NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|674659523|gb|AIL27287|]
View 

gelsolin, partial [Susana annulata]

Protein Classification

gelsolin/scinderin family protein( domain architecture ID 10336928)

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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; ...
 167-259 1.11e-39

Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


:

Pssm-ID: 200447 [Multi-domain]  Cd Length: 99  Bit Score: 132.81  E-value: 1.11e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659523 167 YTRLFRCSNEKGYFtISEKCTDFCQDDLADDDIMVLDNGEQVFLWLGARCSEVEIKLAYKSAQVYIQHLRVKQPERPRKL 246
Cdd:cd11291    1 KPRLFRCSNESGFF-KVEEISDFSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYIETDPLGRSKPRTPI 79

                         90
                 ....*....|...
gi 674659523 247 FLTAKSKESRRFT 259
Cdd:cd11291   80 YLVKQGNEPPTFT 92
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 55-156 4.29e-33

Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


:

Pssm-ID: 200444  Cd Length: 92  Bit Score: 115.79  E-value: 4.29e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659523  55 NKVEFYHLRSNGSaLCTRLIQVNPDALLLNSAFCYILNVPFnnddesgIVYVWIGSQADPEEARLVEEIAEEMFnnPWIS 134
Cdd:cd11288    1 SPTRLFQVRGNGS-GNTRAVEVDADASSLNSNDVFVLKTPS-------SVYLWVGKGSSEDERELAKDVASFLK--PKAS 70

                         90       100
                 ....*....|....*....|..
gi 674659523 135 LQVLNEGEEPDNFFWVGIGGKK 156
Cdd:cd11288   71 LQEVAEGSEPDEFWEALGGKSE 92
ADF_gelsolin super family cl15697
Actin depolymerization factor/cofilin- and gelsolin-like domains; Actin depolymerization ...
 1-35 8.99e-06

Actin depolymerization factor/cofilin- and gelsolin-like domains; Actin depolymerization factor/cofilin-like domains are present in a family of essential eukaryotic actin regulatory proteins; these proteins enhance the turnover rate of actin and interact with actin monomers as well as actin filaments.


The actual alignment was detected with superfamily member cd11280:

Pssm-ID: 472830  Cd Length: 88  Bit Score: 43.13  E-value: 8.99e-06
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 674659523   1 FTFSLQKKFKSLFGEKLEVVRTHQQQENLKFMAHF 35
Cdd:cd11280   54 AAALLAKELDEERKGKPEIVRIRQGQEPREFWSLF 88
 
Name Accession Description Interval E-value
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 167-259 1.11e-39

Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200447 [Multi-domain]  Cd Length: 99  Bit Score: 132.81  E-value: 1.11e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659523 167 YTRLFRCSNEKGYFtISEKCTDFCQDDLADDDIMVLDNGEQVFLWLGARCSEVEIKLAYKSAQVYIQHLRVKQPERPRKL 246
Cdd:cd11291    1 KPRLFRCSNESGFF-KVEEISDFSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYIETDPLGRSKPRTPI 79

                         90
                 ....*....|...
gi 674659523 247 FLTAKSKESRRFT 259
Cdd:cd11291   80 YLVKQGNEPPTFT 92
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 55-156 4.29e-33

Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200444  Cd Length: 92  Bit Score: 115.79  E-value: 4.29e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659523  55 NKVEFYHLRSNGSaLCTRLIQVNPDALLLNSAFCYILNVPFnnddesgIVYVWIGSQADPEEARLVEEIAEEMFnnPWIS 134
Cdd:cd11288    1 SPTRLFQVRGNGS-GNTRAVEVDADASSLNSNDVFVLKTPS-------SVYLWVGKGSSEDERELAKDVASFLK--PKAS 70

                         90       100
                 ....*....|....*....|..
gi 674659523 135 LQVLNEGEEPDNFFWVGIGGKK 156
Cdd:cd11288   71 LQEVAEGSEPDEFWEALGGKSE 92
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 172-259 3.51e-17

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 74.25  E-value: 3.51e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659523   172 RCSNEKGYFTISEKCTDFCQDDLADDDIMVLDNGEQVFLWLGARCSEVEIKLAYKSAQVYIQHLRvkqpERPRKLFLTAK 251
Cdd:smart00262   1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLG----PGPVQVRVVDE 76


                   ....*...
gi 674659523   252 SKESRRFT 259
Cdd:smart00262  77 GKEPPEFW 84
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 60-154 8.58e-16

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: 70.40  E-value: 8.58e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659523    60 YHLRSNGSaLCTRLIQVNPDALLLNSAFCYILnvpfnndDESGIVYVWIGSQADPEEARLVEEIAEEMFNN---PWISLQ 136
Cdd:smart00262   1 FLVRVKGK-RNVRVPEVPFSQGSLNSGDCYIL-------DTGSEIYVWVGKKSSQDEKKKAAELAVELDDTlgpGPVQVR 72

                           90
                   ....*....|....*...
gi 674659523   137 VLNEGEEPDNFFWVGIGG 154
Cdd:smart00262  73 VVDEGKEPPEFWSLFGGW 90
Gelsolin pfam00626
Gelsolin repeat;
188-258 1.30e-10

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 56.16  E-value: 1.30e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 674659523  188 DFCQDDLADDDIMVLDNGEQVFLWLGARCSEVEIKLAYKSAQVYIQHLRVKQPErprkLFLTAKSKESRRF 258
Cdd:pfam00626   9 PLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDERFPLPE----VIRVPQGKEPARF 75
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 1-35 8.99e-06

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


Pssm-ID: 200436  Cd Length: 88  Bit Score: 43.13  E-value: 8.99e-06
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 674659523   1 FTFSLQKKFKSLFGEKLEVVRTHQQQENLKFMAHF 35
Cdd:cd11280   54 AAALLAKELDEERKGKPEIVRIRQGQEPREFWSLF 88
Gelsolin pfam00626
Gelsolin repeat;
76-147 1.48e-03

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 36.52  E-value: 1.48e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 674659523   76 VNPDALLLNSAFCYILnvpfnndDESGIVYVWIGSQADPEE---ARLVEEIAEEMFNNPWISLQVLNEGEEPDNF 147
Cdd:pfam00626   8 VPLSQESLNSGDCYLL-------DNGFTIFLWVGKGSSLLEklfAALLAAQLDDDERFPLPEVIRVPQGKEPARF 75
 
Name Accession Description Interval E-value
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 167-259 1.11e-39

Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200447 [Multi-domain]  Cd Length: 99  Bit Score: 132.81  E-value: 1.11e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659523 167 YTRLFRCSNEKGYFtISEKCTDFCQDDLADDDIMVLDNGEQVFLWLGARCSEVEIKLAYKSAQVYIQHLRVKQPERPRKL 246
Cdd:cd11291    1 KPRLFRCSNESGFF-KVEEISDFSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYIETDPLGRSKPRTPI 79

                         90
                 ....*....|...
gi 674659523 247 FLTAKSKESRRFT 259
Cdd:cd11291   80 YLVKQGNEPPTFT 92
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 55-156 4.29e-33

Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200444  Cd Length: 92  Bit Score: 115.79  E-value: 4.29e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659523  55 NKVEFYHLRSNGSaLCTRLIQVNPDALLLNSAFCYILNVPFnnddesgIVYVWIGSQADPEEARLVEEIAEEMFnnPWIS 134
Cdd:cd11288    1 SPTRLFQVRGNGS-GNTRAVEVDADASSLNSNDVFVLKTPS-------SVYLWVGKGSSEDERELAKDVASFLK--PKAS 70

                         90       100
                 ....*....|....*....|..
gi 674659523 135 LQVLNEGEEPDNFFWVGIGGKK 156
Cdd:cd11288   71 LQEVAEGSEPDEFWEALGGKSE 92
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 172-259 3.51e-17

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 74.25  E-value: 3.51e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659523   172 RCSNEKGYFTISEKCTDFCQDDLADDDIMVLDNGEQVFLWLGARCSEVEIKLAYKSAQVYIQHLRvkqpERPRKLFLTAK 251
Cdd:smart00262   1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLG----PGPVQVRVVDE 76


                   ....*...
gi 674659523   252 SKESRRFT 259
Cdd:smart00262  77 GKEPPEFW 84
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 60-154 8.58e-16

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: 70.40  E-value: 8.58e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659523    60 YHLRSNGSaLCTRLIQVNPDALLLNSAFCYILnvpfnndDESGIVYVWIGSQADPEEARLVEEIAEEMFNN---PWISLQ 136
Cdd:smart00262   1 FLVRVKGK-RNVRVPEVPFSQGSLNSGDCYIL-------DTGSEIYVWVGKKSSQDEKKKAAELAVELDDTlgpGPVQVR 72

                           90
                   ....*....|....*...
gi 674659523   137 VLNEGEEPDNFFWVGIGG 154
Cdd:smart00262  73 VVDEGKEPPEFWSLFGGW 90
Gelsolin pfam00626
Gelsolin repeat;
188-258 1.30e-10

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 56.16  E-value: 1.30e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 674659523  188 DFCQDDLADDDIMVLDNGEQVFLWLGARCSEVEIKLAYKSAQVYIQHLRVKQPErprkLFLTAKSKESRRF 258
Cdd:pfam00626   9 PLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDERFPLPE----VIRVPQGKEPARF 75
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 82-147 1.47e-08

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: 51.10  E-value: 1.47e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659523  82 LLNSAFCYILnvpfnnDDESGIvYVWIGSQADPEEARLVEEIAEEMFN----NPWISLQVLNEGEEPDNF 147
Cdd:cd11292   30 MLDSEDCYIL------DCGSEI-FVWVGKGASLDERKAALKNAEEFLRkkkrPPYTQVTRVTEGGESALF 92
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 168-233 4.06e-08

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


Pssm-ID: 200448  Cd Length: 98  Bit Score: 49.94  E-value: 4.06e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 674659523 168 TRLFRCSNEKGYFTISEKCTD-FCQDDLADDDIMVLDNGEQVFLWLGARCSEVEIKLAYKSAQVYIQ 233
Cdd:cd11292    4 KKLYKVSDASGKLKLTEVAEGsLNQEMLDSEDCYILDCGSEIFVWVGKGASLDERKAALKNAEEFLR 70
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 168-259 1.11e-06

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


Pssm-ID: 200436  Cd Length: 88  Bit Score: 45.82  E-value: 1.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659523 168 TRLFRCSNeKGYFTISEkcTDFCQDDLADDDIMVLDNGEQVFLWLGARCSEVEiklaYKSAQVYIQHLRVKQPERPRKLf 247
Cdd:cd11280    2 PRLYRVRG-SKAIEIEE--VPLASSSLDSDDVFVLDTGSEIYIWQGRASSQAE----LAAAALLAKELDEERKGKPEIV- 73

                         90
                 ....*....|..
gi 674659523 248 LTAKSKESRRFT 259
Cdd:cd11280   74 RIRQGQEPREFW 85
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 60-149 5.12e-06

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


Pssm-ID: 200436  Cd Length: 88  Bit Score: 43.90  E-value: 5.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659523  60 YHLRSNGSalcTRLIQVNPDALLLNSAFCYILnvpfnndDESGIVYVWIGSQADPEE---ARLV-EEIAEEMFNNPWISL 135
Cdd:cd11280    5 YRVRGSKA---IEIEEVPLASSSLDSDDVFVL-------DTGSEIYIWQGRASSQAElaaAALLaKELDEERKGKPEIVR 74

                         90
                 ....*....|....
gi 674659523 136 QVlnEGEEPDnFFW 149
Cdd:cd11280   75 IR--QGQEPR-EFW 85
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 1-35 8.99e-06

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


Pssm-ID: 200436  Cd Length: 88  Bit Score: 43.13  E-value: 8.99e-06
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 674659523   1 FTFSLQKKFKSLFGEKLEVVRTHQQQENLKFMAHF 35
Cdd:cd11280   54 AAALLAKELDEERKGKPEIVRIRQGQEPREFWSLF 88
Gelsolin pfam00626
Gelsolin repeat;
76-147 1.48e-03

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 36.52  E-value: 1.48e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 674659523   76 VNPDALLLNSAFCYILnvpfnndDESGIVYVWIGSQADPEE---ARLVEEIAEEMFNNPWISLQVLNEGEEPDNF 147
Cdd:pfam00626   8 VPLSQESLNSGDCYLL-------DNGFTIFLWVGKGSSLLEklfAALLAAQLDDDERFPLPEVIRVPQGKEPARF 75
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
 88-148 1.63e-03

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: 36.87  E-value: 1.63e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 674659523  88 CYI-LNVPFNNDDESGIVYVWIGSQADPEE----ARLVEEIAEEMFNNPwISLQVLnEGEEPDNFF 148
Cdd:cd11293   35 CYIvLYTYQGGGKEEHILYFWQGRHSSQDEraaaALLTVELDEELKGRA-VQVRVV-QGKEPPHFL 98
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 104-147 1.73e-03

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: 36.89  E-value: 1.73e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 674659523 104 VYVWIGSQADPEEARLVEEIAEEMFNN-------PWISLQVLNEGEEPDNF 147
Cdd:cd11291   41 VFVWVGSESSDEEKKEALTSAKKYIETdplgrskPRTPIYLVKQGNEPPTF 91
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 168-239 2.34e-03

Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200444  Cd Length: 92  Bit Score: 36.44  E-value: 2.34e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 674659523 168 TRLFR-CSNEKGyftisekCTDFCQDD-----LADDDIMVLDNGEQVFLWLGARCSEVEIKLAYKSAQVYIQHLRVKQ 239
Cdd:cd11288    3 TRLFQvRGNGSG-------NTRAVEVDadassLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVASFLKPKASLQE 73
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH