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Conserved domains on  [gi|569003567|ref|XP_006525855|]
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supervillin isoform X1 [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; ...
 1719-1832 3.20e-44

Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


:

Pssm-ID: 200449  Cd Length: 101  Bit Score: 155.89  E-value: 3.20e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003567 1719 QFEIATVSVDVWHILEFDYSRLPRQSIGQFHEGDAYVVKWKYMastavgsrqkgehlvrVAGKEKCVYFFWQGRHSTVSE 1798
Cdd:cd11293     1 MYDDGSGKVEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQ----------------GGGKEEHILYFWQGRHSSQDE 64

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 569003567 1799 KGTSALMTVELDEE---RGAQVQVLQGKEPPCFLQCF 1832
Cdd:cd11293    65 RAAAALLTVELDEElkgRAVQVRVVQGKEPPHFLALF 101
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 1415-1511 2.77e-35

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


:

Pssm-ID: 200445  Cd Length: 92  Bit Score: 130.05  E-value: 2.77e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003567 1415 KLMLLQIKGRRHVQTRLVEPRASSLNSGDCFLLLSPQYCFLWVGEFSNVIEKAKASELATLIQTKRELGCRATYIQTIEE 1494
Cdd:cd11289     1 KPRLLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKVIVLDEGD 80

                          90
                  ....*....|....*..
gi 569003567 1495 GiNTHTHaakdFWKLLG 1511
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; ...
 1852-1957 1.66e-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: 1.66e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003567 1852 SEWRLYCVRGEVPMEGNLLEVACHCSSLRSRTSMVVLNINKalIYLWHGCKAQGHTKEVGRTAANKIKEECpleaglhss 1931
Cdd:cd11288     1 SPTRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKTPSS--VYLWVGKGSSEDERELAKDVASFLKPKA--------- 69

                          90       100
                  ....*....|....*....|....*.
gi 569003567 1932 snvTIHECDEGSEPLGFWDALGRRDR 1957
Cdd:cd11288    70 ---SLQEVAEGSEPDEFWEALGGKSE 92
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 1536-1636 6.25e-18

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


:

Pssm-ID: 200436  Cd Length: 88  Bit Score: 80.49  E-value: 6.25e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003567 1536 NCVYRLTDDKlvpdDDYWGKIPKCS-LLQSKEVLVFDFGSEVYVWHGKEVTLAQRKIAFQLAKHLWNGtfdyencdinpl 1614
Cdd:cd11280     2 PRLYRVRGSK----AIEIEEVPLASsSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKELDEE------------ 65

                          90       100
                  ....*....|....*....|...
gi 569003567 1615 DPGECNPLIPRKGQG-RPDWAIF 1636
Cdd:cd11280    66 RKGKPEIVRIRQGQEpREFWSLF 88
VHP pfam02209
Villin headpiece domain;
2152-2187 7.42e-15

Villin headpiece domain;


:

Pssm-ID: 460493  Cd Length: 36  Bit Score: 70.10  E-value: 7.42e-15
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 569003567  2152 YLTDEDFEFALDMSRDEFNALPTWKQVNLKKSKGLF 2187
Cdd:pfam02209    1 YLSDEDFEEVFGMSREEFYKLPKWKQNNLKKKAGLF 36
ADF_gelsolin super family cl15697
Actin depolymerization factor/cofilin- and gelsolin-like domains; Actin depolymerization ...
 1974-2096 2.73e-13

Actin depolymerization factor/cofilin- and gelsolin-like domains; Actin depolymerization factor/cofilin-like domains are present in a family of essential eukaryotic actin regulatory proteins; these proteins enhance the turnover rate of actin and interact with actin monomers as well as actin filaments.


The actual alignment was detected with superfamily member cd11291:

Pssm-ID: 472830 [Multi-domain]  Cd Length: 99  Bit Score: 67.71  E-value: 2.73e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003567 1974 PRLFILSSSSGDFSATEFVypaqapsavssmPFLQEDLYSApqpALFLVDNHHEVYLWQGWWPTENKItgsarirwasdr 2053
Cdd:cd11291     2 PRLFRCSNESGFFKVEEIS------------DFSQDDLDTD---DIMLLDTGDEVFVWVGSESSDEEK------------ 54

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 569003567 2054 KSAMETVLQYCRGKNLKRPPPKS--YLIHAGLEPLTFTNMFPSWE 2096
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; ...
 1719-1832 3.20e-44

Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200449  Cd Length: 101  Bit Score: 155.89  E-value: 3.20e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003567 1719 QFEIATVSVDVWHILEFDYSRLPRQSIGQFHEGDAYVVKWKYMastavgsrqkgehlvrVAGKEKCVYFFWQGRHSTVSE 1798
Cdd:cd11293     1 MYDDGSGKVEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQ----------------GGGKEEHILYFWQGRHSSQDE 64

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 569003567 1799 KGTSALMTVELDEE---RGAQVQVLQGKEPPCFLQCF 1832
Cdd:cd11293    65 RAAAALLTVELDEElkgRAVQVRVVQGKEPPHFLALF 101
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 1415-1511 2.77e-35

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


Pssm-ID: 200445  Cd Length: 92  Bit Score: 130.05  E-value: 2.77e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003567 1415 KLMLLQIKGRRHVQTRLVEPRASSLNSGDCFLLLSPQYCFLWVGEFSNVIEKAKASELATLIQTKRELGCRATYIQTIEE 1494
Cdd:cd11289     1 KPRLLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKVIVLDEGD 80

                          90
                  ....*....|....*..
gi 569003567 1495 GiNTHTHaakdFWKLLG 1511
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; ...
 1852-1957 1.66e-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: 1.66e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003567 1852 SEWRLYCVRGEVPMEGNLLEVACHCSSLRSRTSMVVLNINKalIYLWHGCKAQGHTKEVGRTAANKIKEECpleaglhss 1931
Cdd:cd11288     1 SPTRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKTPSS--VYLWVGKGSSEDERELAKDVASFLKPKA--------- 69

                          90       100
                  ....*....|....*....|....*.
gi 569003567 1932 snvTIHECDEGSEPLGFWDALGRRDR 1957
Cdd:cd11288    70 ---SLQEVAEGSEPDEFWEALGGKSE 92
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1418-1512 5.89e-22

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 91.97  E-value: 5.89e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003567   1418 LLQIKGRRHVQTRLVEPRASSLNSGDCFLLLSPQYCFLWVGEFSNVIEKAKASELATLIqtKRELGCRATYIQTIEEGIN 1497
Cdd:smart00262    2 LVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVEL--DDTLGPGPVQVRVVDEGKE 79

                            90
                    ....*....|....*
gi 569003567   1498 THThaakdFWKLLGG 1512
Cdd:smart00262   80 PPE-----FWSLFGG 89
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 1536-1636 6.25e-18

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


Pssm-ID: 200436  Cd Length: 88  Bit Score: 80.49  E-value: 6.25e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003567 1536 NCVYRLTDDKlvpdDDYWGKIPKCS-LLQSKEVLVFDFGSEVYVWHGKEVTLAQRKIAFQLAKHLWNGtfdyencdinpl 1614
Cdd:cd11280     2 PRLYRVRGSK----AIEIEEVPLASsSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKELDEE------------ 65

                          90       100
                  ....*....|....*....|...
gi 569003567 1615 DPGECNPLIPRKGQG-RPDWAIF 1636
Cdd:cd11280    66 RKGKPEIVRIRQGQEpREFWSLF 88
VHP pfam02209
Villin headpiece domain;
2152-2187 7.42e-15

Villin headpiece domain;


Pssm-ID: 460493  Cd Length: 36  Bit Score: 70.10  E-value: 7.42e-15
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 569003567  2152 YLTDEDFEFALDMSRDEFNALPTWKQVNLKKSKGLF 2187
Cdd:pfam02209    1 YLSDEDFEEVFGMSREEFYKLPKWKQNNLKKKAGLF 36
VHP smart00153
Villin headpiece domain;
2152-2187 1.23e-14

Villin headpiece domain;


Pssm-ID: 128458  Cd Length: 36  Bit Score: 69.27  E-value: 1.23e-14
                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 569003567   2152 YLTDEDFEFALDMSRDEFNALPTWKQVNLKKSKGLF 2187
Cdd:smart00153    1 YLSDEDFEEVFGMTREEFYKLPLWKQNQLKKKKGLF 36
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 1974-2096 2.73e-13

Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200447 [Multi-domain]  Cd Length: 99  Bit Score: 67.71  E-value: 2.73e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003567 1974 PRLFILSSSSGDFSATEFVypaqapsavssmPFLQEDLYSApqpALFLVDNHHEVYLWQGWWPTENKItgsarirwasdr 2053
Cdd:cd11291     2 PRLFRCSNESGFFKVEEIS------------DFSQDDLDTD---DIMLLDTGDEVFVWVGSESSDEEK------------ 54

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 569003567 2054 KSAMETVLQYCRGKNLKRPPPKS--YLIHAGLEPLTFTNMFPSWE 2096
Cdd:cd11291    55 KEALTSAKKYIETDPLGRSKPRTpiYLVKQGNEPPTFTGYFHAWD 99
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1729-1835 1.01e-12

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 65.78  E-value: 1.01e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003567   1729 VWHILEFDYSRLPRQ--SIGQFHEGDAYVVKWkymastavgsrqkGEHLvrvagkekcvyFFWQGRHSTVSEKGTSALMT 1806
Cdd:smart00262    2 LVRVKGKRNVRVPEVpfSQGSLNSGDCYILDT-------------GSEI-----------YVWVGKKSSQDEKKKAAELA 57

                            90       100       110
                    ....*....|....*....|....*....|...
gi 569003567   1807 VELDEERG---AQVQ-VLQGKEPPCFLQCFQGG 1835
Cdd:smart00262   58 VELDDTLGpgpVQVRvVDEGKEPPEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1857-1953 1.22e-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: 1.22e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003567   1857 YCVRGEVPMEGNLLEVACHCSSLRSRTSMVVLNinKALIYLWHGCKAQGHTKEVGRTAANKIKEECPleaglhsSSNVTI 1936
Cdd:smart00262    1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDT--GSEIYVWVGKKSSQDEKKKAAELAVELDDTLG-------PGPVQV 71

                            90
                    ....*....|....*..
gi 569003567   1937 HECDEGSEPLGFWDALG 1953
Cdd:smart00262   72 RVVDEGKEPPEFWSLFG 88
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 2001-2095 1.08e-06

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 48.44  E-value: 1.08e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003567   2001 VSSMPFLQEDLYSApqpALFLVDNHHEVYLWQGwwptenkiTGSARirwaSDRKSAMETVLQYCrgKNLKRPPPKSYLIH 2080
Cdd:smart00262   13 VPEVPFSQGSLNSG---DCYILDTGSEIYVWVG--------KKSSQ----DEKKKAAELAVELD--DTLGPGPVQVRVVD 75

                            90
                    ....*....|....*
gi 569003567   2081 AGLEPLTFTNMFPSW 2095
Cdd:smart00262   76 EGKEPPEFWSLFGGW 90
Gelsolin pfam00626
Gelsolin repeat;
1436-1495 5.76e-06

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 46.15  E-value: 5.76e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569003567  1436 ASSLNSGDCFLLLSPQYCFLWVGEFSNVIEKAKASELAT-LIQTKRelgCRATYIQTIEEG 1495
Cdd:pfam00626   12 QESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAqLDDDER---FPLPEVIRVPQG 69
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1557-1655 7.91e-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: 7.91e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003567   1557 PKCSLLQSKEVLVFDFGSEVYVWHGKEVTLAQRKIAFQLAKHLwngtFDYENcdinpldpgecnpliPRKGQGRpdwaif 1636
Cdd:smart00262   18 FSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVEL----DDTLG---------------PGPVQVR------ 72

                            90
                    ....*....|....*....
gi 569003567   1637 gRVTEHNETILFKEKFLDW 1655
Cdd:smart00262   73 -VVDEGKEPPEFWSLFGGW 90
Gelsolin pfam00626
Gelsolin repeat;
1787-1829 9.46e-03

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 36.90  E-value: 9.46e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 569003567  1787 FFWQGRHSTVSEKGTSALMTVELD-EERGA---QVQVLQGKEPPCFL 1829
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; ...
 1719-1832 3.20e-44

Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200449  Cd Length: 101  Bit Score: 155.89  E-value: 3.20e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003567 1719 QFEIATVSVDVWHILEFDYSRLPRQSIGQFHEGDAYVVKWKYMastavgsrqkgehlvrVAGKEKCVYFFWQGRHSTVSE 1798
Cdd:cd11293     1 MYDDGSGKVEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQ----------------GGGKEEHILYFWQGRHSSQDE 64

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 569003567 1799 KGTSALMTVELDEE---RGAQVQVLQGKEPPCFLQCF 1832
Cdd:cd11293    65 RAAAALLTVELDEElkgRAVQVRVVQGKEPPHFLALF 101
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 1415-1511 2.77e-35

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


Pssm-ID: 200445  Cd Length: 92  Bit Score: 130.05  E-value: 2.77e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003567 1415 KLMLLQIKGRRHVQTRLVEPRASSLNSGDCFLLLSPQYCFLWVGEFSNVIEKAKASELATLIQTKRELGCRATYIQTIEE 1494
Cdd:cd11289     1 KPRLLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKVIVLDEGD 80

                          90
                  ....*....|....*..
gi 569003567 1495 GiNTHTHaakdFWKLLG 1511
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; ...
 1852-1957 1.66e-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: 1.66e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003567 1852 SEWRLYCVRGEVPMEGNLLEVACHCSSLRSRTSMVVLNINKalIYLWHGCKAQGHTKEVGRTAANKIKEECpleaglhss 1931
Cdd:cd11288     1 SPTRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKTPSS--VYLWVGKGSSEDERELAKDVASFLKPKA--------- 69

                          90       100
                  ....*....|....*....|....*.
gi 569003567 1932 snvTIHECDEGSEPLGFWDALGRRDR 1957
Cdd:cd11288    70 ---SLQEVAEGSEPDEFWEALGGKSE 92
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1418-1512 5.89e-22

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 91.97  E-value: 5.89e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003567   1418 LLQIKGRRHVQTRLVEPRASSLNSGDCFLLLSPQYCFLWVGEFSNVIEKAKASELATLIqtKRELGCRATYIQTIEEGIN 1497
Cdd:smart00262    2 LVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVEL--DDTLGPGPVQVRVVDEGKE 79

                            90
                    ....*....|....*
gi 569003567   1498 THThaakdFWKLLGG 1512
Cdd:smart00262   80 PPE-----FWSLFGG 89
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 1536-1636 6.25e-18

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


Pssm-ID: 200436  Cd Length: 88  Bit Score: 80.49  E-value: 6.25e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003567 1536 NCVYRLTDDKlvpdDDYWGKIPKCS-LLQSKEVLVFDFGSEVYVWHGKEVTLAQRKIAFQLAKHLWNGtfdyencdinpl 1614
Cdd:cd11280     2 PRLYRVRGSK----AIEIEEVPLASsSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKELDEE------------ 65

                          90       100
                  ....*....|....*....|...
gi 569003567 1615 DPGECNPLIPRKGQG-RPDWAIF 1636
Cdd:cd11280    66 RKGKPEIVRIRQGQEpREFWSLF 88
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 1417-1515 6.57e-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: 6.57e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003567 1417 MLLQIKGRRHVQTRLVE--PRASSLNSGDCFLLLSPQYCFLWVGEFSNVIEKAKASELATLIQTKRElgcratyIQTIEE 1494
Cdd:cd11288     4 RLFQVRGNGSGNTRAVEvdADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVASFLKPKAS-------LQEVAE 76

                          90       100
                  ....*....|....*....|.
gi 569003567 1495 GINThthaaKDFWKLLGGQTS 1515
Cdd:cd11288    77 GSEP-----DEFWEALGGKSE 92
VHP pfam02209
Villin headpiece domain;
2152-2187 7.42e-15

Villin headpiece domain;


Pssm-ID: 460493  Cd Length: 36  Bit Score: 70.10  E-value: 7.42e-15
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 569003567  2152 YLTDEDFEFALDMSRDEFNALPTWKQVNLKKSKGLF 2187
Cdd:pfam02209    1 YLSDEDFEEVFGMSREEFYKLPKWKQNNLKKKAGLF 36
VHP smart00153
Villin headpiece domain;
2152-2187 1.23e-14

Villin headpiece domain;


Pssm-ID: 128458  Cd Length: 36  Bit Score: 69.27  E-value: 1.23e-14
                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 569003567   2152 YLTDEDFEFALDMSRDEFNALPTWKQVNLKKSKGLF 2187
Cdd:smart00153    1 YLSDEDFEEVFGMTREEFYKLPLWKQNQLKKKKGLF 36
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 1974-2096 2.73e-13

Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200447 [Multi-domain]  Cd Length: 99  Bit Score: 67.71  E-value: 2.73e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003567 1974 PRLFILSSSSGDFSATEFVypaqapsavssmPFLQEDLYSApqpALFLVDNHHEVYLWQGWWPTENKItgsarirwasdr 2053
Cdd:cd11291     2 PRLFRCSNESGFFKVEEIS------------DFSQDDLDTD---DIMLLDTGDEVFVWVGSESSDEEK------------ 54

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 569003567 2054 KSAMETVLQYCRGKNLKRPPPKS--YLIHAGLEPLTFTNMFPSWE 2096
Cdd:cd11291    55 KEALTSAKKYIETDPLGRSKPRTpiYLVKQGNEPPTFTGYFHAWD 99
gelsolin_S1_like cd11290
Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; ...
 1727-1841 2.93e-13

Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin_like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200446  Cd Length: 113  Bit Score: 68.02  E-value: 2.93e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003567 1727 VDVWHILEFDYSRLPRQSIGQFHEGDAYVVkwkyMASTAVGSrqkgehlvrvaGKEKCVYFFWQGRHSTVSEKGTSALMT 1806
Cdd:cd11290    10 LQIWRIENFELVPVPESFYGKFYEGDSYIV----LKTTLDPS-----------GSLSYDIHYWLGKEASQDEAGAAAIKA 74

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 569003567 1807 VELDEERGAQ-VQV--LQGKEPPCFLQCFQGGMVVHSG 1841
Cdd:cd11290    75 VELDDYLGGRpVQHreVQGHESEEFLSYFKKGIIYIEG 112
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1729-1835 1.01e-12

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 65.78  E-value: 1.01e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003567   1729 VWHILEFDYSRLPRQ--SIGQFHEGDAYVVKWkymastavgsrqkGEHLvrvagkekcvyFFWQGRHSTVSEKGTSALMT 1806
Cdd:smart00262    2 LVRVKGKRNVRVPEVpfSQGSLNSGDCYILDT-------------GSEI-----------YVWVGKKSSQDEKKKAAELA 57

                            90       100       110
                    ....*....|....*....|....*....|...
gi 569003567   1807 VELDEERG---AQVQ-VLQGKEPPCFLQCFQGG 1835
Cdd:smart00262   58 VELDDTLGpgpVQVRvVDEGKEPPEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1857-1953 1.22e-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: 1.22e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003567   1857 YCVRGEVPMEGNLLEVACHCSSLRSRTSMVVLNinKALIYLWHGCKAQGHTKEVGRTAANKIKEECPleaglhsSSNVTI 1936
Cdd:smart00262    1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDT--GSEIYVWVGKKSSQDEKKKAAELAVELDDTLG-------PGPVQV 71

                            90
                    ....*....|....*..
gi 569003567   1937 HECDEGSEPLGFWDALG 1953
Cdd:smart00262   72 RVVDEGKEPPEFWSLFG 88
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 1973-2092 7.08e-11

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


Pssm-ID: 200436  Cd Length: 88  Bit Score: 60.46  E-value: 7.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003567 1973 APRLFILSSSSgdfsATEFVYPAQAPSAVSSMPFLQEDLYSapqpalflvdnhhEVYLWQGWwptenkitGSARIRWASD 2052
Cdd:cd11280     1 PPRLYRVRGSK----AIEIEEVPLASSSLDSDDVFVLDTGS-------------EIYIWQGR--------ASSQAELAAA 55

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 569003567 2053 RKSAMETVLQYcrgknlkRPPPKSYLIHAGLEPLTFTNMF 2092
Cdd:cd11280    56 ALLAKELDEER-------KGKPEIVRIRQGQEPREFWSLF 88
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 1560-1652 8.60e-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: 8.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003567 1560 SLLQSKEVLVFDFGSEVYVWHGKEVTLAQRKIAFQLA-KHLwngtfdyencdinpldpgecnpliprKGQGRPDWAIFGR 1638
Cdd:cd11292    29 EMLDSEDCYILDCGSEIFVWVGKGASLDERKAALKNAeEFL--------------------------RKKKRPPYTQVTR 82

                          90
                  ....*....|....
gi 569003567 1639 VTEHNETILFKEKF 1652
Cdd:cd11292    83 VTEGGESALFKSKF 96
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 2001-2095 1.08e-06

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 48.44  E-value: 1.08e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003567   2001 VSSMPFLQEDLYSApqpALFLVDNHHEVYLWQGwwptenkiTGSARirwaSDRKSAMETVLQYCrgKNLKRPPPKSYLIH 2080
Cdd:smart00262   13 VPEVPFSQGSLNSG---DCYILDTGSEIYVWVG--------KKSSQ----DEKKKAAELAVELD--DTLGPGPVQVRVVD 75

                            90
                    ....*....|....*
gi 569003567   2081 AGLEPLTFTNMFPSW 2095
Cdd:smart00262   76 EGKEPPEFWSLFGGW 90
Gelsolin pfam00626
Gelsolin repeat;
1436-1495 5.76e-06

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 46.15  E-value: 5.76e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569003567  1436 ASSLNSGDCFLLLSPQYCFLWVGEFSNVIEKAKASELAT-LIQTKRelgCRATYIQTIEEG 1495
Cdd:pfam00626   12 QESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAqLDDDER---FPLPEVIRVPQG 69
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1557-1655 7.91e-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: 7.91e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003567   1557 PKCSLLQSKEVLVFDFGSEVYVWHGKEVTLAQRKIAFQLAKHLwngtFDYENcdinpldpgecnpliPRKGQGRpdwaif 1636
Cdd:smart00262   18 FSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVEL----DDTLG---------------PGPVQVR------ 72

                            90
                    ....*....|....*....
gi 569003567   1637 gRVTEHNETILFKEKFLDW 1655
Cdd:smart00262   73 -VVDEGKEPPEFWSLFGGW 90
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 1784-1832 3.72e-05

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


Pssm-ID: 200436  Cd Length: 88  Bit Score: 44.28  E-value: 3.72e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 569003567 1784 CVYFFWQGRHSTVSEKGTSALMTVELDEERG---AQVQVLQGKEPPCFLQCF 1832
Cdd:cd11280    37 SEIYIWQGRASSQAELAAAALLAKELDEERKgkpEIVRIRQGQEPREFWSLF 88
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 1437-1508 4.10e-05

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


Pssm-ID: 200448  Cd Length: 98  Bit Score: 44.16  E-value: 4.10e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569003567 1437 SSLNSGDCFLLLSPQYCFLWVGEFSNVIEKAKASELAT-LIQTKRElgCRATYIQTIEEGinTHTHAAKDFWK 1508
Cdd:cd11292    29 EMLDSEDCYILDCGSEIFVWVGKGASLDERKAALKNAEeFLRKKKR--PPYTQVTRVTEG--GESALFKSKFA 97
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 1432-1510 6.62e-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: 6.62e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569003567 1432 VEPRASSLNSGDCFLLLSPQYCFLWVGEFSNVIEKAKASELATliQTKRELGCRATYIQtIEEGinthtHAAKDFWKLL 1510
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; ...
 1557-1603 1.32e-04

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


Pssm-ID: 200444  Cd Length: 92  Bit Score: 42.60  E-value: 1.32e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 569003567 1557 PKCSLLQSKEVLVFDFGSEVYVWHGKEVTLAQRKIAFQLAKHLWNGT 1603
Cdd:cd11288    23 ADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVASFLKPKA 69
Gelsolin pfam00626
Gelsolin repeat;
1787-1829 9.46e-03

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 36.90  E-value: 9.46e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 569003567  1787 FFWQGRHSTVSEKGTSALMTVELD-EERGA---QVQVLQGKEPPCFL 1829
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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