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Conserved domains on  [gi|371502127|ref|NP_001243069|]
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macrophage-capping protein isoform 2 [Homo sapiens]

Protein Classification

gelsolin family protein( domain architecture ID 10181753)

gelsolin family protein, similar to Homo sapiens macrophage-capping protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
gelsolin_S1_like cd11290
Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; ...
17-120 8.61e-51

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: 164.32  E-value: 8.61e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371502127  17 QDPGLHVWRVEKLKPVPVAQENQGVFFSGDSYLVLHNGPEE----VSHLHLWIGQQSSRDEQGACAVLAVHLNTLLGERP 92
Cdd:cd11290    6 QKPGLQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDPsgslSYDIHYWLGKEASQDEAGAAAIKAVELDDYLGGRP 85
                         90       100
                 ....*....|....*....|....*...
gi 371502127  93 VQHREVQGNESDLFMSYFPRGLKYQEGG 120
Cdd:cd11290   86 VQHREVQGHESEEFLSYFKKGIIYIEGG 113
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
236-331 4.92e-39

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: 133.53  E-value: 4.92e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371502127 236 LYKVSDATGQMNLTKVADSsPFALELLISDDCFVLDNGlcGKIYIWKGRKANEKERQAALQVAEGFISRMQYAPNTQVEI 315
Cdd:cd11292    6 LYKVSDASGKLKLTEVAEG-SLNQEMLDSEDCYILDCG--SEIFVWVGKGASLDERKAALKNAEEFLRKKKRPPYTQVTR 82
                         90
                 ....*....|....*.
gi 371502127 316 LPQGHESPIFKQFFKD 331
Cdd:cd11292   83 VTEGGESALFKSKFAN 98
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
137-208 5.59e-36

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


:

Pssm-ID: 200445  Cd Length: 92  Bit Score: 125.43  E-value: 5.59e-36
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 371502127 137 KKLYQVKGKKNIRATERALNWDSFNTGDCFILDLGQNIFAWCGGKSNILERNKARDLALAIRDSERQGKAQV 208
Cdd:cd11289    2 PRLLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKV 73
 
Name Accession Description Interval E-value
gelsolin_S1_like cd11290
Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; ...
17-120 8.61e-51

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: 164.32  E-value: 8.61e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371502127  17 QDPGLHVWRVEKLKPVPVAQENQGVFFSGDSYLVLHNGPEE----VSHLHLWIGQQSSRDEQGACAVLAVHLNTLLGERP 92
Cdd:cd11290    6 QKPGLQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDPsgslSYDIHYWLGKEASQDEAGAAAIKAVELDDYLGGRP 85
                         90       100
                 ....*....|....*....|....*...
gi 371502127  93 VQHREVQGNESDLFMSYFPRGLKYQEGG 120
Cdd:cd11290   86 VQHREVQGHESEEFLSYFKKGIIYIEGG 113
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
236-331 4.92e-39

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: 133.53  E-value: 4.92e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371502127 236 LYKVSDATGQMNLTKVADSsPFALELLISDDCFVLDNGlcGKIYIWKGRKANEKERQAALQVAEGFISRMQYAPNTQVEI 315
Cdd:cd11292    6 LYKVSDASGKLKLTEVAEG-SLNQEMLDSEDCYILDCG--SEIFVWVGKGASLDERKAALKNAEEFLRKKKRPPYTQVTR 82
                         90
                 ....*....|....*.
gi 371502127 316 LPQGHESPIFKQFFKD 331
Cdd:cd11292   83 VTEGGESALFKSKFAN 98
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
137-208 5.59e-36

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


Pssm-ID: 200445  Cd Length: 92  Bit Score: 125.43  E-value: 5.59e-36
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 371502127 137 KKLYQVKGKKNIRATERALNWDSFNTGDCFILDLGQNIFAWCGGKSNILERNKARDLALAIRDSERQGKAQV 208
Cdd:cd11289    2 PRLLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKV 73
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
251-332 7.24e-23

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: 7.24e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371502127   251 VADSSPFALELLISDDCFVLDNGlcGKIYIWKGRKANEKERQAALQVAEGFISRMQyAPNTQVEILPQGHESPIFKQFFK 330
Cdd:smart00262  12 RVPEVPFSQGSLNSGDCYILDTG--SEIYVWVGKKSSQDEKKKAAELAVELDDTLG-PGPVQVRVVDEGKEPPEFWSLFG 88

                   ..
gi 371502127   331 DW 332
Cdd:smart00262  89 GW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
138-208 2.20e-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: 89.27  E-value: 2.20e-22
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 371502127   138 KLYQVKGKKNIRATERALNWDSFNTGDCFILDLGQNIFAWCGGKSNILERNKARDLALAIRDSERQGKAQV 208
Cdd:smart00262   1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQV 71
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
22-111 7.29e-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: 88.12  E-value: 7.29e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371502127    22 HVWRVEKLKPVPVAQEN--QGVFFSGDSYLVLHNgpeevSHLHLWIGQQSSRDEQGACAVLAVHLNTLLGERPVQHREV- 98
Cdd:smart00262   1 FLVRVKGKRNVRVPEVPfsQGSLNSGDCYILDTG-----SEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVRVVd 75
                           90
                   ....*....|...
gi 371502127    99 QGNESDLFMSYFP 111
Cdd:smart00262  76 EGKEPPEFWSLFG 88
Gelsolin pfam00626
Gelsolin repeat;
146-208 2.25e-16

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 72.73  E-value: 2.25e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 371502127  146 KNIRATERALNWDSFNTGDCFILDLGQNIFAWCGGKSNILERNKARDLALAIRDSERQGKAQV 208
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDERFPLPEV 63
Gelsolin pfam00626
Gelsolin repeat;
28-107 5.40e-15

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 68.87  E-value: 5.40e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371502127   28 KLKPVPVAQENQGVFFSGDSYLVLHNgpeevSHLHLWIGQQSSRDEQGACAVLAVHLNTL-LGERPVQHREVQGNESDLF 106
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNG-----FTIFLWVGKGSSLLEKLFAALLAAQLDDDeRFPLPEVIRVPQGKEPARF 75

                  .
gi 371502127  107 M 107
Cdd:pfam00626  76 L 76
Gelsolin pfam00626
Gelsolin repeat;
249-326 2.05e-14

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 67.33  E-value: 2.05e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 371502127  249 TKVADSSPFALELLISDDCFVLDNGLcgKIYIWKGRKANEKERQAALQVAEGfISRMQYAPNTQVEILPQGHESPIFK 326
Cdd:pfam00626   2 FVLPPPVPLSQESLNSGDCYLLDNGF--TIFLWVGKGSSLLEKLFAALLAAQ-LDDDERFPLPEVIRVPQGKEPARFL 76
 
Name Accession Description Interval E-value
gelsolin_S1_like cd11290
Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; ...
17-120 8.61e-51

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: 164.32  E-value: 8.61e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371502127  17 QDPGLHVWRVEKLKPVPVAQENQGVFFSGDSYLVLHNGPEE----VSHLHLWIGQQSSRDEQGACAVLAVHLNTLLGERP 92
Cdd:cd11290    6 QKPGLQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDPsgslSYDIHYWLGKEASQDEAGAAAIKAVELDDYLGGRP 85
                         90       100
                 ....*....|....*....|....*...
gi 371502127  93 VQHREVQGNESDLFMSYFPRGLKYQEGG 120
Cdd:cd11290   86 VQHREVQGHESEEFLSYFKKGIIYIEGG 113
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
236-331 4.92e-39

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: 133.53  E-value: 4.92e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371502127 236 LYKVSDATGQMNLTKVADSsPFALELLISDDCFVLDNGlcGKIYIWKGRKANEKERQAALQVAEGFISRMQYAPNTQVEI 315
Cdd:cd11292    6 LYKVSDASGKLKLTEVAEG-SLNQEMLDSEDCYILDCG--SEIFVWVGKGASLDERKAALKNAEEFLRKKKRPPYTQVTR 82
                         90
                 ....*....|....*.
gi 371502127 316 LPQGHESPIFKQFFKD 331
Cdd:cd11292   83 VTEGGESALFKSKFAN 98
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
137-208 5.59e-36

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


Pssm-ID: 200445  Cd Length: 92  Bit Score: 125.43  E-value: 5.59e-36
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 371502127 137 KKLYQVKGKKNIRATERALNWDSFNTGDCFILDLGQNIFAWCGGKSNILERNKARDLALAIRDSERQGKAQV 208
Cdd:cd11289    2 PRLLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKV 73
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
251-332 7.24e-23

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: 7.24e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371502127   251 VADSSPFALELLISDDCFVLDNGlcGKIYIWKGRKANEKERQAALQVAEGFISRMQyAPNTQVEILPQGHESPIFKQFFK 330
Cdd:smart00262  12 RVPEVPFSQGSLNSGDCYILDTG--SEIYVWVGKKSSQDEKKKAAELAVELDDTLG-PGPVQVRVVDEGKEPPEFWSLFG 88

                   ..
gi 371502127   331 DW 332
Cdd:smart00262  89 GW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
138-208 2.20e-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: 89.27  E-value: 2.20e-22
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 371502127   138 KLYQVKGKKNIRATERALNWDSFNTGDCFILDLGQNIFAWCGGKSNILERNKARDLALAIRDSERQGKAQV 208
Cdd:smart00262   1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQV 71
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
22-111 7.29e-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: 88.12  E-value: 7.29e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371502127    22 HVWRVEKLKPVPVAQEN--QGVFFSGDSYLVLHNgpeevSHLHLWIGQQSSRDEQGACAVLAVHLNTLLGERPVQHREV- 98
Cdd:smart00262   1 FLVRVKGKRNVRVPEVPfsQGSLNSGDCYILDTG-----SEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVRVVd 75
                           90
                   ....*....|...
gi 371502127    99 QGNESDLFMSYFP 111
Cdd:smart00262  76 EGKEPPEFWSLFG 88
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
14-110 1.00e-21

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: 88.10  E-value: 1.00e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371502127  14 GSVQdpglhVWRVEKLKPVPVAQENQGVFFSGDSYLVLHN---GPEEVSHLHLWIGQQSSRDEQGACAVLAVHLNTLLGE 90
Cdd:cd11293    7 GKVE-----VWRIENDEKVPVPKEEYGQFYGGDCYIVLYTyqgGGKEEHILYFWQGRHSSQDERAAAALLTVELDEELKG 81
                         90       100
                 ....*....|....*....|
gi 371502127  91 RPVQHREVQGNESDLFMSYF 110
Cdd:cd11293   82 RAVQVRVVQGKEPPHFLALF 101
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
236-329 7.72e-21

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: 85.11  E-value: 7.72e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371502127 236 LYKVSDATgQMNLTKVADSSpfalELLISDDCFVLDNGLcgKIYIWKGRKANEKERQAALQVAEGFISRmqYAPNTQVEI 315
Cdd:cd11280    4 LYRVRGSK-AIEIEEVPLAS----SSLDSDDVFVLDTGS--EIYIWQGRASSQAELAAAALLAKELDEE--RKGKPEIVR 74
                         90
                 ....*....|....
gi 371502127 316 LPQGHESPIFKQFF 329
Cdd:cd11280   75 IRQGQEPREFWSLF 88
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
22-110 2.62e-19

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: 81.26  E-value: 2.62e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371502127  22 HVWRVEKLK---PVPVAQENQgVFFSGDSYLVLHNgpeevSHLHLWIGQQSSRDEQGACAVLAVHLNTLLGERPVQHREV 98
Cdd:cd11280    3 RLYRVRGSKaieIEEVPLASS-SLDSDDVFVLDTG-----SEIYIWQGRASSQAELAAAALLAKELDEERKGKPEIVRIR 76
                         90
                 ....*....|..
gi 371502127  99 QGNESDLFMSYF 110
Cdd:cd11280   77 QGQEPREFWSLF 88
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
236-333 2.47e-17

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: 76.18  E-value: 2.47e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371502127 236 LYKVSDATGqmnLTKVADSSPFALELLISDDCFVLDNGlcGKIYIWKGRKANEKERQAALQVAEGFISRM---QYAPNTQ 312
Cdd:cd11291    4 LFRCSNESG---FFKVEEISDFSQDDLDTDDIMLLDTG--DEVFVWVGSESSDEEKKEALTSAKKYIETDplgRSKPRTP 78
                         90       100
                 ....*....|....*....|.
gi 371502127 313 VEILPQGHESPIFKQFFKDWK 333
Cdd:cd11291   79 IYLVKQGNEPPTFTGYFHAWD 99
Gelsolin pfam00626
Gelsolin repeat;
146-208 2.25e-16

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 72.73  E-value: 2.25e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 371502127  146 KNIRATERALNWDSFNTGDCFILDLGQNIFAWCGGKSNILERNKARDLALAIRDSERQGKAQV 208
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDERFPLPEV 63
Gelsolin pfam00626
Gelsolin repeat;
28-107 5.40e-15

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 68.87  E-value: 5.40e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371502127   28 KLKPVPVAQENQGVFFSGDSYLVLHNgpeevSHLHLWIGQQSSRDEQGACAVLAVHLNTL-LGERPVQHREVQGNESDLF 106
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNG-----FTIFLWVGKGSSLLEKLFAALLAAQLDDDeRFPLPEVIRVPQGKEPARF 75

                  .
gi 371502127  107 M 107
Cdd:pfam00626  76 L 76
Gelsolin pfam00626
Gelsolin repeat;
249-326 2.05e-14

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 67.33  E-value: 2.05e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 371502127  249 TKVADSSPFALELLISDDCFVLDNGLcgKIYIWKGRKANEKERQAALQVAEGfISRMQYAPNTQVEILPQGHESPIFK 326
Cdd:pfam00626   2 FVLPPPVPLSQESLNSGDCYLLDNGF--TIFLWVGKGSSLLEKLFAALLAAQ-LDDDERFPLPEVIRVPQGKEPARFL 76
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
139-209 4.50e-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: 58.53  E-value: 4.50e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 371502127 139 LYQVKGKKNIRATERALNWDSFNTGDCFILDLGQNIFAWCGGKSNILERNKARDLALAIrDSERQGKAQVL 209
Cdd:cd11280    4 LYRVRGSKAIEIEEVPLASSSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKEL-DEERKGKPEIV 73
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
261-325 7.48e-08

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: 49.54  E-value: 7.48e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 371502127 261 LLISDDCFVLDNGlcGKIYIWKGRKANEKERQAALQVAEgFISrmqyaPNTQVEILPQGHESPIF 325
Cdd:cd11288   27 SLNSNDVFVLKTP--SSVYLWVGKGSSEDERELAKDVAS-FLK-----PKASLQEVAEGSEPDEF 83
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
138-194 3.80e-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: 47.61  E-value: 3.80e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 371502127 138 KLYQVKG--KKNIRATERALNWDSFNTGDCFILDLGQNIFAWCGGKSNILERNKARDLA 194
Cdd:cd11288    4 RLFQVRGngSGNTRAVEVDADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVA 62
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
158-195 2.30e-04

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: 39.59  E-value: 2.30e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 371502127 158 DSFNTGDCFILDLGQNIFAWCGGKSNILERNKARDLAL 195
Cdd:cd11291   25 DDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAK 62
 
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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