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Conserved domains on  [gi|1820722642|ref|XP_032620354|]
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LOW QUALITY PROTEIN: villin-1 [Chelonoidis abingdonii]

Protein Classification

gelsolin_S4_like and gelsolin_S6_like domain-containing protein( domain architecture ID 10336970)

protein containing domains gelsolin_S3_like, gelsolin_S4_like, gelsolin_S5_like, and gelsolin_S6_like

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; ...
 327-427 3.36e-49

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: 167.83  E-value: 3.36e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820722642 327 MVDDGSGEVEVWRIEDLELAPVDMRWLGHFYGGDCYLILYKYLVNNKQHYIIYIWQGRHASKDEITASAYQAVILDQQYD 406
Cdd:cd11293     1 MYDDGSGKVEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQGGGKEEHILYFWQGRHSSQDERAAAALLTVELDEELK 80

                          90       100
                  ....*....|....*....|.
gi 1820722642 407 NAAVQVRVPMGKEPAHLMAIF 427
Cdd:cd11293    81 GRAVQVRVVQGKEPPHFLALF 101
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 448-538 4.75e-46

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: 158.93  E-value: 4.75e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820722642 448 PSTRLFHVHGTNEYNTKAIEVPPRASSLNSNDVFVLKTQACCYLWYGKGCSGDEREMAKTVA-DLITKTEKLVIAEGQEP 526
Cdd:cd11288     1 SPTRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVAsFLKPKASLQEVAEGSEP 80

                          90
                  ....*....|..
gi 1820722642 527 DNFWVALGGKSQ 538
Cdd:cd11288    81 DEFWEALGGKSE 92
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 554-650 1.45e-45

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: 157.84  E-value: 1.45e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820722642 554 PRLFECSNQTGTFVATEITDFNQDDLEDDDVFLLDTWDQVFFWIGEHANETEKKEAAVMAQEYLRTHPSGRD-PDTPIIV 632
Cdd:cd11291     2 PRLFRCSNESGFFKVEEISDFSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYIETDPLGRSkPRTPIYL 81

                          90
                  ....*....|....*...
gi 1820722642 633 VKQGYEPPTFTGWFLAWD 650
Cdd:cd11291    82 VKQGNEPPTFTGYFHAWD 99
ADF_gelsolin super family cl15697
Actin depolymerization factor/cofilin- and gelsolin-like domains; Actin depolymerization ...
 17-85 3.26e-32

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 cd11290:

Pssm-ID: 472830  Cd Length: 113  Bit Score: 120.79  E-value: 3.26e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820722642  17 PGLQIWRIEKMEMVLVPPKSYGNFYEGDCYVLLATHKTG-NSFRYDIHYWLGRESSQDEQGAAAIYTTQI 85
Cdd:cd11290     8 PGLQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDPsGSLSYDIHYWLGKEASQDEAGAAAIKAVEL 77
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 185-280 5.83e-30

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: 113.88  E-value: 5.83e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820722642 185 KLYK*ClDAEGNLVIQEVATRP*TQDLLQHEDCYILDQGgSTIYVWKG*KSTKEEKQQAMSRALGFIKAKDYSPSTAWQT 264
Cdd:cd11292     5 KLYKVS-DASGKLKLTEVAEGSLNQEMLDSEDCYILDCG-SEIFVWVGKGASLDERKAALKNAEEFLRKKKRPPYTQVTR 82

                          90
                  ....*....|....*.
gi 1820722642 265 RTTG*ESAMFKQLFQK 280
Cdd:cd11292    83 VTEGGESALFKSKFAN 98
ADF_gelsolin super family cl15697
Actin depolymerization factor/cofilin- and gelsolin-like domains; Actin depolymerization ...
 80-137 5.22e-24

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 cd11289:

Pssm-ID: 472830  Cd Length: 92  Bit Score: 96.54  E-value: 5.22e-24
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1820722642  80 IYTTQiVEMSWNSFNQGDVFLLDLGKLIIQWNGPESNRAERLKGINLAKDIRDRERGG 137
Cdd:cd11289    13 VRARE-VELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLG 69
VHP pfam02209
Villin headpiece domain;
725-760 7.11e-14

Villin headpiece domain;


:

Pssm-ID: 460493  Cd Length: 36  Bit Score: 65.86  E-value: 7.11e-14
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1820722642 725 HLSGDDFNTVFGMPQTAFAALPLWKQQKLKKEKGLF 760
Cdd:pfam02209   1 YLSDEDFEEVFGMSREEFYKLPKWKQNNLKKKAGLF 36
 
Name Accession Description Interval E-value
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
 327-427 3.36e-49

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: 167.83  E-value: 3.36e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820722642 327 MVDDGSGEVEVWRIEDLELAPVDMRWLGHFYGGDCYLILYKYLVNNKQHYIIYIWQGRHASKDEITASAYQAVILDQQYD 406
Cdd:cd11293     1 MYDDGSGKVEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQGGGKEEHILYFWQGRHSSQDERAAAALLTVELDEELK 80

                          90       100
                  ....*....|....*....|.
gi 1820722642 407 NAAVQVRVPMGKEPAHLMAIF 427
Cdd:cd11293    81 GRAVQVRVVQGKEPPHFLALF 101
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 448-538 4.75e-46

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: 158.93  E-value: 4.75e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820722642 448 PSTRLFHVHGTNEYNTKAIEVPPRASSLNSNDVFVLKTQACCYLWYGKGCSGDEREMAKTVA-DLITKTEKLVIAEGQEP 526
Cdd:cd11288     1 SPTRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVAsFLKPKASLQEVAEGSEP 80

                          90
                  ....*....|..
gi 1820722642 527 DNFWVALGGKSQ 538
Cdd:cd11288    81 DEFWEALGGKSE 92
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 554-650 1.45e-45

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: 157.84  E-value: 1.45e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820722642 554 PRLFECSNQTGTFVATEITDFNQDDLEDDDVFLLDTWDQVFFWIGEHANETEKKEAAVMAQEYLRTHPSGRD-PDTPIIV 632
Cdd:cd11291     2 PRLFRCSNESGFFKVEEISDFSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYIETDPLGRSkPRTPIYL 81

                          90
                  ....*....|....*...
gi 1820722642 633 VKQGYEPPTFTGWFLAWD 650
Cdd:cd11291    82 VKQGNEPPTFTGYFHAWD 99
gelsolin_S1_like cd11290
Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; ...
 17-85 3.26e-32

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: 120.79  E-value: 3.26e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820722642  17 PGLQIWRIEKMEMVLVPPKSYGNFYEGDCYVLLATHKTG-NSFRYDIHYWLGRESSQDEQGAAAIYTTQI 85
Cdd:cd11290     8 PGLQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDPsGSLSYDIHYWLGKEASQDEAGAAAIKAVEL 77
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 185-280 5.83e-30

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: 113.88  E-value: 5.83e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820722642 185 KLYK*ClDAEGNLVIQEVATRP*TQDLLQHEDCYILDQGgSTIYVWKG*KSTKEEKQQAMSRALGFIKAKDYSPSTAWQT 264
Cdd:cd11292     5 KLYKVS-DASGKLKLTEVAEGSLNQEMLDSEDCYILDCG-SEIFVWVGKGASLDERKAALKNAEEFLRKKKRPPYTQVTR 82

                          90
                  ....*....|....*.
gi 1820722642 265 RTTG*ESAMFKQLFQK 280
Cdd:cd11292    83 VTEGGESALFKSKFAN 98
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 453-536 1.82e-25

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 100.83  E-value: 1.82e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820722642  453 FHVHGTNEYNTKAIEVPPRASSLNSNDVFVLKTQACCYLWYGKGCSGDEREMAKTVADLI------TKTEKLVIAEGQEP 526
Cdd:smart00262   1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELddtlgpGPVQVRVVDEGKEP 80

                           90
                   ....*....|
gi 1820722642  527 DNFWVALGGK 536
Cdd:smart00262  81 PEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 558-649 2.75e-24

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: 97.36  E-value: 2.75e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820722642  558 ECSNQTGTFVATEIT-DFNQDDLEDDDVFLLDTWDQVFFWIGEHANETEKKEAAVMAQEYLRTHPSGRdpdTPIIVVKQG 636
Cdd:smart00262   1 FLVRVKGKRNVRVPEvPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGP---VQVRVVDEG 77

                           90
                   ....*....|...
gi 1820722642  637 YEPPTFTGWFLAW 649
Cdd:smart00262  78 KEPPEFWSLFGGW 90
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 80-137 5.22e-24

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: 96.54  E-value: 5.22e-24
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1820722642  80 IYTTQiVEMSWNSFNQGDVFLLDLGKLIIQWNGPESNRAERLKGINLAKDIRDRERGG 137
Cdd:cd11289    13 VRARE-VELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLG 69
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 336-430 5.99e-20

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: 85.04  E-value: 5.99e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820722642  336 EVWRIED---LELAPVDMRWlGHFYGGDCYLILYkylvnnkqHYIIYIWQGRHASKDEITASAYQAVILDQQYDNAAVQV 412
Cdd:smart00262   1 FLVRVKGkrnVRVPEVPFSQ-GSLNSGDCYILDT--------GSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQV 71

                           90
                   ....*....|....*....
gi 1820722642  413 R-VPMGKEPAHLMAIFKGK 430
Cdd:smart00262  72 RvVDEGKEPPEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 190-281 5.24e-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: 76.56  E-value: 5.24e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820722642  190 CLDAEGNLVIqEVATRP*TQDLLQHEDCYILDQGgSTIYVWKG*KSTKEEKQQAMSRALGFIKaKDYSPSTAWQTRTTG* 269
Cdd:smart00262   2 LVRVKGKRNV-RVPEVPFSQGSLNSGDCYILDTG-SEIYVWVGKKSSQDEKKKAAELAVELDD-TLGPGPVQVRVVDEGK 78

                           90
                   ....*....|..
gi 1820722642  270 ESAMFKQLFQKW 281
Cdd:smart00262  79 EPPEFWSLFGGW 90
Gelsolin pfam00626
Gelsolin repeat;
565-642 5.88e-17

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 75.81  E-value: 5.88e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820722642 565 TFVATEITDFNQDDLEDDDVFLLDTWDQVFFWIGEHANETEKKEAAVMAQEYLRTHpsgRDPDTPIIVVKQGYEPPTF 642
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDE---RFPLPEVIRVPQGKEPARF 75
VHP pfam02209
Villin headpiece domain;
725-760 7.11e-14

Villin headpiece domain;


Pssm-ID: 460493  Cd Length: 36  Bit Score: 65.86  E-value: 7.11e-14
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1820722642 725 HLSGDDFNTVFGMPQTAFAALPLWKQQKLKKEKGLF 760
Cdd:pfam02209   1 YLSDEDFEEVFGMSREEFYKLPKWKQNNLKKKAGLF 36
Gelsolin pfam00626
Gelsolin repeat;
344-424 1.68e-13

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 66.18  E-value: 1.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820722642 344 ELAPVDMRWLGHFYGGDCYLILykylvnnkQHYIIYIWQGRHASKDEITASAYQAV-ILDQQYDNAAVQVRVPMGKEPAH 422
Cdd:pfam00626   3 VLPPPVPLSQESLNSGDCYLLD--------NGFTIFLWVGKGSSLLEKLFAALLAAqLDDDERFPLPEVIRVPQGKEPAR 74


                  ..
gi 1820722642 423 LM 424
Cdd:pfam00626  75 FL 76
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 20-88 5.47e-13

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 65.01  E-value: 5.47e-13
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820722642   20 QIWRIEKMEMVLVP--PKSYGNFYEGDCYVLLATHktgnsfryDIHYWLGRESSQDEQGAAAIYTTQIVEM 88
Cdd:smart00262   1 FLVRVKGKRNVRVPevPFSQGSLNSGDCYILDTGS--------EIYVWVGKKSSQDEKKKAAELAVELDDT 63
Gelsolin pfam00626
Gelsolin repeat;
84-139 3.45e-12

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 62.33  E-value: 3.45e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1820722642  84 QIVEMSWNSFNQGDVFLLDLGKLIIQWNGPESNRAERLKGINLAKDIRDRERGGVP 139
Cdd:pfam00626   6 PPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDERFPLP 61
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 86-137 5.73e-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: 62.31  E-value: 5.73e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1820722642   86 VEMSWNSFNQGDVFLLDLGKLIIQWNGPESNRAERLKGINLAKDIRDRERGG 137
Cdd:smart00262  16 VPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPG 67
VHP smart00153
Villin headpiece domain;
725-760 5.85e-12

Villin headpiece domain;


Pssm-ID: 128458  Cd Length: 36  Bit Score: 60.41  E-value: 5.85e-12
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1820722642  725 HLSGDDFNTVFGMPQTAFAALPLWKQQKLKKEKGLF 760
Cdd:smart00153   1 YLSDEDFEEVFGMTREEFYKLPLWKQNQLKKKKGLF 36
Gelsolin pfam00626
Gelsolin repeat;
198-275 1.23e-11

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 60.78  E-value: 1.23e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820722642 198 VIQEVATRP*TQDLLQHEDCYILDQGgSTIYVWKG*KSTKEEKQQAMSRALGFIKaKDYSPSTAWQTRTTG*ESAMFK 275
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNG-FTIFLWVGKGSSLLEKLFAALLAAQLDD-DERFPLPEVIRVPQGKEPARFL 76
Gelsolin pfam00626
Gelsolin repeat;
26-85 3.21e-10

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 56.93  E-value: 3.21e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820722642  26 KMEMVLVPPKSYGNFYEGDCYVLLAThktgnsfrYDIHYWLGRESSQDEQGAAAIYTTQI 85
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNG--------FTIFLWVGKGSSLLEKLFAALLAAQL 52
Gelsolin pfam00626
Gelsolin repeat;
462-530 6.98e-05

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 41.52  E-value: 6.98e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820722642 462 NTKAIEVPPRASSLNSNDVFVLKTQACCYLWYGKGCSGDEREMAKTVA------DLITKTEKLVIAEGQEPDNFW 530
Cdd:pfam00626   2 FVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAaqldddERFPLPEVIRVPQGKEPARFL 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; ...
 327-427 3.36e-49

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: 167.83  E-value: 3.36e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820722642 327 MVDDGSGEVEVWRIEDLELAPVDMRWLGHFYGGDCYLILYKYLVNNKQHYIIYIWQGRHASKDEITASAYQAVILDQQYD 406
Cdd:cd11293     1 MYDDGSGKVEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQGGGKEEHILYFWQGRHSSQDERAAAALLTVELDEELK 80

                          90       100
                  ....*....|....*....|.
gi 1820722642 407 NAAVQVRVPMGKEPAHLMAIF 427
Cdd:cd11293    81 GRAVQVRVVQGKEPPHFLALF 101
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 448-538 4.75e-46

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: 158.93  E-value: 4.75e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820722642 448 PSTRLFHVHGTNEYNTKAIEVPPRASSLNSNDVFVLKTQACCYLWYGKGCSGDEREMAKTVA-DLITKTEKLVIAEGQEP 526
Cdd:cd11288     1 SPTRLFQVRGNGSGNTRAVEVDADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVAsFLKPKASLQEVAEGSEP 80

                          90
                  ....*....|..
gi 1820722642 527 DNFWVALGGKSQ 538
Cdd:cd11288    81 DEFWEALGGKSE 92
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 554-650 1.45e-45

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: 157.84  E-value: 1.45e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820722642 554 PRLFECSNQTGTFVATEITDFNQDDLEDDDVFLLDTWDQVFFWIGEHANETEKKEAAVMAQEYLRTHPSGRD-PDTPIIV 632
Cdd:cd11291     2 PRLFRCSNESGFFKVEEISDFSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYIETDPLGRSkPRTPIYL 81

                          90
                  ....*....|....*...
gi 1820722642 633 VKQGYEPPTFTGWFLAWD 650
Cdd:cd11291    82 VKQGNEPPTFTGYFHAWD 99
gelsolin_S1_like cd11290
Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; ...
 17-85 3.26e-32

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: 120.79  E-value: 3.26e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820722642  17 PGLQIWRIEKMEMVLVPPKSYGNFYEGDCYVLLATHKTG-NSFRYDIHYWLGRESSQDEQGAAAIYTTQI 85
Cdd:cd11290     8 PGLQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDPsGSLSYDIHYWLGKEASQDEAGAAAIKAVEL 77
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 185-280 5.83e-30

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: 113.88  E-value: 5.83e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820722642 185 KLYK*ClDAEGNLVIQEVATRP*TQDLLQHEDCYILDQGgSTIYVWKG*KSTKEEKQQAMSRALGFIKAKDYSPSTAWQT 264
Cdd:cd11292     5 KLYKVS-DASGKLKLTEVAEGSLNQEMLDSEDCYILDCG-SEIFVWVGKGASLDERKAALKNAEEFLRKKKRPPYTQVTR 82

                          90
                  ....*....|....*.
gi 1820722642 265 RTTG*ESAMFKQLFQK 280
Cdd:cd11292    83 VTEGGESALFKSKFAN 98
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 453-536 1.82e-25

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 100.83  E-value: 1.82e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820722642  453 FHVHGTNEYNTKAIEVPPRASSLNSNDVFVLKTQACCYLWYGKGCSGDEREMAKTVADLI------TKTEKLVIAEGQEP 526
Cdd:smart00262   1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELddtlgpGPVQVRVVDEGKEP 80

                           90
                   ....*....|
gi 1820722642  527 DNFWVALGGK 536
Cdd:smart00262  81 PEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 558-649 2.75e-24

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: 97.36  E-value: 2.75e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820722642  558 ECSNQTGTFVATEIT-DFNQDDLEDDDVFLLDTWDQVFFWIGEHANETEKKEAAVMAQEYLRTHPSGRdpdTPIIVVKQG 636
Cdd:smart00262   1 FLVRVKGKRNVRVPEvPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGP---VQVRVVDEG 77

                           90
                   ....*....|...
gi 1820722642  637 YEPPTFTGWFLAW 649
Cdd:smart00262  78 KEPPEFWSLFGGW 90
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 80-137 5.22e-24

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: 96.54  E-value: 5.22e-24
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1820722642  80 IYTTQiVEMSWNSFNQGDVFLLDLGKLIIQWNGPESNRAERLKGINLAKDIRDRERGG 137
Cdd:cd11289    13 VRARE-VELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLG 69
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
 19-88 3.85e-22

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: 91.56  E-value: 3.85e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820722642  19 LQIWRIEKMEMVLVPPKSYGNFYEGDCYVLLATHKTGNSFRYDIHYWLGRESSQDEQGAAAIYTTQIVEM 88
Cdd:cd11293     9 VEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTYQGGGKEEHILYFWQGRHSSQDERAAAALLTVELDEE 78
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 551-646 1.01e-21

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: 90.39  E-value: 1.01e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820722642 551 SITPRLFECSNQTGTFVATEITD--FNQDDLEDDDVFLLDTWDQVFFWIGEHANETEKKEAAVMAQEYLRTHpsGRDPDT 628
Cdd:cd11292     1 AEQKKLYKVSDASGKLKLTEVAEgsLNQEMLDSEDCYILDCGSEIFVWVGKGASLDERKAALKNAEEFLRKK--KRPPYT 78

                          90
                  ....*....|....*...
gi 1820722642 629 PIIVVKQGYEPPTFTGWF 646
Cdd:cd11292    79 QVTRVTEGGESALFKSKF 96
gelsolin_S1_like cd11290
Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; ...
 335-437 2.93e-20

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: 86.51  E-value: 2.93e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820722642 335 VEVWRIEDLELAPVDMRWLGHFYGGDCYLILYKYLV-NNKQHYIIYIWQGRHASKDEITASAYQAVILDQQYDNAAVQVR 413
Cdd:cd11290    10 LQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDpSGSLSYDIHYWLGKEASQDEAGAAAIKAVELDDYLGGRPVQHR 89

                          90       100
                  ....*....|....*....|....
gi 1820722642 414 VPMGKEPAHLMAIFKgKMVVYAGG 437
Cdd:cd11290    90 EVQGHESEEFLSYFK-KGIIYIEG 112
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 336-430 5.99e-20

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: 85.04  E-value: 5.99e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820722642  336 EVWRIED---LELAPVDMRWlGHFYGGDCYLILYkylvnnkqHYIIYIWQGRHASKDEITASAYQAVILDQQYDNAAVQV 412
Cdd:smart00262   1 FLVRVKGkrnVRVPEVPFSQ-GSLNSGDCYILDT--------GSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQV 71

                           90
                   ....*....|....*....
gi 1820722642  413 R-VPMGKEPAHLMAIFKGK 430
Cdd:smart00262  72 RvVDEGKEPPEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 190-281 5.24e-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: 76.56  E-value: 5.24e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820722642  190 CLDAEGNLVIqEVATRP*TQDLLQHEDCYILDQGgSTIYVWKG*KSTKEEKQQAMSRALGFIKaKDYSPSTAWQTRTTG* 269
Cdd:smart00262   2 LVRVKGKRNV-RVPEVPFSQGSLNSGDCYILDTG-SEIYVWVGKKSSQDEKKKAAELAVELDD-TLGPGPVQVRVVDEGK 78

                           90
                   ....*....|..
gi 1820722642  270 ESAMFKQLFQKW 281
Cdd:smart00262  79 EPPEFWSLFGGW 90
Gelsolin pfam00626
Gelsolin repeat;
565-642 5.88e-17

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 75.81  E-value: 5.88e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820722642 565 TFVATEITDFNQDDLEDDDVFLLDTWDQVFFWIGEHANETEKKEAAVMAQEYLRTHpsgRDPDTPIIVVKQGYEPPTF 642
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDE---RFPLPEVIRVPQGKEPARF 75
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 554-646 2.23e-16

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: 74.71  E-value: 2.23e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820722642 554 PRLFECSNQTGTFVATEITDFNqdDLEDDDVFLLDTWDQVFFWIGEHANETEKKEAAVMAQEYLRThpsgRDPDTPIIVV 633
Cdd:cd11280     2 PRLYRVRGSKAIEIEEVPLASS--SLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKELDEE----RKGKPEIVRI 75

                          90
                  ....*....|...
gi 1820722642 634 KQGYEPPTFTGWF 646
Cdd:cd11280    76 RQGQEPREFWSLF 88
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 450-534 6.83e-16

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: 73.43  E-value: 6.83e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820722642 450 TRLFHVHGtnEYNTKAIEVPPRASSLNSNDVFVLKTQACCYLWYGKGCSGDEREMAKTVADLI--------TKTEKLVIA 521
Cdd:cd11289     2 PRLLHVKG--RRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIrderrlgrAKVIVLDEG 79

                          90
                  ....*....|...
gi 1820722642 522 EGQEPDNFWVALG 534
Cdd:cd11289    80 DTNESPEFWKVLG 92
VHP pfam02209
Villin headpiece domain;
725-760 7.11e-14

Villin headpiece domain;


Pssm-ID: 460493  Cd Length: 36  Bit Score: 65.86  E-value: 7.11e-14
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1820722642 725 HLSGDDFNTVFGMPQTAFAALPLWKQQKLKKEKGLF 760
Cdd:pfam02209   1 YLSDEDFEEVFGMSREEFYKLPKWKQNNLKKKAGLF 36
Gelsolin pfam00626
Gelsolin repeat;
344-424 1.68e-13

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 66.18  E-value: 1.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820722642 344 ELAPVDMRWLGHFYGGDCYLILykylvnnkQHYIIYIWQGRHASKDEITASAYQAV-ILDQQYDNAAVQVRVPMGKEPAH 422
Cdd:pfam00626   3 VLPPPVPLSQESLNSGDCYLLD--------NGFTIFLWVGKGSSLLEKLFAALLAAqLDDDERFPLPEVIRVPQGKEPAR 74


                  ..
gi 1820722642 423 LM 424
Cdd:pfam00626  75 FL 76
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 20-88 5.47e-13

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 65.01  E-value: 5.47e-13
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820722642   20 QIWRIEKMEMVLVP--PKSYGNFYEGDCYVLLATHktgnsfryDIHYWLGRESSQDEQGAAAIYTTQIVEM 88
Cdd:smart00262   1 FLVRVKGKRNVRVPevPFSQGSLNSGDCYILDTGS--------EIYVWVGKKSSQDEKKKAAELAVELDDT 63
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 449-530 3.42e-12

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


Pssm-ID: 200436  Cd Length: 88  Bit Score: 62.77  E-value: 3.42e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820722642 449 STRLFHVHGTNeyNTKAIEVPPRASSLNSNDVFVLKTQACCYLWYGKGCSGDEREMAKTVADLITKTEK-----LVIAEG 523
Cdd:cd11280     1 PPRLYRVRGSK--AIEIEEVPLASSSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKELDEERKgkpeiVRIRQG 78


                  ....*..
gi 1820722642 524 QEPDNFW 530
Cdd:cd11280    79 QEPREFW 85
Gelsolin pfam00626
Gelsolin repeat;
84-139 3.45e-12

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 62.33  E-value: 3.45e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1820722642  84 QIVEMSWNSFNQGDVFLLDLGKLIIQWNGPESNRAERLKGINLAKDIRDRERGGVP 139
Cdd:pfam00626   6 PPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDERFPLP 61
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 86-137 5.73e-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: 62.31  E-value: 5.73e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1820722642   86 VEMSWNSFNQGDVFLLDLGKLIIQWNGPESNRAERLKGINLAKDIRDRERGG 137
Cdd:smart00262  16 VPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPG 67
VHP smart00153
Villin headpiece domain;
725-760 5.85e-12

Villin headpiece domain;


Pssm-ID: 128458  Cd Length: 36  Bit Score: 60.41  E-value: 5.85e-12
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1820722642  725 HLSGDDFNTVFGMPQTAFAALPLWKQQKLKKEKGLF 760
Cdd:smart00153   1 YLSDEDFEEVFGMTREEFYKLPLWKQNQLKKKKGLF 36
Gelsolin pfam00626
Gelsolin repeat;
198-275 1.23e-11

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 60.78  E-value: 1.23e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820722642 198 VIQEVATRP*TQDLLQHEDCYILDQGgSTIYVWKG*KSTKEEKQQAMSRALGFIKaKDYSPSTAWQTRTTG*ESAMFK 275
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNG-FTIFLWVGKGSSLLEKLFAALLAAQLDD-DERFPLPEVIRVPQGKEPARFL 76
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 337-427 1.24e-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: 61.23  E-value: 1.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820722642 337 VWRIED---LELAPVDMRwLGHFYGGDCYLILYKYlvnnkqhyIIYIWQGRHASKDEITASAYQAVILDQQYDNAAVQVR 413
Cdd:cd11280     4 LYRVRGskaIEIEEVPLA-SSSLDSDDVFVLDTGS--------EIYIWQGRASSQAELAAAALLAKELDEERKGKPEIVR 74

                          90
                  ....*....|....
gi 1820722642 414 VPMGKEPAHLMAIF 427
Cdd:cd11280    75 IRQGQEPREFWSLF 88
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 190-281 5.68e-11

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: 59.62  E-value: 5.68e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820722642 190 CLDAEGNLVIQEVAtrP*TQDLLQHEDCYILDQGgSTIYVWKG*KSTKEEKQQAMSRALGFIK---AKDYSPSTAWQTRT 266
Cdd:cd11291     7 CSNESGFFKVEEIS--DFSQDDLDTDDIMLLDTG-DEVFVWVGSESSDEEKKEALTSAKKYIEtdpLGRSKPRTPIYLVK 83

                          90
                  ....*....|....*
gi 1820722642 267 TG*ESAMFKQLFQKW 281
Cdd:cd11291    84 QGNEPPTFTGYFHAW 98
Gelsolin pfam00626
Gelsolin repeat;
26-85 3.21e-10

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 56.93  E-value: 3.21e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820722642  26 KMEMVLVPPKSYGNFYEGDCYVLLAThktgnsfrYDIHYWLGRESSQDEQGAAAIYTTQI 85
Cdd:pfam00626   1 KFVLPPPVPLSQESLNSGDCYLLDNG--------FTIFLWVGKGSSLLEKLFAALLAAQL 52
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 20-88 5.96e-10

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: 56.61  E-value: 5.96e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820722642  20 QIWRIEK---MEMVLVPPKSYgNFYEGDCYVLLathktgnsFRYDIHYWLGRESSQDEQGAAAIYTTQIVEM 88
Cdd:cd11280     3 RLYRVRGskaIEIEEVPLASS-SLDSDDVFVLD--------TGSEIYIWQGRASSQAELAAAALLAKELDEE 65
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 447-529 5.12e-07

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: 48.40  E-value: 5.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820722642 447 VPSTRLFHVH-GTNEYNTKAIEVPPRASS-LNSNDVFVLKTQACCYLWYGKGCSGDEREMA-KTVADLITKTEK------ 517
Cdd:cd11292     1 AEQKKLYKVSdASGKLKLTEVAEGSLNQEmLDSEDCYILDCGSEIFVWVGKGASLDERKAAlKNAEEFLRKKKRppytqv 80

                          90
                  ....*....|..
gi 1820722642 518 LVIAEGQEPDNF 529
Cdd:cd11292    81 TRVTEGGESALF 92
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 212-255 1.85e-06

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: 46.46  E-value: 1.85e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1820722642 212 LQHEDCYILDQGgSTIYVWKG*KSTKEEKQQAMSRALGfIKAKD 255
Cdd:cd11289    25 LNSGDVFILDLG-STIYQWNGSKSNRFEKAKAMQLAQG-IRDER 66
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 193-278 2.38e-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: 2.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820722642 193 AEGNLVIQEVATRP*tqDLLQHEDCYILDQGgSTIYVWKG*KSTKEEKQQAMSRALGFIKAkdYSPSTAWQTRTTG*ESA 272
Cdd:cd11280     9 GSKAIEIEEVPLAS---SSLDSDDVFVLDTG-SEIYIWQGRASSQAELAAAALLAKELDEE--RKGKPEIVRIRQGQEPR 82


                  ....*.
gi 1820722642 273 MFKQLF 278
Cdd:cd11280    83 EFWSLF 88
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 554-642 3.63e-05

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: 42.99  E-value: 3.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820722642 554 PRLFECSNQTgTFVATEItDFNQDDLEDDDVFLLDTWDQVFFWIGEHANETEKKEAAVMAQeYLRTHPSGRDPDTPIIVV 633
Cdd:cd11289     2 PRLLHVKGRR-NVRAREV-ELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQ-GIRDERRLGRAKVIVLDE 78


                  ....*....
gi 1820722642 634 KQGYEPPTF 642
Cdd:cd11289    79 GDTNESPEF 87
Gelsolin pfam00626
Gelsolin repeat;
462-530 6.98e-05

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 41.52  E-value: 6.98e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820722642 462 NTKAIEVPPRASSLNSNDVFVLKTQACCYLWYGKGCSGDEREMAKTVA------DLITKTEKLVIAEGQEPDNFW 530
Cdd:pfam00626   2 FVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAaqldddERFPLPEVIRVPQGKEPARFL 76
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 91-139 1.04e-04

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: 41.58  E-value: 1.04e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1820722642  91 NSFNQGDVFLLDLGKLIIQWNGPESNRAERLKGINLAKDIrDRERGGVP 139
Cdd:cd11280    23 SSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKEL-DEERKGKP 70
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
 216-278 2.35e-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: 38.02  E-value: 2.35e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820722642 216 DCYIL----DQGGST---IYVWKG*KSTKEEKQQAMSRALGFIKAKDYSPStawQTRTT-G*ESAMFKQLF 278
Cdd:cd11293    34 DCYIVlytyQGGGKEehiLYFWQGRHSSQDERAAAALLTVELDEELKGRAV---QVRVVqGKEPPHFLALF 101
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 216-274 5.01e-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: 36.83  E-value: 5.01e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1820722642 216 DCYILdQGGSTIYVWKG*KSTKEEKQQAMSRalgfikAKDYSPSTAWQTRTTG*ESAMF 274
Cdd:cd11288    32 DVFVL-KTPSSVYLWVGKGSSEDERELAKDV------ASFLKPKASLQEVAEGSEPDEF 83
 
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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