMSRDEFNALPTWKQVNLKKSKGLF 2171
Cdd:pfam02209    1 YLSDEDFEEVFGMSREEFYKLPKWKQNNLKKKAGLF 36
VHP smart00153
Villin headpiece domain;
2136-2171 1.28e-14

Villin headpiece domain;


Pssm-ID: 128458  Cd Length: 36  Bit Score: 69.27  E-value: 1.28e-14
                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 2228568390  2136 YLTDEDFEFALDMSRDEFNALPTWKQVNLKKSKGLF 2171
Cdd:smart00153    1 YLSDEDFEEVFGMTREEFYKLPLWKQNQLKKKKGLF 36
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 1958-2080 2.55e-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: 2.55e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568390 1958 PRLFILSSSSGDFSATEFVypaqapsavssmPFLQEDLYSApqpALFLVDNHHEVYLWQGWWPTENKItgsarirwasdr 2037
Cdd:cd11291      2 PRLFRCSNESGFFKVEEIS------------DFSQDDLDTD---DIMLLDTGDEVFVWVGSESSDEEK------------ 54

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 2228568390 2038 KSAMETVLQYCRGKNLKRPPPKS--YLIHAGLEPLTFTNMFPSWE 2080
Cdd:cd11291     55 KEALTSAKKYIETDPLGRSKPRTpiYLVKQGNEPPTFTGYFHAWD 99
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1713-1819 1.00e-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: 1.00e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568390  1713 VWHILEFDYSRLPRQ--SIGQFHEGDAYVVKWkymastavgsrqkGEHLvrvagkekcvyFFWQGRHSTVSEKGTSALMT 1790
Cdd:smart00262    2 LVRVKGKRNVRVPEVpfSQGSLNSGDCYILDT-------------GSEI-----------YVWVGKKSSQDEKKKAAELA 57

                            90       100       110
                    ....*....|....*....|....*....|...
gi 2228568390  1791 VELDEERG---AQVQ-VLQGKEPPCFLQCFQGG 1819
Cdd:smart00262   58 VELDDTLGpgpVQVRvVDEGKEPPEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1841-1937 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 2228568390  1841 YCVRGEVPMEGNLLEVACHCSSLRSRTSMVVLNinKALIYLWHGCKAQGHTKEVGRTAANKIKEECPleaglhsSSNVTI 1920
Cdd:smart00262    1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDT--GSEIYVWVGKKSSQDEKKKAAELAVELDDTLG-------PGPVQV 71

                            90
                    ....*....|....*..
gi 2228568390  1921 HECDEGSEPLGFWDALG 1937
Cdd:smart00262   72 RVVDEGKEPPEFWSLFG 88
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1985-2079 1.07e-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: 1.07e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568390  1985 VSSMPFLQEDLYSApqpALFLVDNHHEVYLWQGwwptenkiTGSARirwaSDRKSAMETVLQYCrgKNLKRPPPKSYLIH 2064
Cdd:smart00262   13 VPEVPFSQGSLNSG---DCYILDTGSEIYVWVG--------KKSSQ----DEKKKAAELAVELD--DTLGPGPVQVRVVD 75

                            90
                    ....*....|....*
gi 2228568390  2065 AGLEPLTFTNMFPSW 2079
Cdd:smart00262   76 EGKEPPEFWSLFGGW 90
Gelsolin pfam00626
Gelsolin repeat;
1420-1479 5.61e-06

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 46.15  E-value: 5.61e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2228568390 1420 ASSLNSGDCFLLLSPQYCFLWVGEFSNVIEKAKASELAT-LIQTKRelgCRATYIQTIEEG 1479
Cdd:pfam00626   12 QESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAqLDDDER---FPLPEVIRVPQG 69
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1541-1639 7.85e-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: 7.85e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568390  1541 PKCSLLQSKEVLVFDFGSEVYVWHGKEVTLAQRKIAFQLAKHLwngtFDYENcdinpldpgecnpliPRKGQGRpdwaif 1620
Cdd:smart00262   18 FSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVEL----DDTLG---------------PGPVQVR------ 72

                            90
                    ....*....|....*....
gi 2228568390  1621 gRVTEHNETILFKEKFLDW 1639
Cdd:smart00262   73 -VVDEGKEPPEFWSLFGGW 90
Gelsolin pfam00626
Gelsolin repeat;
1771-1813 9.30e-03

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 36.90  E-value: 9.30e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 2228568390 1771 FFWQGRHSTVSEKGTSALMTVELD-EERGA---QVQVLQGKEPPCFL 1813
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; ...
 1703-1816 3.18e-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: 3.18e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568390 1703 QFEIATVSVDVWHILEFDYSRLPRQSIGQFHEGDAYVVKWKYMastavgsrqkgehlvrVAGKEKCVYFFWQGRHSTVSE 1782
Cdd:cd11293      1 MYDDGSGKVEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQ----------------GGGKEEHILYFWQGRHSSQDE 64

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2228568390 1783 KGTSALMTVELDEE---RGAQVQVLQGKEPPCFLQCF 1816
Cdd:cd11293     65 RAAAALLTVELDEElkgRAVQVRVVQGKEPPHFLALF 101
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 1399-1495 2.75e-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: 2.75e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568390 1399 KLMLLQIKGRRHVQTRLVEPRASSLNSGDCFLLLSPQYCFLWVGEFSNVIEKAKASELATLIQTKRELGCRATYIQTIEE 1478
Cdd:cd11289      1 KPRLLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKVIVLDEGD 80

                           90
                   ....*....|....*..
gi 2228568390 1479 GiNTHTHaakdFWKLLG 1495
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; ...
 1836-1941 1.54e-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: 1.54e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568390 1836 SEWRLYCVRGEVPMEGNLLEVACHCSSLRSRTSMVVLNINKalIYLWHGCKAQGHTKEVGRTAANKIKEECpleaglhss 1915
Cdd:cd11288      1 SPTRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKTPSS--VYLWVGKGSSEDERELAKDVASFLKPKA--------- 69

                           90       100
                   ....*....|....*....|....*.
gi 2228568390 1916 snvTIHECDEGSEPLGFWDALGRRDR 1941
Cdd:cd11288     70 ---SLQEVAEGSEPDEFWEALGGKSE 92
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1402-1496 5.84e-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: 5.84e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568390  1402 LLQIKGRRHVQTRLVEPRASSLNSGDCFLLLSPQYCFLWVGEFSNVIEKAKASELATLIqtKRELGCRATYIQTIEEGIN 1481
Cdd:smart00262    2 LVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVEL--DDTLGPGPVQVRVVDEGKE 79

                            90
                    ....*....|....*
gi 2228568390  1482 THThaakdFWKLLGG 1496
Cdd:smart00262   80 PPE-----FWSLFGG 89
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 1520-1620 6.32e-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: 6.32e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568390 1520 NCVYRLTDDKlvpdDDYWGKIPKCS-LLQSKEVLVFDFGSEVYVWHGKEVTLAQRKIAFQLAKHLWNGtfdyencdinpl 1598
Cdd:cd11280      2 PRLYRVRGSK----AIEIEEVPLASsSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKELDEE------------ 65

                           90       100
                   ....*....|....*....|...
gi 2228568390 1599 DPGECNPLIPRKGQG-RPDWAIF 1620
Cdd:cd11280     66 RKGKPEIVRIRQGQEpREFWSLF 88
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 1401-1499 6.09e-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: 6.09e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568390 1401 MLLQIKGRRHVQTRLVE--PRASSLNSGDCFLLLSPQYCFLWVGEFSNVIEKAKASELATLIQTKRElgcratyIQTIEE 1478
Cdd:cd11288      4 RLFQVRGNGSGNTRAVEvdADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVASFLKPKAS-------LQEVAE 76

                           90       100
                   ....*....|....*....|.
gi 2228568390 1479 GINThthaaKDFWKLLGGQTS 1499
Cdd:cd11288     77 GSEP-----DEFWEALGGKSE 92
VHP pfam02209
Villin headpiece domain;
2136-2171 7.73e-15

Villin headpiece domain;


Pssm-ID: 460493  Cd Length: 36  Bit Score: 70.10  E-value: 7.73e-15
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 2228568390 2136 YLTDEDFEFALDMSRDEFNALPTWKQVNLKKSKGLF 2171
Cdd:pfam02209    1 YLSDEDFEEVFGMSREEFYKLPKWKQNNLKKKAGLF 36
VHP smart00153
Villin headpiece domain;
2136-2171 1.28e-14

Villin headpiece domain;


Pssm-ID: 128458  Cd Length: 36  Bit Score: 69.27  E-value: 1.28e-14
                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 2228568390  2136 YLTDEDFEFALDMSRDEFNALPTWKQVNLKKSKGLF 2171
Cdd:smart00153    1 YLSDEDFEEVFGMTREEFYKLPLWKQNQLKKKKGLF 36
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 1958-2080 2.55e-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: 2.55e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568390 1958 PRLFILSSSSGDFSATEFVypaqapsavssmPFLQEDLYSApqpALFLVDNHHEVYLWQGWWPTENKItgsarirwasdr 2037
Cdd:cd11291      2 PRLFRCSNESGFFKVEEIS------------DFSQDDLDTD---DIMLLDTGDEVFVWVGSESSDEEK------------ 54

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 2228568390 2038 KSAMETVLQYCRGKNLKRPPPKS--YLIHAGLEPLTFTNMFPSWE 2080
Cdd:cd11291     55 KEALTSAKKYIETDPLGRSKPRTpiYLVKQGNEPPTFTGYFHAWD 99
gelsolin_S1_like cd11290
Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; ...
 1711-1825 2.90e-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: 2.90e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568390 1711 VDVWHILEFDYSRLPRQSIGQFHEGDAYVVkwkyMASTAVGSrqkgehlvrvaGKEKCVYFFWQGRHSTVSEKGTSALMT 1790
Cdd:cd11290     10 LQIWRIENFELVPVPESFYGKFYEGDSYIV----LKTTLDPS-----------GSLSYDIHYWLGKEASQDEAGAAAIKA 74

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2228568390 1791 VELDEERGAQ-VQV--LQGKEPPCFLQCFQGGMVVHSG 1825
Cdd:cd11290     75 VELDDYLGGRpVQHreVQGHESEEFLSYFKKGIIYIEG 112
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1713-1819 1.00e-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: 1.00e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568390  1713 VWHILEFDYSRLPRQ--SIGQFHEGDAYVVKWkymastavgsrqkGEHLvrvagkekcvyFFWQGRHSTVSEKGTSALMT 1790
Cdd:smart00262    2 LVRVKGKRNVRVPEVpfSQGSLNSGDCYILDT-------------GSEI-----------YVWVGKKSSQDEKKKAAELA 57

                            90       100       110
                    ....*....|....*....|....*....|...
gi 2228568390  1791 VELDEERG---AQVQ-VLQGKEPPCFLQCFQGG 1819
Cdd:smart00262   58 VELDDTLGpgpVQVRvVDEGKEPPEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1841-1937 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 2228568390  1841 YCVRGEVPMEGNLLEVACHCSSLRSRTSMVVLNinKALIYLWHGCKAQGHTKEVGRTAANKIKEECPleaglhsSSNVTI 1920
Cdd:smart00262    1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDT--GSEIYVWVGKKSSQDEKKKAAELAVELDDTLG-------PGPVQV 71

                            90
                    ....*....|....*..
gi 2228568390  1921 HECDEGSEPLGFWDALG 1937
Cdd:smart00262   72 RVVDEGKEPPEFWSLFG 88
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 1957-2076 7.10e-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: 7.10e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568390 1957 APRLFILSSSSgdfsATEFVYPAQAPSAVSSMPFLQEDLYSapqpalflvdnhhEVYLWQGWwptenkitGSARIRWASD 2036
Cdd:cd11280      1 PPRLYRVRGSK----AIEIEEVPLASSSLDSDDVFVLDTGS-------------EIYIWQGR--------ASSQAELAAA 55

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 2228568390 2037 RKSAMETVLQYcrgknlkRPPPKSYLIHAGLEPLTFTNMF 2076
Cdd:cd11280     56 ALLAKELDEER-------KGKPEIVRIRQGQEPREFWSLF 88
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 1544-1636 8.53e-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: 8.53e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568390 1544 SLLQSKEVLVFDFGSEVYVWHGKEVTLAQRKIAFQLA-KHLwngtfdyencdinpldpgecnpliprKGQGRPDWAIFGR 1622
Cdd:cd11292     29 EMLDSEDCYILDCGSEIFVWVGKGASLDERKAALKNAeEFL--------------------------RKKKRPPYTQVTR 82

                           90
                   ....*....|....
gi 2228568390 1623 VTEHNETILFKEKF 1636
Cdd:cd11292     83 VTEGGESALFKSKF 96
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1985-2079 1.07e-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: 1.07e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568390  1985 VSSMPFLQEDLYSApqpALFLVDNHHEVYLWQGwwptenkiTGSARirwaSDRKSAMETVLQYCrgKNLKRPPPKSYLIH 2064
Cdd:smart00262   13 VPEVPFSQGSLNSG---DCYILDTGSEIYVWVG--------KKSSQ----DEKKKAAELAVELD--DTLGPGPVQVRVVD 75

                            90
                    ....*....|....*
gi 2228568390  2065 AGLEPLTFTNMFPSW 2079
Cdd:smart00262   76 EGKEPPEFWSLFGGW 90
Gelsolin pfam00626
Gelsolin repeat;
1420-1479 5.61e-06

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 46.15  E-value: 5.61e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2228568390 1420 ASSLNSGDCFLLLSPQYCFLWVGEFSNVIEKAKASELAT-LIQTKRelgCRATYIQTIEEG 1479
Cdd:pfam00626   12 QESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAqLDDDER---FPLPEVIRVPQG 69
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1541-1639 7.85e-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: 7.85e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228568390  1541 PKCSLLQSKEVLVFDFGSEVYVWHGKEVTLAQRKIAFQLAKHLwngtFDYENcdinpldpgecnpliPRKGQGRpdwaif 1620
Cdd:smart00262   18 FSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVEL----DDTLG---------------PGPVQVR------ 72

                            90
                    ....*....|....*....
gi 2228568390  1621 gRVTEHNETILFKEKFLDW 1639
Cdd:smart00262   73 -VVDEGKEPPEFWSLFGGW 90
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 1768-1816 3.73e-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: 3.73e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2228568390 1768 CVYFFWQGRHSTVSEKGTSALMTVELDEERG---AQVQVLQGKEPPCFLQCF 1816
Cdd:cd11280     37 SEIYIWQGRASSQAELAAAALLAKELDEERKgkpEIVRIRQGQEPREFWSLF 88
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 1421-1492 4.07e-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: 4.07e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2228568390 1421 SSLNSGDCFLLLSPQYCFLWVGEFSNVIEKAKASELAT-LIQTKRElgCRATYIQTIEEGinTHTHAAKDFWK 1492
Cdd:cd11292     29 EMLDSEDCYILDCGSEIFVWVGKGASLDERKAALKNAEeFLRKKKR--PPYTQVTRVTEG--GESALFKSKFA 97
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 1416-1494 6.57e-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: 6.57e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2228568390 1416 VEPRASSLNSGDCFLLLSPQYCFLWVGEFSNVIEKAKASELATliQTKRELGCRATYIQtIEEGinthtHAAKDFWKLL 1494
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; ...
 1541-1587 1.29e-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: 1.29e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 2228568390 1541 PKCSLLQSKEVLVFDFGSEVYVWHGKEVTLAQRKIAFQLAKHLWNGT 1587
Cdd:cd11288     23 ADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVASFLKPKA 69
Gelsolin pfam00626
Gelsolin repeat;
1771-1813 9.30e-03

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 36.90  E-value: 9.30e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 2228568390 1771 FFWQGRHSTVSEKGTSALMTVELD-EERGA---QVQVLQGKEPPCFL 1813
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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