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Conserved domains on  [gi|530410136|ref|XP_005256612|]
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protein flightless-1 homolog isoform X1 [Homo sapiens]

Protein Classification

flightless-1 family protein( domain architecture ID 11469395)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
gelsolin_S1_like cd11290
Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; ...
 492-604 1.78e-61

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


:

Pssm-ID: 200446  Cd Length: 113  Bit Score: 205.15  E-value: 1.78e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136  492 TEDVGQLPGLTIWQIENFVPVLVEEAFHGKFYEADCYIVLKTFLDDSGSLNWEIYYWIGGEATLDKKACSAIHAVNLRNY 571
Cdd:cd11290     1 FEGVGQKPGLQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDPSGSLSYDIHYWLGKEASQDEAGAAAIKAVELDDY 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 530410136  572 LGAECRTVREEMGDESEEFLQVFDNDISYIEGG 604
Cdd:cd11290    81 LGGRPVQHREVQGHESEEFLSYFKKGIIYIEGG 113
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 1163-1289 9.40e-43

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: 150.91  E-value: 9.40e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136 1163 HTRLFRCSNEKGYFaVTEKCSDFCQDDLADDDIMLLDNGQEVYMWVGTQTSQVEIKLSLKAcqviwveggprwacgqgrv 1242
Cdd:cd11291     1 KPRLFRCSNESGFF-KVEEISDFSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTS------------------- 60

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 530410136 1243 itqgslspCQVYIQHMRSKEHERPRRLRLVRKGNEQHAFTRCFHAWS 1289
Cdd:cd11291    61 --------AKKYIETDPLGRSKPRTPIYLVKQGNEPPTFTGYFHAWD 99
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
24-375 7.39e-40

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


:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 153.55  E-value: 7.39e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136   24 YFPENVKAMTSLRWLKLNRTglcylpEELAALQKLEHLSVSHNNLTTLHGELSSLPSLRAIVARANSLKNsgVPDDIFKL 103
Cdd:COG4886    87 LGLTDLGDLTNLTELDLSGN------EELSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTD--LPEPLGNL 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136  104 DDLSVLDLSHNQLTECPRELENAKNMLVLNLSHNSIDTIPNQLFiNLTDLLYLDLSENRLESLPPQMRRLVHLQTLVLNG 183
Cdd:COG4886   159 TNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLG-NLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSN 237

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136  184 NpllhaQLRQLPamtalqtlhlrstqrtqsnlptSLEGLSNLADVDLSCNDLTRVPEcLYTLPSLRRLNLSSNQITELSL 263
Cdd:COG4886   238 N-----QLTDLP----------------------ELGNLTNLEELDLSNNQLTDLPP-LANLTNLKTLDLSNNQLTDLKL 289

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136  264 cidqWVHVETLNLSRNQLTSLPSAICKLSKLKKLYLNSNKLDFDGLPSGIGKLTNLEEFMAANNNLELVPESLCRCPKLR 343
Cdd:COG4886   290 ----KELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTL 365

                         330       340       350
                  ....*....|....*....|....*....|..
gi 530410136  344 KLVLNKNHLVTLPEAIHFLTEIEVLDVRENPN 375
Cdd:COG4886   366 LLTLGLLGLLEATLLTLALLLLTLLLLLLTTT 397
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 1053-1152 4.80e-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: 4.80e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136 1053 QPSLYQIRTNGSaLCTRCIQINTDSSLLNSEFCFILKVPFesednqgIVYAWVGRASDPDEAKLAEDILNTMFDtSYSKQ 1132
Cdd:cd11288     2 PTRLFQVRGNGS-GNTRAVEVDADASSLNSNDVFVLKTPS-------SVYLWVGKGSSEDERELAKDVASFLKP-KASLQ 72

                          90       100
                  ....*....|....*....|
gi 530410136 1133 VINEGEEPENFFWVGIGAQK 1152
Cdd:cd11288    73 EVAEGSEPDEFWEALGGKSE 92
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 723-837 1.08e-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: 1.08e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136  723 PPQPKLYKVGLGLGYLELPQINYKLsvehkqrpkvelmprmrLLQSLLDTRCVYILDCWSDVFIWLGRKSPRLVRAAALK 802
Cdd:cd11292     1 AEQKKLYKVSDASGKLKLTEVAEGS-----------------LNQEMLDSEDCYILDCGSEIFVWVGKGASLDERKAALK 63

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 530410136  803 LGQELCGMLHRPRHATVSRSLEGTEAQVFKAKFKN 837
Cdd:cd11292    64 NAEEFLRKKKRPPYTQVTRVTEGGESALFKSKFAN 98
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 619-706 2.28e-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: 2.28e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136  619 TRMYRVYGKKNIKLEPVPLKGTSLDPRFVFLLDRGLDIYVWRGAQATLSSTTKARLFAEKINKnERKGKAEITLLVQGQE 698
Cdd:cd11280     2 PRLYRVRGSKAIEIEEVPLASSSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKELDE-ERKGKPEIVRIRQGQE 80


                  ....*...
gi 530410136  699 LPEFWEAL 706
Cdd:cd11280    81 PREFWSLF 88
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 974-1034 1.15e-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: 1.15e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530410136  974 KQPEEDFQCIVYFWQGReASNMGWLTFTFSLQKKFESLFPGKLEVVRMTQQQENPKFLSHF 1034
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; ...
 492-604 1.78e-61

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


Pssm-ID: 200446  Cd Length: 113  Bit Score: 205.15  E-value: 1.78e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136  492 TEDVGQLPGLTIWQIENFVPVLVEEAFHGKFYEADCYIVLKTFLDDSGSLNWEIYYWIGGEATLDKKACSAIHAVNLRNY 571
Cdd:cd11290     1 FEGVGQKPGLQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDPSGSLSYDIHYWLGKEASQDEAGAAAIKAVELDDY 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 530410136  572 LGAECRTVREEMGDESEEFLQVFDNDISYIEGG 604
Cdd:cd11290    81 LGGRPVQHREVQGHESEEFLSYFKKGIIYIEGG 113
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 1163-1289 9.40e-43

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: 150.91  E-value: 9.40e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136 1163 HTRLFRCSNEKGYFaVTEKCSDFCQDDLADDDIMLLDNGQEVYMWVGTQTSQVEIKLSLKAcqviwveggprwacgqgrv 1242
Cdd:cd11291     1 KPRLFRCSNESGFF-KVEEISDFSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTS------------------- 60

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 530410136 1243 itqgslspCQVYIQHMRSKEHERPRRLRLVRKGNEQHAFTRCFHAWS 1289
Cdd:cd11291    61 --------AKKYIETDPLGRSKPRTPIYLVKQGNEPPTFTGYFHAWD 99
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
24-375 7.39e-40

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 153.55  E-value: 7.39e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136   24 YFPENVKAMTSLRWLKLNRTglcylpEELAALQKLEHLSVSHNNLTTLHGELSSLPSLRAIVARANSLKNsgVPDDIFKL 103
Cdd:COG4886    87 LGLTDLGDLTNLTELDLSGN------EELSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTD--LPEPLGNL 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136  104 DDLSVLDLSHNQLTECPRELENAKNMLVLNLSHNSIDTIPNQLFiNLTDLLYLDLSENRLESLPPQMRRLVHLQTLVLNG 183
Cdd:COG4886   159 TNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLG-NLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSN 237

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136  184 NpllhaQLRQLPamtalqtlhlrstqrtqsnlptSLEGLSNLADVDLSCNDLTRVPEcLYTLPSLRRLNLSSNQITELSL 263
Cdd:COG4886   238 N-----QLTDLP----------------------ELGNLTNLEELDLSNNQLTDLPP-LANLTNLKTLDLSNNQLTDLKL 289

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136  264 cidqWVHVETLNLSRNQLTSLPSAICKLSKLKKLYLNSNKLDFDGLPSGIGKLTNLEEFMAANNNLELVPESLCRCPKLR 343
Cdd:COG4886   290 ----KELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTL 365

                         330       340       350
                  ....*....|....*....|....*....|..
gi 530410136  344 KLVLNKNHLVTLPEAIHFLTEIEVLDVRENPN 375
Cdd:COG4886   366 LLTLGLLGLLEATLLTLALLLLTLLLLLLTTT 397
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 1053-1152 4.80e-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: 4.80e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136 1053 QPSLYQIRTNGSaLCTRCIQINTDSSLLNSEFCFILKVPFesednqgIVYAWVGRASDPDEAKLAEDILNTMFDtSYSKQ 1132
Cdd:cd11288     2 PTRLFQVRGNGS-GNTRAVEVDADASSLNSNDVFVLKTPS-------SVYLWVGKGSSEDERELAKDVASFLKP-KASLQ 72

                          90       100
                  ....*....|....*....|
gi 530410136 1133 VINEGEEPENFFWVGIGAQK 1152
Cdd:cd11288    73 EVAEGSEPDEFWEALGGKSE 92
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 723-837 1.08e-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: 1.08e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136  723 PPQPKLYKVGLGLGYLELPQINYKLsvehkqrpkvelmprmrLLQSLLDTRCVYILDCWSDVFIWLGRKSPRLVRAAALK 802
Cdd:cd11292     1 AEQKKLYKVSDASGKLKLTEVAEGS-----------------LNQEMLDSEDCYILDCGSEIFVWVGKGASLDERKAALK 63

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 530410136  803 LGQELCGMLHRPRHATVSRSLEGTEAQVFKAKFKN 837
Cdd:cd11292    64 NAEEFLRKKKRPPYTQVTRVTEGGESALFKSKFAN 98
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 619-706 2.28e-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: 2.28e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136  619 TRMYRVYGKKNIKLEPVPLKGTSLDPRFVFLLDRGLDIYVWRGAQATLSSTTKARLFAEKINKnERKGKAEITLLVQGQE 698
Cdd:cd11280     2 PRLYRVRGSKAIEIEEVPLASSSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKELDE-ERKGKPEIVRIRQGQE 80


                  ....*...
gi 530410136  699 LPEFWEAL 706
Cdd:cd11280    81 PREFWSLF 88
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 7-373 3.81e-24

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 110.32  E-value: 3.81e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136    7 LPFVRGVDLSGNDFKGGyFPENV-KAMTSLRWLKL---NRTGlcylPEELAALQKLEHLSVSHNNLT-TLHGELSSLPSL 81
Cdd:PLN00113   92 LPYIQTINLSNNQLSGP-IPDDIfTTSSSLRYLNLsnnNFTG----SIPRGSIPNLETLDLSNNMLSgEIPNDIGSFSSL 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136   82 RAIVARANSLKNSgVPDDIFKLDDLSVLDLSHNQLT-ECPRELENAKNMLVLNLSHNSID-TIPNQLFiNLTDLLYLDLS 159
Cdd:PLN00113  167 KVLDLGGNVLVGK-IPNSLTNLTSLEFLTLASNQLVgQIPRELGQMKSLKWIYLGYNNLSgEIPYEIG-GLTSLNHLDLV 244

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136  160 ENRLE-SLPPQMRRLVHLQTLVLNGNPLLHAQLRQLPAMTALQTLHLrSTQRTQSNLPTSLEGLSNLADVDLSCNDLT-R 237
Cdd:PLN00113  245 YNNLTgPIPSSLGNLKNLQYLFLYQNKLSGPIPPSIFSLQKLISLDL-SDNSLSGEIPELVIQLQNLEILHLFSNNFTgK 323

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136  238 VPECLYTLPSLRRLNLSSNQIT-ELSLCIDQWVHVETLNLSRNQLTS-LPSAICKLsklkklylnsnkldfdglpsgiGK 315
Cdd:PLN00113  324 IPVALTSLPRLQVLQLWSNKFSgEIPKNLGKHNNLTVLDLSTNNLTGeIPEGLCSS----------------------GN 381

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136  316 LTNLEEFmaaNNNLE-LVPESLCRCPKLRKLVLNKNHLV-TLPEAIHFLTEIEVLDVREN 373
Cdd:PLN00113  382 LFKLILF---SNSLEgEIPKSLGACRSLRRVRLQDNSFSgELPSEFTKLPLVYFLDISNN 438
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 620-708 1.04e-23

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 96.21  E-value: 1.04e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136    620 RMYRVYGKKNIKLEPVPLKGTSLDPRFVFLLDRGLDIYVWRGAQATLSSTTKARLFAEKINKNERKGKAEITLLVQGQEL 699
Cdd:smart00262    1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVRVVDEGKEP 80


                    ....*....
gi 530410136    700 PEFWEALGG 708
Cdd:smart00262   81 PEFWSLFGG 89
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 974-1034 1.15e-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: 1.15e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530410136  974 KQPEEDFQCIVYFWQGReASNMGWLTFTFSLQKKFESLFPGKLEVVRMTQQQENPKFLSHF 1034
Cdd:cd11280    29 DVFVLDTGSEIYIWQGR-ASSQAELAAAALLAKELDEERKGKPEIVRIRQGQEPREFWSLF 88
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 751-838 2.28e-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: 2.28e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136    751 HKQRPKVELMPRMRLLQSLLDTRCVYILDCWSDVFIWLGRKSPRLVRAAALKLGQELCGMLHrPRHATVSRSLEGTEAQV 830
Cdd:smart00262    4 RVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLG-PGPVQVRVVDEGKEPPE 82


                    ....*...
gi 530410136    831 FKAKFKNW 838
Cdd:smart00262   83 FWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1168-1288 3.43e-18

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 80.80  E-value: 3.43e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136   1168 RCSNEKGYFAVTEKCSDFCQDDLADDDIMLLDNGQEVYMWVGTQTSQVEIKLSLKAcqviwveggprwacgqgrvitqgs 1247
Cdd:smart00262    1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAEL------------------------ 56

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|.
gi 530410136   1248 lspCQVYIQHMRSkeheRPRRLRLVRKGNEQHAFTRCFHAW 1288
Cdd:smart00262   57 ---AVELDDTLGP----GPVQVRVVDEGKEPPEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 503-596 5.06e-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: 80.03  E-value: 5.06e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136    503 IWQIENFVPVLVEE--AFHGKFYEADCYIVLKTflddsgslnWEIYYWIGGEATLDKKACSAIHAVNLRNYLGAECRTVR 580
Cdd:smart00262    2 LVRVKGKRNVRVPEvpFSQGSLNSGDCYILDTG---------SEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVR 72

                            90
                    ....*....|....*..
gi 530410136    581 E-EMGDESEEFLQVFDN 596
Cdd:smart00262   73 VvDEGKEPPEFWSLFGG 89
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1057-1149 5.75e-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: 74.25  E-value: 5.75e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136   1057 YQIRTNGSaLCTRCIQINTDSSLLNSEFCFILkvpfeseDNQGIVYAWVGRASDPDEAKLAEDILNTMFDTSYSK----Q 1132
Cdd:smart00262    1 FLVRVKGK-RNVRVPEVPFSQGSLNSGDCYIL-------DTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGpvqvR 72

                            90
                    ....*....|....*..
gi 530410136   1133 VINEGEEPENFFWVGIG 1149
Cdd:smart00262   73 VVDEGKEPPEFWSLFGG 89
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 103-285 2.42e-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: 76.36  E-value: 2.42e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136  103 LDDLSVLDLSHNQLTECPrELENAKNMLVLNLSHNSIDTIPNqlFINLTDLLYLDLSENRLESLPPqMRRLVHLQTLVLN 182
Cdd:cd21340     1 LKRITHLYLNDKNITKID-NLSLCKNLKVLYLYDNKITKIEN--LEFLTNLTHLYLQNNQIEKIEN-LENLVNLKKLYLG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136  183 GNPLlhAQLRQLPAMTALQTLHLrSTQRTQSNL-----PTSLEGLSN-LADVDLSCNDLTRVpECLYTLPSLRRLNLSSN 256
Cdd:cd21340    77 GNRI--SVVEGLENLTNLEELHI-ENQRLPPGEkltfdPRSLAALSNsLRVLNISGNNIDSL-EPLAPLRNLEQLDASNN 152

                         170       180       190
                  ....*....|....*....|....*....|..
gi 530410136  257 QIT---ELSLCIDQWVHVETLNLSRNQLTSLP 285
Cdd:cd21340   153 QISdleELLDLLSSWPSLRELDLTGNPVCKKP 184
Gelsolin pfam00626
Gelsolin repeat;
628-703 2.32e-14

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 69.26  E-value: 2.32e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530410136   628 KNIKLEPVPLKGTSLDPRFVFLLDRGLDIYVWRGAQATLSSTTKARLFAEKINKNERKGKAEITLLVQGQELPEFW 703
Cdd:pfam00626    1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDERFPLPEVIRVPQGKEPARFL 76
Gelsolin pfam00626
Gelsolin repeat;
508-591 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 530410136   508 NFVPVLVEEAFHGKFYEADCYIVLKTFlddsgslnwEIYYWIGGEATLDKKACSAIHAVNLR-NYLGAECRTVREEMGDE 586
Cdd:pfam00626    1 KFVLPPPVPLSQESLNSGDCYLLDNGF---------TIFLWVGKGSSLLEKLFAALLAAQLDdDERFPLPEVIRVPQGKE 71


                   ....*
gi 530410136   587 SEEFL 591
Cdd:pfam00626   72 PARFL 76
LRR_8 pfam13855
Leucine rich repeat;
131-186 2.42e-11

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 60.23  E-value: 2.42e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 530410136   131 VLNLSHNSIDTIPNQLFINLTDLLYLDLSENRLESLPPQM-RRLVHLQTLVLNGNPL 186
Cdd:pfam13855    5 SLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAfSGLPSLRYLDLSGNRL 61
Gelsolin pfam00626
Gelsolin repeat;
756-832 4.45e-06

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 45.76  E-value: 4.45e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530410136   756 KVELMPRMRLLQSLLDTRCVYILDCWSDVFIWLGRKSPRLVRAAALKLGQELcGMLHRPRHATVSRSLEGTEAQVFK 832
Cdd:pfam00626    1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQL-DDDERFPLPEVIRVPQGKEPARFL 76
Gelsolin pfam00626
Gelsolin repeat;
1181-1220 8.01e-06

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 44.99  E-value: 8.01e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 530410136  1181 KCSDFCQDDLADDDIMLLDNGQEVYMWVGTQTSQVEIKLS 1220
Cdd:pfam00626    6 PPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFA 45
Gelsolin pfam00626
Gelsolin repeat;
1076-1143 1.37e-05

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 44.22  E-value: 1.37e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530410136  1076 DSSLLNSEFCFILkvpfeseDNQGIVYAWVGRASDPDE----AKLAEDILNTMFDTSYSKQVINEGEEPENF 1143
Cdd:pfam00626   11 SQESLNSGDCYLL-------DNGFTIFLWVGKGSSLLEklfaALLAAQLDDDERFPLPEVIRVPQGKEPARF 75
 
Name Accession Description Interval E-value
gelsolin_S1_like cd11290
Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; ...
 492-604 1.78e-61

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


Pssm-ID: 200446  Cd Length: 113  Bit Score: 205.15  E-value: 1.78e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136  492 TEDVGQLPGLTIWQIENFVPVLVEEAFHGKFYEADCYIVLKTFLDDSGSLNWEIYYWIGGEATLDKKACSAIHAVNLRNY 571
Cdd:cd11290     1 FEGVGQKPGLQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDPSGSLSYDIHYWLGKEASQDEAGAAAIKAVELDDY 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 530410136  572 LGAECRTVREEMGDESEEFLQVFDNDISYIEGG 604
Cdd:cd11290    81 LGGRPVQHREVQGHESEEFLSYFKKGIIYIEGG 113
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 1163-1289 9.40e-43

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: 150.91  E-value: 9.40e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136 1163 HTRLFRCSNEKGYFaVTEKCSDFCQDDLADDDIMLLDNGQEVYMWVGTQTSQVEIKLSLKAcqviwveggprwacgqgrv 1242
Cdd:cd11291     1 KPRLFRCSNESGFF-KVEEISDFSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTS------------------- 60

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 530410136 1243 itqgslspCQVYIQHMRSKEHERPRRLRLVRKGNEQHAFTRCFHAWS 1289
Cdd:cd11291    61 --------AKKYIETDPLGRSKPRTPIYLVKQGNEPPTFTGYFHAWD 99
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
24-375 7.39e-40

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 153.55  E-value: 7.39e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136   24 YFPENVKAMTSLRWLKLNRTglcylpEELAALQKLEHLSVSHNNLTTLHGELSSLPSLRAIVARANSLKNsgVPDDIFKL 103
Cdd:COG4886    87 LGLTDLGDLTNLTELDLSGN------EELSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTD--LPEPLGNL 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136  104 DDLSVLDLSHNQLTECPRELENAKNMLVLNLSHNSIDTIPNQLFiNLTDLLYLDLSENRLESLPPQMRRLVHLQTLVLNG 183
Cdd:COG4886   159 TNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLG-NLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSN 237

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136  184 NpllhaQLRQLPamtalqtlhlrstqrtqsnlptSLEGLSNLADVDLSCNDLTRVPEcLYTLPSLRRLNLSSNQITELSL 263
Cdd:COG4886   238 N-----QLTDLP----------------------ELGNLTNLEELDLSNNQLTDLPP-LANLTNLKTLDLSNNQLTDLKL 289

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136  264 cidqWVHVETLNLSRNQLTSLPSAICKLSKLKKLYLNSNKLDFDGLPSGIGKLTNLEEFMAANNNLELVPESLCRCPKLR 343
Cdd:COG4886   290 ----KELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTL 365

                         330       340       350
                  ....*....|....*....|....*....|..
gi 530410136  344 KLVLNKNHLVTLPEAIHFLTEIEVLDVRENPN 375
Cdd:COG4886   366 LLTLGLLGLLEATLLTLALLLLTLLLLLLTTT 397
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
38-374 4.34e-39

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 151.24  E-value: 4.34e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136   38 LKLNRTGLCYLPEELAALQKLEHLSVSHNNLTTLHGELSSLPSLRAIVARANSLKNSGVPDDIFKLDDLSVLDLSHNQLT 117
Cdd:COG4886     4 LLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136  118 E---CPRELENAKNMLVLNLSHNsidtipnQLFINLTDLLYLDLSENRLESLPPQMRRLVHLQTLVLNGNPLlhaqlrql 194
Cdd:COG4886    84 LlllGLTDLGDLTNLTELDLSGN-------EELSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQL-------- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136  195 pamtalqtlhlrstqrtqSNLPTSLEGLSNLADVDLSCNDLTRVPECLYTLPSLRRLNLSSNQITELSLCIDQWVHVETL 274
Cdd:COG4886   149 ------------------TDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLEEL 210

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136  275 NLSRNQLTSLPSAicklsklkklylnsnkldfdglpsgIGKLTNLEEFMAANNNLELVPEsLCRCPKLRKLVLNKNHLVT 354
Cdd:COG4886   211 DLSGNQLTDLPEP-------------------------LANLTNLETLDLSNNQLTDLPE-LGNLTNLEELDLSNNQLTD 264

                         330       340
                  ....*....|....*....|
gi 530410136  355 LPEAIHfLTEIEVLDVRENP 374
Cdd:COG4886   265 LPPLAN-LTNLKTLDLSNNQ 283
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 1053-1152 4.80e-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: 4.80e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136 1053 QPSLYQIRTNGSaLCTRCIQINTDSSLLNSEFCFILKVPFesednqgIVYAWVGRASDPDEAKLAEDILNTMFDtSYSKQ 1132
Cdd:cd11288     2 PTRLFQVRGNGS-GNTRAVEVDADASSLNSNDVFVLKTPS-------SVYLWVGKGSSEDERELAKDVASFLKP-KASLQ 72

                          90       100
                  ....*....|....*....|
gi 530410136 1133 VINEGEEPENFFWVGIGAQK 1152
Cdd:cd11288    73 EVAEGSEPDEFWEALGGKSE 92
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 723-837 1.08e-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: 1.08e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136  723 PPQPKLYKVGLGLGYLELPQINYKLsvehkqrpkvelmprmrLLQSLLDTRCVYILDCWSDVFIWLGRKSPRLVRAAALK 802
Cdd:cd11292     1 AEQKKLYKVSDASGKLKLTEVAEGS-----------------LNQEMLDSEDCYILDCGSEIFVWVGKGASLDERKAALK 63

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 530410136  803 LGQELCGMLHRPRHATVSRSLEGTEAQVFKAKFKN 837
Cdd:cd11292    64 NAEEFLRKKKRPPYTQVTRVTEGGESALFKSKFAN 98
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
7-285 1.78e-31

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 128.90  E-value: 1.78e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136    7 LPFVRGVDLSGNDFKggYFPENVKAMTSLRWLKLNRTGLCYLPEELAALQKLEHLSVSHNNLTTLHGELSSLPSLRaiva 86
Cdd:COG4886   135 LTNLKELDLSNNQLT--DLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLE---- 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136   87 ranslknsgvpddifklddlsVLDLSHNQLTECPRELENAKNMLVLNLSHNSIDTIPNqlFINLTDLLYLDLSENRLESL 166
Cdd:COG4886   209 ---------------------ELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTDLPE--LGNLTNLEELDLSNNQLTDL 265

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136  167 PPQMrRLVHLQTLVLNGNPLLHAQLRQLPAMTALQTLHLRSTQRTQSNLPTSLEGLSNLADVDLSCNDLTRVPECLYT-L 245
Cdd:COG4886   266 PPLA-NLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALsL 344

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 530410136  246 PSLRRLNLSSNQITELSLCIDQWVHVETLNLSRNQLTSLP 285
Cdd:COG4886   345 SLLALLTLLLLLNLLSLLLTLLLTLGLLGLLEATLLTLAL 384
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 619-706 2.28e-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: 2.28e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136  619 TRMYRVYGKKNIKLEPVPLKGTSLDPRFVFLLDRGLDIYVWRGAQATLSSTTKARLFAEKINKnERKGKAEITLLVQGQE 698
Cdd:cd11280     2 PRLYRVRGSKAIEIEEVPLASSSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKELDE-ERKGKPEIVRIRQGQE 80


                  ....*...
gi 530410136  699 LPEFWEAL 706
Cdd:cd11280    81 PREFWSLF 88
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 7-373 3.81e-24

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 110.32  E-value: 3.81e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136    7 LPFVRGVDLSGNDFKGGyFPENV-KAMTSLRWLKL---NRTGlcylPEELAALQKLEHLSVSHNNLT-TLHGELSSLPSL 81
Cdd:PLN00113   92 LPYIQTINLSNNQLSGP-IPDDIfTTSSSLRYLNLsnnNFTG----SIPRGSIPNLETLDLSNNMLSgEIPNDIGSFSSL 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136   82 RAIVARANSLKNSgVPDDIFKLDDLSVLDLSHNQLT-ECPRELENAKNMLVLNLSHNSID-TIPNQLFiNLTDLLYLDLS 159
Cdd:PLN00113  167 KVLDLGGNVLVGK-IPNSLTNLTSLEFLTLASNQLVgQIPRELGQMKSLKWIYLGYNNLSgEIPYEIG-GLTSLNHLDLV 244

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136  160 ENRLE-SLPPQMRRLVHLQTLVLNGNPLLHAQLRQLPAMTALQTLHLrSTQRTQSNLPTSLEGLSNLADVDLSCNDLT-R 237
Cdd:PLN00113  245 YNNLTgPIPSSLGNLKNLQYLFLYQNKLSGPIPPSIFSLQKLISLDL-SDNSLSGEIPELVIQLQNLEILHLFSNNFTgK 323

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136  238 VPECLYTLPSLRRLNLSSNQIT-ELSLCIDQWVHVETLNLSRNQLTS-LPSAICKLsklkklylnsnkldfdglpsgiGK 315
Cdd:PLN00113  324 IPVALTSLPRLQVLQLWSNKFSgEIPKNLGKHNNLTVLDLSTNNLTGeIPEGLCSS----------------------GN 381

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136  316 LTNLEEFmaaNNNLE-LVPESLCRCPKLRKLVLNKNHLV-TLPEAIHFLTEIEVLDVREN 373
Cdd:PLN00113  382 LFKLILF---SNSLEgEIPKSLGACRSLRRVRLQDNSFSgELPSEFTKLPLVYFLDISNN 438
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 620-708 1.04e-23

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 96.21  E-value: 1.04e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136    620 RMYRVYGKKNIKLEPVPLKGTSLDPRFVFLLDRGLDIYVWRGAQATLSSTTKARLFAEKINKNERKGKAEITLLVQGQEL 699
Cdd:smart00262    1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVRVVDEGKEP 80


                    ....*....
gi 530410136    700 PEFWEALGG 708
Cdd:smart00262   81 PEFWSLFGG 89
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
13-286 1.08e-22

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 102.32  E-value: 1.08e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136   13 VDLSGNDFKGgyFPENVKAMTSLRWLKLNRTGLCYLPEELAALQKLEHLSVSHNNLTTLHGELSSLPSLRaivaranslk 92
Cdd:COG4886   164 LDLSNNQLTD--LPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLE---------- 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136   93 nsgvpddifklddlsVLDLSHNQLTECPrELENAKNMLVLNLSHNSIDTIPNQLfiNLTDLLYLDLSENRLESLppQMRR 172
Cdd:COG4886   232 ---------------TLDLSNNQLTDLP-ELGNLTNLEELDLSNNQLTDLPPLA--NLTNLKTLDLSNNQLTDL--KLKE 291

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136  173 LVHLQTLVLNGNPLLHAQLRqLPAMTALQTLHLRSTQRTQSNLPTSLEGLSNLADVDLSCNDLTRVPECLYTLPSLRRLN 252
Cdd:COG4886   292 LELLLGLNSLLLLLLLLNLL-ELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLG 370

                         250       260       270
                  ....*....|....*....|....*....|....
gi 530410136  253 LSSNQITELSLCIDQWVHVETLNLSRNQLTSLPS 286
Cdd:COG4886   371 LLGLLEATLLTLALLLLTLLLLLLTTTAGVLLLT 404
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 23-329 1.02e-20

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 99.15  E-value: 1.02e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136   23 GYFPENVKAMTSLRWLKLNRTGLC-YLPEELAALQKLEHLSVSHNNLT-TLHGELSSLPSLRAIVARANSLkNSGVPDDI 100
Cdd:PLN00113  274 GPIPPSIFSLQKLISLDLSDNSLSgEIPELVIQLQNLEILHLFSNNFTgKIPVALTSLPRLQVLQLWSNKF-SGEIPKNL 352

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136  101 FKLDDLSVLDLSHNQLT-ECPRELENAKNMLVLNLSHNSIDT-IPNQLFiNLTDLLYLDLSENRLE-SLPPQMRRLVHLQ 177
Cdd:PLN00113  353 GKHNNLTVLDLSTNNLTgEIPEGLCSSGNLFKLILFSNSLEGeIPKSLG-ACRSLRRVRLQDNSFSgELPSEFTKLPLVY 431

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136  178 TLVLNGNPLLHAQLRQLPAMTALQTLHLrSTQRTQSNLPTSLeGLSNLADVDLSCNDLT-RVPECLYTLPSLRRLNLSSN 256
Cdd:PLN00113  432 FLDISNNNLQGRINSRKWDMPSLQMLSL-ARNKFFGGLPDSF-GSKRLENLDLSRNQFSgAVPRKLGSLSELMQLKLSEN 509

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530410136  257 QIT-----ELSLCidqwVHVETLNLSRNQLT-SLPSAICKLSKLKKLYLNSNKLDFDgLPSGIGKLTNLEEFMAANNNL 329
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; ...
 501-594 2.26e-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: 2.26e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136  501 LTIWQIENFVPVLVEEAFHGKFYEADCYIVLKTFlDDSGSLNWEIYYWIGGEATLDKKACSAIHAVNLRNYLGAECRTVR 580
Cdd:cd11293     9 VEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYTY-QGGGKEEHILYFWQGRHSSQDERAAAALLTVELDEELKGRAVQVR 87

                          90
                  ....*....|....
gi 530410136  581 EEMGDESEEFLQVF 594
Cdd:cd11293    88 VVQGKEPPHFLALF 101
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 974-1034 1.15e-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: 1.15e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530410136  974 KQPEEDFQCIVYFWQGReASNMGWLTFTFSLQKKFESLFPGKLEVVRMTQQQENPKFLSHF 1034
Cdd:cd11280    29 DVFVLDTGSEIYIWQGR-ASSQAELAAAALLAKELDEERKGKPEIVRIRQGQEPREFWSLF 88
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 751-838 2.28e-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: 2.28e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136    751 HKQRPKVELMPRMRLLQSLLDTRCVYILDCWSDVFIWLGRKSPRLVRAAALKLGQELCGMLHrPRHATVSRSLEGTEAQV 830
Cdd:smart00262    4 RVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLG-PGPVQVRVVDEGKEPPE 82


                    ....*...
gi 530410136    831 FKAKFKNW 838
Cdd:smart00262   83 FWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1168-1288 3.43e-18

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


Pssm-ID: 214590 [Multi-domain]  Cd Length: 90  Bit Score: 80.80  E-value: 3.43e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136   1168 RCSNEKGYFAVTEKCSDFCQDDLADDDIMLLDNGQEVYMWVGTQTSQVEIKLSLKAcqviwveggprwacgqgrvitqgs 1247
Cdd:smart00262    1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAEL------------------------ 56

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|.
gi 530410136   1248 lspCQVYIQHMRSkeheRPRRLRLVRKGNEQHAFTRCFHAW 1288
Cdd:smart00262   57 ---AVELDDTLGP----GPVQVRVVDEGKEPPEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 503-596 5.06e-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: 80.03  E-value: 5.06e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136    503 IWQIENFVPVLVEE--AFHGKFYEADCYIVLKTflddsgslnWEIYYWIGGEATLDKKACSAIHAVNLRNYLGAECRTVR 580
Cdd:smart00262    2 LVRVKGKRNVRVPEvpFSQGSLNSGDCYILDTG---------SEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVR 72

                            90
                    ....*....|....*..
gi 530410136    581 E-EMGDESEEFLQVFDN 596
Cdd:smart00262   73 VvDEGKEPPEFWSLFGG 89
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 15-352 1.30e-17

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 88.75  E-value: 1.30e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136   15 LSGNDFKGGyFPENVKAMTSLRWLKLNRTGLC-YLPEELAALQKLEHLSVSHNNLT-TLHGELSSLPSLRAIVARANSLK 92
Cdd:PLN00113  195 LASNQLVGQ-IPRELGQMKSLKWIYLGYNNLSgEIPYEIGGLTSLNHLDLVYNNLTgPIPSSLGNLKNLQYLFLYQNKLS 273

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136   93 NSgVPDDIFKLDDLSVLDLSHNQLT-ECPRELENAKNMLVLNL-SHNSIDTIPN-----------QLFIN---------- 149
Cdd:PLN00113  274 GP-IPPSIFSLQKLISLDLSDNSLSgEIPELVIQLQNLEILHLfSNNFTGKIPValtslprlqvlQLWSNkfsgeipknl 352

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136  150 --LTDLLYLDLSENRLES-LPPQMRRLVHLQTLVLNGNPLLHAQLRQLPAMTALQTLHLRSTQRTqSNLPTSLEGLSNLA 226
Cdd:PLN00113  353 gkHNNLTVLDLSTNNLTGeIPEGLCSSGNLFKLILFSNSLEGEIPKSLGACRSLRRVRLQDNSFS-GELPSEFTKLPLVY 431

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136  227 DVDLSCNDLT-RVPECLYTLPSLRRLNLSSNQIT-EL--SLCIDQwvhVETLNLSRNQLTSLpsaicklsklkklylnsn 302
Cdd:PLN00113  432 FLDISNNNLQgRINSRKWDMPSLQMLSLARNKFFgGLpdSFGSKR---LENLDLSRNQFSGA------------------ 490

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 530410136  303 kldfdgLPSGIGKLTNLEEFMAANNNLE-LVPESLCRCPKLRKLVLNKNHL 352
Cdd:PLN00113  491 ------VPRKLGSLSELMQLKLSENKLSgEIPDELSSCKKLVSLDLSHNQL 535
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
26-288 1.85e-16

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 84.75  E-value: 1.85e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136   26 PENVKAMTSLR-WLKLNRTGLC-----------YLPEELAALqklehlSVSHNNLTTLHGELSSlpSLRAIVARANSLkn 93
Cdd:PRK15370  163 ANREEAVQRMRdCLKNNKTELRlkilglttipaCIPEQITTL------ILDNNELKSLPENLQG--NIKTLYANSNQL-- 232

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136   94 SGVPDDIfkLDDLSVLDLSHNQLTECPRELENAknMLVLNLSHNSIDTIPNqlfiNLTD-LLYLDLSENRLESLPPQM-R 171
Cdd:PRK15370  233 TSIPATL--PDTIQEMELSINRITELPERLPSA--LQSLDLFHNKISCLPE----NLPEeLRYLSVYDNSIRTLPAHLpS 304

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136  172 RLVHLqtLVLNGNpllhaqLRQLPAMTALQTLHLRSTQRTQSNLPTSLEglSNLADVDLSCNDLTRVPECLytLPSLRRL 251
Cdd:PRK15370  305 GITHL--NVQSNS------LTALPETLPPGLKTLEAGENALTSLPASLP--PELQVLDVSKNQITVLPETL--PPTITTL 372

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 530410136  252 NLSSNQITELSLCIDqwVHVETLNLSRNQLTSLPSAI 288
Cdd:PRK15370  373 DVSRNALTNLPENLP--AALQIMQASRNNLVRLPESL 407
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1057-1149 5.75e-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: 74.25  E-value: 5.75e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136   1057 YQIRTNGSaLCTRCIQINTDSSLLNSEFCFILkvpfeseDNQGIVYAWVGRASDPDEAKLAEDILNTMFDTSYSK----Q 1132
Cdd:smart00262    1 FLVRVKGK-RNVRVPEVPFSQGSLNSGDCYIL-------DTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGpvqvR 72

                            90
                    ....*....|....*..
gi 530410136   1133 VINEGEEPENFFWVGIG 1149
Cdd:smart00262   73 VVDEGKEPPEFWSLFGG 89
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 103-285 2.42e-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: 76.36  E-value: 2.42e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136  103 LDDLSVLDLSHNQLTECPrELENAKNMLVLNLSHNSIDTIPNqlFINLTDLLYLDLSENRLESLPPqMRRLVHLQTLVLN 182
Cdd:cd21340     1 LKRITHLYLNDKNITKID-NLSLCKNLKVLYLYDNKITKIEN--LEFLTNLTHLYLQNNQIEKIEN-LENLVNLKKLYLG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136  183 GNPLlhAQLRQLPAMTALQTLHLrSTQRTQSNL-----PTSLEGLSN-LADVDLSCNDLTRVpECLYTLPSLRRLNLSSN 256
Cdd:cd21340    77 GNRI--SVVEGLENLTNLEELHI-ENQRLPPGEkltfdPRSLAALSNsLRVLNISGNNIDSL-EPLAPLRNLEQLDASNN 152

                         170       180       190
                  ....*....|....*....|....*....|..
gi 530410136  257 QIT---ELSLCIDQWVHVETLNLSRNQLTSLP 285
Cdd:cd21340   153 QISdleELLDLLSSWPSLRELDLTGNPVCKKP 184
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 618-707 5.13e-15

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


Pssm-ID: 200445  Cd Length: 92  Bit Score: 71.50  E-value: 5.13e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136  618 VTRMYRVYGKKNIKLEPVPLKGTSLDPRFVFLLDRGLDIYVWRGAQATLSSTTKARLFAEKINKNERKGKAEITLLVQG- 696
Cdd:cd11289     1 KPRLLHVKGRRNVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKVIVLDEGd 80

                          90
                  ....*....|..
gi 530410136  697 -QELPEFWEALG 707
Cdd:cd11289    81 tNESPEFWKVLG 92
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
149-374 7.05e-15

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 78.44  E-value: 7.05e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136  149 NLTDLLYLDLSENRLESLPPQMRRLVHLQTLVLNGNPLLHAQLRQLPAMTALQTLHLRSTQRTQSNLPTSLEGLSNLADV 228
Cdd:COG4886     1 LLLLLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136  229 DLSCNDLTrvPECLYTLPSLRRLNLSSNQItelslcIDQWVHVETLNLSRNQLTSLPSAIcklsklkklylnsnkldfdg 308
Cdd:COG4886    81 LLSLLLLG--LTDLGDLTNLTELDLSGNEE------LSNLTNLESLDLSGNQLTDLPEEL-------------------- 132

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530410136  309 lpsgiGKLTNLEEFMAANNNLELVPESLCRCPKLRKLVLNKNHLVTLPEAIHFLTEIEVLDVRENP 374
Cdd:COG4886   133 -----ANLTNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQ 193
Gelsolin pfam00626
Gelsolin repeat;
628-703 2.32e-14

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 69.26  E-value: 2.32e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530410136   628 KNIKLEPVPLKGTSLDPRFVFLLDRGLDIYVWRGAQATLSSTTKARLFAEKINKNERKGKAEITLLVQGQELPEFW 703
Cdd:pfam00626    1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDERFPLPEVIRVPQGKEPARFL 76
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 100-352 4.73e-14

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 77.20  E-value: 4.73e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136  100 IFKLDDLSVLDLSHNQLT-ECPREL-ENAKNMLVLNLSHNSID-TIPNQLFINLTDllyLDLSENRLE-SLPPQMRRLVH 175
Cdd:PLN00113   89 IFRLPYIQTINLSNNQLSgPIPDDIfTTSSSLRYLNLSNNNFTgSIPRGSIPNLET---LDLSNNMLSgEIPNDIGSFSS 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136  176 LQTLVLNGNPLLHAQLRQLPAMTALQTLHLRSTQRT-------------------QSNL----PTSLEGLSNLADVDLSC 232
Cdd:PLN00113  166 LKVLDLGGNVLVGKIPNSLTNLTSLEFLTLASNQLVgqiprelgqmkslkwiylgYNNLsgeiPYEIGGLTSLNHLDLVY 245

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136  233 NDLT-------------------------RVPECLYTLPSLRRLNLSSNQIT-ELSLCIDQWVHVETLNLSRNQLT-SLP 285
Cdd:PLN00113  246 NNLTgpipsslgnlknlqylflyqnklsgPIPPSIFSLQKLISLDLSDNSLSgEIPELVIQLQNLEILHLFSNNFTgKIP 325

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530410136  286 SAICKLSKLKKLYLNSNKLDfDGLPSGIGKLTNLEEFMAANNNLE-LVPESLCRCPKLRKLVLNKNHL 352
Cdd:PLN00113  326 VALTSLPRLQVLQLWSNKFS-GEIPKNLGKHNNLTVLDLSTNNLTgEIPEGLCSSGNLFKLILFSNSL 392
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
191-379 1.29e-13

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 75.89  E-value: 1.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136  191 LRQLPAMTALQTLHLRSTQRTQSNLPTSLEGlsNLADVDLSCNDLTRVPEclyTLP-SLRRLNLSSNQITELSLCIDQwv 269
Cdd:PRK15370  190 LTTIPACIPEQITTLILDNNELKSLPENLQG--NIKTLYANSNQLTSIPA---TLPdTIQEMELSINRITELPERLPS-- 262

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136  270 HVETLNLSRNQLTSLPSAICKLSKLKKLYLNSNKLDFDGLPSGIgkltnlEEFMAANNNLELVPESLcrCPKLRKLVLNK 349
Cdd:PRK15370  263 ALQSLDLFHNKISCLPENLPEELRYLSVYDNSIRTLPAHLPSGI------THLNVQSNSLTALPETL--PPGLKTLEAGE 334

                         170       180       190
                  ....*....|....*....|....*....|
gi 530410136  350 NHLVTLPEAIHflTEIEVLDVRENPNLVMP 379
Cdd:PRK15370  335 NALTSLPASLP--PELQVLDVSKNQITVLP 362
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
127-451 8.44e-13

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 73.19  E-value: 8.44e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136  127 KNMLVLNLSHNSIDTIPNQLFINLTDLLyldLSENRLESLPPQMRrlVHLQTLVLNGNpllhaQLRQLPAmtalqtlhlr 206
Cdd:PRK15370  178 NNKTELRLKILGLTTIPACIPEQITTLI---LDNNELKSLPENLQ--GNIKTLYANSN-----QLTSIPA---------- 237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136  207 stqrtqsNLPTSLEglsnlaDVDLSCNDLTRVPEclyTLPS-LRRLNLSSNQITELSLCIDQwvHVETLNLSRNQLTSLP 285
Cdd:PRK15370  238 -------TLPDTIQ------EMELSINRITELPE---RLPSaLQSLDLFHNKISCLPENLPE--ELRYLSVYDNSIRTLP 299

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136  286 SAICKLSKLKKLYLNSnkLDFdgLPSGIGklTNLEEFMAANNNLELVPESLCrcPKLRKLVLNKNHLVTLPEAIHflTEI 365
Cdd:PRK15370  300 AHLPSGITHLNVQSNS--LTA--LPETLP--PGLKTLEAGENALTSLPASLP--PELQVLDVSKNQITVLPETLP--PTI 369

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136  366 EVLDVRENP--NLvmppkPADRAAEWYNIDFSLQNQLRLAgaspatVAAAAAAGSGPK--------DPMA-RKMRLRRRK 434
Cdd:PRK15370  370 TTLDVSRNAltNL-----PENLPAALQIMQASRNNLVRLP------ESLPHFRGEGPQptriiveyNPFSeRTIQNMQRL 438

                         330
                  ....*....|....*..
gi 530410136  435 DSAQDDQAKQVLKGMSD 451
Cdd:PRK15370  439 MSSVGYQGPRVLFAMGD 455
Gelsolin pfam00626
Gelsolin repeat;
508-591 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 530410136   508 NFVPVLVEEAFHGKFYEADCYIVLKTFlddsgslnwEIYYWIGGEATLDKKACSAIHAVNLR-NYLGAECRTVREEMGDE 586
Cdd:pfam00626    1 KFVLPPPVPLSQESLNSGDCYLLDNGF---------TIFLWVGKGSSLLEKLFAALLAAQLDdDERFPLPEVIRVPQGKE 71


                   ....*
gi 530410136   587 SEEFL 591
Cdd:pfam00626   72 PARFL 76
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 4-256 2.69e-12

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 71.42  E-value: 2.69e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136    4 TGVLPfvRGVDLSGNDFK--------GGYFPENVKAMTSLRWLKLNRTGLC-YLPEELAALQKLEHLSVSHNNLTtlhGE 74
Cdd:PLN00113  369 TGEIP--EGLCSSGNLFKlilfsnslEGEIPKSLGACRSLRRVRLQDNSFSgELPSEFTKLPLVYFLDISNNNLQ---GR 443

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136   75 LSS----LPSLRAIVARANSLknSGVPDDIFKLDDLSVLDLSHNQLTEcprelenaknmlvlnlshnsidTIPNQlFINL 150
Cdd:PLN00113  444 INSrkwdMPSLQMLSLARNKF--FGGLPDSFGSKRLENLDLSRNQFSG----------------------AVPRK-LGSL 498

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136  151 TDLLYLDLSENRLESLPPqmrrlvhlqtlvlngnpllhaqlRQLPAMTALQTLHLRSTQRTqSNLPTSLEGLSNLADVDL 230
Cdd:PLN00113  499 SELMQLKLSENKLSGEIP-----------------------DELSSCKKLVSLDLSHNQLS-GQIPASFSEMPVLSQLDL 554

                         250       260
                  ....*....|....*....|....*..
gi 530410136  231 SCNDLT-RVPECLYTLPSLRRLNLSSN 256
Cdd:PLN00113  555 SQNQLSgEIPKNLGNVESLVQVNISHN 581
LRR_8 pfam13855
Leucine rich repeat;
131-186 2.42e-11

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 60.23  E-value: 2.42e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 530410136   131 VLNLSHNSIDTIPNQLFINLTDLLYLDLSENRLESLPPQM-RRLVHLQTLVLNGNPL 186
Cdd:pfam13855    5 SLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAfSGLPSLRYLDLSGNRL 61
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 619-708 8.78e-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: 8.78e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136  619 TRMYRVYG--KKNIKLEPVPLKGTSLDPRFVFLLDRGLDIYVWRGAQATLSSTTKARLFAEKInknerKGKAEITLLVQG 696
Cdd:cd11288     3 TRLFQVRGngSGNTRAVEVDADASSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVASFL-----KPKASLQEVAEG 77

                          90
                  ....*....|..
gi 530410136  697 QELPEFWEALGG 708
Cdd:cd11288    78 SEPDEFWEALGG 89
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 50-188 1.55e-10

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


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 62.50  E-value: 1.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136   50 EELAALQKLEHLSVSHNNLTTLHGeLSSLPSLRAIVARANSLKnsgVPDDIFKLDDLSVLDLSHNQLT--EC----PREL 123
Cdd:cd21340    40 ENLEFLTNLTHLYLQNNQIEKIEN-LENLVNLKKLYLGGNRIS---VVEGLENLTNLEELHIENQRLPpgEKltfdPRSL 115

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530410136  124 EN-AKNMLVLNLSHNSIDTIpNQLFiNLTDLLYLDLSENRLESLPPQ---MRRLVHLQTLVLNGNPLLH 188
Cdd:cd21340   116 AAlSNSLRVLNISGNNIDSL-EPLA-PLRNLEQLDASNNQISDLEELldlLSSWPSLRELDLTGNPVCK 182
PRK15387 PRK15387
type III secretion system effector E3 ubiquitin transferase SspH2;
131-374 4.16e-10

type III secretion system effector E3 ubiquitin transferase SspH2;


Pssm-ID: 185285 [Multi-domain]  Cd Length: 788  Bit Score: 64.41  E-value: 4.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136  131 VLNLSHNSIDTIPNQLFINLTDLLYLDLSENRLESLPPQMRrlvhlqTLVLNGNpllhaQLRQLPAMTAlQTLHLRSTQR 210
Cdd:PRK15387  205 VLNVGESGLTTLPDCLPAHITTLVIPDNNLTSLPALPPELR------TLEVSGN-----QLTSLPVLPP-GLLELSIFSN 272

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136  211 TQSNLPTSLEGLSNLAdvdLSCNDLTRVPeclYTLPSLRRLNLSSNQITEL-----SLCiDQWVH-------------VE 272
Cdd:PRK15387  273 PLTHLPALPSGLCKLW---IFGNQLTSLP---VLPPGLQELSVSDNQLASLpalpsELC-KLWAYnnqltslptlpsgLQ 345

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136  273 TLNLSRNQLTSLPSaiCKLSKLKKLYLNSNKLDFDGLPSGIGKL--------------TNLEEFMAANNNLELVPeslcR 338
Cdd:PRK15387  346 ELSVSDNQLASLPT--LPSELYKLWAYNNRLTSLPALPSGLKELivsgnrltslpvlpSELKELMVSGNRLTSLP----M 419

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 530410136  339 CPK-LRKLVLNKNHLVTLPEAIHFLTEIEVLDVRENP 374
Cdd:PRK15387  420 LPSgLLSLSVYRNQLTRLPESLIHLSSETTVNLEGNP 456
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 503-594 5.19e-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: 5.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136  503 IWQIENFVPVLVEE--AFHGKFYEADCYIVlktfldDSGSlnwEIYYWIGGEATLDKKACSAIHAVNLRNYLGAECRTVR 580
Cdd:cd11280     4 LYRVRGSKAIEIEEvpLASSSLDSDDVFVL------DTGS---EIYIWQGRASSQAELAAAALLAKELDEERKGKPEIVR 74

                          90
                  ....*....|....
gi 530410136  581 EEMGDESEEFLQVF 594
Cdd:cd11280    75 IRQGQEPREFWSLF 88
LRR_8 pfam13855
Leucine rich repeat;
106-163 3.37e-09

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 54.07  E-value: 3.37e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 530410136   106 LSVLDLSHNQLTECPRE-LENAKNMLVLNLSHNSIDTIPNQLFINLTDLLYLDLSENRL 163
Cdd:pfam13855    3 LRSLDLSNNRLTSLDDGaFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 89-374 7.82e-09

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


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 58.91  E-value: 7.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136   89 NSLKNSGVPDDIFKLDDLSVLDLSHNQLTE-----CPRELENAKNMLVLNLSHNSIDTIPNQL------FINLTDLLYLD 157
Cdd:cd00116     8 ELLKTERATELLPKLLCLQVLRLEGNTLGEeaakaLASALRPQPSLKELCLSLNETGRIPRGLqsllqgLTKGCGLQELD 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136  158 LSEN--------RLESLppqmRRLVHLQTLVLNGNPLLHAQLRQLpaMTALQ--TLHLRSTQRTQSNL-PTSLEGLSN-- 224
Cdd:cd00116    88 LSDNalgpdgcgVLESL----LRSSSLQELKLNNNGLGDRGLRLL--AKGLKdlPPALEKLVLGRNRLeGASCEALAKal 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136  225 -----LADVDLSCNDL-----TRVPECLYTLPSLRRLNLSSNQITE-----LSLCIDQWVHVETLNLSRNQLTSLP-SAI 288
Cdd:cd00116   162 ranrdLKELNLANNGIgdagiRALAEGLKANCNLEVLDLNNNGLTDegasaLAETLASLKSLEVLNLGDNNLTDAGaAAL 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136  289 CklsklkklylnsnkldfDGLPSGIGKLTNLEefmAANNNLELVP-ESLCRC----PKLRKLVLNKNHLVTLPEAIHFLT 363
Cdd:cd00116   242 A-----------------SALLSPNISLLTLS---LSCNDITDDGaKDLAEVlaekESLLELDLRGNKFGEEGAQLLAES 301

                         330
                  ....*....|....*..
gi 530410136  364 ------EIEVLDVRENP 374
Cdd:cd00116   302 llepgnELESLWVKDDS 318
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 618-702 4.24e-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: 4.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136  618 VTRMYRVY-GKKNIKLEPV---PLKGTSLDPRFVFLLDRGLDIYVWRGAQATLSSTTKARLFAEK-INKNERKGKAEITL 692
Cdd:cd11292     3 QKKLYKVSdASGKLKLTEVaegSLNQEMLDSEDCYILDCGSEIFVWVGKGASLDERKAALKNAEEfLRKKKRPPYTQVTR 82

                          90
                  ....*....|
gi 530410136  693 LVQGQELPEF 702
Cdd:cd11292    83 VTEGGESALF 92
LRR_8 pfam13855
Leucine rich repeat;
223-281 5.34e-08

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 50.60  E-value: 5.34e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530410136   223 SNLADVDLSCNDLTRV-PECLYTLPSLRRLNLSSNQITELSL-CIDQWVHVETLNLSRNQL 281
Cdd:pfam13855    1 PNLRSLDLSNNRLTSLdDGAFKGLSNLKVLDLSNNLLTTLSPgAFSGLPSLRYLDLSGNRL 61
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 1051-1143 7.39e-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: 7.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136 1051 AQQPSLYQIRTNGSALCTRCIQINT-DSSLLNSEFCFILkvpfeseDNQGIVYAWVGRASDPDEAK----LAEDILNTMF 1125
Cdd:cd11292     1 AEQKKLYKVSDASGKLKLTEVAEGSlNQEMLDSEDCYIL-------DCGSEIFVWVGKGASLDERKaalkNAEEFLRKKK 73

                          90
                  ....*....|....*....
gi 530410136 1126 DTSYSK-QVINEGEEPENF 1143
Cdd:cd11292    74 RPPYTQvTRVTEGGESALF 92
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 768-835 1.22e-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: 1.22e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530410136  768 SLLDTRCVYILDCWSDVFIWLGRKSPRLVRAAALKLGQELcgmLHRPRHAT-VSRSLEGTEAQVFKAKF 835
Cdd:cd11280    23 SSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKEL---DEERKGKPeIVRIRQGQEPREFWSLF 88
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 767-839 1.30e-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: 1.30e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530410136  767 QSLLDTRCVYILDCWSDVFIWLGRKSPRLVRAAALKLGQ---ELCGMLHRPRHATVSRSLEGTEAQVFKAKFKNWD 839
Cdd:cd11291    24 QDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKkyiETDPLGRSKPRTPIYLVKQGNEPPTFTGYFHAWD 99
PRK15387 PRK15387
type III secretion system effector E3 ubiquitin transferase SspH2;
38-288 2.76e-07

type III secretion system effector E3 ubiquitin transferase SspH2;


Pssm-ID: 185285 [Multi-domain]  Cd Length: 788  Bit Score: 55.17  E-value: 2.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136   38 LKLNRTGLCYLPEELAAlqKLEHLSVSHNNLTTLHgelSSLPSLRAIVARANSLKNSGV-PDDIFKLDDLSvldlshNQL 116
Cdd:PRK15387  206 LNVGESGLTTLPDCLPA--HITTLVIPDNNLTSLP---ALPPELRTLEVSGNQLTSLPVlPPGLLELSIFS------NPL 274

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136  117 TECPRELENAKNMLVLNLSHNSIDTIPnqlfinlTDLLYLDLSENRLESLPPQMRRLVHLQTLvlngnpllHAQLRQLPA 196
Cdd:PRK15387  275 THLPALPSGLCKLWIFGNQLTSLPVLP-------PGLQELSVSDNQLASLPALPSELCKLWAY--------NNQLTSLPT 339

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136  197 M-TALQTLHLRSTQRTQ--------------SNLPTSLEGL-SNLADVDLSCNDLTRVPeclyTLPS-LRRLNLSSNQIT 259
Cdd:PRK15387  340 LpSGLQELSVSDNQLASlptlpselyklwayNNRLTSLPALpSGLKELIVSGNRLTSLP----VLPSeLKELMVSGNRLT 415

                         250       260
                  ....*....|....*....|....*....
gi 530410136  260 ELSLCIDQWVhveTLNLSRNQLTSLPSAI 288
Cdd:PRK15387  416 SLPMLPSGLL---SLSVYRNQLTRLPESL 441
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 1164-1251 8.96e-07

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


Pssm-ID: 200448  Cd Length: 98  Bit Score: 48.40  E-value: 8.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136 1164 TRLFRCSNEKGYFAVTE-KCSDFCQDDLADDDIMLLDNGQEVYMWVGTQTSQVEIKLSLK-ACQVIWVEGGPRWAcgQGR 1241
Cdd:cd11292     4 KKLYKVSDASGKLKLTEvAEGSLNQEMLDSEDCYILDCGSEIFVWVGKGASLDERKAALKnAEEFLRKKKRPPYT--QVT 81

                          90
                  ....*....|
gi 530410136 1242 VITQGSLSPC 1251
Cdd:cd11292    82 RVTEGGESAL 91
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 1164-1291 2.66e-06

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


Pssm-ID: 200436  Cd Length: 88  Bit Score: 46.59  E-value: 2.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136 1164 TRLFRCSNEK-GYFAVTEKCSDfcqdDLADDDIMLLDNGQEVYMWVGTQTSQVEiklslkacqviwveggprwacgqgrv 1242
Cdd:cd11280     2 PRLYRVRGSKaIEIEEVPLASS----SLDSDDVFVLDTGSEIYIWQGRASSQAE-------------------------- 51

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 530410136 1243 itqgsLSPCQVYIQHMRSKEHERPRRLRlVRKGNEQHAFtrcfhaWSAF 1291
Cdd:cd11280    52 -----LAAAALLAKELDEERKGKPEIVR-IRQGQEPREF------WSLF 88
Gelsolin pfam00626
Gelsolin repeat;
756-832 4.45e-06

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 45.76  E-value: 4.45e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530410136   756 KVELMPRMRLLQSLLDTRCVYILDCWSDVFIWLGRKSPRLVRAAALKLGQELcGMLHRPRHATVSRSLEGTEAQVFK 832
Cdd:pfam00626    1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQL-DDDERFPLPEVIRVPQGKEPARFL 76
LRR_8 pfam13855
Leucine rich repeat;
175-258 5.96e-06

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 44.82  E-value: 5.96e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136   175 HLQTLVLNGNPLLHAQlrqlpamtalqtlhlrstqrtqsnlPTSLEGLSNLADVDLSCNDLTRV-PECLYTLPSLRRLNL 253
Cdd:pfam13855    2 NLRSLDLSNNRLTSLD-------------------------DGAFKGLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDL 56


                   ....*
gi 530410136   254 SSNQI 258
Cdd:pfam13855   57 SGNRL 61
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 74-282 6.58e-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: 49.66  E-value: 6.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136   74 ELSSLPSLRAIVARANSLKNSGVPDDIFKLD---DLSVLDLSHNQLTECPRELENAKNMLV-------LNLSHNSIDTIP 143
Cdd:cd00116    18 LLPKLLCLQVLRLEGNTLGEEAAKALASALRpqpSLKELCLSLNETGRIPRGLQSLLQGLTkgcglqeLDLSDNALGPDG 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136  144 NQLFINLT---DLLYLDLSENRLESLPPQM--RRLVHLQ----TLVLNGNPLLHAQLRQ----LPAMTALQTLHLRSTQR 210
Cdd:cd00116    98 CGVLESLLrssSLQELKLNNNGLGDRGLRLlaKGLKDLPpaleKLVLGRNRLEGASCEAlakaLRANRDLKELNLANNGI 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136  211 TQSNLPTSLEGL---SNLADVDLSCNDLTR-----VPECLYTLPSLRRLNLSSNQITELSLC------IDQWVHVETLNL 276
Cdd:cd00116   178 GDAGIRALAEGLkanCNLEVLDLNNNGLTDegasaLAETLASLKSLEVLNLGDNNLTDAGAAalasalLSPNISLLTLSL 257


                  ....*.
gi 530410136  277 SRNQLT 282
Cdd:cd00116   258 SCNDIT 263
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 1053-1145 6.61e-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: 45.82  E-value: 6.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136 1053 QPSLYQIRTNGSalcTRCIQINTDSSLLNSEFCFILkvpfeseDNQGIVYAWVGRASDPDE----AKLAEDILNTMFDTS 1128
Cdd:cd11280     1 PPRLYRVRGSKA---IEIEEVPLASSSLDSDDVFVL-------DTGSEIYIWQGRASSQAElaaaALLAKELDEERKGKP 70

                          90
                  ....*....|....*..
gi 530410136 1129 YSkQVINEGEEPEnFFW 1145
Cdd:cd11280    71 EI-VRIRQGQEPR-EFW 85
Gelsolin pfam00626
Gelsolin repeat;
1181-1220 8.01e-06

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 44.99  E-value: 8.01e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 530410136  1181 KCSDFCQDDLADDDIMLLDNGQEVYMWVGTQTSQVEIKLS 1220
Cdd:pfam00626    6 PPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFA 45
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 75-282 9.20e-06

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


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 49.79  E-value: 9.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136   75 LSSLPSLRAIVARANSLKNSGVPDdIFK----LDDLSVLDLSHNQLT-----ECPRELENAKNMLVLNLSHNSIDtipnq 145
Cdd:COG5238   204 LTQNTTVTTLWLKRNPIGDEGAEI-LAEalkgNKSLTTLDLSNNQIGdegviALAEALKNNTTVETLYLSGNQIG----- 277

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136  146 lfinltdllyldlsENRLESLPPQMRRLVHLQTLVLNGNPL----LHAQLRQLPAMTALQTLHLRSTQRTQSN---LPTS 218
Cdd:COG5238   278 --------------AEGAIALAKALQGNTTLTSLDLSVNRIgdegAIALAEGLQGNKTLHTLNLAYNGIGAQGaiaLAKA 343

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530410136  219 LEGLSNLADVDLSCNDLT-----RVPECLYTLPSLRRLNLSSNQITEL-------SLCIDQwvhVETLNLSRNQLT 282
Cdd:COG5238   344 LQENTTLHSLDLSDNQIGdegaiALAKYLEGNTTLRELNLGKNNIGKQgaealidALQTNR---LHTLILDGNLIG 416
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 33-194 9.29e-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: 9.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136   33 TSLRWLKLNR------------TGLCYLPEELAALQkLEHLSVSHNNLTTLHGELSSLPSLRAIVARANSLKNSGVPD-- 98
Cdd:cd00116   108 SSLQELKLNNnglgdrglrllaKGLKDLPPALEKLV-LGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRAla 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136   99 DIFK-LDDLSVLDLSHNQLT--------ECPRELenaKNMLVLNLSHNSID-----TIPNQLFINLTDLLYLDLSENRLE 164
Cdd:cd00116   187 EGLKaNCNLEVLDLNNNGLTdegasalaETLASL---KSLEVLNLGDNNLTdagaaALASALLSPNISLLTLSLSCNDIT 263

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 530410136  165 -----SLPPQMRRLVHLQTLVLNGNPLLHAQLRQL 194
Cdd:cd00116   264 ddgakDLAEVLAEKESLLELDLRGNKFGEEGAQLL 298
Gelsolin pfam00626
Gelsolin repeat;
1076-1143 1.37e-05

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 44.22  E-value: 1.37e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530410136  1076 DSSLLNSEFCFILkvpfeseDNQGIVYAWVGRASDPDE----AKLAEDILNTMFDTSYSKQVINEGEEPENF 1143
Cdd:pfam00626   11 SQESLNSGDCYLL-------DNGFTIFLWVGKGSSLLEklfaALLAAQLDDDERFPLPEVIRVPQGKEPARF 75
PRK15387 PRK15387
type III secretion system effector E3 ubiquitin transferase SspH2;
41-263 2.74e-05

type III secretion system effector E3 ubiquitin transferase SspH2;


Pssm-ID: 185285 [Multi-domain]  Cd Length: 788  Bit Score: 48.62  E-value: 2.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136   41 NRTGLCYLPEELAALQklehlsVSHNNLTTL-------------HGELSSLPSLRAIVARANSLKN--SGVPDDIFKLDD 105
Cdd:PRK15387  233 NLTSLPALPPELRTLE------VSGNQLTSLpvlppgllelsifSNPLTHLPALPSGLCKLWIFGNqlTSLPVLPPGLQE 306

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136  106 LSVLDlshNQLTECPRELENAKNMLVLNLSHNSIDTIPnqlfinlTDLLYLDLSENRLESLPPQMRRLVHLQTL--VLNG 183
Cdd:PRK15387  307 LSVSD---NQLASLPALPSELCKLWAYNNQLTSLPTLP-------SGLQELSVSDNQLASLPTLPSELYKLWAYnnRLTS 376

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136  184 NPLLHAQLRQLPA----MTALQTLHLRSTQRTQS-NLPTSLEGL-SNLADVDLSCNDLTRVPECLYTLPSLRRLNLSSNQ 257
Cdd:PRK15387  377 LPALPSGLKELIVsgnrLTSLPVLPSELKELMVSgNRLTSLPMLpSGLLSLSVYRNQLTRLPESLIHLSSETTVNLEGNP 456


                  ....*.
gi 530410136  258 ITELSL 263
Cdd:PRK15387  457 LSERTL 462
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 2-139 6.25e-05

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


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 46.58  E-value: 6.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136    2 EATGVLPFVRG---VDLSGNDFKGGYFP---ENVKAMTSLRWLKLNRTGLC-----YLPEELAALQKLEHLSVSHNNLT- 69
Cdd:cd00116   156 ALAKALRANRDlkeLNLANNGIGDAGIRalaEGLKANCNLEVLDLNNNGLTdegasALAETLASLKSLEVLNLGDNNLTd 235

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136   70 ----TLH-GELSSLPSLRAIVARANSLKNSGVPDDIFKLDD---LSVLDLSHNQLTE------CPRELENAKNMLVLNLS 135
Cdd:cd00116   236 agaaALAsALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEkesLLELDLRGNKFGEegaqllAESLLEPGNELESLWVK 315


                  ....
gi 530410136  136 HNSI 139
Cdd:cd00116   316 DDSF 319
LRR_8 pfam13855
Leucine rich repeat;
33-91 7.65e-05

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 41.74  E-value: 7.65e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530410136    33 TSLRWLKLNRTGLCYLPEE-LAALQKLEHLSVSHNNLTTLH-GELSSLPSLRAIVARANSL 91
Cdd:pfam13855    1 PNLRSLDLSNNRLTSLDDGaFKGLSNLKVLDLSNNLLTTLSpGAFSGLPSLRYLDLSGNRL 61
PLN03210 PLN03210
Resistant to P. syringae 6; Provisional
 152-401 8.78e-05

Resistant to P. syringae 6; Provisional


Pssm-ID: 215633 [Multi-domain]  Cd Length: 1153  Bit Score: 47.18  E-value: 8.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136  152 DLLYLDLSENRLESLPPQMRRLVHLQTLVLNGNpllhAQLRQLPAM---TALQTLHLRSTQrTQSNLPTSLEGLSNLADV 228
Cdd:PLN03210  612 NLVKLQMQGSKLEKLWDGVHSLTGLRNIDLRGS----KNLKEIPDLsmaTNLETLKLSDCS-SLVELPSSIQYLNKLEDL 686

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136  229 DLS-CNDLTRVPECLyTLPSLRRLNLSSnqITELSLCIDQWVHVETLNLSRNQLTSLPSAIcklsklkklylnsnkldfd 307
Cdd:PLN03210  687 DMSrCENLEILPTGI-NLKSLYRLNLSG--CSRLKSFPDISTNISWLDLDETAIEEFPSNL------------------- 744

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136  308 glpsgigKLTNLEEFMAANNNLE--------LVPESLCRCPKLRKLVLNKN-HLVTLPEAIHFLTEIEVLDVRENPNLVM 378
Cdd:PLN03210  745 -------RLENLDELILCEMKSEklwervqpLTPLMTMLSPSLTRLFLSDIpSLVELPSSIQNLHKLEHLEIENCINLET 817

                         250       260
                  ....*....|....*....|...
gi 530410136  379 PPKPADRAAeWYNIDFSLQNQLR 401
Cdd:PLN03210  818 LPTGINLES-LESLDLSGCSRLR 839
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 642-702 4.37e-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: 4.37e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530410136  642 LDPRFVFLLDRGLDIYVWRGAQAT----LSSTTKARLFAEKINKNERKGKAEITLLVQGQELPEF 702
Cdd:cd11291    27 LDTDDIMLLDTGDEVFVWVGSESSdeekKEALTSAKKYIETDPLGRSKPRTPIYLVKQGNEPPTF 91
PLN03150 PLN03150
hypothetical protein; Provisional
 90-186 6.21e-04

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 44.04  E-value: 6.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136   90 SLKNSG----VPDDIFKLddlsvldlshnqltecpRELENaknmlvLNLSHNSID-TIPNQLFiNLTDLLYLDLSENRLE 164
Cdd:PLN03150  424 GLDNQGlrgfIPNDISKL-----------------RHLQS------INLSGNSIRgNIPPSLG-SITSLEVLDLSYNSFN 479

                          90       100
                  ....*....|....*....|...
gi 530410136  165 -SLPPQMRRLVHLQTLVLNGNPL 186
Cdd:PLN03150  480 gSIPESLGQLTSLRILNLNGNSL 502
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 246-285 8.35e-04

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


Pssm-ID: 463713 [Multi-domain]  Cd Length: 44  Bit Score: 38.38  E-value: 8.35e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 530410136   246 PSLRRLNLSSNQITELSLcIDQWVHVETLNLSRN-QLTSLP 285
Cdd:pfam12799    1 PNLEVLDLSNNQITDIPP-LAKLPNLETLDLSGNnKITDLS 40
PLN03150 PLN03150
hypothetical protein; Provisional
 166-259 9.19e-04

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 43.65  E-value: 9.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136  166 LPPQMRRLVHLQTLVLNGNPLlhaqlrqlpamtalqtlhlrstqrtQSNLPTSLEGLSNLADVDLSCNDLT-RVPECLYT 244
Cdd:PLN03150  434 IPNDISKLRHLQSINLSGNSI-------------------------RGNIPPSLGSITSLEVLDLSYNSFNgSIPESLGQ 488

                          90
                  ....*....|....*
gi 530410136  245 LPSLRRLNLSSNQIT 259
Cdd:PLN03150  489 LTSLRILNLNGNSLS 503
PRK15387 PRK15387
type III secretion system effector E3 ubiquitin transferase SspH2;
58-199 1.32e-03

type III secretion system effector E3 ubiquitin transferase SspH2;


Pssm-ID: 185285 [Multi-domain]  Cd Length: 788  Bit Score: 43.23  E-value: 1.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136   58 LEHLSVSHNNLTTLHGELSSLPSLRAIVARANSLknSGVPDDifklddLSVLDLSHNQLTECPRELENAKNMLVlnlSHN 137
Cdd:PRK15387  344 LQELSVSDNQLASLPTLPSELYKLWAYNNRLTSL--PALPSG------LKELIVSGNRLTSLPVLPSELKELMV---SGN 412

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530410136  138 SIDTIPnqlfINLTDLLYLDLSENRLESLPPQMRRLVHLQTLVLNGNPLLHAQLRQLPAMTA 199
Cdd:PRK15387  413 RLTSLP----MLPSGLLSLSVYRNQLTRLPESLIHLSSETTVNLEGNPLSERTLQALREITS 470
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 1080-1143 2.24e-03

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: 38.82  E-value: 2.24e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530410136 1080 LNSEFCFILkvpfeseDNQGIVYAWVGRASDPDEAKLAEDILNTMFDTSYSKQ--------VINEGEEPENF 1143
Cdd:cd11291    27 LDTDDIMLL-------DTGDEVFVWVGSESSDEEKKEALTSAKKYIETDPLGRskprtpiyLVKQGNEPPTF 91
PLN03150 PLN03150
hypothetical protein; Provisional
 33-117 2.35e-03

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 42.11  E-value: 2.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136   33 TSLRW----LKLNRTGL-CYLPEELAALQKLEHLSVSHNNLttlHGELS----SLPSLRAIVARANSLkNSGVPDDIFKL 103
Cdd:PLN03150  414 TKGKWfidgLGLDNQGLrGFIPNDISKLRHLQSINLSGNSI---RGNIPpslgSITSLEVLDLSYNSF-NGSIPESLGQL 489

                          90
                  ....*....|....
gi 530410136  104 DDLSVLDLSHNQLT 117
Cdd:PLN03150  490 TSLRILNLNGNSLS 503
PRK15387 PRK15387
type III secretion system effector E3 ubiquitin transferase SspH2;
233-391 2.64e-03

type III secretion system effector E3 ubiquitin transferase SspH2;


Pssm-ID: 185285 [Multi-domain]  Cd Length: 788  Bit Score: 42.07  E-value: 2.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136  233 NDLTRVPEclyTLPSLRRLNLSSNQITELSLCIDQWVHVETLNLSRNQLTSLPSAICKLSKLkklylnSNKL-DFDGLPS 311
Cdd:PRK15387  232 NNLTSLPA---LPPELRTLEVSGNQLTSLPVLPPGLLELSIFSNPLTHLPALPSGLCKLWIF------GNQLtSLPVLPP 302

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136  312 GIGKLTNLEEFMAAnnnLELVPESLCrcpklrKLVLNKNHLVTLPEAIHFLTEIEVLDvreNPNLVMPPKPADRAAEW-Y 390
Cdd:PRK15387  303 GLQELSVSDNQLAS---LPALPSELC------KLWAYNNQLTSLPTLPSGLQELSVSD---NQLASLPTLPSELYKLWaY 370


                  .
gi 530410136  391 N 391
Cdd:PRK15387  371 N 371
LRR_8 pfam13855
Leucine rich repeat;
270-352 3.62e-03

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 37.12  E-value: 3.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530410136   270 HVETLNLSRNQLTSLPSAIcklsklkklylnsnkldFDGLPsgigkltNLEEFMAANNNLE-LVPESLCRCPKLRKLVLN 348
Cdd:pfam13855    2 NLRSLDLSNNRLTSLDDGA-----------------FKGLS-------NLKVLDLSNNLLTtLSPGAFSGLPSLRYLDLS 57


                   ....
gi 530410136   349 KNHL 352
Cdd:pfam13855   58 GNRL 61
LRR_8 pfam13855
Leucine rich repeat;
246-284 3.73e-03

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 37.12  E-value: 3.73e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 530410136   246 PSLRRLNLSSNQITELSlciDQW----VHVETLNLSRNQLTSL 284
Cdd:pfam13855    1 PNLRSLDLSNNRLTSLD---DGAfkglSNLKVLDLSNNLLTTL 40
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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