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Conserved domains on  [gi|568963721|ref|XP_006512123|]
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villin-like protein isoform X1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ADF_gelsolin super family cl15697
Actin depolymerization factor/cofilin- and gelsolin-like domains; Actin depolymerization ...
 16-121 3.45e-39

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 cd11290:

Pssm-ID: 472830  Cd Length: 113  Bit Score: 140.82  E-value: 3.45e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963721  16 LQIWITENLKMLPLPERAHGNFFEECCYVVLHVPQSPKatQGGFSDLHYWIGKDASAEAREAAVSFVQCLQEDLGDQTVL 95
Cdd:cd11290   10 LQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDPS--GSLSYDIHYWLGKEASQDEAGAAAIKAVELDDYLGGRPVQ 87

                         90       100
                 ....*....|....*....|....*.
gi 568963721  96 HRESQGHESDCFHSYFHPGVIYRKGG 121
Cdd:cd11290   88 HREVQGHESEEFLSYFKKGIIYIEGG 113
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
 385-485 9.66e-39

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: 138.94  E-value: 9.66e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963721 385 MVDDGSGKVEVWYIQDLQRQPVHPKYYGQLCSGNCYLVLYTYQKLGCVQYLLYLWQGHQSTVEDTKALNCSAEELDLMHQ 464
Cdd:cd11293    1 MYDDGSGKVEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQGGGKEEHILYFWQGRHSSQDERAAAALLTVELDEELK 80

                         90       100
                 ....*....|....*....|.
gi 568963721 465 GALAQGHVTMGSEPPHFLAIF 485
Cdd:cd11293   81 GRAVQVRVVQGKEPPHFLALF 101
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 611-713 8.55e-37

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: 133.58  E-value: 8.55e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963721 611 QPRLFECSSHAGCLVLTEVLFFGQEDLDKYDIMLLDTCQEassvaqIFLWLG-EAAGEWKKEAVAWGLEYLRTHPAERSL 689
Cdd:cd11291    1 KPRLFRCSNESGFFKVEEISDFSQDDLDTDDIMLLDTGDE------VFVWVGsESSDEEKKEALTSAKKYIETDPLGRSK 74

                         90       100
                 ....*....|....*....|....*
gi 568963721 690 -ATPIFVVKQGHEPATFTGWFVTWD 713
Cdd:cd11291   75 pRTPIYLVKQGNEPPTFTGYFHAWD 99
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 136-229 7.50e-36

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


:

Pssm-ID: 200445  Cd Length: 92  Bit Score: 130.44  E-value: 7.50e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963721 136 VQRLLHIRGRKHVSATEVALSWNSFNKGDIFLLDLGKVMIQWNGPKASISEKARALTLTCNLRDRERGGRAQIAVVDaeN 215
Cdd:cd11289    1 KPRLLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKVIVLD--E 78

                         90
                 ....*....|....
gi 568963721 216 EATNLLRIMEAVLG 229
Cdd:cd11289   79 GDTNESPEFWKVLG 92
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 249-345 8.59e-34

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: 125.05  E-value: 8.59e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963721 249 KANVRLYHVCEKGTDLVVQELATRPLTQDLLQEDGCYLLDQGGfKIYMWQGRKSSPQEKKAALSRAVGFIQAKGYPNYTN 328
Cdd:cd11292    1 AEQKKLYKVSDASGKLKLTEVAEGSLNQEMLDSEDCYILDCGS-EIFVWVGKGASLDERKAALKNAEEFLRKKKRPPYTQ 79

                         90
                 ....*....|....*..
gi 568963721 329 VEVVNDGAESTAFQQLF 345
Cdd:cd11292   80 VTRVTEGGESALFKSKF 96
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 508-596 2.13e-33

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: 123.50  E-value: 2.13e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963721 508 TRLFHVQGTESHNTRTMEVPARASSLTSGDVFFLITSHVCYLWFGKGCHGDQREMARTVVSV-FPGNNKETVLEGQEPLY 586
Cdd:cd11288    3 TRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVASFlKPKASLQEVAEGSEPDE 82

                         90
                 ....*....|
gi 568963721 587 FWEALGGRAP 596
Cdd:cd11288   83 FWEALGGKSE 92
VHP super family cl02491
Villin headpiece domain;
830-850 2.37e-05

Villin headpiece domain;


The actual alignment was detected with superfamily member pfam02209:

Pssm-ID: 470591  Cd Length: 36  Bit Score: 41.98  E-value: 2.37e-05
                          10        20
                  ....*....|....*....|.
gi 568963721  830 YLSDSDFQDIFGKSKEEFYSM 850
Cdd:pfam02209   1 YLSDEDFEEVFGMSREEFYKL 21
 
Name Accession Description Interval E-value
gelsolin_S1_like cd11290
Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; ...
 16-121 3.45e-39

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: 140.82  E-value: 3.45e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963721  16 LQIWITENLKMLPLPERAHGNFFEECCYVVLHVPQSPKatQGGFSDLHYWIGKDASAEAREAAVSFVQCLQEDLGDQTVL 95
Cdd:cd11290   10 LQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDPS--GSLSYDIHYWLGKEASQDEAGAAAIKAVELDDYLGGRPVQ 87

                         90       100
                 ....*....|....*....|....*.
gi 568963721  96 HRESQGHESDCFHSYFHPGVIYRKGG 121
Cdd:cd11290   88 HREVQGHESEEFLSYFKKGIIYIEGG 113
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
 385-485 9.66e-39

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: 138.94  E-value: 9.66e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963721 385 MVDDGSGKVEVWYIQDLQRQPVHPKYYGQLCSGNCYLVLYTYQKLGCVQYLLYLWQGHQSTVEDTKALNCSAEELDLMHQ 464
Cdd:cd11293    1 MYDDGSGKVEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQGGGKEEHILYFWQGRHSSQDERAAAALLTVELDEELK 80

                         90       100
                 ....*....|....*....|.
gi 568963721 465 GALAQGHVTMGSEPPHFLAIF 485
Cdd:cd11293   81 GRAVQVRVVQGKEPPHFLALF 101
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 611-713 8.55e-37

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: 133.58  E-value: 8.55e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963721 611 QPRLFECSSHAGCLVLTEVLFFGQEDLDKYDIMLLDTCQEassvaqIFLWLG-EAAGEWKKEAVAWGLEYLRTHPAERSL 689
Cdd:cd11291    1 KPRLFRCSNESGFFKVEEISDFSQDDLDTDDIMLLDTGDE------VFVWVGsESSDEEKKEALTSAKKYIETDPLGRSK 74

                         90       100
                 ....*....|....*....|....*
gi 568963721 690 -ATPIFVVKQGHEPATFTGWFVTWD 713
Cdd:cd11291   75 pRTPIYLVKQGNEPPTFTGYFHAWD 99
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 136-229 7.50e-36

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


Pssm-ID: 200445  Cd Length: 92  Bit Score: 130.44  E-value: 7.50e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963721 136 VQRLLHIRGRKHVSATEVALSWNSFNKGDIFLLDLGKVMIQWNGPKASISEKARALTLTCNLRDRERGGRAQIAVVDaeN 215
Cdd:cd11289    1 KPRLLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKVIVLD--E 78

                         90
                 ....*....|....
gi 568963721 216 EATNLLRIMEAVLG 229
Cdd:cd11289   79 GDTNESPEFWKVLG 92
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 249-345 8.59e-34

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: 125.05  E-value: 8.59e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963721 249 KANVRLYHVCEKGTDLVVQELATRPLTQDLLQEDGCYLLDQGGfKIYMWQGRKSSPQEKKAALSRAVGFIQAKGYPNYTN 328
Cdd:cd11292    1 AEQKKLYKVSDASGKLKLTEVAEGSLNQEMLDSEDCYILDCGS-EIFVWVGKGASLDERKAALKNAEEFLRKKKRPPYTQ 79

                         90
                 ....*....|....*..
gi 568963721 329 VEVVNDGAESTAFQQLF 345
Cdd:cd11292   80 VTRVTEGGESALFKSKF 96
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 508-596 2.13e-33

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: 123.50  E-value: 2.13e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963721 508 TRLFHVQGTESHNTRTMEVPARASSLTSGDVFFLITSHVCYLWFGKGCHGDQREMARTVVSV-FPGNNKETVLEGQEPLY 586
Cdd:cd11288    3 TRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVASFlKPKASLQEVAEGSEPDE 82

                         90
                 ....*....|
gi 568963721 587 FWEALGGRAP 596
Cdd:cd11288   83 FWEALGGKSE 92
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 255-348 5.78e-19

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: 82.34  E-value: 5.78e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963721   255 YHVCEKGTDLVvqELATRPLTQDLLQEDGCYLLDQGGfKIYMWQGRKSSPQEKKAALSRAVGFIQAKGyPNYTNVEVVND 334
Cdd:smart00262   1 FLVRVKGKRNV--RVPEVPFSQGSLNSGDCYILDTGS-EIYVWVGKKSSQDEKKKAAELAVELDDTLG-PGPVQVRVVDE 76

                           90
                   ....*....|....
gi 568963721   335 GAESTAFQQLFWSW 348
Cdd:smart00262  77 GKEPPEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 138-212 2.98e-17

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: 77.33  E-value: 2.98e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568963721   138 RLLHIRGRKHVSATEVALSWNSFNKGDIFLLDLGKVMIQWNGPKASISEKARALTLTCNLRDRERGGRAQIAVVD 212
Cdd:smart00262   1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVRVVD 75
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 511-593 2.98e-17

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: 77.33  E-value: 2.98e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963721   511 FHVQGTESHNTRTMEVPARASSLTSGDVFFLITSHVCYLWFGKGCHGDQREMARTVVSVFPGNNK------ETVLEGQEP 584
Cdd:smart00262   1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGpgpvqvRVVDEGKEP 80


                   ....*....
gi 568963721   585 LYFWEALGG 593
Cdd:smart00262  81 PEFWSLFGG 89
Gelsolin pfam00626
Gelsolin repeat;
273-341 4.79e-14

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 67.72  E-value: 4.79e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568963721  273 PLTQDLLQEDGCYLLDQGgFKIYMWQGRKSSPQEKKAALSRAVGFIQAKgYPNYTNVEVVNDGAESTAF 341
Cdd:pfam00626   9 PLSQESLNSGDCYLLDNG-FTIFLWVGKGSSLLEKLFAALLAAQLDDDE-RFPLPEVIRVPQGKEPARF 75
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 394-487 9.25e-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: 64.62  E-value: 9.25e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963721   394 EVWYIQDLQRQPVH--PKYYGQLCSGNCYLVLYTYQklgcvqylLYLWQGHQSTVEDTKALNCSAEELDLMHQGALAQGH 471
Cdd:smart00262   1 FLVRVKGKRNVRVPevPFSQGSLNSGDCYILDTGSE--------IYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVR 72

                           90
                   ....*....|....*..
gi 568963721   472 -VTMGSEPPHFLAIFQG 487
Cdd:smart00262  73 vVDEGKEPPEFWSLFGG 89
Gelsolin pfam00626
Gelsolin repeat;
146-221 7.44e-12

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 61.55  E-value: 7.44e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568963721  146 KHVSATEVALSWNSFNKGDIFLLDLGKVMIQWNGPKASISEKARALTLTCNLRDRERGGRAQIAVVDAENEATNLL 221
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDERFPLPEVIRVPQGKEPARFL 76
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 632-712 6.24e-11

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: 59.61  E-value: 6.24e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963721   632 FGQEDLDKYDIMLLDTCQEassvaqIFLWLG-EAAGEWKKEAVAWGLEYLRThpaERSLATPIFVVKQGHEPATFTGWFV 710
Cdd:smart00262  18 FSQGSLNSGDCYILDTGSE------IYVWVGkKSSQDEKKKAAELAVELDDT---LGPGPVQVRVVDEGKEPPEFWSLFG 88


                   ..
gi 568963721   711 TW 712
Cdd:smart00262  89 GW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 17-114 1.79e-10

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: 58.07  E-value: 1.79e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963721    17 QIWITENLKMLPLPER--AHGNFFEECCYVVLHvpqspkatqgGfSDLHYWIGKDASAEAREAAVSFVQCLQEDLGDQTV 94
Cdd:smart00262   1 FLVRVKGKRNVRVPEVpfSQGSLNSGDCYILDT----------G-SEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPV 69

                           90       100
                   ....*....|....*....|.
gi 568963721    95 LHRE-SQGHESDCFHSYFHPG 114
Cdd:smart00262  70 QVRVvDEGKEPPEFWSLFGGW 90
Gelsolin pfam00626
Gelsolin repeat;
23-107 9.06e-06

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 44.22  E-value: 9.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963721   23 NLKMLPLPERAHGNFFEECCYVVLHvpqspkatqggFSDLHYWIGKDAS-AEAREAAVSFVQCLQEDLGDQTVLHRESQG 101
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDN-----------GFTIFLWVGKGSSlLEKLFAALLAAQLDDDERFPLPEVIRVPQG 69


                  ....*.
gi 568963721  102 HESDCF 107
Cdd:pfam00626  70 KEPARF 75
Gelsolin pfam00626
Gelsolin repeat;
405-482 2.02e-05

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 43.45  E-value: 2.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963721  405 PVHPKYYGQLCSGNCYLVLYTYQklgcvqylLYLWQG-HQSTVEDTKALNcSAEELDLMHQGALAQGHV-TMGSEPPHFL 482
Cdd:pfam00626   6 PPVPLSQESLNSGDCYLLDNGFT--------IFLWVGkGSSLLEKLFAAL-LAAQLDDDERFPLPEVIRvPQGKEPARFL 76
VHP pfam02209
Villin headpiece domain;
830-850 2.37e-05

Villin headpiece domain;


Pssm-ID: 460493  Cd Length: 36  Bit Score: 41.98  E-value: 2.37e-05
                          10        20
                  ....*....|....*....|.
gi 568963721  830 YLSDSDFQDIFGKSKEEFYSM 850
Cdd:pfam02209   1 YLSDEDFEEVFGMSREEFYKL 21
VHP smart00153
Villin headpiece domain;
830-850 2.94e-05

Villin headpiece domain;


Pssm-ID: 128458  Cd Length: 36  Bit Score: 41.54  E-value: 2.94e-05
                           10        20
                   ....*....|....*....|.
gi 568963721   830 YLSDSDFQDIFGKSKEEFYSM 850
Cdd:smart00153   1 YLSDEDFEEVFGMTREEFYKL 21
Gelsolin pfam00626
Gelsolin repeat;
625-705 4.62e-04

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 39.60  E-value: 4.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963721  625 VLTEVLFFGQEDLDKYDIMLLDTCQeassvaQIFLWLGEAAGEwkKEAVAWGLEYLRTHPAERSLATPIFVVKQGHEPAT 704
Cdd:pfam00626   3 VLPPPVPLSQESLNSGDCYLLDNGF------TIFLWVGKGSSL--LEKLFAALLAAQLDDDERFPLPEVIRVPQGKEPAR 74


                  .
gi 568963721  705 F 705
Cdd:pfam00626  75 F 75
 
Name Accession Description Interval E-value
gelsolin_S1_like cd11290
Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; ...
 16-121 3.45e-39

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: 140.82  E-value: 3.45e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963721  16 LQIWITENLKMLPLPERAHGNFFEECCYVVLHVPQSPKatQGGFSDLHYWIGKDASAEAREAAVSFVQCLQEDLGDQTVL 95
Cdd:cd11290   10 LQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDPS--GSLSYDIHYWLGKEASQDEAGAAAIKAVELDDYLGGRPVQ 87

                         90       100
                 ....*....|....*....|....*.
gi 568963721  96 HRESQGHESDCFHSYFHPGVIYRKGG 121
Cdd:cd11290   88 HREVQGHESEEFLSYFKKGIIYIEGG 113
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
 385-485 9.66e-39

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: 138.94  E-value: 9.66e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963721 385 MVDDGSGKVEVWYIQDLQRQPVHPKYYGQLCSGNCYLVLYTYQKLGCVQYLLYLWQGHQSTVEDTKALNCSAEELDLMHQ 464
Cdd:cd11293    1 MYDDGSGKVEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQGGGKEEHILYFWQGRHSSQDERAAAALLTVELDEELK 80

                         90       100
                 ....*....|....*....|.
gi 568963721 465 GALAQGHVTMGSEPPHFLAIF 485
Cdd:cd11293   81 GRAVQVRVVQGKEPPHFLALF 101
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 611-713 8.55e-37

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: 133.58  E-value: 8.55e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963721 611 QPRLFECSSHAGCLVLTEVLFFGQEDLDKYDIMLLDTCQEassvaqIFLWLG-EAAGEWKKEAVAWGLEYLRTHPAERSL 689
Cdd:cd11291    1 KPRLFRCSNESGFFKVEEISDFSQDDLDTDDIMLLDTGDE------VFVWVGsESSDEEKKEALTSAKKYIETDPLGRSK 74

                         90       100
                 ....*....|....*....|....*
gi 568963721 690 -ATPIFVVKQGHEPATFTGWFVTWD 713
Cdd:cd11291   75 pRTPIYLVKQGNEPPTFTGYFHAWD 99
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 136-229 7.50e-36

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


Pssm-ID: 200445  Cd Length: 92  Bit Score: 130.44  E-value: 7.50e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963721 136 VQRLLHIRGRKHVSATEVALSWNSFNKGDIFLLDLGKVMIQWNGPKASISEKARALTLTCNLRDRERGGRAQIAVVDaeN 215
Cdd:cd11289    1 KPRLLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKVIVLD--E 78

                         90
                 ....*....|....
gi 568963721 216 EATNLLRIMEAVLG 229
Cdd:cd11289   79 GDTNESPEFWKVLG 92
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 249-345 8.59e-34

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: 125.05  E-value: 8.59e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963721 249 KANVRLYHVCEKGTDLVVQELATRPLTQDLLQEDGCYLLDQGGfKIYMWQGRKSSPQEKKAALSRAVGFIQAKGYPNYTN 328
Cdd:cd11292    1 AEQKKLYKVSDASGKLKLTEVAEGSLNQEMLDSEDCYILDCGS-EIFVWVGKGASLDERKAALKNAEEFLRKKKRPPYTQ 79

                         90
                 ....*....|....*..
gi 568963721 329 VEVVNDGAESTAFQQLF 345
Cdd:cd11292   80 VTRVTEGGESALFKSKF 96
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 508-596 2.13e-33

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: 123.50  E-value: 2.13e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963721 508 TRLFHVQGTESHNTRTMEVPARASSLTSGDVFFLITSHVCYLWFGKGCHGDQREMARTVVSV-FPGNNKETVLEGQEPLY 586
Cdd:cd11288    3 TRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVASFlKPKASLQEVAEGSEPDE 82

                         90
                 ....*....|
gi 568963721 587 FWEALGGRAP 596
Cdd:cd11288   83 FWEALGGKSE 92
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 255-348 5.78e-19

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: 82.34  E-value: 5.78e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963721   255 YHVCEKGTDLVvqELATRPLTQDLLQEDGCYLLDQGGfKIYMWQGRKSSPQEKKAALSRAVGFIQAKGyPNYTNVEVVND 334
Cdd:smart00262   1 FLVRVKGKRNV--RVPEVPFSQGSLNSGDCYILDTGS-EIYVWVGKKSSQDEKKKAAELAVELDDTLG-PGPVQVRVVDE 76

                           90
                   ....*....|....
gi 568963721   335 GAESTAFQQLFWSW 348
Cdd:smart00262  77 GKEPPEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 138-212 2.98e-17

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: 77.33  E-value: 2.98e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568963721   138 RLLHIRGRKHVSATEVALSWNSFNKGDIFLLDLGKVMIQWNGPKASISEKARALTLTCNLRDRERGGRAQIAVVD 212
Cdd:smart00262   1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVRVVD 75
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 511-593 2.98e-17

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: 77.33  E-value: 2.98e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963721   511 FHVQGTESHNTRTMEVPARASSLTSGDVFFLITSHVCYLWFGKGCHGDQREMARTVVSVFPGNNK------ETVLEGQEP 584
Cdd:smart00262   1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGpgpvqvRVVDEGKEP 80


                   ....*....
gi 568963721   585 LYFWEALGG 593
Cdd:smart00262  81 PEFWSLFGG 89
Gelsolin pfam00626
Gelsolin repeat;
273-341 4.79e-14

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 67.72  E-value: 4.79e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568963721  273 PLTQDLLQEDGCYLLDQGgFKIYMWQGRKSSPQEKKAALSRAVGFIQAKgYPNYTNVEVVNDGAESTAF 341
Cdd:pfam00626   9 PLSQESLNSGDCYLLDNG-FTIFLWVGKGSSLLEKLFAALLAAQLDDDE-RFPLPEVIRVPQGKEPARF 75
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 394-487 9.25e-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: 64.62  E-value: 9.25e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963721   394 EVWYIQDLQRQPVH--PKYYGQLCSGNCYLVLYTYQklgcvqylLYLWQGHQSTVEDTKALNCSAEELDLMHQGALAQGH 471
Cdd:smart00262   1 FLVRVKGKRNVRVPevPFSQGSLNSGDCYILDTGSE--------IYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVR 72

                           90
                   ....*....|....*..
gi 568963721   472 -VTMGSEPPHFLAIFQG 487
Cdd:smart00262  73 vVDEGKEPPEFWSLFGG 89
Gelsolin pfam00626
Gelsolin repeat;
146-221 7.44e-12

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 61.55  E-value: 7.44e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568963721  146 KHVSATEVALSWNSFNKGDIFLLDLGKVMIQWNGPKASISEKARALTLTCNLRDRERGGRAQIAVVDAENEATNLL 221
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDERFPLPEVIRVPQGKEPARFL 76
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 253-349 1.05e-11

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: 61.93  E-value: 1.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963721 253 RLYHV-CEKGTdLVVQELAtrPLTQDLLQEDGCYLLDQGGfKIYMWQGRKSSPQEKKAALSRAVGFIQ---AKGYPNYTN 328
Cdd:cd11291    3 RLFRCsNESGF-FKVEEIS--DFSQDDLDTDDIMLLDTGD-EVFVWVGSESSDEEKKEALTSAKKYIEtdpLGRSKPRTP 78

                         90       100
                 ....*....|....*....|.
gi 568963721 329 VEVVNDGAESTAFQQLFWSWS 349
Cdd:cd11291   79 IYLVKQGNEPPTFTGYFHAWD 99
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 632-712 6.24e-11

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: 59.61  E-value: 6.24e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963721   632 FGQEDLDKYDIMLLDTCQEassvaqIFLWLG-EAAGEWKKEAVAWGLEYLRThpaERSLATPIFVVKQGHEPATFTGWFV 710
Cdd:smart00262  18 FSQGSLNSGDCYILDTGSE------IYVWVGkKSSQDEKKKAAELAVELDDT---LGPGPVQVRVVDEGKEPPEFWSLFG 88


                   ..
gi 568963721   711 TW 712
Cdd:smart00262  89 GW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 17-114 1.79e-10

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: 58.07  E-value: 1.79e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963721    17 QIWITENLKMLPLPER--AHGNFFEECCYVVLHvpqspkatqgGfSDLHYWIGKDASAEAREAAVSFVQCLQEDLGDQTV 94
Cdd:smart00262   1 FLVRVKGKRNVRVPEVpfSQGSLNSGDCYILDT----------G-SEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPV 69

                           90       100
                   ....*....|....*....|.
gi 568963721    95 LHRE-SQGHESDCFHSYFHPG 114
Cdd:smart00262  70 QVRVvDEGKEPPEFWSLFGGW 90
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 609-709 2.24e-10

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: 58.03  E-value: 2.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963721 609 SIQPRLFECSSHAGCLVLTEVL--FFGQEDLDKYDIMLLDTcqeassVAQIFLWLG-EAAGEWKKEAVAWGLEYLRTHpa 685
Cdd:cd11292    1 AEQKKLYKVSDASGKLKLTEVAegSLNQEMLDSEDCYILDC------GSEIFVWVGkGASLDERKAALKNAEEFLRKK-- 72

                         90       100
                 ....*....|....*....|....
gi 568963721 686 ERSLATPIFVVKQGHEPATFTGWF 709
Cdd:cd11292   73 KRPPYTQVTRVTEGGESALFKSKF 96
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 507-592 2.90e-10

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: 57.63  E-value: 2.90e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963721 507 DTRLFHVQGTEshNTRTMEVPARASSLTSGDVFFLITSHVCYLWFGKGCH--------------GDQREMARTVVSVFpg 572
Cdd:cd11289    1 KPRLLHVKGRR--NVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNrfekakamqlaqgiRDERRLGRAKVIVL-- 76

                         90       100
                 ....*....|....*....|
gi 568963721 573 nnkeTVLEGQEPLYFWEALG 592
Cdd:cd11289   77 ----DEGDTNESPEFWKVLG 92
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
 8-111 1.58e-09

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: 55.74  E-value: 1.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963721   8 PAIDSHRALQIWITENLKMLPLPERAHGNFFEECCYVVLHVPQspkatQGGFSD--LHYWIGKDASAEAREAAVSFVQCL 85
Cdd:cd11293    1 MYDDGSGKVEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQ-----GGGKEEhiLYFWQGRHSSQDERAAAALLTVEL 75

                         90       100
                 ....*....|....*....|....*.
gi 568963721  86 QEDLGDQTVLHRESQGHESDCFHSYF 111
Cdd:cd11293   76 DEELKGRAVQVRVVQGKEPPHFLALF 101
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 253-345 3.99e-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: 54.30  E-value: 3.99e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963721 253 RLYHvCEKGTDLVVQELATRPltqDLLQEDGCYLLDQGgFKIYMWQGRKSSPQEKKAALSRAVGFIqaKGYPNYTNVEVV 332
Cdd:cd11280    3 RLYR-VRGSKAIEIEEVPLAS---SSLDSDDVFVLDTG-SEIYIWQGRASSQAELAAAALLAKELD--EERKGKPEIVRI 75

                         90
                 ....*....|...
gi 568963721 333 NDGAESTAFQQLF 345
Cdd:cd11280   76 RQGQEPREFWSLF 88
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 507-591 8.90e-08

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: 50.44  E-value: 8.90e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963721 507 DTRLFHVQGteSHNTRTMEVPARASSLTSGDVF-FLITSHVcYLWFGKGCHGDQREMARTVVSVF---PGNNKETVL--E 580
Cdd:cd11280    1 PPRLYRVRG--SKAIEIEEVPLASSSLDSDDVFvLDTGSEI-YIWQGRASSQAELAAAALLAKELdeeRKGKPEIVRirQ 77

                         90
                 ....*....|.
gi 568963721 581 GQEPLYFWEAL 591
Cdd:cd11280   78 GQEPREFWSLF 88
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 138-211 1.70e-07

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: 49.67  E-value: 1.70e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568963721 138 RLLHIRGRKHVSATEVALSWNSFNKGDIFLLDLGKVMIQWNGPKASISEKARALTLTCNLrDRERGGRAQIAVV 211
Cdd:cd11280    3 RLYRVRGSKAIEIEEVPLASSSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKEL-DEERKGKPEIVRI 75
gelsolin_S1_like cd11290
Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; ...
 393-485 8.84e-07

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: 48.37  E-value: 8.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963721 393 VEVWYIQDLQRQPVHPKYYGQLCSGNCYLVLYTYQ-KLGCVQYLLYLWQGHQSTVEDTKALNCSAEELDLMHQGALAQGH 471
Cdd:cd11290   10 LQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLdPSGSLSYDIHYWLGKEASQDEAGAAAIKAVELDDYLGGRPVQHR 89

                         90
                 ....*....|....
gi 568963721 472 VTMGSEPPHFLAIF 485
Cdd:cd11290   90 EVQGHESEEFLSYF 103
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 17-111 1.39e-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: 46.98  E-value: 1.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963721  17 QIWITENLKMLPL--PERAHGNFFEECCYVVLHvpqspkatqggFSDLHYWIGKDASAEAREAAVSFVQCLQEDLGDQTV 94
Cdd:cd11280    3 RLYRVRGSKAIEIeeVPLASSSLDSDDVFVLDT-----------GSEIYIWQGRASSQAELAAAALLAKELDEERKGKPE 71

                         90
                 ....*....|....*..
gi 568963721  95 LHRESQGHESDCFHSYF 111
Cdd:cd11280   72 IVRIRQGQEPREFWSLF 88
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 611-709 1.47e-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: 46.98  E-value: 1.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963721 611 QPRLFECSShAGCLVLTEVLFFGqEDLDKYDIMLLDTCQEassvaqIFLWLGEAAGEWKKEAVAWGLEYLRthpAERSLA 690
Cdd:cd11280    1 PPRLYRVRG-SKAIEIEEVPLAS-SSLDSDDVFVLDTGSE------IYIWQGRASSQAELAAAALLAKELD---EERKGK 69

                         90
                 ....*....|....*....
gi 568963721 691 TPIFVVKQGHEPATFTGWF 709
Cdd:cd11280   70 PEIVRIRQGQEPREFWSLF 88
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 250-348 4.38e-06

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: 45.69  E-value: 4.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963721 250 ANVRLYHVCekGTDlvvqELATRPLTQD----LLQEDGCYLLdQGGFKIYMWQGRKSSPQEKKAALSravgfiQAKGYPN 325
Cdd:cd11288    1 SPTRLFQVR--GNG----SGNTRAVEVDadasSLNSNDVFVL-KTPSSVYLWVGKGSSEDERELAKD------VASFLKP 67

                         90       100
                 ....*....|....*....|...
gi 568963721 326 YTNVEVVNDGAESTAFqqlFWSW 348
Cdd:cd11288   68 KASLQEVAEGSEPDEF---WEAL 87
Gelsolin pfam00626
Gelsolin repeat;
23-107 9.06e-06

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 44.22  E-value: 9.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963721   23 NLKMLPLPERAHGNFFEECCYVVLHvpqspkatqggFSDLHYWIGKDAS-AEAREAAVSFVQCLQEDLGDQTVLHRESQG 101
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDN-----------GFTIFLWVGKGSSlLEKLFAALLAAQLDDDERFPLPEVIRVPQG 69


                  ....*.
gi 568963721  102 HESDCF 107
Cdd:pfam00626  70 KEPARF 75
Gelsolin pfam00626
Gelsolin repeat;
405-482 2.02e-05

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 43.45  E-value: 2.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963721  405 PVHPKYYGQLCSGNCYLVLYTYQklgcvqylLYLWQG-HQSTVEDTKALNcSAEELDLMHQGALAQGHV-TMGSEPPHFL 482
Cdd:pfam00626   6 PPVPLSQESLNSGDCYLLDNGFT--------IFLWVGkGSSLLEKLFAAL-LAAQLDDDERFPLPEVIRvPQGKEPARFL 76
VHP pfam02209
Villin headpiece domain;
830-850 2.37e-05

Villin headpiece domain;


Pssm-ID: 460493  Cd Length: 36  Bit Score: 41.98  E-value: 2.37e-05
                          10        20
                  ....*....|....*....|.
gi 568963721  830 YLSDSDFQDIFGKSKEEFYSM 850
Cdd:pfam02209   1 YLSDEDFEEVFGMSREEFYKL 21
VHP smart00153
Villin headpiece domain;
830-850 2.94e-05

Villin headpiece domain;


Pssm-ID: 128458  Cd Length: 36  Bit Score: 41.54  E-value: 2.94e-05
                           10        20
                   ....*....|....*....|.
gi 568963721   830 YLSDSDFQDIFGKSKEEFYSM 850
Cdd:smart00153   1 YLSDEDFEEVFGMTREEFYKL 21
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 395-485 3.01e-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: 43.13  E-value: 3.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963721 395 VWYIQDLQRQPVhPKYYGQLCSGNCYLVLYtyqklgcvQYLLYLWQGHQSTVEDTKALNCSAEELDLMHQGALAQGHVTM 474
Cdd:cd11280    7 VRGSKAIEIEEV-PLASSSLDSDDVFVLDT--------GSEIYIWQGRASSQAELAAAALLAKELDEERKGKPEIVRIRQ 77

                         90
                 ....*....|.
gi 568963721 475 GSEPPHFLAIF 485
Cdd:cd11280   78 GQEPREFWSLF 88
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 505-587 7.32e-05

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


Pssm-ID: 200448  Cd Length: 98  Bit Score: 42.62  E-value: 7.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963721 505 VSDTRLFHVQ-GTESHNTRTMEV-PARASSLTSGDVFFLITSHVCYLWFGKGCHGDQREMARTVVSVFPGNNK------- 575
Cdd:cd11292    1 AEQKKLYKVSdASGKLKLTEVAEgSLNQEMLDSEDCYILDCGSEIFVWVGKGASLDERKAALKNAEEFLRKKKrppytqv 80

                         90
                 ....*....|..
gi 568963721 576 ETVLEGQEPLYF 587
Cdd:cd11292   81 TRVTEGGESALF 92
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 40-111 9.07e-05

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


Pssm-ID: 200448  Cd Length: 98  Bit Score: 42.24  E-value: 9.07e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568963721  40 ECCYVVLHVpqspkatqggfSDLHYWIGKDASAEAREAAVS----FVQclQEDLGDQTVLHRESQGHESDCFHSYF 111
Cdd:cd11292   34 EDCYILDCG-----------SEIFVWVGKGASLDERKAALKnaeeFLR--KKKRPPYTQVTRVTEGGESALFKSKF 96
Gelsolin pfam00626
Gelsolin repeat;
625-705 4.62e-04

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 39.60  E-value: 4.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963721  625 VLTEVLFFGQEDLDKYDIMLLDTCQeassvaQIFLWLGEAAGEwkKEAVAWGLEYLRTHPAERSLATPIFVVKQGHEPAT 704
Cdd:pfam00626   3 VLPPPVPLSQESLNSGDCYLLDNGF------TIFLWVGKGSSL--LEKLFAALLAAQLDDDERFPLPEVIRVPQGKEPAR 74


                  .
gi 568963721  705 F 705
Cdd:pfam00626  75 F 75
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 138-193 4.16e-03

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: 37.21  E-value: 4.16e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568963721 138 RLLHIRGRKHVS--ATEVALSWNSFNKGDIFLLDLGKVMIQWNGPKASISEKARALTL 193
Cdd:cd11288    4 RLFQVRGNGSGNtrAVEVDADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDV 61
 
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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