NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|372266127|ref|NP_001243193|]
View 

protein flightless-1 homolog isoform 2 [Homo sapiens]

Protein Classification

flightless-1 family protein( domain architecture ID 11469395)

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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; ...
 481-593 1.23e-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: 205.53  E-value: 1.23e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127  481 TEDVGQLPGLTIWQIENFVPVLVEEAFHGKFYEADCYIVLKTFLDDSGSLNWEIYYWIGGEATLDKKACSAIHAVNLRNY 560
Cdd:cd11290     1 FEGVGQKPGLQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDPSGSLSYDIHYWLGKEASQDEAGAAAIKAVELDDY 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 372266127  561 LGAECRTVREEMGDESEEFLQVFDNDISYIEGG 593
Cdd:cd11290    81 LGGRPVQHREVQGHESEEFLSYFKKGIIYIEGG 113
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 1152-1251 7.07e-48

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: 165.55  E-value: 7.07e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127 1152 HTRLFRCSNEKGYFaVTEKCSDFCQDDLADDDIMLLDNGQEVYMWVGTQTSQVEIKLSLKACQVYIQHMRSKEHERPRRL 1231
Cdd:cd11291     1 KPRLFRCSNESGFF-KVEEISDFSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYIETDPLGRSKPRTPI 79

                          90       100
                  ....*....|....*....|
gi 372266127 1232 RLVRKGNEQHAFTRCFHAWS 1251
Cdd:cd11291    80 YLVKQGNEPPTFTGYFHAWD 99
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
13-364 3.98e-39

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


:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 151.24  E-value: 3.98e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127   13 YFPENVKAMTSLRWLKLNRTglcylpEELAALQKLEHLSVSHNNLTTLHGELSSLPSLRAIVARANSLKNsgVPDDIFKL 92
Cdd:COG4886    87 LGLTDLGDLTNLTELDLSGN------EELSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTD--LPEPLGNL 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127   93 DDLSVLDLSHNQLTECPRELENAKNMLVLNLSHNSIDTIPNQLFiNLTDLLYLDLSENRLESLPPQMRRLVHLQTLVLNG 172
Cdd:COG4886   159 TNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLG-NLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSN 237

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127  173 NpllhaQLRQLPamtalqtlhlrstqrtqsnlptSLEGLSNLADVDLSCNDLTRVPEcLYTLPSLRRLNLSSNQITELSL 252
Cdd:COG4886   238 N-----QLTDLP----------------------ELGNLTNLEELDLSNNQLTDLPP-LANLTNLKTLDLSNNQLTDLKL 289

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127  253 CIDQwvhvETLNLSRNQLTSLPSAICKLSKLKKLYLNSNKLDFDGLPSGIGKLTNLEEFMAANNNLELVPESLCRCPKLR 332
Cdd:COG4886   290 KELE----LLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTL 365

                         330       340       350
                  ....*....|....*....|....*....|..
gi 372266127  333 KLVLNKNHLVTLPEAIHFLTEIEVLDVRENPN 364
Cdd:COG4886   366 LLTLGLLGLLEATLLTLALLLLTLLLLLLTTT 397
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 1042-1141 4.66e-36

Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


:

Pssm-ID: 200444  Cd Length: 92  Bit Score: 131.58  E-value: 4.66e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127 1042 QPSLYQIRTNGSaLCTRCIQINTDSSLLNSEFCFILKVPFesednqgIVYAWVGRASDPDEAKLAEDILNTMFDtSYSKQ 1121
Cdd:cd11288     2 PTRLFQVRGNGS-GNTRAVEVDADASSLNSNDVFVLKTPS-------SVYLWVGKGSSEDERELAKDVASFLKP-KASLQ 72

                          90       100
                  ....*....|....*....|
gi 372266127 1122 VINEGEEPENFFWVGIGAQK 1141
Cdd:cd11288    73 EVAEGSEPDEFWEALGGKSE 92
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 712-826 1.11e-32

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


:

Pssm-ID: 200448  Cd Length: 98  Bit Score: 122.36  E-value: 1.11e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127  712 PPQPKLYKVGLGLGYLELPQINYKLsvehkqrpkvelmprmrLLQSLLDTRCVYILDCWSDVFIWLGRKSPRLVRAAALK 791
Cdd:cd11292     1 AEQKKLYKVSDASGKLKLTEVAEGS-----------------LNQEMLDSEDCYILDCGSEIFVWVGKGASLDERKAALK 63

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 372266127  792 LGQELCGMLHRPRHATVSRSLEGTEAQVFKAKFKN 826
Cdd:cd11292    64 NAEEFLRKKKRPPYTQVTRVTEGGESALFKSKFAN 98
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 608-695 2.24e-28

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


:

Pssm-ID: 200436  Cd Length: 88  Bit Score: 109.38  E-value: 2.24e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127  608 TRMYRVYGKKNIKLEPVPLKGTSLDPRFVFLLDRGLDIYVWRGAQATLSSTTKARLFAEKINKnERKGKAEITLLVQGQE 687
Cdd:cd11280     2 PRLYRVRGSKAIEIEEVPLASSSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKELDE-ERKGKPEIVRIRQGQE 80


                  ....*...
gi 372266127  688 LPEFWEAL 695
Cdd:cd11280    81 PREFWSLF 88
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 963-1023 1.12e-18

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


:

Pssm-ID: 200436  Cd Length: 88  Bit Score: 82.03  E-value: 1.12e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 372266127  963 KQPEEDFQCIVYFWQGReASNMGWLTFTFSLQKKFESLFPGKLEVVRMTQQQENPKFLSHF 1023
Cdd:cd11280    29 DVFVLDTGSEIYIWQGR-ASSQAELAAAALLAKELDEERKGKPEIVRIRQGQEPREFWSLF 88
 
Name Accession Description Interval E-value
gelsolin_S1_like cd11290
Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; ...
 481-593 1.23e-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: 205.53  E-value: 1.23e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127  481 TEDVGQLPGLTIWQIENFVPVLVEEAFHGKFYEADCYIVLKTFLDDSGSLNWEIYYWIGGEATLDKKACSAIHAVNLRNY 560
Cdd:cd11290     1 FEGVGQKPGLQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDPSGSLSYDIHYWLGKEASQDEAGAAAIKAVELDDY 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 372266127  561 LGAECRTVREEMGDESEEFLQVFDNDISYIEGG 593
Cdd:cd11290    81 LGGRPVQHREVQGHESEEFLSYFKKGIIYIEGG 113
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 1152-1251 7.07e-48

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: 165.55  E-value: 7.07e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127 1152 HTRLFRCSNEKGYFaVTEKCSDFCQDDLADDDIMLLDNGQEVYMWVGTQTSQVEIKLSLKACQVYIQHMRSKEHERPRRL 1231
Cdd:cd11291     1 KPRLFRCSNESGFF-KVEEISDFSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYIETDPLGRSKPRTPI 79

                          90       100
                  ....*....|....*....|
gi 372266127 1232 RLVRKGNEQHAFTRCFHAWS 1251
Cdd:cd11291    80 YLVKQGNEPPTFTGYFHAWD 99
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
13-364 3.98e-39

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 151.24  E-value: 3.98e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127   13 YFPENVKAMTSLRWLKLNRTglcylpEELAALQKLEHLSVSHNNLTTLHGELSSLPSLRAIVARANSLKNsgVPDDIFKL 92
Cdd:COG4886    87 LGLTDLGDLTNLTELDLSGN------EELSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTD--LPEPLGNL 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127   93 DDLSVLDLSHNQLTECPRELENAKNMLVLNLSHNSIDTIPNQLFiNLTDLLYLDLSENRLESLPPQMRRLVHLQTLVLNG 172
Cdd:COG4886   159 TNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLG-NLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSN 237

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127  173 NpllhaQLRQLPamtalqtlhlrstqrtqsnlptSLEGLSNLADVDLSCNDLTRVPEcLYTLPSLRRLNLSSNQITELSL 252
Cdd:COG4886   238 N-----QLTDLP----------------------ELGNLTNLEELDLSNNQLTDLPP-LANLTNLKTLDLSNNQLTDLKL 289

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127  253 CIDQwvhvETLNLSRNQLTSLPSAICKLSKLKKLYLNSNKLDFDGLPSGIGKLTNLEEFMAANNNLELVPESLCRCPKLR 332
Cdd:COG4886   290 KELE----LLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTL 365

                         330       340       350
                  ....*....|....*....|....*....|..
gi 372266127  333 KLVLNKNHLVTLPEAIHFLTEIEVLDVRENPN 364
Cdd:COG4886   366 LLTLGLLGLLEATLLTLALLLLTLLLLLLTTT 397
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 1042-1141 4.66e-36

Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200444  Cd Length: 92  Bit Score: 131.58  E-value: 4.66e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127 1042 QPSLYQIRTNGSaLCTRCIQINTDSSLLNSEFCFILKVPFesednqgIVYAWVGRASDPDEAKLAEDILNTMFDtSYSKQ 1121
Cdd:cd11288     2 PTRLFQVRGNGS-GNTRAVEVDADASSLNSNDVFVLKTPS-------SVYLWVGKGSSEDERELAKDVASFLKP-KASLQ 72

                          90       100
                  ....*....|....*....|
gi 372266127 1122 VINEGEEPENFFWVGIGAQK 1141
Cdd:cd11288    73 EVAEGSEPDEFWEALGGKSE 92
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 712-826 1.11e-32

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


Pssm-ID: 200448  Cd Length: 98  Bit Score: 122.36  E-value: 1.11e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127  712 PPQPKLYKVGLGLGYLELPQINYKLsvehkqrpkvelmprmrLLQSLLDTRCVYILDCWSDVFIWLGRKSPRLVRAAALK 791
Cdd:cd11292     1 AEQKKLYKVSDASGKLKLTEVAEGS-----------------LNQEMLDSEDCYILDCGSEIFVWVGKGASLDERKAALK 63

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 372266127  792 LGQELCGMLHRPRHATVSRSLEGTEAQVFKAKFKN 826
Cdd:cd11292    64 NAEEFLRKKKRPPYTQVTRVTEGGESALFKSKFAN 98
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 608-695 2.24e-28

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


Pssm-ID: 200436  Cd Length: 88  Bit Score: 109.38  E-value: 2.24e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127  608 TRMYRVYGKKNIKLEPVPLKGTSLDPRFVFLLDRGLDIYVWRGAQATLSSTTKARLFAEKINKnERKGKAEITLLVQGQE 687
Cdd:cd11280     2 PRLYRVRGSKAIEIEEVPLASSSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKELDE-ERKGKPEIVRIRQGQE 80


                  ....*...
gi 372266127  688 LPEFWEAL 695
Cdd:cd11280    81 PREFWSLF 88
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 609-697 8.23e-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: 96.59  E-value: 8.23e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127    609 RMYRVYGKKNIKLEPVPLKGTSLDPRFVFLLDRGLDIYVWRGAQATLSSTTKARLFAEKINKNERKGKAEITLLVQGQEL 688
Cdd:smart00262    1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVRVVDEGKEP 80


                    ....*....
gi 372266127    689 PEFWEALGG 697
Cdd:smart00262   81 PEFWSLFGG 89
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1157-1250 2.13e-23

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 95.44  E-value: 2.13e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127   1157 RCSNEKGYFAVTEKCSDFCQDDLADDDIMLLDNGQEVYMWVGTQTSQVEIKLSLKACQVYIQHMRSkeheRPRRLRLVRK 1236
Cdd:smart00262    1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGP----GPVQVRVVDE 76

                            90
                    ....*....|....
gi 372266127   1237 GNEQHAFTRCFHAW 1250
Cdd:smart00262   77 GKEPPEFWSLFGGW 90
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 12-362 4.32e-21

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 100.31  E-value: 4.32e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127   12 GYFPENVKAMTSLRWLKLNRTGLC-YLPEELAALQKLEHLSVSHNNLT-TLHGELSSLPSLRAIVARANSLkNSGVPDDI 89
Cdd:PLN00113  154 GEIPNDIGSFSSLKVLDLGGNVLVgKIPNSLTNLTSLEFLTLASNQLVgQIPRELGQMKSLKWIYLGYNNL-SGEIPYEI 232

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127   90 FKLDDLSVLDLSHNQLT-ECPRELENAKNMLVLNLSHNSI-DTIPNQLFiNLTDLLYLDLSENRLE-SLPPQMRRLVHLQ 166
Cdd:PLN00113  233 GGLTSLNHLDLVYNNLTgPIPSSLGNLKNLQYLFLYQNKLsGPIPPSIF-SLQKLISLDLSDNSLSgEIPELVIQLQNLE 311

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127  167 TLVLNGNPLLHAQLRQLPAMTALQTLHLRStQRTQSNLPTSLEGLSNLADVDLSCNDLT--------------------- 225
Cdd:PLN00113  312 ILHLFSNNFTGKIPVALTSLPRLQVLQLWS-NKFSGEIPKNLGKHNNLTVLDLSTNNLTgeipeglcssgnlfklilfsn 390

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127  226 ----RVPECLYTLPSLRRLNLSSNQIT-ELSLCIDQWVHVETLNLSRNQLT-SLPSAICKLSKLKKLYLNSNKLdFDGLP 299
Cdd:PLN00113  391 slegEIPKSLGACRSLRRVRLQDNSFSgELPSEFTKLPLVYFLDISNNNLQgRINSRKWDMPSLQMLSLARNKF-FGGLP 469

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 372266127  300 --SGIGKLTNLEefMAANNNLELVPESLCRCPKLRKLVLNKNHLV-TLPEAIHFLTEIEVLDVREN 362
Cdd:PLN00113  470 dsFGSKRLENLD--LSRNQFSGAVPRKLGSLSELMQLKLSENKLSgEIPDELSSCKKLVSLDLSHN 533
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 963-1023 1.12e-18

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


Pssm-ID: 200436  Cd Length: 88  Bit Score: 82.03  E-value: 1.12e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 372266127  963 KQPEEDFQCIVYFWQGReASNMGWLTFTFSLQKKFESLFPGKLEVVRMTQQQENPKFLSHF 1023
Cdd:cd11280    29 DVFVLDTGSEIYIWQGR-ASSQAELAAAALLAKELDEERKGKPEIVRIRQGQEPREFWSLF 88
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 740-827 1.93e-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: 81.18  E-value: 1.93e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127    740 HKQRPKVELMPRMRLLQSLLDTRCVYILDCWSDVFIWLGRKSPRLVRAAALKLGQELCGMLHrPRHATVSRSLEGTEAQV 819
Cdd:smart00262    4 RVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLG-PGPVQVRVVDEGKEPPE 82


                    ....*...
gi 372266127    820 FKAKFKNW 827
Cdd:smart00262   83 FWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 492-585 4.04e-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: 4.04e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127    492 IWQIENFVPVLVEE--AFHGKFYEADCYIVLKTflddsgslnWEIYYWIGGEATLDKKACSAIHAVNLRNYLGAECRTVR 569
Cdd:smart00262    2 LVRVKGKRNVRVPEvpFSQGSLNSGDCYILDTG---------SEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVR 72

                            90
                    ....*....|....*..
gi 372266127    570 E-EMGDESEEFLQVFDN 585
Cdd:smart00262   73 VvDEGKEPPEFWSLFGG 89
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1046-1138 4.77e-16

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 74.64  E-value: 4.77e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127   1046 YQIRTNGSaLCTRCIQINTDSSLLNSEFCFILkvpfeseDNQGIVYAWVGRASDPDEAKLAEDILNTMFDTSYSK----Q 1121
Cdd:smart00262    1 FLVRVKGK-RNVRVPEVPFSQGSLNSGDCYIL-------DTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGpvqvR 72

                            90
                    ....*....|....*..
gi 372266127   1122 VINEGEEPENFFWVGIG 1138
Cdd:smart00262   73 VVDEGKEPPEFWSLFGG 89
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 92-274 4.21e-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: 75.59  E-value: 4.21e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127   92 LDDLSVLDLSHNQLTECPrELENAKNMLVLNLSHNSIDTIPNqlFINLTDLLYLDLSENRLESLPPqMRRLVHLQTLVLN 171
Cdd:cd21340     1 LKRITHLYLNDKNITKID-NLSLCKNLKVLYLYDNKITKIEN--LEFLTNLTHLYLQNNQIEKIEN-LENLVNLKKLYLG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127  172 GNPLlhAQLRQLPAMTALQTLHLrSTQRTQSNL-----PTSLEGLSN-LADVDLSCNDLTRVpECLYTLPSLRRLNLSSN 245
Cdd:cd21340    77 GNRI--SVVEGLENLTNLEELHI-ENQRLPPGEkltfdPRSLAALSNsLRVLNISGNNIDSL-EPLAPLRNLEQLDASNN 152

                         170       180       190
                  ....*....|....*....|....*....|..
gi 372266127  246 QIT---ELSLCIDQWVHVETLNLSRNQLTSLP 274
Cdd:cd21340   153 QISdleELLDLLSSWPSLRELDLTGNPVCKKP 184
Gelsolin pfam00626
Gelsolin repeat;
617-692 2.27e-14

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 69.26  E-value: 2.27e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 372266127   617 KNIKLEPVPLKGTSLDPRFVFLLDRGLDIYVWRGAQATLSSTTKARLFAEKINKNERKGKAEITLLVQGQELPEFW 692
Cdd:pfam00626    1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDERFPLPEVIRVPQGKEPARFL 76
Gelsolin pfam00626
Gelsolin repeat;
497-580 1.63e-12

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 63.87  E-value: 1.63e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127   497 NFVPVLVEEAFHGKFYEADCYIVLKTFlddsgslnwEIYYWIGGEATLDKKACSAIHAVNLR-NYLGAECRTVREEMGDE 575
Cdd:pfam00626    1 KFVLPPPVPLSQESLNSGDCYLLDNGF---------TIFLWVGKGSSLLEKLFAALLAAQLDdDERFPLPEVIRVPQGKE 71


                   ....*
gi 372266127   576 SEEFL 580
Cdd:pfam00626   72 PARFL 76
LRR_8 pfam13855
Leucine rich repeat;
120-175 3.40e-11

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 59.85  E-value: 3.40e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 372266127   120 VLNLSHNSIDTIPNQLFINLTDLLYLDLSENRLESLPPQM-RRLVHLQTLVLNGNPL 175
Cdd:pfam13855    5 SLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAfSGLPSLRYLDLSGNRL 61
Gelsolin pfam00626
Gelsolin repeat;
1170-1243 1.81e-07

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 49.61  E-value: 1.81e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 372266127  1170 KCSDFCQDDLADDDIMLLDNGQEVYMWVGTQTSQVEIklslKACQVYIQHMRSKEHERPRRLRLVRKGNEQHAF 1243
Cdd:pfam00626    6 PPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEK----LFAALLAAQLDDDERFPLPEVIRVPQGKEPARF 75
Gelsolin pfam00626
Gelsolin repeat;
745-821 4.58e-06

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 45.76  E-value: 4.58e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 372266127   745 KVELMPRMRLLQSLLDTRCVYILDCWSDVFIWLGRKSPRLVRAAALKLGQELcGMLHRPRHATVSRSLEGTEAQVFK 821
Cdd:pfam00626    1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQL-DDDERFPLPEVIRVPQGKEPARFL 76
Gelsolin pfam00626
Gelsolin repeat;
1065-1132 1.33e-05

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 44.22  E-value: 1.33e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 372266127  1065 DSSLLNSEFCFILkvpfeseDNQGIVYAWVGRASDPDE----AKLAEDILNTMFDTSYSKQVINEGEEPENF 1132
Cdd:pfam00626   11 SQESLNSGDCYLL-------DNGFTIFLWVGKGSSLLEklfaALLAAQLDDDERFPLPEVIRVPQGKEPARF 75
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 902-1024 1.99e-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: 1.99e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127    902 EGKKFARLPEEEF--GHFYTQDCYVFLCRYwvpveyeeeekkedkeekaegkegeeataeaeekqpeedfqcIVYFWQGR 979
Cdd:smart00262    6 KGKRNVRVPEVPFsqGSLNSGDCYILDTGS------------------------------------------EIYVWVGK 43

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*
gi 372266127    980 EASNMGWLTFTFSLQKKFESLFPGKLEVVRMTQQQENPKFLSHFK 1024
Cdd:smart00262   44 KSSQDEKKKAAELAVELDDTLGPGPVQVRVVDEGKEPPEFWSLFG 88
 
Name Accession Description Interval E-value
gelsolin_S1_like cd11290
Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; ...
 481-593 1.23e-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: 205.53  E-value: 1.23e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127  481 TEDVGQLPGLTIWQIENFVPVLVEEAFHGKFYEADCYIVLKTFLDDSGSLNWEIYYWIGGEATLDKKACSAIHAVNLRNY 560
Cdd:cd11290     1 FEGVGQKPGLQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDPSGSLSYDIHYWLGKEASQDEAGAAAIKAVELDDY 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 372266127  561 LGAECRTVREEMGDESEEFLQVFDNDISYIEGG 593
Cdd:cd11290    81 LGGRPVQHREVQGHESEEFLSYFKKGIIYIEGG 113
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 1152-1251 7.07e-48

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: 165.55  E-value: 7.07e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127 1152 HTRLFRCSNEKGYFaVTEKCSDFCQDDLADDDIMLLDNGQEVYMWVGTQTSQVEIKLSLKACQVYIQHMRSKEHERPRRL 1231
Cdd:cd11291     1 KPRLFRCSNESGFF-KVEEISDFSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYIETDPLGRSKPRTPI 79

                          90       100
                  ....*....|....*....|
gi 372266127 1232 RLVRKGNEQHAFTRCFHAWS 1251
Cdd:cd11291    80 YLVKQGNEPPTFTGYFHAWD 99
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
13-364 3.98e-39

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 151.24  E-value: 3.98e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127   13 YFPENVKAMTSLRWLKLNRTglcylpEELAALQKLEHLSVSHNNLTTLHGELSSLPSLRAIVARANSLKNsgVPDDIFKL 92
Cdd:COG4886    87 LGLTDLGDLTNLTELDLSGN------EELSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTD--LPEPLGNL 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127   93 DDLSVLDLSHNQLTECPRELENAKNMLVLNLSHNSIDTIPNQLFiNLTDLLYLDLSENRLESLPPQMRRLVHLQTLVLNG 172
Cdd:COG4886   159 TNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLG-NLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSN 237

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127  173 NpllhaQLRQLPamtalqtlhlrstqrtqsnlptSLEGLSNLADVDLSCNDLTRVPEcLYTLPSLRRLNLSSNQITELSL 252
Cdd:COG4886   238 N-----QLTDLP----------------------ELGNLTNLEELDLSNNQLTDLPP-LANLTNLKTLDLSNNQLTDLKL 289

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127  253 CIDQwvhvETLNLSRNQLTSLPSAICKLSKLKKLYLNSNKLDFDGLPSGIGKLTNLEEFMAANNNLELVPESLCRCPKLR 332
Cdd:COG4886   290 KELE----LLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTL 365

                         330       340       350
                  ....*....|....*....|....*....|..
gi 372266127  333 KLVLNKNHLVTLPEAIHFLTEIEVLDVRENPN 364
Cdd:COG4886   366 LLTLGLLGLLEATLLTLALLLLTLLLLLLTTT 397
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
27-363 2.45e-38

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 148.93  E-value: 2.45e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127   27 LKLNRTGLCYLPEELAALQKLEHLSVSHNNLTTLHGELSSLPSLRAIVARANSLKNSGVPDDIFKLDDLSVLDLSHNQLT 106
Cdd:COG4886     4 LLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127  107 E---CPRELENAKNMLVLNLSHNsidtipnQLFINLTDLLYLDLSENRLESLPPQMRRLVHLQTLVLNGNPLlhaqlrql 183
Cdd:COG4886    84 LlllGLTDLGDLTNLTELDLSGN-------EELSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQL-------- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127  184 pamtalqtlhlrstqrtqSNLPTSLEGLSNLADVDLSCNDLTRVPECLYTLPSLRRLNLSSNQITELSLCIDQWVHVETL 263
Cdd:COG4886   149 ------------------TDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLEEL 210

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127  264 NLSRNQLTSLPSAicklsklkklylnsnkldfdglpsgIGKLTNLEEFMAANNNLELVPEsLCRCPKLRKLVLNKNHLVT 343
Cdd:COG4886   211 DLSGNQLTDLPEP-------------------------LANLTNLETLDLSNNQLTDLPE-LGNLTNLEELDLSNNQLTD 264

                         330       340
                  ....*....|....*....|
gi 372266127  344 LPEAIHfLTEIEVLDVRENP 363
Cdd:COG4886   265 LPPLAN-LTNLKTLDLSNNQ 283
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 1042-1141 4.66e-36

Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200444  Cd Length: 92  Bit Score: 131.58  E-value: 4.66e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127 1042 QPSLYQIRTNGSaLCTRCIQINTDSSLLNSEFCFILKVPFesednqgIVYAWVGRASDPDEAKLAEDILNTMFDtSYSKQ 1121
Cdd:cd11288     2 PTRLFQVRGNGS-GNTRAVEVDADASSLNSNDVFVLKTPS-------SVYLWVGKGSSEDERELAKDVASFLKP-KASLQ 72

                          90       100
                  ....*....|....*....|
gi 372266127 1122 VINEGEEPENFFWVGIGAQK 1141
Cdd:cd11288    73 EVAEGSEPDEFWEALGGKSE 92
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 712-826 1.11e-32

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


Pssm-ID: 200448  Cd Length: 98  Bit Score: 122.36  E-value: 1.11e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127  712 PPQPKLYKVGLGLGYLELPQINYKLsvehkqrpkvelmprmrLLQSLLDTRCVYILDCWSDVFIWLGRKSPRLVRAAALK 791
Cdd:cd11292     1 AEQKKLYKVSDASGKLKLTEVAEGS-----------------LNQEMLDSEDCYILDCGSEIFVWVGKGASLDERKAALK 63

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 372266127  792 LGQELCGMLHRPRHATVSRSLEGTEAQVFKAKFKN 826
Cdd:cd11292    64 NAEEFLRKKKRPPYTQVTRVTEGGESALFKSKFAN 98
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 608-695 2.24e-28

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


Pssm-ID: 200436  Cd Length: 88  Bit Score: 109.38  E-value: 2.24e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127  608 TRMYRVYGKKNIKLEPVPLKGTSLDPRFVFLLDRGLDIYVWRGAQATLSSTTKARLFAEKINKnERKGKAEITLLVQGQE 687
Cdd:cd11280     2 PRLYRVRGSKAIEIEEVPLASSSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKELDE-ERKGKPEIVRIRQGQE 80


                  ....*...
gi 372266127  688 LPEFWEAL 695
Cdd:cd11280    81 PREFWSLF 88
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 609-697 8.23e-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: 96.59  E-value: 8.23e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127    609 RMYRVYGKKNIKLEPVPLKGTSLDPRFVFLLDRGLDIYVWRGAQATLSSTTKARLFAEKINKNERKGKAEITLLVQGQEL 688
Cdd:smart00262    1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVRVVDEGKEP 80


                    ....*....
gi 372266127    689 PEFWEALGG 697
Cdd:smart00262   81 PEFWSLFGG 89
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1157-1250 2.13e-23

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 95.44  E-value: 2.13e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127   1157 RCSNEKGYFAVTEKCSDFCQDDLADDDIMLLDNGQEVYMWVGTQTSQVEIKLSLKACQVYIQHMRSkeheRPRRLRLVRK 1236
Cdd:smart00262    1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGP----GPVQVRVVDE 76

                            90
                    ....*....|....
gi 372266127   1237 GNEQHAFTRCFHAW 1250
Cdd:smart00262   77 GKEPPEFWSLFGGW 90
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 12-362 4.32e-21

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 100.31  E-value: 4.32e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127   12 GYFPENVKAMTSLRWLKLNRTGLC-YLPEELAALQKLEHLSVSHNNLT-TLHGELSSLPSLRAIVARANSLkNSGVPDDI 89
Cdd:PLN00113  154 GEIPNDIGSFSSLKVLDLGGNVLVgKIPNSLTNLTSLEFLTLASNQLVgQIPRELGQMKSLKWIYLGYNNL-SGEIPYEI 232

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127   90 FKLDDLSVLDLSHNQLT-ECPRELENAKNMLVLNLSHNSI-DTIPNQLFiNLTDLLYLDLSENRLE-SLPPQMRRLVHLQ 166
Cdd:PLN00113  233 GGLTSLNHLDLVYNNLTgPIPSSLGNLKNLQYLFLYQNKLsGPIPPSIF-SLQKLISLDLSDNSLSgEIPELVIQLQNLE 311

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127  167 TLVLNGNPLLHAQLRQLPAMTALQTLHLRStQRTQSNLPTSLEGLSNLADVDLSCNDLT--------------------- 225
Cdd:PLN00113  312 ILHLFSNNFTGKIPVALTSLPRLQVLQLWS-NKFSGEIPKNLGKHNNLTVLDLSTNNLTgeipeglcssgnlfklilfsn 390

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127  226 ----RVPECLYTLPSLRRLNLSSNQIT-ELSLCIDQWVHVETLNLSRNQLT-SLPSAICKLSKLKKLYLNSNKLdFDGLP 299
Cdd:PLN00113  391 slegEIPKSLGACRSLRRVRLQDNSFSgELPSEFTKLPLVYFLDISNNNLQgRINSRKWDMPSLQMLSLARNKF-FGGLP 469

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 372266127  300 --SGIGKLTNLEefMAANNNLELVPESLCRCPKLRKLVLNKNHLV-TLPEAIHFLTEIEVLDVREN 362
Cdd:PLN00113  470 dsFGSKRLENLD--LSRNQFSGAVPRKLGSLSELMQLKLSENKLSgEIPDELSSCKKLVSLDLSHN 533
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
14-275 1.03e-20

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 96.54  E-value: 1.03e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127   14 FPENVKAMTSLRWLKLNRTGLCYLPEELAALQKLEHLSVSHNNLTTLHGELSSLPSLRaivaranslknsgvpddifkld 93
Cdd:COG4886   174 LPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLE---------------------- 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127   94 dlsVLDLSHNQLTECPrELENAKNMLVLNLSHNSIDTIPNQLfiNLTDLLYLDLSENRLESLppQMRRLVHLQTLVLNGN 173
Cdd:COG4886   232 ---TLDLSNNQLTDLP-ELGNLTNLEELDLSNNQLTDLPPLA--NLTNLKTLDLSNNQLTDL--KLKELELLLGLNSLLL 303

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127  174 PLLHAQLRqLPAMTALQTLHLRSTQRTQSNLPTSLEGLSNLADVDLSCNDLTRVPECLYTLPSLRRLNLSSNQITELSLC 253
Cdd:COG4886   304 LLLLLNLL-ELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGLLEATLLTL 382

                         250       260
                  ....*....|....*....|..
gi 372266127  254 IDQWVHVETLNLSRNQLTSLPS 275
Cdd:COG4886   383 ALLLLTLLLLLLTTTAGVLLLT 404
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 12-318 1.11e-20

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 98.77  E-value: 1.11e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127   12 GYFPENVKAMTSLRWLKLNRTGLC-YLPEELAALQKLEHLSVSHNNLT-TLHGELSSLPSLRAIVARANSLkNSGVPDDI 89
Cdd:PLN00113  274 GPIPPSIFSLQKLISLDLSDNSLSgEIPELVIQLQNLEILHLFSNNFTgKIPVALTSLPRLQVLQLWSNKF-SGEIPKNL 352

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127   90 FKLDDLSVLDLSHNQLT-ECPRELENAKNMLVLNLSHNSIDT-IPNQLFiNLTDLLYLDLSENRLE-SLPPQMRRLVHLQ 166
Cdd:PLN00113  353 GKHNNLTVLDLSTNNLTgEIPEGLCSSGNLFKLILFSNSLEGeIPKSLG-ACRSLRRVRLQDNSFSgELPSEFTKLPLVY 431

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127  167 TLVLNGNPLLHAQLRQLPAMTALQTLHLrSTQRTQSNLPTSLeGLSNLADVDLSCNDLT-RVPECLYTLPSLRRLNLSSN 245
Cdd:PLN00113  432 FLDISNNNLQGRINSRKWDMPSLQMLSL-ARNKFFGGLPDSF-GSKRLENLDLSRNQFSgAVPRKLGSLSELMQLKLSEN 509

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 372266127  246 QIT-----ELSLCidqwVHVETLNLSRNQLT-SLPSAICKLSKLKKLYLNSNKLDFDgLPSGIGKLTNLEEFMAANNNL 318
Cdd:PLN00113  510 KLSgeipdELSSC----KKLVSLDLSHNQLSgQIPASFSEMPVLSQLDLSQNQLSGE-IPKNLGNVESLVQVNISHNHL 583
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
 490-583 2.19e-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: 2.19e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127  490 LTIWQIENFVPVLVEEAFHGKFYEADCYIVLKTFlDDSGSLNWEIYYWIGGEATLDKKACSAIHAVNLRNYLGAECRTVR 569
Cdd:cd11293     9 VEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTY-QGGGKEEHILYFWQGRHSSQDERAAAALLTVELDEELKGRAVQVR 87

                          90
                  ....*....|....
gi 372266127  570 EEMGDESEEFLQVF 583
Cdd:cd11293    88 VVQGKEPPHFLALF 101
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 963-1023 1.12e-18

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


Pssm-ID: 200436  Cd Length: 88  Bit Score: 82.03  E-value: 1.12e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 372266127  963 KQPEEDFQCIVYFWQGReASNMGWLTFTFSLQKKFESLFPGKLEVVRMTQQQENPKFLSHF 1023
Cdd:cd11280    29 DVFVLDTGSEIYIWQGR-ASSQAELAAAALLAKELDEERKGKPEIVRIRQGQEPREFWSLF 88
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 740-827 1.93e-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: 81.18  E-value: 1.93e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127    740 HKQRPKVELMPRMRLLQSLLDTRCVYILDCWSDVFIWLGRKSPRLVRAAALKLGQELCGMLHrPRHATVSRSLEGTEAQV 819
Cdd:smart00262    4 RVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLG-PGPVQVRVVDEGKEPPE 82


                    ....*...
gi 372266127    820 FKAKFKNW 827
Cdd:smart00262   83 FWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 492-585 4.04e-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: 4.04e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127    492 IWQIENFVPVLVEE--AFHGKFYEADCYIVLKTflddsgslnWEIYYWIGGEATLDKKACSAIHAVNLRNYLGAECRTVR 569
Cdd:smart00262    2 LVRVKGKRNVRVPEvpFSQGSLNSGDCYILDTG---------SEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVR 72

                            90
                    ....*....|....*..
gi 372266127    570 E-EMGDESEEFLQVFDN 585
Cdd:smart00262   73 VvDEGKEPPEFWSLFGG 89
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 12-341 7.10e-17

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 86.44  E-value: 7.10e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127   12 GYFPENVKAMTSLRWLKLNRTGLC-YLPEELAALQKLEHLSVSHNNLT-TLHGELSSLPSLRAIVARANSLKNSgVPDDI 89
Cdd:PLN00113  202 GQIPRELGQMKSLKWIYLGYNNLSgEIPYEIGGLTSLNHLDLVYNNLTgPIPSSLGNLKNLQYLFLYQNKLSGP-IPPSI 280

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127   90 FKLDDLSVLDLSHNQLT-ECPRELENAKNMLVLNL-SHNSIDTIPN-----------QLFIN------------LTDLLY 144
Cdd:PLN00113  281 FSLQKLISLDLSDNSLSgEIPELVIQLQNLEILHLfSNNFTGKIPValtslprlqvlQLWSNkfsgeipknlgkHNNLTV 360

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127  145 LDLSENRLES-LPPQMRRLVHLQTLVLNGNPLLHAQLRQLPAMTALQTLHLRSTQRTqSNLPTSLEGLSNLADVDLSCND 223
Cdd:PLN00113  361 LDLSTNNLTGeIPEGLCSSGNLFKLILFSNSLEGEIPKSLGACRSLRRVRLQDNSFS-GELPSEFTKLPLVYFLDISNNN 439

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127  224 LT-RVPECLYTLPSLRRLNLSSNQIT-EL--SLCIDQwvhVETLNLSRNQLTSLpsaicklsklkklylnsnkldfdgLP 299
Cdd:PLN00113  440 LQgRINSRKWDMPSLQMLSLARNKFFgGLpdSFGSKR---LENLDLSRNQFSGA------------------------VP 492

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 372266127  300 SGIGKLTNLEEFMAANNNLE-LVPESLCRCPKLRKLVLNKNHL 341
Cdd:PLN00113  493 RKLGSLSELMQLKLSENKLSgEIPDELSSCKKLVSLDLSHNQL 535
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
6-277 1.20e-16

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 85.52  E-value: 1.20e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127    6 LRPVPGGYFPENVKAMTSLR-WLKLNRTGLC-----------YLPEELAALqklehlSVSHNNLTTLHGELSSlpSLRAI 73
Cdd:PRK15370  154 VKEAPAKEAANREEAVQRMRdCLKNNKTELRlkilglttipaCIPEQITTL------ILDNNELKSLPENLQG--NIKTL 225

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127   74 VARANSLknSGVPDDIfkLDDLSVLDLSHNQLTECPRELENAknMLVLNLSHNSIDTIPNqlfiNLTD-LLYLDLSENRL 152
Cdd:PRK15370  226 YANSNQL--TSIPATL--PDTIQEMELSINRITELPERLPSA--LQSLDLFHNKISCLPE----NLPEeLRYLSVYDNSI 295

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127  153 ESLPPQM-RRLVHLqtLVLNGNpllhaqLRQLPAMTALQTLHLRSTQRTQSNLPTSLEglSNLADVDLSCNDLTRVPECL 231
Cdd:PRK15370  296 RTLPAHLpSGITHL--NVQSNS------LTALPETLPPGLKTLEAGENALTSLPASLP--PELQVLDVSKNQITVLPETL 365

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 372266127  232 ytLPSLRRLNLSSNQITELSLCIDqwVHVETLNLSRNQLTSLPSAI 277
Cdd:PRK15370  366 --PPTITTLDVSRNALTNLPENLP--AALQIMQASRNNLVRLPESL 407
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 47-362 2.63e-16

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 84.51  E-value: 2.63e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127   47 LEHLSVSHNNLTtlhGELS--SLPSLRAIvARANSLKNSGVPDDIFKLDDLSVLDL------------------------ 100
Cdd:PLN00113  120 LRYLNLSNNNFT---GSIPrgSIPNLETL-DLSNNMLSGEIPNDIGSFSSLKVLDLggnvlvgkipnsltnltslefltl 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127  101 SHNQLT-ECPRELENAKNMLVLNLSHNSID-TIPNQLFiNLTDLLYLDLSENRLE-SLPPQMRRLVHLQTLVLNGNPLLH 177
Cdd:PLN00113  196 ASNQLVgQIPRELGQMKSLKWIYLGYNNLSgEIPYEIG-GLTSLNHLDLVYNNLTgPIPSSLGNLKNLQYLFLYQNKLSG 274

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127  178 AQLRQLPAMTALQTLHLrSTQRTQSNLPTSLEGLSNLADVDLSCNDLT-RVPECLYTLPSLRRLNLSSNQIT-ELSLCID 255
Cdd:PLN00113  275 PIPPSIFSLQKLISLDL-SDNSLSGEIPELVIQLQNLEILHLFSNNFTgKIPVALTSLPRLQVLQLWSNKFSgEIPKNLG 353

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127  256 QWVHVETLNLSRNQLTS-LPSAICKLsklkklylnsnkldfdglpsgiGKLTNLEEFmaaNNNLE-LVPESLCRCPKLRK 333
Cdd:PLN00113  354 KHNNLTVLDLSTNNLTGeIPEGLCSS----------------------GNLFKLILF---SNSLEgEIPKSLGACRSLRR 408

                         330       340       350
                  ....*....|....*....|....*....|
gi 372266127  334 LVLNKNHLV-TLPEAIHFLTEIEVLDVREN 362
Cdd:PLN00113  409 VRLQDNSFSgELPSEFTKLPLVYFLDISNN 438
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1046-1138 4.77e-16

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 74.64  E-value: 4.77e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127   1046 YQIRTNGSaLCTRCIQINTDSSLLNSEFCFILkvpfeseDNQGIVYAWVGRASDPDEAKLAEDILNTMFDTSYSK----Q 1121
Cdd:smart00262    1 FLVRVKGK-RNVRVPEVPFSQGSLNSGDCYIL-------DTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGpvqvR 72

                            90
                    ....*....|....*..
gi 372266127   1122 VINEGEEPENFFWVGIG 1138
Cdd:smart00262   73 VVDEGKEPPEFWSLFGG 89
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 92-274 4.21e-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: 75.59  E-value: 4.21e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127   92 LDDLSVLDLSHNQLTECPrELENAKNMLVLNLSHNSIDTIPNqlFINLTDLLYLDLSENRLESLPPqMRRLVHLQTLVLN 171
Cdd:cd21340     1 LKRITHLYLNDKNITKID-NLSLCKNLKVLYLYDNKITKIEN--LEFLTNLTHLYLQNNQIEKIEN-LENLVNLKKLYLG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127  172 GNPLlhAQLRQLPAMTALQTLHLrSTQRTQSNL-----PTSLEGLSN-LADVDLSCNDLTRVpECLYTLPSLRRLNLSSN 245
Cdd:cd21340    77 GNRI--SVVEGLENLTNLEELHI-ENQRLPPGEkltfdPRSLAALSNsLRVLNISGNNIDSL-EPLAPLRNLEQLDASNN 152

                         170       180       190
                  ....*....|....*....|....*....|..
gi 372266127  246 QIT---ELSLCIDQWVHVETLNLSRNQLTSLP 274
Cdd:cd21340   153 QISdleELLDLLSSWPSLRELDLTGNPVCKKP 184
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 607-696 4.92e-15

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


Pssm-ID: 200445  Cd Length: 92  Bit Score: 71.50  E-value: 4.92e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127  607 VTRMYRVYGKKNIKLEPVPLKGTSLDPRFVFLLDRGLDIYVWRGAQATLSSTTKARLFAEKINKNERKGKAEITLLVQG- 685
Cdd:cd11289     1 KPRLLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKVIVLDEGd 80

                          90
                  ....*....|..
gi 372266127  686 -QELPEFWEALG 696
Cdd:cd11289    81 tNESPEFWKVLG 92
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
138-363 1.61e-14

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 77.28  E-value: 1.61e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127  138 NLTDLLYLDLSENRLESLPPQMRRLVHLQTLVLNGNPLLHAQLRQLPAMTALQTLHLRSTQRTQSNLPTSLEGLSNLADV 217
Cdd:COG4886     1 LLLLLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127  218 DLSCNDLTrvPECLYTLPSLRRLNLSSNQItelslcIDQWVHVETLNLSRNQLTSLPSAIcklsklkklylnsnkldfdg 297
Cdd:COG4886    81 LLSLLLLG--LTDLGDLTNLTELDLSGNEE------LSNLTNLESLDLSGNQLTDLPEEL-------------------- 132

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 372266127  298 lpsgiGKLTNLEEFMAANNNLELVPESLCRCPKLRKLVLNKNHLVTLPEAIHFLTEIEVLDVRENP 363
Cdd:COG4886   133 -----ANLTNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQ 193
Gelsolin pfam00626
Gelsolin repeat;
617-692 2.27e-14

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 69.26  E-value: 2.27e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 372266127   617 KNIKLEPVPLKGTSLDPRFVFLLDRGLDIYVWRGAQATLSSTTKARLFAEKINKNERKGKAEITLLVQGQELPEFW 692
Cdd:pfam00626    1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDERFPLPEVIRVPQGKEPARFL 76
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 89-341 5.03e-14

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 77.20  E-value: 5.03e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127   89 IFKLDDLSVLDLSHNQLT-ECPREL-ENAKNMLVLNLSHNSID-TIPNQLFINLTDllyLDLSENRLE-SLPPQMRRLVH 164
Cdd:PLN00113   89 IFRLPYIQTINLSNNQLSgPIPDDIfTTSSSLRYLNLSNNNFTgSIPRGSIPNLET---LDLSNNMLSgEIPNDIGSFSS 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127  165 LQTLVLNGNPLLHAQLRQLPAMTALQTLHLRSTQRT-------------------QSNL----PTSLEGLSNLADVDLSC 221
Cdd:PLN00113  166 LKVLDLGGNVLVGKIPNSLTNLTSLEFLTLASNQLVgqiprelgqmkslkwiylgYNNLsgeiPYEIGGLTSLNHLDLVY 245

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127  222 NDLT-------------------------RVPECLYTLPSLRRLNLSSNQIT-ELSLCIDQWVHVETLNLSRNQLT-SLP 274
Cdd:PLN00113  246 NNLTgpipsslgnlknlqylflyqnklsgPIPPSIFSLQKLISLDLSDNSLSgEIPELVIQLQNLEILHLFSNNFTgKIP 325

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 372266127  275 SAICKLSKLKKLYLNSNKLDfDGLPSGIGKLTNLEEFMAANNNLE-LVPESLCRCPKLRKLVLNKNHL 341
Cdd:PLN00113  326 VALTSLPRLQVLQLWSNKFS-GEIPKNLGKHNNLTVLDLSTNNLTgEIPEGLCSSGNLFKLILFSNSL 392
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
180-368 1.22e-13

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 75.89  E-value: 1.22e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127  180 LRQLPAMTALQTLHLRSTQRTQSNLPTSLEGlsNLADVDLSCNDLTRVPEclyTLP-SLRRLNLSSNQITELSLCIDQwv 258
Cdd:PRK15370  190 LTTIPACIPEQITTLILDNNELKSLPENLQG--NIKTLYANSNQLTSIPA---TLPdTIQEMELSINRITELPERLPS-- 262

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127  259 HVETLNLSRNQLTSLPSAICKLSKLKKLYLNSNKLDFDGLPSGIgkltnlEEFMAANNNLELVPESLcrCPKLRKLVLNK 338
Cdd:PRK15370  263 ALQSLDLFHNKISCLPENLPEELRYLSVYDNSIRTLPAHLPSGI------THLNVQSNSLTALPETL--PPGLKTLEAGE 334

                         170       180       190
                  ....*....|....*....|....*....|
gi 372266127  339 NHLVTLPEAIHflTEIEVLDVRENPNLVMP 368
Cdd:PRK15370  335 NALTSLPASLP--PELQVLDVSKNQITVLP 362
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
116-440 8.05e-13

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 73.19  E-value: 8.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127  116 KNMLVLNLSHNSIDTIPNQLFINLTDLLyldLSENRLESLPPQMRrlVHLQTLVLNGNpllhaQLRQLPAmtalqtlhlr 195
Cdd:PRK15370  178 NNKTELRLKILGLTTIPACIPEQITTLI---LDNNELKSLPENLQ--GNIKTLYANSN-----QLTSIPA---------- 237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127  196 stqrtqsNLPTSLEglsnlaDVDLSCNDLTRVPEclyTLPS-LRRLNLSSNQITELSLCIDQwvHVETLNLSRNQLTSLP 274
Cdd:PRK15370  238 -------TLPDTIQ------EMELSINRITELPE---RLPSaLQSLDLFHNKISCLPENLPE--ELRYLSVYDNSIRTLP 299

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127  275 SAICKLSKLKKLYLNSnkLDFdgLPSGIGklTNLEEFMAANNNLELVPESLCrcPKLRKLVLNKNHLVTLPEAIHflTEI 354
Cdd:PRK15370  300 AHLPSGITHLNVQSNS--LTA--LPETLP--PGLKTLEAGENALTSLPASLP--PELQVLDVSKNQITVLPETLP--PTI 369

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127  355 EVLDVRENP--NLvmppkPADRAAEWYNIDFSLQNQLRLAgaspatVAAAAAAGSGPK--------DPMA-RKMRLRRRK 423
Cdd:PRK15370  370 TTLDVSRNAltNL-----PENLPAALQIMQASRNNLVRLP------ESLPHFRGEGPQptriiveyNPFSeRTIQNMQRL 438

                         330
                  ....*....|....*..
gi 372266127  424 DSAQDDQAKQVLKGMSD 440
Cdd:PRK15370  439 MSSVGYQGPRVLFAMGD 455
Gelsolin pfam00626
Gelsolin repeat;
497-580 1.63e-12

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 63.87  E-value: 1.63e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127   497 NFVPVLVEEAFHGKFYEADCYIVLKTFlddsgslnwEIYYWIGGEATLDKKACSAIHAVNLR-NYLGAECRTVREEMGDE 575
Cdd:pfam00626    1 KFVLPPPVPLSQESLNSGDCYLLDNGF---------TIFLWVGKGSSLLEKLFAALLAAQLDdDERFPLPEVIRVPQGKE 71


                   ....*
gi 372266127   576 SEEFL 580
Cdd:pfam00626   72 PARFL 76
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 1153-1253 2.47e-11

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


Pssm-ID: 200436  Cd Length: 88  Bit Score: 60.84  E-value: 2.47e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127 1153 TRLFRCSNEK-GYFAVTEKCSDfcqdDLADDDIMLLDNGQEVYMWVGTQTSQVEiklsLKACQVYIQHMRSKEHERPRRL 1231
Cdd:cd11280     2 PRLYRVRGSKaIEIEEVPLASS----SLDSDDVFVLDTGSEIYIWQGRASSQAE----LAAAALLAKELDEERKGKPEIV 73

                          90       100
                  ....*....|....*....|..
gi 372266127 1232 RlVRKGNEQHAFtrcfhaWSAF 1253
Cdd:cd11280    74 R-IRQGQEPREF------WSLF 88
LRR_8 pfam13855
Leucine rich repeat;
120-175 3.40e-11

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 59.85  E-value: 3.40e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 372266127   120 VLNLSHNSIDTIPNQLFINLTDLLYLDLSENRLESLPPQM-RRLVHLQTLVLNGNPL 175
Cdd:pfam13855    5 SLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAfSGLPSLRYLDLSGNRL 61
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 608-697 8.51e-11

Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; Gelsolin repeats occur in gelsolin, severin, villin, advillin, villidin, supervillin, flightless, quail, fragmin, and other proteins, usually in several copies. They co-occur with villin headpiece domains, leucine-rich repeats, and several other domains. These gelsolin-related actin binding proteins (GRABPs) play regulatory roles in the assembly and disassembly of actin filaments; they are involved in F-actin capping, uncapping, severing, or the nucleation of actin filaments. Severing of actin filaments is Ca2+ dependent. Villins are also linked to generating bundles of F-actin with uniform filament polarity, which is most likely mediated by their extra villin headpiece domain. Many family members have also adopted functions in the nucleus, including the regulation of transcription. Supervillin, gelsolin, and flightless I are involved in intracellular signaling via nuclear hormone receptors. The gelsolin-like domain is distantly related to the actin depolymerizing domains found in cofilin and similar proteins.


Pssm-ID: 200444  Cd Length: 92  Bit Score: 59.55  E-value: 8.51e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127  608 TRMYRVYG--KKNIKLEPVPLKGTSLDPRFVFLLDRGLDIYVWRGAQATLSSTTKARLFAEKInknerKGKAEITLLVQG 685
Cdd:cd11288     3 TRLFQVRGngSGNTRAVEVDADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVASFL-----KPKASLQEVAEG 77

                          90
                  ....*....|..
gi 372266127  686 QELPEFWEALGG 697
Cdd:cd11288    78 SEPDEFWEALGG 89
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 39-177 2.33e-10

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


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 61.73  E-value: 2.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127   39 EELAALQKLEHLSVSHNNLTTLHGeLSSLPSLRAIVARANSLKnsgVPDDIFKLDDLSVLDLSHNQLT--EC----PREL 112
Cdd:cd21340    40 ENLEFLTNLTHLYLQNNQIEKIEN-LENLVNLKKLYLGGNRIS---VVEGLENLTNLEELHIENQRLPpgEKltfdPRSL 115

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 372266127  113 EN-AKNMLVLNLSHNSIDTIpNQLFiNLTDLLYLDLSENRLESLPPQ---MRRLVHLQTLVLNGNPLLH 177
Cdd:cd21340   116 AAlSNSLRVLNISGNNIDSL-EPLA-PLRNLEQLDASNNQISDLEELldlLSSWPSLRELDLTGNPVCK 182
PRK15387 PRK15387
type III secretion system effector E3 ubiquitin transferase SspH2;
120-363 3.81e-10

type III secretion system effector E3 ubiquitin transferase SspH2;


Pssm-ID: 185285 [Multi-domain]  Cd Length: 788  Bit Score: 64.41  E-value: 3.81e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127  120 VLNLSHNSIDTIPNQLFINLTDLLYLDLSENRLESLPPQMRrlvhlqTLVLNGNpllhaQLRQLPAMTAlQTLHLRSTQR 199
Cdd:PRK15387  205 VLNVGESGLTTLPDCLPAHITTLVIPDNNLTSLPALPPELR------TLEVSGN-----QLTSLPVLPP-GLLELSIFSN 272

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127  200 TQSNLPTSLEGLSNLAdvdLSCNDLTRVPeclYTLPSLRRLNLSSNQITEL-----SLCiDQWVH-------------VE 261
Cdd:PRK15387  273 PLTHLPALPSGLCKLW---IFGNQLTSLP---VLPPGLQELSVSDNQLASLpalpsELC-KLWAYnnqltslptlpsgLQ 345

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127  262 TLNLSRNQLTSLPSaiCKLSKLKKLYLNSNKLDFDGLPSGIGKL--------------TNLEEFMAANNNLELVPeslcR 327
Cdd:PRK15387  346 ELSVSDNQLASLPT--LPSELYKLWAYNNRLTSLPALPSGLKELivsgnrltslpvlpSELKELMVSGNRLTSLP----M 419

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 372266127  328 CPK-LRKLVLNKNHLVTLPEAIHFLTEIEVLDVRENP 363
Cdd:PRK15387  420 LPSgLLSLSVYRNQLTRLPESLIHLSSETTVNLEGNP 456
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 492-583 5.03e-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: 5.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127  492 IWQIENFVPVLVEE--AFHGKFYEADCYIVlktfldDSGSlnwEIYYWIGGEATLDKKACSAIHAVNLRNYLGAECRTVR 569
Cdd:cd11280     4 LYRVRGSKAIEIEEvpLASSSLDSDDVFVL------DTGS---EIYIWQGRASSQAELAAAALLAKELDEERKGKPEIVR 74

                          90
                  ....*....|....
gi 372266127  570 EEMGDESEEFLQVF 583
Cdd:cd11280    75 IRQGQEPREFWSLF 88
LRR_8 pfam13855
Leucine rich repeat;
95-152 4.48e-09

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 53.68  E-value: 4.48e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 372266127    95 LSVLDLSHNQLTECPRE-LENAKNMLVLNLSHNSIDTIPNQLFINLTDLLYLDLSENRL 152
Cdd:pfam13855    3 LRSLDLSNNRLTSLDDGaFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 1153-1247 1.18e-08

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


Pssm-ID: 200448  Cd Length: 98  Bit Score: 53.79  E-value: 1.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127 1153 TRLFRCSNEKGYFAVTE-KCSDFCQDDLADDDIMLLDNGQEVYMWVGTQTSQVEIKLSLKACQVYIQhmrskEHERPRRL 1231
Cdd:cd11292     4 KKLYKVSDASGKLKLTEvAEGSLNQEMLDSEDCYILDCGSEIFVWVGKGASLDERKAALKNAEEFLR-----KKKRPPYT 78

                          90
                  ....*....|....*...
gi 372266127 1232 RLVR--KGNEQHAFTRCF 1247
Cdd:cd11292    79 QVTRvtEGGESALFKSKF 96
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 78-363 1.45e-08

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: 57.75  E-value: 1.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127   78 NSLKNSGVPDDIFKLDDLSVLDLSHNQLTE-----CPRELENAKNMLVLNLSHNSIDTIPNQL------FINLTDLLYLD 146
Cdd:cd00116     8 ELLKTERATELLPKLLCLQVLRLEGNTLGEeaakaLASALRPQPSLKELCLSLNETGRIPRGLqsllqgLTKGCGLQELD 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127  147 LSEN--------RLESLppqmRRLVHLQTLVLNGNPLLHAQLRQLpaMTALQ--TLHLRSTQRTQSNL-PTSLEGLSN-- 213
Cdd:cd00116    88 LSDNalgpdgcgVLESL----LRSSSLQELKLNNNGLGDRGLRLL--AKGLKdlPPALEKLVLGRNRLeGASCEALAKal 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127  214 -----LADVDLSCNDL-----TRVPECLYTLPSLRRLNLSSNQITE-----LSLCIDQWVHVETLNLSRNQLTSLP-SAI 277
Cdd:cd00116   162 ranrdLKELNLANNGIgdagiRALAEGLKANCNLEVLDLNNNGLTDegasaLAETLASLKSLEVLNLGDNNLTDAGaAAL 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127  278 CklsklkklylnsnkldfDGLPSGIGKLTNLEefmAANNNLELVP-ESLCRC----PKLRKLVLNKNHLVTLPEAIHFLT 352
Cdd:cd00116   242 A-----------------SALLSPNISLLTLS---LSCNDITDDGaKDLAEVlaekESLLELDLRGNKFGEEGAQLLAES 301

                         330
                  ....*....|....*..
gi 372266127  353 ------EIEVLDVRENP 363
Cdd:cd00116   302 llepgnELESLWVKDDS 318
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 607-691 4.36e-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: 52.25  E-value: 4.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127  607 VTRMYRVY-GKKNIKLEPV---PLKGTSLDPRFVFLLDRGLDIYVWRGAQATLSSTTKARLFAEK-INKNERKGKAEITL 681
Cdd:cd11292     3 QKKLYKVSdASGKLKLTEVaegSLNQEMLDSEDCYILDCGSEIFVWVGKGASLDERKAALKNAEEfLRKKKRPPYTQVTR 82

                          90
                  ....*....|
gi 372266127  682 LVQGQELPEF 691
Cdd:cd11292    83 VTEGGESALF 92
LRR_8 pfam13855
Leucine rich repeat;
212-270 7.37e-08

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 50.22  E-value: 7.37e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 372266127   212 SNLADVDLSCNDLTRV-PECLYTLPSLRRLNLSSNQITELSL-CIDQWVHVETLNLSRNQL 270
Cdd:pfam13855    1 PNLRSLDLSNNRLTSLdDGAFKGLSNLKVLDLSNNLLTTLSPgAFSGLPSLRYLDLSGNRL 61
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 1040-1132 7.68e-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: 51.48  E-value: 7.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127 1040 AQQPSLYQIRTNGSALCTRCIQINT-DSSLLNSEFCFILkvpfeseDNQGIVYAWVGRASDPDEAK----LAEDILNTMF 1114
Cdd:cd11292     1 AEQKKLYKVSDASGKLKLTEVAEGSlNQEMLDSEDCYIL-------DCGSEIFVWVGKGASLDERKaalkNAEEFLRKKK 73

                          90
                  ....*....|....*....
gi 372266127 1115 DTSYSK-QVINEGEEPENF 1132
Cdd:cd11292    74 RPPYTQvTRVTEGGESALF 92
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 757-824 1.19e-07

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


Pssm-ID: 200436  Cd Length: 88  Bit Score: 50.44  E-value: 1.19e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 372266127  757 SLLDTRCVYILDCWSDVFIWLGRKSPRLVRAAALKLGQELcgmLHRPRHAT-VSRSLEGTEAQVFKAKF 824
Cdd:cd11280    23 SSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKEL---DEERKGKPeIVRIRQGQEPREFWSLF 88
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 756-828 1.26e-07

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


Pssm-ID: 200447 [Multi-domain]  Cd Length: 99  Bit Score: 50.76  E-value: 1.26e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 372266127  756 QSLLDTRCVYILDCWSDVFIWLGRKSPRLVRAAALKLGQ---ELCGMLHRPRHATVSRSLEGTEAQVFKAKFKNWD 828
Cdd:cd11291    24 QDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKkyiETDPLGRSKPRTPIYLVKQGNEPPTFTGYFHAWD 99
Gelsolin pfam00626
Gelsolin repeat;
1170-1243 1.81e-07

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 49.61  E-value: 1.81e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 372266127  1170 KCSDFCQDDLADDDIMLLDNGQEVYMWVGTQTSQVEIklslKACQVYIQHMRSKEHERPRRLRLVRKGNEQHAF 1243
Cdd:pfam00626    6 PPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEK----LFAALLAAQLDDDERFPLPEVIRVPQGKEPARF 75
PRK15387 PRK15387
type III secretion system effector E3 ubiquitin transferase SspH2;
27-277 2.53e-07

type III secretion system effector E3 ubiquitin transferase SspH2;


Pssm-ID: 185285 [Multi-domain]  Cd Length: 788  Bit Score: 55.17  E-value: 2.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127   27 LKLNRTGLCYLPEELAAlqKLEHLSVSHNNLTTLHgelSSLPSLRAIVARANSLKNSGV-PDDIFKLDDLSvldlshNQL 105
Cdd:PRK15387  206 LNVGESGLTTLPDCLPA--HITTLVIPDNNLTSLP---ALPPELRTLEVSGNQLTSLPVlPPGLLELSIFS------NPL 274

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127  106 TECPRELENAKNMLVLNLSHNSIDTIPnqlfinlTDLLYLDLSENRLESLPPQMRRLVHLQTLvlngnpllHAQLRQLPA 185
Cdd:PRK15387  275 THLPALPSGLCKLWIFGNQLTSLPVLP-------PGLQELSVSDNQLASLPALPSELCKLWAY--------NNQLTSLPT 339

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127  186 M-TALQTLHLRSTQRTQ--------------SNLPTSLEGL-SNLADVDLSCNDLTRVPeclyTLPS-LRRLNLSSNQIT 248
Cdd:PRK15387  340 LpSGLQELSVSDNQLASlptlpselyklwayNNRLTSLPALpSGLKELIVSGNRLTSLP----VLPSeLKELMVSGNRLT 415

                         250       260
                  ....*....|....*....|....*....
gi 372266127  249 ELSLCIDQWVhveTLNLSRNQLTSLPSAI 277
Cdd:PRK15387  416 SLPMLPSGLL---SLSVYRNQLTRLPESL 441
Gelsolin pfam00626
Gelsolin repeat;
745-821 4.58e-06

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 45.76  E-value: 4.58e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 372266127   745 KVELMPRMRLLQSLLDTRCVYILDCWSDVFIWLGRKSPRLVRAAALKLGQELcGMLHRPRHATVSRSLEGTEAQVFK 821
Cdd:pfam00626    1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQL-DDDERFPLPEVIRVPQGKEPARFL 76
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 1042-1134 6.47e-06

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


Pssm-ID: 200436  Cd Length: 88  Bit Score: 45.44  E-value: 6.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127 1042 QPSLYQIRTNGSalcTRCIQINTDSSLLNSEFCFILkvpfeseDNQGIVYAWVGRASDPDE----AKLAEDILNTMFDTS 1117
Cdd:cd11280     1 PPRLYRVRGSKA---IEIEEVPLASSSLDSDDVFVL-------DTGSEIYIWQGRASSQAElaaaALLAKELDEERKGKP 70

                          90
                  ....*....|....*..
gi 372266127 1118 YSkQVINEGEEPEnFFW 1134
Cdd:cd11280    71 EI-VRIRQGQEPR-EFW 85
LRR_8 pfam13855
Leucine rich repeat;
164-247 8.90e-06

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 44.44  E-value: 8.90e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127   164 HLQTLVLNGNPLLHAQlrqlpamtalqtlhlrstqrtqsnlPTSLEGLSNLADVDLSCNDLTRV-PECLYTLPSLRRLNL 242
Cdd:pfam13855    2 NLRSLDLSNNRLTSLD-------------------------DGAFKGLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDL 56


                   ....*
gi 372266127   243 SSNQI 247
Cdd:pfam13855   57 SGNRL 61
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 63-271 9.05e-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: 49.28  E-value: 9.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127   63 ELSSLPSLRAIVARANSLKNSGVPDDIFKLD---DLSVLDLSHNQLTECPRELENAKNMLV-------LNLSHNSIDTIP 132
Cdd:cd00116    18 LLPKLLCLQVLRLEGNTLGEEAAKALASALRpqpSLKELCLSLNETGRIPRGLQSLLQGLTkgcglqeLDLSDNALGPDG 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127  133 NQLFINLT---DLLYLDLSENRLESLPPQM--RRLVHLQ----TLVLNGNPLLHAQLRQ----LPAMTALQTLHLRSTQR 199
Cdd:cd00116    98 CGVLESLLrssSLQELKLNNNGLGDRGLRLlaKGLKDLPpaleKLVLGRNRLEGASCEAlakaLRANRDLKELNLANNGI 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127  200 TQSNLPTSLEGL---SNLADVDLSCNDLTR-----VPECLYTLPSLRRLNLSSNQITELSLC------IDQWVHVETLNL 265
Cdd:cd00116   178 GDAGIRALAEGLkanCNLEVLDLNNNGLTDegasaLAETLASLKSLEVLNLGDNNLTDAGAAalasalLSPNISLLTLSL 257


                  ....*.
gi 372266127  266 SRNQLT 271
Cdd:cd00116   258 SCNDIT 263
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 64-271 1.10e-05

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


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 49.40  E-value: 1.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127   64 LSSLPSLRAIVARANSLKNSGVPDdIFK----LDDLSVLDLSHNQLT-----ECPRELENAKNMLVLNLSHNSIDtipnq 134
Cdd:COG5238   204 LTQNTTVTTLWLKRNPIGDEGAEI-LAEalkgNKSLTTLDLSNNQIGdegviALAEALKNNTTVETLYLSGNQIG----- 277

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127  135 lfinltdllyldlsENRLESLPPQMRRLVHLQTLVLNGNPL----LHAQLRQLPAMTALQTLHLRSTQRTQSN---LPTS 207
Cdd:COG5238   278 --------------AEGAIALAKALQGNTTLTSLDLSVNRIgdegAIALAEGLQGNKTLHTLNLAYNGIGAQGaiaLAKA 343

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 372266127  208 LEGLSNLADVDLSCNDLT-----RVPECLYTLPSLRRLNLSSNQITEL-------SLCIDQwvhVETLNLSRNQLT 271
Cdd:COG5238   344 LQENTTLHSLDLSDNQIGdegaiALAKYLEGNTTLRELNLGKNNIGKQgaealidALQTNR---LHTLILDGNLIG 416
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 22-183 1.20e-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: 1.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127   22 TSLRWLKLNR------------TGLCYLPEELAALQkLEHLSVSHNNLTTLHGELSSLPSLRAIVARANSLKNSGVPD-- 87
Cdd:cd00116   108 SSLQELKLNNnglgdrglrllaKGLKDLPPALEKLV-LGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRAla 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127   88 DIFK-LDDLSVLDLSHNQLT--------ECPRELenaKNMLVLNLSHNSID-----TIPNQLFINLTDLLYLDLSENRLE 153
Cdd:cd00116   187 EGLKaNCNLEVLDLNNNGLTdegasalaETLASL---KSLEVLNLGDNNLTdagaaALASALLSPNISLLTLSLSCNDIT 263

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 372266127  154 -----SLPPQMRRLVHLQTLVLNGNPLLHAQLRQL 183
Cdd:cd00116   264 ddgakDLAEVLAEKESLLELDLRGNKFGEEGAQLL 298
Gelsolin pfam00626
Gelsolin repeat;
1065-1132 1.33e-05

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 44.22  E-value: 1.33e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 372266127  1065 DSSLLNSEFCFILkvpfeseDNQGIVYAWVGRASDPDE----AKLAEDILNTMFDTSYSKQVINEGEEPENF 1132
Cdd:pfam00626   11 SQESLNSGDCYLL-------DNGFTIFLWVGKGSSLLEklfaALLAAQLDDDERFPLPEVIRVPQGKEPARF 75
PRK15387 PRK15387
type III secretion system effector E3 ubiquitin transferase SspH2;
30-252 2.39e-05

type III secretion system effector E3 ubiquitin transferase SspH2;


Pssm-ID: 185285 [Multi-domain]  Cd Length: 788  Bit Score: 48.62  E-value: 2.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127   30 NRTGLCYLPEELAALQklehlsVSHNNLTTL-------------HGELSSLPSLRAIVARANSLKN--SGVPDDIFKLDD 94
Cdd:PRK15387  233 NLTSLPALPPELRTLE------VSGNQLTSLpvlppgllelsifSNPLTHLPALPSGLCKLWIFGNqlTSLPVLPPGLQE 306

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127   95 LSVLDlshNQLTECPRELENAKNMLVLNLSHNSIDTIPnqlfinlTDLLYLDLSENRLESLPPQMRRLVHLQTL--VLNG 172
Cdd:PRK15387  307 LSVSD---NQLASLPALPSELCKLWAYNNQLTSLPTLP-------SGLQELSVSDNQLASLPTLPSELYKLWAYnnRLTS 376

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127  173 NPLLHAQLRQLPA----MTALQTLHLRSTQRTQS-NLPTSLEGL-SNLADVDLSCNDLTRVPECLYTLPSLRRLNLSSNQ 246
Cdd:PRK15387  377 LPALPSGLKELIVsgnrLTSLPVLPSELKELMVSgNRLTSLPMLpSGLLSLSVYRNQLTRLPESLIHLSSETTVNLEGNP 456


                  ....*.
gi 372266127  247 ITELSL 252
Cdd:PRK15387  457 LSERTL 462
PLN03210 PLN03210
Resistant to P. syringae 6; Provisional
 141-390 9.80e-05

Resistant to P. syringae 6; Provisional


Pssm-ID: 215633 [Multi-domain]  Cd Length: 1153  Bit Score: 46.79  E-value: 9.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127  141 DLLYLDLSENRLESLPPQMRRLVHLQTLVLNGNpllhAQLRQLPAM---TALQTLHLRSTQrTQSNLPTSLEGLSNLADV 217
Cdd:PLN03210  612 NLVKLQMQGSKLEKLWDGVHSLTGLRNIDLRGS----KNLKEIPDLsmaTNLETLKLSDCS-SLVELPSSIQYLNKLEDL 686

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127  218 DLS-CNDLTRVPECLyTLPSLRRLNLSSnqITELSLCIDQWVHVETLNLSRNQLTSLPSAIcklsklkklylnsnkldfd 296
Cdd:PLN03210  687 DMSrCENLEILPTGI-NLKSLYRLNLSG--CSRLKSFPDISTNISWLDLDETAIEEFPSNL------------------- 744

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127  297 glpsgigKLTNLEEFMAANNNLE--------LVPESLCRCPKLRKLVLNKN-HLVTLPEAIHFLTEIEVLDVRENPNLVM 367
Cdd:PLN03210  745 -------RLENLDELILCEMKSEklwervqpLTPLMTMLSPSLTRLFLSDIpSLVELPSSIQNLHKLEHLEIENCINLET 817

                         250       260
                  ....*....|....*....|...
gi 372266127  368 PPKPADRAAeWYNIDFSLQNQLR 390
Cdd:PLN03210  818 LPTGINLES-LESLDLSGCSRLR 839
LRR_8 pfam13855
Leucine rich repeat;
22-80 1.04e-04

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 41.36  E-value: 1.04e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 372266127    22 TSLRWLKLNRTGLCYLPEE-LAALQKLEHLSVSHNNLTTLH-GELSSLPSLRAIVARANSL 80
Cdd:pfam13855    1 PNLRSLDLSNNRLTSLDDGaFKGLSNLKVLDLSNNLLTTLSpGAFSGLPSLRYLDLSGNRL 61
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 902-1024 1.99e-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: 1.99e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127    902 EGKKFARLPEEEF--GHFYTQDCYVFLCRYwvpveyeeeekkedkeekaegkegeeataeaeekqpeedfqcIVYFWQGR 979
Cdd:smart00262    6 KGKRNVRVPEVPFsqGSLNSGDCYILDTGS------------------------------------------EIYVWVGK 43

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*
gi 372266127    980 EASNMGWLTFTFSLQKKFESLFPGKLEVVRMTQQQENPKFLSHFK 1024
Cdd:smart00262   44 KSSQDEKKKAAELAVELDDTLGPGPVQVRVVDEGKEPPEFWSLFG 88
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 19-128 3.05e-04

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: 44.27  E-value: 3.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127   19 KAMTSLRWLKLNRTGLC-----YLPEELAALQKLEHLSVSHNNLT-----TLH-GELSSLPSLRAIVARANSLKNSGVPD 87
Cdd:cd00116   190 KANCNLEVLDLNNNGLTdegasALAETLASLKSLEVLNLGDNNLTdagaaALAsALLSPNISLLTLSLSCNDITDDGAKD 269

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 372266127   88 DIFKLDD---LSVLDLSHNQLTE------CPRELENAKNMLVLNLSHNSI 128
Cdd:cd00116   270 LAEVLAEkesLLELDLRGNKFGEegaqllAESLLEPGNELESLWVKDDSF 319
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 631-691 4.23e-04

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


Pssm-ID: 200447 [Multi-domain]  Cd Length: 99  Bit Score: 40.74  E-value: 4.23e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 372266127  631 LDPRFVFLLDRGLDIYVWRGAQAT----LSSTTKARLFAEKINKNERKGKAEITLLVQGQELPEF 691
Cdd:cd11291    27 LDTDDIMLLDTGDEVFVWVGSESSdeekKEALTSAKKYIETDPLGRSKPRTPIYLVKQGNEPPTF 91
PLN03150 PLN03150
hypothetical protein; Provisional
 79-175 6.00e-04

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 44.04  E-value: 6.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127   79 SLKNSG----VPDDIFKLddlsvldlshnqltecpRELENaknmlvLNLSHNSID-TIPNQLFiNLTDLLYLDLSENRLE 153
Cdd:PLN03150  424 GLDNQGlrgfIPNDISKL-----------------RHLQS------INLSGNSIRgNIPPSLG-SITSLEVLDLSYNSFN 479

                          90       100
                  ....*....|....*....|...
gi 372266127  154 -SLPPQMRRLVHLQTLVLNGNPL 175
Cdd:PLN03150  480 gSIPESLGQLTSLRILNLNGNSL 502
PLN03150 PLN03150
hypothetical protein; Provisional
 155-248 8.88e-04

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 43.65  E-value: 8.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127  155 LPPQMRRLVHLQTLVLNGNPLlhaqlrqlpamtalqtlhlrstqrtQSNLPTSLEGLSNLADVDLSCNDLT-RVPECLYT 233
Cdd:PLN03150  434 IPNDISKLRHLQSINLSGNSI-------------------------RGNIPPSLGSITSLEVLDLSYNSFNgSIPESLGQ 488

                          90
                  ....*....|....*
gi 372266127  234 LPSLRRLNLSSNQIT 248
Cdd:PLN03150  489 LTSLRILNLNGNSLS 503
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 235-274 1.16e-03

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


Pssm-ID: 463713 [Multi-domain]  Cd Length: 44  Bit Score: 38.00  E-value: 1.16e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 372266127   235 PSLRRLNLSSNQITELSLcIDQWVHVETLNLSRN-QLTSLP 274
Cdd:pfam12799    1 PNLEVLDLSNNQITDIPP-LAKLPNLETLDLSGNnKITDLS 40
PRK15387 PRK15387
type III secretion system effector E3 ubiquitin transferase SspH2;
47-188 1.25e-03

type III secretion system effector E3 ubiquitin transferase SspH2;


Pssm-ID: 185285 [Multi-domain]  Cd Length: 788  Bit Score: 43.23  E-value: 1.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127   47 LEHLSVSHNNLTTLHGELSSLPSLRAIVARANSLknSGVPDDifklddLSVLDLSHNQLTECPRELENAKNMLVlnlSHN 126
Cdd:PRK15387  344 LQELSVSDNQLASLPTLPSELYKLWAYNNRLTSL--PALPSG------LKELIVSGNRLTSLPVLPSELKELMV---SGN 412

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 372266127  127 SIDTIPnqlfINLTDLLYLDLSENRLESLPPQMRRLVHLQTLVLNGNPLLHAQLRQLPAMTA 188
Cdd:PRK15387  413 RLTSLP----MLPSGLLSLSVYRNQLTRLPESLIHLSSETTVNLEGNPLSERTLQALREITS 470
PLN03150 PLN03150
hypothetical protein; Provisional
 22-106 2.27e-03

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 42.11  E-value: 2.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127   22 TSLRW----LKLNRTGL-CYLPEELAALQKLEHLSVSHNNLttlHGELS----SLPSLRAIVARANSLkNSGVPDDIFKL 92
Cdd:PLN03150  414 TKGKWfidgLGLDNQGLrGFIPNDISKLRHLQSINLSGNSI---RGNIPpslgSITSLEVLDLSYNSF-NGSIPESLGQL 489

                          90
                  ....*....|....
gi 372266127   93 DDLSVLDLSHNQLT 106
Cdd:PLN03150  490 TSLRILNLNGNSLS 503
PRK15387 PRK15387
type III secretion system effector E3 ubiquitin transferase SspH2;
222-380 2.49e-03

type III secretion system effector E3 ubiquitin transferase SspH2;


Pssm-ID: 185285 [Multi-domain]  Cd Length: 788  Bit Score: 42.07  E-value: 2.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127  222 NDLTRVPEclyTLPSLRRLNLSSNQITELSLCIDQWVHVETLNLSRNQLTSLPSAICKLSKLkklylnSNKL-DFDGLPS 300
Cdd:PRK15387  232 NNLTSLPA---LPPELRTLEVSGNQLTSLPVLPPGLLELSIFSNPLTHLPALPSGLCKLWIF------GNQLtSLPVLPP 302

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127  301 GIGKLTNLEEFMAAnnnLELVPESLCrcpklrKLVLNKNHLVTLPEAIHFLTEIEVLDvreNPNLVMPPKPADRAAEW-Y 379
Cdd:PRK15387  303 GLQELSVSDNQLAS---LPALPSELC------KLWAYNNQLTSLPTLPSGLQELSVSD---NQLASLPTLPSELYKLWaY 370


                  .
gi 372266127  380 N 380
Cdd:PRK15387  371 N 371
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 1153-1247 2.67e-03

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


Pssm-ID: 200445  Cd Length: 92  Bit Score: 38.37  E-value: 2.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127 1153 TRLFRCSNEKgYFAVTEkcSDFCQDDLADDDIMLLDNGQEVYMWVGTQTSQVEIklsLKACQvYIQHMRSKEHERPRRLR 1232
Cdd:cd11289     2 PRLLHVKGRR-NVRARE--VELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEK---AKAMQ-LAQGIRDERRLGRAKVI 74

                          90
                  ....*....|....*..
gi 372266127 1233 LVR--KGNEQHAFTRCF 1247
Cdd:cd11289    75 VLDegDTNESPEFWKVL 91
LRR_8 pfam13855
Leucine rich repeat;
235-273 4.76e-03

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 36.73  E-value: 4.76e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 372266127   235 PSLRRLNLSSNQITELSlciDQW----VHVETLNLSRNQLTSL 273
Cdd:pfam13855    1 PNLRSLDLSNNRLTSLD---DGAfkglSNLKVLDLSNNLLTTL 40
LRR_8 pfam13855
Leucine rich repeat;
259-341 5.00e-03

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 36.73  E-value: 5.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127   259 HVETLNLSRNQLTSLPSAIcklsklkklylnsnkldFDGLPsgigkltNLEEFMAANNNLE-LVPESLCRCPKLRKLVLN 337
Cdd:pfam13855    2 NLRSLDLSNNRLTSLDDGA-----------------FKGLS-------NLKVLDLSNNLLTtLSPGAFSGLPSLRYLDLS 57


                   ....
gi 372266127   338 KNHL 341
Cdd:pfam13855   58 GNRL 61
PLN03210 PLN03210
Resistant to P. syringae 6; Provisional
 6-393 8.52e-03

Resistant to P. syringae 6; Provisional


Pssm-ID: 215633 [Multi-domain]  Cd Length: 1153  Bit Score: 40.63  E-value: 8.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127    6 LRPVPGGYFPENVKAMtSLRWLKLNRtgLCYLPEELAALQKLEhLSVSHN-----------NLTTLH-GELSSLPSLRAI 73
Cdd:PLN03210  601 LRCMPSNFRPENLVKL-QMQGSKLEK--LWDGVHSLTGLRNID-LRGSKNlkeipdlsmatNLETLKlSDCSSLVELPSS 676

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127   74 VARANSLKNSgvpdDIFKLDDLSVLDLSHN-------QLTECPRE---LENAKNMLVLNLSHNSIDTIPNQLfiNLTDLL 143
Cdd:PLN03210  677 IQYLNKLEDL----DMSRCENLEILPTGINlkslyrlNLSGCSRLksfPDISTNISWLDLDETAIEEFPSNL--RLENLD 750

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127  144 YLDLSENRLESLPPQMRRLVHLQTLVLngnpllhaqlrqlPAMTALqtlhLRSTQRTQSNLPTSLEGLSNLADVDL-SCN 222
Cdd:PLN03210  751 ELILCEMKSEKLWERVQPLTPLMTMLS-------------PSLTRL----FLSDIPSLVELPSSIQNLHKLEHLEIeNCI 813

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127  223 DLTRVPECLyTLPSLRRLNLSSnqITELSLCIDQWVHVETLNLSRNQLTSLPSAICklsklkklylnsnkldfdglpsgi 302
Cdd:PLN03210  814 NLETLPTGI-NLESLESLDLSG--CSRLRTFPDISTNISDLNLSRTGIEEVPWWIE------------------------ 866

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266127  303 gKLTNLEEF-MAANNNLELVPESLCRCPKLRKlvLNKNHLVTLPEAIHFLTEIEVLDVRENPNLVMPPKPADRAAEWYNI 381
Cdd:PLN03210  867 -KFSNLSFLdMNGCNNLQRVSLNISKLKHLET--VDFSDCGALTEASWNGSPSEVAMATDNIHSKLPSTVCINFINCFNL 943

                         410
                  ....*....|....*....
gi 372266127  382 DF-------SLQNQLRLAG 393
Cdd:PLN03210  944 DQeallqqqSIFKQLILSG 962
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH