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Conserved domains on  [gi|1720392836|ref|XP_030106273|]
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supervillin isoform X13 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
 1401-1514 2.73e-44

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: 155.89  E-value: 2.73e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392836 1401 QFEIATVSVDVWHILEFDYSRLPRQSIGQFHEGDAYVVKWKYMastavgsrqkgehlvrVAGKEKCVYFFWQGRHSTVSE 1480
Cdd:cd11293      1 MYDDGSGKVEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQ----------------GGGKEEHILYFWQGRHSSQDE 64

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1720392836 1481 KGTSALMTVELDEE---RGAQVQVLQGKEPPCFLQCF 1514
Cdd:cd11293     65 RAAAALLTVELDEElkgRAVQVRVVQGKEPPHFLALF 101
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 1097-1189 2.68e-35

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


:

Pssm-ID: 200445  Cd Length: 92  Bit Score: 130.05  E-value: 2.68e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392836 1097 KLMLLQIKGRRHVQTRLVEPRASSLNSGDCFLLLSPQYCFLWVGEFSNVIEKAKASELATLIQTKRELGCRATYIQTIEE 1176
Cdd:cd11289      1 KPRLLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKVIVLDEGD 80

                           90
                   ....*....|...
gi 1720392836 1177 GiNTHTHAAKDFW 1189
Cdd:cd11289     81 T-NESPEFWKVLG 92
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 1534-1639 1.31e-26

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: 105.01  E-value: 1.31e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392836 1534 SEWRLYCVRGEVPMEGNLLEVACHCSSLRSRTSMVVLNINKalIYLWHGCKAQGHTKEVGRTAANKIKEECpleaglhss 1613
Cdd:cd11288      1 SPTRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKTPSS--VYLWVGKGSSEDERELAKDVASFLKPKA--------- 69

                           90       100
                   ....*....|....*....|....*.
gi 1720392836 1614 snvTIHECDEGSEPLGFWDALGRRDR 1639
Cdd:cd11288     70 ---SLQEVAEGSEPDEFWEALGGKSE 92
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 1218-1318 5.59e-18

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: 80.49  E-value: 5.59e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392836 1218 NCVYRLTDDKlvpdDDYWGKIPKCS-LLQSKEVLVFDFGSEVYVWHGKEVTLAQRKIAFQLAKHLWNGtfdyencdinpl 1296
Cdd:cd11280      2 PRLYRVRGSK----AIEIEEVPLASsSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKELDEE------------ 65

                           90       100
                   ....*....|....*....|...
gi 1720392836 1297 DPGECNPLIPRKGQG-RPDWAIF 1318
Cdd:cd11280     66 RKGKPEIVRIRQGQEpREFWSLF 88
VHP pfam02209
Villin headpiece domain;
1834-1869 7.71e-15

Villin headpiece domain;


:

Pssm-ID: 460493  Cd Length: 36  Bit Score: 69.71  E-value: 7.71e-15
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1720392836 1834 YLTDEDFEFALDMSRDEFNALPTWKQVNLKKSKGLF 1869
Cdd:pfam02209    1 YLSDEDFEEVFGMSREEFYKLPKWKQNNLKKKAGLF 36
ADF_gelsolin super family cl15697
Actin depolymerization factor/cofilin- and gelsolin-like domains; Actin depolymerization ...
 1656-1778 2.26e-13

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 cd11291:

Pssm-ID: 472830 [Multi-domain]  Cd Length: 99  Bit Score: 67.71  E-value: 2.26e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392836 1656 PRLFILSSSSGDFSATEFVypaqapsavssmPFLQEDLYSApqpALFLVDNHHEVYLWQGWWPTENKItgsarirwasdr 1735
Cdd:cd11291      2 PRLFRCSNESGFFKVEEIS------------DFSQDDLDTD---DIMLLDTGDEVFVWVGSESSDEEK------------ 54

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1720392836 1736 KSAMETVLQYCRGKNLKRPPPKS--YLIHAGLEPLTFTNMFPSWE 1778
Cdd:cd11291     55 KEALTSAKKYIETDPLGRSKPRTpiYLVKQGNEPPTFTGYFHAWD 99
PTZ00441 super family cl25523
sporozoite surface protein 2 (SSP2); Provisional
 177-335 3.64e-04

sporozoite surface protein 2 (SSP2); Provisional


The actual alignment was detected with superfamily member PTZ00441:

Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 45.34  E-value: 3.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392836  177 DCTPLGSNMSDQEQLLNVENQRRVQDPPLGEDGSSAFFsERSISFPEVPRSPkQIP--SSPLQQPASPNHPGDSPLPTEA 254
Cdd:PTZ00441   338 DGNPNEENLFPPGDDEVPDESNVPPNPPNVPGGSNSEF-SSDVENPPNPPNP-DIPeqEPNIPEDSNKEVPEDVPMEPED 415

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392836  255 RASQ-----SRVERSAEGIG-----LPMERERGSRKPRRYLSPGESRKTSERF-----RTQPITSAERKESDrYPSGsei 319
Cdd:PTZ00441   416 DRDNnfnepKKPENKGDGQNepvipKPLDNERDQSNKNKQVNPGNRHNSEDRYtrphgRNNENRNYNNKNSD-IPKH--- 491

                          170
                   ....*....|....*.
gi 1720392836  320 PVVEDEEKVDERAKLS 335
Cdd:PTZ00441   492 PERSEHEQPEDKKKKS 507
 
Name Accession Description Interval E-value
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
 1401-1514 2.73e-44

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: 155.89  E-value: 2.73e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392836 1401 QFEIATVSVDVWHILEFDYSRLPRQSIGQFHEGDAYVVKWKYMastavgsrqkgehlvrVAGKEKCVYFFWQGRHSTVSE 1480
Cdd:cd11293      1 MYDDGSGKVEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQ----------------GGGKEEHILYFWQGRHSSQDE 64

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1720392836 1481 KGTSALMTVELDEE---RGAQVQVLQGKEPPCFLQCF 1514
Cdd:cd11293     65 RAAAALLTVELDEElkgRAVQVRVVQGKEPPHFLALF 101
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 1097-1189 2.68e-35

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


Pssm-ID: 200445  Cd Length: 92  Bit Score: 130.05  E-value: 2.68e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392836 1097 KLMLLQIKGRRHVQTRLVEPRASSLNSGDCFLLLSPQYCFLWVGEFSNVIEKAKASELATLIQTKRELGCRATYIQTIEE 1176
Cdd:cd11289      1 KPRLLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKVIVLDEGD 80

                           90
                   ....*....|...
gi 1720392836 1177 GiNTHTHAAKDFW 1189
Cdd:cd11289     81 T-NESPEFWKVLG 92
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 1534-1639 1.31e-26

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: 105.01  E-value: 1.31e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392836 1534 SEWRLYCVRGEVPMEGNLLEVACHCSSLRSRTSMVVLNINKalIYLWHGCKAQGHTKEVGRTAANKIKEECpleaglhss 1613
Cdd:cd11288      1 SPTRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKTPSS--VYLWVGKGSSEDERELAKDVASFLKPKA--------- 69

                           90       100
                   ....*....|....*....|....*.
gi 1720392836 1614 snvTIHECDEGSEPLGFWDALGRRDR 1639
Cdd:cd11288     70 ---SLQEVAEGSEPDEFWEALGGKSE 92
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1100-1194 5.02e-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: 91.97  E-value: 5.02e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392836  1100 LLQIKGRRHVQTRLVEPRASSLNSGDCFLLLSPQYCFLWVGEFSNVIEKAKASELATLIqtKRELGCRATYIQTIEEGIN 1179
Cdd:smart00262    2 LVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVEL--DDTLGPGPVQVRVVDEGKE 79

                            90
                    ....*....|....*
gi 1720392836  1180 THThaakdFWKLLGG 1194
Cdd:smart00262   80 PPE-----FWSLFGG 89
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 1218-1318 5.59e-18

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: 80.49  E-value: 5.59e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392836 1218 NCVYRLTDDKlvpdDDYWGKIPKCS-LLQSKEVLVFDFGSEVYVWHGKEVTLAQRKIAFQLAKHLWNGtfdyencdinpl 1296
Cdd:cd11280      2 PRLYRVRGSK----AIEIEEVPLASsSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKELDEE------------ 65

                           90       100
                   ....*....|....*....|...
gi 1720392836 1297 DPGECNPLIPRKGQG-RPDWAIF 1318
Cdd:cd11280     66 RKGKPEIVRIRQGQEpREFWSLF 88
VHP pfam02209
Villin headpiece domain;
1834-1869 7.71e-15

Villin headpiece domain;


Pssm-ID: 460493  Cd Length: 36  Bit Score: 69.71  E-value: 7.71e-15
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1720392836 1834 YLTDEDFEFALDMSRDEFNALPTWKQVNLKKSKGLF 1869
Cdd:pfam02209    1 YLSDEDFEEVFGMSREEFYKLPKWKQNNLKKKAGLF 36
VHP smart00153
Villin headpiece domain;
1834-1869 1.25e-14

Villin headpiece domain;


Pssm-ID: 128458  Cd Length: 36  Bit Score: 69.27  E-value: 1.25e-14
                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 1720392836  1834 YLTDEDFEFALDMSRDEFNALPTWKQVNLKKSKGLF 1869
Cdd:smart00153    1 YLSDEDFEEVFGMTREEFYKLPLWKQNQLKKKKGLF 36
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 1656-1778 2.26e-13

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: 67.71  E-value: 2.26e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392836 1656 PRLFILSSSSGDFSATEFVypaqapsavssmPFLQEDLYSApqpALFLVDNHHEVYLWQGWWPTENKItgsarirwasdr 1735
Cdd:cd11291      2 PRLFRCSNESGFFKVEEIS------------DFSQDDLDTD---DIMLLDTGDEVFVWVGSESSDEEK------------ 54

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1720392836 1736 KSAMETVLQYCRGKNLKRPPPKS--YLIHAGLEPLTFTNMFPSWE 1778
Cdd:cd11291     55 KEALTSAKKYIETDPLGRSKPRTpiYLVKQGNEPPTFTGYFHAWD 99
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1411-1517 8.60e-13

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 65.78  E-value: 8.60e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392836  1411 VWHILEFDYSRLPRQ--SIGQFHEGDAYVVKWkymastavgsrqkGEHLvrvagkekcvyFFWQGRHSTVSEKGTSALMT 1488
Cdd:smart00262    2 LVRVKGKRNVRVPEVpfSQGSLNSGDCYILDT-------------GSEI-----------YVWVGKKSSQDEKKKAAELA 57

                            90       100       110
                    ....*....|....*....|....*....|...
gi 1720392836  1489 VELDEERG---AQVQ-VLQGKEPPCFLQCFQGG 1517
Cdd:smart00262   58 VELDDTLGpgpVQVRvVDEGKEPPEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1539-1635 1.04e-12

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 65.39  E-value: 1.04e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392836  1539 YCVRGEVPMEGNLLEVACHCSSLRSRTSMVVLNinKALIYLWHGCKAQGHTKEVGRTAANKIKEECPleaglhsSSNVTI 1618
Cdd:smart00262    1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDT--GSEIYVWVGKKSSQDEKKKAAELAVELDDTLG-------PGPVQV 71

                            90
                    ....*....|....*..
gi 1720392836  1619 HECDEGSEPLGFWDALG 1635
Cdd:smart00262   72 RVVDEGKEPPEFWSLFG 88
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1683-1777 9.19e-07

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: 48.44  E-value: 9.19e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392836  1683 VSSMPFLQEDLYSApqpALFLVDNHHEVYLWQGwwptenkiTGSARirwaSDRKSAMETVLQYCrgKNLKRPPPKSYLIH 1762
Cdd:smart00262   13 VPEVPFSQGSLNSG---DCYILDTGSEIYVWVG--------KKSSQ----DEKKKAAELAVELD--DTLGPGPVQVRVVD 75

                            90
                    ....*....|....*
gi 1720392836  1763 AGLEPLTFTNMFPSW 1777
Cdd:smart00262   76 EGKEPPEFWSLFGGW 90
Gelsolin pfam00626
Gelsolin repeat;
1118-1177 4.82e-06

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 46.15  E-value: 4.82e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720392836 1118 ASSLNSGDCFLLLSPQYCFLWVGEFSNVIEKAKASELAT-LIQTKRelgCRATYIQTIEEG 1177
Cdd:pfam00626   12 QESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAqLDDDER---FPLPEVIRVPQG 69
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1239-1337 6.74e-06

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: 46.13  E-value: 6.74e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392836  1239 PKCSLLQSKEVLVFDFGSEVYVWHGKEVTLAQRKIAFQLAKHLwngtFDYENcdinpldpgecnpliPRKGQGRpdwaif 1318
Cdd:smart00262   18 FSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVEL----DDTLG---------------PGPVQVR------ 72

                            90
                    ....*....|....*....
gi 1720392836  1319 gRVTEHNETILFKEKFLDW 1337
Cdd:smart00262   73 -VVDEGKEPPEFWSLFGGW 90
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 177-335 3.64e-04

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 45.34  E-value: 3.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392836  177 DCTPLGSNMSDQEQLLNVENQRRVQDPPLGEDGSSAFFsERSISFPEVPRSPkQIP--SSPLQQPASPNHPGDSPLPTEA 254
Cdd:PTZ00441   338 DGNPNEENLFPPGDDEVPDESNVPPNPPNVPGGSNSEF-SSDVENPPNPPNP-DIPeqEPNIPEDSNKEVPEDVPMEPED 415

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392836  255 RASQ-----SRVERSAEGIG-----LPMERERGSRKPRRYLSPGESRKTSERF-----RTQPITSAERKESDrYPSGsei 319
Cdd:PTZ00441   416 DRDNnfnepKKPENKGDGQNepvipKPLDNERDQSNKNKQVNPGNRHNSEDRYtrphgRNNENRNYNNKNSD-IPKH--- 491

                          170
                   ....*....|....*.
gi 1720392836  320 PVVEDEEKVDERAKLS 335
Cdd:PTZ00441   492 PERSEHEQPEDKKKKS 507
Gelsolin pfam00626
Gelsolin repeat;
1469-1511 7.83e-03

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 36.90  E-value: 7.83e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1720392836 1469 FFWQGRHSTVSEKGTSALMTVELD-EERGA---QVQVLQGKEPPCFL 1511
Cdd:pfam00626   30 FLWVGKGSSLLEKLFAALLAAQLDdDERFPlpeVIRVPQGKEPARFL 76
 
Name Accession Description Interval E-value
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
 1401-1514 2.73e-44

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: 155.89  E-value: 2.73e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392836 1401 QFEIATVSVDVWHILEFDYSRLPRQSIGQFHEGDAYVVKWKYMastavgsrqkgehlvrVAGKEKCVYFFWQGRHSTVSE 1480
Cdd:cd11293      1 MYDDGSGKVEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQ----------------GGGKEEHILYFWQGRHSSQDE 64

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1720392836 1481 KGTSALMTVELDEE---RGAQVQVLQGKEPPCFLQCF 1514
Cdd:cd11293     65 RAAAALLTVELDEElkgRAVQVRVVQGKEPPHFLALF 101
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 1097-1189 2.68e-35

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


Pssm-ID: 200445  Cd Length: 92  Bit Score: 130.05  E-value: 2.68e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392836 1097 KLMLLQIKGRRHVQTRLVEPRASSLNSGDCFLLLSPQYCFLWVGEFSNVIEKAKASELATLIQTKRELGCRATYIQTIEE 1176
Cdd:cd11289      1 KPRLLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKVIVLDEGD 80

                           90
                   ....*....|...
gi 1720392836 1177 GiNTHTHAAKDFW 1189
Cdd:cd11289     81 T-NESPEFWKVLG 92
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 1534-1639 1.31e-26

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: 105.01  E-value: 1.31e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392836 1534 SEWRLYCVRGEVPMEGNLLEVACHCSSLRSRTSMVVLNINKalIYLWHGCKAQGHTKEVGRTAANKIKEECpleaglhss 1613
Cdd:cd11288      1 SPTRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKTPSS--VYLWVGKGSSEDERELAKDVASFLKPKA--------- 69

                           90       100
                   ....*....|....*....|....*.
gi 1720392836 1614 snvTIHECDEGSEPLGFWDALGRRDR 1639
Cdd:cd11288     70 ---SLQEVAEGSEPDEFWEALGGKSE 92
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1100-1194 5.02e-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: 91.97  E-value: 5.02e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392836  1100 LLQIKGRRHVQTRLVEPRASSLNSGDCFLLLSPQYCFLWVGEFSNVIEKAKASELATLIqtKRELGCRATYIQTIEEGIN 1179
Cdd:smart00262    2 LVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVEL--DDTLGPGPVQVRVVDEGKE 79

                            90
                    ....*....|....*
gi 1720392836  1180 THThaakdFWKLLGG 1194
Cdd:smart00262   80 PPE-----FWSLFGG 89
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 1218-1318 5.59e-18

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: 80.49  E-value: 5.59e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392836 1218 NCVYRLTDDKlvpdDDYWGKIPKCS-LLQSKEVLVFDFGSEVYVWHGKEVTLAQRKIAFQLAKHLWNGtfdyencdinpl 1296
Cdd:cd11280      2 PRLYRVRGSK----AIEIEEVPLASsSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKELDEE------------ 65

                           90       100
                   ....*....|....*....|...
gi 1720392836 1297 DPGECNPLIPRKGQG-RPDWAIF 1318
Cdd:cd11280     66 RKGKPEIVRIRQGQEpREFWSLF 88
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 1099-1197 5.08e-17

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: 77.66  E-value: 5.08e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392836 1099 MLLQIKGRRHVQTRLVE--PRASSLNSGDCFLLLSPQYCFLWVGEFSNVIEKAKASELATLIQTKRElgcratyIQTIEE 1176
Cdd:cd11288      4 RLFQVRGNGSGNTRAVEvdADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVASFLKPKAS-------LQEVAE 76

                           90       100
                   ....*....|....*....|.
gi 1720392836 1177 GINThthaaKDFWKLLGGQTS 1197
Cdd:cd11288     77 GSEP-----DEFWEALGGKSE 92
VHP pfam02209
Villin headpiece domain;
1834-1869 7.71e-15

Villin headpiece domain;


Pssm-ID: 460493  Cd Length: 36  Bit Score: 69.71  E-value: 7.71e-15
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1720392836 1834 YLTDEDFEFALDMSRDEFNALPTWKQVNLKKSKGLF 1869
Cdd:pfam02209    1 YLSDEDFEEVFGMSREEFYKLPKWKQNNLKKKAGLF 36
VHP smart00153
Villin headpiece domain;
1834-1869 1.25e-14

Villin headpiece domain;


Pssm-ID: 128458  Cd Length: 36  Bit Score: 69.27  E-value: 1.25e-14
                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 1720392836  1834 YLTDEDFEFALDMSRDEFNALPTWKQVNLKKSKGLF 1869
Cdd:smart00153    1 YLSDEDFEEVFGMTREEFYKLPLWKQNQLKKKKGLF 36
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 1656-1778 2.26e-13

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: 67.71  E-value: 2.26e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392836 1656 PRLFILSSSSGDFSATEFVypaqapsavssmPFLQEDLYSApqpALFLVDNHHEVYLWQGWWPTENKItgsarirwasdr 1735
Cdd:cd11291      2 PRLFRCSNESGFFKVEEIS------------DFSQDDLDTD---DIMLLDTGDEVFVWVGSESSDEEK------------ 54

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1720392836 1736 KSAMETVLQYCRGKNLKRPPPKS--YLIHAGLEPLTFTNMFPSWE 1778
Cdd:cd11291     55 KEALTSAKKYIETDPLGRSKPRTpiYLVKQGNEPPTFTGYFHAWD 99
gelsolin_S1_like cd11290
Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; ...
 1409-1523 2.49e-13

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: 68.02  E-value: 2.49e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392836 1409 VDVWHILEFDYSRLPRQSIGQFHEGDAYVVkwkyMASTAVGSrqkgehlvrvaGKEKCVYFFWQGRHSTVSEKGTSALMT 1488
Cdd:cd11290     10 LQIWRIENFELVPVPESFYGKFYEGDSYIV----LKTTLDPS-----------GSLSYDIHYWLGKEASQDEAGAAAIKA 74

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1720392836 1489 VELDEERGAQ-VQV--LQGKEPPCFLQCFQGGMVVHSG 1523
Cdd:cd11290     75 VELDDYLGGRpVQHreVQGHESEEFLSYFKKGIIYIEG 112
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1411-1517 8.60e-13

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 65.78  E-value: 8.60e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392836  1411 VWHILEFDYSRLPRQ--SIGQFHEGDAYVVKWkymastavgsrqkGEHLvrvagkekcvyFFWQGRHSTVSEKGTSALMT 1488
Cdd:smart00262    2 LVRVKGKRNVRVPEVpfSQGSLNSGDCYILDT-------------GSEI-----------YVWVGKKSSQDEKKKAAELA 57

                            90       100       110
                    ....*....|....*....|....*....|...
gi 1720392836  1489 VELDEERG---AQVQ-VLQGKEPPCFLQCFQGG 1517
Cdd:smart00262   58 VELDDTLGpgpVQVRvVDEGKEPPEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1539-1635 1.04e-12

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 65.39  E-value: 1.04e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392836  1539 YCVRGEVPMEGNLLEVACHCSSLRSRTSMVVLNinKALIYLWHGCKAQGHTKEVGRTAANKIKEECPleaglhsSSNVTI 1618
Cdd:smart00262    1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDT--GSEIYVWVGKKSSQDEKKKAAELAVELDDTLG-------PGPVQV 71

                            90
                    ....*....|....*..
gi 1720392836  1619 HECDEGSEPLGFWDALG 1635
Cdd:smart00262   72 RVVDEGKEPPEFWSLFG 88
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 1655-1774 6.34e-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: 60.46  E-value: 6.34e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392836 1655 APRLFILSSSSgdfsATEFVYPAQAPSAVSSMPFLQEDLYSapqpalflvdnhhEVYLWQGWwptenkitGSARIRWASD 1734
Cdd:cd11280      1 PPRLYRVRGSK----AIEIEEVPLASSSLDSDDVFVLDTGS-------------EIYIWQGR--------ASSQAELAAA 55

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1720392836 1735 RKSAMETVLQYcrgknlkRPPPKSYLIHAGLEPLTFTNMF 1774
Cdd:cd11280     56 ALLAKELDEER-------KGKPEIVRIRQGQEPREFWSLF 88
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 1242-1334 7.32e-09

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: 54.95  E-value: 7.32e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392836 1242 SLLQSKEVLVFDFGSEVYVWHGKEVTLAQRKIAFQLA-KHLwngtfdyencdinpldpgecnpliprKGQGRPDWAIFGR 1320
Cdd:cd11292     29 EMLDSEDCYILDCGSEIFVWVGKGASLDERKAALKNAeEFL--------------------------RKKKRPPYTQVTR 82

                           90
                   ....*....|....
gi 1720392836 1321 VTEHNETILFKEKF 1334
Cdd:cd11292     83 VTEGGESALFKSKF 96
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1683-1777 9.19e-07

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: 48.44  E-value: 9.19e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392836  1683 VSSMPFLQEDLYSApqpALFLVDNHHEVYLWQGwwptenkiTGSARirwaSDRKSAMETVLQYCrgKNLKRPPPKSYLIH 1762
Cdd:smart00262   13 VPEVPFSQGSLNSG---DCYILDTGSEIYVWVG--------KKSSQ----DEKKKAAELAVELD--DTLGPGPVQVRVVD 75

                            90
                    ....*....|....*
gi 1720392836  1763 AGLEPLTFTNMFPSW 1777
Cdd:smart00262   76 EGKEPPEFWSLFGGW 90
Gelsolin pfam00626
Gelsolin repeat;
1118-1177 4.82e-06

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 46.15  E-value: 4.82e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720392836 1118 ASSLNSGDCFLLLSPQYCFLWVGEFSNVIEKAKASELAT-LIQTKRelgCRATYIQTIEEG 1177
Cdd:pfam00626   12 QESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAqLDDDER---FPLPEVIRVPQG 69
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1239-1337 6.74e-06

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: 46.13  E-value: 6.74e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392836  1239 PKCSLLQSKEVLVFDFGSEVYVWHGKEVTLAQRKIAFQLAKHLwngtFDYENcdinpldpgecnpliPRKGQGRpdwaif 1318
Cdd:smart00262   18 FSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVEL----DDTLG---------------PGPVQVR------ 72

                            90
                    ....*....|....*....
gi 1720392836  1319 gRVTEHNETILFKEKFLDW 1337
Cdd:smart00262   73 -VVDEGKEPPEFWSLFGGW 90
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 1466-1514 3.26e-05

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


Pssm-ID: 200436  Cd Length: 88  Bit Score: 44.28  E-value: 3.26e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1720392836 1466 CVYFFWQGRHSTVSEKGTSALMTVELDEERG---AQVQVLQGKEPPCFLQCF 1514
Cdd:cd11280     37 SEIYIWQGRASSQAELAAAALLAKELDEERKgkpEIVRIRQGQEPREFWSLF 88
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 1119-1190 3.46e-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: 44.16  E-value: 3.46e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720392836 1119 SSLNSGDCFLLLSPQYCFLWVGEFSNVIEKAKASELAT-LIQTKRElgCRATYIQTIEEGinTHTHAAKDFWK 1190
Cdd:cd11292     29 EMLDSEDCYILDCGSEIFVWVGKGASLDERKAALKNAEeFLRKKKR--PPYTQVTRVTEG--GESALFKSKFA 97
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 1114-1192 5.69e-05

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


Pssm-ID: 200436  Cd Length: 88  Bit Score: 43.51  E-value: 5.69e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720392836 1114 VEPRASSLNSGDCFLLLSPQYCFLWVGEFSNVIEKAKASELATliQTKRELGCRATYIQtIEEGinthtHAAKDFWKLL 1192
Cdd:cd11280     18 VPLASSSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAK--ELDEERKGKPEIVR-IRQG-----QEPREFWSLF 88
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 1239-1285 1.11e-04

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: 42.60  E-value: 1.11e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1720392836 1239 PKCSLLQSKEVLVFDFGSEVYVWHGKEVTLAQRKIAFQLAKHLWNGT 1285
Cdd:cd11288     23 ADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVASFLKPKA 69
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 177-335 3.64e-04

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 45.34  E-value: 3.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392836  177 DCTPLGSNMSDQEQLLNVENQRRVQDPPLGEDGSSAFFsERSISFPEVPRSPkQIP--SSPLQQPASPNHPGDSPLPTEA 254
Cdd:PTZ00441   338 DGNPNEENLFPPGDDEVPDESNVPPNPPNVPGGSNSEF-SSDVENPPNPPNP-DIPeqEPNIPEDSNKEVPEDVPMEPED 415

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392836  255 RASQ-----SRVERSAEGIG-----LPMERERGSRKPRRYLSPGESRKTSERF-----RTQPITSAERKESDrYPSGsei 319
Cdd:PTZ00441   416 DRDNnfnepKKPENKGDGQNepvipKPLDNERDQSNKNKQVNPGNRHNSEDRYtrphgRNNENRNYNNKNSD-IPKH--- 491

                          170
                   ....*....|....*.
gi 1720392836  320 PVVEDEEKVDERAKLS 335
Cdd:PTZ00441   492 PERSEHEQPEDKKKKS 507
Gelsolin pfam00626
Gelsolin repeat;
1469-1511 7.83e-03

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 36.90  E-value: 7.83e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1720392836 1469 FFWQGRHSTVSEKGTSALMTVELD-EERGA---QVQVLQGKEPPCFL 1511
Cdd:pfam00626   30 FLWVGKGSSLLEKLFAALLAAQLDdDERFPlpeVIRVPQGKEPARFL 76
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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