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Conserved domains on  [gi|1207111496|ref|XP_021335687|]
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supervillin isoform X2 [Danio rerio]

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; ...
 1769-1880 6.53e-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: 155.12  E-value: 6.53e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207111496 1769 FEISTLSVDVWHILEFDYSRLPKQSIGQFHEGDTYVVKWKYMISravgkrlhseriigpGKEKCCYFFWQGRNSTVNEKG 1848
Cdd:cd11293      2 YDDGSGKVEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQGG---------------GKEEHILYFWQGRHSSQDERA 66

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1207111496 1849 TSALMTVELDEE---RGAQVQVQQGKEPPCFLQCF 1880
Cdd:cd11293     67 AAALLTVELDEElkgRAVQVRVVQGKEPPHFLALF 101
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 1465-1561 6.48e-33

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: 123.50  E-value: 6.48e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207111496 1465 KLMLIQVKGRRHVQTRLVEPRASSLNSGDCFLLITPHHCFIWIGEFANVIEKAKAAELATFVQTKHDLGCRASYVQTIEE 1544
Cdd:cd11289      1 KPRLLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKVIVLDEGD 80

                           90
                   ....*....|....*..
gi 1207111496 1545 GANTHThaakdFWKILG 1561
Cdd:cd11289     81 TNESPE-----FWKVLG 92
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 1902-2005 3.75e-24

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: 98.46  E-value: 3.75e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207111496 1902 WRLYCVRGEKPIEGHLLEAVCHCSSLRSRTSMILLNiPKaSLYLWHGCKAQVHTRDVGRTTANKIKEqcpleaglhsssK 1981
Cdd:cd11288      3 TRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKT-PS-SVYLWVGKGSSEDERELAKDVASFLKP------------K 68

                           90       100
                   ....*....|....*....|....
gi 1207111496 1982 VSIQECDEGAEPQGFWEALGKRDR 2005
Cdd:cd11288     69 ASLQEVAEGSEPDEFWEALGGKSE 92
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 1586-1686 3.64e-16

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: 75.48  E-value: 3.64e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207111496 1586 NCIYRLMEDKlvphDDYWGRVPRCS-MLNPKEVLVFDFGSEVYVWHGKEVTLAQRKVAFQLAKHLWNGtfdytncdinpl 1664
Cdd:cd11280      2 PRLYRVRGSK----AIEIEEVPLASsSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKELDEE------------ 65

                           90       100
                   ....*....|....*....|...
gi 1207111496 1665 DPGECNALIPRKGQG-RPDWAVF 1686
Cdd:cd11280     66 RKGKPEIVRIRQGQEpREFWSLF 88
ADF_gelsolin super family cl15697
Actin depolymerization factor/cofilin- and gelsolin-like domains; Actin depolymerization ...
 2022-2143 2.72e-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: 2.72e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207111496 2022 PRLFQLSSASGeFAAVEFVYPsrepnlvnsmpFLQEDLytATQpALFLVDNHHEVYLWQGwwpqdSESTgsarirwDSDR 2101
Cdd:cd11291      2 PRLFRCSNESG-FFKVEEISD-----------FSQDDL--DTD-DIMLLDTGDEVFVWVG-----SESS-------DEEK 54

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1207111496 2102 KCAMETVLQYSK----EKNEKKTPKsYLIHAGLEPLTFTNMFPSWE 2143
Cdd:cd11291     55 KEALTSAKKYIEtdplGRSKPRTPI-YLVKQGNEPPTFTGYFHAWD 99
VHP pfam02209
Villin headpiece domain;
2199-2241 2.18e-12

Villin headpiece domain;


:

Pssm-ID: 460493  Cd Length: 36  Bit Score: 63.17  E-value: 2.18e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1207111496 2199 YLSDEDFEgvgasgkKALEMTRSEYEALPGWKQVNVKKAKGLF 2241
Cdd:pfam02209    1 YLSDEDFE-------EVFGMSREEFYKLPKWKQNNLKKKAGLF 36
 
Name Accession Description Interval E-value
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
 1769-1880 6.53e-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: 155.12  E-value: 6.53e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207111496 1769 FEISTLSVDVWHILEFDYSRLPKQSIGQFHEGDTYVVKWKYMISravgkrlhseriigpGKEKCCYFFWQGRNSTVNEKG 1848
Cdd:cd11293      2 YDDGSGKVEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQGG---------------GKEEHILYFWQGRHSSQDERA 66

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1207111496 1849 TSALMTVELDEE---RGAQVQVQQGKEPPCFLQCF 1880
Cdd:cd11293     67 AAALLTVELDEElkgRAVQVRVVQGKEPPHFLALF 101
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 1465-1561 6.48e-33

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: 123.50  E-value: 6.48e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207111496 1465 KLMLIQVKGRRHVQTRLVEPRASSLNSGDCFLLITPHHCFIWIGEFANVIEKAKAAELATFVQTKHDLGCRASYVQTIEE 1544
Cdd:cd11289      1 KPRLLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKVIVLDEGD 80

                           90
                   ....*....|....*..
gi 1207111496 1545 GANTHThaakdFWKILG 1561
Cdd:cd11289     81 TNESPE-----FWKVLG 92
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 1902-2005 3.75e-24

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: 98.46  E-value: 3.75e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207111496 1902 WRLYCVRGEKPIEGHLLEAVCHCSSLRSRTSMILLNiPKaSLYLWHGCKAQVHTRDVGRTTANKIKEqcpleaglhsssK 1981
Cdd:cd11288      3 TRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKT-PS-SVYLWVGKGSSEDERELAKDVASFLKP------------K 68

                           90       100
                   ....*....|....*....|....
gi 1207111496 1982 VSIQECDEGAEPQGFWEALGKRDR 2005
Cdd:cd11288     69 ASLQEVAEGSEPDEFWEALGGKSE 92
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1468-1562 1.87e-21

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 90.43  E-value: 1.87e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207111496  1468 LIQVKGRRHVQTRLVEPRASSLNSGDCFLLITPHHCFIWIGEFANVIEKAKAAELAtfVQTKHDLGCRASYVQTIEEGAN 1547
Cdd:smart00262    2 LVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELA--VELDDTLGPGPVQVRVVDEGKE 79

                            90
                    ....*....|....*
gi 1207111496  1548 THThaakdFWKILGG 1562
Cdd:smart00262   80 PPE-----FWSLFGG 89
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 1586-1686 3.64e-16

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: 75.48  E-value: 3.64e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207111496 1586 NCIYRLMEDKlvphDDYWGRVPRCS-MLNPKEVLVFDFGSEVYVWHGKEVTLAQRKVAFQLAKHLWNGtfdytncdinpl 1664
Cdd:cd11280      2 PRLYRVRGSK----AIEIEEVPLASsSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKELDEE------------ 65

                           90       100
                   ....*....|....*....|...
gi 1207111496 1665 DPGECNALIPRKGQG-RPDWAVF 1686
Cdd:cd11280     66 RKGKPEIVRIRQGQEpREFWSLF 88
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 2022-2143 2.72e-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: 2.72e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207111496 2022 PRLFQLSSASGeFAAVEFVYPsrepnlvnsmpFLQEDLytATQpALFLVDNHHEVYLWQGwwpqdSESTgsarirwDSDR 2101
Cdd:cd11291      2 PRLFRCSNESG-FFKVEEISD-----------FSQDDL--DTD-DIMLLDTGDEVFVWVG-----SESS-------DEEK 54

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1207111496 2102 KCAMETVLQYSK----EKNEKKTPKsYLIHAGLEPLTFTNMFPSWE 2143
Cdd:cd11291     55 KEALTSAKKYIEtdplGRSKPRTPI-YLVKQGNEPPTFTGYFHAWD 99
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1778-1883 9.39e-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: 9.39e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207111496  1778 VWHILEFDYSRLP--KQSIGQFHEGDTYVVKWKYMIsravgkrlhseriigpgkekccyFFWQGRNSTVNEKGTSALMTV 1855
Cdd:smart00262    2 LVRVKGKRNVRVPevPFSQGSLNSGDCYILDTGSEI-----------------------YVWVGKKSSQDEKKKAAELAV 58

                            90       100       110
                    ....*....|....*....|....*....|..
gi 1207111496  1856 ELDEERG---AQVQ-VQQGKEPPCFLQCFNGG 1883
Cdd:smart00262   59 ELDDTLGpgpVQVRvVDEGKEPPEFWSLFGGW 90
VHP pfam02209
Villin headpiece domain;
2199-2241 2.18e-12

Villin headpiece domain;


Pssm-ID: 460493  Cd Length: 36  Bit Score: 63.17  E-value: 2.18e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1207111496 2199 YLSDEDFEgvgasgkKALEMTRSEYEALPGWKQVNVKKAKGLF 2241
Cdd:pfam02209    1 YLSDEDFE-------EVFGMSREEFYKLPKWKQNNLKKKAGLF 36
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1905-2001 2.88e-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: 64.62  E-value: 2.88e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207111496  1905 YCVRGEKPIEGHLLEAVCHCSSLRSRTSMILLNipKASLYLWHGCKAQVHTRDVGRTTANKIKEQCPleaglhsSSKVSI 1984
Cdd:smart00262    1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDT--GSEIYVWVGKKSSQDEKKKAAELAVELDDTLG-------PGPVQV 71

                            90
                    ....*....|....*..
gi 1207111496  1985 QECDEGAEPQGFWEALG 2001
Cdd:smart00262   72 RVVDEGKEPPEFWSLFG 88
VHP smart00153
Villin headpiece domain;
2199-2241 1.10e-10

Villin headpiece domain;


Pssm-ID: 128458  Cd Length: 36  Bit Score: 58.10  E-value: 1.10e-10
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 1207111496  2199 YLSDEDFEgvgasgkKALEMTRSEYEALPGWKQVNVKKAKGLF 2241
Cdd:smart00153    1 YLSDEDFE-------EVFGMTREEFYKLPLWKQNQLKKKKGLF 36
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 2053-2142 9.63e-08

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: 51.52  E-value: 9.63e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207111496  2053 PFLQEDLYTAtqpALFLVDNHHEVYLWQGwwpqdSESTgsarirwDSDRKCAMETVLQYSKEKNEKKTPkSYLIHAGLEP 2132
Cdd:smart00262   17 PFSQGSLNSG---DCYILDTGSEIYVWVG-----KKSS-------QDEKKKAAELAVELDDTLGPGPVQ-VRVVDEGKEP 80

                            90
                    ....*....|
gi 1207111496  2133 LTFTNMFPSW 2142
Cdd:smart00262   81 PEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1610-1705 1.63e-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: 48.06  E-value: 1.63e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207111496  1610 SMLNPKEVLVFDFGSEVYVWHGKEVTLAQRKVAFQLAKHLWNGtfdytncdinpldpgecnaLIPRKGQGRpdwavfgRL 1689
Cdd:smart00262   21 GSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDT-------------------LGPGPVQVR-------VV 74

                            90
                    ....*....|....*.
gi 1207111496  1690 TQHNETTLFKEKFLDW 1705
Cdd:smart00262   75 DEGKEPPEFWSLFGGW 90
Gelsolin pfam00626
Gelsolin repeat;
1486-1523 1.97e-06

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 47.30  E-value: 1.97e-06
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1207111496 1486 ASSLNSGDCFLLITPHHCFIWIGEFANVIEKAKAAELA 1523
Cdd:pfam00626   12 QESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLA 49
Gelsolin pfam00626
Gelsolin repeat;
1835-1877 4.09e-03

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 38.06  E-value: 4.09e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1207111496 1835 FFWQGRNSTVNEKGTSALMTVELD-EERGA---QVQVQQGKEPPCFL 1877
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; ...
 1769-1880 6.53e-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: 155.12  E-value: 6.53e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207111496 1769 FEISTLSVDVWHILEFDYSRLPKQSIGQFHEGDTYVVKWKYMISravgkrlhseriigpGKEKCCYFFWQGRNSTVNEKG 1848
Cdd:cd11293      2 YDDGSGKVEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQGG---------------GKEEHILYFWQGRHSSQDERA 66

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1207111496 1849 TSALMTVELDEE---RGAQVQVQQGKEPPCFLQCF 1880
Cdd:cd11293     67 AAALLTVELDEElkgRAVQVRVVQGKEPPHFLALF 101
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 1465-1561 6.48e-33

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: 123.50  E-value: 6.48e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207111496 1465 KLMLIQVKGRRHVQTRLVEPRASSLNSGDCFLLITPHHCFIWIGEFANVIEKAKAAELATFVQTKHDLGCRASYVQTIEE 1544
Cdd:cd11289      1 KPRLLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKVIVLDEGD 80

                           90
                   ....*....|....*..
gi 1207111496 1545 GANTHThaakdFWKILG 1561
Cdd:cd11289     81 TNESPE-----FWKVLG 92
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 1902-2005 3.75e-24

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: 98.46  E-value: 3.75e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207111496 1902 WRLYCVRGEKPIEGHLLEAVCHCSSLRSRTSMILLNiPKaSLYLWHGCKAQVHTRDVGRTTANKIKEqcpleaglhsssK 1981
Cdd:cd11288      3 TRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKT-PS-SVYLWVGKGSSEDERELAKDVASFLKP------------K 68

                           90       100
                   ....*....|....*....|....
gi 1207111496 1982 VSIQECDEGAEPQGFWEALGKRDR 2005
Cdd:cd11288     69 ASLQEVAEGSEPDEFWEALGGKSE 92
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1468-1562 1.87e-21

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 90.43  E-value: 1.87e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207111496  1468 LIQVKGRRHVQTRLVEPRASSLNSGDCFLLITPHHCFIWIGEFANVIEKAKAAELAtfVQTKHDLGCRASYVQTIEEGAN 1547
Cdd:smart00262    2 LVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELA--VELDDTLGPGPVQVRVVDEGKE 79

                            90
                    ....*....|....*
gi 1207111496  1548 THThaakdFWKILGG 1562
Cdd:smart00262   80 PPE-----FWSLFGG 89
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 1467-1565 8.22e-18

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: 80.35  E-value: 8.22e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207111496 1467 MLIQVKGRRHVQTRLVE--PRASSLNSGDCFLLITPHHCFIWIGEFANVIEKAKAAELATFvqtkhdLGCRASYvQTIEE 1544
Cdd:cd11288      4 RLFQVRGNGSGNTRAVEvdADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVASF------LKPKASL-QEVAE 76

                           90       100
                   ....*....|....*....|.
gi 1207111496 1545 GANThthaaKDFWKILGGQTS 1565
Cdd:cd11288     77 GSEP-----DEFWEALGGKSE 92
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 1586-1686 3.64e-16

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: 75.48  E-value: 3.64e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207111496 1586 NCIYRLMEDKlvphDDYWGRVPRCS-MLNPKEVLVFDFGSEVYVWHGKEVTLAQRKVAFQLAKHLWNGtfdytncdinpl 1664
Cdd:cd11280      2 PRLYRVRGSK----AIEIEEVPLASsSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKELDEE------------ 65

                           90       100
                   ....*....|....*....|...
gi 1207111496 1665 DPGECNALIPRKGQG-RPDWAVF 1686
Cdd:cd11280     66 RKGKPEIVRIRQGQEpREFWSLF 88
gelsolin_S1_like cd11290
Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; ...
 1776-1889 6.99e-14

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: 69.94  E-value: 6.99e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207111496 1776 VDVWHILEFDYSRLPKQSIGQFHEGDTYVVkwkymisravgkrLHSERiigPGKEKCCY--FFWQGRNSTVNEKGTSALM 1853
Cdd:cd11290     10 LQIWRIENFELVPVPESFYGKFYEGDSYIV-------------LKTTL---DPSGSLSYdiHYWLGKEASQDEAGAAAIK 73

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1207111496 1854 TVELDEERGAQ-VQVQ--QGKEPPCFLQCFNGGMIVHAG 1889
Cdd:cd11290     74 AVELDDYLGGRpVQHRevQGHESEEFLSYFKKGIIYIEG 112
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 2022-2143 2.72e-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: 2.72e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207111496 2022 PRLFQLSSASGeFAAVEFVYPsrepnlvnsmpFLQEDLytATQpALFLVDNHHEVYLWQGwwpqdSESTgsarirwDSDR 2101
Cdd:cd11291      2 PRLFRCSNESG-FFKVEEISD-----------FSQDDL--DTD-DIMLLDTGDEVFVWVG-----SESS-------DEEK 54

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1207111496 2102 KCAMETVLQYSK----EKNEKKTPKsYLIHAGLEPLTFTNMFPSWE 2143
Cdd:cd11291     55 KEALTSAKKYIEtdplGRSKPRTPI-YLVKQGNEPPTFTGYFHAWD 99
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1778-1883 9.39e-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: 9.39e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207111496  1778 VWHILEFDYSRLP--KQSIGQFHEGDTYVVKWKYMIsravgkrlhseriigpgkekccyFFWQGRNSTVNEKGTSALMTV 1855
Cdd:smart00262    2 LVRVKGKRNVRVPevPFSQGSLNSGDCYILDTGSEI-----------------------YVWVGKKSSQDEKKKAAELAV 58

                            90       100       110
                    ....*....|....*....|....*....|..
gi 1207111496  1856 ELDEERG---AQVQ-VQQGKEPPCFLQCFNGG 1883
Cdd:smart00262   59 ELDDTLGpgpVQVRvVDEGKEPPEFWSLFGGW 90
VHP pfam02209
Villin headpiece domain;
2199-2241 2.18e-12

Villin headpiece domain;


Pssm-ID: 460493  Cd Length: 36  Bit Score: 63.17  E-value: 2.18e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1207111496 2199 YLSDEDFEgvgasgkKALEMTRSEYEALPGWKQVNVKKAKGLF 2241
Cdd:pfam02209    1 YLSDEDFE-------EVFGMSREEFYKLPKWKQNNLKKKAGLF 36
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1905-2001 2.88e-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: 64.62  E-value: 2.88e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207111496  1905 YCVRGEKPIEGHLLEAVCHCSSLRSRTSMILLNipKASLYLWHGCKAQVHTRDVGRTTANKIKEQCPleaglhsSSKVSI 1984
Cdd:smart00262    1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDT--GSEIYVWVGKKSSQDEKKKAAELAVELDDTLG-------PGPVQV 71

                            90
                    ....*....|....*..
gi 1207111496  1985 QECDEGAEPQGFWEALG 2001
Cdd:smart00262   72 RVVDEGKEPPEFWSLFG 88
VHP smart00153
Villin headpiece domain;
2199-2241 1.10e-10

Villin headpiece domain;


Pssm-ID: 128458  Cd Length: 36  Bit Score: 58.10  E-value: 1.10e-10
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 1207111496  2199 YLSDEDFEgvgasgkKALEMTRSEYEALPGWKQVNVKKAKGLF 2241
Cdd:smart00153    1 YLSDEDFE-------EVFGMTREEFYKLPLWKQNQLKKKKGLF 36
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 1610-1702 3.97e-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: 55.72  E-value: 3.97e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207111496 1610 SMLNPKEVLVFDFGSEVYVWHGKEVTLAQRKVAFQLAkhlwngtfdytncdinpldpgecNALIPRKgqGRPDWAVFGRL 1689
Cdd:cd11292     29 EMLDSEDCYILDCGSEIFVWVGKGASLDERKAALKNA-----------------------EEFLRKK--KRPPYTQVTRV 83

                           90
                   ....*....|...
gi 1207111496 1690 TQHNETTLFKEKF 1702
Cdd:cd11292     84 TEGGESALFKSKF 96
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 2022-2139 6.33e-09

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


Pssm-ID: 200436  Cd Length: 88  Bit Score: 55.07  E-value: 6.33e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207111496 2022 PRLFQLSSASgefaAVEFVYPSREPNLVNSMPFLQEDLYTatqpalflvdnhhEVYLWQGWwpqdsestGSARIRWDSDR 2101
Cdd:cd11280      2 PRLYRVRGSK----AIEIEEVPLASSSLDSDDVFVLDTGS-------------EIYIWQGR--------ASSQAELAAAA 56

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1207111496 2102 KCAMETvlqyskEKNEKKTPKSYLIHAGLEPLTFTNMF 2139
Cdd:cd11280     57 LLAKEL------DEERKGKPEIVRIRQGQEPREFWSLF 88
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 2053-2142 9.63e-08

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: 51.52  E-value: 9.63e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207111496  2053 PFLQEDLYTAtqpALFLVDNHHEVYLWQGwwpqdSESTgsarirwDSDRKCAMETVLQYSKEKNEKKTPkSYLIHAGLEP 2132
Cdd:smart00262   17 PFSQGSLNSG---DCYILDTGSEIYVWVG-----KKSS-------QDEKKKAAELAVELDDTLGPGPVQ-VRVVDEGKEP 80

                            90
                    ....*....|
gi 1207111496  2133 LTFTNMFPSW 2142
Cdd:smart00262   81 PEFWSLFGGW 90
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 1487-1558 5.33e-07

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: 49.56  E-value: 5.33e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207111496 1487 SSLNSGDCFLLITPHHCFIWIGEFANVIEKAKAAELAT-FVQTKHdlgcRASY--VQTIEEGAntHTHAAKDFWK 1558
Cdd:cd11292     29 EMLDSEDCYILDCGSEIFVWVGKGASLDERKAALKNAEeFLRKKK----RPPYtqVTRVTEGG--ESALFKSKFA 97
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1610-1705 1.63e-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: 48.06  E-value: 1.63e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207111496  1610 SMLNPKEVLVFDFGSEVYVWHGKEVTLAQRKVAFQLAKHLWNGtfdytncdinpldpgecnaLIPRKGQGRpdwavfgRL 1689
Cdd:smart00262   21 GSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDT-------------------LGPGPVQVR-------VV 74

                            90
                    ....*....|....*.
gi 1207111496  1690 TQHNETTLFKEKFLDW 1705
Cdd:smart00262   75 DEGKEPPEFWSLFGGW 90
Gelsolin pfam00626
Gelsolin repeat;
1486-1523 1.97e-06

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 47.30  E-value: 1.97e-06
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1207111496 1486 ASSLNSGDCFLLITPHHCFIWIGEFANVIEKAKAAELA 1523
Cdd:pfam00626   12 QESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLA 49
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 1482-1560 2.59e-06

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: 47.36  E-value: 2.59e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207111496 1482 VEPRASSLNSGDCFLLITPHHCFIWIGEFANVIEKAKAAELAtfVQTKHDLGCRASYVQtIEEGanthtHAAKDFWKIL 1560
Cdd:cd11280     18 VPLASSSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLA--KELDEERKGKPEIVR-IRQG-----QEPREFWSLF 88
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 1607-1653 3.02e-05

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: 44.53  E-value: 3.02e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1207111496 1607 PRCSMLNPKEVLVFDFGSEVYVWHGKEVTLAQRKVAFQLAKHLWNGT 1653
Cdd:cd11288     23 ADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVASFLKPKA 69
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 1835-1880 7.55e-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: 7.55e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1207111496 1835 FFWQGRNSTVNEKGTSALMTVELDEERG---AQVQVQQGKEPPCFLQCF 1880
Cdd:cd11280     40 YIWQGRASSQAELAAAALLAKELDEERKgkpEIVRIRQGQEPREFWSLF 88
Gelsolin pfam00626
Gelsolin repeat;
1835-1877 4.09e-03

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 38.06  E-value: 4.09e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1207111496 1835 FFWQGRNSTVNEKGTSALMTVELD-EERGA---QVQVQQGKEPPCFL 1877
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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