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Conserved domains on  [gi|695271686|ref|NP_001289136|]
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protein flightless-1 homolog isoform 2 [Mus musculus]

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 1.59e-61

Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin_like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


:

Pssm-ID: 200446  Cd Length: 113  Bit Score: 205.15  E-value: 1.59e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686  491 TEDVGQLPGLTIWQIENFVPVLVEEAFHGKFYEADCYIVLKTFLDDSGSLNWEIYYWIGGEATLDKKACSAIHAVNLRNY 570
Cdd:cd11290     1 FEGVGQKPGLQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDPSGSLSYDIHYWLGKEASQDEAGAAAIKAVELDDY 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 695271686  571 LGAECRTVREEMGDESEEFLQVFDNDISYIEGG 603
Cdd:cd11290    81 LGGRPVQHREVQGHESEEFLSYFKKGIIYIEGG 113
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 1164-1263 1.17e-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: 1.17e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686 1164 HTRLFRCSNEKGYFaVTEKCSDFCQDDLADDDIMLLDNGQEVYMWVGTQTSQVEIKLSLKACQVYIQHTRSKEHERPRRL 1243
Cdd:cd11291     1 KPRLFRCSNESGFF-KVEEISDFSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYIETDPLGRSKPRTPI 79

                          90       100
                  ....*....|....*....|
gi 695271686 1244 RLVRKGNEQRAFTRCFHAWS 1263
Cdd:cd11291    80 YLVKQGNEPPTFTGYFHAWD 99
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
38-374 7.72e-39

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


:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 150.47  E-value: 7.72e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686   38 LKLNRTGLCYLPEELAALQKLEHLSVSHNHLTTLHGELSSLPSLRAIVARANSLKNSGVPDDIFKLDDLSVLDLSHNQLT 117
Cdd:COG4886     4 LLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686  118 E---CPRELENAKNMLVLNLSHNgidsipnQLFINLTDLLYLDLSENRLESLPPQMRRLVHLQTLVLNGNPLlhaqlrql 194
Cdd:COG4886    84 LlllGLTDLGDLTNLTELDLSGN-------EELSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQL-------- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686  195 pammalqtlhlrntqrtqSNLPTSLEGLSNLSDVDLSCNDLTRVPECLYTLPSLRRLNLSSNQIAELSLCIDQWVHLETL 274
Cdd:COG4886   149 ------------------TDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLEEL 210

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686  275 NLSRNQLTSLPSAickltklkklylnsnkldfdglpsgIGKLTSLEEFMAANNNLELIPEsLCRCPKLKKLVLNKNRLVT 354
Cdd:COG4886   211 DLSGNQLTDLPEP-------------------------LANLTNLETLDLSNNQLTDLPE-LGNLTNLEELDLSNNQLTD 264

                         330       340
                  ....*....|....*....|
gi 695271686  355 LPEAIHfLTEIQVLDVRENP 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; ...
 1054-1153 2.18e-35

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: 129.66  E-value: 2.18e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686 1054 QPTLYQIRTNGSaLCTRCIQINTDSSLLNSEFCFILKVPFesednqgIVYAWVGRASDPDEAKLAEDILNTMFDaSYSKQ 1133
Cdd:cd11288     2 PTRLFQVRGNGS-GNTRAVEVDADASSLNSNDVFVLKTPS-------SVYLWVGKGSSEDERELAKDVASFLKP-KASLQ 72

                          90       100
                  ....*....|....*....|
gi 695271686 1134 VINEGEEPENFFWVGIGAQK 1153
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 6.95e-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: 6.95e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686  722 PPQPKLYKVGLGLGYLELPQINYKLsvehkkrpkvelmpgmrLLQSLLDTRCVYILDCWSDVFIWLGRKSPRLVRAAALK 801
Cdd:cd11292     1 AEQKKLYKVSDASGKLKLTEVAEGS-----------------LNQEMLDSEDCYILDCGSEIFVWVGKGASLDERKAALK 63

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 695271686  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 6.21e-27

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: 105.53  E-value: 6.21e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686  618 TRMYRVYGKKNIKLEPVPLKGSSLDPRFVFLLDQGLDIYVWRGAQATLSNTTKARLFAEKINKnERKGKAEITLLVQGQE 697
Cdd:cd11280     2 PRLYRVRGSKAIEIEEVPLASSSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKELDE-ERKGKPEIVRIRQGQE 80


                  ....*
gi 695271686  698 PPGFW 702
Cdd:cd11280    81 PREFW 85
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 980-1035 1.81e-17

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: 78.56  E-value: 1.81e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 695271686  980 DFQCIVYFWQGReASNMGWLTFTFSLQKKFESLFPGKLEVVRMTQQQENPKFLSHF 1035
Cdd:cd11280    34 DTGSEIYIWQGR-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 1.59e-61

Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin_like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200446  Cd Length: 113  Bit Score: 205.15  E-value: 1.59e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686  491 TEDVGQLPGLTIWQIENFVPVLVEEAFHGKFYEADCYIVLKTFLDDSGSLNWEIYYWIGGEATLDKKACSAIHAVNLRNY 570
Cdd:cd11290     1 FEGVGQKPGLQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDPSGSLSYDIHYWLGKEASQDEAGAAAIKAVELDDY 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 695271686  571 LGAECRTVREEMGDESEEFLQVFDNDISYIEGG 603
Cdd:cd11290    81 LGGRPVQHREVQGHESEEFLSYFKKGIIYIEGG 113
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 1164-1263 1.17e-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: 1.17e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686 1164 HTRLFRCSNEKGYFaVTEKCSDFCQDDLADDDIMLLDNGQEVYMWVGTQTSQVEIKLSLKACQVYIQHTRSKEHERPRRL 1243
Cdd:cd11291     1 KPRLFRCSNESGFF-KVEEISDFSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYIETDPLGRSKPRTPI 79

                          90       100
                  ....*....|....*....|
gi 695271686 1244 RLVRKGNEQRAFTRCFHAWS 1263
Cdd:cd11291    80 YLVKQGNEPPTFTGYFHAWD 99
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
38-374 7.72e-39

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 150.47  E-value: 7.72e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686   38 LKLNRTGLCYLPEELAALQKLEHLSVSHNHLTTLHGELSSLPSLRAIVARANSLKNSGVPDDIFKLDDLSVLDLSHNQLT 117
Cdd:COG4886     4 LLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686  118 E---CPRELENAKNMLVLNLSHNgidsipnQLFINLTDLLYLDLSENRLESLPPQMRRLVHLQTLVLNGNPLlhaqlrql 194
Cdd:COG4886    84 LlllGLTDLGDLTNLTELDLSGN-------EELSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQL-------- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686  195 pammalqtlhlrntqrtqSNLPTSLEGLSNLSDVDLSCNDLTRVPECLYTLPSLRRLNLSSNQIAELSLCIDQWVHLETL 274
Cdd:COG4886   149 ------------------TDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLEEL 210

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686  275 NLSRNQLTSLPSAickltklkklylnsnkldfdglpsgIGKLTSLEEFMAANNNLELIPEsLCRCPKLKKLVLNKNRLVT 354
Cdd:COG4886   211 DLSGNQLTDLPEP-------------------------LANLTNLETLDLSNNQLTDLPE-LGNLTNLEELDLSNNQLTD 264

                         330       340
                  ....*....|....*....|
gi 695271686  355 LPEAIHfLTEIQVLDVRENP 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; ...
 1054-1153 2.18e-35

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: 129.66  E-value: 2.18e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686 1054 QPTLYQIRTNGSaLCTRCIQINTDSSLLNSEFCFILKVPFesednqgIVYAWVGRASDPDEAKLAEDILNTMFDaSYSKQ 1133
Cdd:cd11288     2 PTRLFQVRGNGS-GNTRAVEVDADASSLNSNDVFVLKTPS-------SVYLWVGKGSSEDERELAKDVASFLKP-KASLQ 72

                          90       100
                  ....*....|....*....|
gi 695271686 1134 VINEGEEPENFFWVGIGAQK 1153
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 6.95e-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: 6.95e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686  722 PPQPKLYKVGLGLGYLELPQINYKLsvehkkrpkvelmpgmrLLQSLLDTRCVYILDCWSDVFIWLGRKSPRLVRAAALK 801
Cdd:cd11292     1 AEQKKLYKVSDASGKLKLTEVAEGS-----------------LNQEMLDSEDCYILDCGSEIFVWVGKGASLDERKAALK 63

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 695271686  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 6.21e-27

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: 105.53  E-value: 6.21e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686  618 TRMYRVYGKKNIKLEPVPLKGSSLDPRFVFLLDQGLDIYVWRGAQATLSNTTKARLFAEKINKnERKGKAEITLLVQGQE 697
Cdd:cd11280     2 PRLYRVRGSKAIEIEEVPLASSSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKELDE-ERKGKPEIVRIRQGQE 80


                  ....*
gi 695271686  698 PPGFW 702
Cdd:cd11280    81 PREFW 85
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 619-707 1.27e-24

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 98.90  E-value: 1.27e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686    619 RMYRVYGKKNIKLEPVPLKGSSLDPRFVFLLDQGLDIYVWRGAQATLSNTTKARLFAEKINKNERKGKAEITLLVQGQEP 698
Cdd:smart00262    1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVRVVDEGKEP 80


                    ....*....
gi 695271686    699 PGFWDVLGG 707
Cdd:smart00262   81 PEFWSLFGG 89
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 5-352 3.42e-23

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 107.24  E-value: 3.42e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686    5 GVLPFVRGVDLSGNDFKGGyFPENVKAMTSLRWLKLNRTGLC-YLPEELAALQKLEHLSVSHNHLT-TLHGELSSLPSLR 82
Cdd:PLN00113  137 GSIPNLETLDLSNNMLSGE-IPNDIGSFSSLKVLDLGGNVLVgKIPNSLTNLTSLEFLTLASNQLVgQIPRELGQMKSLK 215

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686   83 AIVARANSLkNSGVPDDIFKLDDLSVLDLSHNQLT-ECPRELENAKNMLVLNLSHNGI-DSIPNQLFiNLTDLLYLDLSE 160
Cdd:PLN00113  216 WIYLGYNNL-SGEIPYEIGGLTSLNHLDLVYNNLTgPIPSSLGNLKNLQYLFLYQNKLsGPIPPSIF-SLQKLISLDLSD 293

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686  161 NRLE-SLPPQMRRLVHLQTLVLNGNPLLHAQLRQLPAMMALQTLHLRnTQRTQSNLPTSLEGLSNLSDVDLSCNDLT--- 236
Cdd:PLN00113  294 NSLSgEIPELVIQLQNLEILHLFSNNFTGKIPVALTSLPRLQVLQLW-SNKFSGEIPKNLGKHNNLTVLDLSTNNLTgei 372

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686  237 ----------------------RVPECLYTLPSLRRLNLSSNQIA-ELS----------------------LCIDQW--V 269
Cdd:PLN00113  373 peglcssgnlfklilfsnslegEIPKSLGACRSLRRVRLQDNSFSgELPseftklplvyfldisnnnlqgrINSRKWdmP 452

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686  270 HLETLNLSRNQLT-SLPSAickltklkKLYLNSNKLD-----FDG-LPSGIGKLTSLEEFMAANNNLE-LIPESLCRCPK 341
Cdd:PLN00113  453 SLQMLSLARNKFFgGLPDS--------FGSKRLENLDlsrnqFSGaVPRKLGSLSELMQLKLSENKLSgEIPDELSSCKK 524

                         410
                  ....*....|.
gi 695271686  342 LKKLVLNKNRL 352
Cdd:PLN00113  525 LVSLDLSHNQL 535
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1169-1262 6.04e-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: 6.04e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686   1169 RCSNEKGYFAVTEKCSDFCQDDLADDDIMLLDNGQEVYMWVGTQTSQVEIKLSLKACQVYIQHtrskEHERPRRLRLVRK 1248
Cdd:smart00262    1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDT----LGPGPVQVRVVDE 76

                            90
                    ....*....|....
gi 695271686   1249 GNEQRAFTRCFHAW 1262
Cdd:smart00262   77 GKEPPEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 750-837 3.43e-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: 80.41  E-value: 3.43e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686    750 HKKRPKVELMPGMRLLQSLLDTRCVYILDCWSDVFIWLGRKSPRLVRAAALKLGQELCGMLHrPRHTVVSRSLEGTEAQV 829
Cdd:smart00262    4 RVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLG-PGPVQVRVVDEGKEPPE 82


                    ....*...
gi 695271686    830 FKAKFKNW 837
Cdd:smart00262   83 FWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 502-595 4.16e-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: 80.41  E-value: 4.16e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686    502 IWQIENFVPVLVEE--AFHGKFYEADCYIVLKTflddsgslnWEIYYWIGGEATLDKKACSAIHAVNLRNYLGAECRTVR 579
Cdd:smart00262    2 LVRVKGKRNVRVPEvpFSQGSLNSGDCYILDTG---------SEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVR 72

                            90
                    ....*....|....*..
gi 695271686    580 E-EMGDESEEFLQVFDN 595
Cdd:smart00262   73 VvDEGKEPPEFWSLFGG 89
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 980-1035 1.81e-17

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: 78.56  E-value: 1.81e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 695271686  980 DFQCIVYFWQGReASNMGWLTFTFSLQKKFESLFPGKLEVVRMTQQQENPKFLSHF 1035
Cdd:cd11280    34 DTGSEIYIWQGR-ASSQAELAAAALLAKELDEERKGKPEIVRIRQGQEPREFWSLF 88
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 103-285 1.40e-15

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: 77.13  E-value: 1.40e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686  103 LDDLSVLDLSHNQLTECPrELENAKNMLVLNLSHNGIDSIPNqlFINLTDLLYLDLSENRLESLPPqMRRLVHLQTLVLN 182
Cdd:cd21340     1 LKRITHLYLNDKNITKID-NLSLCKNLKVLYLYDNKITKIEN--LEFLTNLTHLYLQNNQIEKIEN-LENLVNLKKLYLG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686  183 GNPLlhAQLRQLPAMMALQTLHLRNtQRTQSNL-----PTSLEGLSN-LSDVDLSCNDLTRVpECLYTLPSLRRLNLSSN 256
Cdd:cd21340    77 GNRI--SVVEGLENLTNLEELHIEN-QRLPPGEkltfdPRSLAALSNsLRVLNISGNNIDSL-EPLAPLRNLEQLDASNN 152

                         170       180       190
                  ....*....|....*....|....*....|..
gi 695271686  257 QIA---ELSLCIDQWVHLETLNLSRNQLTSLP 285
Cdd:cd21340   153 QISdleELLDLLSSWPSLRELDLTGNPVCKKP 184
Gelsolin pfam00626
Gelsolin repeat;
627-702 1.57e-15

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 72.34  E-value: 1.57e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695271686   627 KNIKLEPVPLKGSSLDPRFVFLLDQGLDIYVWRGAQATLSNTTKARLFAEKINKNERKGKAEITLLVQGQEPPGFW 702
Cdd:pfam00626    1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDERFPLPEVIRVPQGKEPARFL 76
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1058-1150 1.69e-15

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 73.10  E-value: 1.69e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686   1058 YQIRTNGSaLCTRCIQINTDSSLLNSEFCFILkvpfeseDNQGIVYAWVGRASDPDE----AKLAEDILNTMFDASYSKQ 1133
Cdd:smart00262    1 FLVRVKGK-RNVRVPEVPFSQGSLNSGDCYIL-------DTGSEIYVWVGKKSSQDEkkkaAELAVELDDTLGPGPVQVR 72

                            90
                    ....*....|....*..
gi 695271686   1134 VINEGEEPENFFWVGIG 1150
Cdd:smart00262   73 VVDEGKEPPEFWSLFGG 89
Gelsolin pfam00626
Gelsolin repeat;
507-590 1.74e-12

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 63.87  E-value: 1.74e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686   507 NFVPVLVEEAFHGKFYEADCYIVLKTFlddsgslnwEIYYWIGGEATLDKKACSAIHAVNLR-NYLGAECRTVREEMGDE 585
Cdd:pfam00626    1 KFVLPPPVPLSQESLNSGDCYLLDNGF---------TIFLWVGKGSSLLEKLFAALLAAQLDdDERFPLPEVIRVPQGKE 71


                   ....*
gi 695271686   586 SEEFL 590
Cdd:pfam00626   72 PARFL 76
LRR_8 pfam13855
Leucine rich repeat;
131-186 3.37e-11

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 59.85  E-value: 3.37e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 695271686   131 VLNLSHNGIDSIPNQLFINLTDLLYLDLSENRLESLPPQM-RRLVHLQTLVLNGNPL 186
Cdd:pfam13855    5 SLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAfSGLPSLRYLDLSGNRL 61
Gelsolin pfam00626
Gelsolin repeat;
1182-1255 5.80e-07

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 48.07  E-value: 5.80e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695271686  1182 KCSDFCQDDLADDDIMLLDNGQEVYMWVGTQTSQVEIKLSLKACQVYIQHTRskeHERPRRLRLVRkGNEQRAF 1255
Cdd:pfam00626    6 PPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDER---FPLPEVIRVPQ-GKEPARF 75
Gelsolin pfam00626
Gelsolin repeat;
755-831 1.70e-06

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 46.92  E-value: 1.70e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695271686   755 KVELMPGMRLLQSLLDTRCVYILDCWSDVFIWLGRKSPRLVRAAALKLGQELcGMLHRPRHTVVSRSLEGTEAQVFK 831
Cdd:pfam00626    1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQL-DDDERFPLPEVIRVPQGKEPARFL 76
Gelsolin pfam00626
Gelsolin repeat;
1077-1144 2.44e-05

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 43.45  E-value: 2.44e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695271686  1077 DSSLLNSEFCFILkvpfeseDNQGIVYAWVGRASDPDE----AKLAEDILNTMFDASYSKQVINEGEEPENF 1144
Cdd:pfam00626   11 SQESLNSGDCYLL-------DNGFTIFLWVGKGSSLLEklfaALLAAQLDDDERFPLPEVIRVPQGKEPARF 75
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 912-1036 2.17e-04

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 41.51  E-value: 2.17e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686    912 EGRKFTRLPEEEF--GHFYTQDCYVFLCRYwvpveyeeeektedkegkasaearegeeaaaeaeekqpeedfqcIVYFWQ 989
Cdd:smart00262    6 KGKRNVRVPEVPFsqGSLNSGDCYILDTGS--------------------------------------------EIYVWV 41

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*..
gi 695271686    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 1.59e-61

Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin_like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200446  Cd Length: 113  Bit Score: 205.15  E-value: 1.59e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686  491 TEDVGQLPGLTIWQIENFVPVLVEEAFHGKFYEADCYIVLKTFLDDSGSLNWEIYYWIGGEATLDKKACSAIHAVNLRNY 570
Cdd:cd11290     1 FEGVGQKPGLQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDPSGSLSYDIHYWLGKEASQDEAGAAAIKAVELDDY 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 695271686  571 LGAECRTVREEMGDESEEFLQVFDNDISYIEGG 603
Cdd:cd11290    81 LGGRPVQHREVQGHESEEFLSYFKKGIIYIEGG 113
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 1164-1263 1.17e-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: 1.17e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686 1164 HTRLFRCSNEKGYFaVTEKCSDFCQDDLADDDIMLLDNGQEVYMWVGTQTSQVEIKLSLKACQVYIQHTRSKEHERPRRL 1243
Cdd:cd11291     1 KPRLFRCSNESGFF-KVEEISDFSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYIETDPLGRSKPRTPI 79

                          90       100
                  ....*....|....*....|
gi 695271686 1244 RLVRKGNEQRAFTRCFHAWS 1263
Cdd:cd11291    80 YLVKQGNEPPTFTGYFHAWD 99
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
38-374 7.72e-39

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 150.47  E-value: 7.72e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686   38 LKLNRTGLCYLPEELAALQKLEHLSVSHNHLTTLHGELSSLPSLRAIVARANSLKNSGVPDDIFKLDDLSVLDLSHNQLT 117
Cdd:COG4886     4 LLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686  118 E---CPRELENAKNMLVLNLSHNgidsipnQLFINLTDLLYLDLSENRLESLPPQMRRLVHLQTLVLNGNPLlhaqlrql 194
Cdd:COG4886    84 LlllGLTDLGDLTNLTELDLSGN-------EELSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQL-------- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686  195 pammalqtlhlrntqrtqSNLPTSLEGLSNLSDVDLSCNDLTRVPECLYTLPSLRRLNLSSNQIAELSLCIDQWVHLETL 274
Cdd:COG4886   149 ------------------TDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLEEL 210

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686  275 NLSRNQLTSLPSAickltklkklylnsnkldfdglpsgIGKLTSLEEFMAANNNLELIPEsLCRCPKLKKLVLNKNRLVT 354
Cdd:COG4886   211 DLSGNQLTDLPEP-------------------------LANLTNLETLDLSNNQLTDLPE-LGNLTNLEELDLSNNQLTD 264

                         330       340
                  ....*....|....*....|
gi 695271686  355 LPEAIHfLTEIQVLDVRENP 374
Cdd:COG4886   265 LPPLAN-LTNLKTLDLSNNQ 283
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
24-263 7.17e-38

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 147.77  E-value: 7.17e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686   24 YFPENVKAMTSLRWLKLNRTglcylpEELAALQKLEHLSVSHNHLTTLHGELSSLPSLRAIVARANSLKNsgVPDDIFKL 103
Cdd:COG4886    87 LGLTDLGDLTNLTELDLSGN------EELSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTD--LPEPLGNL 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686  104 DDLSVLDLSHNQLTECPRELENAKNMLVLNLSHNGIDSIPNQLFiNLTDLLYLDLSENRLESLPPQMRRLVHLQTLVLNG 183
Cdd:COG4886   159 TNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLG-NLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSN 237

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686  184 NpllhaQLRQLPammalqtlhlrntqrtqsnlptSLEGLSNLSDVDLSCNDLTRVPEcLYTLPSLRRLNLSSNQIAELSL 263
Cdd:COG4886   238 N-----QLTDLP----------------------ELGNLTNLEELDLSNNQLTDLPP-LANLTNLKTLDLSNNQLTDLKL 289
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 1054-1153 2.18e-35

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: 129.66  E-value: 2.18e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686 1054 QPTLYQIRTNGSaLCTRCIQINTDSSLLNSEFCFILKVPFesednqgIVYAWVGRASDPDEAKLAEDILNTMFDaSYSKQ 1133
Cdd:cd11288     2 PTRLFQVRGNGS-GNTRAVEVDADASSLNSNDVFVLKTPS-------SVYLWVGKGSSEDERELAKDVASFLKP-KASLQ 72

                          90       100
                  ....*....|....*....|
gi 695271686 1134 VINEGEEPENFFWVGIGAQK 1153
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 6.95e-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: 6.95e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686  722 PPQPKLYKVGLGLGYLELPQINYKLsvehkkrpkvelmpgmrLLQSLLDTRCVYILDCWSDVFIWLGRKSPRLVRAAALK 801
Cdd:cd11292     1 AEQKKLYKVSDASGKLKLTEVAEGS-----------------LNQEMLDSEDCYILDCGSEIFVWVGKGASLDERKAALK 63

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 695271686  802 LGQELCGMLHRPRHTVVSRSLEGTEAQVFKAKFKN 836
Cdd:cd11292    64 NAEEFLRKKKRPPYTQVTRVTEGGESALFKSKFAN 98
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
7-287 7.35e-31

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 126.97  E-value: 7.35e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686    7 LPFVRGVDLSGNDFKggYFPENVKAMTSLRWLKLNRTGLCYLPEELAALQKLEHLSVSHNHLTTLHGELSSLPSLRaiva 86
Cdd:COG4886   135 LTNLKELDLSNNQLT--DLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLE---- 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686   87 ranslknsgvpddifklddlsVLDLSHNQLTECPRELENAKNMLVLNLSHNGIDSIPNqlFINLTDLLYLDLSENRLESL 166
Cdd:COG4886   209 ---------------------ELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTDLPE--LGNLTNLEELDLSNNQLTDL 265

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686  167 PPQMrRLVHLQTLVLNGNPLLHAQLRQLPammALQTLHLRNTQRTQSNLPTSLEGLSNLSDVDLSCNDLTRVPECLYTLP 246
Cdd:COG4886   266 PPLA-NLTNLKTLDLSNNQLTDLKLKELE---LLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLA 341

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 695271686  247 SLRRLNLSSNQIAELSLCIDQWVHLETLNLSRNQLTSLPSA 287
Cdd:COG4886   342 LSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGLLEATLLTL 382
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 618-702 6.21e-27

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: 105.53  E-value: 6.21e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686  618 TRMYRVYGKKNIKLEPVPLKGSSLDPRFVFLLDQGLDIYVWRGAQATLSNTTKARLFAEKINKnERKGKAEITLLVQGQE 697
Cdd:cd11280     2 PRLYRVRGSKAIEIEEVPLASSSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKELDE-ERKGKPEIVRIRQGQE 80


                  ....*
gi 695271686  698 PPGFW 702
Cdd:cd11280    81 PREFW 85
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 619-707 1.27e-24

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 98.90  E-value: 1.27e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686    619 RMYRVYGKKNIKLEPVPLKGSSLDPRFVFLLDQGLDIYVWRGAQATLSNTTKARLFAEKINKNERKGKAEITLLVQGQEP 698
Cdd:smart00262    1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVRVVDEGKEP 80


                    ....*....
gi 695271686    699 PGFWDVLGG 707
Cdd:smart00262   81 PEFWSLFGG 89
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 5-352 3.42e-23

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 107.24  E-value: 3.42e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686    5 GVLPFVRGVDLSGNDFKGGyFPENVKAMTSLRWLKLNRTGLC-YLPEELAALQKLEHLSVSHNHLT-TLHGELSSLPSLR 82
Cdd:PLN00113  137 GSIPNLETLDLSNNMLSGE-IPNDIGSFSSLKVLDLGGNVLVgKIPNSLTNLTSLEFLTLASNQLVgQIPRELGQMKSLK 215

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686   83 AIVARANSLkNSGVPDDIFKLDDLSVLDLSHNQLT-ECPRELENAKNMLVLNLSHNGI-DSIPNQLFiNLTDLLYLDLSE 160
Cdd:PLN00113  216 WIYLGYNNL-SGEIPYEIGGLTSLNHLDLVYNNLTgPIPSSLGNLKNLQYLFLYQNKLsGPIPPSIF-SLQKLISLDLSD 293

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686  161 NRLE-SLPPQMRRLVHLQTLVLNGNPLLHAQLRQLPAMMALQTLHLRnTQRTQSNLPTSLEGLSNLSDVDLSCNDLT--- 236
Cdd:PLN00113  294 NSLSgEIPELVIQLQNLEILHLFSNNFTGKIPVALTSLPRLQVLQLW-SNKFSGEIPKNLGKHNNLTVLDLSTNNLTgei 372

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686  237 ----------------------RVPECLYTLPSLRRLNLSSNQIA-ELS----------------------LCIDQW--V 269
Cdd:PLN00113  373 peglcssgnlfklilfsnslegEIPKSLGACRSLRRVRLQDNSFSgELPseftklplvyfldisnnnlqgrINSRKWdmP 452

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686  270 HLETLNLSRNQLT-SLPSAickltklkKLYLNSNKLD-----FDG-LPSGIGKLTSLEEFMAANNNLE-LIPESLCRCPK 341
Cdd:PLN00113  453 SLQMLSLARNKFFgGLPDS--------FGSKRLENLDlsrnqFSGaVPRKLGSLSELMQLKLSENKLSgEIPDELSSCKK 524

                         410
                  ....*....|.
gi 695271686  342 LKKLVLNKNRL 352
Cdd:PLN00113  525 LVSLDLSHNQL 535
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1169-1262 6.04e-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: 6.04e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686   1169 RCSNEKGYFAVTEKCSDFCQDDLADDDIMLLDNGQEVYMWVGTQTSQVEIKLSLKACQVYIQHtrskEHERPRRLRLVRK 1248
Cdd:smart00262    1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDT----LGPGPVQVRVVDE 76

                            90
                    ....*....|....
gi 695271686   1249 GNEQRAFTRCFHAW 1262
Cdd:smart00262   77 GKEPPEFWSLFGGW 90
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 7-373 6.11e-23

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 106.09  E-value: 6.11e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686    7 LPFVRGVDLSGNDFKGGyFPENV-KAMTSLRWLKL---NRTGlcylPEELAALQKLEHLSVSHNHLT-TLHGELSSLPSL 81
Cdd:PLN00113   92 LPYIQTINLSNNQLSGP-IPDDIfTTSSSLRYLNLsnnNFTG----SIPRGSIPNLETLDLSNNMLSgEIPNDIGSFSSL 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686   82 RAIVARANSLKNSgVPDDIFKLDDLSVLDLSHNQLT-ECPRELENAKNMLVLNLSHNGID-SIPNQLFiNLTDLLYLDLS 159
Cdd:PLN00113  167 KVLDLGGNVLVGK-IPNSLTNLTSLEFLTLASNQLVgQIPRELGQMKSLKWIYLGYNNLSgEIPYEIG-GLTSLNHLDLV 244

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686  160 ENRLE-SLPPQMRRLVHLQTLVLNGNPLLHAQLRQLPAMMALQTLHLRNTQRTqSNLPTSLEGLSNLSDVDLSCNDLT-R 237
Cdd:PLN00113  245 YNNLTgPIPSSLGNLKNLQYLFLYQNKLSGPIPPSIFSLQKLISLDLSDNSLS-GEIPELVIQLQNLEILHLFSNNFTgK 323

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686  238 VPECLYTLPSLRRLNLSSNQIA-ELSLCIDQWVHLETLNLSRNQLTS-LPSAICKLtklkklylnsnkldfdglpsgiGK 315
Cdd:PLN00113  324 IPVALTSLPRLQVLQLWSNKFSgEIPKNLGKHNNLTVLDLSTNNLTGeIPEGLCSS----------------------GN 381

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686  316 LTSLEEFmaaNNNLE-LIPESLCRCPKLKKLVLNKNRLV-TLPEAIHFLTEIQVLDVREN 373
Cdd:PLN00113  382 LFKLILF---SNSLEgEIPKSLGACRSLRRVRLQDNSFSgELPSEFTKLPLVYFLDISNN 438
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
13-286 6.87e-22

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 100.01  E-value: 6.87e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686   13 VDLSGNDFKGgyFPENVKAMTSLRWLKLNRTGLCYLPEELAALQKLEHLSVSHNHLTTLHGELSSLPSLRaivaranslk 92
Cdd:COG4886   164 LDLSNNQLTD--LPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLE---------- 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686   93 nsgvpddifklddlsVLDLSHNQLTECPrELENAKNMLVLNLSHNGIDSIPNQLfiNLTDLLYLDLSENRLESLppqmrR 172
Cdd:COG4886   232 ---------------TLDLSNNQLTDLP-ELGNLTNLEELDLSNNQLTDLPPLA--NLTNLKTLDLSNNQLTDL-----K 288

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686  173 LVHLQTLVLNGNPLLHAQLRQLPAMM--ALQTLHLRNTQRTQSNLPTSLEGLSNLSDVDLSCNDLTRVPECLYTLPSLRR 250
Cdd:COG4886   289 LKELELLLGLNSLLLLLLLLNLLELLilLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLT 368

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 695271686  251 LNLSSNQIAELSLCIDQWVHLETLNLSRNQLTSLPS 286
Cdd:COG4886   369 LGLLGLLEATLLTLALLLLTLLLLLLTTTAGVLLLT 404
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 23-329 2.64e-20

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 97.61  E-value: 2.64e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686   23 GYFPENVKAMTSLRWLKLNRTGLC-YLPEELAALQKLEHLSVSHNHLT-TLHGELSSLPSLRAIVARANSLkNSGVPDDI 100
Cdd:PLN00113  274 GPIPPSIFSLQKLISLDLSDNSLSgEIPELVIQLQNLEILHLFSNNFTgKIPVALTSLPRLQVLQLWSNKF-SGEIPKNL 352

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686  101 FKLDDLSVLDLSHNQLT-ECPRELENAKNMLVLNLSHNGIDS-IPNQLFiNLTDLLYLDLSENRLE-SLPPQMRRLVHLQ 177
Cdd:PLN00113  353 GKHNNLTVLDLSTNNLTgEIPEGLCSSGNLFKLILFSNSLEGeIPKSLG-ACRSLRRVRLQDNSFSgELPSEFTKLPLVY 431

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686  178 TLVLNGNPLLHAQLRQLPAMMALQTLHL-RNtqRTQSNLPTSLeGLSNLSDVDLSCNDLT-RVPECLYTLPSLRRLNLSS 255
Cdd:PLN00113  432 FLDISNNNLQGRINSRKWDMPSLQMLSLaRN--KFFGGLPDSF-GSKRLENLDLSRNQFSgAVPRKLGSLSELMQLKLSE 508

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686  256 NQIA-----ELSLCidqwVHLETLNLSRNQLT-SLPSAICKLTKLKKLYLNSNKLDFDgLPSGIGKLTSLEEFMAANNNL 329
Cdd:PLN00113  509 NKLSgeipdELSSC----KKLVSLDLSHNQLSgQIPASFSEMPVLSQLDLSQNQLSGE-IPKNLGNVESLVQVNISHNHL 583
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
 500-593 2.21e-19

Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200449  Cd Length: 101  Bit Score: 84.24  E-value: 2.21e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686  500 LTIWQIENFVPVLVEEAFHGKFYEADCYIVLKTFlDDSGSLNWEIYYWIGGEATLDKKACSAIHAVNLRNYLGAECRTVR 579
Cdd:cd11293     9 VEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTY-QGGGKEEHILYFWQGRHSSQDERAAAALLTVELDEELKGRAVQVR 87

                          90
                  ....*....|....
gi 695271686  580 EEMGDESEEFLQVF 593
Cdd:cd11293    88 VVQGKEPPHFLALF 101
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 750-837 3.43e-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: 80.41  E-value: 3.43e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686    750 HKKRPKVELMPGMRLLQSLLDTRCVYILDCWSDVFIWLGRKSPRLVRAAALKLGQELCGMLHrPRHTVVSRSLEGTEAQV 829
Cdd:smart00262    4 RVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLG-PGPVQVRVVDEGKEPPE 82


                    ....*...
gi 695271686    830 FKAKFKNW 837
Cdd:smart00262   83 FWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 502-595 4.16e-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: 80.41  E-value: 4.16e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686    502 IWQIENFVPVLVEE--AFHGKFYEADCYIVLKTflddsgslnWEIYYWIGGEATLDKKACSAIHAVNLRNYLGAECRTVR 579
Cdd:smart00262    2 LVRVKGKRNVRVPEvpFSQGSLNSGDCYILDTG---------SEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVR 72

                            90
                    ....*....|....*..
gi 695271686    580 E-EMGDESEEFLQVFDN 595
Cdd:smart00262   73 VvDEGKEPPEFWSLFGG 89
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 980-1035 1.81e-17

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: 78.56  E-value: 1.81e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 695271686  980 DFQCIVYFWQGReASNMGWLTFTFSLQKKFESLFPGKLEVVRMTQQQENPKFLSHF 1035
Cdd:cd11280    34 DTGSEIYIWQGR-ASSQAELAAAALLAKELDEERKGKPEIVRIRQGQEPREFWSLF 88
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
26-288 2.14e-16

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 84.75  E-value: 2.14e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686   26 PENVKAMTSLR-WLKLNRTGLC-----------YLPEELAAL--QKLEHLSVSHNhlttLHGELSSLpslraiVARANSL 91
Cdd:PRK15370  163 ANREEAVQRMRdCLKNNKTELRlkilglttipaCIPEQITTLilDNNELKSLPEN----LQGNIKTL------YANSNQL 232

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686   92 knSGVPDDIfkLDDLSVLDLSHNQLTECPRELENAknMLVLNLSHNGIDSIPNqlfiNLTD-LLYLDLSENRLESLPPQM 170
Cdd:PRK15370  233 --TSIPATL--PDTIQEMELSINRITELPERLPSA--LQSLDLFHNKISCLPE----NLPEeLRYLSVYDNSIRTLPAHL 302

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686  171 -RRLVHLqtLVLNGNpllhaqLRQLPAMMALQTLHLRNTQRTQSNLPTSLEglSNLSDVDLSCNDLTRVPECLytLPSLR 249
Cdd:PRK15370  303 pSGITHL--NVQSNS------LTALPETLPPGLKTLEAGENALTSLPASLP--PELQVLDVSKNQITVLPETL--PPTIT 370

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 695271686  250 RLNLSSNQIAELSLCIDqwVHLETLNLSRNQLTSLPSAI 288
Cdd:PRK15370  371 TLDVSRNALTNLPENLP--AALQIMQASRNNLVRLPESL 407
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 103-285 1.40e-15

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: 77.13  E-value: 1.40e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686  103 LDDLSVLDLSHNQLTECPrELENAKNMLVLNLSHNGIDSIPNqlFINLTDLLYLDLSENRLESLPPqMRRLVHLQTLVLN 182
Cdd:cd21340     1 LKRITHLYLNDKNITKID-NLSLCKNLKVLYLYDNKITKIEN--LEFLTNLTHLYLQNNQIEKIEN-LENLVNLKKLYLG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686  183 GNPLlhAQLRQLPAMMALQTLHLRNtQRTQSNL-----PTSLEGLSN-LSDVDLSCNDLTRVpECLYTLPSLRRLNLSSN 256
Cdd:cd21340    77 GNRI--SVVEGLENLTNLEELHIEN-QRLPPGEkltfdPRSLAALSNsLRVLNISGNNIDSL-EPLAPLRNLEQLDASNN 152

                         170       180       190
                  ....*....|....*....|....*....|..
gi 695271686  257 QIA---ELSLCIDQWVHLETLNLSRNQLTSLP 285
Cdd:cd21340   153 QISdleELLDLLSSWPSLRELDLTGNPVCKKP 184
Gelsolin pfam00626
Gelsolin repeat;
627-702 1.57e-15

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 72.34  E-value: 1.57e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695271686   627 KNIKLEPVPLKGSSLDPRFVFLLDQGLDIYVWRGAQATLSNTTKARLFAEKINKNERKGKAEITLLVQGQEPPGFW 702
Cdd:pfam00626    1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDERFPLPEVIRVPQGKEPARFL 76
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1058-1150 1.69e-15

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 73.10  E-value: 1.69e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686   1058 YQIRTNGSaLCTRCIQINTDSSLLNSEFCFILkvpfeseDNQGIVYAWVGRASDPDE----AKLAEDILNTMFDASYSKQ 1133
Cdd:smart00262    1 FLVRVKGK-RNVRVPEVPFSQGSLNSGDCYIL-------DTGSEIYVWVGKKSSQDEkkkaAELAVELDDTLGPGPVQVR 72

                            90
                    ....*....|....*..
gi 695271686   1134 VINEGEEPENFFWVGIG 1150
Cdd:smart00262   73 VVDEGKEPPEFWSLFGG 89
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 617-706 1.82e-15

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


Pssm-ID: 200445  Cd Length: 92  Bit Score: 73.04  E-value: 1.82e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686  617 VTRMYRVYGKKNIKLEPVPLKGSSLDPRFVFLLDQGLDIYVWRGAQATLSNTTKARLFAEKINKNERKGKAEITLLVQG- 695
Cdd:cd11289     1 KPRLLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKVIVLDEGd 80

                          90
                  ....*....|..
gi 695271686  696 -QEPPGFWDVLG 706
Cdd:cd11289    81 tNESPEFWKVLG 92
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
191-379 9.29e-15

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 79.36  E-value: 9.29e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686  191 LRQLPAMMALQTLHLRNTQRTQSNLPTSLEGlsNLSDVDLSCNDLTRVPEclyTLP-SLRRLNLSSNQIAELSLCIDQwv 269
Cdd:PRK15370  190 LTTIPACIPEQITTLILDNNELKSLPENLQG--NIKTLYANSNQLTSIPA---TLPdTIQEMELSINRITELPERLPS-- 262

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686  270 HLETLNLSRNQLTSLPSAICKLTKLKKLYLNSNKLDFDGLPSGIgkltslEEFMAANNNLELIPESLcrCPKLKKLVLNK 349
Cdd:PRK15370  263 ALQSLDLFHNKISCLPENLPEELRYLSVYDNSIRTLPAHLPSGI------THLNVQSNSLTALPETL--PPGLKTLEAGE 334

                         170       180       190
                  ....*....|....*....|....*....|
gi 695271686  350 NRLVTLPEAIHflTEIQVLDVRENPSLVMP 379
Cdd:PRK15370  335 NALTSLPASLP--PELQVLDVSKNQITVLP 362
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
127-379 2.06e-14

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 78.20  E-value: 2.06e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686  127 KNMLVLNLSHNGIDSIPNQLFINLTDLLyldLSENRLESLPPQMRrlVHLQTLVLNGNpllhaQLRQLPAmmalqtlhlr 206
Cdd:PRK15370  178 NNKTELRLKILGLTTIPACIPEQITTLI---LDNNELKSLPENLQ--GNIKTLYANSN-----QLTSIPA---------- 237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686  207 ntqrtqsNLPTSLEglsnlsDVDLSCNDLTRVPEclyTLPS-LRRLNLSSNQIAELSLCIDQwvHLETLNLSRNQLTSLP 285
Cdd:PRK15370  238 -------TLPDTIQ------EMELSINRITELPE---RLPSaLQSLDLFHNKISCLPENLPE--ELRYLSVYDNSIRTLP 299

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686  286 SAICKLTKLKKLYLNSNKLDFDGLPSGigkltsLEEFMAANNNLELIPESLCrcPKLKKLVLNKNRLVTLPEAIHflTEI 365
Cdd:PRK15370  300 AHLPSGITHLNVQSNSLTALPETLPPG------LKTLEAGENALTSLPASLP--PELQVLDVSKNQITVLPETLP--PTI 369

                         250
                  ....*....|....
gi 695271686  366 QVLDVRENPSLVMP 379
Cdd:PRK15370  370 TTLDVSRNALTNLP 383
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 127-356 3.87e-13

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: 70.20  E-value: 3.87e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686  127 KNMLVLNLSHNGIDSIPNqlFINLTDLLYLDLSENRLESLP--PQMRRLVHLQtlvlngnpLLHAQLRQLPammalqtlh 204
Cdd:cd21340     2 KRITHLYLNDKNITKIDN--LSLCKNLKVLYLYDNKITKIEnlEFLTNLTHLY--------LQNNQIEKIE--------- 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686  205 lrntqrtqsnlptSLEGLSNLSDVDLSCNDLTRVpECLYTLPSLRRLNLSSNQIAE-LSLCID----QWV--HLETLNLS 277
Cdd:cd21340    63 -------------NLENLVNLKKLYLGGNRISVV-EGLENLTNLEELHIENQRLPPgEKLTFDprslAALsnSLRVLNIS 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686  278 RNQLTSLpsaickltklkklylnsnkldfdglpSGIGKLTSLEEFMAANNNLELIPE---SLCRCPKLKKLVLNKNRLVT 354
Cdd:cd21340   129 GNNIDSL--------------------------EPLAPLRNLEQLDASNNQISDLEElldLLSSWPSLRELDLTGNPVCK 182


                  ..
gi 695271686  355 LP 356
Cdd:cd21340   183 KP 184
Gelsolin pfam00626
Gelsolin repeat;
507-590 1.74e-12

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 63.87  E-value: 1.74e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686   507 NFVPVLVEEAFHGKFYEADCYIVLKTFlddsgslnwEIYYWIGGEATLDKKACSAIHAVNLR-NYLGAECRTVREEMGDE 585
Cdd:pfam00626    1 KFVLPPPVPLSQESLNSGDCYLLDNGF---------TIFLWVGKGSSLLEKLFAALLAAQLDdDERFPLPEVIRVPQGKE 71


                   ....*
gi 695271686   586 SEEFL 590
Cdd:pfam00626   72 PARFL 76
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 618-707 8.37e-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: 62.63  E-value: 8.37e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686  618 TRMYRVYG--KKNIKLEPVPLKGSSLDPRFVFLLDQGLDIYVWRGAQATLSNTTKARLFAEKInknerKGKAEITLLVQG 695
Cdd:cd11288     3 TRLFQVRGngSGNTRAVEVDADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVASFL-----KPKASLQEVAEG 77

                          90
                  ....*....|..
gi 695271686  696 QEPPGFWDVLGG 707
Cdd:cd11288    78 SEPDEFWEALGG 89
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 4-256 1.28e-11

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 69.49  E-value: 1.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686    4 TGVLPfvRGVDLSGNDFK--------GGYFPENVKAMTSLRWLKLNRTGLC-YLPEELAALQKLEHLSVSHNHLTtlhGE 74
Cdd:PLN00113  369 TGEIP--EGLCSSGNLFKlilfsnslEGEIPKSLGACRSLRRVRLQDNSFSgELPSEFTKLPLVYFLDISNNNLQ---GR 443

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686   75 LSS----LPSLRAIVARANSLknSGVPDDIFKLDDLSVLDLSHNQLTEcprelenaknmlvlnlshngidSIPNQlFINL 150
Cdd:PLN00113  444 INSrkwdMPSLQMLSLARNKF--FGGLPDSFGSKRLENLDLSRNQFSG----------------------AVPRK-LGSL 498

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686  151 TDLLYLDLSENRLESLPPqmrrlvhlqtlvlngnpllhaqlRQLPAMMALQTLHLRNTQRTqSNLPTSLEGLSNLSDVDL 230
Cdd:PLN00113  499 SELMQLKLSENKLSGEIP-----------------------DELSSCKKLVSLDLSHNQLS-GQIPASFSEMPVLSQLDL 554

                         250       260
                  ....*....|....*....|....*..
gi 695271686  231 SCNDLT-RVPECLYTLPSLRRLNLSSN 256
Cdd:PLN00113  555 SQNQLSgEIPKNLGNVESLVQVNISHN 581
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 1165-1265 2.05e-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: 2.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686 1165 TRLFRCSNEK-GYFAVTEKCSDfcqdDLADDDIMLLDNGQEVYMWVGTQTSQVEiklsLKACQVYIQHTRSKEHERPRRL 1243
Cdd:cd11280     2 PRLYRVRGSKaIEIEEVPLASS----SLDSDDVFVLDTGSEIYIWQGRASSQAE----LAAAALLAKELDEERKGKPEIV 73

                          90       100
                  ....*....|....*....|..
gi 695271686 1244 RlVRKGNEQRAFtrcfhaWSTF 1265
Cdd:cd11280    74 R-IRQGQEPREF------WSLF 88
LRR_8 pfam13855
Leucine rich repeat;
131-186 3.37e-11

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 59.85  E-value: 3.37e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 695271686   131 VLNLSHNGIDSIPNQLFINLTDLLYLDLSENRLESLPPQM-RRLVHLQTLVLNGNPL 186
Cdd:pfam13855    5 SLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAfSGLPSLRYLDLSGNRL 61
PRK15387 PRK15387
type III secretion system effector E3 ubiquitin transferase SspH2;
131-356 4.99e-11

type III secretion system effector E3 ubiquitin transferase SspH2;


Pssm-ID: 185285 [Multi-domain]  Cd Length: 788  Bit Score: 67.11  E-value: 4.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686  131 VLNLSHNGIDSIPNQLFINLTDLLYLDLSENRLESLPPQMRrlvhlqTLVLNGNpllhaQLRQLPaMMALQTLHLRNTQR 210
Cdd:PRK15387  205 VLNVGESGLTTLPDCLPAHITTLVIPDNNLTSLPALPPELR------TLEVSGN-----QLTSLP-VLPPGLLELSIFSN 272

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686  211 TQSNLPTSLEGLSNLSdvdLSCNDLTRVPeclYTLPSLRRLNLSSNQIAEL-----SLCiDQWVH-------------LE 272
Cdd:PRK15387  273 PLTHLPALPSGLCKLW---IFGNQLTSLP---VLPPGLQELSVSDNQLASLpalpsELC-KLWAYnnqltslptlpsgLQ 345

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686  273 TLNLSRNQLTSLPSaiCKLTKLKKLYLNSNKLDFDGLPSGigkltsLEEFMAANNNLELIPeslCRCPKLKKLVLNKNRL 352
Cdd:PRK15387  346 ELSVSDNQLASLPT--LPSELYKLWAYNNRLTSLPALPSG------LKELIVSGNRLTSLP---VLPSELKELMVSGNRL 414


                  ....
gi 695271686  353 VTLP 356
Cdd:PRK15387  415 TSLP 418
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 50-188 9.04e-11

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: 63.27  E-value: 9.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686   50 EELAALQKLEHLSVSHNHLTTLHGeLSSLPSLRAIVARANSLKnsgVPDDIFKLDDLSVLDLSHNQLT--EC----PREL 123
Cdd:cd21340    40 ENLEFLTNLTHLYLQNNQIEKIEN-LENLVNLKKLYLGGNRIS---VVEGLENLTNLEELHIENQRLPpgEKltfdPRSL 115

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695271686  124 EN-AKNMLVLNLSHNGIDSIpNQLFiNLTDLLYLDLSENRLESLPPQ---MRRLVHLQTLVLNGNPLLH 188
Cdd:cd21340   116 AAlSNSLRVLNISGNNIDSL-EPLA-PLRNLEQLDASNNQISDLEELldlLSSWPSLRELDLTGNPVCK 182
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 502-593 4.22e-10

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


Pssm-ID: 200436  Cd Length: 88  Bit Score: 57.38  E-value: 4.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686  502 IWQIENFVPVLVEE--AFHGKFYEADCYIVlktfldDSGSlnwEIYYWIGGEATLDKKACSAIHAVNLRNYLGAECRTVR 579
Cdd:cd11280     4 LYRVRGSKAIEIEEvpLASSSLDSDDVFVL------DTGS---EIYIWQGRASSQAELAAAALLAKELDEERKGKPEIVR 74

                          90
                  ....*....|....
gi 695271686  580 EEMGDESEEFLQVF 593
Cdd:cd11280    75 IRQGQEPREFWSLF 88
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 617-701 1.80e-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: 1.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686  617 VTRMYRVY-GKKNIKLEPV---PLKGSSLDPRFVFLLDQGLDIYVWRGAQATLSNTTKARLFAEK-INKNERKGKAEITL 691
Cdd:cd11292     3 QKKLYKVSdASGKLKLTEVaegSLNQEMLDSEDCYILDCGSEIFVWVGKGASLDERKAALKNAEEfLRKKKRPPYTQVTR 82

                          90
                  ....*....|
gi 695271686  692 LVQGQEPPGF 701
Cdd:cd11292    83 VTEGGESALF 92
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 766-838 1.47e-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: 1.47e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695271686  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 2.33e-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: 52.76  E-value: 2.33e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695271686  767 SLLDTRCVYILDCWSDVFIWLGRKSPRLVRAAALKLGQELcgMLHRPRHTVVSRSLEGTEAQVFKAKF 834
Cdd:cd11280    23 SSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKEL--DEERKGKPEIVRIRQGQEPREFWSLF 88
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 1054-1144 4.54e-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: 4.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686 1054 QPTLYQIRTNGSALCTRCIQINT-DSSLLNSEFCFILkvpfeseDNQGIVYAWVGRASDPDEAK----LAEDILNTMFDA 1128
Cdd:cd11292     3 QKKLYKVSDASGKLKLTEVAEGSlNQEMLDSEDCYIL-------DCGSEIFVWVGKGASLDERKaalkNAEEFLRKKKRP 75

                          90
                  ....*....|....*..
gi 695271686 1129 SYSK-QVINEGEEPENF 1144
Cdd:cd11292    76 PYTQvTRVTEGGESALF 92
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 1165-1259 5.00e-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: 5.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686 1165 TRLFRCSNEKGYFAVTE-KCSDFCQDDLADDDIMLLDNGQEVYMWVGTQTSQVEIKLSLKACQVYIQhtrskEHERPRRL 1243
Cdd:cd11292     4 KKLYKVSDASGKLKLTEvAEGSLNQEMLDSEDCYILDCGSEIFVWVGKGASLDERKAALKNAEEFLR-----KKKRPPYT 78

                          90
                  ....*....|....*...
gi 695271686 1244 RLVR--KGNEQRAFTRCF 1259
Cdd:cd11292    79 QVTRvtEGGESALFKSKF 96
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 89-352 1.02e-07

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: 55.44  E-value: 1.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686   89 NSLKNSGVPDDIFKLDDLSVLDLSHNQLTE-----CPRELENAKNMLVLNLSHNGIDSIPNQL------FINLTDLLYLD 157
Cdd:cd00116     8 ELLKTERATELLPKLLCLQVLRLEGNTLGEeaakaLASALRPQPSLKELCLSLNETGRIPRGLqsllqgLTKGCGLQELD 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686  158 LSEN--------RLESLppqmRRLVHLQTLVLNGN-------PLLHAQLRQLPamMALQTLHL-RNTQRTQSNLPTSLEG 221
Cdd:cd00116    88 LSDNalgpdgcgVLESL----LRSSSLQELKLNNNglgdrglRLLAKGLKDLP--PALEKLVLgRNRLEGASCEALAKAL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686  222 LSN--LSDVDLSCNDL-----TRVPECLYTLPSLRRLNLSSNQIAE-----LSLCIDQWVHLETLNLSRNQLTSLP-SAI 288
Cdd:cd00116   162 RANrdLKELNLANNGIgdagiRALAEGLKANCNLEVLDLNNNGLTDegasaLAETLASLKSLEVLNLGDNNLTDAGaAAL 241

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695271686  289 CkltklkklylnsnkldfDGLPSGIGKLTSLEefmAANNNLELIP-ESLCRC----PKLKKLVLNKNRL 352
Cdd:cd00116   242 A-----------------SALLSPNISLLTLS---LSCNDITDDGaKDLAEVlaekESLLELDLRGNKF 290
LRR_8 pfam13855
Leucine rich repeat;
106-163 1.05e-07

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 49.83  E-value: 1.05e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 695271686   106 LSVLDLSHNQLTECPRE-LENAKNMLVLNLSHNGIDSIPNQLFINLTDLLYLDLSENRL 163
Cdd:pfam13855    3 LRSLDLSNNRLTSLDDGaFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
LRR_8 pfam13855
Leucine rich repeat;
223-281 2.27e-07

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 48.67  E-value: 2.27e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695271686   223 SNLSDVDLSCNDLTRV-PECLYTLPSLRRLNLSSNQIAELSL-CIDQWVHLETLNLSRNQL 281
Cdd:pfam13855    1 PNLRSLDLSNNRLTSLdDGAFKGLSNLKVLDLSNNLLTTLSPgAFSGLPSLRYLDLSGNRL 61
Gelsolin pfam00626
Gelsolin repeat;
1182-1255 5.80e-07

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 48.07  E-value: 5.80e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695271686  1182 KCSDFCQDDLADDDIMLLDNGQEVYMWVGTQTSQVEIKLSLKACQVYIQHTRskeHERPRRLRLVRkGNEQRAF 1255
Cdd:pfam00626    6 PPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDER---FPLPEVIRVPQ-GKEPARF 75
LRR_8 pfam13855
Leucine rich repeat;
200-258 6.88e-07

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 47.52  E-value: 6.88e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695271686   200 LQTLHLRNtqrtqSNL----PTSLEGLSNLSDVDLSCNDLTRV-PECLYTLPSLRRLNLSSNQI 258
Cdd:pfam13855    3 LRSLDLSN-----NRLtsldDGAFKGLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
Gelsolin pfam00626
Gelsolin repeat;
755-831 1.70e-06

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 46.92  E-value: 1.70e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695271686   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 ...
 74-282 2.92e-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: 50.82  E-value: 2.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686   74 ELSSLPSLRAIVARANSLKNSGVPDDIFKLD---DLSVLDLSHNQLTECPRELENAKNMLV-------LNLSHNGIDSIP 143
Cdd:cd00116    18 LLPKLLCLQVLRLEGNTLGEEAAKALASALRpqpSLKELCLSLNETGRIPRGLQSLLQGLTkgcglqeLDLSDNALGPDG 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686  144 NQLFINLT---DLLYLDLSENRLESLPPQM--RRLVHLQ----TLVLNGNPLLHAQLRQ----LPAMMALQTLHLRNTQR 210
Cdd:cd00116    98 CGVLESLLrssSLQELKLNNNGLGDRGLRLlaKGLKDLPpaleKLVLGRNRLEGASCEAlakaLRANRDLKELNLANNGI 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686  211 TQSNLPTSLEGL---SNLSDVDLSCNDLTR-----VPECLYTLPSLRRLNLSSNQIAELSLC------IDQWVHLETLNL 276
Cdd:cd00116   178 GDAGIRALAEGLkanCNLEVLDLNNNGLTDegasaLAETLASLKSLEVLNLGDNNLTDAGAAalasalLSPNISLLTLSL 257


                  ....*.
gi 695271686  277 SRNQLT 282
Cdd:cd00116   258 SCNDIT 263
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 1054-1146 2.93e-06

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


Pssm-ID: 200436  Cd Length: 88  Bit Score: 46.59  E-value: 2.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686 1054 QPTLYQIRTNGSalcTRCIQINTDSSLLNSEFCFILkvpfeseDNQGIVYAWVGRASDPDE----AKLAEDILNTMFDAS 1129
Cdd:cd11280     1 PPRLYRVRGSKA---IEIEEVPLASSSLDSDDVFVL-------DTGSEIYIWQGRASSQAElaaaALLAKELDEERKGKP 70

                          90
                  ....*....|....*..
gi 695271686 1130 YSkQVINEGEEPEnFFW 1146
Cdd:cd11280    71 EI-VRIRQGQEPR-EFW 85
PRK15387 PRK15387
type III secretion system effector E3 ubiquitin transferase SspH2;
38-325 5.02e-06

type III secretion system effector E3 ubiquitin transferase SspH2;


Pssm-ID: 185285 [Multi-domain]  Cd Length: 788  Bit Score: 50.93  E-value: 5.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686   38 LKLNRTGLCYLPEELAAlqKLEHLSVSHNHLTTLHgelSSLPSLRAIVARANSLKNSGV-PDDIFKLDDLSvldlshNQL 116
Cdd:PRK15387  206 LNVGESGLTTLPDCLPA--HITTLVIPDNNLTSLP---ALPPELRTLEVSGNQLTSLPVlPPGLLELSIFS------NPL 274

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686  117 TECPRELENAKNMLVLNlshNGIDSIPnqlfINLTDLLYLDLSENRLESLPPQMRRLVHLQTLvlngnpllHAQLRQLPA 196
Cdd:PRK15387  275 THLPALPSGLCKLWIFG---NQLTSLP----VLPPGLQELSVSDNQLASLPALPSELCKLWAY--------NNQLTSLPT 339

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686  197 M-MALQTLHLRNTQRTQ--------------SNLPTSLEGL-SNLSDVDLSCNDLTRVPeclyTLPS-LRRLNLSSNQIA 259
Cdd:PRK15387  340 LpSGLQELSVSDNQLASlptlpselyklwayNNRLTSLPALpSGLKELIVSGNRLTSLP----VLPSeLKELMVSGNRLT 415

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695271686  260 ELSLCIDQwvhLETLNLSRNQLTSLPSAICkltklkkLYLNSNKLDFDGLPSGIGKLTSLEEFMAA 325
Cdd:PRK15387  416 SLPMLPSG---LLSLSVYRNQLTRLPESLI-------HLSSETTVNLEGNPLSERTLQALREITSA 471
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 641-703 8.94e-06

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: 45.75  E-value: 8.94e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695271686  641 LDPRFVFLLDQGLDIYVWRGAQAT-----LSNTTkARLFAEKINKNERKGKAEITLLVQGQEPPGF------WD 703
Cdd:cd11291    27 LDTDDIMLLDTGDEVFVWVGSESSdeekkEALTS-AKKYIETDPLGRSKPRTPIYLVKQGNEPPTFtgyfhaWD 99
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 33-200 1.30e-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: 48.89  E-value: 1.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686   33 TSLRWLKLNR------------TGLCYLPEELAALQkLEHLSVSHNHLTTLHGELSSLPSLRAIVARANSLKNSGVPD-- 98
Cdd:cd00116   108 SSLQELKLNNnglgdrglrllaKGLKDLPPALEKLV-LGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRAla 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686   99 DIFK-LDDLSVLDLSHNQLT--------ECPRELenaKNMLVLNLSHNGIDSIP-----NQLFINLTDLLYLDLSENRLE 164
Cdd:cd00116   187 EGLKaNCNLEVLDLNNNGLTdegasalaETLASL---KSLEVLNLGDNNLTDAGaaalaSALLSPNISLLTLSLSCNDIT 263

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 695271686  165 -----SLPPQMRRLVHLQTLVLNGNPL------LHAQLRQLPAMMAL 200
Cdd:cd00116   264 ddgakDLAEVLAEKESLLELDLRGNKFgeegaqLLAESLLEPGNELE 310
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 106-284 1.43e-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: 49.02  E-value: 1.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686  106 LSVLDLSHNQL-TECPRELENA----KNMLVLNLSHNGID----SIPNQLFINLTDLLYLDLSENRL---------ESLp 167
Cdd:COG5238   182 VETVYLGCNQIgDEGIEELAEAltqnTTVTTLWLKRNPIGdegaEILAEALKGNKSLTTLDLSNNQIgdegvialaEAL- 260

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686  168 pQMRRLVHlqTLVLNGNPLLHAQLRQLPAMMA----LQTLHLRNTQ---RTQSNLPTSLEGLSNLSDVDLSCNDLT---- 236
Cdd:COG5238   261 -KNNTTVE--TLYLSGNQIGAEGAIALAKALQgnttLTSLDLSVNRigdEGAIALAEGLQGNKTLHTLNLAYNGIGaqga 337

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 695271686  237 -RVPECLYTLPSLRRLNLSSNQI-----AELSLCIDQWVHLETLNLSRNQLTSL 284
Cdd:COG5238   338 iALAKALQENTTLHSLDLSDNQIgdegaIALAKYLEGNTTLRELNLGKNNIGKQ 391
Gelsolin pfam00626
Gelsolin repeat;
1077-1144 2.44e-05

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 43.45  E-value: 2.44e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695271686  1077 DSSLLNSEFCFILkvpfeseDNQGIVYAWVGRASDPDE----AKLAEDILNTMFDASYSKQVINEGEEPENF 1144
Cdd:pfam00626   11 SQESLNSGDCYLL-------DNGFTIFLWVGKGSSLLEklfaALLAAQLDDDERFPLPEVIRVPQGKEPARF 75
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 1-282 3.67e-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: 47.86  E-value: 3.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686    1 MEATGVLPFVRGVDLSGN---DFKGGYFPENVKAMTSLRWLKLNRT-----GLCYLPEELAALQKLEHLSVSHNHLTTlh 72
Cdd:COG5238   173 MAKALQNNSVETVYLGCNqigDEGIEELAEALTQNTTVTTLWLKRNpigdeGAEILAEALKGNKSLTTLDLSNNQIGD-- 250

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686   73 gelsslpslRAIVARANSLKNSgvpddifklDDLSVLDLSHNQLTecprelenaknmlvlnlsHNGIDSIPNQLFINlTD 152
Cdd:COG5238   251 ---------EGVIALAEALKNN---------TTVETLYLSGNQIG------------------AEGAIALAKALQGN-TT 293

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686  153 LLYLDLSENRL-----ESLPPQMRRLVHLQTLVLNGNPLLHAQLRQLPAmmALQTLhlrntqrtqsnlptsleglSNLSD 227
Cdd:COG5238   294 LTSLDLSVNRIgdegaIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAK--ALQEN-------------------TTLHS 352

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695271686  228 VDLSCNDLT-----RVPECLYTLPSLRRLNLSSNQIAEL-------SLCIDQwvhLETLNLSRNQLT 282
Cdd:COG5238   353 LDLSDNQIGdegaiALAKYLEGNTTLRELNLGKNNIGKQgaealidALQTNR---LHTLILDGNLIG 416
PRK15387 PRK15387
type III secretion system effector E3 ubiquitin transferase SspH2;
8-263 8.35e-05

type III secretion system effector E3 ubiquitin transferase SspH2;


Pssm-ID: 185285 [Multi-domain]  Cd Length: 788  Bit Score: 47.08  E-value: 8.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686    8 PFVRGVDLSGNDFKG-GYFPENVKAMT----SLRWLKLNRTGLCYL---PEELAALQ----KLEHLSVSHNhlttlhgEL 75
Cdd:PRK15387  242 PELRTLEVSGNQLTSlPVLPPGLLELSifsnPLTHLPALPSGLCKLwifGNQLTSLPvlppGLQELSVSDN-------QL 314

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686   76 SSLPSLRAIVARANSLKN--SGVPDDIFKLDDLSVLDlshNQLTECPrelenaknmlvlnlshngidSIPNQLFinltdl 153
Cdd:PRK15387  315 ASLPALPSELCKLWAYNNqlTSLPTLPSGLQELSVSD---NQLASLP--------------------TLPSELY------ 365

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686  154 lYLDLSENRLESLPPQMRrlvHLQTLVLNGN-----PLLHAQLRQLpaMMALQTLhlrntqrtqSNLPTSLEGLSNLSdv 228
Cdd:PRK15387  366 -KLWAYNNRLTSLPALPS---GLKELIVSGNrltslPVLPSELKEL--MVSGNRL---------TSLPMLPSGLLSLS-- 428

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 695271686  229 dLSCNDLTRVPECLYTLPSLRRLNLSSNQIAELSL 263
Cdd:PRK15387  429 -VYRNQLTRLPESLIHLSSETTVNLEGNPLSERTL 462
LRR_8 pfam13855
Leucine rich repeat;
56-116 1.76e-04

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 40.59  E-value: 1.76e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695271686    56 QKLEHLSVSHNHLTTLHGE-LSSLPSLRAIVARANSLKNSGvPDDIFKLDDLSVLDLSHNQL 116
Cdd:pfam13855    1 PNLRSLDLSNNRLTSLDDGaFKGLSNLKVLDLSNNLLTTLS-PGAFSGLPSLRYLDLSGNRL 61
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 912-1036 2.17e-04

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 41.51  E-value: 2.17e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686    912 EGRKFTRLPEEEF--GHFYTQDCYVFLCRYwvpveyeeeektedkegkasaearegeeaaaeaeekqpeedfqcIVYFWQ 989
Cdd:smart00262    6 KGKRNVRVPEVPFsqGSLNSGDCYILDTGS--------------------------------------------EIYVWV 41

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*..
gi 695271686    990 GREASNMGWLTFTFSLQKKFESLFPGKLEVVRMTQQQENPKFLSHFK 1036
Cdd:smart00262   42 GKKSSQDEKKKAAELAVELDDTLGPGPVQVRVVDEGKEPPEFWSLFG 88
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 246-285 3.41e-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: 39.54  E-value: 3.41e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 695271686   246 PSLRRLNLSSNQIAELSLcIDQWVHLETLNLSRN-QLTSLP 285
Cdd:pfam12799    1 PNLEVLDLSNNQITDIPP-LAKLPNLETLDLSGNnKITDLS 40
LRR_8 pfam13855
Leucine rich repeat;
33-91 4.58e-04

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 39.43  E-value: 4.58e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695271686    33 TSLRWLKLNRTGLCYLPEE-LAALQKLEHLSVSHNHLTTLH-GELSSLPSLRAIVARANSL 91
Cdd:pfam13855    1 PNLRSLDLSNNRLTSLDDGaFKGLSNLKVLDLSNNLLTTLSpGAFSGLPSLRYLDLSGNRL 61
PLN03150 PLN03150
hypothetical protein; Provisional
 166-259 7.84e-04

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 43.65  E-value: 7.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686  166 LPPQMRRLVHLQTLVLNGNPLlhaqlrqlpammalqtlhlrntqrtQSNLPTSLEGLSNLSDVDLSCNDLT-RVPECLYT 244
Cdd:PLN03150  434 IPNDISKLRHLQSINLSGNSI-------------------------RGNIPPSLGSITSLEVLDLSYNSFNgSIPESLGQ 488

                          90
                  ....*....|....*
gi 695271686  245 LPSLRRLNLSSNQIA 259
Cdd:PLN03150  489 LTSLRILNLNGNSLS 503
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 2-137 1.60e-03

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: 42.34  E-value: 1.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686    2 EATGVLPFVRG---VDLSGNDFKGGYFP---ENVKAMTSLRWLKLNRTGLC-----YLPEELAALQKLEHLSVSHNHLT- 69
Cdd:cd00116   156 ALAKALRANRDlkeLNLANNGIGDAGIRalaEGLKANCNLEVLDLNNNGLTdegasALAETLASLKSLEVLNLGDNNLTd 235

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686   70 ----TLH-GELSSLPSLRAIVARANSLKNSGVPDDIFKLDD---LSVLDLSHNQLTE------CPRELENAKNMLVLNLS 135
Cdd:cd00116   236 agaaALAsALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEkesLLELDLRGNKFGEegaqllAESLLEPGNELESLWVK 315


                  ..
gi 695271686  136 HN 137
Cdd:cd00116   316 DD 317
PLN03150 PLN03150
hypothetical protein; Provisional
 90-204 2.00e-03

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 42.50  E-value: 2.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686   90 SLKNSG----VPDDIFKLddlsvldlshnqltecpRELENaknmlvLNLSHNGIDSIPNQLFINLTDLLYLDLSENRLE- 164
Cdd:PLN03150  424 GLDNQGlrgfIPNDISKL-----------------RHLQS------INLSGNSIRGNIPPSLGSITSLEVLDLSYNSFNg 480

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 695271686  165 SLPPQMRRLVHLQTLVLNGNPLLHaqlrQLPAMMALQTLH 204
Cdd:PLN03150  481 SIPESLGQLTSLRILNLNGNSLSG----RVPAALGGRLLH 516
PLN03210 PLN03210
Resistant to P. syringae 6; Provisional
 127-401 2.70e-03

Resistant to P. syringae 6; Provisional


Pssm-ID: 215633 [Multi-domain]  Cd Length: 1153  Bit Score: 42.17  E-value: 2.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686  127 KNMLVLNLSHNGIDS--IPNQLFINLTDLLYLDLSENRLES-------LPPQMRRLVH-LQTLVLNGNPLlhaqlRQLPA 196
Cdd:PLN03210  532 KKVLGITLDIDEIDElhIHENAFKGMRNLLFLKFYTKKWDQkkevrwhLPEGFDYLPPkLRLLRWDKYPL-----RCMPS 606

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686  197 mmALQTLHLRNTQRTQSNLPTSLEG---LSNLSDVDL-SCNDLTRVPEcLYTLPSLRRLNLSS-NQIAELSLCIDQWVHL 271
Cdd:PLN03210  607 --NFRPENLVKLQMQGSKLEKLWDGvhsLTGLRNIDLrGSKNLKEIPD-LSMATNLETLKLSDcSSLVELPSSIQYLNKL 683

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686  272 ETLNLSR-NQLTSLPSAICKLTKLKKLYLNSNKLD-FDGLPSGIGKL----TSLEEFmAANNNLE-LIPESLCRC----- 339
Cdd:PLN03210  684 EDLDMSRcENLEILPTGINLKSLYRLNLSGCSRLKsFPDISTNISWLdldeTAIEEF-PSNLRLEnLDELILCEMksekl 762

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695271686  340 ---------------PKLKKLVLNKN-RLVTLPEAIHFLTEIQVLDVRENPSLVMPPKPADRTAeWYNIDFSLQNQLR 401
Cdd:PLN03210  763 wervqpltplmtmlsPSLTRLFLSDIpSLVELPSSIQNLHKLEHLEIENCINLETLPTGINLES-LESLDLSGCSRLR 839
PLN03150 PLN03150
hypothetical protein; Provisional
 33-117 4.50e-03

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 41.34  E-value: 4.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695271686   33 TSLRW----LKLNRTGL-CYLPEELAALQKLEHLSVSHNhltTLHGELS----SLPSLRAIVARANSLkNSGVPDDIFKL 103
Cdd:PLN03150  414 TKGKWfidgLGLDNQGLrGFIPNDISKLRHLQSINLSGN---SIRGNIPpslgSITSLEVLDLSYNSF-NGSIPESLGQL 489

                          90
                  ....*....|....
gi 695271686  104 DDLSVLDLSHNQLT 117
Cdd:PLN03150  490 TSLRILNLNGNSLS 503
LRR_8 pfam13855
Leucine rich repeat;
246-284 6.53e-03

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 36.35  E-value: 6.53e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 695271686   246 PSLRRLNLSSNQIAELSlciDQW----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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