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Conserved domains on  [gi|372266129|ref|NP_001243194|]
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protein flightless-1 homolog isoform 3 [Homo sapiens]

Protein Classification

flightless-1 family protein( domain architecture ID 11469395)

flightless-1 family protein such as flightless I (FliI), which is an actin-remodelling protein as well as a nuclear receptor co-activator with ability to interact with various other proteins important in cellular signaling

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
gelsolin_S1_like cd11290
Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; ...
 437-549 2.05e-61

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: 204.76  E-value: 2.05e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129  437 TEDVGQLPGLTIWQIENFVPVLVEEAFHGKFYEADCYIVLKTFLDDSGSLNWEIYYWIGGEATLDKKACSAIHAVNLRNY 516
Cdd:cd11290     1 FEGVGQKPGLQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDPSGSLSYDIHYWLGKEASQDEAGAAAIKAVELDDY 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 372266129  517 LGAECRTVREEMGDESEEFLQVFDNDISYIEGG 549
Cdd:cd11290    81 LGGRPVQHREVQGHESEEFLSYFKKGIIYIEGG 113
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 1108-1207 1.18e-47

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: 164.78  E-value: 1.18e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129 1108 HTRLFRCSNEKGYFaVTEKCSDFCQDDLADDDIMLLDNGQEVYMWVGTQTSQVEIKLSLKACQVYIQHMRSKEHERPRRL 1187
Cdd:cd11291     1 KPRLFRCSNESGFF-KVEEISDFSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYIETDPLGRSKPRTPI 79

                          90       100
                  ....*....|....*....|
gi 372266129 1188 RLVRKGNEQHAFTRCFHAWS 1207
Cdd:cd11291    80 YLVKQGNEPPTFTGYFHAWD 99
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
7-321 5.33e-38

Leucine-rich repeat (LRR) protein [Transcription];


:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 148.16  E-value: 5.33e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129    7 LPFVRGVDLSGNdfkggyfpENVKAMTSLRWLKLNRTGLCYLPEELAALQKLEHLSVSHNNLTTLHGELSSLPSLRAIVA 86
Cdd:COG4886    95 LTNLTELDLSGN--------EELSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLPEPLGNLTNLKSLDL 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129   87 RANSLknSGVPDDIFKLDDLSVLDLSHNQLTECPRELENAKNMLVLNLSHNR------QLPAMTALQTLHLRSTQRTqsN 160
Cdd:COG4886   167 SNNQL--TDLPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLEELDLSGNQltdlpePLANLTNLETLDLSNNQLT--D 242

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129  161 LPtSLEGLSNLADVDLSCNDLTRVPEcLYTLPSLRRLNLSSNQITELSLCIDQwvhvETLNLSRNQLTSLPSAICKLSKL 240
Cdd:COG4886   243 LP-ELGNLTNLEELDLSNNQLTDLPP-LANLTNLKTLDLSNNQLTDLKLKELE----LLLGLNSLLLLLLLLNLLELLIL 316

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129  241 KKLYLNSNKLDFDGLPSGIGKLTNLEEFMAANNNLELVPESLCRCPKLRKLVLNKNHLVTLPEAIHFLTEIEVLDVRENP 320
Cdd:COG4886   317 LLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGLLEATLLTLALLLLTLLLLLLTT 396


                  .
gi 372266129  321 N 321
Cdd:COG4886   397 T 397
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 998-1097 5.20e-36

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: 131.58  E-value: 5.20e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129  998 QPSLYQIRTNGSaLCTRCIQINTDSSLLNSEFCFILKVPFesednqgIVYAWVGRASDPDEAKLAEDILNTMFDtSYSKQ 1077
Cdd:cd11288     2 PTRLFQVRGNGS-GNTRAVEVDADASSLNSNDVFVLKTPS-------SVYLWVGKGSSEDERELAKDVASFLKP-KASLQ 72

                          90       100
                  ....*....|....*....|
gi 372266129 1078 VINEGEEPENFFWVGIGAQK 1097
Cdd:cd11288    73 EVAEGSEPDEFWEALGGKSE 92
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 668-782 1.62e-32

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: 121.59  E-value: 1.62e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129  668 PPQPKLYKVGLGLGYLELPQINYKLsvehkqrpkvelmprmrLLQSLLDTRCVYILDCWSDVFIWLGRKSPRLVRAAALK 747
Cdd:cd11292     1 AEQKKLYKVSDASGKLKLTEVAEGS-----------------LNQEMLDSEDCYILDCGSEIFVWVGKGASLDERKAALK 63

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 372266129  748 LGQELCGMLHRPRHATVSRSLEGTEAQVFKAKFKN 782
Cdd:cd11292    64 NAEEFLRKKKRPPYTQVTRVTEGGESALFKSKFAN 98
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 564-651 2.52e-28

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: 109.38  E-value: 2.52e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129  564 TRMYRVYGKKNIKLEPVPLKGTSLDPRFVFLLDRGLDIYVWRGAQATLSSTTKARLFAEKINKnERKGKAEITLLVQGQE 643
Cdd:cd11280     2 PRLYRVRGSKAIEIEEVPLASSSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKELDE-ERKGKPEIVRIRQGQE 80


                  ....*...
gi 372266129  644 LPEFWEAL 651
Cdd:cd11280    81 PREFWSLF 88
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 919-979 1.24e-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: 81.65  E-value: 1.24e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 372266129  919 KQPEEDFQCIVYFWQGReASNMGWLTFTFSLQKKFESLFPGKLEVVRMTQQQENPKFLSHF 979
Cdd:cd11280    29 DVFVLDTGSEIYIWQGR-ASSQAELAAAALLAKELDEERKGKPEIVRIRQGQEPREFWSLF 88
 
Name Accession Description Interval E-value
gelsolin_S1_like cd11290
Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; ...
 437-549 2.05e-61

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: 204.76  E-value: 2.05e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129  437 TEDVGQLPGLTIWQIENFVPVLVEEAFHGKFYEADCYIVLKTFLDDSGSLNWEIYYWIGGEATLDKKACSAIHAVNLRNY 516
Cdd:cd11290     1 FEGVGQKPGLQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDPSGSLSYDIHYWLGKEASQDEAGAAAIKAVELDDY 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 372266129  517 LGAECRTVREEMGDESEEFLQVFDNDISYIEGG 549
Cdd:cd11290    81 LGGRPVQHREVQGHESEEFLSYFKKGIIYIEGG 113
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 1108-1207 1.18e-47

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: 164.78  E-value: 1.18e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129 1108 HTRLFRCSNEKGYFaVTEKCSDFCQDDLADDDIMLLDNGQEVYMWVGTQTSQVEIKLSLKACQVYIQHMRSKEHERPRRL 1187
Cdd:cd11291     1 KPRLFRCSNESGFF-KVEEISDFSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYIETDPLGRSKPRTPI 79

                          90       100
                  ....*....|....*....|
gi 372266129 1188 RLVRKGNEQHAFTRCFHAWS 1207
Cdd:cd11291    80 YLVKQGNEPPTFTGYFHAWD 99
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
7-321 5.33e-38

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 148.16  E-value: 5.33e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129    7 LPFVRGVDLSGNdfkggyfpENVKAMTSLRWLKLNRTGLCYLPEELAALQKLEHLSVSHNNLTTLHGELSSLPSLRAIVA 86
Cdd:COG4886    95 LTNLTELDLSGN--------EELSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLPEPLGNLTNLKSLDL 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129   87 RANSLknSGVPDDIFKLDDLSVLDLSHNQLTECPRELENAKNMLVLNLSHNR------QLPAMTALQTLHLRSTQRTqsN 160
Cdd:COG4886   167 SNNQL--TDLPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLEELDLSGNQltdlpePLANLTNLETLDLSNNQLT--D 242

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129  161 LPtSLEGLSNLADVDLSCNDLTRVPEcLYTLPSLRRLNLSSNQITELSLCIDQwvhvETLNLSRNQLTSLPSAICKLSKL 240
Cdd:COG4886   243 LP-ELGNLTNLEELDLSNNQLTDLPP-LANLTNLKTLDLSNNQLTDLKLKELE----LLLGLNSLLLLLLLLNLLELLIL 316

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129  241 KKLYLNSNKLDFDGLPSGIGKLTNLEEFMAANNNLELVPESLCRCPKLRKLVLNKNHLVTLPEAIHFLTEIEVLDVRENP 320
Cdd:COG4886   317 LLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGLLEATLLTLALLLLTLLLLLLTT 396


                  .
gi 372266129  321 N 321
Cdd:COG4886   397 T 397
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 998-1097 5.20e-36

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: 131.58  E-value: 5.20e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129  998 QPSLYQIRTNGSaLCTRCIQINTDSSLLNSEFCFILKVPFesednqgIVYAWVGRASDPDEAKLAEDILNTMFDtSYSKQ 1077
Cdd:cd11288     2 PTRLFQVRGNGS-GNTRAVEVDADASSLNSNDVFVLKTPS-------SVYLWVGKGSSEDERELAKDVASFLKP-KASLQ 72

                          90       100
                  ....*....|....*....|
gi 372266129 1078 VINEGEEPENFFWVGIGAQK 1097
Cdd:cd11288    73 EVAEGSEPDEFWEALGGKSE 92
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 668-782 1.62e-32

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: 121.59  E-value: 1.62e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129  668 PPQPKLYKVGLGLGYLELPQINYKLsvehkqrpkvelmprmrLLQSLLDTRCVYILDCWSDVFIWLGRKSPRLVRAAALK 747
Cdd:cd11292     1 AEQKKLYKVSDASGKLKLTEVAEGS-----------------LNQEMLDSEDCYILDCGSEIFVWVGKGASLDERKAALK 63

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 372266129  748 LGQELCGMLHRPRHATVSRSLEGTEAQVFKAKFKN 782
Cdd:cd11292    64 NAEEFLRKKKRPPYTQVTRVTEGGESALFKSKFAN 98
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 564-651 2.52e-28

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: 109.38  E-value: 2.52e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129  564 TRMYRVYGKKNIKLEPVPLKGTSLDPRFVFLLDRGLDIYVWRGAQATLSSTTKARLFAEKINKnERKGKAEITLLVQGQE 643
Cdd:cd11280     2 PRLYRVRGSKAIEIEEVPLASSSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKELDE-ERKGKPEIVRIRQGQE 80


                  ....*...
gi 372266129  644 LPEFWEAL 651
Cdd:cd11280    81 PREFWSLF 88
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 565-653 1.24e-23

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 96.21  E-value: 1.24e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129    565 RMYRVYGKKNIKLEPVPLKGTSLDPRFVFLLDRGLDIYVWRGAQATLSSTTKARLFAEKINKNERKGKAEITLLVQGQEL 644
Cdd:smart00262    1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVRVVDEGKEP 80


                    ....*....
gi 372266129    645 PEFWEALGG 653
Cdd:smart00262   81 PEFWSLFGG 89
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1113-1206 3.13e-23

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 95.05  E-value: 3.13e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129   1113 RCSNEKGYFAVTEKCSDFCQDDLADDDIMLLDNGQEVYMWVGTQTSQVEIKLSLKACQVYIQHMRSkeheRPRRLRLVRK 1192
Cdd:smart00262    1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGP----GPVQVRVVDE 76

                            90
                    ....*....|....
gi 372266129   1193 GNEQHAFTRCFHAW 1206
Cdd:smart00262   77 GKEPPEFWSLFGGW 90
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 7-298 1.82e-22

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 104.54  E-value: 1.82e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129    7 LPFVRGVDLSGNDFKGGyFPENV-KAMTSLRWLKL---NRTGlcylPEELAALQKLEHLSVSHNNLT-TLHGELSSLPSL 81
Cdd:PLN00113   92 LPYIQTINLSNNQLSGP-IPDDIfTTSSSLRYLNLsnnNFTG----SIPRGSIPNLETLDLSNNMLSgEIPNDIGSFSSL 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129   82 RAIVARANSLKNSgVPDDIFKLDDLSVLDLSHNQLT-ECPRELENAKNMLVLNLSHN-------RQLPAMTALQTLHLRS 153
Cdd:PLN00113  167 KVLDLGGNVLVGK-IPNSLTNLTSLEFLTLASNQLVgQIPRELGQMKSLKWIYLGYNnlsgeipYEIGGLTSLNHLDLVY 245

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129  154 TQRTQSnLPTSLEGLSNLADVDLSCNDLT-RVPECLYTLPSLRRLNLSSNQIT-ELSLCIDQWVHVETLNLSRNQLT-SL 230
Cdd:PLN00113  246 NNLTGP-IPSSLGNLKNLQYLFLYQNKLSgPIPPSIFSLQKLISLDLSDNSLSgEIPELVIQLQNLEILHLFSNNFTgKI 324

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 372266129  231 PSAICKLSKLKKLYLNSNKLDfDGLPSGIGKLTNLEEFMAANNNLE-LVPESLCRCPKLRKLVLNKNHL 298
Cdd:PLN00113  325 PVALTSLPRLQVLQLWSNKFS-GEIPKNLGKHNNLTVLDLSTNNLTgEIPEGLCSSGNLFKLILFSNSL 392
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 919-979 1.24e-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: 81.65  E-value: 1.24e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 372266129  919 KQPEEDFQCIVYFWQGReASNMGWLTFTFSLQKKFESLFPGKLEVVRMTQQQENPKFLSHF 979
Cdd:cd11280    29 DVFVLDTGSEIYIWQGR-ASSQAELAAAALLAKELDEERKGKPEIVRIRQGQEPREFWSLF 88
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 696-783 2.69e-18

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: 80.80  E-value: 2.69e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129    696 HKQRPKVELMPRMRLLQSLLDTRCVYILDCWSDVFIWLGRKSPRLVRAAALKLGQELCGMLHrPRHATVSRSLEGTEAQV 775
Cdd:smart00262    4 RVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLG-PGPVQVRVVDEGKEPPE 82


                    ....*...
gi 372266129    776 FKAKFKNW 783
Cdd:smart00262   83 FWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 448-541 6.40e-18

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: 79.64  E-value: 6.40e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129    448 IWQIENFVPVLVEE--AFHGKFYEADCYIVLKTflddsgslnWEIYYWIGGEATLDKKACSAIHAVNLRNYLGAECRTVR 525
Cdd:smart00262    2 LVRVKGKRNVRVPEvpFSQGSLNSGDCYILDTG---------SEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVR 72

                            90
                    ....*....|....*..
gi 372266129    526 E-EMGDESEEFLQVFDN 541
Cdd:smart00262   73 VvDEGKEPPEFWSLFGG 89
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1002-1094 7.12e-16

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 73.87  E-value: 7.12e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129   1002 YQIRTNGSaLCTRCIQINTDSSLLNSEFCFILkvpfeseDNQGIVYAWVGRASDPDEAKLAEDILNTMFDTSYSK----Q 1077
Cdd:smart00262    1 FLVRVKGK-RNVRVPEVPFSQGSLNSGDCYIL-------DTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGpvqvR 72

                            90
                    ....*....|....*..
gi 372266129   1078 VINEGEEPENFFWVGIG 1094
Cdd:smart00262   73 VVDEGKEPPEFWSLFGG 89
Gelsolin pfam00626
Gelsolin repeat;
573-648 2.02e-14

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 69.26  E-value: 2.02e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 372266129   573 KNIKLEPVPLKGTSLDPRFVFLLDRGLDIYVWRGAQATLSSTTKARLFAEKINKNERKGKAEITLLVQGQELPEFW 648
Cdd:pfam00626    1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDERFPLPEVIRVPQGKEPARFL 76
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 55-231 7.94e-14

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 72.13  E-value: 7.94e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129   55 LQKLEHLSVSHNNLTTLhGELSSLPSLRAIVARANSLKNSgvpDDIFKLDDLSVLDLSHNQLTECPrELENAKNMLVLNL 134
Cdd:cd21340     1 LKRITHLYLNDKNITKI-DNLSLCKNLKVLYLYDNKITKI---ENLEFLTNLTHLYLQNNQIEKIE-NLENLVNLKKLYL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129  135 SHNR-----QLPAMTALQTLHLrSTQRTQSNL-----PTSLEGLSN-LADVDLSCNDLTRVpECLYTLPSLRRLNLSSNQ 203
Cdd:cd21340    76 GGNRisvveGLENLTNLEELHI-ENQRLPPGEkltfdPRSLAALSNsLRVLNISGNNIDSL-EPLAPLRNLEQLDASNNQ 153

                         170       180       190
                  ....*....|....*....|....*....|.
gi 372266129  204 IT---ELSLCIDQWVHVETLNLSRNQLTSLP 231
Cdd:cd21340   154 ISdleELLDLLSSWPSLRELDLTGNPVCKKP 184
Gelsolin pfam00626
Gelsolin repeat;
453-536 1.44e-12

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 63.87  E-value: 1.44e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129   453 NFVPVLVEEAFHGKFYEADCYIVLKTFlddsgslnwEIYYWIGGEATLDKKACSAIHAVNLR-NYLGAECRTVREEMGDE 531
Cdd:pfam00626    1 KFVLPPPVPLSQESLNSGDCYLLDNGF---------TIFLWVGKGSSLLEKLFAALLAAQLDdDERFPLPEVIRVPQGKE 71


                   ....*
gi 372266129   532 SEEFL 536
Cdd:pfam00626   72 PARFL 76
LRR_8 pfam13855
Leucine rich repeat;
169-227 3.31e-08

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 50.99  E-value: 3.31e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 372266129   169 SNLADVDLSCNDLTRV-PECLYTLPSLRRLNLSSNQITELSL-CIDQWVHVETLNLSRNQL 227
Cdd:pfam13855    1 PNLRSLDLSNNRLTSLdDGAFKGLSNLKVLDLSNNLLTTLSPgAFSGLPSLRYLDLSGNRL 61
Gelsolin pfam00626
Gelsolin repeat;
1126-1199 1.68e-07

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 49.61  E-value: 1.68e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 372266129  1126 KCSDFCQDDLADDDIMLLDNGQEVYMWVGTQTSQVEIklslKACQVYIQHMRSKEHERPRRLRLVRKGNEQHAF 1199
Cdd:pfam00626    6 PPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEK----LFAALLAAQLDDDERFPLPEVIRVPQGKEPARF 75
Gelsolin pfam00626
Gelsolin repeat;
701-777 3.96e-06

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 45.76  E-value: 3.96e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 372266129   701 KVELMPRMRLLQSLLDTRCVYILDCWSDVFIWLGRKSPRLVRAAALKLGQELcGMLHRPRHATVSRSLEGTEAQVFK 777
Cdd:pfam00626    1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQL-DDDERFPLPEVIRVPQGKEPARFL 76
Gelsolin pfam00626
Gelsolin repeat;
1021-1088 1.23e-05

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 44.22  E-value: 1.23e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 372266129  1021 DSSLLNSEFCFILkvpfeseDNQGIVYAWVGRASDPDE----AKLAEDILNTMFDTSYSKQVINEGEEPENF 1088
Cdd:pfam00626   11 SQESLNSGDCYLL-------DNGFTIFLWVGKGSSLLEklfaALLAAQLDDDERFPLPEVIRVPQGKEPARF 75
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 858-980 2.62e-04

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: 41.12  E-value: 2.62e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129    858 EGKKFARLPEEEF--GHFYTQDCYVFLCRYwvpveyeeeekkedkeekaegkegeeataeaeekqpeedfqcIVYFWQGR 935
Cdd:smart00262    6 KGKRNVRVPEVPFsqGSLNSGDCYILDTGS------------------------------------------EIYVWVGK 43

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*
gi 372266129    936 EASNMGWLTFTFSLQKKFESLFPGKLEVVRMTQQQENPKFLSHFK 980
Cdd:smart00262   44 KSSQDEKKKAAELAVELDDTLGPGPVQVRVVDEGKEPPEFWSLFG 88
 
Name Accession Description Interval E-value
gelsolin_S1_like cd11290
Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; ...
 437-549 2.05e-61

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: 204.76  E-value: 2.05e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129  437 TEDVGQLPGLTIWQIENFVPVLVEEAFHGKFYEADCYIVLKTFLDDSGSLNWEIYYWIGGEATLDKKACSAIHAVNLRNY 516
Cdd:cd11290     1 FEGVGQKPGLQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDPSGSLSYDIHYWLGKEASQDEAGAAAIKAVELDDY 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 372266129  517 LGAECRTVREEMGDESEEFLQVFDNDISYIEGG 549
Cdd:cd11290    81 LGGRPVQHREVQGHESEEFLSYFKKGIIYIEGG 113
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 1108-1207 1.18e-47

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: 164.78  E-value: 1.18e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129 1108 HTRLFRCSNEKGYFaVTEKCSDFCQDDLADDDIMLLDNGQEVYMWVGTQTSQVEIKLSLKACQVYIQHMRSKEHERPRRL 1187
Cdd:cd11291     1 KPRLFRCSNESGFF-KVEEISDFSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYIETDPLGRSKPRTPI 79

                          90       100
                  ....*....|....*....|
gi 372266129 1188 RLVRKGNEQHAFTRCFHAWS 1207
Cdd:cd11291    80 YLVKQGNEPPTFTGYFHAWD 99
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
7-321 5.33e-38

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 148.16  E-value: 5.33e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129    7 LPFVRGVDLSGNdfkggyfpENVKAMTSLRWLKLNRTGLCYLPEELAALQKLEHLSVSHNNLTTLHGELSSLPSLRAIVA 86
Cdd:COG4886    95 LTNLTELDLSGN--------EELSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLPEPLGNLTNLKSLDL 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129   87 RANSLknSGVPDDIFKLDDLSVLDLSHNQLTECPRELENAKNMLVLNLSHNR------QLPAMTALQTLHLRSTQRTqsN 160
Cdd:COG4886   167 SNNQL--TDLPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLEELDLSGNQltdlpePLANLTNLETLDLSNNQLT--D 242

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129  161 LPtSLEGLSNLADVDLSCNDLTRVPEcLYTLPSLRRLNLSSNQITELSLCIDQwvhvETLNLSRNQLTSLPSAICKLSKL 240
Cdd:COG4886   243 LP-ELGNLTNLEELDLSNNQLTDLPP-LANLTNLKTLDLSNNQLTDLKLKELE----LLLGLNSLLLLLLLLNLLELLIL 316

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129  241 KKLYLNSNKLDFDGLPSGIGKLTNLEEFMAANNNLELVPESLCRCPKLRKLVLNKNHLVTLPEAIHFLTEIEVLDVRENP 320
Cdd:COG4886   317 LLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGLLEATLLTLALLLLTLLLLLLTT 396


                  .
gi 372266129  321 N 321
Cdd:COG4886   397 T 397
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
16-320 6.44e-38

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 147.77  E-value: 6.44e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129   16 SGNDFKGGYFPENVKAMTSLRWLKLNRTGLCYLPEELAALQKLEHLSVSHNNLTTLHGELSSLPSLRAIVARANSLK--N 93
Cdd:COG4886    23 TLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTelD 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129   94 SGVPDDIFKLDDLSVLDLSHNQLTECPRELENAKNMLVLNLSHNrQLpamtalqtlhlrstqrtqSNLPTSLEGLSNLAD 173
Cdd:COG4886   103 LSGNEELSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNN-QL------------------TDLPEPLGNLTNLKS 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129  174 VDLSCNDLTRVPECLYTLPSLRRLNLSSNQITELSLCIDQWVHVETLNLSRNQLTSLPSAicklsklkklylnsnkldfd 253
Cdd:COG4886   164 LDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLEELDLSGNQLTDLPEP-------------------- 223

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 372266129  254 glpsgIGKLTNLEEFMAANNNLELVPEsLCRCPKLRKLVLNKNHLVTLPEAIHfLTEIEVLDVRENP 320
Cdd:COG4886   224 -----LANLTNLETLDLSNNQLTDLPE-LGNLTNLEELDLSNNQLTDLPPLAN-LTNLKTLDLSNNQ 283
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
38-319 4.16e-36

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 142.38  E-value: 4.16e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129   38 LKLNRTGLCYLPEELAALQKLEHLSVSHNNLTTLHGELSSLPSLRAIVARANSLKNSGVPDDIFKLDDLSVLDLSHNQLT 117
Cdd:COG4886     4 LLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129  118 E---CPRELENAKNMLVLNLSHNRQLPAMTALQTLHLRSTQRTqsNLPTSLEGLSNLADVDLSCNDLTRVPECLYTLPSL 194
Cdd:COG4886    84 LlllGLTDLGDLTNLTELDLSGNEELSNLTNLESLDLSGNQLT--DLPEELANLTNLKELDLSNNQLTDLPEPLGNLTNL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129  195 RRLNLSSNQITELSLCIDQWVHVETLNLSRNQLTSLPSAIcklsklkklylnsnkldfdglpsgiGKLTNLEEFMAANNN 274
Cdd:COG4886   162 KSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPL-------------------------GNLTNLEELDLSGNQ 216

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 372266129  275 LELVPESLCRCPKLRKLVLNKNHLVTLPEaIHFLTEIEVLDVREN 319
Cdd:COG4886   217 LTDLPEPLANLTNLETLDLSNNQLTDLPE-LGNLTNLEELDLSNN 260
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 998-1097 5.20e-36

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: 131.58  E-value: 5.20e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129  998 QPSLYQIRTNGSaLCTRCIQINTDSSLLNSEFCFILKVPFesednqgIVYAWVGRASDPDEAKLAEDILNTMFDtSYSKQ 1077
Cdd:cd11288     2 PTRLFQVRGNGS-GNTRAVEVDADASSLNSNDVFVLKTPS-------SVYLWVGKGSSEDERELAKDVASFLKP-KASLQ 72

                          90       100
                  ....*....|....*....|
gi 372266129 1078 VINEGEEPENFFWVGIGAQK 1097
Cdd:cd11288    73 EVAEGSEPDEFWEALGGKSE 92
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 668-782 1.62e-32

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: 121.59  E-value: 1.62e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129  668 PPQPKLYKVGLGLGYLELPQINYKLsvehkqrpkvelmprmrLLQSLLDTRCVYILDCWSDVFIWLGRKSPRLVRAAALK 747
Cdd:cd11292     1 AEQKKLYKVSDASGKLKLTEVAEGS-----------------LNQEMLDSEDCYILDCGSEIFVWVGKGASLDERKAALK 63

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 372266129  748 LGQELCGMLHRPRHATVSRSLEGTEAQVFKAKFKN 782
Cdd:cd11292    64 NAEEFLRKKKRPPYTQVTRVTEGGESALFKSKFAN 98
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 564-651 2.52e-28

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: 109.38  E-value: 2.52e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129  564 TRMYRVYGKKNIKLEPVPLKGTSLDPRFVFLLDRGLDIYVWRGAQATLSSTTKARLFAEKINKnERKGKAEITLLVQGQE 643
Cdd:cd11280     2 PRLYRVRGSKAIEIEEVPLASSSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKELDE-ERKGKPEIVRIRQGQE 80


                  ....*...
gi 372266129  644 LPEFWEAL 651
Cdd:cd11280    81 PREFWSLF 88
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
66-319 2.30e-24

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 107.33  E-value: 2.30e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129   66 NNLTTLHGELSSLPSLRAIVARANSLKNSGVPDDIFKLDDLSVLDLSHNQLTECPRELENAKNMLVLNLSHNRQLPAMTA 145
Cdd:COG4886     3 LLLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129  146 LQTLhlrstqrtqsNLPTSLEGLSNLADVDLSCNDLtrvpecLYTLPSLRRLNLSSNQITELSLCIDQWVHVETLNLSRN 225
Cdd:COG4886    83 SLLL----------LGLTDLGDLTNLTELDLSGNEE------LSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNN 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129  226 QLTSLPSAIcklsklkklylnsnkldfdglpsgiGKLTNLEEFMAANNNLELVPESLCRCPKLRKLVLNKNHLVTLPEAI 305
Cdd:COG4886   147 QLTDLPEPL-------------------------GNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPL 201

                         250
                  ....*....|....
gi 372266129  306 HFLTEIEVLDVREN 319
Cdd:COG4886   202 GNLTNLEELDLSGN 215
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 565-653 1.24e-23

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 96.21  E-value: 1.24e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129    565 RMYRVYGKKNIKLEPVPLKGTSLDPRFVFLLDRGLDIYVWRGAQATLSSTTKARLFAEKINKNERKGKAEITLLVQGQEL 644
Cdd:smart00262    1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVRVVDEGKEP 80


                    ....*....
gi 372266129    645 PEFWEALGG 653
Cdd:smart00262   81 PEFWSLFGG 89
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1113-1206 3.13e-23

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 95.05  E-value: 3.13e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129   1113 RCSNEKGYFAVTEKCSDFCQDDLADDDIMLLDNGQEVYMWVGTQTSQVEIKLSLKACQVYIQHMRSkeheRPRRLRLVRK 1192
Cdd:smart00262    1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGP----GPVQVRVVDE 76

                            90
                    ....*....|....
gi 372266129   1193 GNEQHAFTRCFHAW 1206
Cdd:smart00262   77 GKEPPEFWSLFGGW 90
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 7-298 1.82e-22

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 104.54  E-value: 1.82e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129    7 LPFVRGVDLSGNDFKGGyFPENV-KAMTSLRWLKL---NRTGlcylPEELAALQKLEHLSVSHNNLT-TLHGELSSLPSL 81
Cdd:PLN00113   92 LPYIQTINLSNNQLSGP-IPDDIfTTSSSLRYLNLsnnNFTG----SIPRGSIPNLETLDLSNNMLSgEIPNDIGSFSSL 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129   82 RAIVARANSLKNSgVPDDIFKLDDLSVLDLSHNQLT-ECPRELENAKNMLVLNLSHN-------RQLPAMTALQTLHLRS 153
Cdd:PLN00113  167 KVLDLGGNVLVGK-IPNSLTNLTSLEFLTLASNQLVgQIPRELGQMKSLKWIYLGYNnlsgeipYEIGGLTSLNHLDLVY 245

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129  154 TQRTQSnLPTSLEGLSNLADVDLSCNDLT-RVPECLYTLPSLRRLNLSSNQIT-ELSLCIDQWVHVETLNLSRNQLT-SL 230
Cdd:PLN00113  246 NNLTGP-IPSSLGNLKNLQYLFLYQNKLSgPIPPSIFSLQKLISLDLSDNSLSgEIPELVIQLQNLEILHLFSNNFTgKI 324

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 372266129  231 PSAICKLSKLKKLYLNSNKLDfDGLPSGIGKLTNLEEFMAANNNLE-LVPESLCRCPKLRKLVLNKNHL 298
Cdd:PLN00113  325 PVALTSLPRLQVLQLWSNKFS-GEIPKNLGKHNNLTVLDLSTNNLTgEIPEGLCSSGNLFKLILFSNSL 392
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
 446-539 2.11e-19

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: 84.24  E-value: 2.11e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129  446 LTIWQIENFVPVLVEEAFHGKFYEADCYIVLKTFlDDSGSLNWEIYYWIGGEATLDKKACSAIHAVNLRNYLGAECRTVR 525
Cdd:cd11293     9 VEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTY-QGGGKEEHILYFWQGRHSSQDERAAAALLTVELDEELKGRAVQVR 87

                          90
                  ....*....|....
gi 372266129  526 EEMGDESEEFLQVF 539
Cdd:cd11293    88 VVQGKEPPHFLALF 101
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 919-979 1.24e-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: 81.65  E-value: 1.24e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 372266129  919 KQPEEDFQCIVYFWQGReASNMGWLTFTFSLQKKFESLFPGKLEVVRMTQQQENPKFLSHF 979
Cdd:cd11280    29 DVFVLDTGSEIYIWQGR-ASSQAELAAAALLAKELDEERKGKPEIVRIRQGQEPREFWSLF 88
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 696-783 2.69e-18

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: 80.80  E-value: 2.69e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129    696 HKQRPKVELMPRMRLLQSLLDTRCVYILDCWSDVFIWLGRKSPRLVRAAALKLGQELCGMLHrPRHATVSRSLEGTEAQV 775
Cdd:smart00262    4 RVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLG-PGPVQVRVVDEGKEPPE 82


                    ....*...
gi 372266129    776 FKAKFKNW 783
Cdd:smart00262   83 FWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 448-541 6.40e-18

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: 79.64  E-value: 6.40e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129    448 IWQIENFVPVLVEE--AFHGKFYEADCYIVLKTflddsgslnWEIYYWIGGEATLDKKACSAIHAVNLRNYLGAECRTVR 525
Cdd:smart00262    2 LVRVKGKRNVRVPEvpFSQGSLNSGDCYILDTG---------SEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVR 72

                            90
                    ....*....|....*..
gi 372266129    526 E-EMGDESEEFLQVFDN 541
Cdd:smart00262   73 VvDEGKEPPEFWSLFGG 89
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 15-319 1.83e-17

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 88.37  E-value: 1.83e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129   15 LSGNDFKGGyFPENVKAMTSLRWLKLNRTGLC-YLPEELAALQKLEHLSVSHNNLT-TLHGELSSLPSLRAIVARANSLK 92
Cdd:PLN00113  195 LASNQLVGQ-IPRELGQMKSLKWIYLGYNNLSgEIPYEIGGLTSLNHLDLVYNNLTgPIPSSLGNLKNLQYLFLYQNKLS 273

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129   93 NSgVPDDIFKLDDLSVLDLSHNQLT-ECPRELENAKNMLVLNLSHN-------RQLPAMTALQTLHLRStQRTQSNLPTS 164
Cdd:PLN00113  274 GP-IPPSIFSLQKLISLDLSDNSLSgEIPELVIQLQNLEILHLFSNnftgkipVALTSLPRLQVLQLWS-NKFSGEIPKN 351

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129  165 LEGLSNLADVDLSCNDLT-------------------------RVPECLYTLPSLRRLNLSSNQIT-ELSLCIDQWVHVE 218
Cdd:PLN00113  352 LGKHNNLTVLDLSTNNLTgeipeglcssgnlfklilfsnslegEIPKSLGACRSLRRVRLQDNSFSgELPSEFTKLPLVY 431

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129  219 TLNLSRNQLT-SLPSAICKLSKLKKLYLNSNKLdFDGLP--SGIGKLTNLEefMAANNNLELVPESLCRCPKLRKLVLNK 295
Cdd:PLN00113  432 FLDISNNNLQgRINSRKWDMPSLQMLSLARNKF-FGGLPdsFGSKRLENLD--LSRNQFSGAVPRKLGSLSELMQLKLSE 508

                         330       340
                  ....*....|....*....|....*
gi 372266129  296 NHLV-TLPEAIHFLTEIEVLDVREN 319
Cdd:PLN00113  509 NKLSgEIPDELSSCKKLVSLDLSHN 533
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 23-298 4.94e-16

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 83.74  E-value: 4.94e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129   23 GYFPENVKAMTSLRWLKLNRTGLC-YLPEELAALQKLEHLSVSHNNLT-TLHGELSSLPSLRAIVARANSLkNSGVPDDI 100
Cdd:PLN00113  274 GPIPPSIFSLQKLISLDLSDNSLSgEIPELVIQLQNLEILHLFSNNFTgKIPVALTSLPRLQVLQLWSNKF-SGEIPKNL 352

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129  101 FKLDDLSVLDLSHNQLT-ECPRELENAKNMLVLNLSHNR---QLP-AMTALQTLHlrsTQRTQSN-----LPTSLEGLSN 170
Cdd:PLN00113  353 GKHNNLTVLDLSTNNLTgEIPEGLCSSGNLFKLILFSNSlegEIPkSLGACRSLR---RVRLQDNsfsgeLPSEFTKLPL 429

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129  171 LADVDLSCNDLT-RVPECLYTLPSLRRLNLSSNQIT-EL--SLCIDQwvhVETLNLSRNQLTSLpsaicklsklkklyln 246
Cdd:PLN00113  430 VYFLDISNNNLQgRINSRKWDMPSLQMLSLARNKFFgGLpdSFGSKR---LENLDLSRNQFSGA---------------- 490

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 372266129  247 snkldfdgLPSGIGKLTNLEEFMAANNNLE-LVPESLCRCPKLRKLVLNKNHL 298
Cdd:PLN00113  491 --------VPRKLGSLSELMQLKLSENKLSgEIPDELSSCKKLVSLDLSHNQL 535
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1002-1094 7.12e-16

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 73.87  E-value: 7.12e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129   1002 YQIRTNGSaLCTRCIQINTDSSLLNSEFCFILkvpfeseDNQGIVYAWVGRASDPDEAKLAEDILNTMFDTSYSK----Q 1077
Cdd:smart00262    1 FLVRVKGK-RNVRVPEVPFSQGSLNSGDCYIL-------DTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGpvqvR 72

                            90
                    ....*....|....*..
gi 372266129   1078 VINEGEEPENFFWVGIG 1094
Cdd:smart00262   73 VVDEGKEPPEFWSLFGG 89
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
103-320 1.84e-15

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 80.36  E-value: 1.84e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129  103 LDDLSVLDLSHNQLTECPRELENAKNMLVLNLSHNRQLPAMTALQTLHLRSTQRTQSNLPTSLEGLSNLADVDLSCNDLT 182
Cdd:COG4886     4 LLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129  183 RVPECLYT---LPSLRRLNLSSNQItelslcIDQWVHVETLNLSRNQLTSLPSAIcklsklkklylnsnkldfdglpsgi 259
Cdd:COG4886    84 LLLLGLTDlgdLTNLTELDLSGNEE------LSNLTNLESLDLSGNQLTDLPEEL------------------------- 132

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 372266129  260 GKLTNLEEFMAANNNLELVPESLCRCPKLRKLVLNKNHLVTLPEAIHFLTEIEVLDVRENP 320
Cdd:COG4886   133 ANLTNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQ 193
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 563-652 5.34e-15

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: 71.50  E-value: 5.34e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129  563 VTRMYRVYGKKNIKLEPVPLKGTSLDPRFVFLLDRGLDIYVWRGAQATLSSTTKARLFAEKINKNERKGKAEITLLVQG- 641
Cdd:cd11289     1 KPRLLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKVIVLDEGd 80

                          90
                  ....*....|..
gi 372266129  642 -QELPEFWEALG 652
Cdd:cd11289    81 tNESPEFWKVLG 92
Gelsolin pfam00626
Gelsolin repeat;
573-648 2.02e-14

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 69.26  E-value: 2.02e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 372266129   573 KNIKLEPVPLKGTSLDPRFVFLLDRGLDIYVWRGAQATLSSTTKARLFAEKINKNERKGKAEITLLVQGQELPEFW 648
Cdd:pfam00626    1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDERFPLPEVIRVPQGKEPARFL 76
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 4-202 3.91e-14

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 77.58  E-value: 3.91e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129    4 TGVLPfvRGVDLSGNDFK--------GGYFPENVKAMTSLRWLKLNRTGLC-YLPEELAALQKLEHLSVSHNNLTtlhGE 74
Cdd:PLN00113  369 TGEIP--EGLCSSGNLFKlilfsnslEGEIPKSLGACRSLRRVRLQDNSFSgELPSEFTKLPLVYFLDISNNNLQ---GR 443

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129   75 LSS----LPSLRAIVARANSLknSGVPDDIFKLDDLSVLDLSHNQLTEC-PRELENAKNMLVLNLSHN-------RQLPA 142
Cdd:PLN00113  444 INSrkwdMPSLQMLSLARNKF--FGGLPDSFGSKRLENLDLSRNQFSGAvPRKLGSLSELMQLKLSENklsgeipDELSS 521

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 372266129  143 MTALQTLHLRSTQRTqSNLPTSLEGLSNLADVDLSCNDLT-RVPECLYTLPSLRRLNLSSN 202
Cdd:PLN00113  522 CKKLVSLDLSHNQLS-GQIPASFSEMPVLSQLDLSQNQLSgEIPKNLGNVESLVQVNISHN 581
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 55-231 7.94e-14

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 72.13  E-value: 7.94e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129   55 LQKLEHLSVSHNNLTTLhGELSSLPSLRAIVARANSLKNSgvpDDIFKLDDLSVLDLSHNQLTECPrELENAKNMLVLNL 134
Cdd:cd21340     1 LKRITHLYLNDKNITKI-DNLSLCKNLKVLYLYDNKITKI---ENLEFLTNLTHLYLQNNQIEKIE-NLENLVNLKKLYL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129  135 SHNR-----QLPAMTALQTLHLrSTQRTQSNL-----PTSLEGLSN-LADVDLSCNDLTRVpECLYTLPSLRRLNLSSNQ 203
Cdd:cd21340    76 GGNRisvveGLENLTNLEELHI-ENQRLPPGEkltfdPRSLAALSNsLRVLNISGNNIDSL-EPLAPLRNLEQLDASNNQ 153

                         170       180       190
                  ....*....|....*....|....*....|.
gi 372266129  204 IT---ELSLCIDQWVHVETLNLSRNQLTSLP 231
Cdd:cd21340   154 ISdleELLDLLSSWPSLRELDLTGNPVCKKP 184
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 103-315 9.69e-14

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 71.74  E-value: 9.69e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129  103 LDDLSVLDLSHNQLTECPrELENAKNMLVL-----NLSHNRQLPAMTALQTLHLrstqrtQSNLPTSLEGLSNLAD---V 174
Cdd:cd21340     1 LKRITHLYLNDKNITKID-NLSLCKNLKVLylydnKITKIENLEFLTNLTHLYL------QNNQIEKIENLENLVNlkkL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129  175 DLSCNDLTRVpECLYTLPSLRRLNLSSNQI-TELSLCID----QWV--HVETLNLSRNQLTSLpsaicklsklkklylns 247
Cdd:cd21340    74 YLGGNRISVV-EGLENLTNLEELHIENQRLpPGEKLTFDprslAALsnSLRVLNISGNNIDSL----------------- 135

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 372266129  248 nkldfdglpSGIGKLTNLEEFMAANNNL----ELVpESLCRCPKLRKLVLNKNHLVTLP----EAIHFLTEIEVLD 315
Cdd:cd21340   136 ---------EPLAPLRNLEQLDASNNQIsdleELL-DLLSSWPSLRELDLTGNPVCKKPkyrdKIILASKSLEVLD 201
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
26-282 5.14e-13

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 73.58  E-value: 5.14e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129   26 PENVKAMTSLR-WLKLNRTGLC-----------YLPEELAALqklehlSVSHNNLTTLHGELSSlpSLRAIVARANSLKN 93
Cdd:PRK15370  163 ANREEAVQRMRdCLKNNKTELRlkilglttipaCIPEQITTL------ILDNNELKSLPENLQG--NIKTLYANSNQLTS 234

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129   94 --SGVPDDIFKLD---------------DLSVLDLSHNQLTECPRELENAKNMLVLNLSHNRQLPAMTALQTLHLRSTQR 156
Cdd:PRK15370  235 ipATLPDTIQEMElsinritelperlpsALQSLDLFHNKISCLPENLPEELRYLSVYDNSIRTLPAHLPSGITHLNVQSN 314

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129  157 TQSNLPTSLEglSNLADVDLSCNDLTRVPECLytLPSLRRLNLSSNQITELSLCIDQwvHVETLNLSRNQLTSLPsaick 236
Cdd:PRK15370  315 SLTALPETLP--PGLKTLEAGENALTSLPASL--PPELQVLDVSKNQITVLPETLPP--TITTLDVSRNALTNLP----- 383

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 372266129  237 lsklkklylnsnkldfDGLPSGigkltnLEEFMAANNNLELVPESL 282
Cdd:PRK15370  384 ----------------ENLPAA------LQIMQASRNNLVRLPESL 407
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
123-325 8.44e-13

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 72.81  E-value: 8.44e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129  123 LENAKNMLVLNLSHNRQLPAMTALQTLHLRSTQRTQSNLPTSLEGlsNLADVDLSCNDLTRVPEclyTLP-SLRRLNLSS 201
Cdd:PRK15370  176 LKNNKTELRLKILGLTTIPACIPEQITTLILDNNELKSLPENLQG--NIKTLYANSNQLTSIPA---TLPdTIQEMELSI 250

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129  202 NQITELSLCIDQwvHVETLNLSRNQLTSLPSAICKLSKLKKLYLNSNKLDFDGLPSGIGKL---------------TNLE 266
Cdd:PRK15370  251 NRITELPERLPS--ALQSLDLFHNKISCLPENLPEELRYLSVYDNSIRTLPAHLPSGITHLnvqsnsltalpetlpPGLK 328

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 372266129  267 EFMAANNNLELVPESLCrcPKLRKLVLNKNHLVTLPEAIHflTEIEVLDVRENPNLVMP 325
Cdd:PRK15370  329 TLEAGENALTSLPASLP--PELQVLDVSKNQITVLPETLP--PTITTLDVSRNALTNLP 383
Gelsolin pfam00626
Gelsolin repeat;
453-536 1.44e-12

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 63.87  E-value: 1.44e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129   453 NFVPVLVEEAFHGKFYEADCYIVLKTFlddsgslnwEIYYWIGGEATLDKKACSAIHAVNLR-NYLGAECRTVREEMGDE 531
Cdd:pfam00626    1 KFVLPPPVPLSQESLNSGDCYLLDNGF---------TIFLWVGKGSSLLEKLFAALLAAQLDdDERFPLPEVIRVPQGKE 71


                   ....*
gi 372266129   532 SEEFL 536
Cdd:pfam00626   72 PARFL 76
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 1109-1209 2.73e-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: 60.84  E-value: 2.73e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129 1109 TRLFRCSNEK-GYFAVTEKCSDfcqdDLADDDIMLLDNGQEVYMWVGTQTSQVEiklsLKACQVYIQHMRSKEHERPRRL 1187
Cdd:cd11280     2 PRLYRVRGSKaIEIEEVPLASS----SLDSDDVFVLDTGSEIYIWQGRASSQAE----LAAAALLAKELDEERKGKPEIV 73

                          90       100
                  ....*....|....*....|..
gi 372266129 1188 RlVRKGNEQHAFtrcfhaWSAF 1209
Cdd:cd11280    74 R-IRQGQEPREF------WSLF 88
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 564-653 9.22e-11

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: 59.55  E-value: 9.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129  564 TRMYRVYG--KKNIKLEPVPLKGTSLDPRFVFLLDRGLDIYVWRGAQATLSSTTKARLFAEKINKnerkgKAEITLLVQG 641
Cdd:cd11288     3 TRLFQVRGngSGNTRAVEVDADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVASFLKP-----KASLQEVAEG 77

                          90
                  ....*....|..
gi 372266129  642 QELPEFWEALGG 653
Cdd:cd11288    78 SEPDEFWEALGG 89
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 448-539 5.56e-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: 56.99  E-value: 5.56e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129  448 IWQIENFVPVLVEE--AFHGKFYEADCYIVlktfldDSGSlnwEIYYWIGGEATLDKKACSAIHAVNLRNYLGAECRTVR 525
Cdd:cd11280     4 LYRVRGSKAIEIEEvpLASSSLDSDDVFVL------DTGS---EIYIWQGRASSQAELAAAALLAKELDEERKGKPEIVR 74

                          90
                  ....*....|....
gi 372266129  526 EEMGDESEEFLQVF 539
Cdd:cd11280    75 IRQGQEPREFWSLF 88
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 100-319 1.24e-08

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 59.48  E-value: 1.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129  100 IFKLDDLSVLDLSHNQLT-ECPREL-ENAKNMLVLNLSHNR---QLP--AMTALQTLHLrSTQRTQSNLPTSLEGLSNLA 172
Cdd:PLN00113   89 IFRLPYIQTINLSNNQLSgPIPDDIfTTSSSLRYLNLSNNNftgSIPrgSIPNLETLDL-SNNMLSGEIPNDIGSFSSLK 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129  173 DVDLSCNDLT-RVPECLYTLPSLRRLNLSSNQIT-----EL----SLcidQWVHVETLNLSRN------QLTSLpsaick 236
Cdd:PLN00113  168 VLDLGGNVLVgKIPNSLTNLTSLEFLTLASNQLVgqiprELgqmkSL---KWIYLGYNNLSGEipyeigGLTSL------ 238

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129  237 lsklkklylnsNKLDF------DGLPSGIGKLTNLEEFMAANNNLE-LVPESLCRCPKLRKLVLNKNHLV-TLPEAIHFL 308
Cdd:PLN00113  239 -----------NHLDLvynnltGPIPSSLGNLKNLQYLFLYQNKLSgPIPPSIFSLQKLISLDLSDNSLSgEIPELVIQL 307

                         250
                  ....*....|.
gi 372266129  309 TEIEVLDVREN 319
Cdd:PLN00113  308 QNLEILHLFSN 318
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 1109-1203 1.45e-08

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


Pssm-ID: 200448  Cd Length: 98  Bit Score: 53.41  E-value: 1.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129 1109 TRLFRCSNEKGYFAVTE-KCSDFCQDDLADDDIMLLDNGQEVYMWVGTQTSQVEIKLSLKACQVYIQhmrskEHERPRRL 1187
Cdd:cd11292     4 KKLYKVSDASGKLKLTEvAEGSLNQEMLDSEDCYILDCGSEIFVWVGKGASLDERKAALKNAEEFLR-----KKKRPPYT 78

                          90
                  ....*....|....*...
gi 372266129 1188 RLVR--KGNEQHAFTRCF 1203
Cdd:cd11292    79 QVTRvtEGGESALFKSKF 96
LRR_8 pfam13855
Leucine rich repeat;
169-227 3.31e-08

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 50.99  E-value: 3.31e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 372266129   169 SNLADVDLSCNDLTRV-PECLYTLPSLRRLNLSSNQITELSL-CIDQWVHVETLNLSRNQL 227
Cdd:pfam13855    1 PNLRSLDLSNNRLTSLdDGAFKGLSNLKVLDLSNNLLTTLSPgAFSGLPSLRYLDLSGNRL 61
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 563-647 5.01e-08

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


Pssm-ID: 200448  Cd Length: 98  Bit Score: 51.87  E-value: 5.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129  563 VTRMYRVY-GKKNIKLEPV---PLKGTSLDPRFVFLLDRGLDIYVWRGAQATLSSTTKARLFAEK-INKNERKGKAEITL 637
Cdd:cd11292     3 QKKLYKVSdASGKLKLTEVaegSLNQEMLDSEDCYILDCGSEIFVWVGKGASLDERKAALKNAEEfLRKKKRPPYTQVTR 82

                          90
                  ....*....|
gi 372266129  638 LVQGQELPEF 647
Cdd:cd11292    83 VTEGGESALF 92
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 1-228 9.03e-08

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 55.95  E-value: 9.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129    1 MEATGVLPFVRGVDLSGN---DFKGGYFPENVKAMTSLRWLKLNRT-----GLCYLPEELAALQKLEHLSVSHNNLTTlh 72
Cdd:COG5238   173 MAKALQNNSVETVYLGCNqigDEGIEELAEALTQNTTVTTLWLKRNpigdeGAEILAEALKGNKSLTTLDLSNNQIGD-- 250

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129   73 gelsslpslRAIVARANSLKNSgvpddifklDDLSVLDLSHNQLTE-----CPRELENAKNMLVLNLSHNR--------- 138
Cdd:COG5238   251 ---------EGVIALAEALKNN---------TTVETLYLSGNQIGAegaiaLAKALQGNTTLTSLDLSVNRigdegaial 312

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129  139 --QLPAMTALQTLHLRSTQRTQSN---LPTSLEGLSNLADVDLSCNDLT-----RVPECLYTLPSLRRLNLSSNQITEL- 207
Cdd:COG5238   313 aeGLQGNKTLHTLNLAYNGIGAQGaiaLAKALQENTTLHSLDLSDNQIGdegaiALAKYLEGNTTLRELNLGKNNIGKQg 392

                         250       260
                  ....*....|....*....|....*..
gi 372266129  208 ------SLCIDQwvhVETLNLSRNQLT 228
Cdd:COG5238   393 aealidALQTNR---LHTLILDGNLIG 416
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 996-1088 9.08e-08

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


Pssm-ID: 200448  Cd Length: 98  Bit Score: 51.10  E-value: 9.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129  996 AQQPSLYQIRTNGSALCTRCIQINT-DSSLLNSEFCFILkvpfeseDNQGIVYAWVGRASDPDEAK----LAEDILNTMF 1070
Cdd:cd11292     1 AEQKKLYKVSDASGKLKLTEVAEGSlNQEMLDSEDCYIL-------DCGSEIFVWVGKGASLDERKaalkNAEEFLRKKK 73

                          90
                  ....*....|....*....
gi 372266129 1071 DTSYSK-QVINEGEEPENF 1088
Cdd:cd11292    74 RPPYTQvTRVTEGGESALF 92
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 713-780 1.24e-07

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: 50.44  E-value: 1.24e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 372266129  713 SLLDTRCVYILDCWSDVFIWLGRKSPRLVRAAALKLGQELcgmLHRPRHAT-VSRSLEGTEAQVFKAKF 780
Cdd:cd11280    23 SSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKEL---DEERKGKPeIVRIRQGQEPREFWSLF 88
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 712-784 1.47e-07

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: 50.76  E-value: 1.47e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 372266129  712 QSLLDTRCVYILDCWSDVFIWLGRKSPRLVRAAALKLGQ---ELCGMLHRPRHATVSRSLEGTEAQVFKAKFKNWD 784
Cdd:cd11291    24 QDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKkyiETDPLGRSKPRTPIYLVKQGNEPPTFTGYFHAWD 99
Gelsolin pfam00626
Gelsolin repeat;
1126-1199 1.68e-07

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 49.61  E-value: 1.68e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 372266129  1126 KCSDFCQDDLADDDIMLLDNGQEVYMWVGTQTSQVEIklslKACQVYIQHMRSKEHERPRRLRLVRKGNEQHAF 1199
Cdd:pfam00626    6 PPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEK----LFAALLAAQLDDDERFPLPEVIRVPQGKEPARF 75
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 50-205 3.89e-07

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 52.10  E-value: 3.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129   50 EELAALQKLEHLSVSHNNLTTLHGeLSSLPSLRaivaranslknsgvpddifklddlsVLDLSHNQLT--EC----PREL 123
Cdd:cd21340    62 ENLENLVNLKKLYLGGNRISVVEG-LENLTNLE-------------------------ELHIENQRLPpgEKltfdPRSL 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129  124 EN-AKNMLVLNLSHNRqlpamtaLQTLhlrstqrtqsnlpTSLEGLSNLADVDLSCNDLTRVPE---CLYTLPSLRRLNL 199
Cdd:cd21340   116 AAlSNSLRVLNISGNN-------IDSL-------------EPLAPLRNLEQLDASNNQISDLEElldLLSSWPSLRELDL 175


                  ....*.
gi 372266129  200 SSNQIT 205
Cdd:cd21340   176 TGNPVC 181
LRR_8 pfam13855
Leucine rich repeat;
146-204 4.95e-07

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 47.90  E-value: 4.95e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 372266129   146 LQTLHLRStqrtqSNL----PTSLEGLSNLADVDLSCNDLTRV-PECLYTLPSLRRLNLSSNQI 204
Cdd:pfam13855    3 LRSLDLSN-----NRLtsldDGAFKGLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
PRK15387 PRK15387
type III secretion system effector E3 ubiquitin transferase SspH2;
38-320 5.39e-07

type III secretion system effector E3 ubiquitin transferase SspH2;


Pssm-ID: 185285 [Multi-domain]  Cd Length: 788  Bit Score: 54.01  E-value: 5.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129   38 LKLNRTGLCYLPEELAAlqKLEHLSVSHNNLTtlhgelsSLPSLRAivaranslknsgvpddifkldDLSVLDLSHNQLT 117
Cdd:PRK15387  206 LNVGESGLTTLPDCLPA--HITTLVIPDNNLT-------SLPALPP---------------------ELRTLEVSGNQLT 255

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129  118 ECPRElenAKNMLVLNLSHN--RQLPAM-TALQTLHLRSTQRTqsNLPTSLEGLSNLAdvdLSCNDLTRVPeclyTLPS- 193
Cdd:PRK15387  256 SLPVL---PPGLLELSIFSNplTHLPALpSGLCKLWIFGNQLT--SLPVLPPGLQELS---VSDNQLASLP----ALPSe 323

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129  194 LRRLNLSSNQITELSLCIDQwvhVETLNLSRNQLTSLPSaiCKLSKLKKLYLNSNKLDFDGLPSGIGKL----------- 262
Cdd:PRK15387  324 LCKLWAYNNQLTSLPTLPSG---LQELSVSDNQLASLPT--LPSELYKLWAYNNRLTSLPALPSGLKELivsgnrltslp 398

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 372266129  263 ---TNLEEFMAANNNLELVPeslcRCPK-LRKLVLNKNHLVTLPEAIHFLTEIEVLDVRENP 320
Cdd:PRK15387  399 vlpSELKELMVSGNRLTSLP----MLPSgLLSLSVYRNQLTRLPESLIHLSSETTVNLEGNP 456
Gelsolin pfam00626
Gelsolin repeat;
701-777 3.96e-06

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 45.76  E-value: 3.96e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 372266129   701 KVELMPRMRLLQSLLDTRCVYILDCWSDVFIWLGRKSPRLVRAAALKLGQELcGMLHRPRHATVSRSLEGTEAQVFK 777
Cdd:pfam00626    1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQL-DDDERFPLPEVIRVPQGKEPARFL 76
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 26-228 5.34e-06

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 50.05  E-value: 5.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129   26 PENVKAMTSLRWLKLNRTGLCY-LPEELAALQK---LEHLSVSHNNLTTLHGelsslpslrAIVARAnsLKNSGVpddif 101
Cdd:cd00116    74 LQGLTKGCGLQELDLSDNALGPdGCGVLESLLRsssLQELKLNNNGLGDRGL---------RLLAKG--LKDLPP----- 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129  102 kldDLSVLDLSHNQLT-ECPRELENAknmlvlnlshnrqLPAMTALQTLHLRSTQRTQSNLPTSLEGL---SNLADVDLS 177
Cdd:cd00116   138 ---ALEKLVLGRNRLEgASCEALAKA-------------LRANRDLKELNLANNGIGDAGIRALAEGLkanCNLEVLDLN 201

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 372266129  178 CNDLTR-----VPECLYTLPSLRRLNLSSNQITELSLC------IDQWVHVETLNLSRNQLT 228
Cdd:cd00116   202 NNGLTDegasaLAETLASLKSLEVLNLGDNNLTDAGAAalasalLSPNISLLTLSLSCNDIT 263
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 998-1090 7.29e-06

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


Pssm-ID: 200436  Cd Length: 88  Bit Score: 45.44  E-value: 7.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129  998 QPSLYQIRTNGSalcTRCIQINTDSSLLNSEFCFILkvpfeseDNQGIVYAWVGRASDPDE----AKLAEDILNTMFDTS 1073
Cdd:cd11280     1 PPRLYRVRGSKA---IEIEEVPLASSSLDSDDVFVL-------DTGSEIYIWQGRASSQAElaaaALLAKELDEERKGKP 70

                          90
                  ....*....|....*..
gi 372266129 1074 YSkQVINEGEEPEnFFW 1090
Cdd:cd11280    71 EI-VRIRQGQEPR-EFW 85
Gelsolin pfam00626
Gelsolin repeat;
1021-1088 1.23e-05

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 44.22  E-value: 1.23e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 372266129  1021 DSSLLNSEFCFILkvpfeseDNQGIVYAWVGRASDPDE----AKLAEDILNTMFDTSYSKQVINEGEEPENF 1088
Cdd:pfam00626   11 SQESLNSGDCYLL-------DNGFTIFLWVGKGSSLLEklfaALLAAQLDDDERFPLPEVIRVPQGKEPARF 75
LRR_8 pfam13855
Leucine rich repeat;
33-91 4.98e-05

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 42.13  E-value: 4.98e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 372266129    33 TSLRWLKLNRTGLCYLPEE-LAALQKLEHLSVSHNNLTTLH-GELSSLPSLRAIVARANSL 91
Cdd:pfam13855    1 PNLRSLDLSNNRLTSLDDGaFKGLSNLKVLDLSNNLLTTLSpGAFSGLPSLRYLDLSGNRL 61
PLN03150 PLN03150
hypothetical protein; Provisional
 140-205 2.16e-04

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 45.58  E-value: 2.16e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 372266129  140 LPAMTALQTLHLrSTQRTQSNLPTSLEGLSNLADVDLSCNDLT-RVPECLYTLPSLRRLNLSSNQIT 205
Cdd:PLN03150  438 ISKLRHLQSINL-SGNSIRGNIPPSLGSITSLEVLDLSYNSFNgSIPESLGQLTSLRILNLNGNSLS 503
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 858-980 2.62e-04

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: 41.12  E-value: 2.62e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129    858 EGKKFARLPEEEF--GHFYTQDCYVFLCRYwvpveyeeeekkedkeekaegkegeeataeaeekqpeedfqcIVYFWQGR 935
Cdd:smart00262    6 KGKRNVRVPEVPFsqGSLNSGDCYILDTGS------------------------------------------EIYVWVGK 43

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*
gi 372266129    936 EASNMGWLTFTFSLQKKFESLFPGKLEVVRMTQQQENPKFLSHFK 980
Cdd:smart00262   44 KSSQDEKKKAAELAVELDDTLGPGPVQVRVVDEGKEPPEFWSLFG 88
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 587-647 4.59e-04

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


Pssm-ID: 200447 [Multi-domain]  Cd Length: 99  Bit Score: 40.74  E-value: 4.59e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 372266129  587 LDPRFVFLLDRGLDIYVWRGAQAT----LSSTTKARLFAEKINKNERKGKAEITLLVQGQELPEF 647
Cdd:cd11291    27 LDTDDIMLLDTGDEVFVWVGSESSdeekKEALTSAKKYIETDPLGRSKPRTPIYLVKQGNEPPTF 91
LRR_8 pfam13855
Leucine rich repeat;
79-138 4.97e-04

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 39.43  E-value: 4.97e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 372266129    79 PSLRAIVARANSLknSGVPDDIFK-LDDLSVLDLSHNQLTE-CPRELENAKNMLVLNLSHNR 138
Cdd:pfam13855    1 PNLRSLDLSNNRL--TSLDDGAFKgLSNLKVLDLSNNLLTTlSPGAFSGLPSLRYLDLSGNR 60
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 192-231 5.54e-04

Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.


Pssm-ID: 463713 [Multi-domain]  Cd Length: 44  Bit Score: 38.77  E-value: 5.54e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 372266129   192 PSLRRLNLSSNQITELSLcIDQWVHVETLNLSRN-QLTSLP 231
Cdd:pfam12799    1 PNLEVLDLSNNQITDIPP-LAKLPNLETLDLSGNnKITDLS 40
PRK15387 PRK15387
type III secretion system effector E3 ubiquitin transferase SspH2;
8-209 6.40e-04

type III secretion system effector E3 ubiquitin transferase SspH2;


Pssm-ID: 185285 [Multi-domain]  Cd Length: 788  Bit Score: 44.00  E-value: 6.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129    8 PFVRGVDLSGNDFKG-GYFPENVKAMT----SLRWLKLNRTGLCYL---PEELAALQ----KLEHLSVSHNNLTTL---- 71
Cdd:PRK15387  242 PELRTLEVSGNQLTSlPVLPPGLLELSifsnPLTHLPALPSGLCKLwifGNQLTSLPvlppGLQELSVSDNQLASLpalp 321

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129   72 ---------HGELSSLPSL----RAIVARANSLKN-SGVPDDIFKLDDLSvldlshNQLTECPRELENAKNMLVlnlSHN 137
Cdd:PRK15387  322 selcklwayNNQLTSLPTLpsglQELSVSDNQLASlPTLPSELYKLWAYN------NRLTSLPALPSGLKELIV---SGN 392

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 372266129  138 R--QLPAM-TALQTLHLRSTQRTqsNLPTSLEGLSNLAdvdLSCNDLTRVPECLYTLPSLRRLNLSSNQITELSL 209
Cdd:PRK15387  393 RltSLPVLpSELKELMVSGNRLT--SLPMLPSGLLSLS---VYRNQLTRLPESLIHLSSETTVNLEGNPLSERTL 462
PRK15387 PRK15387
type III secretion system effector E3 ubiquitin transferase SspH2;
179-337 2.00e-03

type III secretion system effector E3 ubiquitin transferase SspH2;


Pssm-ID: 185285 [Multi-domain]  Cd Length: 788  Bit Score: 42.46  E-value: 2.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129  179 NDLTRVPEclyTLPSLRRLNLSSNQITELSLCIDQWVHVETLNLSRNQLTSLPSAICKLSKLkklylnSNKL-DFDGLPS 257
Cdd:PRK15387  232 NNLTSLPA---LPPELRTLEVSGNQLTSLPVLPPGLLELSIFSNPLTHLPALPSGLCKLWIF------GNQLtSLPVLPP 302

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129  258 GIGKLTNLEEFMAAnnnLELVPESLCrcpklrKLVLNKNHLVTLPEAIHFLTEIEVLDvreNPNLVMPPKPADRAAEW-Y 336
Cdd:PRK15387  303 GLQELSVSDNQLAS---LPALPSELC------KLWAYNNQLTSLPTLPSGLQELSVSD---NQLASLPTLPSELYKLWaY 370


                  .
gi 372266129  337 N 337
Cdd:PRK15387  371 N 371
LRR_8 pfam13855
Leucine rich repeat;
216-298 2.19e-03

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 37.50  E-value: 2.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129   216 HVETLNLSRNQLTSLPSAIcklsklkklylnsnkldFDGLPsgigkltNLEEFMAANNNLE-LVPESLCRCPKLRKLVLN 294
Cdd:pfam13855    2 NLRSLDLSNNRLTSLDDGA-----------------FKGLS-------NLKVLDLSNNLLTtLSPGAFSGLPSLRYLDLS 57


                   ....
gi 372266129   295 KNHL 298
Cdd:pfam13855   58 GNRL 61
LRR_8 pfam13855
Leucine rich repeat;
192-230 2.47e-03

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 37.50  E-value: 2.47e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 372266129   192 PSLRRLNLSSNQITELSlciDQW----VHVETLNLSRNQLTSL 230
Cdd:pfam13855    1 PNLRSLDLSNNRLTSLD---DGAfkglSNLKVLDLSNNLLTTL 40
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 1109-1203 2.86e-03

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


Pssm-ID: 200445  Cd Length: 92  Bit Score: 37.99  E-value: 2.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129 1109 TRLFRCSNEKgYFAVTEkcSDFCQDDLADDDIMLLDNGQEVYMWVGTQTSQVEIklsLKACQvYIQHMRSKEHERPRRLR 1188
Cdd:cd11289     2 PRLLHVKGRR-NVRARE--VELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEK---AKAMQ-LAQGIRDERRLGRAKVI 74

                          90
                  ....*....|....*..
gi 372266129 1189 LVR--KGNEQHAFTRCF 1203
Cdd:cd11289    75 VLDegDTNESPEFWKVL 91
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 106-146 2.96e-03

Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.


Pssm-ID: 463713 [Multi-domain]  Cd Length: 44  Bit Score: 36.84  E-value: 2.96e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 372266129   106 LSVLDLSHNQLTECPrELENAKNMLVLNLSHNRQLPAMTAL 146
Cdd:pfam12799    3 LEVLDLSNNQITDIP-PLAKLPNLETLDLSGNNKITDLSDL 42
PLN03150 PLN03150
hypothetical protein; Provisional
 33-150 3.48e-03

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 41.73  E-value: 3.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129   33 TSLRW----LKLNRTGL-CYLPEELAALQKLEHLSVSHNNLttlHGELSslPSLRAIVAranslknsgvpddifklddLS 107
Cdd:PLN03150  414 TKGKWfidgLGLDNQGLrGFIPNDISKLRHLQSINLSGNSI---RGNIP--PSLGSITS-------------------LE 469

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 372266129  108 VLDLSHNQLT-ECPRELENAKNMLVLNLSHNR---QLPAMTALQTLH 150
Cdd:PLN03150  470 VLDLSYNSFNgSIPESLGQLTSLRILNLNGNSlsgRVPAALGGRLLH 516
PLN03210 PLN03210
Resistant to P. syringae 6; Provisional
 133-347 5.36e-03

Resistant to P. syringae 6; Provisional


Pssm-ID: 215633 [Multi-domain]  Cd Length: 1153  Bit Score: 41.01  E-value: 5.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129  133 NLSHNRQLPAMTALQTLHLRSTQrTQSNLPTSLEGLSNLADVDLS-CNDLTRVPECLyTLPSLRRLNLSSnqITELSLCI 211
Cdd:PLN03210  646 NLKEIPDLSMATNLETLKLSDCS-SLVELPSSIQYLNKLEDLDMSrCENLEILPTGI-NLKSLYRLNLSG--CSRLKSFP 721

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129  212 DQWVHVETLNLSRNQLTSLPSAIcklsklkklylnsnkldfdglpsgigKLTNLEEFMAANNNLE--------LVPESLC 283
Cdd:PLN03210  722 DISTNISWLDLDETAIEEFPSNL--------------------------RLENLDELILCEMKSEklwervqpLTPLMTM 775

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 372266129  284 RCPKLRKLVLNKN-HLVTLPEAIHFLTEIEVLDVRENPNLVMPPKPADRAAeWYNIDFSLQNQLR 347
Cdd:PLN03210  776 LSPSLTRLFLSDIpSLVELPSSIQNLHKLEHLEIENCINLETLPTGINLES-LESLDLSGCSRLR 839
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 176-319 8.44e-03

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 40.60  E-value: 8.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266129  176 LSCNDLTRVpeclytlpslRRLNLSSNQIT-ELSLCIDQWVHVETLNLSRNQLT-SLPSAICKLSKLKKLYLNSNKlDFD 253
Cdd:PLN00113   63 ITCNNSSRV----------VSIDLSGKNISgKISSAIFRLPYIQTINLSNNQLSgPIPDDIFTTSSSLRYLNLSNN-NFT 131

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 372266129  254 G-LPSgiGKLTNLEEFMAANNNLE-LVPESLCRCPKLRKLVLNKNHLV-TLPEAIHFLTEIEVLDVREN 319
Cdd:PLN00113  132 GsIPR--GSIPNLETLDLSNNMLSgEIPNDIGSFSSLKVLDLGGNVLVgKIPNSLTNLTSLEFLTLASN 198
 
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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