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Conserved domains on  [gi|14916473|ref|NP_149119|]
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scinderin isoform 2 [Homo sapiens]

Protein Classification

gelsolin/scinderin family protein( domain architecture ID 10181863)

gelsolin/scinderin family protein similar to portion of Homo sapiens gelsolin, a calcium-regulated, actin-modulating protein that binds to the plus (or barbed) ends of actin monomers or filaments, preventing monomer exchange (end-blocking or capping), and to portion of Homo sapiens scinderin, a Ca(2+)-dependent actin filament-severing protein that has a regulatory function in exocytosis by affecting the organization of the microfilament network underneath the plasma membrane

CATH:  3.40.20.10
Gene Ontology:  GO:0051015
PubMed:  14527663|15526166
SCOP:  4001825

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; ...
 366-464 3.66e-54

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: 176.33  E-value: 3.66e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14916473 366 PPRLYGCSNKTGRFVIEEIPGeFTQDDLAEDDVMLLDAWEQIFIWIGKDANEVEKKESLKSAKMYLETDPSGRDK-RTPI 444
Cdd:cd11291   1 KPRLFRCSNESGFFKVEEISD-FSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYIETDPLGRSKpRTPI 79

                        90       100
                ....*....|....*....|
gi 14916473 445 VIIKQGHEPPTFTGWFLGWD 464
Cdd:cd11291  80 YLVKQGNEPPTFTGYFHAWD 99
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
 143-239 9.72e-47

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: 157.05  E-value: 9.72e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14916473 143 MVDDGSGKVEIWRVENNGRIQVDQNSYGEFYGGDCYIILYTYPRG----QIIYTWQGANATRDELTTSAFLTVQLDRSLG 218
Cdd:cd11293   1 MYDDGSGKVEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQGGgkeeHILYFWQGRHSSQDERAAAALLTVELDEELK 80

                        90       100
                ....*....|....*....|.
gi 14916473 219 GQAVQIRVSQGKEPVHLLSLF 239
Cdd:cd11293  81 GRAVQVRVVQGKEPPHFLALF 101
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 1-99 9.89e-43

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: 146.24  E-value: 9.89e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14916473   1 MAKLYMVSDASGSMRVTVVAEEnPFSMAMLLSEECFILDHGAakQIFVWKGKDANPQERKAAMKTAEEFLQQMNYSKNTQ 80
Cdd:cd11292   3 QKKLYKVSDASGKLKLTEVAEG-SLNQEMLDSEDCYILDCGS--EIFVWVGKGASLDERKAALKNAEEFLRKKKRPPYTQ 79

                        90
                ....*....|....*....
gi 14916473  81 IQVLPEGGETPIFKQFFKD 99
Cdd:cd11292  80 VTRVTEGGESALFKSKFAN 98
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 261-351 5.07e-42

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: 144.30  E-value: 5.07e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14916473 261 PPTRLFQVRRNLASITRIVEVDVDANSLNSNDVFVLKLPqNSGYIWVGKGASQEEEKGAEYVASVLK--CKTLRIQEGEE 338
Cdd:cd11288   1 SPTRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKTP-SSVYLWVGKGSSEDERELAKDVASFLKpkASLQEVAEGSE 79

                        90
                ....*....|...
gi 14916473 339 PEEFWNSLGGKKD 351
Cdd:cd11288  80 PDEFWEALGGKSE 92
 
Name Accession Description Interval E-value
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 366-464 3.66e-54

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: 176.33  E-value: 3.66e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14916473 366 PPRLYGCSNKTGRFVIEEIPGeFTQDDLAEDDVMLLDAWEQIFIWIGKDANEVEKKESLKSAKMYLETDPSGRDK-RTPI 444
Cdd:cd11291   1 KPRLFRCSNESGFFKVEEISD-FSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYIETDPLGRSKpRTPI 79

                        90       100
                ....*....|....*....|
gi 14916473 445 VIIKQGHEPPTFTGWFLGWD 464
Cdd:cd11291  80 YLVKQGNEPPTFTGYFHAWD 99
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
 143-239 9.72e-47

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: 157.05  E-value: 9.72e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14916473 143 MVDDGSGKVEIWRVENNGRIQVDQNSYGEFYGGDCYIILYTYPRG----QIIYTWQGANATRDELTTSAFLTVQLDRSLG 218
Cdd:cd11293   1 MYDDGSGKVEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQGGgkeeHILYFWQGRHSSQDERAAAALLTVELDEELK 80

                        90       100
                ....*....|....*....|.
gi 14916473 219 GQAVQIRVSQGKEPVHLLSLF 239
Cdd:cd11293  81 GRAVQVRVVQGKEPPHFLALF 101
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 1-99 9.89e-43

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: 146.24  E-value: 9.89e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14916473   1 MAKLYMVSDASGSMRVTVVAEEnPFSMAMLLSEECFILDHGAakQIFVWKGKDANPQERKAAMKTAEEFLQQMNYSKNTQ 80
Cdd:cd11292   3 QKKLYKVSDASGKLKLTEVAEG-SLNQEMLDSEDCYILDCGS--EIFVWVGKGASLDERKAALKNAEEFLRKKKRPPYTQ 79

                        90
                ....*....|....*....
gi 14916473  81 IQVLPEGGETPIFKQFFKD 99
Cdd:cd11292  80 VTRVTEGGESALFKSKFAN 98
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 261-351 5.07e-42

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: 144.30  E-value: 5.07e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14916473 261 PPTRLFQVRRNLASITRIVEVDVDANSLNSNDVFVLKLPqNSGYIWVGKGASQEEEKGAEYVASVLK--CKTLRIQEGEE 338
Cdd:cd11288   1 SPTRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKTP-SSVYLWVGKGSSEDERELAKDVASFLKpkASLQEVAEGSE 79

                        90
                ....*....|...
gi 14916473 339 PEEFWNSLGGKKD 351
Cdd:cd11288  80 PDEFWEALGGKSE 92
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 372-463 2.81e-26

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: 101.60  E-value: 2.81e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14916473    372 CSNKTGRFVIEEIPGEFTQDDLAEDDVMLLDAWEQIFIWIGKDANEVEKKESLKSAKMYLETDPSGrdkRTPIVIIKQGH 451
Cdd:smart00262   2 LVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPG---PVQVRVVDEGK 78

                           90
                   ....*....|..
gi 14916473    452 EPPTFTGWFLGW 463
Cdd:smart00262  79 EPPEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 12-100 3.61e-25

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: 98.90  E-value: 3.61e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14916473     12 GSMRVTVVAEENPFSMAMLLSEECFILDHGAakQIFVWKGKDANPQERKAAMKTAEEFLQQMNySKNTQIQVLPEGGETP 91
Cdd:smart00262   5 VKGKRNVRVPEVPFSQGSLNSGDCYILDTGS--EIYVWVGKKSSQDEKKKAAELAVELDDTLG-PGPVQVRVVDEGKEPP 81


                   ....*....
gi 14916473     92 IFKQFFKDW 100
Cdd:smart00262  82 EFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 152-242 2.66e-22

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 90.81  E-value: 2.66e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14916473    152 EIWRVENNGRIQVDQ--NSYGEFYGGDCYIILYtyprGQIIYTWQGANATRDELTTSAFLTVQLDRSLGGQAVQIR-VSQ 228
Cdd:smart00262   1 FLVRVKGKRNVRVPEvpFSQGSLNSGDCYILDT----GSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVRvVDE 76

                           90
                   ....*....|....
gi 14916473    229 GKEPVHLLSLFKDK 242
Cdd:smart00262  77 GKEPPEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 266-349 3.96e-21

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 87.35  E-value: 3.96e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14916473    266 FQVRRNLASITRIVEVDVDANSLNSNDVFVLKLPQNSgYIWVGKGASQEEEKGAEYVASVL-------KCKTLRIQEGEE 338
Cdd:smart00262   1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEI-YVWVGKKSSQDEKKKAAELAVELddtlgpgPVQVRVVDEGKE 79

                           90
                   ....*....|.
gi 14916473    339 PEEFWNSLGGK 349
Cdd:smart00262  80 PPEFWSLFGGW 90
Gelsolin pfam00626
Gelsolin repeat;
379-456 4.87e-15

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 70.03  E-value: 4.87e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14916473   379 FVIEEIPGEFTQDDLAEDDVMLLDAWEQIFIWIGKDANEVEKKESLKSAKMYLETDpsgRDKRTPIVIIKQGHEPPTF 456
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDE---RFPLPEVIRVPQGKEPARF 75
Gelsolin pfam00626
Gelsolin repeat;
16-94 3.00e-14

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 67.72  E-value: 3.00e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14916473    16 VTVVAEENPFSMAMLLSEECFILDHGaaKQIFVWKGKDANPQERKAAMKTAEEFLQQMnYSKNTQIQVLPEGGETPIFK 94
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNG--FTIFLWVGKGSSLLEKLFAALLAAQLDDDE-RFPLPEVIRVPQGKEPARFL 76
Gelsolin pfam00626
Gelsolin repeat;
163-236 2.58e-11

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 59.24  E-value: 2.58e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14916473   163 QVDQNSYGEFYGGDCYIILYtyprGQIIYTWQGANATRDELTTSAFLTVQLDRS-LGGQAVQIRVSQGKEPVHLL 236
Cdd:pfam00626   6 PPVPLSQESLNSGDCYLLDN----GFTIFLWVGKGSSLLEKLFAALLAAQLDDDeRFPLPEVIRVPQGKEPARFL 76
Gelsolin pfam00626
Gelsolin repeat;
279-343 3.77e-07

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 47.30  E-value: 3.77e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14916473   279 VEVDVDANSLNSNDVFVLKLPQNSgYIWVGKGASQEEEKGAEYVASVL-------KCKTLRIQEGEEPEEFW 343
Cdd:pfam00626   6 PPVPLSQESLNSGDCYLLDNGFTI-FLWVGKGSSLLEKLFAALLAAQLddderfpLPEVIRVPQGKEPARFL 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; ...
 366-464 3.66e-54

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: 176.33  E-value: 3.66e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14916473 366 PPRLYGCSNKTGRFVIEEIPGeFTQDDLAEDDVMLLDAWEQIFIWIGKDANEVEKKESLKSAKMYLETDPSGRDK-RTPI 444
Cdd:cd11291   1 KPRLFRCSNESGFFKVEEISD-FSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYIETDPLGRSKpRTPI 79

                        90       100
                ....*....|....*....|
gi 14916473 445 VIIKQGHEPPTFTGWFLGWD 464
Cdd:cd11291  80 YLVKQGNEPPTFTGYFHAWD 99
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
 143-239 9.72e-47

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: 157.05  E-value: 9.72e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14916473 143 MVDDGSGKVEIWRVENNGRIQVDQNSYGEFYGGDCYIILYTYPRG----QIIYTWQGANATRDELTTSAFLTVQLDRSLG 218
Cdd:cd11293   1 MYDDGSGKVEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQGGgkeeHILYFWQGRHSSQDERAAAALLTVELDEELK 80

                        90       100
                ....*....|....*....|.
gi 14916473 219 GQAVQIRVSQGKEPVHLLSLF 239
Cdd:cd11293  81 GRAVQVRVVQGKEPPHFLALF 101
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 1-99 9.89e-43

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: 146.24  E-value: 9.89e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14916473   1 MAKLYMVSDASGSMRVTVVAEEnPFSMAMLLSEECFILDHGAakQIFVWKGKDANPQERKAAMKTAEEFLQQMNYSKNTQ 80
Cdd:cd11292   3 QKKLYKVSDASGKLKLTEVAEG-SLNQEMLDSEDCYILDCGS--EIFVWVGKGASLDERKAALKNAEEFLRKKKRPPYTQ 79

                        90
                ....*....|....*....
gi 14916473  81 IQVLPEGGETPIFKQFFKD 99
Cdd:cd11292  80 VTRVTEGGESALFKSKFAN 98
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 261-351 5.07e-42

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: 144.30  E-value: 5.07e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14916473 261 PPTRLFQVRRNLASITRIVEVDVDANSLNSNDVFVLKLPqNSGYIWVGKGASQEEEKGAEYVASVLK--CKTLRIQEGEE 338
Cdd:cd11288   1 SPTRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKTP-SSVYLWVGKGSSEDERELAKDVASFLKpkASLQEVAEGSE 79

                        90
                ....*....|...
gi 14916473 339 PEEFWNSLGGKKD 351
Cdd:cd11288  80 PDEFWEALGGKSE 92
gelsolin_S1_like cd11290
Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; ...
 151-250 6.20e-28

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: 106.92  E-value: 6.20e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14916473 151 VEIWRVENNGRIQVDQNSYGEFYGGDCYIILYTYPRGQI-----IYTWQGANATRDELTTSAFLTVQLDRSLGGQAVQIR 225
Cdd:cd11290  10 LQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDPSGslsydIHYWLGKEASQDEAGAAAIKAVELDDYLGGRPVQHR 89

                        90       100
                ....*....|....*....|....*
gi 14916473 226 VSQGKEPVHLLSLFkdKPLIIYKNG 250
Cdd:cd11290  90 EVQGHESEEFLSYF--KKGIIYIEG 112
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 372-463 2.81e-26

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: 101.60  E-value: 2.81e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14916473    372 CSNKTGRFVIEEIPGEFTQDDLAEDDVMLLDAWEQIFIWIGKDANEVEKKESLKSAKMYLETDPSGrdkRTPIVIIKQGH 451
Cdd:smart00262   2 LVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPG---PVQVRVVDEGK 78

                           90
                   ....*....|..
gi 14916473    452 EPPTFTGWFLGW 463
Cdd:smart00262  79 EPPEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 12-100 3.61e-25

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: 98.90  E-value: 3.61e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14916473     12 GSMRVTVVAEENPFSMAMLLSEECFILDHGAakQIFVWKGKDANPQERKAAMKTAEEFLQQMNySKNTQIQVLPEGGETP 91
Cdd:smart00262   5 VKGKRNVRVPEVPFSQGSLNSGDCYILDTGS--EIYVWVGKKSSQDEKKKAAELAVELDDTLG-PGPVQVRVVDEGKEPP 81


                   ....*....
gi 14916473     92 IFKQFFKDW 100
Cdd:smart00262  82 EFWSLFGGW 90
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 366-460 8.16e-23

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: 92.05  E-value: 8.16e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14916473 366 PPRLYGCSNKTgRFVIEEIPGEFTqdDLAEDDVMLLDAWEQIFIWIGKDANEVEKKESLKSAKMYLETdpsgRDKRTPIV 445
Cdd:cd11280   1 PPRLYRVRGSK-AIEIEEVPLASS--SLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKELDEE----RKGKPEIV 73

                        90
                ....*....|....*
gi 14916473 446 IIKQGHEPPTFTGWF 460
Cdd:cd11280  74 RIRQGQEPREFWSLF 88
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 152-242 2.66e-22

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 90.81  E-value: 2.66e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14916473    152 EIWRVENNGRIQVDQ--NSYGEFYGGDCYIILYtyprGQIIYTWQGANATRDELTTSAFLTVQLDRSLGGQAVQIR-VSQ 228
Cdd:smart00262   1 FLVRVKGKRNVRVPEvpFSQGSLNSGDCYILDT----GSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVRvVDE 76

                           90
                   ....*....|....
gi 14916473    229 GKEPVHLLSLFKDK 242
Cdd:smart00262  77 GKEPPEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 266-349 3.96e-21

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 87.35  E-value: 3.96e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14916473    266 FQVRRNLASITRIVEVDVDANSLNSNDVFVLKLPQNSgYIWVGKGASQEEEKGAEYVASVL-------KCKTLRIQEGEE 338
Cdd:smart00262   1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEI-YVWVGKKSSQDEKKKAAELAVELddtlgpgPVQVRVVDEGKE 79

                           90
                   ....*....|.
gi 14916473    339 PEEFWNSLGGK 349
Cdd:smart00262  80 PPEFWSLFGGW 90
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 262-346 4.78e-20

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: 84.34  E-value: 4.78e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14916473 262 PTRLFQVRRNlaSITRIVEVDVDANSLNSNDVFVLKLpQNSGYIWVGKGASQEEEKGAEYVASVL------KCKTLRIQE 335
Cdd:cd11280   1 PPRLYRVRGS--KAIEIEEVPLASSSLDSDDVFVLDT-GSEIYIWQGRASSQAELAAAALLAKELdeerkgKPEIVRIRQ 77

                        90
                ....*....|.
gi 14916473 336 GEEPEEFWNSL 346
Cdd:cd11280  78 GQEPREFWSLF 88
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 367-460 1.58e-19

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: 83.07  E-value: 1.58e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14916473 367 PRLYGCSNKTGRFVIEEIP-GEFTQDDLAEDDVMLLDAWEQIFIWIGKDANEVEKKESLKSAKMYLETdpSGRDKRTPIV 445
Cdd:cd11292   4 KKLYKVSDASGKLKLTEVAeGSLNQEMLDSEDCYILDCGSEIFVWVGKGASLDERKAALKNAEEFLRK--KKRPPYTQVT 81

                        90
                ....*....|....*
gi 14916473 446 IIKQGHEPPTFTGWF 460
Cdd:cd11292  82 RVTEGGESALFKSKF 96
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 3-100 2.20e-18

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: 80.03  E-value: 2.20e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14916473   3 KLYMVSDASGsmrVTVVAEENPFSMAMLLSEECFILDHGaaKQIFVWKGKDANPQERKAAMKTAEEFLQQMNYSKN---T 79
Cdd:cd11291   3 RLFRCSNESG---FFKVEEISDFSQDDLDTDDIMLLDTG--DEVFVWVGSESSDEEKKEALTSAKKYIETDPLGRSkprT 77

                        90       100
                ....*....|....*....|.
gi 14916473  80 QIQVLPEGGETPIFKQFFKDW 100
Cdd:cd11291  78 PIYLVKQGNEPPTFTGYFHAW 98
Gelsolin pfam00626
Gelsolin repeat;
379-456 4.87e-15

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 70.03  E-value: 4.87e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14916473   379 FVIEEIPGEFTQDDLAEDDVMLLDAWEQIFIWIGKDANEVEKKESLKSAKMYLETDpsgRDKRTPIVIIKQGHEPPTF 456
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDE---RFPLPEVIRVPQGKEPARF 75
Gelsolin pfam00626
Gelsolin repeat;
16-94 3.00e-14

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 67.72  E-value: 3.00e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14916473    16 VTVVAEENPFSMAMLLSEECFILDHGaaKQIFVWKGKDANPQERKAAMKTAEEFLQQMnYSKNTQIQVLPEGGETPIFK 94
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNG--FTIFLWVGKGSSLLEKLFAALLAAQLDDDE-RFPLPEVIRVPQGKEPARFL 76
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 153-239 1.24e-12

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: 63.54  E-value: 1.24e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14916473 153 IWRVENNGRI---QVDQNSYgEFYGGDCYIILYtyprGQIIYTWQGANATRDELTTSAFLTVQLDRSLGGQAVQIRVSQG 229
Cdd:cd11280   4 LYRVRGSKAIeieEVPLASS-SLDSDDVFVLDT----GSEIYIWQGRASSQAELAAAALLAKELDEERKGKPEIVRIRQG 78

                        90
                ....*....|
gi 14916473 230 KEPVHLLSLF 239
Cdd:cd11280  79 QEPREFWSLF 88
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 262-347 6.57e-12

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: 61.48  E-value: 6.57e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14916473 262 PTRLFQV--RRNlasiTRIVEVDVDANSLNSNDVFVLKLPQNSgYIWVGKGASQEEE-KGAEYVASVL------KCKTLR 332
Cdd:cd11289   1 KPRLLHVkgRRN----VRAREVELSWSSLNSGDVFILDLGSTI-YQWNGSKSNRFEKaKAMQLAQGIRderrlgRAKVIV 75

                        90
                ....*....|....*..
gi 14916473 333 IQEGE--EPEEFWNSLG 347
Cdd:cd11289  76 LDEGDtnESPEFWKVLG 92
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 4-97 1.96e-11

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


Pssm-ID: 200436  Cd Length: 88  Bit Score: 60.07  E-value: 1.96e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14916473   4 LYMVSdASGSMRVtvvaEENPFSMAMLLSEECFILDHGAakQIFVWKGKDANPQERKAAMKTAEEFLQQmnYSKNTQIQV 83
Cdd:cd11280   4 LYRVR-GSKAIEI----EEVPLASSSLDSDDVFVLDTGS--EIYIWQGRASSQAELAAAALLAKELDEE--RKGKPEIVR 74

                        90
                ....*....|....
gi 14916473  84 LPEGGETPIFKQFF 97
Cdd:cd11280  75 IRQGQEPREFWSLF 88
Gelsolin pfam00626
Gelsolin repeat;
163-236 2.58e-11

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 59.24  E-value: 2.58e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14916473   163 QVDQNSYGEFYGGDCYIILYtyprGQIIYTWQGANATRDELTTSAFLTVQLDRS-LGGQAVQIRVSQGKEPVHLL 236
Cdd:pfam00626   6 PPVPLSQESLNSGDCYLLDN----GFTIFLWVGKGSSLLEKLFAALLAAQLDDDeRFPLPEVIRVPQGKEPARFL 76
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 15-99 9.40e-08

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: 49.54  E-value: 9.40e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14916473  15 RVTVVAEENPFSMAMLLSEECFILDHGaaKQIFVWKGKDANPQERKAAMktaeEFLQQMNYSKN---TQIQVLpEGGETP 91
Cdd:cd11289  10 RRNVRAREVELSWSSLNSGDVFILDLG--STIYQWNGSKSNRFEKAKAM----QLAQGIRDERRlgrAKVIVL-DEGDTN 82


                ....*...
gi 14916473  92 IFKQFFKD 99
Cdd:cd11289  83 ESPEFWKV 90
Gelsolin pfam00626
Gelsolin repeat;
279-343 3.77e-07

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 47.30  E-value: 3.77e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14916473   279 VEVDVDANSLNSNDVFVLKLPQNSgYIWVGKGASQEEEKGAEYVASVL-------KCKTLRIQEGEEPEEFW 343
Cdd:pfam00626   6 PPVPLSQESLNSGDCYLLDNGFTI-FLWVGKGSSLLEKLFAALLAAQLddderfpLPEVIRVPQGKEPARFL 76
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 22-93 9.08e-07

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: 46.84  E-value: 9.08e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14916473  22 ENPFSMAMLLSEECFILDHGaaKQIFVWKGKDANPQERKAAMKTAEeflqqmNYSKNTQIQVLPEGGETPIF 93
Cdd:cd11288  20 EVDADASSLNSNDVFVLKTP--SSVYLWVGKGSSEDERELAKDVAS------FLKPKASLQEVAEGSEPDEF 83
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 288-342 5.26e-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: 41.85  E-value: 5.26e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14916473 288 LNSNDVFVLKlpQNSG-YIWVGKGASQEEEKGA-----EYVASVLKCKTL---RIQEGEEPEEF 342
Cdd:cd11292  31 LDSEDCYILD--CGSEiFVWVGKGASLDERKAAlknaeEFLRKKKRPPYTqvtRVTEGGESALF 92
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 366-456 1.60e-03

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: 37.60  E-value: 1.60e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14916473 366 PPRLYGCSnktGRFVIEEIPGEFTQDDLAEDDVMLLDAWEQIFIWIGKDANEVEKKESLKSAKMYLETDPSGRDKrTPIV 445
Cdd:cd11289   1 KPRLLHVK---GRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAK-VIVL 76

                        90
                ....*....|.
gi 14916473 446 IIKQGHEPPTF 456
Cdd:cd11289  77 DEGDTNESPEF 87
 
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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