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Conserved domains on  [gi|568963735|ref|XP_006512130|]
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villin-like protein isoform X7 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
219-321 1.77e-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: 132.42  E-value: 1.77e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963735 219 QPRLFECSSHAGCLVLTEVLFFGQEDLDKYDIMLLDTCQEassvaqIFLWLG-EAAGEWKKEAVAWGLEYLRTHPAERSL 297
Cdd:cd11291    1 KPRLFRCSNESGFFKVEEISDFSQDDLDTDDIMLLDTGDE------VFVWVGsESSDEEKKEALTSAKKYIETDPLGRSK 74
                         90       100
                 ....*....|....*....|....*
gi 568963735 298 -ATPIFVVKQGHEPATFTGWFVTWD 321
Cdd:cd11291   75 pRTPIYLVKQGNEPPTFTGYFHAWD 99
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
116-204 2.80e-34

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: 2.80e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963735 116 TRLFHVQGTESHNTRTMEVPARASSLTSGDVFFLITSHVCYLWFGKGCHGDQREMARTVVSV-FPGNNKETVLEGQEPLY 194
Cdd:cd11288    3 TRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVASFlKPKASLQEVAEGSEPDE 82
                         90
                 ....*....|
gi 568963735 195 FWEALGGRAP 204
Cdd:cd11288   83 FWEALGGKSE 92
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
2-93 3.99e-33

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: 120.84  E-value: 3.99e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963735   2 QVWYIQDLQRQPVHPKYYGQLCSGNCYLVLYTYQKLGCVQYLLYLWQGHQSTVEDTKALNCSAEELDLMHQGALAQGHVT 81
Cdd:cd11293   10 EVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQGGGKEEHILYFWQGRHSSQDERAAAALLTVELDEELKGRAVQVRVV 89
                         90
                 ....*....|..
gi 568963735  82 MGSEPPHFLAIF 93
Cdd:cd11293   90 QGKEPPHFLALF 101
VHP super family cl02491
Villin headpiece domain;
438-458 1.41e-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: 1.41e-05
                          10        20
                  ....*....|....*....|.
gi 568963735  438 YLSDSDFQDIFGKSKEEFYSM 458
Cdd:pfam02209   1 YLSDEDFEEVFGMSREEFYKL 21
 
Name Accession Description Interval E-value
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
219-321 1.77e-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: 132.42  E-value: 1.77e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963735 219 QPRLFECSSHAGCLVLTEVLFFGQEDLDKYDIMLLDTCQEassvaqIFLWLG-EAAGEWKKEAVAWGLEYLRTHPAERSL 297
Cdd:cd11291    1 KPRLFRCSNESGFFKVEEISDFSQDDLDTDDIMLLDTGDE------VFVWVGsESSDEEKKEALTSAKKYIETDPLGRSK 74
                         90       100
                 ....*....|....*....|....*
gi 568963735 298 -ATPIFVVKQGHEPATFTGWFVTWD 321
Cdd:cd11291   75 pRTPIYLVKQGNEPPTFTGYFHAWD 99
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
116-204 2.80e-34

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: 2.80e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963735 116 TRLFHVQGTESHNTRTMEVPARASSLTSGDVFFLITSHVCYLWFGKGCHGDQREMARTVVSV-FPGNNKETVLEGQEPLY 194
Cdd:cd11288    3 TRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVASFlKPKASLQEVAEGSEPDE 82
                         90
                 ....*....|
gi 568963735 195 FWEALGGRAP 204
Cdd:cd11288   83 FWEALGGKSE 92
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
2-93 3.99e-33

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: 120.84  E-value: 3.99e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963735   2 QVWYIQDLQRQPVHPKYYGQLCSGNCYLVLYTYQKLGCVQYLLYLWQGHQSTVEDTKALNCSAEELDLMHQGALAQGHVT 81
Cdd:cd11293   10 EVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQGGGKEEHILYFWQGRHSSQDERAAAALLTVELDEELKGRAVQVRVV 89
                         90
                 ....*....|..
gi 568963735  82 MGSEPPHFLAIF 93
Cdd:cd11293   90 QGKEPPHFLALF 101
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
119-201 1.53e-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: 1.53e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963735   119 FHVQGTESHNTRTMEVPARASSLTSGDVFFLITSHVCYLWFGKGCHGDQREMARTVVSVFPGNNK------ETVLEGQEP 192
Cdd:smart00262   1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGpgpvqvRVVDEGKEP 80

                   ....*....
gi 568963735   193 LYFWEALGG 201
Cdd:smart00262  81 PEFWSLFGG 89
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
2-95 3.45e-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: 65.01  E-value: 3.45e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963735     2 QVWYIQDLQRQPVH--PKYYGQLCSGNCYLVLYTYQklgcvqylLYLWQGHQSTVEDTKALNCSAEELDLMHQGALAQGH 79
Cdd:smart00262   1 FLVRVKGKRNVRVPevPFSQGSLNSGDCYILDTGSE--------IYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVR 72
                           90
                   ....*....|....*..
gi 568963735    80 -VTMGSEPPHFLAIFQG 95
Cdd:smart00262  73 vVDEGKEPPEFWSLFGG 89
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
240-320 3.38e-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: 59.23  E-value: 3.38e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963735   240 FGQEDLDKYDIMLLDTCQEassvaqIFLWLG-EAAGEWKKEAVAWGLEYLRThpaERSLATPIFVVKQGHEPATFTGWFV 318
Cdd:smart00262  18 FSQGSLNSGDCYILDTGSE------IYVWVGkKSSQDEKKKAAELAVELDDT---LGPGPVQVRVVDEGKEPPEFWSLFG 88

                   ..
gi 568963735   319 TW 320
Cdd:smart00262  89 GW 90
Gelsolin pfam00626
Gelsolin repeat;
13-90 1.23e-05

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 43.07  E-value: 1.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963735   13 PVHPKYYGQLCSGNCYLVLYTYQklgcvqylLYLWQG-HQSTVEDTKALNcSAEELDLMHQGALAQGHV-TMGSEPPHFL 90
Cdd:pfam00626   6 PPVPLSQESLNSGDCYLLDNGFT--------IFLWVGkGSSLLEKLFAAL-LAAQLDDDERFPLPEVIRvPQGKEPARFL 76
VHP pfam02209
Villin headpiece domain;
438-458 1.41e-05

Villin headpiece domain;


Pssm-ID: 460493  Cd Length: 36  Bit Score: 41.98  E-value: 1.41e-05
                          10        20
                  ....*....|....*....|.
gi 568963735  438 YLSDSDFQDIFGKSKEEFYSM 458
Cdd:pfam02209   1 YLSDEDFEEVFGMSREEFYKL 21
VHP smart00153
Villin headpiece domain;
438-458 1.93e-05

Villin headpiece domain;


Pssm-ID: 128458  Cd Length: 36  Bit Score: 41.54  E-value: 1.93e-05
                           10        20
                   ....*....|....*....|.
gi 568963735   438 YLSDSDFQDIFGKSKEEFYSM 458
Cdd:smart00153   1 YLSDEDFEEVFGMTREEFYKL 21
Gelsolin pfam00626
Gelsolin repeat;
233-313 2.71e-04

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 39.21  E-value: 2.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963735  233 VLTEVLFFGQEDLDKYDIMLLDTCQeassvaQIFLWLGEAAGEwkKEAVAWGLEYLRTHPAERSLATPIFVVKQGHEPAT 312
Cdd:pfam00626   3 VLPPPVPLSQESLNSGDCYLLDNGF------TIFLWVGKGSSL--LEKLFAALLAAQLDDDERFPLPEVIRVPQGKEPAR 74

                  .
gi 568963735  313 F 313
Cdd:pfam00626  75 F 75
Gelsolin pfam00626
Gelsolin repeat;
133-196 6.21e-03

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 35.75  E-value: 6.21e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963735  133 EVPARASSLTSGDVFFLITSHVCYLWFGKGCHGDQREMARTVVSVFPGNNK------ETVLEGQEPLYFW 196
Cdd:pfam00626   7 PVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDERfplpevIRVPQGKEPARFL 76
 
Name Accession Description Interval E-value
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
219-321 1.77e-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: 132.42  E-value: 1.77e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963735 219 QPRLFECSSHAGCLVLTEVLFFGQEDLDKYDIMLLDTCQEassvaqIFLWLG-EAAGEWKKEAVAWGLEYLRTHPAERSL 297
Cdd:cd11291    1 KPRLFRCSNESGFFKVEEISDFSQDDLDTDDIMLLDTGDE------VFVWVGsESSDEEKKEALTSAKKYIETDPLGRSK 74
                         90       100
                 ....*....|....*....|....*
gi 568963735 298 -ATPIFVVKQGHEPATFTGWFVTWD 321
Cdd:cd11291   75 pRTPIYLVKQGNEPPTFTGYFHAWD 99
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
116-204 2.80e-34

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: 2.80e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963735 116 TRLFHVQGTESHNTRTMEVPARASSLTSGDVFFLITSHVCYLWFGKGCHGDQREMARTVVSV-FPGNNKETVLEGQEPLY 194
Cdd:cd11288    3 TRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVASFlKPKASLQEVAEGSEPDE 82
                         90
                 ....*....|
gi 568963735 195 FWEALGGRAP 204
Cdd:cd11288   83 FWEALGGKSE 92
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
2-93 3.99e-33

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: 120.84  E-value: 3.99e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963735   2 QVWYIQDLQRQPVHPKYYGQLCSGNCYLVLYTYQKLGCVQYLLYLWQGHQSTVEDTKALNCSAEELDLMHQGALAQGHVT 81
Cdd:cd11293   10 EVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQGGGKEEHILYFWQGRHSSQDERAAAALLTVELDEELKGRAVQVRVV 89
                         90
                 ....*....|..
gi 568963735  82 MGSEPPHFLAIF 93
Cdd:cd11293   90 QGKEPPHFLALF 101
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
119-201 1.53e-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: 1.53e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963735   119 FHVQGTESHNTRTMEVPARASSLTSGDVFFLITSHVCYLWFGKGCHGDQREMARTVVSVFPGNNK------ETVLEGQEP 192
Cdd:smart00262   1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGpgpvqvRVVDEGKEP 80

                   ....*....
gi 568963735   193 LYFWEALGG 201
Cdd:smart00262  81 PEFWSLFGG 89
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
2-95 3.45e-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: 65.01  E-value: 3.45e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963735     2 QVWYIQDLQRQPVH--PKYYGQLCSGNCYLVLYTYQklgcvqylLYLWQGHQSTVEDTKALNCSAEELDLMHQGALAQGH 79
Cdd:smart00262   1 FLVRVKGKRNVRVPevPFSQGSLNSGDCYILDTGSE--------IYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVR 72
                           90
                   ....*....|....*..
gi 568963735    80 -VTMGSEPPHFLAIFQG 95
Cdd:smart00262  73 vVDEGKEPPEFWSLFGG 89
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
240-320 3.38e-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: 59.23  E-value: 3.38e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963735   240 FGQEDLDKYDIMLLDTCQEassvaqIFLWLG-EAAGEWKKEAVAWGLEYLRThpaERSLATPIFVVKQGHEPATFTGWFV 318
Cdd:smart00262  18 FSQGSLNSGDCYILDTGSE------IYVWVGkKSSQDEKKKAAELAVELDDT---LGPGPVQVRVVDEGKEPPEFWSLFG 88

                   ..
gi 568963735   319 TW 320
Cdd:smart00262  89 GW 90
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
217-317 1.17e-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: 1.17e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963735 217 SIQPRLFECSSHAGCLVLTEVL--FFGQEDLDKYDIMLLDTcqeassVAQIFLWLG-EAAGEWKKEAVAWGLEYLRTHpa 293
Cdd:cd11292    1 AEQKKLYKVSDASGKLKLTEVAegSLNQEMLDSEDCYILDC------GSEIFVWVGkGASLDERKAALKNAEEFLRKK-- 72
                         90       100
                 ....*....|....*....|....
gi 568963735 294 ERSLATPIFVVKQGHEPATFTGWF 317
Cdd:cd11292   73 KRPPYTQVTRVTEGGESALFKSKF 96
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
115-200 1.33e-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: 1.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963735 115 DTRLFHVQGTEshNTRTMEVPARASSLTSGDVFFLITSHVCYLWFGKGCH--------------GDQREMARTVVSVFpg 180
Cdd:cd11289    1 KPRLLHVKGRR--NVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNrfekakamqlaqgiRDERRLGRAKVIVL-- 76
                         90       100
                 ....*....|....*....|
gi 568963735 181 nnkeTVLEGQEPLYFWEALG 200
Cdd:cd11289   77 ----DEGDTNESPEFWKVLG 92
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
115-199 6.99e-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: 50.06  E-value: 6.99e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963735 115 DTRLFHVQGteSHNTRTMEVPARASSLTSGDVF-FLITSHVcYLWFGKGCHGDQREMARTVVSVF---PGNNKETVL--E 188
Cdd:cd11280    1 PPRLYRVRG--SKAIEIEEVPLASSSLDSDDVFvLDTGSEI-YIWQGRASSQAELAAAALLAKELdeeRKGKPEIVRirQ 77
                         90
                 ....*....|.
gi 568963735 189 GQEPLYFWEAL 199
Cdd:cd11280   78 GQEPREFWSLF 88
gelsolin_S1_like cd11290
Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; ...
1-93 2.16e-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: 49.14  E-value: 2.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963735   1 MQVWYIQDLQRQPVHPKYYGQLCSGNCYLVLYTYQ-KLGCVQYLLYLWQGHQSTVEDTKALNCSAEELDLMHQGALAQGH 79
Cdd:cd11290   10 LQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLdPSGSLSYDIHYWLGKEASQDEAGAAAIKAVELDDYLGGRPVQHR 89
                         90
                 ....*....|....
gi 568963735  80 VTMGSEPPHFLAIF 93
Cdd:cd11290   90 EVQGHESEEFLSYF 103
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
219-317 1.11e-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: 46.59  E-value: 1.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963735 219 QPRLFECSShAGCLVLTEVLFFGqEDLDKYDIMLLDTCQEassvaqIFLWLGEAAGEWKKEAVAWGLEYLRthpAERSLA 298
Cdd:cd11280    1 PPRLYRVRG-SKAIEIEEVPLAS-SSLDSDDVFVLDTGSE------IYIWQGRASSQAELAAAALLAKELD---EERKGK 69
                         90
                 ....*....|....*....
gi 568963735 299 TPIFVVKQGHEPATFTGWF 317
Cdd:cd11280   70 PEIVRIRQGQEPREFWSLF 88
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
1-93 3.76e-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: 45.05  E-value: 3.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963735   1 MQVWYIQDLQRQPVhPKYYGQLCSGNCYLVLYtyqklgcvQYLLYLWQGHQSTVEDTKALNCSAEELDLMHQGALAQGHV 80
Cdd:cd11280    5 YRVRGSKAIEIEEV-PLASSSLDSDDVFVLDT--------GSEIYIWQGRASSQAELAAAALLAKELDEERKGKPEIVRI 75
                         90
                 ....*....|...
gi 568963735  81 TMGSEPPHFLAIF 93
Cdd:cd11280   76 RQGQEPREFWSLF 88
Gelsolin pfam00626
Gelsolin repeat;
13-90 1.23e-05

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 43.07  E-value: 1.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963735   13 PVHPKYYGQLCSGNCYLVLYTYQklgcvqylLYLWQG-HQSTVEDTKALNcSAEELDLMHQGALAQGHV-TMGSEPPHFL 90
Cdd:pfam00626   6 PPVPLSQESLNSGDCYLLDNGFT--------IFLWVGkGSSLLEKLFAAL-LAAQLDDDERFPLPEVIRvPQGKEPARFL 76
VHP pfam02209
Villin headpiece domain;
438-458 1.41e-05

Villin headpiece domain;


Pssm-ID: 460493  Cd Length: 36  Bit Score: 41.98  E-value: 1.41e-05
                          10        20
                  ....*....|....*....|.
gi 568963735  438 YLSDSDFQDIFGKSKEEFYSM 458
Cdd:pfam02209   1 YLSDEDFEEVFGMSREEFYKL 21
VHP smart00153
Villin headpiece domain;
438-458 1.93e-05

Villin headpiece domain;


Pssm-ID: 128458  Cd Length: 36  Bit Score: 41.54  E-value: 1.93e-05
                           10        20
                   ....*....|....*....|.
gi 568963735   438 YLSDSDFQDIFGKSKEEFYSM 458
Cdd:smart00153   1 YLSDEDFEEVFGMTREEFYKL 21
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
113-195 3.82e-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: 3.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963735 113 VSDTRLFHVQ-GTESHNTRTMEV-PARASSLTSGDVFFLITSHVCYLWFGKGCHGDQREMARTVVSVFPGNNK------- 183
Cdd:cd11292    1 AEQKKLYKVSdASGKLKLTEVAEgSLNQEMLDSEDCYILDCGSEIFVWVGKGASLDERKAALKNAEEFLRKKKrppytqv 80
                         90
                 ....*....|..
gi 568963735 184 ETVLEGQEPLYF 195
Cdd:cd11292   81 TRVTEGGESALF 92
Gelsolin pfam00626
Gelsolin repeat;
233-313 2.71e-04

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 39.21  E-value: 2.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963735  233 VLTEVLFFGQEDLDKYDIMLLDTCQeassvaQIFLWLGEAAGEwkKEAVAWGLEYLRTHPAERSLATPIFVVKQGHEPAT 312
Cdd:pfam00626   3 VLPPPVPLSQESLNSGDCYLLDNGF------TIFLWVGKGSSL--LEKLFAALLAAQLDDDERFPLPEVIRVPQGKEPAR 74

                  .
gi 568963735  313 F 313
Cdd:pfam00626  75 F 75
Gelsolin pfam00626
Gelsolin repeat;
133-196 6.21e-03

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 35.75  E-value: 6.21e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963735  133 EVPARASSLTSGDVFFLITSHVCYLWFGKGCHGDQREMARTVVSVFPGNNK------ETVLEGQEPLYFW 196
Cdd:pfam00626   7 PVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDERfplpevIRVPQGKEPARFL 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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