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Conserved domains on  [gi|301069339|ref|NP_001030338|]
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supervillin a isoform 2 [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; ...
 1291-1402 6.27e-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: 154.74  E-value: 6.27e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301069339 1291 FEISTLSVDVWHILEFDYSRLPKQSIGQFHEGDTYVVKWKYMISravgkrlhseriigpGKEKCCYFFWQGRNSTVNEKG 1370
Cdd:cd11293     2 YDDGSGKVEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQGG---------------GKEEHILYFWQGRHSSQDERA 66

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 301069339 1371 TSALMTVELDEE---RGAQVQVQQGKEPPCFLQCF 1402
Cdd:cd11293    67 AAALLTVELDEElkgRAVQVRVVQGKEPPHFLALF 101
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 987-1083 4.65e-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: 4.65e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301069339  987 KLMLIQVKGRRHVQTRLVEPRASSLNSGDCFLLITPHHCFIWIGEFANVIEKAKAAELATFVQTKHDLGCRASYVQTIEE 1066
Cdd:cd11289     1 KPRLLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKVIVLDEGD 80

                          90
                  ....*....|....*..
gi 301069339 1067 GANTHThaakdFWKILG 1083
Cdd:cd11289    81 TNESPE-----FWKVLG 92
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 1424-1527 3.24e-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: 98.07  E-value: 3.24e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301069339 1424 WRLYCVRGEKPIEGHLLEAVCHCSSLRSRTSMILLNiPKaSLYLWHGCKAQVHTRDVGRTTANKIKEqcpleaglhsssK 1503
Cdd:cd11288     3 TRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKT-PS-SVYLWVGKGSSEDERELAKDVASFLKP------------K 68

                          90       100
                  ....*....|....*....|....
gi 301069339 1504 VSIQECDEGAEPQGFWEALGKRDR 1527
Cdd:cd11288    69 ASLQEVAEGSEPDEFWEALGGKSE 92
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 1108-1208 2.47e-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: 2.47e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301069339 1108 NCIYRLMEDKlvphDDYWGRVPRCS-MLNPKEVLVFDFGSEVYVWHGKEVTLAQRKVAFQLAKHLWNGtfdytncdinpl 1186
Cdd:cd11280     2 PRLYRVRGSK----AIEIEEVPLASsSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKELDEE------------ 65

                          90       100
                  ....*....|....*....|...
gi 301069339 1187 DPGECNALIPRKGQG-RPDWAVF 1208
Cdd:cd11280    66 RKGKPEIVRIRQGQEpREFWSLF 88
ADF_gelsolin super family cl15697
Actin depolymerization factor/cofilin- and gelsolin-like domains; Actin depolymerization ...
 1544-1665 2.51e-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: 67.32  E-value: 2.51e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301069339 1544 PRLFQLSSASGeFAAVEFVYPsrepnlvnsmpFLQEDLytATQpALFLVDNHHEVYLWQGwwpqdSESTgsarirwDSDR 1623
Cdd:cd11291     2 PRLFRCSNESG-FFKVEEISD-----------FSQDDL--DTD-DIMLLDTGDEVFVWVG-----SESS-------DEEK 54

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 301069339 1624 KCAMETVLQYSK----EKNEKKTPKsYLIHAGLEPLTFTNMFPSWE 1665
Cdd:cd11291    55 KEALTSAKKYIEtdplGRSKPRTPI-YLVKQGNEPPTFTGYFHAWD 99
VHP pfam02209
Villin headpiece domain;
1721-1763 2.80e-12

Villin headpiece domain;


:

Pssm-ID: 460493  Cd Length: 36  Bit Score: 62.40  E-value: 2.80e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 301069339  1721 YLSDEDFEgvgasgkKALEMTRSEYEALPGWKQVNVKKAKGLF 1763
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; ...
 1291-1402 6.27e-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: 154.74  E-value: 6.27e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301069339 1291 FEISTLSVDVWHILEFDYSRLPKQSIGQFHEGDTYVVKWKYMISravgkrlhseriigpGKEKCCYFFWQGRNSTVNEKG 1370
Cdd:cd11293     2 YDDGSGKVEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQGG---------------GKEEHILYFWQGRHSSQDERA 66

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 301069339 1371 TSALMTVELDEE---RGAQVQVQQGKEPPCFLQCF 1402
Cdd:cd11293    67 AAALLTVELDEElkgRAVQVRVVQGKEPPHFLALF 101
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 987-1083 4.65e-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: 4.65e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301069339  987 KLMLIQVKGRRHVQTRLVEPRASSLNSGDCFLLITPHHCFIWIGEFANVIEKAKAAELATFVQTKHDLGCRASYVQTIEE 1066
Cdd:cd11289     1 KPRLLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKVIVLDEGD 80

                          90
                  ....*....|....*..
gi 301069339 1067 GANTHThaakdFWKILG 1083
Cdd:cd11289    81 TNESPE-----FWKVLG 92
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 1424-1527 3.24e-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: 98.07  E-value: 3.24e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301069339 1424 WRLYCVRGEKPIEGHLLEAVCHCSSLRSRTSMILLNiPKaSLYLWHGCKAQVHTRDVGRTTANKIKEqcpleaglhsssK 1503
Cdd:cd11288     3 TRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKT-PS-SVYLWVGKGSSEDERELAKDVASFLKP------------K 68

                          90       100
                  ....*....|....*....|....
gi 301069339 1504 VSIQECDEGAEPQGFWEALGKRDR 1527
Cdd:cd11288    69 ASLQEVAEGSEPDEFWEALGGKSE 92
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 990-1084 1.94e-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: 1.94e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301069339    990 LIQVKGRRHVQTRLVEPRASSLNSGDCFLLITPHHCFIWIGEFANVIEKAKAAELAtfVQTKHDLGCRASYVQTIEEGAN 1069
Cdd:smart00262    2 LVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELA--VELDDTLGPGPVQVRVVDEGKE 79

                            90
                    ....*....|....*
gi 301069339   1070 THThaakdFWKILGG 1084
Cdd:smart00262   80 PPE-----FWSLFGG 89
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 1108-1208 2.47e-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: 2.47e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301069339 1108 NCIYRLMEDKlvphDDYWGRVPRCS-MLNPKEVLVFDFGSEVYVWHGKEVTLAQRKVAFQLAKHLWNGtfdytncdinpl 1186
Cdd:cd11280     2 PRLYRVRGSK----AIEIEEVPLASsSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKELDEE------------ 65

                          90       100
                  ....*....|....*....|...
gi 301069339 1187 DPGECNALIPRKGQG-RPDWAVF 1208
Cdd:cd11280    66 RKGKPEIVRIRQGQEpREFWSLF 88
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 1544-1665 2.51e-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: 67.32  E-value: 2.51e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301069339 1544 PRLFQLSSASGeFAAVEFVYPsrepnlvnsmpFLQEDLytATQpALFLVDNHHEVYLWQGwwpqdSESTgsarirwDSDR 1623
Cdd:cd11291     2 PRLFRCSNESG-FFKVEEISD-----------FSQDDL--DTD-DIMLLDTGDEVFVWVG-----SESS-------DEEK 54

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 301069339 1624 KCAMETVLQYSK----EKNEKKTPKsYLIHAGLEPLTFTNMFPSWE 1665
Cdd:cd11291    55 KEALTSAKKYIEtdplGRSKPRTPI-YLVKQGNEPPTFTGYFHAWD 99
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1300-1405 9.76e-13

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 65.39  E-value: 9.76e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301069339   1300 VWHILEFDYSRLP--KQSIGQFHEGDTYVVKWKYMIsravgkrlhseriigpgkekccyFFWQGRNSTVNEKGTSALMTV 1377
Cdd:smart00262    2 LVRVKGKRNVRVPevPFSQGSLNSGDCYILDTGSEI-----------------------YVWVGKKSSQDEKKKAAELAV 58

                            90       100       110
                    ....*....|....*....|....*....|..
gi 301069339   1378 ELDEERG---AQVQ-VQQGKEPPCFLQCFNGG 1405
Cdd:smart00262   59 ELDDTLGpgpVQVRvVDEGKEPPEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1427-1523 2.80e-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: 64.24  E-value: 2.80e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301069339   1427 YCVRGEKPIEGHLLEAVCHCSSLRSRTSMILLNipKASLYLWHGCKAQVHTRDVGRTTANKIKEQCPleaglhsSSKVSI 1506
Cdd:smart00262    1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDT--GSEIYVWVGKKSSQDEKKKAAELAVELDDTLG-------PGPVQV 71

                            90
                    ....*....|....*..
gi 301069339   1507 QECDEGAEPQGFWEALG 1523
Cdd:smart00262   72 RVVDEGKEPPEFWSLFG 88
VHP pfam02209
Villin headpiece domain;
1721-1763 2.80e-12

Villin headpiece domain;


Pssm-ID: 460493  Cd Length: 36  Bit Score: 62.40  E-value: 2.80e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 301069339  1721 YLSDEDFEgvgasgkKALEMTRSEYEALPGWKQVNVKKAKGLF 1763
Cdd:pfam02209    1 YLSDEDFE-------EVFGMSREEFYKLPKWKQNNLKKKAGLF 36
VHP smart00153
Villin headpiece domain;
1721-1763 1.48e-10

Villin headpiece domain;


Pssm-ID: 128458  Cd Length: 36  Bit Score: 57.71  E-value: 1.48e-10
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 301069339   1721 YLSDEDFEgvgasgkKALEMTRSEYEALPGWKQVNVKKAKGLF 1763
Cdd:smart00153    1 YLSDEDFE-------EVFGMTREEFYKLPLWKQNQLKKKKGLF 36
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1575-1664 9.72e-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: 51.14  E-value: 9.72e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301069339   1575 PFLQEDLYTAtqpALFLVDNHHEVYLWQGwwpqdSESTgsarirwDSDRKCAMETVLQYSKEKNEKKTPkSYLIHAGLEP 1654
Cdd:smart00262   17 PFSQGSLNSG---DCYILDTGSEIYVWVG-----KKSS-------QDEKKKAAELAVELDDTLGPGPVQ-VRVVDEGKEP 80

                            90
                    ....*....|
gi 301069339   1655 LTFTNMFPSW 1664
Cdd:smart00262   81 PEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1132-1227 1.55e-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: 47.67  E-value: 1.55e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301069339   1132 SMLNPKEVLVFDFGSEVYVWHGKEVTLAQRKVAFQLAKHLWNGtfdytncdinpldpgecnaLIPRKGQGRpdwavfgRL 1211
Cdd:smart00262   21 GSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDT-------------------LGPGPVQVR-------VV 74

                            90
                    ....*....|....*.
gi 301069339   1212 TQHNETTLFKEKFLDW 1227
Cdd:smart00262   75 DEGKEPPEFWSLFGGW 90
Gelsolin pfam00626
Gelsolin repeat;
1008-1045 1.74e-06

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 47.30  E-value: 1.74e-06
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 301069339  1008 ASSLNSGDCFLLITPHHCFIWIGEFANVIEKAKAAELA 1045
Cdd:pfam00626   12 QESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLA 49
Gelsolin pfam00626
Gelsolin repeat;
1357-1399 3.30e-03

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 38.06  E-value: 3.30e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 301069339  1357 FFWQGRNSTVNEKGTSALMTVELD-EERGA---QVQVQQGKEPPCFL 1399
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; ...
 1291-1402 6.27e-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: 154.74  E-value: 6.27e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301069339 1291 FEISTLSVDVWHILEFDYSRLPKQSIGQFHEGDTYVVKWKYMISravgkrlhseriigpGKEKCCYFFWQGRNSTVNEKG 1370
Cdd:cd11293     2 YDDGSGKVEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQGG---------------GKEEHILYFWQGRHSSQDERA 66

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 301069339 1371 TSALMTVELDEE---RGAQVQVQQGKEPPCFLQCF 1402
Cdd:cd11293    67 AAALLTVELDEElkgRAVQVRVVQGKEPPHFLALF 101
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 987-1083 4.65e-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: 4.65e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301069339  987 KLMLIQVKGRRHVQTRLVEPRASSLNSGDCFLLITPHHCFIWIGEFANVIEKAKAAELATFVQTKHDLGCRASYVQTIEE 1066
Cdd:cd11289     1 KPRLLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKVIVLDEGD 80

                          90
                  ....*....|....*..
gi 301069339 1067 GANTHThaakdFWKILG 1083
Cdd:cd11289    81 TNESPE-----FWKVLG 92
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 1424-1527 3.24e-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: 98.07  E-value: 3.24e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301069339 1424 WRLYCVRGEKPIEGHLLEAVCHCSSLRSRTSMILLNiPKaSLYLWHGCKAQVHTRDVGRTTANKIKEqcpleaglhsssK 1503
Cdd:cd11288     3 TRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKT-PS-SVYLWVGKGSSEDERELAKDVASFLKP------------K 68

                          90       100
                  ....*....|....*....|....
gi 301069339 1504 VSIQECDEGAEPQGFWEALGKRDR 1527
Cdd:cd11288    69 ASLQEVAEGSEPDEFWEALGGKSE 92
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 990-1084 1.94e-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: 1.94e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301069339    990 LIQVKGRRHVQTRLVEPRASSLNSGDCFLLITPHHCFIWIGEFANVIEKAKAAELAtfVQTKHDLGCRASYVQTIEEGAN 1069
Cdd:smart00262    2 LVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELA--VELDDTLGPGPVQVRVVDEGKE 79

                            90
                    ....*....|....*
gi 301069339   1070 THThaakdFWKILGG 1084
Cdd:smart00262   80 PPE-----FWSLFGG 89
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 989-1087 7.24e-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: 79.97  E-value: 7.24e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301069339  989 MLIQVKGRRHVQTRLVE--PRASSLNSGDCFLLITPHHCFIWIGEFANVIEKAKAAELATFvqtkhdLGCRASYvQTIEE 1066
Cdd:cd11288     4 RLFQVRGNGSGNTRAVEvdADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVASF------LKPKASL-QEVAE 76

                          90       100
                  ....*....|....*....|.
gi 301069339 1067 GANThthaaKDFWKILGGQTS 1087
Cdd:cd11288    77 GSEP-----DEFWEALGGKSE 92
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 1108-1208 2.47e-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: 2.47e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301069339 1108 NCIYRLMEDKlvphDDYWGRVPRCS-MLNPKEVLVFDFGSEVYVWHGKEVTLAQRKVAFQLAKHLWNGtfdytncdinpl 1186
Cdd:cd11280     2 PRLYRVRGSK----AIEIEEVPLASsSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKELDEE------------ 65

                          90       100
                  ....*....|....*....|...
gi 301069339 1187 DPGECNALIPRKGQG-RPDWAVF 1208
Cdd:cd11280    66 RKGKPEIVRIRQGQEpREFWSLF 88
gelsolin_S1_like cd11290
Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; ...
 1298-1411 8.13e-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: 69.17  E-value: 8.13e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301069339 1298 VDVWHILEFDYSRLPKQSIGQFHEGDTYVVkwkymisravgkrLHSERIiGPGKEKCCYFFWQGRNSTVNEKGTSALMTV 1377
Cdd:cd11290    10 LQIWRIENFELVPVPESFYGKFYEGDSYIV-------------LKTTLD-PSGSLSYDIHYWLGKEASQDEAGAAAIKAV 75

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 301069339 1378 ELDEERGAQ-VQVQ--QGKEPPCFLQCFNGGMIVHAG 1411
Cdd:cd11290    76 ELDDYLGGRpVQHRevQGHESEEFLSYFKKGIIYIEG 112
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 1544-1665 2.51e-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: 67.32  E-value: 2.51e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301069339 1544 PRLFQLSSASGeFAAVEFVYPsrepnlvnsmpFLQEDLytATQpALFLVDNHHEVYLWQGwwpqdSESTgsarirwDSDR 1623
Cdd:cd11291     2 PRLFRCSNESG-FFKVEEISD-----------FSQDDL--DTD-DIMLLDTGDEVFVWVG-----SESS-------DEEK 54

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 301069339 1624 KCAMETVLQYSK----EKNEKKTPKsYLIHAGLEPLTFTNMFPSWE 1665
Cdd:cd11291    55 KEALTSAKKYIEtdplGRSKPRTPI-YLVKQGNEPPTFTGYFHAWD 99
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1300-1405 9.76e-13

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 65.39  E-value: 9.76e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301069339   1300 VWHILEFDYSRLP--KQSIGQFHEGDTYVVKWKYMIsravgkrlhseriigpgkekccyFFWQGRNSTVNEKGTSALMTV 1377
Cdd:smart00262    2 LVRVKGKRNVRVPevPFSQGSLNSGDCYILDTGSEI-----------------------YVWVGKKSSQDEKKKAAELAV 58

                            90       100       110
                    ....*....|....*....|....*....|..
gi 301069339   1378 ELDEERG---AQVQ-VQQGKEPPCFLQCFNGG 1405
Cdd:smart00262   59 ELDDTLGpgpVQVRvVDEGKEPPEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1427-1523 2.80e-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: 64.24  E-value: 2.80e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301069339   1427 YCVRGEKPIEGHLLEAVCHCSSLRSRTSMILLNipKASLYLWHGCKAQVHTRDVGRTTANKIKEQCPleaglhsSSKVSI 1506
Cdd:smart00262    1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDT--GSEIYVWVGKKSSQDEKKKAAELAVELDDTLG-------PGPVQV 71

                            90
                    ....*....|....*..
gi 301069339   1507 QECDEGAEPQGFWEALG 1523
Cdd:smart00262   72 RVVDEGKEPPEFWSLFG 88
VHP pfam02209
Villin headpiece domain;
1721-1763 2.80e-12

Villin headpiece domain;


Pssm-ID: 460493  Cd Length: 36  Bit Score: 62.40  E-value: 2.80e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 301069339  1721 YLSDEDFEgvgasgkKALEMTRSEYEALPGWKQVNVKKAKGLF 1763
Cdd:pfam02209    1 YLSDEDFE-------EVFGMSREEFYKLPKWKQNNLKKKAGLF 36
VHP smart00153
Villin headpiece domain;
1721-1763 1.48e-10

Villin headpiece domain;


Pssm-ID: 128458  Cd Length: 36  Bit Score: 57.71  E-value: 1.48e-10
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 301069339   1721 YLSDEDFEgvgasgkKALEMTRSEYEALPGWKQVNVKKAKGLF 1763
Cdd:smart00153    1 YLSDEDFE-------EVFGMTREEFYKLPLWKQNQLKKKKGLF 36
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 1132-1224 3.10e-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: 3.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301069339 1132 SMLNPKEVLVFDFGSEVYVWHGKEVTLAQRKVAFQLAkhlwngtfdytncdinpldpgecNALIPRKgqGRPDWAVFGRL 1211
Cdd:cd11292    29 EMLDSEDCYILDCGSEIFVWVGKGASLDERKAALKNA-----------------------EEFLRKK--KRPPYTQVTRV 83

                          90
                  ....*....|...
gi 301069339 1212 TQHNETTLFKEKF 1224
Cdd:cd11292    84 TEGGESALFKSKF 96
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 1544-1661 4.45e-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: 4.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301069339 1544 PRLFQLSSASgefaAVEFVYPSREPNLVNSMPFLQEDLYTatqpalflvdnhhEVYLWQGWwpqdsestGSARIRWDSDR 1623
Cdd:cd11280     2 PRLYRVRGSK----AIEIEEVPLASSSLDSDDVFVLDTGS-------------EIYIWQGR--------ASSQAELAAAA 56

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 301069339 1624 KCAMETvlqyskEKNEKKTPKSYLIHAGLEPLTFTNMF 1661
Cdd:cd11280    57 LLAKEL------DEERKGKPEIVRIRQGQEPREFWSLF 88
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1575-1664 9.72e-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: 51.14  E-value: 9.72e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301069339   1575 PFLQEDLYTAtqpALFLVDNHHEVYLWQGwwpqdSESTgsarirwDSDRKCAMETVLQYSKEKNEKKTPkSYLIHAGLEP 1654
Cdd:smart00262   17 PFSQGSLNSG---DCYILDTGSEIYVWVG-----KKSS-------QDEKKKAAELAVELDDTLGPGPVQ-VRVVDEGKEP 80

                            90
                    ....*....|
gi 301069339   1655 LTFTNMFPSW 1664
Cdd:smart00262   81 PEFWSLFGGW 90
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 1009-1080 4.17e-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: 4.17e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 301069339 1009 SSLNSGDCFLLITPHHCFIWIGEFANVIEKAKAAELAT-FVQTKHdlgcRASY--VQTIEEGAntHTHAAKDFWK 1080
Cdd:cd11292    29 EMLDSEDCYILDCGSEIFVWVGKGASLDERKAALKNAEeFLRKKK----RPPYtqVTRVTEGG--ESALFKSKFA 97
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1132-1227 1.55e-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: 47.67  E-value: 1.55e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301069339   1132 SMLNPKEVLVFDFGSEVYVWHGKEVTLAQRKVAFQLAKHLWNGtfdytncdinpldpgecnaLIPRKGQGRpdwavfgRL 1211
Cdd:smart00262   21 GSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDT-------------------LGPGPVQVR-------VV 74

                            90
                    ....*....|....*.
gi 301069339   1212 TQHNETTLFKEKFLDW 1227
Cdd:smart00262   75 DEGKEPPEFWSLFGGW 90
Gelsolin pfam00626
Gelsolin repeat;
1008-1045 1.74e-06

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 47.30  E-value: 1.74e-06
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 301069339  1008 ASSLNSGDCFLLITPHHCFIWIGEFANVIEKAKAAELA 1045
Cdd:pfam00626   12 QESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLA 49
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 1004-1082 1.81e-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: 47.75  E-value: 1.81e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 301069339 1004 VEPRASSLNSGDCFLLITPHHCFIWIGEFANVIEKAKAAELAtfVQTKHDLGCRASYVQtIEEGanthtHAAKDFWKIL 1082
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; ...
 1129-1175 2.45e-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: 2.45e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 301069339 1129 PRCSMLNPKEVLVFDFGSEVYVWHGKEVTLAQRKVAFQLAKHLWNGT 1175
Cdd:cd11288    23 ADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVASFLKPKA 69
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 1357-1402 5.52e-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: 5.52e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 301069339 1357 FFWQGRNSTVNEKGTSALMTVELDEERG---AQVQVQQGKEPPCFLQCF 1402
Cdd:cd11280    40 YIWQGRASSQAELAAAALLAKELDEERKgkpEIVRIRQGQEPREFWSLF 88
Gelsolin pfam00626
Gelsolin repeat;
1357-1399 3.30e-03

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 38.06  E-value: 3.30e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 301069339  1357 FFWQGRNSTVNEKGTSALMTVELD-EERGA---QVQVQQGKEPPCFL 1399
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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