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Conserved domains on  [gi|564372233|ref|XP_006246530|]
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protein flightless-1 homolog isoform X1 [Rattus norvegicus]

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; ...
 491-603 5.29e-60

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: 200.91  E-value: 5.29e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233  491 TEDVGQLPGLTIWQIENFVPVLVEEAFHGKFYEADCYIVLKTFLDDSGSLNWEIYYWIGGEATLDKKACSAIHAVNLRNY 570
Cdd:cd11290     1 FEGVGQKPGLQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDPSGSLSYDIHYWLGKEASQDEAGAAAIKAVELDDY 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 564372233  571 LGAECRTAREEMGDESEGFLQVFDNDISYIEGG 603
Cdd:cd11290    81 LGGRPVQHREVQGHESEEFLSYFKKGIIYIEGG 113
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 1163-1262 1.33e-46

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: 162.08  E-value: 1.33e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233 1163 HTRLFRCSNEKGYFaVTEKCSDFCQDDLADDDIMLLDNGQEVYMWVGTQTSQVEIKLSLKACQVYIQHTRSKEHERPRRL 1242
Cdd:cd11291     1 KPRLFRCSNESGFF-KVEEISDFSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYIETDPLGRSKPRTPI 79

                          90       100
                  ....*....|....*....|
gi 564372233 1243 RLVRKGNEQRAFTRCFHAWS 1262
Cdd:cd11291    80 YLVKQGNEPPTFTGYFHAWD 99
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
38-374 1.09e-38

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


:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 150.08  E-value: 1.09e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233   38 LKLNRTGLCYLPEELAALQKLEHLSVSHNNLTTLHGELSSLPSLRAIVARANSLKNSGVPDDIFKLDDLSVLDLSHNQLT 117
Cdd:COG4886     4 LLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233  118 E---CPRELENAKNMLVLNLSHNsidsipnQLFINLTDLLYLDLSENRLESLPPQMRRLVHLQTLVLNGNPLlhaqlrql 194
Cdd:COG4886    84 LlllGLTDLGDLTNLTELDLSGN-------EELSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQL-------- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233  195 pammalqtlhlrntqrtqSNLPTSLEGLSNLSDVDLSCNDLTRVPECLYTLPNLHRLNLSSNQIAELSLCIDQWVHLETL 274
Cdd:COG4886   149 ------------------TDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLEEL 210

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233  275 NLSRNQLTSLPSAickltklkklylnsnkldfdglpsgIGKLTSLEEFMAANNNLELIPEsLCRCPKLRKLVLNKNRLVT 354
Cdd:COG4886   211 DLSGNQLTDLPEP-------------------------LANLTNLETLDLSNNQLTDLPE-LGNLTNLEELDLSNNQLTD 264

                         330       340
                  ....*....|....*....|
gi 564372233  355 LPEAIHfLTEIEVLDVRENP 374
Cdd:COG4886   265 LPPLAN-LTNLKTLDLSNNQ 283
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 1053-1152 9.37e-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: 130.81  E-value: 9.37e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233 1053 QPTLYQIRTNGSaLCTRCIQINTDSSLLNSEFCFILKVPFesednqgIVYAWVGRASDPDEAKLAEDILNTMFdPSYSKQ 1132
Cdd:cd11288     2 PTRLFQVRGNGS-GNTRAVEVDADASSLNSNDVFVLKTPS-------SVYLWVGKGSSEDERELAKDVASFLK-PKASLQ 72

                          90       100
                  ....*....|....*....|
gi 564372233 1133 VINEGEEPENFFWVGIGAQK 1152
Cdd:cd11288    73 EVAEGSEPDEFWEALGGKSE 92
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 722-836 7.88e-33

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: 122.74  E-value: 7.88e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233  722 PPQPKLYKVGLGLGYLELPQINYKLsvehkkrpkvelmpgmrLLQSLLDTRCVYILDCWSDVFIWLGRKSPRLVRAAALK 801
Cdd:cd11292     1 AEQKKLYKVSDASGKLKLTEVAEGS-----------------LNQEMLDSEDCYILDCGSEIFVWVGKGASLDERKAALK 63

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 564372233  802 LGQELCGMLHRPRHTVVSRSLEGTEAQVFKAKFKN 836
Cdd:cd11292    64 NAEEFLRKKKRPPYTQVTRVTEGGESALFKSKFAN 98
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 618-702 8.63e-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: 107.84  E-value: 8.63e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233  618 TRMYRVYGKKNIKLEPVPLKGTSLDPRFVFLLDQGLDIYVWRGAQATLSNTTKARLFAEKMNKnERKGKAEITLLVQGQE 697
Cdd:cd11280     2 PRLYRVRGSKAIEIEEVPLASSSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKELDE-ERKGKPEIVRIRQGQE 80


                  ....*
gi 564372233  698 PPEFW 702
Cdd:cd11280    81 PREFW 85
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 975-1035 8.57e-19

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


:

Pssm-ID: 200436  Cd Length: 88  Bit Score: 82.42  E-value: 8.57e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564372233  975 KQPEEDFQCIVYFWQGReASNMGWLTFTFSLQKKFESLFPGKLEVVRMTQQQENPKFLSHF 1035
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; ...
 491-603 5.29e-60

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: 200.91  E-value: 5.29e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233  491 TEDVGQLPGLTIWQIENFVPVLVEEAFHGKFYEADCYIVLKTFLDDSGSLNWEIYYWIGGEATLDKKACSAIHAVNLRNY 570
Cdd:cd11290     1 FEGVGQKPGLQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDPSGSLSYDIHYWLGKEASQDEAGAAAIKAVELDDY 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 564372233  571 LGAECRTAREEMGDESEGFLQVFDNDISYIEGG 603
Cdd:cd11290    81 LGGRPVQHREVQGHESEEFLSYFKKGIIYIEGG 113
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 1163-1262 1.33e-46

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: 162.08  E-value: 1.33e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233 1163 HTRLFRCSNEKGYFaVTEKCSDFCQDDLADDDIMLLDNGQEVYMWVGTQTSQVEIKLSLKACQVYIQHTRSKEHERPRRL 1242
Cdd:cd11291     1 KPRLFRCSNESGFF-KVEEISDFSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYIETDPLGRSKPRTPI 79

                          90       100
                  ....*....|....*....|
gi 564372233 1243 RLVRKGNEQRAFTRCFHAWS 1262
Cdd:cd11291    80 YLVKQGNEPPTFTGYFHAWD 99
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
38-374 1.09e-38

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 150.08  E-value: 1.09e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233   38 LKLNRTGLCYLPEELAALQKLEHLSVSHNNLTTLHGELSSLPSLRAIVARANSLKNSGVPDDIFKLDDLSVLDLSHNQLT 117
Cdd:COG4886     4 LLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233  118 E---CPRELENAKNMLVLNLSHNsidsipnQLFINLTDLLYLDLSENRLESLPPQMRRLVHLQTLVLNGNPLlhaqlrql 194
Cdd:COG4886    84 LlllGLTDLGDLTNLTELDLSGN-------EELSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQL-------- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233  195 pammalqtlhlrntqrtqSNLPTSLEGLSNLSDVDLSCNDLTRVPECLYTLPNLHRLNLSSNQIAELSLCIDQWVHLETL 274
Cdd:COG4886   149 ------------------TDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLEEL 210

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233  275 NLSRNQLTSLPSAickltklkklylnsnkldfdglpsgIGKLTSLEEFMAANNNLELIPEsLCRCPKLRKLVLNKNRLVT 354
Cdd:COG4886   211 DLSGNQLTDLPEP-------------------------LANLTNLETLDLSNNQLTDLPE-LGNLTNLEELDLSNNQLTD 264

                         330       340
                  ....*....|....*....|
gi 564372233  355 LPEAIHfLTEIEVLDVRENP 374
Cdd:COG4886   265 LPPLAN-LTNLKTLDLSNNQ 283
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 1053-1152 9.37e-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: 130.81  E-value: 9.37e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233 1053 QPTLYQIRTNGSaLCTRCIQINTDSSLLNSEFCFILKVPFesednqgIVYAWVGRASDPDEAKLAEDILNTMFdPSYSKQ 1132
Cdd:cd11288     2 PTRLFQVRGNGS-GNTRAVEVDADASSLNSNDVFVLKTPS-------SVYLWVGKGSSEDERELAKDVASFLK-PKASLQ 72

                          90       100
                  ....*....|....*....|
gi 564372233 1133 VINEGEEPENFFWVGIGAQK 1152
Cdd:cd11288    73 EVAEGSEPDEFWEALGGKSE 92
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 722-836 7.88e-33

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: 122.74  E-value: 7.88e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233  722 PPQPKLYKVGLGLGYLELPQINYKLsvehkkrpkvelmpgmrLLQSLLDTRCVYILDCWSDVFIWLGRKSPRLVRAAALK 801
Cdd:cd11292     1 AEQKKLYKVSDASGKLKLTEVAEGS-----------------LNQEMLDSEDCYILDCGSEIFVWVGKGASLDERKAALK 63

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 564372233  802 LGQELCGMLHRPRHTVVSRSLEGTEAQVFKAKFKN 836
Cdd:cd11292    64 NAEEFLRKKKRPPYTQVTRVTEGGESALFKSKFAN 98
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 618-702 8.63e-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: 107.84  E-value: 8.63e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233  618 TRMYRVYGKKNIKLEPVPLKGTSLDPRFVFLLDQGLDIYVWRGAQATLSNTTKARLFAEKMNKnERKGKAEITLLVQGQE 697
Cdd:cd11280     2 PRLYRVRGSKAIEIEEVPLASSSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKELDE-ERKGKPEIVRIRQGQE 80


                  ....*
gi 564372233  698 PPEFW 702
Cdd:cd11280    81 PREFW 85
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 619-707 3.70e-25

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 100.44  E-value: 3.70e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233    619 RMYRVYGKKNIKLEPVPLKGTSLDPRFVFLLDQGLDIYVWRGAQATLSNTTKARLFAEKMNKNERKGKAEITLLVQGQEP 698
Cdd:smart00262    1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVRVVDEGKEP 80


                    ....*....
gi 564372233    699 PEFWDVLGG 707
Cdd:smart00262   81 PEFWSLFGG 89
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 5-352 2.17e-23

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 107.63  E-value: 2.17e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233    5 GVLPFVRGVDLSGNDFKGGyFPENVKAMTSLRWLKLNRTGLC-YLPEELAALQKLEHLSVSHNNLT-TLHGELSSLPSLR 82
Cdd:PLN00113  137 GSIPNLETLDLSNNMLSGE-IPNDIGSFSSLKVLDLGGNVLVgKIPNSLTNLTSLEFLTLASNQLVgQIPRELGQMKSLK 215

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233   83 AIVARANSLkNSGVPDDIFKLDDLSVLDLSHNQLT-ECPRELENAKNMLVLNLSHNSI-DSIPNQLFiNLTDLLYLDLSE 160
Cdd:PLN00113  216 WIYLGYNNL-SGEIPYEIGGLTSLNHLDLVYNNLTgPIPSSLGNLKNLQYLFLYQNKLsGPIPPSIF-SLQKLISLDLSD 293

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233  161 NRLE-SLPPQMRRLVHLQTLVLNGNPLLHAQLRQLPAMMALQTLHLRnTQRTQSNLPTSLEGLSNLSDVDLSCNDLT-RV 238
Cdd:PLN00113  294 NSLSgEIPELVIQLQNLEILHLFSNNFTGKIPVALTSLPRLQVLQLW-SNKFSGEIPKNLGKHNNLTVLDLSTNNLTgEI 372

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233  239 PECLYTLPNLHRLNLSSNQI-----AELSLC----------------------------------------ID--QW--V 269
Cdd:PLN00113  373 PEGLCSSGNLFKLILFSNSLegeipKSLGACrslrrvrlqdnsfsgelpseftklplvyfldisnnnlqgrINsrKWdmP 452

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233  270 HLETLNLSRNQLT-SLPSAickltklkKLYLNSNKLD-----FDG-LPSGIGKLTSLEEFMAANNNLE-LIPESLCRCPK 341
Cdd:PLN00113  453 SLQMLSLARNKFFgGLPDS--------FGSKRLENLDlsrnqFSGaVPRKLGSLSELMQLKLSENKLSgEIPDELSSCKK 524

                         410
                  ....*....|.
gi 564372233  342 LRKLVLNKNRL 352
Cdd:PLN00113  525 LVSLDLSHNQL 535
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1168-1261 5.92e-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: 94.28  E-value: 5.92e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233   1168 RCSNEKGYFAVTEKCSDFCQDDLADDDIMLLDNGQEVYMWVGTQTSQVEIKLSLKACQVYIQHtrskEHERPRRLRLVRK 1247
Cdd:smart00262    1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDT----LGPGPVQVRVVDE 76

                            90
                    ....*....|....
gi 564372233   1248 GNEQRAFTRCFHAW 1261
Cdd:smart00262   77 GKEPPEFWSLFGGW 90
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 975-1035 8.57e-19

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


Pssm-ID: 200436  Cd Length: 88  Bit Score: 82.42  E-value: 8.57e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564372233  975 KQPEEDFQCIVYFWQGReASNMGWLTFTFSLQKKFESLFPGKLEVVRMTQQQENPKFLSHF 1035
Cdd:cd11280    29 DVFVLDTGSEIYIWQGR-ASSQAELAAAALLAKELDEERKGKPEIVRIRQGQEPREFWSLF 88
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 750-837 3.36e-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: 3.36e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233    750 HKKRPKVELMPGMRLLQSLLDTRCVYILDCWSDVFIWLGRKSPRLVRAAALKLGQELCGMLHrPRHTVVSRSLEGTEAQV 829
Cdd:smart00262    4 RVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLG-PGPVQVRVVDEGKEPPE 82


                    ....*...
gi 564372233    830 FKAKFKNW 837
Cdd:smart00262   83 FWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 502-595 1.80e-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: 75.79  E-value: 1.80e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233    502 IWQIENFVPVLVEE--AFHGKFYEADCYIVLKTflddsgslnWEIYYWIGGEATLDKKACSAIHAVNLRNYLGAE-CRTA 578
Cdd:smart00262    2 LVRVKGKRNVRVPEvpFSQGSLNSGDCYILDTG---------SEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGpVQVR 72

                            90
                    ....*....|....*..
gi 564372233    579 REEMGDESEGFLQVFDN 595
Cdd:smart00262   73 VVDEGKEPPEFWSLFGG 89
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1057-1149 4.49e-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: 74.64  E-value: 4.49e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233   1057 YQIRTNGSaLCTRCIQINTDSSLLNSEFCFILkvpfeseDNQGIVYAWVGRASDPDE----AKLAEDILNTMFDPSYSKQ 1132
Cdd:smart00262    1 FLVRVKGK-RNVRVPEVPFSQGSLNSGDCYIL-------DTGSEIYVWVGKKSSQDEkkkaAELAVELDDTLGPGPVQVR 72

                            90
                    ....*....|....*..
gi 564372233   1133 VINEGEEPENFFWVGIG 1149
Cdd:smart00262   73 VVDEGKEPPEFWSLFGG 89
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 103-285 5.11e-16

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: 78.29  E-value: 5.11e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233  103 LDDLSVLDLSHNQLTECPrELENAKNMLVLNLSHNSIDSIPNqlFINLTDLLYLDLSENRLESLPPqMRRLVHLQTLVLN 182
Cdd:cd21340     1 LKRITHLYLNDKNITKID-NLSLCKNLKVLYLYDNKITKIEN--LEFLTNLTHLYLQNNQIEKIEN-LENLVNLKKLYLG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233  183 GNPLlhAQLRQLPAMMALQTLHLRNtQRTQSNL-----PTSLEGLSN-LSDVDLSCNDLTRVpECLYTLPNLHRLNLSSN 256
Cdd:cd21340    77 GNRI--SVVEGLENLTNLEELHIEN-QRLPPGEkltfdPRSLAALSNsLRVLNISGNNIDSL-EPLAPLRNLEQLDASNN 152

                         170       180       190
                  ....*....|....*....|....*....|..
gi 564372233  257 QIA---ELSLCIDQWVHLETLNLSRNQLTSLP 285
Cdd:cd21340   153 QISdleELLDLLSSWPSLRELDLTGNPVCKKP 184
Gelsolin pfam00626
Gelsolin repeat;
627-702 6.64e-15

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 70.80  E-value: 6.64e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564372233   627 KNIKLEPVPLKGTSLDPRFVFLLDQGLDIYVWRGAQATLSNTTKARLFAEKMNKNERKGKAEITLLVQGQEPPEFW 702
Cdd:pfam00626    1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDERFPLPEVIRVPQGKEPARFL 76
LRR_8 pfam13855
Leucine rich repeat;
131-186 1.68e-11

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 60.62  E-value: 1.68e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 564372233   131 VLNLSHNSIDSIPNQLFINLTDLLYLDLSENRLESLPPQM-RRLVHLQTLVLNGNPL 186
Cdd:pfam13855    5 SLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAfSGLPSLRYLDLSGNRL 61
Gelsolin pfam00626
Gelsolin repeat;
507-590 2.60e-11

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 60.40  E-value: 2.60e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233   507 NFVPVLVEEAFHGKFYEADCYIVLKTFlddsgslnwEIYYWIGGEATLDKKACSAIHAVNLR-NYLGAECRTAREEMGDE 585
Cdd:pfam00626    1 KFVLPPPVPLSQESLNSGDCYLLDNGF---------TIFLWVGKGSSLLEKLFAALLAAQLDdDERFPLPEVIRVPQGKE 71


                   ....*
gi 564372233   586 SEGFL 590
Cdd:pfam00626   72 PARFL 76
Gelsolin pfam00626
Gelsolin repeat;
1181-1254 5.74e-07

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 48.07  E-value: 5.74e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564372233  1181 KCSDFCQDDLADDDIMLLDNGQEVYMWVGTQTSQVEIKLSLKACQVYIQHTRskeHERPRRLRLVRkGNEQRAF 1254
Cdd:pfam00626    6 PPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDER---FPLPEVIRVPQ-GKEPARF 75
Gelsolin pfam00626
Gelsolin repeat;
755-831 1.68e-06

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 46.92  E-value: 1.68e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564372233   755 KVELMPGMRLLQSLLDTRCVYILDCWSDVFIWLGRKSPRLVRAAALKLGQELcGMLHRPRHTVVSRSLEGTEAQVFK 831
Cdd:pfam00626    1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQL-DDDERFPLPEVIRVPQGKEPARFL 76
Gelsolin pfam00626
Gelsolin repeat;
1076-1143 5.19e-06

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 45.38  E-value: 5.19e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564372233  1076 DSSLLNSEFCFILkvpfeseDNQGIVYAWVGRASDPDE----AKLAEDILNTMFDPSYSKQVINEGEEPENF 1143
Cdd:pfam00626   11 SQESLNSGDCYLL-------DNGFTIFLWVGKGSSLLEklfaALLAAQLDDDERFPLPEVIRVPQGKEPARF 75
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 912-1036 1.12e-03

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: 39.20  E-value: 1.12e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233    912 EGRKFTRLAEEEF--GHFYTQDCYVFLCRYwvpveyeeeekpedkegkasaegreeeeaaaeteekqpeedfqcIVYFWQ 989
Cdd:smart00262    6 KGKRNVRVPEVPFsqGSLNSGDCYILDTGS--------------------------------------------EIYVWV 41

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*..
gi 564372233    990 GREASNMGWLTFTFSLQKKFESLFPGKLEVVRMTQQQENPKFLSHFK 1036
Cdd:smart00262   42 GKKSSQDEKKKAAELAVELDDTLGPGPVQVRVVDEGKEPPEFWSLFG 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; ...
 491-603 5.29e-60

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: 200.91  E-value: 5.29e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233  491 TEDVGQLPGLTIWQIENFVPVLVEEAFHGKFYEADCYIVLKTFLDDSGSLNWEIYYWIGGEATLDKKACSAIHAVNLRNY 570
Cdd:cd11290     1 FEGVGQKPGLQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDPSGSLSYDIHYWLGKEASQDEAGAAAIKAVELDDY 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 564372233  571 LGAECRTAREEMGDESEGFLQVFDNDISYIEGG 603
Cdd:cd11290    81 LGGRPVQHREVQGHESEEFLSYFKKGIIYIEGG 113
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 1163-1262 1.33e-46

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: 162.08  E-value: 1.33e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233 1163 HTRLFRCSNEKGYFaVTEKCSDFCQDDLADDDIMLLDNGQEVYMWVGTQTSQVEIKLSLKACQVYIQHTRSKEHERPRRL 1242
Cdd:cd11291     1 KPRLFRCSNESGFF-KVEEISDFSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYIETDPLGRSKPRTPI 79

                          90       100
                  ....*....|....*....|
gi 564372233 1243 RLVRKGNEQRAFTRCFHAWS 1262
Cdd:cd11291    80 YLVKQGNEPPTFTGYFHAWD 99
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
38-374 1.09e-38

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 150.08  E-value: 1.09e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233   38 LKLNRTGLCYLPEELAALQKLEHLSVSHNNLTTLHGELSSLPSLRAIVARANSLKNSGVPDDIFKLDDLSVLDLSHNQLT 117
Cdd:COG4886     4 LLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233  118 E---CPRELENAKNMLVLNLSHNsidsipnQLFINLTDLLYLDLSENRLESLPPQMRRLVHLQTLVLNGNPLlhaqlrql 194
Cdd:COG4886    84 LlllGLTDLGDLTNLTELDLSGN-------EELSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQL-------- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233  195 pammalqtlhlrntqrtqSNLPTSLEGLSNLSDVDLSCNDLTRVPECLYTLPNLHRLNLSSNQIAELSLCIDQWVHLETL 274
Cdd:COG4886   149 ------------------TDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLEEL 210

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233  275 NLSRNQLTSLPSAickltklkklylnsnkldfdglpsgIGKLTSLEEFMAANNNLELIPEsLCRCPKLRKLVLNKNRLVT 354
Cdd:COG4886   211 DLSGNQLTDLPEP-------------------------LANLTNLETLDLSNNQLTDLPE-LGNLTNLEELDLSNNQLTD 264

                         330       340
                  ....*....|....*....|
gi 564372233  355 LPEAIHfLTEIEVLDVRENP 374
Cdd:COG4886   265 LPPLAN-LTNLKTLDLSNNQ 283
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
24-375 1.39e-38

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 149.70  E-value: 1.39e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233   24 YFPENVKAMTSLRWLKLNRTglcylpEELAALQKLEHLSVSHNNLTTLHGELSSLPSLRAIVARANSLKNsgVPDDIFKL 103
Cdd:COG4886    87 LGLTDLGDLTNLTELDLSGN------EELSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTD--LPEPLGNL 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233  104 DDLSVLDLSHNQLTECPRELENAKNMLVLNLSHNSIDSIPNQLFiNLTDLLYLDLSENRLESLPPQMRRLVHLQTLVLNG 183
Cdd:COG4886   159 TNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLG-NLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSN 237

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233  184 NpllhaQLRQLPammalqtlhlrntqrtqsnlptSLEGLSNLSDVDLSCNDLTRVPEcLYTLPNLHRLNLSSNQIAELSL 263
Cdd:COG4886   238 N-----QLTDLP----------------------ELGNLTNLEELDLSNNQLTDLPP-LANLTNLKTLDLSNNQLTDLKL 289

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233  264 cidqWVHLETLNLSRNQLTSLPSAICKLTKLKKLYLNSNKLDFDGLPSGIGKLTSLEEFMAANNNLELIPESLCRCPKLR 343
Cdd:COG4886   290 ----KELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTL 365

                         330       340       350
                  ....*....|....*....|....*....|..
gi 564372233  344 KLVLNKNRLVTLPEAIHFLTEIEVLDVRENPS 375
Cdd:COG4886   366 LLTLGLLGLLEATLLTLALLLLTLLLLLLTTT 397
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 1053-1152 9.37e-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: 130.81  E-value: 9.37e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233 1053 QPTLYQIRTNGSaLCTRCIQINTDSSLLNSEFCFILKVPFesednqgIVYAWVGRASDPDEAKLAEDILNTMFdPSYSKQ 1132
Cdd:cd11288     2 PTRLFQVRGNGS-GNTRAVEVDADASSLNSNDVFVLKTPS-------SVYLWVGKGSSEDERELAKDVASFLK-PKASLQ 72

                          90       100
                  ....*....|....*....|
gi 564372233 1133 VINEGEEPENFFWVGIGAQK 1152
Cdd:cd11288    73 EVAEGSEPDEFWEALGGKSE 92
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 722-836 7.88e-33

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: 122.74  E-value: 7.88e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233  722 PPQPKLYKVGLGLGYLELPQINYKLsvehkkrpkvelmpgmrLLQSLLDTRCVYILDCWSDVFIWLGRKSPRLVRAAALK 801
Cdd:cd11292     1 AEQKKLYKVSDASGKLKLTEVAEGS-----------------LNQEMLDSEDCYILDCGSEIFVWVGKGASLDERKAALK 63

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 564372233  802 LGQELCGMLHRPRHTVVSRSLEGTEAQVFKAKFKN 836
Cdd:cd11292    64 NAEEFLRKKKRPPYTQVTRVTEGGESALFKSKFAN 98
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
7-286 7.48e-31

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 126.97  E-value: 7.48e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233    7 LPFVRGVDLSGNDFKggYFPENVKAMTSLRWLKLNRTGLCYLPEELAALQKLEHLSVSHNNLTTLHGELSSLPSLRaiva 86
Cdd:COG4886   135 LTNLKELDLSNNQLT--DLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLE---- 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233   87 ranslknsgvpddifklddlsVLDLSHNQLTECPRELENAKNMLVLNLSHNSIDSIPNqlFINLTDLLYLDLSENRLESL 166
Cdd:COG4886   209 ---------------------ELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTDLPE--LGNLTNLEELDLSNNQLTDL 265

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233  167 PPQMrRLVHLQTLVLNGNPLLHAQLRQLPA----MMALQTLHLRNTQRTQSNLPTSLEGLSNLSDVDLSCNDLTRVPECL 242
Cdd:COG4886   266 PPLA-NLTNLKTLDLSNNQLTDLKLKELELllglNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSL 344

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 564372233  243 YTLPNLHRLNLSSNQIAELSLCIDQWVHLETLNLSRNQLTSLPS 286
Cdd:COG4886   345 SLLALLTLLLLLNLLSLLLTLLLTLGLLGLLEATLLTLALLLLT 388
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 618-702 8.63e-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: 107.84  E-value: 8.63e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233  618 TRMYRVYGKKNIKLEPVPLKGTSLDPRFVFLLDQGLDIYVWRGAQATLSNTTKARLFAEKMNKnERKGKAEITLLVQGQE 697
Cdd:cd11280     2 PRLYRVRGSKAIEIEEVPLASSSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKELDE-ERKGKPEIVRIRQGQE 80


                  ....*
gi 564372233  698 PPEFW 702
Cdd:cd11280    81 PREFW 85
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 619-707 3.70e-25

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 100.44  E-value: 3.70e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233    619 RMYRVYGKKNIKLEPVPLKGTSLDPRFVFLLDQGLDIYVWRGAQATLSNTTKARLFAEKMNKNERKGKAEITLLVQGQEP 698
Cdd:smart00262    1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVRVVDEGKEP 80


                    ....*....
gi 564372233    699 PEFWDVLGG 707
Cdd:smart00262   81 PEFWSLFGG 89
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 5-352 2.17e-23

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 107.63  E-value: 2.17e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233    5 GVLPFVRGVDLSGNDFKGGyFPENVKAMTSLRWLKLNRTGLC-YLPEELAALQKLEHLSVSHNNLT-TLHGELSSLPSLR 82
Cdd:PLN00113  137 GSIPNLETLDLSNNMLSGE-IPNDIGSFSSLKVLDLGGNVLVgKIPNSLTNLTSLEFLTLASNQLVgQIPRELGQMKSLK 215

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233   83 AIVARANSLkNSGVPDDIFKLDDLSVLDLSHNQLT-ECPRELENAKNMLVLNLSHNSI-DSIPNQLFiNLTDLLYLDLSE 160
Cdd:PLN00113  216 WIYLGYNNL-SGEIPYEIGGLTSLNHLDLVYNNLTgPIPSSLGNLKNLQYLFLYQNKLsGPIPPSIF-SLQKLISLDLSD 293

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233  161 NRLE-SLPPQMRRLVHLQTLVLNGNPLLHAQLRQLPAMMALQTLHLRnTQRTQSNLPTSLEGLSNLSDVDLSCNDLT-RV 238
Cdd:PLN00113  294 NSLSgEIPELVIQLQNLEILHLFSNNFTGKIPVALTSLPRLQVLQLW-SNKFSGEIPKNLGKHNNLTVLDLSTNNLTgEI 372

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233  239 PECLYTLPNLHRLNLSSNQI-----AELSLC----------------------------------------ID--QW--V 269
Cdd:PLN00113  373 PEGLCSSGNLFKLILFSNSLegeipKSLGACrslrrvrlqdnsfsgelpseftklplvyfldisnnnlqgrINsrKWdmP 452

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233  270 HLETLNLSRNQLT-SLPSAickltklkKLYLNSNKLD-----FDG-LPSGIGKLTSLEEFMAANNNLE-LIPESLCRCPK 341
Cdd:PLN00113  453 SLQMLSLARNKFFgGLPDS--------FGSKRLENLDlsrnqFSGaVPRKLGSLSELMQLKLSENKLSgEIPDELSSCKK 524

                         410
                  ....*....|.
gi 564372233  342 LRKLVLNKNRL 352
Cdd:PLN00113  525 LVSLDLSHNQL 535
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1168-1261 5.92e-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: 94.28  E-value: 5.92e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233   1168 RCSNEKGYFAVTEKCSDFCQDDLADDDIMLLDNGQEVYMWVGTQTSQVEIKLSLKACQVYIQHtrskEHERPRRLRLVRK 1247
Cdd:smart00262    1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDT----LGPGPVQVRVVDE 76

                            90
                    ....*....|....
gi 564372233   1248 GNEQRAFTRCFHAW 1261
Cdd:smart00262   77 GKEPPEFWSLFGGW 90
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 7-352 1.04e-22

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 105.32  E-value: 1.04e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233    7 LPFVRGVDLSGNDFKGGyFPENV-KAMTSLRWLKL---NRTGlcylPEELAALQKLEHLSVSHNNLT-TLHGELSSLPSL 81
Cdd:PLN00113   92 LPYIQTINLSNNQLSGP-IPDDIfTTSSSLRYLNLsnnNFTG----SIPRGSIPNLETLDLSNNMLSgEIPNDIGSFSSL 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233   82 RAIVARANSLKNSgVPDDIFKLDDLSVLDLSHNQLT-ECPRELENAKNMLVLNLSHNSID-SIPNQLFiNLTDLLYLDLS 159
Cdd:PLN00113  167 KVLDLGGNVLVGK-IPNSLTNLTSLEFLTLASNQLVgQIPRELGQMKSLKWIYLGYNNLSgEIPYEIG-GLTSLNHLDLV 244

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233  160 ENRLE-SLPPQMRRLVHLQTLVLNGNPLlhaqlrqlpammalqtlhlrntqrtQSNLPTSLEGLSNLSDVDLSCNDLtrv 238
Cdd:PLN00113  245 YNNLTgPIPSSLGNLKNLQYLFLYQNKL-------------------------SGPIPPSIFSLQKLISLDLSDNSL--- 296

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233  239 peclytlpnlhrlnlsSNQIAELslcIDQWVHLETLNLSRNQLT-SLPSAICKLTKLKKLYLNSNKLDfDGLPSGIGKLT 317
Cdd:PLN00113  297 ----------------SGEIPEL---VIQLQNLEILHLFSNNFTgKIPVALTSLPRLQVLQLWSNKFS-GEIPKNLGKHN 356

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 564372233  318 SLEEFMAANNNLE-LIPESLCRCPKLRKLVLNKNRL 352
Cdd:PLN00113  357 NLTVLDLSTNNLTgEIPEGLCSSGNLFKLILFSNSL 392
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
13-286 3.62e-22

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 100.78  E-value: 3.62e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233   13 VDLSGNDFKGgyFPENVKAMTSLRWLKLNRTGLCYLPEELAALQKLEHLSVSHNNLTTLHGELSSLPSLRaivaranslk 92
Cdd:COG4886   164 LDLSNNQLTD--LPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLE---------- 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233   93 nsgvpddifklddlsVLDLSHNQLTECPrELENAKNMLVLNLSHNSIDSIPNQLfiNLTDLLYLDLSENRLESLppqmrR 172
Cdd:COG4886   232 ---------------TLDLSNNQLTDLP-ELGNLTNLEELDLSNNQLTDLPPLA--NLTNLKTLDLSNNQLTDL-----K 288

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233  173 LVHLQTLVLNGNPLLHAQLRQLPAMM--ALQTLHLRNTQRTQSNLPTSLEGLSNLSDVDLSCNDLTRVPECLYTLPNLHR 250
Cdd:COG4886   289 LKELELLLGLNSLLLLLLLLNLLELLilLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLT 368

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 564372233  251 LNLSSNQIAELSLCIDQWVHLETLNLSRNQLTSLPS 286
Cdd:COG4886   369 LGLLGLLEATLLTLALLLLTLLLLLLTTTAGVLLLT 404
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 23-329 3.95e-21

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 100.31  E-value: 3.95e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233   23 GYFPENVKAMTSLRWLKLNRTGLC-YLPEELAALQKLEHLSVSHNNLT-TLHGELSSLPSLRAIVARANSLkNSGVPDDI 100
Cdd:PLN00113  274 GPIPPSIFSLQKLISLDLSDNSLSgEIPELVIQLQNLEILHLFSNNFTgKIPVALTSLPRLQVLQLWSNKF-SGEIPKNL 352

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233  101 FKLDDLSVLDLSHNQLT-ECPRELENAKNMLVLNLSHNSIDS-IPNQLFiNLTDLLYLDLSENRLE-SLPPQMRRLVHLQ 177
Cdd:PLN00113  353 GKHNNLTVLDLSTNNLTgEIPEGLCSSGNLFKLILFSNSLEGeIPKSLG-ACRSLRRVRLQDNSFSgELPSEFTKLPLVY 431

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233  178 TLVLNGNPLLHAQLRQLPAMMALQTLHL-RNtqRTQSNLPTSLeGLSNLSDVDLSCNDLT-RVPECLYTLPNLHRLNLSS 255
Cdd:PLN00113  432 FLDISNNNLQGRINSRKWDMPSLQMLSLaRN--KFFGGLPDSF-GSKRLENLDLSRNQFSgAVPRKLGSLSELMQLKLSE 508

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233  256 NQIA-----ELSLCidqwVHLETLNLSRNQLT-SLPSAICKLTKLKKLYLNSNKLDFDgLPSGIGKLTSLEEFMAANNNL 329
Cdd:PLN00113  509 NKLSgeipdELSSC----KKLVSLDLSHNQLSgQIPASFSEMPVLSQLDLSQNQLSGE-IPKNLGNVESLVQVNISHNHL 583
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 975-1035 8.57e-19

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


Pssm-ID: 200436  Cd Length: 88  Bit Score: 82.42  E-value: 8.57e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564372233  975 KQPEEDFQCIVYFWQGReASNMGWLTFTFSLQKKFESLFPGKLEVVRMTQQQENPKFLSHF 1035
Cdd:cd11280    29 DVFVLDTGSEIYIWQGR-ASSQAELAAAALLAKELDEERKGKPEIVRIRQGQEPREFWSLF 88
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
 500-593 2.41e-18

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: 81.55  E-value: 2.41e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233  500 LTIWQIENFVPVLVEEAFHGKFYEADCYIVLKTFlDDSGSLNWEIYYWIGGEATLDKKACSAIHAVNLRNYLGAECRTAR 579
Cdd:cd11293     9 VEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTY-QGGGKEEHILYFWQGRHSSQDERAAAALLTVELDEELKGRAVQVR 87

                          90
                  ....*....|....
gi 564372233  580 EEMGDESEGFLQVF 593
Cdd:cd11293    88 VVQGKEPPHFLALF 101
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 750-837 3.36e-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: 3.36e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233    750 HKKRPKVELMPGMRLLQSLLDTRCVYILDCWSDVFIWLGRKSPRLVRAAALKLGQELCGMLHrPRHTVVSRSLEGTEAQV 829
Cdd:smart00262    4 RVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLG-PGPVQVRVVDEGKEPPE 82


                    ....*...
gi 564372233    830 FKAKFKNW 837
Cdd:smart00262   83 FWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 502-595 1.80e-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: 75.79  E-value: 1.80e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233    502 IWQIENFVPVLVEE--AFHGKFYEADCYIVLKTflddsgslnWEIYYWIGGEATLDKKACSAIHAVNLRNYLGAE-CRTA 578
Cdd:smart00262    2 LVRVKGKRNVRVPEvpFSQGSLNSGDCYILDTG---------SEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGpVQVR 72

                            90
                    ....*....|....*..
gi 564372233    579 REEMGDESEGFLQVFDN 595
Cdd:smart00262   73 VVDEGKEPPEFWSLFGG 89
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
26-288 2.19e-16

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 84.75  E-value: 2.19e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233   26 PENVKAMTSLR-WLKLNRTGLC-----------YLPEELAALqklehlSVSHNNLTTLHGELSSlpSLRAIVARANSLkn 93
Cdd:PRK15370  163 ANREEAVQRMRdCLKNNKTELRlkilglttipaCIPEQITTL------ILDNNELKSLPENLQG--NIKTLYANSNQL-- 232

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233   94 SGVPDDIfkLDDLSVLDLSHNQLTECPRELENAknMLVLNLSHNSIDSIPNqlfiNLTD-LLYLDLSENRLESLPPQM-R 171
Cdd:PRK15370  233 TSIPATL--PDTIQEMELSINRITELPERLPSA--LQSLDLFHNKISCLPE----NLPEeLRYLSVYDNSIRTLPAHLpS 304

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233  172 RLVHLqtLVLNGNpllhaqLRQLPAMMALQTLHLRNTQRTQSNLPTSLEglSNLSDVDLSCNDLTRVPECLytLPNLHRL 251
Cdd:PRK15370  305 GITHL--NVQSNS------LTALPETLPPGLKTLEAGENALTSLPASLP--PELQVLDVSKNQITVLPETL--PPTITTL 372

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 564372233  252 NLSSNQIAELSLCIDqwVHLETLNLSRNQLTSLPSAI 288
Cdd:PRK15370  373 DVSRNALTNLPENLP--AALQIMQASRNNLVRLPESL 407
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1057-1149 4.49e-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: 74.64  E-value: 4.49e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233   1057 YQIRTNGSaLCTRCIQINTDSSLLNSEFCFILkvpfeseDNQGIVYAWVGRASDPDE----AKLAEDILNTMFDPSYSKQ 1132
Cdd:smart00262    1 FLVRVKGK-RNVRVPEVPFSQGSLNSGDCYIL-------DTGSEIYVWVGKKSSQDEkkkaAELAVELDDTLGPGPVQVR 72

                            90
                    ....*....|....*..
gi 564372233   1133 VINEGEEPENFFWVGIG 1149
Cdd:smart00262   73 VVDEGKEPPEFWSLFGG 89
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 103-285 5.11e-16

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: 78.29  E-value: 5.11e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233  103 LDDLSVLDLSHNQLTECPrELENAKNMLVLNLSHNSIDSIPNqlFINLTDLLYLDLSENRLESLPPqMRRLVHLQTLVLN 182
Cdd:cd21340     1 LKRITHLYLNDKNITKID-NLSLCKNLKVLYLYDNKITKIEN--LEFLTNLTHLYLQNNQIEKIEN-LENLVNLKKLYLG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233  183 GNPLlhAQLRQLPAMMALQTLHLRNtQRTQSNL-----PTSLEGLSN-LSDVDLSCNDLTRVpECLYTLPNLHRLNLSSN 256
Cdd:cd21340    77 GNRI--SVVEGLENLTNLEELHIEN-QRLPPGEkltfdPRSLAALSNsLRVLNISGNNIDSL-EPLAPLRNLEQLDASNN 152

                         170       180       190
                  ....*....|....*....|....*....|..
gi 564372233  257 QIA---ELSLCIDQWVHLETLNLSRNQLTSLP 285
Cdd:cd21340   153 QISdleELLDLLSSWPSLRELDLTGNPVCKKP 184
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 617-706 5.95e-16

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


Pssm-ID: 200445  Cd Length: 92  Bit Score: 74.20  E-value: 5.95e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233  617 VTRMYRVYGKKNIKLEPVPLKGTSLDPRFVFLLDQGLDIYVWRGAQATLSNTTKARLFAEKMNKNERKGKAEITLLVQG- 695
Cdd:cd11289     1 KPRLLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKVIVLDEGd 80

                          90
                  ....*....|..
gi 564372233  696 -QEPPEFWDVLG 706
Cdd:cd11289    81 tNESPEFWKVLG 92
Gelsolin pfam00626
Gelsolin repeat;
627-702 6.64e-15

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 70.80  E-value: 6.64e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564372233   627 KNIKLEPVPLKGTSLDPRFVFLLDQGLDIYVWRGAQATLSNTTKARLFAEKMNKNERKGKAEITLLVQGQEPPEFW 702
Cdd:pfam00626    1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDERFPLPEVIRVPQGKEPARFL 76
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
191-379 6.08e-14

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 76.66  E-value: 6.08e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233  191 LRQLPAMMALQTLHLRNTQRTQSNLPTSLEGlsNLSDVDLSCNDLTRVPEclyTLPN-LHRLNLSSNQIAELSLCIDQwv 269
Cdd:PRK15370  190 LTTIPACIPEQITTLILDNNELKSLPENLQG--NIKTLYANSNQLTSIPA---TLPDtIQEMELSINRITELPERLPS-- 262

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233  270 HLETLNLSRNQLTSLPSAICKLTKLKKLYLNSNKLDFDGLPSGIgkltslEEFMAANNNLELIPESLcrCPKLRKLVLNK 349
Cdd:PRK15370  263 ALQSLDLFHNKISCLPENLPEELRYLSVYDNSIRTLPAHLPSGI------THLNVQSNSLTALPETL--PPGLKTLEAGE 334

                         170       180       190
                  ....*....|....*....|....*....|
gi 564372233  350 NRLVTLPEAIHflTEIEVLDVRENPSLVMP 379
Cdd:PRK15370  335 NALTSLPASLP--PELQVLDVSKNQITVLP 362
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 127-369 1.08e-12

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: 68.66  E-value: 1.08e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233  127 KNMLVLNLSHNSIDSIPNqlFINLTDLLYLDLSENRLESLP--PQMRRLVHLQtlvlngnpLLHAQLRQLPammalqtlh 204
Cdd:cd21340     2 KRITHLYLNDKNITKIDN--LSLCKNLKVLYLYDNKITKIEnlEFLTNLTHLY--------LQNNQIEKIE--------- 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233  205 lrntqrtqsnlptSLEGLSNLSDVDLSCNDLTRVpECLYTLPNLHRLNLSSNQIAE-LSLCID----QWV--HLETLNLS 277
Cdd:cd21340    63 -------------NLENLVNLKKLYLGGNRISVV-EGLENLTNLEELHIENQRLPPgEKLTFDprslAALsnSLRVLNIS 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233  278 RNQLTSLpsaickltklkklylnsnkldfdglpSGIGKLTSLEEFMAANNNLELIPE---SLCRCPKLRKLVLNKNRLVT 354
Cdd:cd21340   129 GNNIDSL--------------------------EPLAPLRNLEQLDASNNQISDLEElldLLSSWPSLRELDLTGNPVCK 182

                         250
                  ....*....|....*....
gi 564372233  355 LP----EAIHFLTEIEVLD 369
Cdd:cd21340   183 KPkyrdKIILASKSLEVLD 201
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
127-379 1.26e-12

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 72.42  E-value: 1.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233  127 KNMLVLNLSHNSIDSIPNQLFINLTDLLyldLSENRLESLPPQMRrlVHLQTLVLNGNpllhaQLRQLPAMM--ALQTLH 204
Cdd:PRK15370  178 NNKTELRLKILGLTTIPACIPEQITTLI---LDNNELKSLPENLQ--GNIKTLYANSN-----QLTSIPATLpdTIQEME 247

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233  205 LRNTQRTQ--SNLPTSLEGLsnlsdvDLSCNDLTRVPEclyTLPNlhrlnlssnqiaelslcidqwvHLETLNLSRNQLT 282
Cdd:PRK15370  248 LSINRITElpERLPSALQSL------DLFHNKISCLPE---NLPE----------------------ELRYLSVYDNSIR 296

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233  283 SLPSAICKLTKLKKLYLNSNKLDFDGLPSGigkltsLEEFMAANNNLELIPESLCrcPKLRKLVLNKNRLVTLPEAIHfl 362
Cdd:PRK15370  297 TLPAHLPSGITHLNVQSNSLTALPETLPPG------LKTLEAGENALTSLPASLP--PELQVLDVSKNQITVLPETLP-- 366

                         250
                  ....*....|....*..
gi 564372233  363 TEIEVLDVRENPSLVMP 379
Cdd:PRK15370  367 PTITTLDVSRNALTNLP 383
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 618-707 3.87e-12

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: 63.40  E-value: 3.87e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233  618 TRMYRVYG--KKNIKLEPVPLKGTSLDPRFVFLLDQGLDIYVWRGAQATLSNTTKARLFAEKMnknerKGKAEITLLVQG 695
Cdd:cd11288     3 TRLFQVRGngSGNTRAVEVDADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVASFL-----KPKASLQEVAEG 77

                          90
                  ....*....|..
gi 564372233  696 QEPPEFWDVLGG 707
Cdd:cd11288    78 SEPDEFWEALGG 89
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 4-256 1.01e-11

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 69.88  E-value: 1.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233    4 TGVLPfvRGVDLSGNDFK--------GGYFPENVKAMTSLRWLKLNRTGLC-YLPEELAALQKLEHLSVSHNNLTtlhGE 74
Cdd:PLN00113  369 TGEIP--EGLCSSGNLFKlilfsnslEGEIPKSLGACRSLRRVRLQDNSFSgELPSEFTKLPLVYFLDISNNNLQ---GR 443

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233   75 LSS----LPSLRAIVARANSLknSGVPDDIFKLDDLSVLDLSHNQLTEcprelenaknmlvlnlshnsidSIPNQlFINL 150
Cdd:PLN00113  444 INSrkwdMPSLQMLSLARNKF--FGGLPDSFGSKRLENLDLSRNQFSG----------------------AVPRK-LGSL 498

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233  151 TDLLYLDLSENRLESLPPqmrrlvhlqtlvlngnpllhaqlRQLPAMMALQTLHLRNTQRTqSNLPTSLEGLSNLSDVDL 230
Cdd:PLN00113  499 SELMQLKLSENKLSGEIP-----------------------DELSSCKKLVSLDLSHNQLS-GQIPASFSEMPVLSQLDL 554

                         250       260
                  ....*....|....*....|....*..
gi 564372233  231 SCNDLT-RVPECLYTLPNLHRLNLSSN 256
Cdd:PLN00113  555 SQNQLSgEIPKNLGNVESLVQVNISHN 581
LRR_8 pfam13855
Leucine rich repeat;
131-186 1.68e-11

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 60.62  E-value: 1.68e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 564372233   131 VLNLSHNSIDSIPNQLFINLTDLLYLDLSENRLESLPPQM-RRLVHLQTLVLNGNPL 186
Cdd:pfam13855    5 SLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAfSGLPSLRYLDLSGNRL 61
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 1164-1264 2.11e-11

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


Pssm-ID: 200436  Cd Length: 88  Bit Score: 61.23  E-value: 2.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233 1164 TRLFRCSNEK-GYFAVTEKCSDfcqdDLADDDIMLLDNGQEVYMWVGTQTSQVEiklsLKACQVYIQHTRSKEHERPRRL 1242
Cdd:cd11280     2 PRLYRVRGSKaIEIEEVPLASS----SLDSDDVFVLDTGSEIYIWQGRASSQAE----LAAAALLAKELDEERKGKPEIV 73

                          90       100
                  ....*....|....*....|..
gi 564372233 1243 RlVRKGNEQRAFtrcfhaWSTF 1264
Cdd:cd11280    74 R-IRQGQEPREF------WSLF 88
Gelsolin pfam00626
Gelsolin repeat;
507-590 2.60e-11

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 60.40  E-value: 2.60e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233   507 NFVPVLVEEAFHGKFYEADCYIVLKTFlddsgslnwEIYYWIGGEATLDKKACSAIHAVNLR-NYLGAECRTAREEMGDE 585
Cdd:pfam00626    1 KFVLPPPVPLSQESLNSGDCYLLDNGF---------TIFLWVGKGSSLLEKLFAALLAAQLDdDERFPLPEVIRVPQGKE 71


                   ....*
gi 564372233   586 SEGFL 590
Cdd:pfam00626   72 PARFL 76
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 50-188 1.26e-10

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: 62.50  E-value: 1.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233   50 EELAALQKLEHLSVSHNNLTTLHGeLSSLPSLRAIVARANSLKnsgVPDDIFKLDDLSVLDLSHNQLT--EC----PREL 123
Cdd:cd21340    40 ENLEFLTNLTHLYLQNNQIEKIEN-LENLVNLKKLYLGGNRIS---VVEGLENLTNLEELHIENQRLPpgEKltfdPRSL 115

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564372233  124 EN-AKNMLVLNLSHNSIDSIpNQLFiNLTDLLYLDLSENRLESLPPQ---MRRLVHLQTLVLNGNPLLH 188
Cdd:cd21340   116 AAlSNSLRVLNISGNNIDSL-EPLA-PLRNLEQLDASNNQISDLEELldlLSSWPSLRELDLTGNPVCK 182
PRK15387 PRK15387
type III secretion system effector E3 ubiquitin transferase SspH2;
131-374 1.87e-10

type III secretion system effector E3 ubiquitin transferase SspH2;


Pssm-ID: 185285 [Multi-domain]  Cd Length: 788  Bit Score: 65.57  E-value: 1.87e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233  131 VLNLSHNSIDSIPNQLFINLTDLLYLDLSENRLESLPPQMRrlvhlqTLVLNGNpllhaQLRQLPaMMALQTLHLRNTQR 210
Cdd:PRK15387  205 VLNVGESGLTTLPDCLPAHITTLVIPDNNLTSLPALPPELR------TLEVSGN-----QLTSLP-VLPPGLLELSIFSN 272

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233  211 TQSNLPTSLEGLSNLSdvdLSCNDLTRVPeclYTLPNLHRLNLSSNQIAEL-----SLCiDQWVH-------------LE 272
Cdd:PRK15387  273 PLTHLPALPSGLCKLW---IFGNQLTSLP---VLPPGLQELSVSDNQLASLpalpsELC-KLWAYnnqltslptlpsgLQ 345

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233  273 TLNLSRNQLTSLPSaiCKLTKLKKLYLNSNKLDFDGLPSGIGKL--------------TSLEEFMAANNNLELIPeslcR 338
Cdd:PRK15387  346 ELSVSDNQLASLPT--LPSELYKLWAYNNRLTSLPALPSGLKELivsgnrltslpvlpSELKELMVSGNRLTSLP----M 419

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 564372233  339 CPK-LRKLVLNKNRLVTLPEAIHFLTEIEVLDVRENP 374
Cdd:PRK15387  420 LPSgLLSLSVYRNQLTRLPESLIHLSSETTVNLEGNP 456
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 617-701 1.57e-09

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


Pssm-ID: 200448  Cd Length: 98  Bit Score: 56.10  E-value: 1.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233  617 VTRMYRVY-GKKNIKLEPV---PLKGTSLDPRFVFLLDQGLDIYVWRGAQATLSNTTKARLFAEK-MNKNERKGKAEITL 691
Cdd:cd11292     3 QKKLYKVSdASGKLKLTEVaegSLNQEMLDSEDCYILDCGSEIFVWVGKGASLDERKAALKNAEEfLRKKKRPPYTQVTR 82

                          90
                  ....*....|
gi 564372233  692 LVQGQEPPEF 701
Cdd:cd11292    83 VTEGGESALF 92
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 1053-1143 3.17e-09

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


Pssm-ID: 200448  Cd Length: 98  Bit Score: 55.33  E-value: 3.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233 1053 QPTLYQIRTNGSALCTRCIQINT-DSSLLNSEFCFILkvpfeseDNQGIVYAWVGRASDPDEAK----LAEDILNTMFDP 1127
Cdd:cd11292     3 QKKLYKVSDASGKLKLTEVAEGSlNQEMLDSEDCYIL-------DCGSEIFVWVGKGASLDERKaalkNAEEFLRKKKRP 75

                          90
                  ....*....|....*..
gi 564372233 1128 SYSK-QVINEGEEPENF 1143
Cdd:cd11292    76 PYTQvTRVTEGGESALF 92
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 89-375 5.57e-09

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: 59.29  E-value: 5.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233   89 NSLKNSGVPDDIFKLDDLSVLDLSHNQLTE-----CPRELENAKNMLVLNLSHNSIDSIPNQL------FINLTDLLYLD 157
Cdd:cd00116     8 ELLKTERATELLPKLLCLQVLRLEGNTLGEeaakaLASALRPQPSLKELCLSLNETGRIPRGLqsllqgLTKGCGLQELD 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233  158 LSEN--------RLESLppqmRRLVHLQTLVLNGN-------PLLHAQLRQLPamMALQTLHL-RNTQRTQSNLPTSLEG 221
Cdd:cd00116    88 LSDNalgpdgcgVLESL----LRSSSLQELKLNNNglgdrglRLLAKGLKDLP--PALEKLVLgRNRLEGASCEALAKAL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233  222 LSN--LSDVDLSCNDL-----TRVPECLYTLPNLHRLNLSSNQIAE-----LSLCIDQWVHLETLNLSRNQLTSLP-SAI 288
Cdd:cd00116   162 RANrdLKELNLANNGIgdagiRALAEGLKANCNLEVLDLNNNGLTDegasaLAETLASLKSLEVLNLGDNNLTDAGaAAL 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233  289 CkltklkklylnsnkldfDGLPSGIGKLTSLEefmAANNNLELIP-ESLCRC----PKLRKLVLNKNRLVTLPEAIHFLT 363
Cdd:cd00116   242 A-----------------SALLSPNISLLTLS---LSCNDITDDGaKDLAEVlaekESLLELDLRGNKFGEEGAQLLAES 301

                         330
                  ....*....|....*...
gi 564372233  364 ------EIEVLDVRENPS 375
Cdd:cd00116   302 llepgnELESLWVKDDSF 319
LRR_8 pfam13855
Leucine rich repeat;
106-163 8.97e-09

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 52.91  E-value: 8.97e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 564372233   106 LSVLDLSHNQLTECPRE-LENAKNMLVLNLSHNSIDSIPNQLFINLTDLLYLDLSENRL 163
Cdd:pfam13855    3 LRSLDLSNNRLTSLDDGaFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 766-838 1.53e-08

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: 53.46  E-value: 1.53e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564372233  766 QSLLDTRCVYILDCWSDVFIWLGRKSPRLVRAAALKLGQ---ELCGMLHRPRHTVVSRSLEGTEAQVFKAKFKNWD 838
Cdd:cd11291    24 QDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKkyiETDPLGRSKPRTPIYLVKQGNEPPTFTGYFHAWD 99
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 767-834 2.38e-08

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: 52.37  E-value: 2.38e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564372233  767 SLLDTRCVYILDCWSDVFIWLGRKSPRLVRAAALKLGQELcgMLHRPRHTVVSRSLEGTEAQVFKAKF 834
Cdd:cd11280    23 SSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKEL--DEERKGKPEIVRIRQGQEPREFWSLF 88
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 502-593 2.40e-08

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: 52.37  E-value: 2.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233  502 IWQIENFVPVLVEE--AFHGKFYEADCYIVlktfldDSGSlnwEIYYWIGGEATLDKKACSAIHAVNLRNYLGAECRTAR 579
Cdd:cd11280     4 LYRVRGSKAIEIEEvpLASSSLDSDDVFVL------DTGS---EIYIWQGRASSQAELAAAALLAKELDEERKGKPEIVR 74

                          90
                  ....*....|....
gi 564372233  580 EEMGDESEGFLQVF 593
Cdd:cd11280    75 IRQGQEPREFWSLF 88
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 1164-1258 5.14e-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: 5.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233 1164 TRLFRCSNEKGYFAVTE-KCSDFCQDDLADDDIMLLDNGQEVYMWVGTQTSQVEIKLSLKACQVYIQhtrskEHERPRRL 1242
Cdd:cd11292     4 KKLYKVSDASGKLKLTEvAEGSLNQEMLDSEDCYILDCGSEIFVWVGKGASLDERKAALKNAEEFLR-----KKKRPPYT 78

                          90
                  ....*....|....*...
gi 564372233 1243 RLVR--KGNEQRAFTRCF 1258
Cdd:cd11292    79 QVTRvtEGGESALFKSKF 96
Gelsolin pfam00626
Gelsolin repeat;
1181-1254 5.74e-07

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 48.07  E-value: 5.74e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564372233  1181 KCSDFCQDDLADDDIMLLDNGQEVYMWVGTQTSQVEIKLSLKACQVYIQHTRskeHERPRRLRLVRkGNEQRAF 1254
Cdd:pfam00626    6 PPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDER---FPLPEVIRVPQ-GKEPARF 75
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 641-703 9.13e-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: 48.45  E-value: 9.13e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564372233  641 LDPRFVFLLDQGLDIYVWRGAQAT-----LSNTTkARLFAEKMNKNERKGKAEITLLVQGQEPPEF------WD 703
Cdd:cd11291    27 LDTDDIMLLDTGDEVFVWVGSESSdeekkEALTS-AKKYIETDPLGRSKPRTPIYLVKQGNEPPTFtgyfhaWD 99
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 106-284 1.05e-06

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: 52.87  E-value: 1.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233  106 LSVLDLSHNQL-TECPRELENA----KNMLVLNLSHNSID----SIPNQLFINLTDLLYLDLSENRL---------ESLp 167
Cdd:COG5238   182 VETVYLGCNQIgDEGIEELAEAltqnTTVTTLWLKRNPIGdegaEILAEALKGNKSLTTLDLSNNQIgdegvialaEAL- 260

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233  168 pQMRRLVHlqTLVLNGNPLLHAQLRQLPAMMA----LQTLHLRNTQ---RTQSNLPTSLEGLSNLSDVDLSCNDLT---- 236
Cdd:COG5238   261 -KNNTTVE--TLYLSGNQIGAEGAIALAKALQgnttLTSLDLSVNRigdEGAIALAEGLQGNKTLHTLNLAYNGIGaqga 337

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 564372233  237 -RVPECLYTLPNLHRLNLSSNQI-----AELSLCIDQWVHLETLNLSRNQLTSL 284
Cdd:COG5238   338 iALAKALQENTTLHSLDLSDNQIgdegaIALAKYLEGNTTLRELNLGKNNIGKQ 391
LRR_8 pfam13855
Leucine rich repeat;
223-281 1.33e-06

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 46.75  E-value: 1.33e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564372233   223 SNLSDVDLSCNDLTRV-PECLYTLPNLHRLNLSSNQIAELSL-CIDQWVHLETLNLSRNQL 281
Cdd:pfam13855    1 PNLRSLDLSNNRLTSLdDGAFKGLSNLKVLDLSNNLLTTLSPgAFSGLPSLRYLDLSGNRL 61
Gelsolin pfam00626
Gelsolin repeat;
755-831 1.68e-06

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 46.92  E-value: 1.68e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564372233   755 KVELMPGMRLLQSLLDTRCVYILDCWSDVFIWLGRKSPRLVRAAALKLGQELcGMLHRPRHTVVSRSLEGTEAQVFK 831
Cdd:pfam00626    1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQL-DDDERFPLPEVIRVPQGKEPARFL 76
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 33-200 5.10e-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: 5.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233   33 TSLRWLKLNR------------TGLCYLPEELAALQkLEHLSVSHNNLTTLHGELSSLPSLRAIVARANSLKNSGVPD-- 98
Cdd:cd00116   108 SSLQELKLNNnglgdrglrllaKGLKDLPPALEKLV-LGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRAla 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233   99 DIFK-LDDLSVLDLSHNQLT--------ECPRELenaKNMLVLNLSHNSIDSIP-----NQLFINLTDLLYLDLSENRLE 164
Cdd:cd00116   187 EGLKaNCNLEVLDLNNNGLTdegasalaETLASL---KSLEVLNLGDNNLTDAGaaalaSALLSPNISLLTLSLSCNDIT 263

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 564372233  165 -----SLPPQMRRLVHLQTLVLNGNPL------LHAQLRQLPAMMAL 200
Cdd:cd00116   264 ddgakDLAEVLAEKESLLELDLRGNKFgeegaqLLAESLLEPGNELE 310
PRK15387 PRK15387
type III secretion system effector E3 ubiquitin transferase SspH2;
38-325 5.19e-06

type III secretion system effector E3 ubiquitin transferase SspH2;


Pssm-ID: 185285 [Multi-domain]  Cd Length: 788  Bit Score: 50.93  E-value: 5.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233   38 LKLNRTGLCYLPEELAAlqKLEHLSVSHNNLTTLHgelSSLPSLRAIVARANSLKNSGV-PDDIFKLDDLSvldlshNQL 116
Cdd:PRK15387  206 LNVGESGLTTLPDCLPA--HITTLVIPDNNLTSLP---ALPPELRTLEVSGNQLTSLPVlPPGLLELSIFS------NPL 274

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233  117 TECPRELENAKNMLVLNlshNSIDSIPnqlfINLTDLLYLDLSENRLESLPPQMRRLVHLQTLvlngnpllHAQLRQLPA 196
Cdd:PRK15387  275 THLPALPSGLCKLWIFG---NQLTSLP----VLPPGLQELSVSDNQLASLPALPSELCKLWAY--------NNQLTSLPT 339

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233  197 M-MALQTLHLRNTQRTQ--------------SNLPTSLEGL-SNLSDVDLSCNDLTRVPeclyTLPN-LHRLNLSSNQIA 259
Cdd:PRK15387  340 LpSGLQELSVSDNQLASlptlpselyklwayNNRLTSLPALpSGLKELIVSGNRLTSLP----VLPSeLKELMVSGNRLT 415

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564372233  260 ELSLCIDQwvhLETLNLSRNQLTSLPSAICkltklkkLYLNSNKLDFDGLPSGIGKLTSLEEFMAA 325
Cdd:PRK15387  416 SLPMLPSG---LLSLSVYRNQLTRLPESLI-------HLSSETTVNLEGNPLSERTLQALREITSA 471
Gelsolin pfam00626
Gelsolin repeat;
1076-1143 5.19e-06

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 45.38  E-value: 5.19e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564372233  1076 DSSLLNSEFCFILkvpfeseDNQGIVYAWVGRASDPDE----AKLAEDILNTMFDPSYSKQVINEGEEPENF 1143
Cdd:pfam00626   11 SQESLNSGDCYLL-------DNGFTIFLWVGKGSSLLEklfaALLAAQLDDDERFPLPEVIRVPQGKEPARF 75
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 1053-1145 1.59e-05

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


Pssm-ID: 200436  Cd Length: 88  Bit Score: 44.67  E-value: 1.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233 1053 QPTLYQIRTNGSalcTRCIQINTDSSLLNSEFCFILkvpfeseDNQGIVYAWVGRASDPDE----AKLAEDILNTMFD-P 1127
Cdd:cd11280     1 PPRLYRVRGSKA---IEIEEVPLASSSLDSDDVFVL-------DTGSEIYIWQGRASSQAElaaaALLAKELDEERKGkP 70

                          90
                  ....*....|....*...
gi 564372233 1128 SYskQVINEGEEPEnFFW 1145
Cdd:cd11280    71 EI--VRIRQGQEPR-EFW 85
LRR_8 pfam13855
Leucine rich repeat;
200-258 2.07e-05

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 43.28  E-value: 2.07e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564372233   200 LQTLHLRNtqrtqSNL----PTSLEGLSNLSDVDLSCNDLTRV-PECLYTLPNLHRLNLSSNQI 258
Cdd:pfam13855    3 LRSLDLSN-----NRLtsldDGAFKGLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 75-282 4.10e-05

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: 47.48  E-value: 4.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233   75 LSSLPSLRAIVARANSLKNSGVPDdIFK----LDDLSVLDLSHNQLT-----ECPRELENAKNMLVLNLSHNSID----- 140
Cdd:COG5238   204 LTQNTTVTTLWLKRNPIGDEGAEI-LAEalkgNKSLTTLDLSNNQIGdegviALAEALKNNTTVETLYLSGNQIGaegai 282

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233  141 SIPNQLFINlTDLLYLDLSENRL-----ESLPPQMRRLVHLQTLVLNGNPLLHAQLRQLPAmmALQTLhlrntqrtqsnl 215
Cdd:COG5238   283 ALAKALQGN-TTLTSLDLSVNRIgdegaIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAK--ALQEN------------ 347

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564372233  216 ptsleglSNLSDVDLSCNDLT-----RVPECLYTLPNLHRLNLSSNQIAEL-------SLCIDQwvhLETLNLSRNQLT 282
Cdd:COG5238   348 -------TTLHSLDLSDNQIGdegaiALAKYLEGNTTLRELNLGKNNIGKQgaealidALQTNR---LHTLILDGNLIG 416
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 2-139 5.99e-05

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: 46.58  E-value: 5.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233    2 EATGVLPFVRG---VDLSGNDFKGGYFP---ENVKAMTSLRWLKLNRTGLC-----YLPEELAALQKLEHLSVSHNNLT- 69
Cdd:cd00116   156 ALAKALRANRDlkeLNLANNGIGDAGIRalaEGLKANCNLEVLDLNNNGLTdegasALAETLASLKSLEVLNLGDNNLTd 235

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233   70 ----TLH-GELSSLPSLRAIVARANSLKNSGVPDDIFKLDD---LSVLDLSHNQLTE------CPRELENAKNMLVLNLS 135
Cdd:cd00116   236 agaaALAsALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEkesLLELDLRGNKFGEegaqllAESLLEPGNELESLWVK 315


                  ....
gi 564372233  136 HNSI 139
Cdd:cd00116   316 DDSF 319
LRR_8 pfam13855
Leucine rich repeat;
33-91 1.13e-04

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 41.36  E-value: 1.13e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564372233    33 TSLRWLKLNRTGLCYLPEE-LAALQKLEHLSVSHNNLTTLH-GELSSLPSLRAIVARANSL 91
Cdd:pfam13855    1 PNLRSLDLSNNRLTSLDDGaFKGLSNLKVLDLSNNLLTTLSpGAFSGLPSLRYLDLSGNRL 61
PLN03210 PLN03210
Resistant to P. syringae 6; Provisional
 127-401 2.21e-04

Resistant to P. syringae 6; Provisional


Pssm-ID: 215633 [Multi-domain]  Cd Length: 1153  Bit Score: 45.64  E-value: 2.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233  127 KNMLVLNLSHNSIDS--IPNQLFINLTDLLYLDLSENRLES-------LPPQMRRLVH-LQTLVLNGNPLlhaqlRQLPA 196
Cdd:PLN03210  532 KKVLGITLDIDEIDElhIHENAFKGMRNLLFLKFYTKKWDQkkevrwhLPEGFDYLPPkLRLLRWDKYPL-----RCMPS 606

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233  197 mmALQTLHLRNTQRTQSNLPTSLEG---LSNLSDVDL-SCNDLTRVPEcLYTLPNLHRLNLSS-NQIAELSLCIDQWVHL 271
Cdd:PLN03210  607 --NFRPENLVKLQMQGSKLEKLWDGvhsLTGLRNIDLrGSKNLKEIPD-LSMATNLETLKLSDcSSLVELPSSIQYLNKL 683

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233  272 ETLNLSR-NQLTSLPSAICKLTKLKKLYLNSNKLD-FDGLPSGIGKL----TSLEEFmAANNNLE-LIPESLCRC----- 339
Cdd:PLN03210  684 EDLDMSRcENLEILPTGINLKSLYRLNLSGCSRLKsFPDISTNISWLdldeTAIEEF-PSNLRLEnLDELILCEMksekl 762

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564372233  340 ---------------PKLRKLVLNKN-RLVTLPEAIHFLTEIEVLDVRENPSLVMPPKPADHTAeWYNIDFSLQNQLR 401
Cdd:PLN03210  763 wervqpltplmtmlsPSLTRLFLSDIpSLVELPSSIQNLHKLEHLEIENCINLETLPTGINLES-LESLDLSGCSRLR 839
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 246-285 3.76e-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: 39.15  E-value: 3.76e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 564372233   246 PNLHRLNLSSNQIAELSLcIDQWVHLETLNLSRN-QLTSLP 285
Cdd:pfam12799    1 PNLEVLDLSNNQITDIPP-LAKLPNLETLDLSGNnKITDLS 40
PLN03150 PLN03150
hypothetical protein; Provisional
 90-204 4.42e-04

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 44.42  E-value: 4.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233   90 SLKNSG----VPDDIFKLddlsvldlshnqltecpRELENaknmlvLNLSHNSIDSIPNQLFINLTDLLYLDLSENRLE- 164
Cdd:PLN03150  424 GLDNQGlrgfIPNDISKL-----------------RHLQS------INLSGNSIRGNIPPSLGSITSLEVLDLSYNSFNg 480

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 564372233  165 SLPPQMRRLVHLQTLVLNGNPLLHaqlrQLPAMMALQTLH 204
Cdd:PLN03150  481 SIPESLGQLTSLRILNLNGNSLSG----RVPAALGGRLLH 516
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 912-1036 1.12e-03

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: 39.20  E-value: 1.12e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233    912 EGRKFTRLAEEEF--GHFYTQDCYVFLCRYwvpveyeeeekpedkegkasaegreeeeaaaeteekqpeedfqcIVYFWQ 989
Cdd:smart00262    6 KGKRNVRVPEVPFsqGSLNSGDCYILDTGS--------------------------------------------EIYVWV 41

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*..
gi 564372233    990 GREASNMGWLTFTFSLQKKFESLFPGKLEVVRMTQQQENPKFLSHFK 1036
Cdd:smart00262   42 GKKSSQDEKKKAAELAVELDDTLGPGPVQVRVVDEGKEPPEFWSLFG 88
LRR_8 pfam13855
Leucine rich repeat;
270-352 1.68e-03

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 37.89  E-value: 1.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233   270 HLETLNLSRNQLTSLPSAIckltklkklylnsnkldFDGLPSgigkltsLEEFMAANNNLELI-PESLCRCPKLRKLVLN 348
Cdd:pfam13855    2 NLRSLDLSNNRLTSLDDGA-----------------FKGLSN-------LKVLDLSNNLLTTLsPGAFSGLPSLRYLDLS 57


                   ....
gi 564372233   349 KNRL 352
Cdd:pfam13855   58 GNRL 61
PLN03150 PLN03150
hypothetical protein; Provisional
 33-117 2.29e-03

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 42.11  E-value: 2.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372233   33 TSLRW----LKLNRTGL-CYLPEELAALQKLEHLSVSHNNlttLHGELS----SLPSLRAIVARANSLkNSGVPDDIFKL 103
Cdd:PLN03150  414 TKGKWfidgLGLDNQGLrGFIPNDISKLRHLQSINLSGNS---IRGNIPpslgSITSLEVLDLSYNSF-NGSIPESLGQL 489

                          90
                  ....*....|....
gi 564372233  104 DDLSVLDLSHNQLT 117
Cdd:PLN03150  490 TSLRILNLNGNSLS 503
LRR_8 pfam13855
Leucine rich repeat;
246-284 4.57e-03

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 36.73  E-value: 4.57e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 564372233   246 PNLHRLNLSSNQIAELSlciDQW----VHLETLNLSRNQLTSL 284
Cdd:pfam13855    1 PNLRSLDLSNNRLTSLD---DGAfkglSNLKVLDLSNNLLTTL 40
 
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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