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Conserved domains on  [gi|1907129396|ref|XP_036016975|]
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supervillin isoform X10 [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; ...
 1648-1761 3.09e-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: 3.09e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129396 1648 QFEIATVSVDVWHILEFDYSRLPRQSIGQFHEGDAYVVKWKYMastavgsrqkgehlvrVAGKEKCVYFFWQGRHSTVSE 1727
Cdd:cd11293      1 MYDDGSGKVEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQ----------------GGGKEEHILYFWQGRHSSQDE 64

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1907129396 1728 KGTSALMTVELDEE---RGAQVQVLQGKEPPCFLQCF 1761
Cdd:cd11293     65 RAAAALLTVELDEElkgRAVQVRVVQGKEPPHFLALF 101
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 1344-1440 2.36e-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: 2.36e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129396 1344 KLMLLQIKGRRHVQTRLVEPRASSLNSGDCFLLLSPQYCFLWVGEFSNVIEKAKASELATLIQTKRELGCRATYIQTIEE 1423
Cdd:cd11289      1 KPRLLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKVIVLDEGD 80

                           90
                   ....*....|....*..
gi 1907129396 1424 GiNTHTHaakdFWKLLG 1440
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; ...
 1781-1886 1.53e-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: 1.53e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129396 1781 SEWRLYCVRGEVPMEGNLLEVACHCSSLRSRTSMVVLNINKalIYLWHGCKAQGHTKEVGRTAANKIKEECpleaglhss 1860
Cdd:cd11288      1 SPTRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKTPSS--VYLWVGKGSSEDERELAKDVASFLKPKA--------- 69

                           90       100
                   ....*....|....*....|....*.
gi 1907129396 1861 snvTIHECDEGSEPLGFWDALGRRDR 1886
Cdd:cd11288     70 ---SLQEVAEGSEPDEFWEALGGKSE 92
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 1465-1565 5.22e-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: 5.22e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129396 1465 NCVYRLTDDKlvpdDDYWGKIPKCS-LLQSKEVLVFDFGSEVYVWHGKEVTLAQRKIAFQLAKHLWNGtfdyencdinpl 1543
Cdd:cd11280      2 PRLYRVRGSK----AIEIEEVPLASsSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKELDEE------------ 65

                           90       100
                   ....*....|....*....|...
gi 1907129396 1544 DPGECNPLIPRKGQG-RPDWAIF 1565
Cdd:cd11280     66 RKGKPEIVRIRQGQEpREFWSLF 88
VHP pfam02209
Villin headpiece domain;
2081-2116 7.69e-15

Villin headpiece domain;


:

Pssm-ID: 460493  Cd Length: 36  Bit Score: 69.71  E-value: 7.69e-15
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1907129396 2081 YLTDEDFEFALDMSRDEFNALPTWKQVNLKKSKGLF 2116
Cdd:pfam02209    1 YLSDEDFEEVFGMSREEFYKLPKWKQNNLKKKAGLF 36
ADF_gelsolin super family cl15697
Actin depolymerization factor/cofilin- and gelsolin-like domains; Actin depolymerization ...
 1903-2025 2.69e-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: 2.69e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129396 1903 PRLFILSSSSGDFSATEFVypaqapsavssmPFLQEDLYSApqpALFLVDNHHEVYLWQGWWPTENKItgsarirwasdr 1982
Cdd:cd11291      2 PRLFRCSNESGFFKVEEIS------------DFSQDDLDTD---DIMLLDTGDEVFVWVGSESSDEEK------------ 54

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1907129396 1983 KSAMETVLQYCRGKNLKRPPPKS--YLIHAGLEPLTFTNMFPSWE 2025
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; ...
 1648-1761 3.09e-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: 3.09e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129396 1648 QFEIATVSVDVWHILEFDYSRLPRQSIGQFHEGDAYVVKWKYMastavgsrqkgehlvrVAGKEKCVYFFWQGRHSTVSE 1727
Cdd:cd11293      1 MYDDGSGKVEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQ----------------GGGKEEHILYFWQGRHSSQDE 64

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1907129396 1728 KGTSALMTVELDEE---RGAQVQVLQGKEPPCFLQCF 1761
Cdd:cd11293     65 RAAAALLTVELDEElkgRAVQVRVVQGKEPPHFLALF 101
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 1344-1440 2.36e-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: 2.36e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129396 1344 KLMLLQIKGRRHVQTRLVEPRASSLNSGDCFLLLSPQYCFLWVGEFSNVIEKAKASELATLIQTKRELGCRATYIQTIEE 1423
Cdd:cd11289      1 KPRLLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKVIVLDEGD 80

                           90
                   ....*....|....*..
gi 1907129396 1424 GiNTHTHaakdFWKLLG 1440
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; ...
 1781-1886 1.53e-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: 1.53e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129396 1781 SEWRLYCVRGEVPMEGNLLEVACHCSSLRSRTSMVVLNINKalIYLWHGCKAQGHTKEVGRTAANKIKEECpleaglhss 1860
Cdd:cd11288      1 SPTRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKTPSS--VYLWVGKGSSEDERELAKDVASFLKPKA--------- 69

                           90       100
                   ....*....|....*....|....*.
gi 1907129396 1861 snvTIHECDEGSEPLGFWDALGRRDR 1886
Cdd:cd11288     70 ---SLQEVAEGSEPDEFWEALGGKSE 92
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1347-1441 5.69e-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: 5.69e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129396  1347 LLQIKGRRHVQTRLVEPRASSLNSGDCFLLLSPQYCFLWVGEFSNVIEKAKASELATLIqtKRELGCRATYIQTIEEGIN 1426
Cdd:smart00262    2 LVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVEL--DDTLGPGPVQVRVVDEGKE 79

                            90
                    ....*....|....*
gi 1907129396  1427 THThaakdFWKLLGG 1441
Cdd:smart00262   80 PPE-----FWSLFGG 89
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 1465-1565 5.22e-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: 5.22e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129396 1465 NCVYRLTDDKlvpdDDYWGKIPKCS-LLQSKEVLVFDFGSEVYVWHGKEVTLAQRKIAFQLAKHLWNGtfdyencdinpl 1543
Cdd:cd11280      2 PRLYRVRGSK----AIEIEEVPLASsSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKELDEE------------ 65

                           90       100
                   ....*....|....*....|...
gi 1907129396 1544 DPGECNPLIPRKGQG-RPDWAIF 1565
Cdd:cd11280     66 RKGKPEIVRIRQGQEpREFWSLF 88
VHP pfam02209
Villin headpiece domain;
2081-2116 7.69e-15

Villin headpiece domain;


Pssm-ID: 460493  Cd Length: 36  Bit Score: 69.71  E-value: 7.69e-15
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1907129396 2081 YLTDEDFEFALDMSRDEFNALPTWKQVNLKKSKGLF 2116
Cdd:pfam02209    1 YLSDEDFEEVFGMSREEFYKLPKWKQNNLKKKAGLF 36
VHP smart00153
Villin headpiece domain;
2081-2116 1.20e-14

Villin headpiece domain;


Pssm-ID: 128458  Cd Length: 36  Bit Score: 69.27  E-value: 1.20e-14
                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 1907129396  2081 YLTDEDFEFALDMSRDEFNALPTWKQVNLKKSKGLF 2116
Cdd:smart00153    1 YLSDEDFEEVFGMTREEFYKLPLWKQNQLKKKKGLF 36
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 1903-2025 2.69e-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: 2.69e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129396 1903 PRLFILSSSSGDFSATEFVypaqapsavssmPFLQEDLYSApqpALFLVDNHHEVYLWQGWWPTENKItgsarirwasdr 1982
Cdd:cd11291      2 PRLFRCSNESGFFKVEEIS------------DFSQDDLDTD---DIMLLDTGDEVFVWVGSESSDEEK------------ 54

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1907129396 1983 KSAMETVLQYCRGKNLKRPPPKS--YLIHAGLEPLTFTNMFPSWE 2025
Cdd:cd11291     55 KEALTSAKKYIETDPLGRSKPRTpiYLVKQGNEPPTFTGYFHAWD 99
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1658-1764 9.76e-13

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 65.78  E-value: 9.76e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129396  1658 VWHILEFDYSRLPRQ--SIGQFHEGDAYVVKWkymastavgsrqkGEHLvrvagkekcvyFFWQGRHSTVSEKGTSALMT 1735
Cdd:smart00262    2 LVRVKGKRNVRVPEVpfSQGSLNSGDCYILDT-------------GSEI-----------YVWVGKKSSQDEKKKAAELA 57

                            90       100       110
                    ....*....|....*....|....*....|...
gi 1907129396  1736 VELDEERG---AQVQ-VLQGKEPPCFLQCFQGG 1764
Cdd:smart00262   58 VELDDTLGpgpVQVRvVDEGKEPPEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1786-1882 1.18e-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: 1.18e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129396  1786 YCVRGEVPMEGNLLEVACHCSSLRSRTSMVVLNinKALIYLWHGCKAQGHTKEVGRTAANKIKEECPleaglhsSSNVTI 1865
Cdd:smart00262    1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDT--GSEIYVWVGKKSSQDEKKKAAELAVELDDTLG-------PGPVQV 71

                            90
                    ....*....|....*..
gi 1907129396  1866 HECDEGSEPLGFWDALG 1882
Cdd:smart00262   72 RVVDEGKEPPEFWSLFG 88
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1930-2024 1.04e-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: 1.04e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129396  1930 VSSMPFLQEDLYSApqpALFLVDNHHEVYLWQGwwptenkiTGSARirwaSDRKSAMETVLQYCrgKNLKRPPPKSYLIH 2009
Cdd:smart00262   13 VPEVPFSQGSLNSG---DCYILDTGSEIYVWVG--------KKSSQ----DEKKKAAELAVELD--DTLGPGPVQVRVVD 75

                            90
                    ....*....|....*
gi 1907129396  2010 AGLEPLTFTNMFPSW 2024
Cdd:smart00262   76 EGKEPPEFWSLFGGW 90
Gelsolin pfam00626
Gelsolin repeat;
1365-1424 5.57e-06

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 46.15  E-value: 5.57e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907129396 1365 ASSLNSGDCFLLLSPQYCFLWVGEFSNVIEKAKASELAT-LIQTKRelgCRATYIQTIEEG 1424
Cdd:pfam00626   12 QESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAqLDDDER---FPLPEVIRVPQG 69
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1486-1584 7.64e-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: 7.64e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129396  1486 PKCSLLQSKEVLVFDFGSEVYVWHGKEVTLAQRKIAFQLAKHLwngtFDYENcdinpldpgecnpliPRKGQGRpdwaif 1565
Cdd:smart00262   18 FSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVEL----DDTLG---------------PGPVQVR------ 72

                            90
                    ....*....|....*....
gi 1907129396  1566 gRVTEHNETILFKEKFLDW 1584
Cdd:smart00262   73 -VVDEGKEPPEFWSLFGGW 90
Gelsolin pfam00626
Gelsolin repeat;
1716-1758 9.15e-03

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 36.90  E-value: 9.15e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1907129396 1716 FFWQGRHSTVSEKGTSALMTVELD-EERGA---QVQVLQGKEPPCFL 1758
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; ...
 1648-1761 3.09e-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: 3.09e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129396 1648 QFEIATVSVDVWHILEFDYSRLPRQSIGQFHEGDAYVVKWKYMastavgsrqkgehlvrVAGKEKCVYFFWQGRHSTVSE 1727
Cdd:cd11293      1 MYDDGSGKVEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQ----------------GGGKEEHILYFWQGRHSSQDE 64

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1907129396 1728 KGTSALMTVELDEE---RGAQVQVLQGKEPPCFLQCF 1761
Cdd:cd11293     65 RAAAALLTVELDEElkgRAVQVRVVQGKEPPHFLALF 101
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 1344-1440 2.36e-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: 2.36e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129396 1344 KLMLLQIKGRRHVQTRLVEPRASSLNSGDCFLLLSPQYCFLWVGEFSNVIEKAKASELATLIQTKRELGCRATYIQTIEE 1423
Cdd:cd11289      1 KPRLLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKVIVLDEGD 80

                           90
                   ....*....|....*..
gi 1907129396 1424 GiNTHTHaakdFWKLLG 1440
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; ...
 1781-1886 1.53e-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: 1.53e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129396 1781 SEWRLYCVRGEVPMEGNLLEVACHCSSLRSRTSMVVLNINKalIYLWHGCKAQGHTKEVGRTAANKIKEECpleaglhss 1860
Cdd:cd11288      1 SPTRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKTPSS--VYLWVGKGSSEDERELAKDVASFLKPKA--------- 69

                           90       100
                   ....*....|....*....|....*.
gi 1907129396 1861 snvTIHECDEGSEPLGFWDALGRRDR 1886
Cdd:cd11288     70 ---SLQEVAEGSEPDEFWEALGGKSE 92
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1347-1441 5.69e-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: 5.69e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129396  1347 LLQIKGRRHVQTRLVEPRASSLNSGDCFLLLSPQYCFLWVGEFSNVIEKAKASELATLIqtKRELGCRATYIQTIEEGIN 1426
Cdd:smart00262    2 LVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVEL--DDTLGPGPVQVRVVDEGKE 79

                            90
                    ....*....|....*
gi 1907129396  1427 THThaakdFWKLLGG 1441
Cdd:smart00262   80 PPE-----FWSLFGG 89
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 1465-1565 5.22e-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: 5.22e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129396 1465 NCVYRLTDDKlvpdDDYWGKIPKCS-LLQSKEVLVFDFGSEVYVWHGKEVTLAQRKIAFQLAKHLWNGtfdyencdinpl 1543
Cdd:cd11280      2 PRLYRVRGSK----AIEIEEVPLASsSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKELDEE------------ 65

                           90       100
                   ....*....|....*....|...
gi 1907129396 1544 DPGECNPLIPRKGQG-RPDWAIF 1565
Cdd:cd11280     66 RKGKPEIVRIRQGQEpREFWSLF 88
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 1346-1444 6.05e-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: 6.05e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129396 1346 MLLQIKGRRHVQTRLVE--PRASSLNSGDCFLLLSPQYCFLWVGEFSNVIEKAKASELATLIQTKRElgcratyIQTIEE 1423
Cdd:cd11288      4 RLFQVRGNGSGNTRAVEvdADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVASFLKPKAS-------LQEVAE 76

                           90       100
                   ....*....|....*....|.
gi 1907129396 1424 GINThthaaKDFWKLLGGQTS 1444
Cdd:cd11288     77 GSEP-----DEFWEALGGKSE 92
VHP pfam02209
Villin headpiece domain;
2081-2116 7.69e-15

Villin headpiece domain;


Pssm-ID: 460493  Cd Length: 36  Bit Score: 69.71  E-value: 7.69e-15
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1907129396 2081 YLTDEDFEFALDMSRDEFNALPTWKQVNLKKSKGLF 2116
Cdd:pfam02209    1 YLSDEDFEEVFGMSREEFYKLPKWKQNNLKKKAGLF 36
VHP smart00153
Villin headpiece domain;
2081-2116 1.20e-14

Villin headpiece domain;


Pssm-ID: 128458  Cd Length: 36  Bit Score: 69.27  E-value: 1.20e-14
                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 1907129396  2081 YLTDEDFEFALDMSRDEFNALPTWKQVNLKKSKGLF 2116
Cdd:smart00153    1 YLSDEDFEEVFGMTREEFYKLPLWKQNQLKKKKGLF 36
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 1903-2025 2.69e-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: 2.69e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129396 1903 PRLFILSSSSGDFSATEFVypaqapsavssmPFLQEDLYSApqpALFLVDNHHEVYLWQGWWPTENKItgsarirwasdr 1982
Cdd:cd11291      2 PRLFRCSNESGFFKVEEIS------------DFSQDDLDTD---DIMLLDTGDEVFVWVGSESSDEEK------------ 54

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1907129396 1983 KSAMETVLQYCRGKNLKRPPPKS--YLIHAGLEPLTFTNMFPSWE 2025
Cdd:cd11291     55 KEALTSAKKYIETDPLGRSKPRTpiYLVKQGNEPPTFTGYFHAWD 99
gelsolin_S1_like cd11290
Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; ...
 1656-1770 2.83e-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: 2.83e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129396 1656 VDVWHILEFDYSRLPRQSIGQFHEGDAYVVkwkyMASTAVGSrqkgehlvrvaGKEKCVYFFWQGRHSTVSEKGTSALMT 1735
Cdd:cd11290     10 LQIWRIENFELVPVPESFYGKFYEGDSYIV----LKTTLDPS-----------GSLSYDIHYWLGKEASQDEAGAAAIKA 74

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1907129396 1736 VELDEERGAQ-VQV--LQGKEPPCFLQCFQGGMVVHSG 1770
Cdd:cd11290     75 VELDDYLGGRpVQHreVQGHESEEFLSYFKKGIIYIEG 112
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1658-1764 9.76e-13

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 65.78  E-value: 9.76e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129396  1658 VWHILEFDYSRLPRQ--SIGQFHEGDAYVVKWkymastavgsrqkGEHLvrvagkekcvyFFWQGRHSTVSEKGTSALMT 1735
Cdd:smart00262    2 LVRVKGKRNVRVPEVpfSQGSLNSGDCYILDT-------------GSEI-----------YVWVGKKSSQDEKKKAAELA 57

                            90       100       110
                    ....*....|....*....|....*....|...
gi 1907129396  1736 VELDEERG---AQVQ-VLQGKEPPCFLQCFQGG 1764
Cdd:smart00262   58 VELDDTLGpgpVQVRvVDEGKEPPEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1786-1882 1.18e-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: 1.18e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129396  1786 YCVRGEVPMEGNLLEVACHCSSLRSRTSMVVLNinKALIYLWHGCKAQGHTKEVGRTAANKIKEECPleaglhsSSNVTI 1865
Cdd:smart00262    1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDT--GSEIYVWVGKKSSQDEKKKAAELAVELDDTLG-------PGPVQV 71

                            90
                    ....*....|....*..
gi 1907129396  1866 HECDEGSEPLGFWDALG 1882
Cdd:smart00262   72 RVVDEGKEPPEFWSLFG 88
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 1902-2021 6.46e-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: 6.46e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129396 1902 APRLFILSSSSgdfsATEFVYPAQAPSAVSSMPFLQEDLYSapqpalflvdnhhEVYLWQGWwptenkitGSARIRWASD 1981
Cdd:cd11280      1 PPRLYRVRGSK----AIEIEEVPLASSSLDSDDVFVLDTGS-------------EIYIWQGR--------ASSQAELAAA 55

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1907129396 1982 RKSAMETVLQYcrgknlkRPPPKSYLIHAGLEPLTFTNMF 2021
Cdd:cd11280     56 ALLAKELDEER-------KGKPEIVRIRQGQEPREFWSLF 88
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 1489-1581 8.73e-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: 54.56  E-value: 8.73e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129396 1489 SLLQSKEVLVFDFGSEVYVWHGKEVTLAQRKIAFQLA-KHLwngtfdyencdinpldpgecnpliprKGQGRPDWAIFGR 1567
Cdd:cd11292     29 EMLDSEDCYILDCGSEIFVWVGKGASLDERKAALKNAeEFL--------------------------RKKKRPPYTQVTR 82

                           90
                   ....*....|....
gi 1907129396 1568 VTEHNETILFKEKF 1581
Cdd:cd11292     83 VTEGGESALFKSKF 96
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1930-2024 1.04e-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: 1.04e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129396  1930 VSSMPFLQEDLYSApqpALFLVDNHHEVYLWQGwwptenkiTGSARirwaSDRKSAMETVLQYCrgKNLKRPPPKSYLIH 2009
Cdd:smart00262   13 VPEVPFSQGSLNSG---DCYILDTGSEIYVWVG--------KKSSQ----DEKKKAAELAVELD--DTLGPGPVQVRVVD 75

                            90
                    ....*....|....*
gi 1907129396  2010 AGLEPLTFTNMFPSW 2024
Cdd:smart00262   76 EGKEPPEFWSLFGGW 90
Gelsolin pfam00626
Gelsolin repeat;
1365-1424 5.57e-06

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 46.15  E-value: 5.57e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907129396 1365 ASSLNSGDCFLLLSPQYCFLWVGEFSNVIEKAKASELAT-LIQTKRelgCRATYIQTIEEG 1424
Cdd:pfam00626   12 QESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAqLDDDER---FPLPEVIRVPQG 69
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1486-1584 7.64e-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: 7.64e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129396  1486 PKCSLLQSKEVLVFDFGSEVYVWHGKEVTLAQRKIAFQLAKHLwngtFDYENcdinpldpgecnpliPRKGQGRpdwaif 1565
Cdd:smart00262   18 FSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVEL----DDTLG---------------PGPVQVR------ 72

                            90
                    ....*....|....*....
gi 1907129396  1566 gRVTEHNETILFKEKFLDW 1584
Cdd:smart00262   73 -VVDEGKEPPEFWSLFGGW 90
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 1713-1761 3.63e-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: 3.63e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907129396 1713 CVYFFWQGRHSTVSEKGTSALMTVELDEERG---AQVQVLQGKEPPCFLQCF 1761
Cdd:cd11280     37 SEIYIWQGRASSQAELAAAALLAKELDEERKgkpEIVRIRQGQEPREFWSLF 88
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 1366-1437 4.04e-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: 4.04e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907129396 1366 SSLNSGDCFLLLSPQYCFLWVGEFSNVIEKAKASELAT-LIQTKRElgCRATYIQTIEEGinTHTHAAKDFWK 1437
Cdd:cd11292     29 EMLDSEDCYILDCGSEIFVWVGKGASLDERKAALKNAEeFLRKKKR--PPYTQVTRVTEG--GESALFKSKFA 97
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 1361-1439 6.15e-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: 6.15e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907129396 1361 VEPRASSLNSGDCFLLLSPQYCFLWVGEFSNVIEKAKASELATliQTKRELGCRATYIQtIEEGinthtHAAKDFWKLL 1439
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; ...
 1486-1532 1.27e-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: 1.27e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1907129396 1486 PKCSLLQSKEVLVFDFGSEVYVWHGKEVTLAQRKIAFQLAKHLWNGT 1532
Cdd:cd11288     23 ADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVASFLKPKA 69
Gelsolin pfam00626
Gelsolin repeat;
1716-1758 9.15e-03

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 36.90  E-value: 9.15e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1907129396 1716 FFWQGRHSTVSEKGTSALMTVELD-EERGA---QVQVLQGKEPPCFL 1758
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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