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Conserved domains on  [gi|3004660|gb|AAC28407|]
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flightless [Drosophila melanogaster]

Protein Classification

flightless-1 family protein( domain architecture ID 11469395)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
gelsolin_S1_like cd11290
Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; ...
 491-602 9.11e-58

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: 194.36  E-value: 9.11e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660   491 KDDGQLPGLTIWEIENFLPNKIEEVVHGKFYEGDCYIVLKTKFDDLGLLDWEIFFWIGNEATLDKRACAAIHAVNLRNFL 570
Cdd:cd11290    2 EGVGQKPGLQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDPSGSLSYDIHYWLGKEASQDEAGAAAIKAVELDDYL 81

                         90       100       110
                 ....*....|....*....|....*....|..
gi 3004660   571 GARCRTVREEQGDESEQFLSLFETEVIYIEGG 602
Cdd:cd11290   82 GGRPVQHREVQGHESEEFLSYFKKGIIYIEGG 113
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 1151-1250 1.10e-46

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


:

Pssm-ID: 200447 [Multi-domain]  Cd Length: 99  Bit Score: 162.08  E-value: 1.10e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660  1151 YTRLFRCSNERGYyTVAEKCADFCQDDLADDDIMILDNGEHVFLWMGPRCSEVEVKLAYKSAQVYIQHMRIKQPERPRKL 1230
Cdd:cd11291    1 KPRLFRCSNESGF-FKVEEISDFSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYIETDPLGRSKPRTPI 79

                         90       100
                 ....*....|....*....|
gi 3004660  1231 FLTMKNKESRRFTKCFHGWS 1250
Cdd:cd11291   80 YLVKQGNEPPTFTGYFHAWD 99
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
33-405 1.51e-43

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


:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 164.34  E-value: 1.51e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660    33 WLTLDRTQLAEIPEELGHLQKLEHLSLNHNRLEKIFGELTELSCLRSLDLRHNQlknsgippELFHLEELTTLDLSHNKL 112
Cdd:COG4886   54 SLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNE--------ELSNLTNLESLDLSGNQL 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660   113 KEVPEGLERAKNLIVLNLSNNQIESIPTPLFiHLTDLLFLDLSHNRLETLPPQTRRLINLKTLDLSHNPLELF--QLRQL 190
Cdd:COG4886  126 TDLPEELANLTNLKELDLSNNQLTDLPEPLG-NLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLpePLGNL 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660   191 PSLQSLEVlkmSGTQrtLLNFPTSIDSLANLCELDLSHNSLPKLPDcVYNVVTLVRLNLSDNELTELTAGVELwQRLESL 270
Cdd:COG4886  205 TNLEELDL---SGNQ--LTDLPEPLANLTNLETLDLSNNQLTDLPE-LGNLTNLEELDLSNNQLTDLPPLANL-TNLKTL 277

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660   271 NLSRNQLVALpaALCKLPKLRRLLVNDNKLNFEGIPSGIGKLGALEVFSAANNLLEMVPEGLCRCGALKQLNLSCNRLIT 350
Cdd:COG4886  278 DLSNNQLTDL--KLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLL 355

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 3004660   351 LPDAIHLLEGLDQLDLRNNPELVMPPKPSEASKATSLEFYNIDFSLQTQLRLAGA 405
Cdd:COG4886  356 LNLLSLLLTLLLTLGLLGLLEATLLTLALLLLTLLLLLLTTTAGVLLLTLALLDA 410
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 729-828 1.51e-37

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: 136.23  E-value: 1.51e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660   729 PVQPRLYQVQLGMGYLELPQVELPeqKLCHTLLNSKHVYILDCYTDLFVWFGKKSTRLVRAAAVKLSRELFNMMDRPDYA 808
Cdd:cd11292    1 AEQKKLYKVSDASGKLKLTEVAEG--SLNQEMLDSEDCYILDCGSEIFVWVGKGASLDERKAALKNAEEFLRKKKRPPYT 78

                         90       100
                 ....*....|....*....|
gi 3004660   809 LVMRVPEGNEMQIFRTKFAG 828
Cdd:cd11292   79 QVTRVTEGGESALFKSKFAN 98
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 1037-1141 7.18e-33

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: 122.34  E-value: 7.18e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660  1037 SPVEFFHLRSNGgALTTRLIQINPDAVHLNSAFCYILHVPFeteddsqsgIVYVWIGSKACNEEAKLVQDIAEQMFnsPW 1116
Cdd:cd11288    1 SPTRLFQVRGNG-SGNTRAVEVDADASSLNSNDVFVLKTPS---------SVYLWVGKGSSEDERELAKDVASFLK--PK 68

                         90       100
                 ....*....|....*....|....*
gi 3004660  1117 VSLQILNEGDEPENfFWVALGGRKP 1141
Cdd:cd11288   69 ASLQEVAEGSEPDE-FWEALGGKSE 92
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 618-706 1.90e-26

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: 103.99  E-value: 1.90e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660   618 TRLYLVHAYGAtIHLEPVAPAITSLDPRHAFVLDLGTHIYIWMGERSKNTLNSKARLMAEKISKtERKNKCEIQLERQGE 697
Cdd:cd11280    2 PRLYRVRGSKA-IEIEEVPLASSSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKELDE-ERKGKPEIVRIRQGQ 79


                 ....*....
gi 3004660   698 ESAEFWQGL 706
Cdd:cd11280   80 EPREFWSLF 88
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 920-1015 1.49e-20

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: 87.42  E-value: 1.49e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660   920 CYVFLCRYC--IPIEEPENGSEDganpaadvskSSANNQPEDEIQCVVYFWQGRNAgNMGWLTFTFTLQKKFKAMFGEEL 997
Cdd:cd11280    2 PRLYRVRGSkaIEIEEVPLASSS----------LDSDDVFVLDTGSEIYIWQGRAS-SQAELAAAALLAKELDEERKGKP 70

                         90
                 ....*....|....*...
gi 3004660   998 EVVRIFQQQENLKFMSHF 1015
Cdd:cd11280   71 EIVRIRQGQEPREFWSLF 88
 
Name Accession Description Interval E-value
gelsolin_S1_like cd11290
Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; ...
 491-602 9.11e-58

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: 194.36  E-value: 9.11e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660   491 KDDGQLPGLTIWEIENFLPNKIEEVVHGKFYEGDCYIVLKTKFDDLGLLDWEIFFWIGNEATLDKRACAAIHAVNLRNFL 570
Cdd:cd11290    2 EGVGQKPGLQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDPSGSLSYDIHYWLGKEASQDEAGAAAIKAVELDDYL 81

                         90       100       110
                 ....*....|....*....|....*....|..
gi 3004660   571 GARCRTVREEQGDESEQFLSLFETEVIYIEGG 602
Cdd:cd11290   82 GGRPVQHREVQGHESEEFLSYFKKGIIYIEGG 113
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 1151-1250 1.10e-46

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


Pssm-ID: 200447 [Multi-domain]  Cd Length: 99  Bit Score: 162.08  E-value: 1.10e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660  1151 YTRLFRCSNERGYyTVAEKCADFCQDDLADDDIMILDNGEHVFLWMGPRCSEVEVKLAYKSAQVYIQHMRIKQPERPRKL 1230
Cdd:cd11291    1 KPRLFRCSNESGF-FKVEEISDFSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYIETDPLGRSKPRTPI 79

                         90       100
                 ....*....|....*....|
gi 3004660  1231 FLTMKNKESRRFTKCFHGWS 1250
Cdd:cd11291   80 YLVKQGNEPPTFTGYFHAWD 99
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
33-405 1.51e-43

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 164.34  E-value: 1.51e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660    33 WLTLDRTQLAEIPEELGHLQKLEHLSLNHNRLEKIFGELTELSCLRSLDLRHNQlknsgippELFHLEELTTLDLSHNKL 112
Cdd:COG4886   54 SLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNE--------ELSNLTNLESLDLSGNQL 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660   113 KEVPEGLERAKNLIVLNLSNNQIESIPTPLFiHLTDLLFLDLSHNRLETLPPQTRRLINLKTLDLSHNPLELF--QLRQL 190
Cdd:COG4886  126 TDLPEELANLTNLKELDLSNNQLTDLPEPLG-NLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLpePLGNL 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660   191 PSLQSLEVlkmSGTQrtLLNFPTSIDSLANLCELDLSHNSLPKLPDcVYNVVTLVRLNLSDNELTELTAGVELwQRLESL 270
Cdd:COG4886  205 TNLEELDL---SGNQ--LTDLPEPLANLTNLETLDLSNNQLTDLPE-LGNLTNLEELDLSNNQLTDLPPLANL-TNLKTL 277

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660   271 NLSRNQLVALpaALCKLPKLRRLLVNDNKLNFEGIPSGIGKLGALEVFSAANNLLEMVPEGLCRCGALKQLNLSCNRLIT 350
Cdd:COG4886  278 DLSNNQLTDL--KLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLL 355

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 3004660   351 LPDAIHLLEGLDQLDLRNNPELVMPPKPSEASKATSLEFYNIDFSLQTQLRLAGA 405
Cdd:COG4886  356 LNLLSLLLTLLLTLGLLGLLEATLLTLALLLLTLLLLLLTTTAGVLLLTLALLDA 410
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 729-828 1.51e-37

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: 136.23  E-value: 1.51e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660   729 PVQPRLYQVQLGMGYLELPQVELPeqKLCHTLLNSKHVYILDCYTDLFVWFGKKSTRLVRAAAVKLSRELFNMMDRPDYA 808
Cdd:cd11292    1 AEQKKLYKVSDASGKLKLTEVAEG--SLNQEMLDSEDCYILDCGSEIFVWVGKGASLDERKAALKNAEEFLRKKKRPPYT 78

                         90       100
                 ....*....|....*....|
gi 3004660   809 LVMRVPEGNEMQIFRTKFAG 828
Cdd:cd11292   79 QVTRVTEGGESALFKSKFAN 98
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 1037-1141 7.18e-33

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: 122.34  E-value: 7.18e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660  1037 SPVEFFHLRSNGgALTTRLIQINPDAVHLNSAFCYILHVPFeteddsqsgIVYVWIGSKACNEEAKLVQDIAEQMFnsPW 1116
Cdd:cd11288    1 SPTRLFQVRGNG-SGNTRAVEVDADASSLNSNDVFVLKTPS---------SVYLWVGKGSSEDERELAKDVASFLK--PK 68

                         90       100
                 ....*....|....*....|....*
gi 3004660  1117 VSLQILNEGDEPENfFWVALGGRKP 1141
Cdd:cd11288   69 ASLQEVAEGSEPDE-FWEALGGKSE 92
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 15-369 7.00e-30

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 128.81  E-value: 7.00e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660     15 NDFSATFPSSMRQMSRVQWLTLDRTQLA-EIPEELGHLQKLEHLSLNHNRLE-KIFGELTELSCLRSLDLRHNQLKNSgI 92
Cdd:PLN00113  198 NQLVGQIPRELGQMKSLKWIYLGYNNLSgEIPYEIGGLTSLNHLDLVYNNLTgPIPSSLGNLKNLQYLFLYQNKLSGP-I 276

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660     93 PPELFHLEELTTLDLSHNKLK-EVPEGLERAKNLIVLNL-SNNQIESIPTPLfIHLTDLLFLDLSHNRLE-TLPPQTRRL 169
Cdd:PLN00113  277 PPSIFSLQKLISLDLSDNSLSgEIPELVIQLQNLEILHLfSNNFTGKIPVAL-TSLPRLQVLQLWSNKFSgEIPKNLGKH 355

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660    170 INLKTLDLSHNPL------------ELFQL--------RQLP-SLQSLEVLKMSGTQRTLLN--FPTSIDSLANLCELDL 226
Cdd:PLN00113  356 NNLTVLDLSTNNLtgeipeglcssgNLFKLilfsnsleGEIPkSLGACRSLRRVRLQDNSFSgeLPSEFTKLPLVYFLDI 435

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660    227 SHNSLP-KLPDCVYNVVTLVRLNLSDN----ELTELTAGvelwQRLESLNLSRNQLV-ALPAALCKLPKLRRLLVNDNKL 300
Cdd:PLN00113  436 SNNNLQgRINSRKWDMPSLQMLSLARNkffgGLPDSFGS----KRLENLDLSRNQFSgAVPRKLGSLSELMQLKLSENKL 511

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3004660    301 NFEgIP---SGIGKLGALEVfsAANNLLEMVPEGLCRCGALKQLNLSCNRLI-TLPDAIHLLEGLDQLDLRNN 369
Cdd:PLN00113  512 SGE-IPdelSSCKKLVSLDL--SHNQLSGQIPASFSEMPVLSQLDLSQNQLSgEIPKNLGNVESLVQVNISHN 581
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 618-706 1.90e-26

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: 103.99  E-value: 1.90e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660   618 TRLYLVHAYGAtIHLEPVAPAITSLDPRHAFVLDLGTHIYIWMGERSKNTLNSKARLMAEKISKtERKNKCEIQLERQGE 697
Cdd:cd11280    2 PRLYRVRGSKA-IEIEEVPLASSSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKELDE-ERKGKPEIVRIRQGQ 79


                 ....*....
gi 3004660   698 ESAEFWQGL 706
Cdd:cd11280   80 EPREFWSLF 88
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 748-829 3.94e-22

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: 91.97  E-value: 3.94e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660      748 QVELPEQKLCHTLLNSKHVYILDCYTDLFVWFGKKSTRLVRAAAVKLSRELFNMMdRPDYALVMRVPEGNEMQIFRTKFA 827
Cdd:smart00262   10 NVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTL-GPGPVQVRVVDEGKEPPEFWSLFG 88


                    ..
gi 3004660      828 GW 829
Cdd:smart00262   89 GW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1156-1249 6.73e-22

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: 91.20  E-value: 6.73e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660     1156 RCSNERGYYTVAEKCADFCQDDLADDDIMILDNGEHVFLWMGPRCSEVEVKLAYKSAQVYIQHMRikqpERPRKLFLTMK 1235
Cdd:smart00262    1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLG----PGPVQVRVVDE 76

                            90
                    ....*....|....
gi 3004660     1236 NKESRRFTKCFHGW 1249
Cdd:smart00262   77 GKEPPEFWSLFGGW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 621-707 5.89e-21

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: 88.50  E-value: 5.89e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660      621 YLVHAYGA-TIHLEPVAPAITSLDPRHAFVLDLGTHIYIWMGERSKNTLNSKARLMAEKISKTERKNKCEIQLERQGEES 699
Cdd:smart00262    1 FLVRVKGKrNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVRVVDEGKEP 80


                    ....*...
gi 3004660      700 AEFWQGLG 707
Cdd:smart00262   81 PEFWSLFG 88
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 920-1015 1.49e-20

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: 87.42  E-value: 1.49e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660   920 CYVFLCRYC--IPIEEPENGSEDganpaadvskSSANNQPEDEIQCVVYFWQGRNAgNMGWLTFTFTLQKKFKAMFGEEL 997
Cdd:cd11280    2 PRLYRVRGSkaIEIEEVPLASSS----------LDSDDVFVLDTGSEIYIWQGRAS-SQAELAAAALLAKELDEERKGKP 70

                         90
                 ....*....|....*...
gi 3004660   998 EVVRIFQQQENLKFMSHF 1015
Cdd:cd11280   71 EIVRIRQGQEPREFWSLF 88
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 99-300 2.85e-19

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: 87.92  E-value: 2.85e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660    99 LEELTTLDLSHNKLKEVpEGLERAKNLIVLNLSNNQIESIPTplFIHLTDLLFLDLSHNRLETLPPqTRRLINLKTLDLS 178
Cdd:cd21340    1 LKRITHLYLNDKNITKI-DNLSLCKNLKVLYLYDNKITKIEN--LEFLTNLTHLYLQNNQIEKIEN-LENLVNLKKLYLG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660   179 HNplELFQLRQLPSLQSLEVLKMSGtQRTLLNF-----PTSIDSLAN-LCELDLSHNSLPKLpDCVYNVVTLVRLNLSDN 252
Cdd:cd21340   77 GN--RISVVEGLENLTNLEELHIEN-QRLPPGEkltfdPRSLAALSNsLRVLNISGNNIDSL-EPLAPLRNLEQLDASNN 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 3004660   253 ELT---ELTAGVELWQRLESLNLSRNqlvalPaaLCKLPKLR-RLLVNDNKL 300
Cdd:cd21340  153 QISdleELLDLLSSWPSLRELDLTGN-----P--VCKKPKYRdKIILASKSL 197
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 501-592 4.06e-19

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: 83.11  E-value: 4.06e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660      501 IWEIENFLPNKIEEV--VHGKFYEGDCYIVLKTkfddlglldWEIFFWIGNEATLDKRACAAIHAVNLRNFLGARCRTVR 578
Cdd:smart00262    2 LVRVKGKRNVRVPEVpfSQGSLNSGDCYILDTG---------SEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVR 72

                            90
                    ....*....|....*
gi 3004660      579 E-EQGDESEQFLSLF 592
Cdd:smart00262   73 VvDEGKEPPEFWSLF 87
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1042-1138 3.68e-17

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: 77.72  E-value: 3.68e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660     1042 FHLRSNGgALTTRLIQINPDAVHLNSAFCYILHVPfeteddsqsGIVYVWIGSKACNEEAKLVQDIAEQMF---NSPWVS 1118
Cdd:smart00262    1 FLVRVKG-KRNVRVPEVPFSQGSLNSGDCYILDTG---------SEIYVWVGKKSSQDEKKKAAELAVELDdtlGPGPVQ 70

                            90       100
                    ....*....|....*....|
gi 3004660     1119 LQILNEGDEPENfFWVALGG 1138
Cdd:smart00262   71 VRVVDEGKEPPE-FWSLFGG 89
Gelsolin pfam00626
Gelsolin repeat;
748-823 1.88e-12

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 63.87  E-value: 1.88e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3004660     748 QVELPEQKLCHTLLNSKHVYILDCYTDLFVWFGKKSTRLVRAAAVKLSRELfNMMDRPDYALVMRVPEGNEMQIFR 823
Cdd:pfam00626    2 FVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQL-DDDERFPLPEVIRVPQGKEPARFL 76
LRR_8 pfam13855
Leucine rich repeat;
101-159 2.88e-11

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 59.85  E-value: 2.88e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660     101 ELTTLDLSHNKLKEVPEG-LERAKNLIVLNLSNNQIESIPTPLFIHLTDLLFLDLSHNRL 159
Cdd:pfam13855    2 NLRSLDLSNNRLTSLDDGaFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
Gelsolin pfam00626
Gelsolin repeat;
517-589 8.82e-11

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 58.86  E-value: 8.82e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3004660     517 HGKFYEGDCYIVLKTKfddlglldwEIFFWIGNEATLDKRACAAIHAVNLR-NFLGARCRTVREEQGDESEQFL 589
Cdd:pfam00626   12 QESLNSGDCYLLDNGF---------TIFLWVGKGSSLLEKLFAALLAAQLDdDERFPLPEVIRVPQGKEPARFL 76
Gelsolin pfam00626
Gelsolin repeat;
1165-1242 9.63e-11

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 58.86  E-value: 9.63e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3004660    1165 TVAEKCADFCQDDLADDDIMILDNGEHVFLWMGPRCSEVEVKLAYKSAQVYIQHMRIKQPErprkLFLTMKNKESRRF 1242
Cdd:pfam00626    2 FVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDERFPLPE----VIRVPQGKEPARF 75
Gelsolin pfam00626
Gelsolin repeat;
633-703 7.35e-10

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 56.55  E-value: 7.35e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3004660     633 EPVAPAITSLDPRHAFVLDLGTHIYIWMGERSKNTLNSKARLMAEKISKTERKNKCEIQLERQGEESAEFW 703
Cdd:pfam00626    6 PPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDERFPLPEVIRVPQGKEPARFL 76
 
Name Accession Description Interval E-value
gelsolin_S1_like cd11290
Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins; ...
 491-602 9.11e-58

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: 194.36  E-value: 9.11e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660   491 KDDGQLPGLTIWEIENFLPNKIEEVVHGKFYEGDCYIVLKTKFDDLGLLDWEIFFWIGNEATLDKRACAAIHAVNLRNFL 570
Cdd:cd11290    2 EGVGQKPGLQIWRIENFELVPVPESFYGKFYEGDSYIVLKTTLDPSGSLSYDIHYWLGKEASQDEAGAAAIKAVELDDYL 81

                         90       100       110
                 ....*....|....*....|....*....|..
gi 3004660   571 GARCRTVREEQGDESEQFLSLFETEVIYIEGG 602
Cdd:cd11290   82 GGRPVQHREVQGHESEEFLSYFKKGIIYIEGG 113
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 1151-1250 1.10e-46

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


Pssm-ID: 200447 [Multi-domain]  Cd Length: 99  Bit Score: 162.08  E-value: 1.10e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660  1151 YTRLFRCSNERGYyTVAEKCADFCQDDLADDDIMILDNGEHVFLWMGPRCSEVEVKLAYKSAQVYIQHMRIKQPERPRKL 1230
Cdd:cd11291    1 KPRLFRCSNESGF-FKVEEISDFSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYIETDPLGRSKPRTPI 79

                         90       100
                 ....*....|....*....|
gi 3004660  1231 FLTMKNKESRRFTKCFHGWS 1250
Cdd:cd11291   80 YLVKQGNEPPTFTGYFHAWD 99
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
33-405 1.51e-43

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 164.34  E-value: 1.51e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660    33 WLTLDRTQLAEIPEELGHLQKLEHLSLNHNRLEKIFGELTELSCLRSLDLRHNQlknsgippELFHLEELTTLDLSHNKL 112
Cdd:COG4886   54 SLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNE--------ELSNLTNLESLDLSGNQL 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660   113 KEVPEGLERAKNLIVLNLSNNQIESIPTPLFiHLTDLLFLDLSHNRLETLPPQTRRLINLKTLDLSHNPLELF--QLRQL 190
Cdd:COG4886  126 TDLPEELANLTNLKELDLSNNQLTDLPEPLG-NLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLpePLGNL 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660   191 PSLQSLEVlkmSGTQrtLLNFPTSIDSLANLCELDLSHNSLPKLPDcVYNVVTLVRLNLSDNELTELTAGVELwQRLESL 270
Cdd:COG4886  205 TNLEELDL---SGNQ--LTDLPEPLANLTNLETLDLSNNQLTDLPE-LGNLTNLEELDLSNNQLTDLPPLANL-TNLKTL 277

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660   271 NLSRNQLVALpaALCKLPKLRRLLVNDNKLNFEGIPSGIGKLGALEVFSAANNLLEMVPEGLCRCGALKQLNLSCNRLIT 350
Cdd:COG4886  278 DLSNNQLTDL--KLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLL 355

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 3004660   351 LPDAIHLLEGLDQLDLRNNPELVMPPKPSEASKATSLEFYNIDFSLQTQLRLAGA 405
Cdd:COG4886  356 LNLLSLLLTLLLTLGLLGLLEATLLTLALLLLTLLLLLLTTTAGVLLLTLALLDA 410
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
27-303 1.77e-43

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 164.34  E-value: 1.77e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660    27 QMSRVQWLTLDRTQLAEIPEELGHLQKLEHLSLNHNRLEKIFGELTELSCLRSLDLRHNQLknSGIPPELFHLEELTTLD 106
Cdd:COG4886  111 NLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQL--TDLPEELGNLTNLKELD 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660   107 LSHNKLKEVPEGLERAKNLIVLNLSNNQIESIPTPLFiHLTDLLFLDLSHNRLETLpPQTRRLINLKTLDLSHNPLElfQ 186
Cdd:COG4886  189 LSNNQITDLPEPLGNLTNLEELDLSGNQLTDLPEPLA-NLTNLETLDLSNNQLTDL-PELGNLTNLEELDLSNNQLT--D 264

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660   187 LRQLPSLQSLEVLKMSGTQRTLLNF-----PTSIDSLANLCELDLSHNSLPKLPDCVYNVVTLVRLNLSDNELTELTAGV 261
Cdd:COG4886  265 LPPLANLTNLKTLDLSNNQLTDLKLkelelLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSL 344

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 3004660   262 ELWQRLESLNLSRNQLVALPAALCKLPKLRRLLVNDNKLNFE 303
Cdd:COG4886  345 SLLALLTLLLLLNLLSLLLTLLLTLGLLGLLEATLLTLALLL 386
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
10-284 1.04e-42

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 162.03  E-value: 1.04e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660    10 VDFTKNDFSaTFPSSMRQMSRVQWLTLDRTQLAEIPEELGHLQKLEHLSLNHNRLEKIFGELTELSCLRSLDLRHNQLKN 89
Cdd:COG4886  118 LDLSGNQLT-DLPEELANLTNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITD 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660    90 sgIPPELFHLEELTTLDLSHNKLKEVPEGLERAKNLIVLNLSNNQIESIPTplFIHLTDLLFLDLSHNRLETLPPQTrRL 169
Cdd:COG4886  197 --LPEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTDLPE--LGNLTNLEELDLSNNQLTDLPPLA-NL 271

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660   170 INLKTLDLSHNPLELFQLRQLPSLQSLEVLKMSGTQRTLLN----FPTSIDSLANLCELDLSHNSLPKLPDCVYNVVTLV 245
Cdd:COG4886  272 TNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLEllilLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLT 351

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 3004660   246 RLNLSDNELTELTAGVELWQRLESLNLSRNQLVALPAAL 284
Cdd:COG4886  352 LLLLLNLLSLLLTLLLTLGLLGLLEATLLTLALLLLTLL 390
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
51-402 1.74e-38

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 149.31  E-value: 1.74e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660    51 LQKLEHLSLNHNRLEKIFGELTELSCLRSLDLRHNQLKNSGIPPELFHLEELTTLDLSHNklkevpEGLERAKNLIVLNL 130
Cdd:COG4886   47 LLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGN------EELSNLTNLESLDL 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660   131 SNNQIESIPTPLFiHLTDLLFLDLSHNRLETLPPQTRRLINLKTLDLSHNPLElfqlrqlpslqslevlkmsgtqrtllN 210
Cdd:COG4886  121 SGNQLTDLPEELA-NLTNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLT--------------------------D 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660   211 FPTSIDSLANLCELDLSHNSLPKLPDCVYNVVTLVRLNLSDNELTELTAGVELWQRLESLNLSRNQLVALPaALCKLPKL 290
Cdd:COG4886  174 LPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTDLP-ELGNLTNL 252

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660   291 RRLLVNDNKLnfEGIPSgIGKLGALEVFSAANN-LLEMVPEGLCRCGALKQLNLSCNRLITLPDAIHLLEGLDQLDLRNN 369
Cdd:COG4886  253 EELDLSNNQL--TDLPP-LANLTNLKTLDLSNNqLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLL 329

                        330       340       350
                 ....*....|....*....|....*....|...
gi 3004660   370 PELVMPPKPSEASKATSLEFYNIDFSLQTQLRL 402
Cdd:COG4886  330 LKGLLVTLTTLALSLSLLALLTLLLLLNLLSLL 362
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 729-828 1.51e-37

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: 136.23  E-value: 1.51e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660   729 PVQPRLYQVQLGMGYLELPQVELPeqKLCHTLLNSKHVYILDCYTDLFVWFGKKSTRLVRAAAVKLSRELFNMMDRPDYA 808
Cdd:cd11292    1 AEQKKLYKVSDASGKLKLTEVAEG--SLNQEMLDSEDCYILDCGSEIFVWVGKGASLDERKAALKNAEEFLRKKKRPPYT 78

                         90       100
                 ....*....|....*....|
gi 3004660   809 LVMRVPEGNEMQIFRTKFAG 828
Cdd:cd11292   79 QVTRVTEGGESALFKSKFAN 98
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
87-370 8.81e-36

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 141.61  E-value: 8.81e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660    87 LKNSGIPPELFHLEELTTLDLSHNKLKEVPEGLERAKNLIVLNLSNNQIESIPTPLFIHLTDLLFLDLSHNRLETL---P 163
Cdd:COG4886   10 LKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLllgL 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660   164 PQTRRLINLKTLDLSHNplelfqlRQLPSLQSLEVLKMSGTQrtLLNFPTSIDSLANLCELDLSHNSLPKLPDCVYNVVT 243
Cdd:COG4886   90 TDLGDLTNLTELDLSGN-------EELSNLTNLESLDLSGNQ--LTDLPEELANLTNLKELDLSNNQLTDLPEPLGNLTN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660   244 LVRLNLSDNELTELTAGVELWQRLESLNLSRNQLVALPAALCKLPKLRRLLVNDNKLnfEGIPSGIGKLGALEVFSAANN 323
Cdd:COG4886  161 LKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLEELDLSGNQL--TDLPEPLANLTNLETLDLSNN 238

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 3004660   324 LLEMVPEgLCRCGALKQLNLSCNRLITLPDAIHlLEGLDQLDLRNNP 370
Cdd:COG4886  239 QLTDLPE-LGNLTNLEELDLSNNQLTDLPPLAN-LTNLKTLDLSNNQ 283
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
4-268 8.83e-35

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 138.53  E-value: 8.83e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660     4 LPFVRGVDFTKNDFSaTFPSSMRQMSRVQWLTLDRTQLAEIPEELGHLQKLEHLSLNHNRLEKIFGELTELSCLRSLDLR 83
Cdd:COG4886  135 LTNLKELDLSNNQLT-DLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLEELDLS 213

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660    84 HNQLKNsgIPPELFHLEELTTLDLSHNKLKEVPEgLERAKNLIVLNLSNNQIESIPTPLfiHLTDLLFLDLSHNRLETLP 163
Cdd:COG4886  214 GNQLTD--LPEPLANLTNLETLDLSNNQLTDLPE-LGNLTNLEELDLSNNQLTDLPPLA--NLTNLKTLDLSNNQLTDLK 288

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660   164 PQT----RRLINLKTLDLSHNPLELFQLRQLPSLQSLEVLKMSGTQRTLLNFPTSIDSL-ANLCELDLSHNSLPKLPDCV 238
Cdd:COG4886  289 LKElellLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLaLLTLLLLLNLLSLLLTLLLT 368

                        250       260       270
                 ....*....|....*....|....*....|
gi 3004660   239 YNVVTLVRLNLSDNELTELTAGVELWQRLE 268
Cdd:COG4886  369 LGLLGLLEATLLTLALLLLTLLLLLLTTTA 398
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
98-369 1.31e-33

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 135.06  E-value: 1.31e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660    98 HLEELTTLDLSHNKLKEVPEGLERAKNLIVLNLSNNQIESIPTPLFIHLTDLLFLDLSHNRLETLPPQTRRLINLKTLDL 177
Cdd:COG4886    3 LLLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660   178 SHNPLELFQLRQLPSLQSLEvlkmsgtqrtlLNFPTSIDSLANLCELDLSHNSLPKLPDCVYNVVTLVRLNLSDNELTEL 257
Cdd:COG4886   83 SLLLLGLTDLGDLTNLTELD-----------LSGNEELSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDL 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660   258 TAGVELWQRLESLNLSRNQLVALPAALCKLPKLRRLLVNDNKLNFegIPSGIGKLGALEVFSAANNLLEMVPEGLCRCGA 337
Cdd:COG4886  152 PEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITD--LPEPLGNLTNLEELDLSGNQLTDLPEPLANLTN 229

                        250       260       270
                 ....*....|....*....|....*....|..
gi 3004660   338 LKQLNLSCNRLITLPDaIHLLEGLDQLDLRNN 369
Cdd:COG4886  230 LETLDLSNNQLTDLPE-LGNLTNLEELDLSNN 260
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 1037-1141 7.18e-33

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: 122.34  E-value: 7.18e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660  1037 SPVEFFHLRSNGgALTTRLIQINPDAVHLNSAFCYILHVPFeteddsqsgIVYVWIGSKACNEEAKLVQDIAEQMFnsPW 1116
Cdd:cd11288    1 SPTRLFQVRGNG-SGNTRAVEVDADASSLNSNDVFVLKTPS---------SVYLWVGKGSSEDERELAKDVASFLK--PK 68

                         90       100
                 ....*....|....*....|....*
gi 3004660  1117 VSLQILNEGDEPENfFWVALGGRKP 1141
Cdd:cd11288   69 ASLQEVAEGSEPDE-FWEALGGKSE 92
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
124-369 3.70e-31

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 127.74  E-value: 3.70e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660   124 NLIVLNLSNNQIESIPTPLFIHLTDLLFLDLSHNRLETLPPQTRRLINLKTLDLSHNPLELFQLRQLPSLQSLEVLKMSG 203
Cdd:COG4886    1 LLLLLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660   204 TQRTLLNFPTSIDSLANLCELDLSHNSLpklpdcVYNVVTLVRLNLSDNELTELTAGVELWQRLESLNLSRNQLVALPAA 283
Cdd:COG4886   81 LLSLLLLGLTDLGDLTNLTELDLSGNEE------LSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLPEP 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660   284 LCKLPKLRRLLVNDNKLnfEGIPSGIGKLGALEVFSAANNLLEMVPEGLCRCGALKQLNLSCNRLITLPDAIHLLEGLDQ 363
Cdd:COG4886  155 LGNLTNLKSLDLSNNQL--TDLPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLET 232


                 ....*.
gi 3004660   364 LDLRNN 369
Cdd:COG4886  233 LDLSNN 238
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 15-369 7.00e-30

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 128.81  E-value: 7.00e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660     15 NDFSATFPSSMRQMSRVQWLTLDRTQLA-EIPEELGHLQKLEHLSLNHNRLE-KIFGELTELSCLRSLDLRHNQLKNSgI 92
Cdd:PLN00113  198 NQLVGQIPRELGQMKSLKWIYLGYNNLSgEIPYEIGGLTSLNHLDLVYNNLTgPIPSSLGNLKNLQYLFLYQNKLSGP-I 276

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660     93 PPELFHLEELTTLDLSHNKLK-EVPEGLERAKNLIVLNL-SNNQIESIPTPLfIHLTDLLFLDLSHNRLE-TLPPQTRRL 169
Cdd:PLN00113  277 PPSIFSLQKLISLDLSDNSLSgEIPELVIQLQNLEILHLfSNNFTGKIPVAL-TSLPRLQVLQLWSNKFSgEIPKNLGKH 355

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660    170 INLKTLDLSHNPL------------ELFQL--------RQLP-SLQSLEVLKMSGTQRTLLN--FPTSIDSLANLCELDL 226
Cdd:PLN00113  356 NNLTVLDLSTNNLtgeipeglcssgNLFKLilfsnsleGEIPkSLGACRSLRRVRLQDNSFSgeLPSEFTKLPLVYFLDI 435

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660    227 SHNSLP-KLPDCVYNVVTLVRLNLSDN----ELTELTAGvelwQRLESLNLSRNQLV-ALPAALCKLPKLRRLLVNDNKL 300
Cdd:PLN00113  436 SNNNLQgRINSRKWDMPSLQMLSLARNkffgGLPDSFGS----KRLENLDLSRNQFSgAVPRKLGSLSELMQLKLSENKL 511

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3004660    301 NFEgIP---SGIGKLGALEVfsAANNLLEMVPEGLCRCGALKQLNLSCNRLI-TLPDAIHLLEGLDQLDLRNN 369
Cdd:PLN00113  512 SGE-IPdelSSCKKLVSLDL--SHNQLSGQIPASFSEMPVLSQLDLSQNQLSgEIPKNLGNVESLVQVNISHN 581
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
10-271 6.08e-27

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 115.03  E-value: 6.08e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660    10 VDFTKNDFSaTFPSSMRQMSRVQWLTLDRTQLAEIPEELGHLQKLEHLSLNHNRLEKIFGELTELSCLRSLDLRHNQLKN 89
Cdd:COG4886  164 LDLSNNQLT-DLPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTD 242

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660    90 sgiPPELFHLEELTTLDLSHNKLKEVPEgLERAKNLIVLNLSNNQIESiptplfIHLTDLLFLDLSHNRLETLPPQTRRL 169
Cdd:COG4886  243 ---LPELGNLTNLEELDLSNNQLTDLPP-LANLTNLKTLDLSNNQLTD------LKLKELELLLGLNSLLLLLLLLNLLE 312

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660   170 INLKTLDLSHNPLELFQLRQLPSLQSLEVLKMSGTQRTLLNFPTSIDSLANLCELDLSHNSLPKLPDCVYNVVTLVRLNL 249
Cdd:COG4886  313 LLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGLLEATLLTLALLLLTLLLL 392

                        250       260
                 ....*....|....*....|..
gi 3004660   250 SDNELTELTAGVELWQRLESLN 271
Cdd:COG4886  393 LLTTTAGVLLLTLALLDAVNTE 414
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 618-706 1.90e-26

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: 103.99  E-value: 1.90e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660   618 TRLYLVHAYGAtIHLEPVAPAITSLDPRHAFVLDLGTHIYIWMGERSKNTLNSKARLMAEKISKtERKNKCEIQLERQGE 697
Cdd:cd11280    2 PRLYRVRGSKA-IEIEEVPLASSSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKELDE-ERKGKPEIVRIRQGQ 79


                 ....*....
gi 3004660   698 ESAEFWQGL 706
Cdd:cd11280   80 EPREFWSLF 88
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 4-397 2.48e-25

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 113.79  E-value: 2.48e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660      4 LPFVRGVDFTKNDFSATFPSSMRQMSRVQWLTLDRTQL-AEIPEELGHLQKLEHLSLNHNRLE-KIFGELTELSCLRSLD 81
Cdd:PLN00113  139 IPNLETLDLSNNMLSGEIPNDIGSFSSLKVLDLGGNVLvGKIPNSLTNLTSLEFLTLASNQLVgQIPRELGQMKSLKWIY 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660     82 LRHNQLkNSGIPPELFHLEELTTLDLSHNKLK-EVPEGLERAKNLIVLNLSNNQIE-SIPTPLFiHLTDLLFLDLSHNRL 159
Cdd:PLN00113  219 LGYNNL-SGEIPYEIGGLTSLNHLDLVYNNLTgPIPSSLGNLKNLQYLFLYQNKLSgPIPPSIF-SLQKLISLDLSDNSL 296

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660    160 ETLPPQTrrLINLKTLDLSHnpleLFQ----------LRQLPSLQSLEVL--KMSGtqrtllNFPTSIDSLANLCELDLS 227
Cdd:PLN00113  297 SGEIPEL--VIQLQNLEILH----LFSnnftgkipvaLTSLPRLQVLQLWsnKFSG------EIPKNLGKHNNLTVLDLS 364

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660    228 HNSLP-KLPDCVYNVVTLVRLNLSDNEL-TELTAGVELWQRLESLNLSRNQLVA-LPAALCKLPKLRRLLVNDNklNFEG 304
Cdd:PLN00113  365 TNNLTgEIPEGLCSSGNLFKLILFSNSLeGEIPKSLGACRSLRRVRLQDNSFSGeLPSEFTKLPLVYFLDISNN--NLQG 442

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660    305 -IPSGIGKLGALEVFS-AANNLLEMVPEgLCRCGALKQLNLSCNRLI-TLPDAIHLLEGLDQLDLRNNpEL--VMPPKPS 379
Cdd:PLN00113  443 rINSRKWDMPSLQMLSlARNKFFGGLPD-SFGSKRLENLDLSRNQFSgAVPRKLGSLSELMQLKLSEN-KLsgEIPDELS 520

                         410
                  ....*....|....*...
gi 3004660    380 EASKATSLEFYNIDFSLQ 397
Cdd:PLN00113  521 SCKKLVSLDLSHNQLSGQ 538
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 748-829 3.94e-22

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: 91.97  E-value: 3.94e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660      748 QVELPEQKLCHTLLNSKHVYILDCYTDLFVWFGKKSTRLVRAAAVKLSRELFNMMdRPDYALVMRVPEGNEMQIFRTKFA 827
Cdd:smart00262   10 NVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTL-GPGPVQVRVVDEGKEPPEFWSLFG 88


                    ..
gi 3004660      828 GW 829
Cdd:smart00262   89 GW 90
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1156-1249 6.73e-22

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: 91.20  E-value: 6.73e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660     1156 RCSNERGYYTVAEKCADFCQDDLADDDIMILDNGEHVFLWMGPRCSEVEVKLAYKSAQVYIQHMRikqpERPRKLFLTMK 1235
Cdd:smart00262    1 FLVRVKGKRNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLG----PGPVQVRVVDE 76

                            90
                    ....*....|....
gi 3004660     1236 NKESRRFTKCFHGW 1249
Cdd:smart00262   77 GKEPPEFWSLFGGW 90
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 72-369 8.45e-22

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 102.62  E-value: 8.45e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660     72 TELSCLRSLDLRHnqlKN-SG-IPPELFHLEELTTLDLSHNKLK-EVPEGL-ERAKNLIVLNLSNNQIE-SIPTPlfiHL 146
Cdd:PLN00113   66 NNSSRVVSIDLSG---KNiSGkISSAIFRLPYIQTINLSNNQLSgPIPDDIfTTSSSLRYLNLSNNNFTgSIPRG---SI 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660    147 TDLLFLDLSHNRLE-TLPPQTRRLINLKTLDLSHNPLELFQLRQLPSLQSLEVLKMSGTQ------------RTL----L 209
Cdd:PLN00113  140 PNLETLDLSNNMLSgEIPNDIGSFSSLKVLDLGGNVLVGKIPNSLTNLTSLEFLTLASNQlvgqiprelgqmKSLkwiyL 219

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660    210 NF-------PTSIDSLANLCELDLSHNSLP-------------------------KLPDCVYNVVTLVRLNLSDNELT-E 256
Cdd:PLN00113  220 GYnnlsgeiPYEIGGLTSLNHLDLVYNNLTgpipsslgnlknlqylflyqnklsgPIPPSIFSLQKLISLDLSDNSLSgE 299

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660    257 LTAGVELWQRLESLNLSRNQLVA-LPAALCKLPKLRRLLVNDNKLNFEgIPSGIGKLGALEVFS-AANNLLEMVPEGLCR 334
Cdd:PLN00113  300 IPELVIQLQNLEILHLFSNNFTGkIPVALTSLPRLQVLQLWSNKFSGE-IPKNLGKHNNLTVLDlSTNNLTGEIPEGLCS 378

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 3004660    335 CGALKQLNLSCNRLIT-LPDAIHLLEGLDQLDLRNN 369
Cdd:PLN00113  379 SGNLFKLILFSNSLEGeIPKSLGACRSLRRVRLQDN 414
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 621-707 5.89e-21

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: 88.50  E-value: 5.89e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660      621 YLVHAYGA-TIHLEPVAPAITSLDPRHAFVLDLGTHIYIWMGERSKNTLNSKARLMAEKISKTERKNKCEIQLERQGEES 699
Cdd:smart00262    1 FLVRVKGKrNVRVPEVPFSQGSLNSGDCYILDTGSEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVRVVDEGKEP 80


                    ....*...
gi 3004660      700 AEFWQGLG 707
Cdd:smart00262   81 PEFWSLFG 88
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 10-277 7.62e-21

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 99.54  E-value: 7.62e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660     10 VDFTKNDFSATFPSSMRQMSRVQWLTLDRTQLA-------------------------EIPEELGHLQKLEHLSLNHNRL 64
Cdd:PLN00113  241 LDLVYNNLTGPIPSSLGNLKNLQYLFLYQNKLSgpippsifslqklisldlsdnslsgEIPELVIQLQNLEILHLFSNNF 320

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660     65 E-KIFGELTELSCLRSLDLRHNQLkNSGIPPELFHLEELTTLDLSHNKLK-EVPEGLERAKNLIVLNLSNNQIES-IPTP 141
Cdd:PLN00113  321 TgKIPVALTSLPRLQVLQLWSNKF-SGEIPKNLGKHNNLTVLDLSTNNLTgEIPEGLCSSGNLFKLILFSNSLEGeIPKS 399

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660    142 L-----------------------FIHLTDLLFLDLSHNRLE--------TLP----------------PQTRRLINLKT 174
Cdd:PLN00113  400 LgacrslrrvrlqdnsfsgelpseFTKLPLVYFLDISNNNLQgrinsrkwDMPslqmlslarnkffgglPDSFGSKRLEN 479

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660    175 LDLSHNPLELFQLRQLPSLQSLEVLKMSGTQRTlLNFPTSIDSLANLCELDLSHNSLP-KLPDCVYNVVTLVRLNLSDNE 253
Cdd:PLN00113  480 LDLSRNQFSGAVPRKLGSLSELMQLKLSENKLS-GEIPDELSSCKKLVSLDLSHNQLSgQIPASFSEMPVLSQLDLSQNQ 558

                         330       340
                  ....*....|....*....|....*
gi 3004660    254 LT-ELTAGVELWQRLESLNLSRNQL 277
Cdd:PLN00113  559 LSgEIPKNLGNVESLVQVNISHNHL 583
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 920-1015 1.49e-20

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: 87.42  E-value: 1.49e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660   920 CYVFLCRYC--IPIEEPENGSEDganpaadvskSSANNQPEDEIQCVVYFWQGRNAgNMGWLTFTFTLQKKFKAMFGEEL 997
Cdd:cd11280    2 PRLYRVRGSkaIEIEEVPLASSS----------LDSDDVFVLDTGSEIYIWQGRAS-SQAELAAAALLAKELDEERKGKP 70

                         90
                 ....*....|....*...
gi 3004660   998 EVVRIFQQQENLKFMSHF 1015
Cdd:cd11280   71 EIVRIRQGQEPREFWSLF 88
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 99-300 2.85e-19

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: 87.92  E-value: 2.85e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660    99 LEELTTLDLSHNKLKEVpEGLERAKNLIVLNLSNNQIESIPTplFIHLTDLLFLDLSHNRLETLPPqTRRLINLKTLDLS 178
Cdd:cd21340    1 LKRITHLYLNDKNITKI-DNLSLCKNLKVLYLYDNKITKIEN--LEFLTNLTHLYLQNNQIEKIEN-LENLVNLKKLYLG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660   179 HNplELFQLRQLPSLQSLEVLKMSGtQRTLLNF-----PTSIDSLAN-LCELDLSHNSLPKLpDCVYNVVTLVRLNLSDN 252
Cdd:cd21340   77 GN--RISVVEGLENLTNLEELHIEN-QRLPPGEkltfdPRSLAALSNsLRVLNISGNNIDSL-EPLAPLRNLEQLDASNN 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 3004660   253 ELT---ELTAGVELWQRLESLNLSRNqlvalPaaLCKLPKLR-RLLVNDNKL 300
Cdd:cd21340  153 QISdleELLDLLSSWPSLRELDLTGN-----P--VCKKPKYRdKIILASKSL 197
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 501-592 4.06e-19

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: 83.11  E-value: 4.06e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660      501 IWEIENFLPNKIEEV--VHGKFYEGDCYIVLKTkfddlglldWEIFFWIGNEATLDKRACAAIHAVNLRNFLGARCRTVR 578
Cdd:smart00262    2 LVRVKGKRNVRVPEVpfSQGSLNSGDCYILDTG---------SEIYVWVGKKSSQDEKKKAAELAVELDDTLGPGPVQVR 72

                            90
                    ....*....|....*
gi 3004660      579 E-EQGDESEQFLSLF 592
Cdd:smart00262   73 VvDEGKEPPEFWSLF 87
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
76-332 2.99e-18

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 90.53  E-value: 2.99e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660     76 CLRS--LDLRHNQLKNSGIPPELfhLEELTTLDLSHNKLKEVPEGLEraKNLIVLNLSNNQIESIPTPlfihLTDLL-FL 152
Cdd:PRK15370  175 CLKNnkTELRLKILGLTTIPACI--PEQITTLILDNNELKSLPENLQ--GNIKTLYANSNQLTSIPAT----LPDTIqEM 246

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660    153 DLSHNRLETLPpqtRRLIN-LKTLDLSHNPLELFQlRQLP-SLQSLEVLKMSgtQRTL-LNFPTSIdslanlCELDLSHN 229
Cdd:PRK15370  247 ELSINRITELP---ERLPSaLQSLDLFHNKISCLP-ENLPeELRYLSVYDNS--IRTLpAHLPSGI------THLNVQSN 314

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660    230 SLPKLPDCV-YNVVTLVRlnlSDNELTELTAgvELWQRLESLNLSRNQLVALPAALCklPKLRRLLVNDNKL-NF-EGIP 306
Cdd:PRK15370  315 SLTALPETLpPGLKTLEA---GENALTSLPA--SLPPELQVLDVSKNQITVLPETLP--PTITTLDVSRNALtNLpENLP 387

                         250       260
                  ....*....|....*....|....*.
gi 3004660    307 SgigklgALEVFSAANNLLEMVPEGL 332
Cdd:PRK15370  388 A------ALQIMQASRNNLVRLPESL 407
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
 499-592 3.17e-18

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


Pssm-ID: 200449  Cd Length: 101  Bit Score: 81.16  E-value: 3.17e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660   499 LTIWEIENFLPNKIEEVVHGKFYEGDCYIVLKTkFDDLGLLDWEIFFWIGNEATLDKRACAAIHAVNLRNFLGARCRTVR 578
Cdd:cd11293    9 VEVWRIENDEKVPVPKEEYGQFYGGDCYIVLYT-YQGGGKEEHILYFWQGRHSSQDERAAAALLTVELDEELKGRAVQVR 87

                         90
                 ....*....|....
gi 3004660   579 EEQGDESEQFLSLF 592
Cdd:cd11293   88 VVQGKEPPHFLALF 101
GEL smart00262
Gelsolin homology domain; Gelsolin/severin/villin homology domain. Calcium-binding and ...
 1042-1138 3.68e-17

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: 77.72  E-value: 3.68e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660     1042 FHLRSNGgALTTRLIQINPDAVHLNSAFCYILHVPfeteddsqsGIVYVWIGSKACNEEAKLVQDIAEQMF---NSPWVS 1118
Cdd:smart00262    1 FLVRVKG-KRNVRVPEVPFSQGSLNSGDCYILDTG---------SEIYVWVGKKSSQDEKKKAAELAVELDdtlGPGPVQ 70

                            90       100
                    ....*....|....*....|
gi 3004660     1119 LQILNEGDEPENfFWVALGG 1138
Cdd:smart00262   71 VRVVDEGKEPPE-FWSLFGG 89
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 34-182 3.39e-16

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


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 79.06  E-value: 3.39e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660    34 LTLDRTQLAEIpEELGHLQKLEHLSLNHNRLEKIFGeLTELSCLRSLDLRHNQLknSGIPPeLFHLEELTTLDLSHNKLK 113
Cdd:cd21340    7 LYLNDKNITKI-DNLSLCKNLKVLYLYDNKITKIEN-LEFLTNLTHLYLQNNQI--EKIEN-LENLVNLKKLYLGGNRIS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660   114 EVpEGLER------------------------------AKNLIVLNLSNNQIESIpTPLFiHLTDLLFLDLSHNRLETLP 163
Cdd:cd21340   82 VV-EGLENltnleelhienqrlppgekltfdprslaalSNSLRVLNISGNNIDSL-EPLA-PLRNLEQLDASNNQISDLE 158

                        170       180
                 ....*....|....*....|..
gi 3004660   164 PQT---RRLINLKTLDLSHNPL 182
Cdd:cd21340  159 ELLdllSSWPSLRELDLTGNPV 180
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 4-182 9.18e-14

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 76.43  E-value: 9.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660      4 LPFVRGVDFTKNDFSATFPSSMRQMSRVQWLTLDRTqlaeipeelghlqklehlslnhnrleKIFGELTELSC---LRSL 80
Cdd:PLN00113  427 LPLVYFLDISNNNLQGRINSRKWDMPSLQMLSLARN--------------------------KFFGGLPDSFGskrLENL 480

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660     81 DLRHNQLKNSgIPPELFHLEELTTLDLSHNKLK-EVPEGLERAKNLIVLNLSNNQIE-SIPTPlFIHLTDLLFLDLSHNR 158
Cdd:PLN00113  481 DLSRNQFSGA-VPRKLGSLSELMQLKLSENKLSgEIPDELSSCKKLVSLDLSHNQLSgQIPAS-FSEMPVLSQLDLSQNQ 558

                         170       180
                  ....*....|....*....|....*
gi 3004660    159 LE-TLPPQTRRLINLKTLDLSHNPL 182
Cdd:PLN00113  559 LSgEIPKNLGNVESLVQVNISHNHL 583
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 70-304 3.45e-13

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: 72.00  E-value: 3.45e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660    70 ELTELSCLRSLDLRHNQLKN---SGIPPELFHLEELTTLDLSHNKLKEVPEGLERA-------KNLIVLNLSNN--QIES 137
Cdd:cd00116   18 LLPKLLCLQVLRLEGNTLGEeaaKALASALRPQPSLKELCLSLNETGRIPRGLQSLlqgltkgCGLQELDLSDNalGPDG 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660   138 IPT-PLFIHLTDLLFLDLSHNRLETLPPQ------TRRLINLKTLDLSHNPLELFQLRQ----LPSLQSLEVLKMSgtqr 206
Cdd:cd00116   98 CGVlESLLRSSSLQELKLNNNGLGDRGLRllakglKDLPPALEKLVLGRNRLEGASCEAlakaLRANRDLKELNLA---- 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660   207 tllNFPTSIDSLANLCElDLSHNSLpklpdcvynvvtLVRLNLSDNELTE-----LTAGVELWQRLESLNLSRNQLVALP 281
Cdd:cd00116  174 ---NNGIGDAGIRALAE-GLKANCN------------LEVLDLNNNGLTDegasaLAETLASLKSLEVLNLGDNNLTDAG 237

                        250       260
                 ....*....|....*....|....*....
gi 3004660   282 -AALCK-----LPKLRRLLVNDNKLNFEG 304
Cdd:cd00116  238 aAALASallspNISLLTLSLSCNDITDDG 266
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
19-301 4.13e-13

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 73.96  E-value: 4.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660     19 ATFPSSMRQMSrvqwltLDRTQLAEIPEELGhlqklehlslnhnrlekifgeltelSCLRSLDLRHNQLknSGIPPELfh 98
Cdd:PRK15370  237 ATLPDTIQEME------LSINRITELPERLP-------------------------SALQSLDLFHNKI--SCLPENL-- 281

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660     99 LEELTTLDLSHNKLKEVPEGLerAKNLIVLNLSNNQIESIPtplfihltdllfldlshnrlETLPPqtrrliNLKTLDLS 178
Cdd:PRK15370  282 PEELRYLSVYDNSIRTLPAHL--PSGITHLNVQSNSLTALP--------------------ETLPP------GLKTLEAG 333

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660    179 HNPLELFQLRQLPSLQSLEVlkmSGTQRTLLnfPTSIDSlaNLCELDLSHNSLPKLPDcvynvvtlvrlnlsdneltelt 258
Cdd:PRK15370  334 ENALTSLPASLPPELQVLDV---SKNQITVL--PETLPP--TITTLDVSRNALTNLPE---------------------- 384

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 3004660    259 agvELWQRLESLNLSRNQLVALPAALCKL----PKLRRLLVNDNKLN 301
Cdd:PRK15370  385 ---NLPAALQIMQASRNNLVRLPESLPHFrgegPQPTRIIVEYNPFS 428
Gelsolin pfam00626
Gelsolin repeat;
748-823 1.88e-12

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 63.87  E-value: 1.88e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3004660     748 QVELPEQKLCHTLLNSKHVYILDCYTDLFVWFGKKSTRLVRAAAVKLSRELfNMMDRPDYALVMRVPEGNEMQIFR 823
Cdd:pfam00626    2 FVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQL-DDDERFPLPEVIRVPQGKEPARFL 76
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 618-707 8.94e-12

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


Pssm-ID: 200444  Cd Length: 92  Bit Score: 62.25  E-value: 8.94e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660   618 TRLYLVHAYGAT-IHLEPVAPAITSLDPRHAFVLDLGTHIYIWMGERSkntlNSKARLMAEKISKTeRKNKCEIQLERQG 696
Cdd:cd11288    3 TRLFQVRGNGSGnTRAVEVDADASSLNSNDVFVLKTPSSVYLWVGKGS----SEDERELAKDVASF-LKPKASLQEVAEG 77

                         90
                 ....*....|.
gi 3004660   697 EESAEFWQGLG 707
Cdd:cd11288   78 SEPDEFWEALG 88
PRK15387 PRK15387
type III secretion system effector E3 ubiquitin transferase SspH2;
127-379 9.83e-12

type III secretion system effector E3 ubiquitin transferase SspH2;


Pssm-ID: 185285 [Multi-domain]  Cd Length: 788  Bit Score: 69.42  E-value: 9.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660    127 VLNLSNNQIESIPTPLFIHLTDLLFLDLSHNRLETLPPQtrrlinLKTLDLSHNplelfQLRQLPSLQSlEVLKMSGTQR 206
Cdd:PRK15387  205 VLNVGESGLTTLPDCLPAHITTLVIPDNNLTSLPALPPE------LRTLEVSGN-----QLTSLPVLPP-GLLELSIFSN 272

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660    207 TLLNFPTSIDSLANLCELDLSHNSLPKLPDcvynvvTLVRLNLSDNELTELTAgveLWQRLESLNLSRNQLVALPAalck 286
Cdd:PRK15387  273 PLTHLPALPSGLCKLWIFGNQLTSLPVLPP------GLQELSVSDNQLASLPA---LPSELCKLWAYNNQLTSLPT---- 339

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660    287 LPK-LRRLLVNDNKL-NFEGIPSGIGKLGALevfsaaNNLLEMVPeglCRCGALKQLNLSCNRLITLPdaiHLLEGLDQL 364
Cdd:PRK15387  340 LPSgLQELSVSDNQLaSLPTLPSELYKLWAY------NNRLTSLP---ALPSGLKELIVSGNRLTSLP---VLPSELKEL 407

                         250
                  ....*....|....*
gi 3004660    365 DLRNNPELVMPPKPS 379
Cdd:PRK15387  408 MVSGNRLTSLPMLPS 422
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 79-369 2.24e-11

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: 66.61  E-value: 2.24e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660    79 SLDLRHNQLKNSGIPPELFHLEELTTLDLSHNKLKE-----VPEGLERAKNLIVLNLSNNQIESIPTPL------FIHLT 147
Cdd:cd00116    2 QLSLKGELLKTERATELLPKLLCLQVLRLEGNTLGEeaakaLASALRPQPSLKELCLSLNETGRIPRGLqsllqgLTKGC 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660   148 DLLFLDLSHNRLetLPPQTRRLINLktldLSHNPLELFQLRQlpslQSLEVLKMSGTQRTLLnfptsiDSLANLCELDLS 227
Cdd:cd00116   82 GLQELDLSDNAL--GPDGCGVLESL----LRSSSLQELKLNN----NGLGDRGLRLLAKGLK------DLPPALEKLVLG 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660   228 HNSLP-----KLPDCVYNVVTLVRLNLSDNELTE-----LTAGVELWQRLESLNLSRNQL-----VALPAALCKLPKLRR 292
Cdd:cd00116  146 RNRLEgasceALAKALRANRDLKELNLANNGIGDagiraLAEGLKANCNLEVLDLNNNGLtdegaSALAETLASLKSLEV 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660   293 LLVNDNKLNFEGIpsgigklgalevfsAAnnLLEMVPEGLCRcgaLKQLNLSCNRlITLPDAIHLLEGLDQ------LDL 366
Cdd:cd00116  226 LNLGDNNLTDAGA--------------AA--LASALLSPNIS---LLTLSLSCND-ITDDGAKDLAEVLAEkeslleLDL 285


                 ...
gi 3004660   367 RNN 369
Cdd:cd00116  286 RGN 288
LRR_8 pfam13855
Leucine rich repeat;
101-159 2.88e-11

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 59.85  E-value: 2.88e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660     101 ELTTLDLSHNKLKEVPEG-LERAKNLIVLNLSNNQIESIPTPLFIHLTDLLFLDLSHNRL 159
Cdd:pfam13855    2 NLRSLDLSNNRLTSLDDGaFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 501-592 7.00e-11

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


Pssm-ID: 200436  Cd Length: 88  Bit Score: 59.69  E-value: 7.00e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660   501 IWEIENFLPNKIEEVV--HGKFYEGDCYIVlktkfdDLGLldwEIFFWIGNEATLDKRACAAIHAVNLRNFLGARCRTVR 578
Cdd:cd11280    4 LYRVRGSKAIEIEEVPlaSSSLDSDDVFVL------DTGS---EIYIWQGRASSQAELAAAALLAKELDEERKGKPEIVR 74

                         90
                 ....*....|....
gi 3004660   579 EEQGDESEQFLSLF 592
Cdd:cd11280   75 IRQGQEPREFWSLF 88
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 731-826 7.28e-11

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


Pssm-ID: 200436  Cd Length: 88  Bit Score: 59.69  E-value: 7.28e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660   731 QPRLYQVqlgMGYLELPQVELPeqkLCHTLLNSKHVYILDCYTDLFVWFGKKSTRLVRAAAVKLSRELFNMmdRPDYALV 810
Cdd:cd11280    1 PPRLYRV---RGSKAIEIEEVP---LASSSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKELDEE--RKGKPEI 72

                         90
                 ....*....|....*.
gi 3004660   811 MRVPEGNEMQIFRTKF 826
Cdd:cd11280   73 VRIRQGQEPREFWSLF 88
LRR_8 pfam13855
Leucine rich repeat;
124-182 8.77e-11

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 58.69  E-value: 8.77e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660     124 NLIVLNLSNNQIESIPTPLFIHLTDLLFLDLSHNRLETLPPQT-RRLINLKTLDLSHNPL 182
Cdd:pfam13855    2 NLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAfSGLPSLRYLDLSGNRL 61
Gelsolin pfam00626
Gelsolin repeat;
517-589 8.82e-11

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 58.86  E-value: 8.82e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3004660     517 HGKFYEGDCYIVLKTKfddlglldwEIFFWIGNEATLDKRACAAIHAVNLR-NFLGARCRTVREEQGDESEQFL 589
Cdd:pfam00626   12 QESLNSGDCYLLDNGF---------TIFLWVGKGSSLLEKLFAALLAAQLDdDERFPLPEVIRVPQGKEPARFL 76
Gelsolin pfam00626
Gelsolin repeat;
1165-1242 9.63e-11

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 58.86  E-value: 9.63e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3004660    1165 TVAEKCADFCQDDLADDDIMILDNGEHVFLWMGPRCSEVEVKLAYKSAQVYIQHMRIKQPErprkLFLTMKNKESRRF 1242
Cdd:pfam00626    2 FVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDERFPLPE----VIRVPQGKEPARF 75
PLN03210 PLN03210
Resistant to P. syringae 6; Provisional
 94-353 1.66e-10

Resistant to P. syringae 6; Provisional


Pssm-ID: 215633 [Multi-domain]  Cd Length: 1153  Bit Score: 65.67  E-value: 1.66e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660     94 PELFHLEELTTLDLSHNKLKEVPEGLERAKNLIVLNL--SNNQIEsipTPLFIHLTDLLFLDLSH-NRLETLPPQTRRLI 170
Cdd:PLN03210  605 PSNFRPENLVKLQMQGSKLEKLWDGVHSLTGLRNIDLrgSKNLKE---IPDLSMATNLETLKLSDcSSLVELPSSIQYLN 681

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660    171 NLKTLDLSHnpleLFQLRQLPS---LQSLEVLKMSGTQRtLLNFPtsiDSLANLCELDLSHNSLPKLPdcvynvvTLVRL 247
Cdd:PLN03210  682 KLEDLDMSR----CENLEILPTginLKSLYRLNLSGCSR-LKSFP---DISTNISWLDLDETAIEEFP-------SNLRL 746

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660    248 -NLSDNELTELTAGvELWQRLESLNlsrnqlvalPAALCKLPKLRRLLVNDNKLNFEgIPSGIGKLGALEVFSAANNL-L 325
Cdd:PLN03210  747 eNLDELILCEMKSE-KLWERVQPLT---------PLMTMLSPSLTRLFLSDIPSLVE-LPSSIQNLHKLEHLEIENCInL 815

                         250       260
                  ....*....|....*....|....*....
gi 3004660    326 EMVPEGLcRCGALKQLNLS-CNRLITLPD 353
Cdd:PLN03210  816 ETLPTGI-NLESLESLDLSgCSRLRTFPD 843
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 629-707 6.43e-10

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: 57.25  E-value: 6.43e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660   629 TIHLEPVAPAITSLDPRHAFVLDLGTHIYIWMGERSKNTLNSKARLMAEKISKTERKNKCEIQL--ERQGEESAEFWQGL 706
Cdd:cd11289   12 NVRAREVELSWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGIRDERRLGRAKVIVldEGDTNESPEFWKVL 91


                 .
gi 3004660   707 G 707
Cdd:cd11289   92 G 92
Gelsolin pfam00626
Gelsolin repeat;
633-703 7.35e-10

Gelsolin repeat;


Pssm-ID: 395501 [Multi-domain]  Cd Length: 76  Bit Score: 56.55  E-value: 7.35e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3004660     633 EPVAPAITSLDPRHAFVLDLGTHIYIWMGERSKNTLNSKARLMAEKISKTERKNKCEIQLERQGEESAEFW 703
Cdd:pfam00626    6 PPVPLSQESLNSGDCYLLDNGFTIFLWVGKGSSLLEKLFAALLAAQLDDDERFPLPEVIRVPQGKEPARFL 76
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 22-277 4.77e-09

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


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 59.29  E-value: 4.77e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660    22 PSSMRQMSRVQWLTLDRTQL----AEIPEELGHLQKLEHLSLNHNRLEK-----IFGELTELSC-LRSLDLRHNQLKNSG 91
Cdd:cd00116   74 LQGLTKGCGLQELDLSDNALgpdgCGVLESLLRSSSLQELKLNNNGLGDrglrlLAKGLKDLPPaLEKLVLGRNRLEGAS 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660    92 IPP---ELFHLEELTTLDLSHNKLKE-----VPEGLERAKNLIVLNLSNNQIesiptplfihlTDLLFLDLShnrlETLP 163
Cdd:cd00116  154 CEAlakALRANRDLKELNLANNGIGDagiraLAEGLKANCNLEVLDLNNNGL-----------TDEGASALA----ETLA 218

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660   164 pqtrRLINLKTLDLSHNPLELFQLRQLpslqsleVLKMSGTQRTLLNfptsidslanlceLDLSHNSLP-----KLPDCV 238
Cdd:cd00116  219 ----SLKSLEVLNLGDNNLTDAGAAAL-------ASALLSPNISLLT-------------LSLSCNDITddgakDLAEVL 274

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 3004660   239 YNVVTLVRLNLSDNELTELTAG------VELWQRLESLNLSRNQL 277
Cdd:cd00116  275 AEKESLLELDLRGNKFGEEGAQllaeslLEPGNELESLWVKDDSF 319
LRR_8 pfam13855
Leucine rich repeat;
52-112 1.71e-08

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 52.14  E-value: 1.71e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3004660      52 QKLEHLSLNHNRLEKIFGE-LTELSCLRSLDLRHNQLknSGIPPELF-HLEELTTLDLSHNKL 112
Cdd:pfam13855    1 PNLRSLDLSNNRLTSLDDGaFKGLSNLKVLDLSNNLL--TTLSPGAFsGLPSLRYLDLSGNRL 61
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 1152-1219 3.16e-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: 52.64  E-value: 3.16e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3004660  1152 TRLFRCSNERGY---YTVAEKCadFCQDDLADDDIMILDNGEHVFLWMGPRCSEVEVKLAYKSAQVYIQHM 1219
Cdd:cd11292    4 KKLYKVSDASGKlklTEVAEGS--LNQEMLDSEDCYILDCGSEIFVWVGKGASLDERKAALKNAEEFLRKK 72
PRK15387 PRK15387
type III secretion system effector E3 ubiquitin transferase SspH2;
77-321 5.75e-08

type III secretion system effector E3 ubiquitin transferase SspH2;


Pssm-ID: 185285 [Multi-domain]  Cd Length: 788  Bit Score: 57.48  E-value: 5.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660     77 LRSLDLRHNQLKNSGI-PPELFHLEELTTlDLSHnkLKEVPEGLERaknlivLNLSNNQIESIPtplfIHLTDLLFLDLS 155
Cdd:PRK15387  244 LRTLEVSGNQLTSLPVlPPGLLELSIFSN-PLTH--LPALPSGLCK------LWIFGNQLTSLP----VLPPGLQELSVS 310

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660    156 HNRLETLPPQTRRLINLktldLSHNPlelfQLRQLPSLQS-LEVLKMSGTQrtLLNFPTSIDSLANLCELDLSHNSLPKL 234
Cdd:PRK15387  311 DNQLASLPALPSELCKL----WAYNN----QLTSLPTLPSgLQELSVSDNQ--LASLPTLPSELYKLWAYNNRLTSLPAL 380

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660    235 PDCVYNVVT----LVRLNLSDNELTEL-------TAGVELWQRLESLNLSRNQLVALPAALCKLPklrrllvNDNKLNFE 303
Cdd:PRK15387  381 PSGLKELIVsgnrLTSLPVLPSELKELmvsgnrlTSLPMLPSGLLSLSVYRNQLTRLPESLIHLS-------SETTVNLE 453

                         250
                  ....*....|....*...
gi 3004660    304 GIPSGIGKLGALEVFSAA 321
Cdd:PRK15387  454 GNPLSERTLQALREITSA 471
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 40-270 1.71e-07

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


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 55.18  E-value: 1.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660    40 QLAEIPEELGHLQKLEHLSLNHNR-----LEKIFGELTELSCLRSLDLRHNQLKNSGIPPELFHLE---ELTTLDLSHNK 111
Cdd:COG5238  224 GAEILAEALKGNKSLTTLDLSNNQigdegVIALAEALKNNTTVETLYLSGNQIGAEGAIALAKALQgntTLTSLDLSVNR 303

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660   112 L-----KEVPEGLERAKNLIVLNLSNNQI-ESIPTPLFIHLtdllfldlshnrletlppQTRRliNLKTLDLSHNPLelf 185
Cdd:COG5238  304 IgdegaIALAEGLQGNKTLHTLNLAYNGIgAQGAIALAKAL------------------QENT--TLHSLDLSDNQI--- 360

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660   186 qlrqlpSLQSLEVLKmsgtqrtllnfpTSIDSLANLCELDLSHNSLPK-----LPDCVyNVVTLVRLNLSDNELTELT-- 258
Cdd:COG5238  361 ------GDEGAIALA------------KYLEGNTTLRELNLGKNNIGKqgaeaLIDAL-QTNRLHTLILDGNLIGAEAqq 421

                        250
                 ....*....|..
gi 3004660   259 AGVELWQRLESL 270
Cdd:COG5238  422 RLEQLLERIKSV 433
LRR_8 pfam13855
Leucine rich repeat;
29-87 1.98e-07

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 49.06  E-value: 1.98e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3004660      29 SRVQWLTLDRTQLAEIPEE-LGHLQKLEHLSLNHNRLEKIF-GELTELSCLRSLDLRHNQL 87
Cdd:pfam13855    1 PNLRSLDLSNNRLTSLDDGaFKGLSNLKVLDLSNNLLTTLSpGAFSGLPSLRYLDLSGNRL 61
PLN03210 PLN03210
Resistant to P. syringae 6; Provisional
 29-256 2.12e-07

Resistant to P. syringae 6; Provisional


Pssm-ID: 215633 [Multi-domain]  Cd Length: 1153  Bit Score: 55.65  E-value: 2.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660     29 SRVQWLTLDRTQLAEIPEELgHLQKLEHLSLNHNRLEKIFGELTELSCLRSLdlrhnqlknsgIPPelfhleELTTLDLS 108
Cdd:PLN03210  725 TNISWLDLDETAIEEFPSNL-RLENLDELILCEMKSEKLWERVQPLTPLMTM-----------LSP------SLTRLFLS 786

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660    109 HN-KLKEVPEGLERAKNLIVLNLSN-NQIESIPTPlfIHLTDLLFLDLSH-NRLETLPpqtrrlinlktlDLSHNPLELF 185
Cdd:PLN03210  787 DIpSLVELPSSIQNLHKLEHLEIENcINLETLPTG--INLESLESLDLSGcSRLRTFP------------DISTNISDLN 852

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3004660    186 qlrqLPSLQSLEVlkmsgtqrtllnfPTSIDSLANLCELDLSH-NSLPKLPDCVYNVVTLVRLNLSD-NELTE 256
Cdd:PLN03210  853 ----LSRTGIEEV-------------PWWIEKFSNLSFLDMNGcNNLQRVSLNISKLKHLETVDFSDcGALTE 908
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 731-830 3.28e-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: 49.60  E-value: 3.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660   731 QPRLYQVQLGMGYLELPQVelpeQKLCHTLLNSKHVYILDCYTDLFVWFGKKSTRLVRAAAVKLSRELFNMM-------D 803
Cdd:cd11291    1 KPRLFRCSNESGFFKVEEI----SDFSQDDLDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYIETDplgrskpR 76

                         90       100
                 ....*....|....*....|....*..
gi 3004660   804 RPdyalVMRVPEGNEMQIFRTKFAGWD 830
Cdd:cd11291   77 TP----IYLVKQGNEPPTFTGYFHAWD 99
PLN03210 PLN03210
Resistant to P. syringae 6; Provisional
 37-333 9.97e-07

Resistant to P. syringae 6; Provisional


Pssm-ID: 215633 [Multi-domain]  Cd Length: 1153  Bit Score: 53.34  E-value: 9.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660     37 DRTQLAEIPEELGHLQKLEhlslnhnrlekifgeltelsclrslDLRHNQLKNSGIPPELFHLEELTTLDLSH-NKLKEV 115
Cdd:PLN03210  666 DCSSLVELPSSIQYLNKLE-------------------------DLDMSRCENLEILPTGINLKSLYRLNLSGcSRLKSF 720

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660    116 PeglERAKNLIVLNLSNNQIESIPTPLfiHLTDLLFLDLSHNRLETLPPQTRRLINLKTLdLSHNPLELF-----QLRQL 190
Cdd:PLN03210  721 P---DISTNISWLDLDETAIEEFPSNL--RLENLDELILCEMKSEKLWERVQPLTPLMTM-LSPSLTRLFlsdipSLVEL 794

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660    191 PS----LQSLEVLKMSGTqRTLLNFPTSIDsLANLCELDLSHNS-LPKLPDCVYNVVTlvrLNLSDNELTELTAGVELWQ 265
Cdd:PLN03210  795 PSsiqnLHKLEHLEIENC-INLETLPTGIN-LESLESLDLSGCSrLRTFPDISTNISD---LNLSRTGIEEVPWWIEKFS 869

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3004660    266 RLESLNLSR-NQLVALPAALCKLPKLRRLLVND----NKLNFEGIPSgigklgalEVFSAANNLLEMVPEGLC 333
Cdd:PLN03210  870 NLSFLDMNGcNNLQRVSLNISKLKHLETVDFSDcgalTEASWNGSPS--------EVAMATDNIHSKLPSTVC 934
gelsolin_S4_like cd11293
Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins; ...
 900-1015 1.02e-06

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: 48.42  E-value: 1.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660   900 ENKKFVRLPEEELGRFYTGECYVFLCRYcipieePENGSEDganpaadvskssannqpedeiqCVVYFWQGRNAgNMGWL 979
Cdd:cd11293   15 ENDEKVPVPKEEYGQFYGGDCYIVLYTY------QGGGKEE----------------------HILYFWQGRHS-SQDER 65

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 3004660   980 TFTFTLQKKFKAMFGEELEVVRIFQQQENLKFMSHF 1015
Cdd:cd11293   66 AAAALLTVELDEELKGRAVQVRVVQGKEPPHFLALF 101
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
230-417 1.12e-06

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 53.16  E-value: 1.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660    230 SLPKLPDCVYNVVTlvRLNLSDNELTELTAGVElwQRLESLNLSRNQLVALPAALckLPKLRRLLVNDNKLNF--EGIPS 307
Cdd:PRK15370  168 AVQRMRDCLKNNKT--ELRLKILGLTTIPACIP--EQITTLILDNNELKSLPENL--QGNIKTLYANSNQLTSipATLPD 241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660    308 GIGklgalEVFSAANNLLEMvPEGLCrcGALKQLNLSCNRLITLPDaiHLLEGLDQLDLRNNPELVMPPK-PSEASK--- 383
Cdd:PRK15370  242 TIQ-----EMELSINRITEL-PERLP--SALQSLDLFHNKISCLPE--NLPEELRYLSVYDNSIRTLPAHlPSGITHlnv 311

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 3004660    384 -ATSLEFYNIDFSLQTQLRLAGAAVPPSMPSSATP 417
Cdd:PRK15370  312 qSNSLTALPETLPPGLKTLEAGENALTSLPASLPP 346
LRR_8 pfam13855
Leucine rich repeat;
243-300 1.27e-06

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 46.75  E-value: 1.27e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660     243 TLVRLNLSDNELTELTAGVEL-WQRLESLNLSRNQLVAL-PAALCKLPKLRRLLVNDNKL 300
Cdd:pfam13855    2 NLRSLDLSNNRLTSLDDGAFKgLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
LRR_8 pfam13855
Leucine rich repeat;
152-231 1.54e-06

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 46.36  E-value: 1.54e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660     152 LDLSHNRLETLPPQT-RRLINLKTLDLSHNplelfqlrqlpSLQSLEvlkmsgtqrtllnfPTSIDSLANLCELDLSHNS 230
Cdd:pfam13855    6 LDLSNNRLTSLDDGAfKGLSNLKVLDLSNN-----------LLTTLS--------------PGAFSGLPSLRYLDLSGNR 60


                   .
gi 3004660     231 L 231
Cdd:pfam13855   61 L 61
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 35-279 2.30e-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: 51.71  E-value: 2.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660    35 TLDRTQLAEIPEELGHlQKLEHLSLNHNRLE----KIFGE-LTELSCLRSLDLRHNQLKNSG---IPPELFHLEELTTLD 106
Cdd:COG5238  164 RLGLLAAISMAKALQN-NSVETVYLGCNQIGdegiEELAEaLTQNTTVTTLWLKRNPIGDEGaeiLAEALKGNKSLTTLD 242

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660   107 LSHNKLKEvpEGLER-AKNLIvlnlSNNQIESiptplfihltdllfLDLSHNRL-----ETLPPQTRRLINLKTLDLSHN 180
Cdd:COG5238  243 LSNNQIGD--EGVIAlAEALK----NNTTVET--------------LYLSGNQIgaegaIALAKALQGNTTLTSLDLSVN 302

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660   181 PLELFQLRQL-PSLQ---SLEVLKMSGTQ------RTLLnfpTSIDSLANLCELDLSHNSLPK-----LPDCVYNVVTLV 245
Cdd:COG5238  303 RIGDEGAIALaEGLQgnkTLHTLNLAYNGigaqgaIALA---KALQENTTLHSLDLSDNQIGDegaiaLAKYLEGNTTLR 379

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 3004660   246 RLNLSDNELTELTAgVELWQ-----RLESLNLSRNQLVA 279
Cdd:COG5238  380 ELNLGKNNIGKQGA-EALIDalqtnRLHTLILDGNLIGA 417
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 1065-1131 4.50e-06

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: 46.47  E-value: 4.50e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3004660  1065 LNSAFCYILhvpfetedDSQSGIvYVWIGSKACNEEAKLVQDIAEQMFNS----PWVSLQILNEGDEPENF 1131
Cdd:cd11292   31 LDSEDCYIL--------DCGSEI-FVWVGKGASLDERKAALKNAEEFLRKkkrpPYTQVTRVTEGGESALF 92
PRK15387 PRK15387
type III secretion system effector E3 ubiquitin transferase SspH2;
67-258 5.97e-06

type III secretion system effector E3 ubiquitin transferase SspH2;


Pssm-ID: 185285 [Multi-domain]  Cd Length: 788  Bit Score: 50.55  E-value: 5.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660     67 IFG-ELTELSCL----RSLDLRHNQLKN-SGIPPELFHL----EELTTLdlshnklKEVPEGLERaknlivLNLSNNQIE 136
Cdd:PRK15387  289 IFGnQLTSLPVLppglQELSVSDNQLASlPALPSELCKLwaynNQLTSL-------PTLPSGLQE------LSVSDNQLA 355

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660    137 SIPT-PlfihlTDLLFLDLSHNRLETLPPQTRrliNLKTLDLSHNplelfQLRQLPSLQS-LEVLKMSGTQRTLLNFPTS 214
Cdd:PRK15387  356 SLPTlP-----SELYKLWAYNNRLTSLPALPS---GLKELIVSGN-----RLTSLPVLPSeLKELMVSGNRLTSLPMLPS 422

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 3004660    215 idslaNLCELDLSHNSLPKLPDCVYNVVTLVRLNLSDNELTELT 258
Cdd:PRK15387  423 -----GLLSLSVYRNQLTRLPESLIHLSSETTVNLEGNPLSERT 461
gelsolin_S2_like cd11289
Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins; ...
 731-798 8.13e-06

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: 45.31  E-value: 8.13e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3004660   731 QPRLYQVQlGMGYLELPQVELpeqklCHTLLNSKHVYILDCYTDLFVWFGKKSTRLVRAAAVKLSREL 798
Cdd:cd11289    1 KPRLLHVK-GRRNVRAREVEL-----SWSSLNSGDVFILDLGSTIYQWNGSKSNRFEKAKAMQLAQGI 62
gelsolin_like cd11280
Tandemly repeated domains found in gelsolin, severin, villin, and related proteins; Gelsolin ...
 1152-1252 2.21e-05

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


Pssm-ID: 200436  Cd Length: 88  Bit Score: 44.28  E-value: 2.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660  1152 TRLFRCSNeRGYYTVAEKCADFcqDDLADDDIMILDNGEHVFLWMGPRCSEVEVKLAYKSAQVYIQHMRIK-QPERPRkl 1230
Cdd:cd11280    2 PRLYRVRG-SKAIEIEEVPLAS--SSLDSDDVFVLDTGSEIYIWQGRASSQAELAAAALLAKELDEERKGKpEIVRIR-- 76

                         90       100
                 ....*....|....*....|..
gi 3004660  1231 fltmKNKESRRFtkcfhgWSAF 1252
Cdd:cd11280   77 ----QGQEPREF------WSLF 88
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 123-164 2.35e-05

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: 42.62  E-value: 2.35e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 3004660     123 KNLIVLNLSNNQIESIptPLFIHLTDLLFLDLSHN-RLETLPP 164
Cdd:pfam12799    1 PNLEVLDLSNNQITDI--PPLAKLPNLETLDLSGNnKITDLSD 41
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 38-304 2.66e-05

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


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 48.25  E-value: 2.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660    38 RTQLAEIP-----EELGHLQKLEHLSLNHNRLEKI----FGELTELSCLRSLDLR--HNQLKNSGIPPELFHLEELTTLD 106
Cdd:COG5238   66 EGQGDPGLnpvalEKAAEAFPTQLLVVDWEGAEEVspvaLAETATAVATPPPDLRriMAKTLEDSLILYLALPRRINLIQ 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660   107 LSHNKLKEVPEGLERAKNLIVLnLSNNQIESIPTPLFIHLTDLLFLDLSHNRLETLPPQTRRLINLKTLDLSHNPL---- 182
Cdd:COG5238  146 VLKDPLGGNAVHLLGLAARLGL-LAAISMAKALQNNSVETVYLGCNQIGDEGIEELAEALTQNTTVTTLWLKRNPIgdeg 224

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660   183 --ELFQ-LRQLPSLQSLEvlkMSGTQ---RTLLNFPTSIDSLANLCELDLSHN--------SLPKLpdcVYNVVTLVRLN 248
Cdd:COG5238  225 aeILAEaLKGNKSLTTLD---LSNNQigdEGVIALAEALKNNTTVETLYLSGNqigaegaiALAKA---LQGNTTLTSLD 298

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3004660   249 LSDNELTE-----LTAGVELWQRLESLNLSRNQL-----VALPAALCKLPKLRRLLVNDNKLNFEG 304
Cdd:COG5238  299 LSVNRIGDegaiaLAEGLQGNKTLHTLNLAYNGIgaqgaIALAKALQENTTLHSLDLSDNQIGDEG 364
PLN03150 PLN03150
hypothetical protein; Provisional
 175-291 7.29e-05

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 47.12  E-value: 7.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660    175 LDLSHNPLELFQLRQLPSLQSLEVLKMSGtQRTLLNFPTSIDSLANLCELDLSHNSLP-KLPDCVYNVVTLVRLNLSDNE 253
Cdd:PLN03150  423 LGLDNQGLRGFIPNDISKLRHLQSINLSG-NSIRGNIPPSLGSITSLEVLDLSYNSFNgSIPESLGQLTSLRILNLNGNS 501

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 3004660    254 LT-ELTA--GVELWQRlESLNLSRNqlvalpAALCKLPKLR 291
Cdd:PLN03150  502 LSgRVPAalGGRLLHR-ASFNFTDN------AGLCGIPGLR 535
gelsolin_S5_like cd11288
Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins; ...
 731-818 8.10e-05

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: 42.60  E-value: 8.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660   731 QPRLYQVQlGMGYLELPQVELPEQKlchTLLNSKHVYILDCYTDLFVWFGKKSTRLVRAAAVKLSRELFnmmdrPDYALV 810
Cdd:cd11288    2 PTRLFQVR-GNGSGNTRAVEVDADA---SSLNSNDVFVLKTPSSVYLWVGKGSSEDERELAKDVASFLK-----PKASLQ 72


                 ....*...
gi 3004660   811 MrVPEGNE 818
Cdd:cd11288   73 E-VAEGSE 79
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 102-140 1.32e-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: 40.69  E-value: 1.32e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 3004660     102 LTTLDLSHNKLKEVPeGLERAKNLIVLNLS-NNQIESIPT 140
Cdd:pfam12799    3 LEVLDLSNNQITDIP-PLAKLPNLETLDLSgNNKITDLSD 41
PLN03150 PLN03150
hypothetical protein; Provisional
 57-133 2.25e-04

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 45.58  E-value: 2.25e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3004660     57 LSLNHNRLEKIFG-ELTELSCLRSLDLRHNQLKnSGIPPELFHLEELTTLDLSHNKLK-EVPEGLERAKNLIVLNLSNN 133
Cdd:PLN03150  423 LGLDNQGLRGFIPnDISKLRHLQSINLSGNSIR-GNIPPSLGSITSLEVLDLSYNSFNgSIPESLGQLTSLRILNLNGN 500
PLN03150 PLN03150
hypothetical protein; Provisional
 105-182 2.64e-04

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 45.19  E-value: 2.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660    105 LDLSHNKLK-EVPEGLERAKNLIVLNLSNNQIESIPTPLFIHLTDLLFLDLSHNRLETLPPQTR-RLINLKTLDLSHNPL 182
Cdd:PLN03150  423 LGLDNQGLRgFIPNDISKLRHLQSINLSGNSIRGNIPPSLGSITSLEVLDLSYNSFNGSIPESLgQLTSLRILNLNGNSL 502
PLN03150 PLN03150
hypothetical protein; Provisional
 34-119 3.47e-04

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 44.81  E-value: 3.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660     34 LTLDRTQL-AEIPEELGHLQKLEHLSLNHNRLE-KIFGELTELSCLRSLDLRHNQLkNSGIPPELFHLEELTTLDLSHNK 111
Cdd:PLN03150  423 LGLDNQGLrGFIPNDISKLRHLQSINLSGNSIRgNIPPSLGSITSLEVLDLSYNSF-NGSIPESLGQLTSLRILNLNGNS 501


                  ....*....
gi 3004660    112 LK-EVPEGL 119
Cdd:PLN03150  502 LSgRVPAAL 510
LRR_8 pfam13855
Leucine rich repeat;
220-277 3.90e-04

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 39.82  E-value: 3.90e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3004660     220 NLCELDLSHNSLPKL-PDCVYNVVTLVRLNLSDNELTELTAGVeLWQ--RLESLNLSRNQL 277
Cdd:pfam13855    2 NLRSLDLSNNRLTSLdDGAFKGLSNLKVLDLSNNLLTTLSPGA-FSGlpSLRYLDLSGNRL 61
gelsolin_S6_like cd11291
Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins; ...
 642-702 7.81e-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: 39.97  E-value: 7.81e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3004660   642 LDPRHAFVLDLGTHIYIWMGERSKNTLNSKARLMAEKISKTER----KNKCEIQLERQGEESAEF 702
Cdd:cd11291   27 LDTDDIMLLDTGDEVFVWVGSESSDEEKKEALTSAKKYIETDPlgrsKPRTPIYLVKQGNEPPTF 91
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 52-87 1.22e-03

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


Pssm-ID: 463713 [Multi-domain]  Cd Length: 44  Bit Score: 37.61  E-value: 1.22e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 3004660      52 QKLEHLSLNHNRLEKIfGELTELSCLRSLDLRHNQL 87
Cdd:pfam12799    1 PNLEVLDLSNNQITDI-PPLAKLPNLETLDLSGNNK 35
LRR_8 pfam13855
Leucine rich repeat;
315-370 2.41e-03

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 37.50  E-value: 2.41e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 3004660     315 LEVFSAANNLLEMVPEG-LCRCGALKQLNLSCNRLITL-PDAIHLLEGLDQLDLRNNP 370
Cdd:pfam13855    3 LRSLDLSNNRLTSLDDGaFKGLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNR 60
PLN03150 PLN03150
hypothetical protein; Provisional
 234-310 2.66e-03

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 42.11  E-value: 2.66e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3004660    234 LPDCVYNVVTLVRLNLSDNELT-ELTAGVELWQRLESLNLSRNQLV-ALPAALCKLPKLRRLLVNDNKLNFEgIPSGIG 310
Cdd:PLN03150  434 IPNDISKLRHLQSINLSGNSIRgNIPPSLGSITSLEVLDLSYNSFNgSIPESLGQLTSLRILNLNGNSLSGR-VPAALG 511
gelsolin_S3_like cd11292
Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins; ...
 523-594 4.93e-03

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: 37.61  E-value: 4.93e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3004660   523 GDCYIVlktkfdDLGLldwEIFFWIGNEATLDKRACAAIHAvnlRNFLGA--RCRT---VREEQGDESEQFLSLFET 594
Cdd:cd11292   34 EDCYIL------DCGS---EIFVWVGKGASLDERKAALKNA---EEFLRKkkRPPYtqvTRVTEGGESALFKSKFAN 98
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 142-361 5.06e-03

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: 40.93  E-value: 5.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660   142 LFIHLTDLLFLDLSHNR--LETLPPQTRRLINLKT--LDLSHNPLelfqlrQLPSLQSLEVL-KMSGTQRTLLNFPTSID 216
Cdd:COG5238   82 AEAFPTQLLVVDWEGAEevSPVALAETATAVATPPpdLRRIMAKT------LEDSLILYLALpRRINLIQVLKDPLGGNA 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660   217 SLANLCELDLSHNSLPKLPDCVYNVvTLVRLNLSDNELtELTAGVELWQRLE------SLNLSRN-----QLVALPAALC 285
Cdd:COG5238  156 VHLLGLAARLGLLAAISMAKALQNN-SVETVYLGCNQI-GDEGIEELAEALTqnttvtTLWLKRNpigdeGAEILAEALK 233

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3004660   286 KLPKLRRLLVNDNKLNFEGIpSGIGKlgALEVFSAANNL-----------LEMVPEGLCRCGALKQLNLSCNRlITLPDA 354
Cdd:COG5238  234 GNKSLTTLDLSNNQIGDEGV-IALAE--ALKNNTTVETLylsgnqigaegAIALAKALQGNTTLTSLDLSVNR-IGDEGA 309


                 ....*..
gi 3004660   355 IHLLEGL 361
Cdd:COG5238  310 IALAEGL 316
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 77-112 8.12e-03

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


Pssm-ID: 463713 [Multi-domain]  Cd Length: 44  Bit Score: 35.30  E-value: 8.12e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 3004660      77 LRSLDLRHNQLKNsgIPPeLFHLEELTTLDLSHNKL 112
Cdd:pfam12799    3 LEVLDLSNNQITD--IPP-LAKLPNLETLDLSGNNK 35
 
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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