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Conserved domains on  [gi|1958669085|ref|XP_038945506|]
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leucine-rich repeat and calponin homology domain-containing protein 4 isoform X2 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CH_LRCH4 cd21273
calponin homology (CH) domain found in leucine-rich repeat and calponin homology ...
 544-650 1.78e-52

calponin homology (CH) domain found in leucine-rich repeat and calponin homology domain-containing protein 4; Leucine-rich repeat and calponin homology domain-containing protein 4 (LRCH4), also called leucine-rich repeat neuronal protein 4, or leucine-rich neuronal protein, acts as a novel Toll-like receptor (TLR) accessory protein that regulates the innate immune response. LRCH4 contains a single copy of the CH domain at the C-terminus. CH domains are actin filament (F-actin) binding motifs.


:

Pssm-ID: 409122  Cd Length: 109  Bit Score: 176.63  E-value: 1.78e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085 544 EEKELISQLRQILESRLQQPLPEDLAEALANGVILCQLANQLRPRSVPFIHVPSPAVPKLSALKSRKNVENFLEACRKMG 623
Cdd:cd21273     1 DEKELRAQLRKTLESRLKVTLPEDLAEALSNGAVLCQLANQLRPRSVSIIHVPSPAVPKLSKAKCRKNVENFIEACRKMG 80

                          90       100
                  ....*....|....*....|....*...
gi 1958669085 624 VPEADLCSPSDLLR-GTAQGLQTILEAV 650
Cdd:cd21273    81 VPEVDLCSPSDVLLqGPAAVLRTVLALL 108
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
66-250 8.35e-41

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


:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 154.32  E-value: 8.35e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085  66 DLSDITQAAPSGPLLSLDLSRNRFPEVPEAACQLVSLEGLSLYHNCLRCLNPALGNLTALTYLNLSRNQLSSLPPYICQL 145
Cdd:COG4886   102 DLSGNEELSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNL 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085 146 P-LRVLIISNNKLGALPPDISTLGSLRQLDVSSNELQSLPVELCSLRSLRDLNVRRNQLSTLPdELGDLP-LVRLDFSCN 223
Cdd:COG4886   182 TnLKELDLSNNQITDLPEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTDLP-ELGNLTnLEELDLSNN 260

                         170       180
                  ....*....|....*....|....*..
gi 1958669085 224 RVSRIPVSfCRLRHLQVILLDSNPLQS 250
Cdd:COG4886   261 QLTDLPPL-ANLTNLKTLDLSNNQLTD 286
PRK10263 super family cl35903
DNA translocase FtsK; Provisional
 341-505 2.28e-03

DNA translocase FtsK; Provisional


The actual alignment was detected with superfamily member PRK10263:

Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 41.61  E-value: 2.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085  341 AREPRGPRQPREDGSGDGDLEQIDFIDSHVPGDDEQSAAEEPLPSELSLAAGDMERPSSSRREEPAGEERR--RPDTLHL 418
Cdd:PRK10263   430 QQPYYAPAPEQPVAGNAWQAEEQQSTFAPQSTYQTEQTYQQPAAQEPLYQQPQPVEQQPVVEPEPVVEETKpaRPPLYYF 509

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085  419 WQERERRL--QQQSGAW-----GPSKKDSIPKRGIRATGAGASAPSTQTACNGP----PKSSAAQLGVSGEQGAPTL-PS 486
Cdd:PRK10263   510 EEVEEKRAreREQLAAWyqpipEPVKEPEPIKSSLKAPSVAAVPPVEAAAAVSPlasgVKKATLATGAAATVAAPVFsLA 589

                          170       180
                   ....*....|....*....|
gi 1958669085  487 TSQDPLP-VSGPVTAPVPRP 505
Cdd:PRK10263   590 NSGGPRPqVKEGIGPQLPRP 609
 
Name Accession Description Interval E-value
CH_LRCH4 cd21273
calponin homology (CH) domain found in leucine-rich repeat and calponin homology ...
 544-650 1.78e-52

calponin homology (CH) domain found in leucine-rich repeat and calponin homology domain-containing protein 4; Leucine-rich repeat and calponin homology domain-containing protein 4 (LRCH4), also called leucine-rich repeat neuronal protein 4, or leucine-rich neuronal protein, acts as a novel Toll-like receptor (TLR) accessory protein that regulates the innate immune response. LRCH4 contains a single copy of the CH domain at the C-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409122  Cd Length: 109  Bit Score: 176.63  E-value: 1.78e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085 544 EEKELISQLRQILESRLQQPLPEDLAEALANGVILCQLANQLRPRSVPFIHVPSPAVPKLSALKSRKNVENFLEACRKMG 623
Cdd:cd21273     1 DEKELRAQLRKTLESRLKVTLPEDLAEALSNGAVLCQLANQLRPRSVSIIHVPSPAVPKLSKAKCRKNVENFIEACRKMG 80

                          90       100
                  ....*....|....*....|....*...
gi 1958669085 624 VPEADLCSPSDLLR-GTAQGLQTILEAV 650
Cdd:cd21273    81 VPEVDLCSPSDVLLqGPAAVLRTVLALL 108
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
66-250 8.35e-41

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 154.32  E-value: 8.35e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085  66 DLSDITQAAPSGPLLSLDLSRNRFPEVPEAACQLVSLEGLSLYHNCLRCLNPALGNLTALTYLNLSRNQLSSLPPYICQL 145
Cdd:COG4886   102 DLSGNEELSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNL 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085 146 P-LRVLIISNNKLGALPPDISTLGSLRQLDVSSNELQSLPVELCSLRSLRDLNVRRNQLSTLPdELGDLP-LVRLDFSCN 223
Cdd:COG4886   182 TnLKELDLSNNQITDLPEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTDLP-ELGNLTnLEELDLSNN 260

                         170       180
                  ....*....|....*....|....*..
gi 1958669085 224 RVSRIPVSfCRLRHLQVILLDSNPLQS 250
Cdd:COG4886   261 QLTDLPPL-ANLTNLKTLDLSNNQLTD 286
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
46-229 8.49e-16

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 81.28  E-value: 8.49e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085  46 TLNLSNRRLKHFPRG--------AARSYDLSDITQAAPSgPLLSLDLSRNRFPEVPEaacQLVS-LEGLSLYHNCLRCLN 116
Cdd:PRK15370  203 TLILDNNELKSLPENlqgniktlYANSNQLTSIPATLPD-TIQEMELSINRITELPE---RLPSaLQSLDLFHNKISCLP 278

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085 117 PALGNltALTYLNLSRNQLSSLPPYicqLPLRV--LIISNNKLGALPPDISTlgSLRQLDVSSNELQSLPVELCSlrSLR 194
Cdd:PRK15370  279 ENLPE--ELRYLSVYDNSIRTLPAH---LPSGIthLNVQSNSLTALPETLPP--GLKTLEAGENALTSLPASLPP--ELQ 349

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1958669085 195 DLNVRRNQLSTLPDELGDlPLVRLDFSCNRVSRIP 229
Cdd:PRK15370  350 VLDVSKNQITVLPETLPP-TITTLDVSRNALTNLP 383
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 546-638 6.28e-14

Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 68.11  E-value: 6.28e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085  546 KELISQLRQILESRLQQPLpEDLAEALANGVILCQLANQLRPRSVPFIHVPspavPKLSALKSRKNVENFLEACRKMGvP 625
Cdd:smart00033   1 KTLLRWVNSLLAEYDKPPV-TNFSSDLKDGVALCALLNSLSPGLVDKKKVA----ASLSRFKKIENINLALSFAEKLG-G 74

                           90
                   ....*....|...
gi 1958669085  626 EADLCSPSDLLRG 638
Cdd:smart00033  75 KVVLFEPEDLVEG 87
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 79-207 6.02e-13

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


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 68.66  E-value: 6.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085  79 LLSLDLSRNRFPEVPEAACqLVSLEGLSLYHNCLRCLNpALGNLTALTYLNLSRNQLSSlPPYICQLP---------LRV 149
Cdd:cd21340    48 LTHLYLQNNQIEKIENLEN-LVNLKKLYLGGNRISVVE-GLENLTNLEELHIENQRLPP-GEKLTFDPrslaalsnsLRV 124

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958669085 150 LIISNNKLGALPPdISTLGSLRQLDVSSNELQSLpVELC----SLRSLRDLNVRRNQLSTLP 207
Cdd:cd21340   125 LNISGNNIDSLEP-LAPLRNLEQLDASNNQISDL-EELLdllsSWPSLRELDLTGNPVCKKP 184
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 544-635 2.10e-12

Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 63.84  E-value: 2.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085 544 EEKELISQLRQILESRLQQPLPEDLAEALANGVILCQLANQLRPRSVPFIHVpspavpKLSALKSRKNVENFLE-ACRKM 622
Cdd:pfam00307   3 LEKELLRWINSHLAEYGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKL------NKSEFDKLENINLALDvAEKKL 76

                          90
                  ....*....|...
gi 1958669085 623 GVPEADLcSPSDL 635
Cdd:pfam00307  77 GVPKVLI-EPEDL 88
LRR_8 pfam13855
Leucine rich repeat;
147-203 3.05e-08

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 50.60  E-value: 3.05e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958669085 147 LRVLIISNNKLGALPPDI-STLGSLRQLDVSSNELQSL-PVELCSLRSLRDLNVRRNQL 203
Cdd:pfam13855   3 LRSLDLSNNRLTSLDDGAfKGLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
SCP1 COG5199
Calponin [Cytoskeleton];
547-646 7.48e-05

Calponin [Cytoskeleton];


Pssm-ID: 227526 [Multi-domain]  Cd Length: 178  Bit Score: 44.14  E-value: 7.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085 547 ELISQLRQILESRLQQPL--PEDLAEALANGVILCQLANQLRPRSVPFIHVPSPAVpklsalkSRKNVENFLEACRKMGV 624
Cdd:COG5199    13 KQQKEVTLWIETVLGEKFepPGDLLSLLKDGVRLCRILNEASPLDIKYKESKMPFV-------QMENISSFINGLKKLRV 85

                          90       100
                  ....*....|....*....|....
gi 1958669085 625 PEADLCSPSDLL--RGTAQGLQTI 646
Cdd:COG5199    86 PEYELFQTNDLFeaKDLRQVVICL 109
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 341-505 2.28e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 41.61  E-value: 2.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085  341 AREPRGPRQPREDGSGDGDLEQIDFIDSHVPGDDEQSAAEEPLPSELSLAAGDMERPSSSRREEPAGEERR--RPDTLHL 418
Cdd:PRK10263   430 QQPYYAPAPEQPVAGNAWQAEEQQSTFAPQSTYQTEQTYQQPAAQEPLYQQPQPVEQQPVVEPEPVVEETKpaRPPLYYF 509

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085  419 WQERERRL--QQQSGAW-----GPSKKDSIPKRGIRATGAGASAPSTQTACNGP----PKSSAAQLGVSGEQGAPTL-PS 486
Cdd:PRK10263   510 EEVEEKRAreREQLAAWyqpipEPVKEPEPIKSSLKAPSVAAVPPVEAAAAVSPlasgVKKATLATGAAATVAAPVFsLA 589

                          170       180
                   ....*....|....*....|
gi 1958669085  487 TSQDPLP-VSGPVTAPVPRP 505
Cdd:PRK10263   590 NSGGPRPqVKEGIGPQLPRP 609
LRR smart00370
Leucine-rich repeats, outliers;
122-144 3.01e-03

Leucine-rich repeats, outliers;


Pssm-ID: 197688 [Multi-domain]  Cd Length: 24  Bit Score: 35.41  E-value: 3.01e-03
                           10        20
                   ....*....|....*....|...
gi 1958669085  122 LTALTYLNLSRNQLSSLPPYICQ 144
Cdd:smart00370   1 LPNLRELDLSNNQLSSLPPGAFQ 23
 
Name Accession Description Interval E-value
CH_LRCH4 cd21273
calponin homology (CH) domain found in leucine-rich repeat and calponin homology ...
 544-650 1.78e-52

calponin homology (CH) domain found in leucine-rich repeat and calponin homology domain-containing protein 4; Leucine-rich repeat and calponin homology domain-containing protein 4 (LRCH4), also called leucine-rich repeat neuronal protein 4, or leucine-rich neuronal protein, acts as a novel Toll-like receptor (TLR) accessory protein that regulates the innate immune response. LRCH4 contains a single copy of the CH domain at the C-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409122  Cd Length: 109  Bit Score: 176.63  E-value: 1.78e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085 544 EEKELISQLRQILESRLQQPLPEDLAEALANGVILCQLANQLRPRSVPFIHVPSPAVPKLSALKSRKNVENFLEACRKMG 623
Cdd:cd21273     1 DEKELRAQLRKTLESRLKVTLPEDLAEALSNGAVLCQLANQLRPRSVSIIHVPSPAVPKLSKAKCRKNVENFIEACRKMG 80

                          90       100
                  ....*....|....*....|....*...
gi 1958669085 624 VPEADLCSPSDLLR-GTAQGLQTILEAV 650
Cdd:cd21273    81 VPEVDLCSPSDVLLqGPAAVLRTVLALL 108
CH_LRCH cd21205
calponin homology (CH) domain found in the leucine-rich repeat and calponin homology ...
 547-650 2.13e-50

calponin homology (CH) domain found in the leucine-rich repeat and calponin homology domain-containing protein family; The leucine-rich repeat and calponin homology domain-containing protein (LRCH) family includes LRCH1-4. LRCH1, also called calponin homology domain-containing protein 1, or neuronal protein 81 (NP81), acts as a negative regulator of GTPase Cdc42 by sequestering Cdc42-guanine exchange factor DOCK8. LRCH2 may play a role in the organization of the cytoskeleton. LRCH3 is part of the DISP complex and may regulate the association of septins with actin and thereby regulate the actin cytoskeleton. LRCH4, also called leucine-rich repeat neuronal protein 4, or leucine-rich neuronal protein, acts as a novel Toll-like receptor (TLR) accessory protein that regulates the innate immune response. Members of this family contain a single copy of the CH domain at the C-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409054 [Multi-domain]  Cd Length: 107  Bit Score: 170.56  E-value: 2.13e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085 547 ELISQLRQILESRLQQPLPEDLAEALANGVILCQLANQLRPRSVPFIHVPSPAVPKLSALKSRKNVENFLEACRKMGVPE 626
Cdd:cd21205     1 EQIEQLRKSIESRLKVTLPDDLGEALMDGVVLCHLANHVRPRSVPSIHVPSPAVPKLSMAKCRRNVENFLEACRKLGVPE 80

                          90       100
                  ....*....|....*....|....*.
gi 1958669085 627 ADLCSPSDLL--RGTAQGLQTILEAV 650
Cdd:cd21205    81 ERLCSPGDILeeKGLVRVAVTVQALL 106
CH_LRCH1 cd21270
calponin homology (CH) domain found in leucine-rich repeat and calponin homology ...
 544-655 3.36e-43

calponin homology (CH) domain found in leucine-rich repeat and calponin homology domain-containing protein 1; Leucine-rich repeat and calponin homology domain-containing protein 1 (LRCH1), also called calponin homology domain-containing protein 1, or neuronal protein 81 (NP81), acts as a negative regulator of GTPase CDC42 by sequestering CDC42-guanine exchange factor DOCK8. LRCH1 contains a single copy of the CH domain at the C-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409119  Cd Length: 112  Bit Score: 151.16  E-value: 3.36e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085 544 EEKELISQLRQILESRLQQPLPEDLAEALANGVILCQLANQLRPRSVPFIHVPSPAVPKLSALKSRKNVENFLEACRKMG 623
Cdd:cd21270     1 EERELTEQLRENIETRLKVSLPEDLGAALMDGVVLCHLVNHVRPRSVASIHVPSPAVPKLSMAKCRRNVENFLEACRKIG 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1958669085 624 VPEADLCSPSDLLRGTAQGLQTILEAVILAGG 655
Cdd:cd21270    81 VPEADLCSPYDILQLNLRGIRKTVETLLALGE 112
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
66-250 8.35e-41

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 154.32  E-value: 8.35e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085  66 DLSDITQAAPSGPLLSLDLSRNRFPEVPEAACQLVSLEGLSLYHNCLRCLNPALGNLTALTYLNLSRNQLSSLPPYICQL 145
Cdd:COG4886   102 DLSGNEELSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNL 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085 146 P-LRVLIISNNKLGALPPDISTLGSLRQLDVSSNELQSLPVELCSLRSLRDLNVRRNQLSTLPdELGDLP-LVRLDFSCN 223
Cdd:COG4886   182 TnLKELDLSNNQITDLPEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTDLP-ELGNLTnLEELDLSNN 260

                         170       180
                  ....*....|....*....|....*..
gi 1958669085 224 RVSRIPVSfCRLRHLQVILLDSNPLQS 250
Cdd:COG4886   261 QLTDLPPL-ANLTNLKTLDLSNNQLTD 286
CH_LRCH2 cd21271
calponin homology (CH) domain found in leucine-rich repeat and calponin homology ...
 544-636 1.91e-38

calponin homology (CH) domain found in leucine-rich repeat and calponin homology domain-containing protein 2; Leucine-rich repeat and calponin homology domain-containing protein 2 (LRCH2) may play a role in the organization of the cytoskeleton. It contains a single copy of the CH domain at the C-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409120  Cd Length: 111  Bit Score: 138.14  E-value: 1.91e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085 544 EEKELISQLRQILESRLQQPLPEDLAEALANGVILCQLANQLRPRSVPFIHVPSPAVPKLSALKSRKNVENFLEACRKMG 623
Cdd:cd21271     2 EELELIEQLRENIESRLKVILPEDLGAALMDGVVLCHLANHIRPRSVGSIHVPSPAVPKLSMAKCRRNVENFLDACRKLG 81

                          90
                  ....*....|...
gi 1958669085 624 VPEADLCSPSDLL 636
Cdd:cd21271    82 VPEDKLCLPHHIL 94
CH_LRCH3 cd21272
calponin homology (CH) domain found in leucine-rich repeat and calponin homology ...
 547-648 7.15e-37

calponin homology (CH) domain found in leucine-rich repeat and calponin homology domain-containing protein 3; Leucine-rich repeat and calponin homology domain-containing protein 3 (LRCH3) is part of the DISP (DOCK7-Induced Septin disPlacement) complex. It may regulate the association of septins with actin and thereby regulate the actin cytoskeleton. LRCH3 contains a single copy of the CH domain at the C-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409121  Cd Length: 109  Bit Score: 133.58  E-value: 7.15e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085 547 ELISQLRQILESRLQQPLPEDLAEALANGVILCQLANQLRPRSVPFIHVPSPAVPKLSALKSRKNVENFLEACRKMGVPE 626
Cdd:cd21272     1 ELIEQLRKNIESRLKVSLPSDLGAALTDGVVLCHLANHVRPRSVPSIHVPSPAVPKLTMAKCRRNVENFLEACRRIGVPQ 80

                          90       100
                  ....*....|....*....|....*..
gi 1958669085 627 ADLCSPSDLL--RGTAQ---GLQTILE 648
Cdd:cd21272    81 EQLCLPLHILeeKGLSQvavTVQALLE 107
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
47-252 2.90e-36

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 141.22  E-value: 2.90e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085  47 LNLSNRRLKHFPRGAARSYDLSDITQAAPSGPLLSLDLSRNRFPEVPEAACQLVSLEGLSLYHNclrclnPALGNLTALT 126
Cdd:COG4886    43 LSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGN------EELSNLTNLE 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085 127 YLNLSRNQLSSLPPYICQLP-LRVLIISNNKLGALPPDISTLGSLRQLDVSSNELQSLPVELCSLRSLRDLNVRRNQLST 205
Cdd:COG4886   117 SLDLSGNQLTDLPEELANLTnLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITD 196

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1958669085 206 LPDELGDLP-LVRLDFSCNRVSRIPVSFCRLRHLQVILLDSNPLQSPP 252
Cdd:COG4886   197 LPEPLGNLTnLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTDLP 244
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
46-206 8.36e-30

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 122.35  E-value: 8.36e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085  46 TLNLSNRRLKHFPRgaarsyDLSDITQaapsgpLLSLDLSRNRFPEVPEAACQLVSLEGLSLYHNCLRCLNPALGNLTAL 125
Cdd:COG4886   140 ELDLSNNQLTDLPE------PLGNLTN------LKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLGNLTNL 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085 126 TYLNLSRNQLSSLPPYICQLP-LRVLIISNNKLGALPpDISTLGSLRQLDVSSNELQSLPvELCSLRSLRDLNVRRNQLS 204
Cdd:COG4886   208 EELDLSGNQLTDLPEPLANLTnLETLDLSNNQLTDLP-ELGNLTNLEELDLSNNQLTDLP-PLANLTNLKTLDLSNNQLT 285


                  ..
gi 1958669085 205 TL 206
Cdd:COG4886   286 DL 287
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 545-638 9.36e-23

calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).


Pssm-ID: 409031 [Multi-domain]  Cd Length: 103  Bit Score: 93.17  E-value: 9.36e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085 545 EKELISQLRQILESRLQQPlPEDLAEALANGVILCQLANQLRPRSVPFIHVPSpavpkLSALKSRKNVENFLEACRKMGV 624
Cdd:cd00014     1 EEELLKWINEVLGEELPVS-ITDLFESLRDGVLLCKLINKLSPGSIPKINKKP-----KSPFKKRENINLFLNACKKLGL 74

                          90
                  ....*....|....
gi 1958669085 625 PEADLCSPSDLLRG 638
Cdd:cd00014    75 PELDLFEPEDLYEK 88
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
64-256 1.82e-20

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 94.62  E-value: 1.82e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085  64 SYDLSDITQAAPSGPLLSLDLSRNRFPEVPEAACQLVSLEGLSLYHNCLRCLNPALGNLTALTYLNLSRNQLSSLPPYIC 143
Cdd:COG4886    14 LLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLG 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085 144 QLP-LRVLIISNNKlgalppDISTLGSLRQLDVSSNELQSLPVELCSLRSLRDLNVRRNQLSTLPDELGDLP-LVRLDFS 221
Cdd:COG4886    94 DLTnLTELDLSGNE------ELSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLPEPLGNLTnLKSLDLS 167

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1958669085 222 CNRVSRIPVSFCRLRHLQVILLDSNPLQSPPAQIC 256
Cdd:COG4886   168 NNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLG 202
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
46-229 8.49e-16

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 81.28  E-value: 8.49e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085  46 TLNLSNRRLKHFPRG--------AARSYDLSDITQAAPSgPLLSLDLSRNRFPEVPEaacQLVS-LEGLSLYHNCLRCLN 116
Cdd:PRK15370  203 TLILDNNELKSLPENlqgniktlYANSNQLTSIPATLPD-TIQEMELSINRITELPE---RLPSaLQSLDLFHNKISCLP 278

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085 117 PALGNltALTYLNLSRNQLSSLPPYicqLPLRV--LIISNNKLGALPPDISTlgSLRQLDVSSNELQSLPVELCSlrSLR 194
Cdd:PRK15370  279 ENLPE--ELRYLSVYDNSIRTLPAH---LPSGIthLNVQSNSLTALPETLPP--GLKTLEAGENALTSLPASLPP--ELQ 349

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1958669085 195 DLNVRRNQLSTLPDELGDlPLVRLDFSCNRVSRIP 229
Cdd:PRK15370  350 VLDVSKNQITVLPETLPP-TITTLDVSRNALTNLP 383
CH_dMP20-like cd21207
calponin homology (CH) domain found in Drosophila melanogaster muscle-specific protein 20 ...
 545-635 9.15e-15

calponin homology (CH) domain found in Drosophila melanogaster muscle-specific protein 20 (dMP20) and similar domains; This subfamily contains Drosophila melanogaster muscle-specific protein 20 (dMP20), Echinococcus granulosus myophilin, Dictyostelium discoideum Rac guanine nucleotide exchange factor B (also called Trix), and similar proteins. dMP20 is present only in the synchronous muscles of D. melanogaster. It may be involved in the system linking the nerve impulse with the contraction or the relaxation process. Trix is involved in the regulation of the late steps of the endocytic pathway. dMP20 contains a single copy of the CH domain, while Trix (triple CH-domain array exchange factor) contains three, two type 3 CH domains which are included in this model, and one type 1 CH domain that is not included in this subfamily, but is part of the superfamily. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409056 [Multi-domain]  Cd Length: 107  Bit Score: 70.80  E-value: 9.15e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085 545 EKELISQLRQILESRLQQPLPE--DLAEALANGVILCQLANQLRPRSVPFIHVpspavpKLSALKSRKNVENFLEACRKM 622
Cdd:cd21207     3 DPALEAEALDWIEAVTGEKLDDgkDYEDVLKDGVILCKLINILKPGSVKKINT------SKMAFKLMENIENFLTACKGY 76

                          90
                  ....*....|...
gi 1958669085 623 GVPEADLCSPSDL 635
Cdd:cd21207    77 GVPKTDLFQTVDL 89
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 546-638 6.28e-14

Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 68.11  E-value: 6.28e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085  546 KELISQLRQILESRLQQPLpEDLAEALANGVILCQLANQLRPRSVPFIHVPspavPKLSALKSRKNVENFLEACRKMGvP 625
Cdd:smart00033   1 KTLLRWVNSLLAEYDKPPV-TNFSSDLKDGVALCALLNSLSPGLVDKKKVA----ASLSRFKKIENINLALSFAEKLG-G 74

                           90
                   ....*....|...
gi 1958669085  626 EADLCSPSDLLRG 638
Cdd:smart00033  75 KVVLFEPEDLVEG 87
CH_VAV cd21201
calponin homology (CH) domain found in VAV proteins; VAV proteins function both as cytoplasmic ...
 567-639 2.78e-13

calponin homology (CH) domain found in VAV proteins; VAV proteins function both as cytoplasmic guanine nucleotide exchange factors (GEFs) for Rho GTPases and as scaffold proteins, and they play important roles in cell signaling by coupling cell surface receptors to various effector functions. They play key roles in processes that require cytoskeletal reorganization including immune synapse formation, phagocytosis, cell spreading, and platelet aggregation, among others. Vertebrates have three VAV proteins (VAV1, VAV2, and VAV3). VAV proteins contain several domains that enable their function: N-terminal calponin homology (CH), acidic, RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), C1 (zinc finger), SH2, and two SH3 domains. This model corresponds to the CH domain, an actin-binding domain which is present as a single copy in VAV proteins.


Pssm-ID: 409050  Cd Length: 117  Bit Score: 66.89  E-value: 2.78e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958669085 567 DLAEALANGVILCQLANQLRPRSVPFIHVPSPavPKLSALKSRKNVENFLEACRKM-GVPEADLCSPSDLLRGT 639
Cdd:cd21201    31 DLAQALRDGVLLCQLLNRLSPGSVDDREINLR--PQMSQFLCLKNIRTFLQACRTVfGLRSADLFEPEDLYDVT 102
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 91-253 4.75e-13

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 72.57  E-value: 4.75e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085  91 EVPEAACQLVSLEGLSL-YHNCLRCLNPALGNLTALTYLNLSRNQLS-SLPPYICQLP-LRVLIISNNKL-GALPPDIST 166
Cdd:PLN00113  227 EIPYEIGGLTSLNHLDLvYNNLTGPIPSSLGNLKNLQYLFLYQNKLSgPIPPSIFSLQkLISLDLSDNSLsGEIPELVIQ 306

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085 167 LGSLRQLDVSSNELQ-SLPVELCSLRSLRDLNVRRNQLS-TLPDELGDL-PLVRLDFSCNRVS-RIPVSFCRLRHLQVIL 242
Cdd:PLN00113  307 LQNLEILHLFSNNFTgKIPVALTSLPRLQVLQLWSNKFSgEIPKNLGKHnNLTVLDLSTNNLTgEIPEGLCSSGNLFKLI 386

                         170
                  ....*....|...
gi 1958669085 243 LDSNPLQS--PPA 253
Cdd:PLN00113  387 LFSNSLEGeiPKS 399
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 79-207 6.02e-13

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


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 68.66  E-value: 6.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085  79 LLSLDLSRNRFPEVPEAACqLVSLEGLSLYHNCLRCLNpALGNLTALTYLNLSRNQLSSlPPYICQLP---------LRV 149
Cdd:cd21340    48 LTHLYLQNNQIEKIENLEN-LVNLKKLYLGGNRISVVE-GLENLTNLEELHIENQRLPP-GEKLTFDPrslaalsnsLRV 124

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958669085 150 LIISNNKLGALPPdISTLGSLRQLDVSSNELQSLpVELC----SLRSLRDLNVRRNQLSTLP 207
Cdd:cd21340   125 LNISGNNIDSLEP-LAPLRNLEQLDASNNQISDL-EELLdllsSWPSLRELDLTGNPVCKKP 184
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 544-635 2.10e-12

Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 63.84  E-value: 2.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085 544 EEKELISQLRQILESRLQQPLPEDLAEALANGVILCQLANQLRPRSVPFIHVpspavpKLSALKSRKNVENFLE-ACRKM 622
Cdd:pfam00307   3 LEKELLRWINSHLAEYGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKL------NKSEFDKLENINLALDvAEKKL 76

                          90
                  ....*....|...
gi 1958669085 623 GVPEADLcSPSDL 635
Cdd:pfam00307  77 GVPKVLI-EPEDL 88
CH_SCP1-like cd21210
calponin homology (CH) domain found in Saccharomyces cerevisiae transgelin (SCP1) and similar ...
 553-646 2.24e-12

calponin homology (CH) domain found in Saccharomyces cerevisiae transgelin (SCP1) and similar proteins; The family includes transgelins from Saccharomyces cerevisiae and Schizosaccharomyces pombe, which are also called SCP1 and STG1, respectively. Transgelin, also called calponin homolog 1, has actin-binding and actin-bundling activity. It stabilizes actin filaments against disassembly. Transgelin contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409059 [Multi-domain]  Cd Length: 101  Bit Score: 63.54  E-value: 2.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085 553 RQILESRLQQPLPE-DLAEALANGVILCQLANQLRPRSVPFIH-VPSPAVpklsalkSRKNVENFLEACRKMGVPEADLC 630
Cdd:cd21210     6 REWIEEVLGEKLAQgDLLDALKDGVVLCKLANRILPADIRKYKeSKMPFV-------QMENISAFLNAARKLGVPENDLF 78

                          90
                  ....*....|....*...
gi 1958669085 631 SPSDLL--RGTAQGLQTI 646
Cdd:cd21210    79 QTVDLFerKNPAQVLQCL 96
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 101-252 2.06e-11

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


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 64.04  E-value: 2.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085 101 SLEGLSLYHNCLRCLnPALGNLTALTYLNLSRNQLSSLPPyICQLP-LRVLIISNNKlgalppdIST------LGSLRQL 173
Cdd:cd21340    25 NLKVLYLYDNKITKI-ENLEFLTNLTHLYLQNNQIEKIEN-LENLVnLKKLYLGGNR-------ISVveglenLTNLEEL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085 174 DVSSNEL---QSLPVELCSL----RSLRDLNVRRNQLSTLpDELGDLP-LVRLDFSCNRVSRIP---VSFCRLRHLQVIL 242
Cdd:cd21340    96 HIENQRLppgEKLTFDPRSLaalsNSLRVLNISGNNIDSL-EPLAPLRnLEQLDASNNQISDLEellDLLSSWPSLRELD 174

                         170
                  ....*....|
gi 1958669085 243 LDSNPLQSPP 252
Cdd:cd21340   175 LTGNPVCKKP 184
CH_AtKIN14-like cd21203
calponin homology (CH) domain found in Arabidopsis thaliana Kinesin-like KIN-14 protein family; ...
 566-635 2.10e-11

calponin homology (CH) domain found in Arabidopsis thaliana Kinesin-like KIN-14 protein family; Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. This family includes a group of kinesin-like proteins belonging to KIN-14 protein family. They all contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409052 [Multi-domain]  Cd Length: 112  Bit Score: 61.28  E-value: 2.10e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958669085 566 EDLAEALANGVILCQLANQLRPRSVPFI--HVPSPAVPKLSALKSRKNVENFLEACRKMGVPeadLCSPSDL 635
Cdd:cd21203    24 EEFRLCLRDGVVLCKLLNKLQPGAVPKVveSPDDPDGAAGSAFQYFENVRNFLVAIEEMGLP---TFEASDL 92
CH_LMO7-like cd21208
calponin homology (CH) domain found in LIM domain only protein 7 and similar proteins; This ...
 565-635 5.69e-11

calponin homology (CH) domain found in LIM domain only protein 7 and similar proteins; This family includes LIM domain only protein 7 (LMO-7) and LIM and calponin homology domains-containing protein 1 (LIMCH1), and similar proteins. LMO-7, also called F-box only protein 20, or LOMP, is a transcription regulator for expression of many Emery-Dreifuss muscular dystrophy (EDMD)-relevant genes. It binds to alpha-actinin and AF6/afadin at adherens junctions for epithelial cell-cell adhesion. LIMCH1 acts as an actin stress fiber-associated protein that activates the non-muscle myosin IIa complex by promoting the phosphorylation of its regulatory subunit MRLC/MYL9. It positively regulates actin stress fiber assembly and stabilizes focal adhesions, and therefore negatively regulates cell spreading and cell migration. Members of this family contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409057 [Multi-domain]  Cd Length: 119  Bit Score: 60.05  E-value: 5.69e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958669085 565 PEDLAEALANGVILCQLANQLRPRSVPFIHVPSpavpklSALKSRKNVENFLEACRKMGVPEADLCSPSDL 635
Cdd:cd21208    19 SDDFRESLEDGILLCELINAIKPGSIKKINRLP------TPIAGLDNLNLFLKACEDLGLKDSQLFDPTDL 83
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 46-248 6.07e-11

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 66.02  E-value: 6.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085  46 TLNLSNRRLK-------HFPRGAARSYDLSD--ITQAAPSG--PLL-SLDLSRNRFP-EVPEAACQLVSLEGLSLYHNCL 112
Cdd:PLN00113   97 TINLSNNQLSgpipddiFTTSSSLRYLNLSNnnFTGSIPRGsiPNLeTLDLSNNMLSgEIPNDIGSFSSLKVLDLGGNVL 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085 113 RCLNPA-LGNLTALTYLNLSRNQLS-SLPPYICQL-PLRVLIISNNKL-GALPPDISTLGSLRQLDVSSNELQ-SLPVEL 187
Cdd:PLN00113  177 VGKIPNsLTNLTSLEFLTLASNQLVgQIPRELGQMkSLKWIYLGYNNLsGEIPYEIGGLTSLNHLDLVYNNLTgPIPSSL 256

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958669085 188 CSLRSLRDLNVRRNQLS-TLPDELGDLP-LVRLDFSCNRVS-RIPVSFCRLRHLQVILLDSNPL 248
Cdd:PLN00113  257 GNLKNLQYLFLYQNKLSgPIPPSIFSLQkLISLDLSDNSLSgEIPELVIQLQNLEILHLFSNNF 320
CH_GAS2-like cd21204
calponin homology (CH) domain found in the growth arrest-specific protein 2 family; The growth ...
 546-635 1.58e-09

calponin homology (CH) domain found in the growth arrest-specific protein 2 family; The growth arrest-specific protein 2 (GAS-2) family includes GAS-2, and GAS-2 like proteins, GAS2L1-3. GAS-2 may play a role in apoptosis by acting as a cell death substrate for caspases. GAS2L1 (also called GAS2-related protein on chromosome 22 or growth arrest-specific protein 2-like 1) and GAS2L2 (also called GAS2-related protein on chromosome 17 or growth arrest-specific protein 2-like 2) may be involved in the cross-linking of microtubules and microfilaments. GAS2L3, also called GAS2-like protein 3, is a cytoskeletal linker protein that may promote and stabilize the formation of the actin and microtubule network. Members of this family contain a single copy of the CH domain at the N-terminal region. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409053  Cd Length: 131  Bit Score: 56.51  E-value: 1.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085 546 KELISQ-LRQILESRLQqplPEDLAEALANGVILCQLAN--QLRPRSVPFIHVPSPAVP----------KLSALKSRKNV 612
Cdd:cd21204     8 KEDLAEwLNDLLGDDLT---PDNFLDELRNGVVLCQLAQkiQEAAEKAREAGKKNGPPPsyklkcnenaKPGSFFARDNV 84

                          90       100
                  ....*....|....*....|...
gi 1958669085 613 ENFLEACRKMGVPEADLCSPSDL 635
Cdd:cd21204    85 ANFLRWCRKLGVDEVLLFESEDL 107
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 79-248 1.71e-09

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 61.40  E-value: 1.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085  79 LLSLDLSRNRFP-EVPEAACQLVSLEGLSLYHNCLRCLNPA-------------------------LGNLTALTYLNLSR 132
Cdd:PLN00113  286 LISLDLSDNSLSgEIPELVIQLQNLEILHLFSNNFTGKIPValtslprlqvlqlwsnkfsgeipknLGKHNNLTVLDLST 365

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085 133 NQLSS-LPPYICQLP--LRVLIISNNKLGALPPDISTLGSLRQ------------------------LDVSSNELQ-SLP 184
Cdd:PLN00113  366 NNLTGeIPEGLCSSGnlFKLILFSNSLEGEIPKSLGACRSLRRvrlqdnsfsgelpseftklplvyfLDISNNNLQgRIN 445

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958669085 185 VELCSLRSLRDLNVRRNQLS-TLPDELGDLPLVRLDFSCNRVS-RIPVSFCRLRHLQVILLDSNPL 248
Cdd:PLN00113  446 SRKWDMPSLQMLSLARNKFFgGLPDSFGSKRLENLDLSRNQFSgAVPRKLGSLSELMQLKLSENKL 511
PRK15387 PRK15387
type III secretion system effector E3 ubiquitin transferase SspH2;
54-254 9.13e-09

type III secretion system effector E3 ubiquitin transferase SspH2;


Pssm-ID: 185285 [Multi-domain]  Cd Length: 788  Bit Score: 58.63  E-value: 9.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085  54 LKHFPRGAARSYDLSDITQAAPSGP--LLSLDLSRNRFPEVPEAACQLVSLEGlslYHNCLRCLnPALGnlTALTYLNLS 131
Cdd:PRK15387  277 LPALPSGLCKLWIFGNQLTSLPVLPpgLQELSVSDNQLASLPALPSELCKLWA---YNNQLTSL-PTLP--SGLQELSVS 350

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085 132 RNQLSSLPPYICQLplRVLIISNNKLGALPpdiSTLGSLRQLDVSSNELQSLPVELCSLRSLRDLNVRRNQLSTLPDELG 211
Cdd:PRK15387  351 DNQLASLPTLPSEL--YKLWAYNNRLTSLP---ALPSGLKELIVSGNRLTSLPVLPSELKELMVSGNRLTSLPMLPSGLL 425

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1958669085 212 DLPLVRldfscNRVSRIPVSFCRLRHLQVILLDSNPLQSPPAQ 254
Cdd:PRK15387  426 SLSVYR-----NQLTRLPESLIHLSSETTVNLEGNPLSERTLQ 463
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
46-183 1.22e-08

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 57.64  E-value: 1.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085  46 TLNLSNRRLKHFPRgaarsyDLSDITQaapsgpLLSLDLSRNRFPEVPEAAcQLVSLEGLSLYHNCLRCLnPALGNLTAL 125
Cdd:COG4886   209 ELDLSGNQLTDLPE------PLANLTN------LETLDLSNNQLTDLPELG-NLTNLEELDLSNNQLTDL-PPLANLTNL 274

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958669085 126 TYLNLSRNQLSSLppYICQLPLRVLIISNNKLGALPPDISTLGSLRQLDVSSNELQSL 183
Cdd:COG4886   275 KTLDLSNNQLTDL--KLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLL 330
LRR_8 pfam13855
Leucine rich repeat;
147-203 3.05e-08

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 50.60  E-value: 3.05e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958669085 147 LRVLIISNNKLGALPPDI-STLGSLRQLDVSSNELQSL-PVELCSLRSLRDLNVRRNQL 203
Cdd:pfam13855   3 LRSLDLSNNRLTSLDDGAfKGLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
CH_CNN2 cd21283
calponin homology (CH) domain found in calponin-2; Calponin-2 (CNN2), also called neutral ...
 545-654 3.31e-08

calponin homology (CH) domain found in calponin-2; Calponin-2 (CNN2), also called neutral calponin, or smooth muscle calponin H2, is an actin cytoskeleton-associated regulatory protein that inhibits the activity of myosin-ATPase and cytoskeleton dynamics. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409132 [Multi-domain]  Cd Length: 109  Bit Score: 51.86  E-value: 3.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085 545 EKEliSQLRQILESRLQQPLPEDLAEALANGVILCQLANQLRPRSVPFIHVPSPAVPKLsalksrKNVENFLEACRKMGV 624
Cdd:cd21283     3 QKE--AELRTWIEGLTGRSIGPDFQKGLKDGVILCELMNKLQPGSVPKINRSMQNWHQL------ENLSNFIKAMVSYGM 74

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1958669085 625 PEADLCSPSDLLR-GTAQGLQTILEAviLAG 654
Cdd:cd21283    75 KPVDLFEANDLFEsGNMTQVQVSLLA--LAG 103
CH_CNN1 cd21282
calponin homology (CH) domain found in calponin-1 and similar proteins; Calponin-1 (CNN1), ...
 551-639 3.66e-08

calponin homology (CH) domain found in calponin-1 and similar proteins; Calponin-1 (CNN1), also called basic calponin, or smooth muscle calponin H1, is a thin filament-associated protein that is implicated in the regulation and modulation of smooth muscle contraction. It is capable of binding to actin, calmodulin, troponin C, and tropomyosin. Calponin-1 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409131 [Multi-domain]  Cd Length: 108  Bit Score: 51.80  E-value: 3.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085 551 QLRQILESRLQQPLPEDLAEALANGVILCQLANQLRPRSVPFIHVPSPAVPKLsalksrKNVENFLEACRKMGVPEADLC 630
Cdd:cd21282     7 ELRVWIEGVTGRRIGDNFMDGLKDGVILCELINKLQPGSVRKINESTQNWHKL------ENIGNFIKAIMHYGVKPHDIF 80


                  ....*....
gi 1958669085 631 SPSDLLRGT 639
Cdd:cd21282    81 EANDLFENT 89
CH_CNN cd21211
calponin homology (CH) domain found in the calponin family; Calponin is an actin ...
 550-654 9.40e-08

calponin homology (CH) domain found in the calponin family; Calponin is an actin filament-associated regulatory protein expressed in smooth muscle and many types of non-muscle cells. There are three calponin isoforms, calponin-1, -2, -3. All of them are actin-binding proteins with functions in inhibiting actin-activated myosin ATPase and stabilizing the actin cytoskeleton. Calponin-1 is specifically expressed in smooth muscle cells and plays a role in fine-tuning smooth muscle contractility. Calponin-2 is expressed in both smooth muscle and non-muscle cells and regulates multiple actin cytoskeleton-based functions. Calponin-3 is expressed in the brain and participates in actin cytoskeleton-based activities in embryonic development and myogenesis. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409060 [Multi-domain]  Cd Length: 108  Bit Score: 50.77  E-value: 9.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085 550 SQLRQILESRLQQPLPEDLAEALANGVILCQLANQLRPRSVPFIHVPSPAVPKLsalksrKNVENFLEACRKMGVPEADL 629
Cdd:cd21211     6 AELRTWIEGVTGLSIGPNFQKGLKDGIILCELINKLQPGSVKKINESMQNWHQL------ENIGNFIKAIVSYGMKPHDI 79

                          90       100
                  ....*....|....*....|....*.
gi 1958669085 630 CSPSDLLR-GTAQGLQTILEAviLAG 654
Cdd:cd21211    80 FEANDLFEnGNMTQVQVTLLA--LAG 103
CH_IQGAP cd21206
calponin homology (CH) domain found in the IQ motif containing GTPase activating protein ...
 553-626 1.03e-07

calponin homology (CH) domain found in the IQ motif containing GTPase activating protein family; Members of the IQ motif containing GTPase activating protein (IQGAP) family are associated with the Ras GTP-binding protein and act as essential regulators of cytoskeletal function. There are three known IQGAP family members: IQGAP1, IQGAP2, and IQGAP3. They are multi-domain molecules having a calponin-homology (CH) domain which binds F-actin, IQGAP-specific repeats, a single WW domain, four IQ motifs that mediate interactions with calmodulin, and a RasGAP related domain that binds active Rho family GTPases. IQGAP1 negatively regulates Ras family GTPases by stimulating their intrinsic GTPase activity. It lacks GAP activity. Both IQGAP1 and IQGAP2 specifically bind to Cdc42 and Rac1, but not to RhoA. Despite similarities to part of the sequence of RasGAP, neither IQGAP1 nor IQGAP2 interacts with Ras. IQGAP3 regulates the organization of the cytoskeleton under the regulation of Rac1 and Cdc42 in neuronal cells. The depletion of IQGAP3 is shown to impair neurite or axon outgrowth in neuronal cells with disorganized cytoskeleton.


Pssm-ID: 409055 [Multi-domain]  Cd Length: 118  Bit Score: 50.69  E-value: 1.03e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958669085 553 RQILESRLQQPLP--EDLAEALANGVILCQLANQLRPRSVPFIHVPSPAvpklsalKSRKNVEN---FLEACRKMGVPE 626
Cdd:cd21206    14 KQWIEACLNEELPptTEFEEELRNGVVLAKLANKFAPKLVPLKKIYDVG-------LQFRHTDNinhFLRALKKIGLPK 85
LRR_8 pfam13855
Leucine rich repeat;
81-135 2.58e-07

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 47.90  E-value: 2.58e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958669085  81 SLDLSRNRFPEV-PEAACQLVSLEGLSLYHNCLRCLNP-ALGNLTALTYLNLSRNQL 135
Cdd:pfam13855   5 SLDLSNNRLTSLdDGAFKGLSNLKVLDLSNNLLTTLSPgAFSGLPSLRYLDLSGNRL 61
CH_VAV1 cd21262
calponin homology (CH) domain found in VAV1 protein; VAV1 is expressed predominantly in the ...
 567-636 3.04e-07

calponin homology (CH) domain found in VAV1 protein; VAV1 is expressed predominantly in the hematopoietic system and it plays an important role in the development and activation of B and T cells. It is activated by tyrosine phosphorylation to function as a guanine nucleotide exchange factor (GEF) for Rho GTPases following cell surface receptor activation, triggering various effects such as cytoskeletal reorganization, transcription regulation, cell cycle progression, and calcium mobilization. It also serves as a scaffold protein and has been shown to interact with Ku70, Socs1, Janus kinase 2, SIAH2, S100B, Abl gene, ZAP-70, SLP76, and Syk, among others. VAV proteins contain several domains that enable their function: N-terminal calponin homology (CH), acidic, RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), C1 (zinc finger), SH2, and two SH3 domains. This model corresponds to the CH domain, an actin-binding domain which is present as a single copy in VAV1 protein.


Pssm-ID: 409111  Cd Length: 120  Bit Score: 49.56  E-value: 3.04e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958669085 567 DLAEALANGVILCQLANQLRPRSVPFIHVpsPAVPKLSALKSRKNVENFLEAC-RKMGVPEADLCSPSDLL 636
Cdd:cd21262    31 DLAQALRDGVLLCQLLNNLLPHAVNLREI--NLRPQMSQFLCLKNIRTFLSTCcEKFGLRKSELFEAFDLF 99
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
92-255 3.13e-07

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 53.93  E-value: 3.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085  92 VPEAACQLVsleglsLYHNCLRCLNPAL-GNLTALTylnLSRNQLSSLPPyicQLP--LRVLIISNNKLGALPPDISTlg 168
Cdd:PRK15370  197 IPEQITTLI------LDNNELKSLPENLqGNIKTLY---ANSNQLTSIPA---TLPdtIQEMELSINRITELPERLPS-- 262

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085 169 SLRQLDVSSNELQSLPVELCSlrSLRDLNVRRNQLSTLPDELGDlPLVRLDFSCNRVSRIPVSFCrlRHLQVILLDSNPL 248
Cdd:PRK15370  263 ALQSLDLFHNKISCLPENLPE--ELRYLSVYDNSIRTLPAHLPS-GITHLNVQSNSLTALPETLP--PGLKTLEAGENAL 337


                  ....*..
gi 1958669085 249 QSPPAQI 255
Cdd:PRK15370  338 TSLPASL 344
CH_VAV3 cd21264
calponin homology (CH) domain found in VAV3 protein and similar proteins; VAV3 is ubiquitously ...
 567-646 4.25e-07

calponin homology (CH) domain found in VAV3 protein and similar proteins; VAV3 is ubiquitously expressed and functions as a phosphorylation-dependent guanine nucleotide exchange factor (GEF) for RhoA, RhoG, and Rac1. Its function has been implicated in the hematopoietic, bone, cerebellar, and cardiovascular systems. VAV3 is essential in axon guidance in neurons that control blood pressure and respiration. It is overexpressed in prostate cancer cells and it plays a role in regulating androgen receptor transcriptional activity. VAV proteins contain several domains that enable their function: N-terminal calponin homology (CH), acidic, RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), C1 (zinc finger), SH2, and two SH3 domains. The model corresponds to CH domain, an actin-binding domain which is present as a single copy in VAV3 protein.


Pssm-ID: 409113  Cd Length: 117  Bit Score: 49.19  E-value: 4.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085 567 DLAEALANGVILCQLANQLRPRSVPFIHVpsPAVPKLSALKSRKNVENFLEA-CRKMGVPEADLCSPSDL--LRGTAQGL 643
Cdd:cd21264    31 DLAQTLRDGVLLCQLLNNLRPHSINLKEI--NLRPQMSQFLCLKNIRTFLSAcCETFGMRKSELFEAFDLfdVRDFGKVI 108


                  ...
gi 1958669085 644 QTI 646
Cdd:cd21264   109 ETL 111
CH_CNN3 cd21284
calponin homology (CH) domain found in calponin-3; Calponin-3 (CNN3), also called acidic ...
 540-654 5.86e-07

calponin homology (CH) domain found in calponin-3; Calponin-3 (CNN3), also called acidic isoform calponin, is an F-actin-binding protein that is expressed in the brain and has been shown to control dendritic spine morphology, density, and plasticity by regulating actin cytoskeletal reorganization and dynamics. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409133 [Multi-domain]  Cd Length: 111  Bit Score: 48.36  E-value: 5.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085 540 PQILEEkelisqLRQILESRLQQPLPEDLAEALANGVILCQLANQLRPRSVPFIHVPSPAVPKLsalksrKNVENFLEAC 619
Cdd:cd21284     4 PQKEEE------LRNWIEEVTGMSIGENFQKGLKDGVILCELINKLQPGSIRKINESKLNWHQL------ENIGNFIKAI 71

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1958669085 620 RKMGVPEADLCSPSDLLR-GTAQGLQTILeaVILAG 654
Cdd:cd21284    72 QAYGMKPHDIFEANDLFEnGNMTQVQTTL--LALAG 105
CH_LMO7 cd21277
calponin homology (CH) domain found in LIM domain only protein 7; LIM domain only protein 7 ...
 566-635 9.39e-07

calponin homology (CH) domain found in LIM domain only protein 7; LIM domain only protein 7 (LMO-7), also called F-box only protein 20, or LOMP, is a transcription regulator for expression of many Emery-Dreifuss muscular dystrophy (EDMD)-relevant genes. It binds to alpha-actinin and AF6/afadin at adherens junctions for epithelial cell-cell adhesion. It contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409126 [Multi-domain]  Cd Length: 116  Bit Score: 47.91  E-value: 9.39e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085 566 EDLAEALANGVILCQLANQLRPRSVPFIHVPSPAVPKLSalksrkNVENFLEACRKMGVPEADLCSPSDL 635
Cdd:cd21277    20 KDFRSALENGVLLCDLINKIKPGIIKKINRLSTPIAGLD------NINVFLKACEKLGLKEAQLFHPGDL 83
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 82-207 1.15e-06

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 52.16  E-value: 1.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085  82 LDLSRNRF-PEVPEAAcQLVSLEGLSLYHNCLRCLNP-ALGNLTALTYLNLSRNQLSSLPP---YICQlPLRVLIISNNK 156
Cdd:PLN00113  457 LSLARNKFfGGLPDSF-GSKRLENLDLSRNQFSGAVPrKLGSLSELMQLKLSENKLSGEIPdelSSCK-KLVSLDLSHNQ 534

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958669085 157 L-GALPPDISTLGSLRQLDVSSNELQ-SLPVELCSLRSLRDLNVRRNQL-STLP 207
Cdd:PLN00113  535 LsGQIPASFSEMPVLSQLDLSQNQLSgEIPKNLGNVESLVQVNISHNHLhGSLP 588
LRR_8 pfam13855
Leucine rich repeat;
191-248 2.23e-06

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 45.21  E-value: 2.23e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958669085 191 RSLRDLNVRRNQLSTLPDE-LGDLP-LVRLDFSCNRVSRI-PVSFCRLRHLQVILLDSNPL 248
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGaFKGLSnLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
PLN03150 PLN03150
hypothetical protein; Provisional
 138-220 2.34e-06

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 50.97  E-value: 2.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085 138 LPPYICQLP-LRVLIISNNKL-GALPPDISTLGSLRQLDVSSNELQ-SLPVELCSLRSLRDLNVRRNQLS-TLPDELGDL 213
Cdd:PLN03150  434 IPNDISKLRhLQSINLSGNSIrGNIPPSLGSITSLEVLDLSYNSFNgSIPESLGQLTSLRILNLNGNSLSgRVPAALGGR 513


                  ....*..
gi 1958669085 214 PLVRLDF 220
Cdd:PLN03150  514 LLHRASF 520
PRK15387 PRK15387
type III secretion system effector E3 ubiquitin transferase SspH2;
75-252 3.17e-06

type III secretion system effector E3 ubiquitin transferase SspH2;


Pssm-ID: 185285 [Multi-domain]  Cd Length: 788  Bit Score: 50.55  E-value: 3.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085  75 PSGpLLSLDLSRN---RFPEVPEAACQLvsleglSLYHNCLRCLnPALGnlTALTYLNLSRNQLSSLPPYICQLPlrVLI 151
Cdd:PRK15387  261 PPG-LLELSIFSNpltHLPALPSGLCKL------WIFGNQLTSL-PVLP--PGLQELSVSDNQLASLPALPSELC--KLW 328

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085 152 ISNNKLGALPpdisTLGS-LRQLDVSSNELQSLPVELCSLRSLRDLNVRRNQLSTLPDELGDLPLvrldfSCNRVSRIPV 230
Cdd:PRK15387  329 AYNNQLTSLP----TLPSgLQELSVSDNQLASLPTLPSELYKLWAYNNRLTSLPALPSGLKELIV-----SGNRLTSLPV 399

                         170       180
                  ....*....|....*....|..
gi 1958669085 231 SFCRLRHLQVillDSNPLQSPP 252
Cdd:PRK15387  400 LPSELKELMV---SGNRLTSLP 418
CH_VAV2 cd21263
calponin homology (CH) domain found in VAV2 protein and similar proteins; VAV2 is widely ...
 567-636 6.78e-06

calponin homology (CH) domain found in VAV2 protein and similar proteins; VAV2 is widely expressed and functions as a guanine nucleotide exchange factor (GEF) for RhoA, RhoB and RhoG and also activates Rac1 and Cdc42. It is implicated in many cellular and physiological functions including blood pressure control, eye development, neurite outgrowth and branching, EGFR endocytosis and degradation, and cell cluster morphology, among others. It has been reported to associate with Nek3. VAV proteins contain several domains that enable their function: N-terminal calponin homology (CH), acidic, RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), C1 (zinc finger), SH2, and two SH3 domains. The model corresponds to CH domain, an actin-binding domain which is present as a single copy in VAV2 protein.


Pssm-ID: 409112  Cd Length: 119  Bit Score: 45.72  E-value: 6.78e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958669085 567 DLAEALANGVILCQLANQLRPRSVPFIHVPSPavPKLSALKSRKNVENFLEACR-KMGVPEADLCSPSDLL 636
Cdd:cd21263    31 DLAQALRDGVLLCQLLHNLSPGSIDLKDINFR--PQMSQFLCLKNIRTFLKVCHdKFGLRNSELFDPFDLF 99
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 62-184 9.82e-06

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 49.08  E-value: 9.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085  62 ARSYDLSDITQAAPSGPLLSLDLSRNRFPE-VPEAACQLVSLEGLSLYHNCLRCLNPA-LGNLTALTYLNLSRNQLS-SL 138
Cdd:PLN00113  460 ARNKFFGGLPDSFGSKRLENLDLSRNQFSGaVPRKLGSLSELMQLKLSENKLSGEIPDeLSSCKKLVSLDLSHNQLSgQI 539

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1958669085 139 PPYICQLP-LRVLIISNNKL-GALPPDISTLGSLRQLDVSSNELQ-SLP 184
Cdd:PLN00113  540 PASFSEMPvLSQLDLSQNQLsGEIPKNLGNVESLVQVNISHNHLHgSLP 588
CH_GAS2L1_2 cd21268
calponin homology (CH) domain found in GAS2-like protein 1 (GAS2L1), GAS2L2, and similar ...
 565-635 3.47e-05

calponin homology (CH) domain found in GAS2-like protein 1 (GAS2L1), GAS2L2, and similar proteins; This subfamily includes GAS2L1 (also called GAS2-related protein on chromosome 22 or growth arrest-specific protein 2-like 1) and GAS2L2 (also called GAS2-related protein on chromosome 17 or growth arrest-specific protein 2-like 2). They may be involved in the cross-linking of microtubules and microfilaments. Members of this subfamily contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409117  Cd Length: 142  Bit Score: 44.23  E-value: 3.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085 565 PEDLAEALANGVILCQLAN----------QLRPRSVPFIHVP-------SPAVPKLSaLKSRKNVENFLEACRK-MGVPE 626
Cdd:cd21268    30 ADNFFEKLETGVLLCKHANnvtraarefqAQHPERASPLKLPprevifyRPSAKPGS-FQARDNVSNFINWCRQlLGIPE 108


                  ....*....
gi 1958669085 627 ADLCSPSDL 635
Cdd:cd21268   109 VLLFETDDL 117
CH_TAGLN cd21279
calponin homology (CH) domain found in transgelin; Transgelin, also called 22 kDa ...
 572-638 4.46e-05

calponin homology (CH) domain found in transgelin; Transgelin, also called 22 kDa actin-binding protein, protein WS3-10, or smooth muscle protein 22-alpha (SM22-alpha), acts as an actin cross-linking/gelling protein that may be involved in calcium interactions and in regulating contractile properties of the cell. It may also contribute to replicative senescence. Transgelin contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409128 [Multi-domain]  Cd Length: 121  Bit Score: 43.46  E-value: 4.46e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958669085 572 LANGVILCQLANQLRPRSVPFIHVPSPavPKLSALKSRKNVENFLEACRKMGVPEADLCSPSDLLRG 638
Cdd:cd21279    34 LKNGVVLSKLVNSLYPDGSKPVKIPDN--PPSMVFKQMEQVAQFLKAAEDYGVVKTDMFQTVDLYEG 98
CH_LIMCH1 cd21278
calponin homology (CH) domain found in LIM and calponin homology domains-containing protein 1; ...
 566-635 4.81e-05

calponin homology (CH) domain found in LIM and calponin homology domains-containing protein 1; LIM and calponin homology domains-containing protein 1 (LIMCH1) acts as an actin stress fiber-associated protein that activates the non-muscle myosin IIa complex by promoting the phosphorylation of its regulatory subunit MRLC/MYL9. It positively regulates actin stress fiber assembly and stabilizes focal adhesions, and therefore negatively regulates cell spreading and cell migration. LIMCH1 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409127 [Multi-domain]  Cd Length: 118  Bit Score: 43.32  E-value: 4.81e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958669085 566 EDLAEALANGVILCQLANQLRPRSVPFIH-VPSPavpklsaLKSRKNVENFLEACRKMGVPEADLCSPSDL 635
Cdd:cd21278    20 KDFRSGLENGILLCELLNAIKPGLVKKINrLPTP-------IAGLDNITLFLRGCKELGLKESQLFDPGDL 83
CH_PIX cd21202
calponin homology (CH) domain found in the Pak Interactive eXchange factor family; Pak ...
 568-647 5.46e-05

calponin homology (CH) domain found in the Pak Interactive eXchange factor family; Pak Interactive eXchange factor (PIX) proteins are Rho guanine nucleotide exchange factors (GEFs), which activate small GTPases by exchanging bound GDP for free GTP. They act as GEFs for both Cdc42 and Rac1, and have been implicated in cell motility, adhesion, neurite outgrowth, and cell polarity. Vertebrates contain two proteins from the PIX family, alpha-PIX and beta-PIX. Alpha-PIX, also called Rho guanine nucleotide exchange factor 6 (ARHGEF6), is localized in dendritic spines where it regulates spine morphogenesis. It controls dendritic length and spine density in the hippocampus. Mutations in the ARHGEF6 gene cause X-linked intellectual disability in humans. Beta-PIX, also called Rho guanine nucleotide exchange factor 7 (ARHGEF7), plays important roles in regulating neuroendocrine exocytosis, focal adhesion maturation, cell migration, synaptic vesicle localization, and insulin secretion. Both alpha-PIX and beta-PIX contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409051 [Multi-domain]  Cd Length: 114  Bit Score: 42.90  E-value: 5.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085 568 LAEALANGVILCQLANQLRPRSVPFIHvPSPavpkLSALKSRKNVENFLEACRKMGVPEADLCSPSDLLRGtaQGLQTIL 647
Cdd:cd21202    30 LSESLKNGVVLCRLVNRLKPGTVEKIY-DEP----TTEEECLYNFESFLKACQELGILAEEIFDPNDLYSG--GNFQKVL 102
CH_TAGLN3 cd21281
calponin homology (CH) domain found in transgelin-3; Transgelin-3, also called neuronal ...
 556-638 7.38e-05

calponin homology (CH) domain found in transgelin-3; Transgelin-3, also called neuronal protein 22 (NP22), or neuronal protein NP25, may have a role in alcohol-related adaptations and may mediate regulatory signal transduction pathways in neurons. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409130 [Multi-domain]  Cd Length: 119  Bit Score: 42.64  E-value: 7.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085 556 LESRL------------QQPLP--EDLAEALANGVILCQLANQLRPRSvpfiHVPSPAVPKLS-ALKSRKNVENFLEACR 620
Cdd:cd21281     4 LESRLvdwiiiqcggdiERPQPgrQNFQKWLMDGTILCRLINSLYPPG----KEPIKKISETKmAFKQMEKISQFLQAAE 79

                          90
                  ....*....|....*...
gi 1958669085 621 KMGVPEADLCSPSDLLRG 638
Cdd:cd21281    80 AYGVITTDIFQTVDLWEG 97
SCP1 COG5199
Calponin [Cytoskeleton];
547-646 7.48e-05

Calponin [Cytoskeleton];


Pssm-ID: 227526 [Multi-domain]  Cd Length: 178  Bit Score: 44.14  E-value: 7.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085 547 ELISQLRQILESRLQQPL--PEDLAEALANGVILCQLANQLRPRSVPFIHVPSPAVpklsalkSRKNVENFLEACRKMGV 624
Cdd:COG5199    13 KQQKEVTLWIETVLGEKFepPGDLLSLLKDGVRLCRILNEASPLDIKYKESKMPFV-------QMENISSFINGLKKLRV 85

                          90       100
                  ....*....|....*....|....
gi 1958669085 625 PEADLCSPSDLL--RGTAQGLQTI 646
Cdd:COG5199    86 PEYELFQTNDLFeaKDLRQVVICL 109
CH_TAGLN2 cd21280
calponin homology (CH) domain found in transgelin-2; Transgelin-2, also called epididymis ...
 545-638 7.54e-05

calponin homology (CH) domain found in transgelin-2; Transgelin-2, also called epididymis tissue protein Li 7e, or SM22-alpha homolog, acts as an actin-binding protein that induces actin gelation and regulates the actin cytoskeleton. It may participate in the development and progression of multiple cancers. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409129 [Multi-domain]  Cd Length: 137  Bit Score: 43.33  E-value: 7.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085 545 EKELISQLRQIL------ESRLQQPLP----EDLAEALANGVILCQLANQLRPRSV-PFIHVPSPAVpklsALKSRKNVE 613
Cdd:cd21280     2 DKQYDADLEQILiqwitaQCGKQVGRPqpgrENFQNWLKDGTVLCHLINSLYPKGQaPVKKIQASTM----AFKQMEQIS 77

                          90       100
                  ....*....|....*....|....*
gi 1958669085 614 NFLEACRKMGVPEADLCSPSDLLRG 638
Cdd:cd21280    78 QFLQAAERYGINTTDIFQTVDLWEG 102
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
96-255 7.59e-05

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 45.69  E-value: 7.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085  96 ACQLVSLEGLSLYHNCLRCLNPALGNLTALTYLNLSRNQLSSLPPYICQLPLRVLIISNNKLGALPPDISTLGSLRQLDV 175
Cdd:COG4886     1 LLLLLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085 176 SSNELQSLPVELCSLRSLRDLNVRRNqlstlpDELGDLP-LVRLDFSCNRVSRIPVSFCRLRHLQVILLDSNPLQSPPAQ 254
Cdd:COG4886    81 LLSLLLLGLTDLGDLTNLTELDLSGN------EELSNLTnLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLPEP 154


                  .
gi 1958669085 255 I 255
Cdd:COG4886   155 L 155
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 36-223 1.39e-04

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: 44.78  E-value: 1.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085  36 RALEEAVATGTlNLSNRRLKHFPRGAARSYDLSDITQAAPSgpLLSLDLSRNR-----FPEVPEAACQLVSLEGLSLYHN 110
Cdd:COG5238   198 EELAEALTQNT-TVTTLWLKRNPIGDEGAEILAEALKGNKS--LTTLDLSNNQigdegVIALAEALKNNTTVETLYLSGN 274

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085 111 CLRC-----LNPALGNLTALTYLNLSRNQLS-----SLPPYICQ-LPLRVLIISNNKLG-----ALPPDISTLGSLRQLD 174
Cdd:COG5238   275 QIGAegaiaLAKALQGNTTLTSLDLSVNRIGdegaiALAEGLQGnKTLHTLNLAYNGIGaqgaiALAKALQENTTLHSLD 354

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958669085 175 VSSNEL-----QSLPVELCSLRSLRDLNVRRNQLS-----TLPDELGDLPLVRLDFSCN 223
Cdd:COG5238   355 LSDNQIgdegaIALAKYLEGNTTLRELNLGKNNIGkqgaeALIDALQTNRLHTLILDGN 413
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 563-624 2.72e-04

first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409066 [Multi-domain]  Cd Length: 114  Bit Score: 41.02  E-value: 2.72e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958669085 563 PLPEDLAEALANGVILCQLANQLRPRSVPF--IHVPSPavpkLSALKSRKNVENFLEACRKMGV 624
Cdd:cd21217    28 PDGDDLFEALRDGVLLCKLINKIVPGTIDErkLNKKKP----KNIFEATENLNLALNAAKKIGC 87
LRR_8 pfam13855
Leucine rich repeat;
101-157 3.18e-04

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 39.04  E-value: 3.18e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085 101 SLEGLSLYHNCLRCLNP-ALGNLTALTYLNLSRNQLSSLPPY-ICQLP-LRVLIISNNKL 157
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDDgAFKGLSNLKVLDLSNNLLTTLSPGaFSGLPsLRYLDLSGNRL 61
CH_GAS2 cd21267
calponin homology (CH) domain found in growth arrest-specific protein 2; Growth ...
 566-629 3.32e-04

calponin homology (CH) domain found in growth arrest-specific protein 2; Growth arrest-specific protein 2 (GAS-2) may play a role in apoptosis by acting as a cell death substrate for caspases. It contains a single copy of the CH domain at the N-terminal region. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409116  Cd Length: 136  Bit Score: 41.46  E-value: 3.32e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958669085 566 EDLAEALANGVILCQLANQLRP-------------RSVPFIHVPSPAVPKLSALKSRKNVENFLEACRKMGVPEADL 629
Cdd:cd21267    27 ESFMEKLDNGALLCQLAETLQEkfkensadankpgKSLPVRKIPCRANAPSGSFFARDNTANFLSWCRDVGVGDTCL 103
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 101-140 1.12e-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: 37.22  E-value: 1.12e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1958669085 101 SLEGLSLYHNCLRCLnPALGNLTALTYLNLSRN-QLSSLPP 140
Cdd:pfam12799   2 NLEVLDLSNNQITDI-PPLAKLPNLETLDLSGNnKITDLSD 41
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 112-254 1.14e-03

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


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 41.57  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085 112 LRCLNPALGNLTALTYLNLSRNQLSSLPPYICQL-----PLRVLIISNNKLGALPPDISTLG------SLRQLDVSSNEL 180
Cdd:cd00116    70 LQSLLQGLTKGCGLQELDLSDNALGPDGCGVLESllrssSLQELKLNNNGLGDRGLRLLAKGlkdlppALEKLVLGRNRL 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085 181 -----QSLPVELCSLRSLRDLNVRRNQLS-----TLPDELGDLP-LVRLDFSCNRVSRIPVS-----FCRLRHLQVILLD 244
Cdd:cd00116   150 egascEALAKALRANRDLKELNLANNGIGdagirALAEGLKANCnLEVLDLNNNGLTDEGASalaetLASLKSLEVLNLG 229

                         170
                  ....*....|
gi 1958669085 245 SNPLQSPPAQ 254
Cdd:cd00116   230 DNNLTDAGAA 239
CH_GAS2L3 cd21269
calponin homology (CH) domain found in growth arrest-specific protein 2-like 3; Growth ...
 566-629 1.24e-03

calponin homology (CH) domain found in growth arrest-specific protein 2-like 3; Growth arrest-specific protein 2-like 3 (GAS2L3), also called GAS2-like protein 3, is a cytoskeletal linker protein that may promote and stabilize the formation of the actin and microtubule network. It contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409118  Cd Length: 130  Bit Score: 39.44  E-value: 1.24e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958669085 566 EDLAEALANGVILCQLANQLRPR------SVPFIHVPSPAVP-KLSA----LKSRKNVENFLEACRKMGVPEADL 629
Cdd:cd21269    26 ERFMEELDNGVLLCQLIGVLQSKikeccsTEELKHFPMRKVPcKKDApsgsFFARDNTANFLSWCRAIGVDETYL 100
CH_TAGLN-like cd21209
calponin homology (CH) domain found in the transgelin family; The transgelin (TAGLN) family ...
 572-638 1.72e-03

calponin homology (CH) domain found in the transgelin family; The transgelin (TAGLN) family includes transgelin, transgelin-2 and transgelin-3. Transgelin, also called 22 kDa actin-binding protein, protein WS3-10, or smooth muscle protein 22-alpha (SM22-alpha), acts as an actin cross-linking/gelling protein that may be involved in calcium interactions and in regulating contractile properties of the cell. Transgelin-2, also called epididymis tissue protein Li 7e, or SM22-alpha homolog, acts as an actin-binding protein that induces actin gelation and regulates actin cytoskeleton. It may participate in the development and progression of multiple cancers. Transgelin-3, also called neuronal protein 22 (NP22), or neuronal protein NP25, may have a role in alcohol-related adaptations and may mediate regulatory signal transduction pathways in neurons. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409058 [Multi-domain]  Cd Length: 119  Bit Score: 38.65  E-value: 1.72e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958669085 572 LANGVILCQLANQLRPR-SVPFIHVPSPAVpklsALKSRKNVENFLEACRKMGVPEADLCSPSDLLRG 638
Cdd:cd21209    34 LKDGTVLCKLINSLYPEgSKPVKKIQSSKM----AFKQMEQISQFLKAAEDYGVRTTDIFQTVDLWEG 97
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 341-505 2.28e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 41.61  E-value: 2.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085  341 AREPRGPRQPREDGSGDGDLEQIDFIDSHVPGDDEQSAAEEPLPSELSLAAGDMERPSSSRREEPAGEERR--RPDTLHL 418
Cdd:PRK10263   430 QQPYYAPAPEQPVAGNAWQAEEQQSTFAPQSTYQTEQTYQQPAAQEPLYQQPQPVEQQPVVEPEPVVEETKpaRPPLYYF 509

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085  419 WQERERRL--QQQSGAW-----GPSKKDSIPKRGIRATGAGASAPSTQTACNGP----PKSSAAQLGVSGEQGAPTL-PS 486
Cdd:PRK10263   510 EEVEEKRAreREQLAAWyqpipEPVKEPEPIKSSLKAPSVAAVPPVEAAAAVSPlasgVKKATLATGAAATVAAPVFsLA 589

                          170       180
                   ....*....|....*....|
gi 1958669085  487 TSQDPLP-VSGPVTAPVPRP 505
Cdd:PRK10263   590 NSGGPRPqVKEGIGPQLPRP 609
PLN03150 PLN03150
hypothetical protein; Provisional
 158-231 2.81e-03

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 40.95  E-value: 2.81e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958669085 158 GALPPDISTLGSLRQLDVSSNELQ-SLPVELCSLRSLRDLNVRRNQLS-TLPDELGDLPLVR-LDFSCNRVS-RIPVS 231
Cdd:PLN03150  432 GFIPNDISKLRHLQSINLSGNSIRgNIPPSLGSITSLEVLDLSYNSFNgSIPESLGQLTSLRiLNLNGNSLSgRVPAA 509
LRR smart00370
Leucine-rich repeats, outliers;
122-144 3.01e-03

Leucine-rich repeats, outliers;


Pssm-ID: 197688 [Multi-domain]  Cd Length: 24  Bit Score: 35.41  E-value: 3.01e-03
                           10        20
                   ....*....|....*....|...
gi 1958669085  122 LTALTYLNLSRNQLSSLPPYICQ 144
Cdd:smart00370   1 LPNLRELDLSNNQLSSLPPGAFQ 23
LRR_TYP smart00369
Leucine-rich repeats, typical (most populated) subfamily;
122-144 3.01e-03

Leucine-rich repeats, typical (most populated) subfamily;


Pssm-ID: 197687 [Multi-domain]  Cd Length: 24  Bit Score: 35.41  E-value: 3.01e-03
                           10        20
                   ....*....|....*....|...
gi 1958669085  122 LTALTYLNLSRNQLSSLPPYICQ 144
Cdd:smart00369   1 LPNLRELDLSNNQLSSLPPGAFQ 23
PHA03247 PHA03247
large tegument protein UL36; Provisional
 280-503 4.61e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.69  E-value: 4.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085  280 DLVPSRPPSFSPCPAEDLFPGRRYDGGLDSGFHSVDSGSKRWSgnestddfseLSFRISELAREPRG---PRQPREDGSG 356
Cdd:PHA03247  2620 DTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVS----------RPRRARRLGRAAQAsspPQRPRRRAAR 2689

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085  357 DGDLEQIDFIDSHVPGddeqsAAEEPLPSELSLAAGDMERPSSSRREEPAGEERRRPdtlhlwqererrlqqQSGAWGPS 436
Cdd:PHA03247  2690 PTVGSLTSLADPPPPP-----PTPEPAPHALVSATPLPPGPAAARQASPALPAAPAP---------------PAVPAGPA 2749

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958669085  437 KKDSIPKRGIRATGAGASAPSTQTA-CNGPPKSSAAQLGVSGEQGAPTLPSTSqDPLPVSGPVTAPVP 503
Cdd:PHA03247  2750 TPGGPARPARPPTTAGPPAPAPPAApAAGPPRRLTRPAVASLSESRESLPSPW-DPADPPAAVLAPAA 2816
PRK15387 PRK15387
type III secretion system effector E3 ubiquitin transferase SspH2;
128-256 4.83e-03

type III secretion system effector E3 ubiquitin transferase SspH2;


Pssm-ID: 185285 [Multi-domain]  Cd Length: 788  Bit Score: 40.15  E-value: 4.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669085 128 LNLSRNQLSSLPPYICQLPLRVLIISNN--KLGALPPDistlgsLRQLDVSSNELQSLPVelcSLRSLRDLNVRRNQLST 205
Cdd:PRK15387  206 LNVGESGLTTLPDCLPAHITTLVIPDNNltSLPALPPE------LRTLEVSGNQLTSLPV---LPPGLLELSIFSNPLTH 276

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958669085 206 LPdelgDLP--LVRLDFSCNRVSRIPVSFCRLRHLQVILLDSNPLQSPPAQIC 256
Cdd:PRK15387  277 LP----ALPsgLCKLWIFGNQLTSLPVLPPGLQELSVSDNQLASLPALPSELC 325
CH_alphaPIX cd21265
calponin homology (CH) domain found in alpha-Pak Interactive eXchange factor; Alpha-Pak ...
 565-638 9.15e-03

calponin homology (CH) domain found in alpha-Pak Interactive eXchange factor; Alpha-Pak Interactive eXchange factor (alpha-PIX), also called PAK-interacting exchange factor alpha, Rho guanine nucleotide exchange factor 6 (ARHGEF6), Rac/Cdc42 guanine nucleotide exchange factor 6, or Cool (Cloned out of Library)-2, activates small GTPases by exchanging bound GDP for free GTP. It acts as a GEF for both Cdc42 and Rac1, and is localized in dendritic spines where it regulates spine morphogenesis. It controls dendritic length and spine density in the hippocampus. Mutations in the ARHGEF6 gene cause X-linked intellectual disability in humans. Alpha-PIX contains a single copy of the CH domain at its N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409114  Cd Length: 117  Bit Score: 36.72  E-value: 9.15e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958669085 565 PED-LAEALANGVILCQLANQLRPRSVpFIHVPSPAvpklSALKSRKNVENFLEACRKMGVpeaDLCSPSDLLRG 638
Cdd:cd21265    27 PEEfLKSSLKDGVVLCKLIERLLPGSV-EKYCLEPK----TEADCIGNIKEFLKGCAALKV---ETFEPDDLYTG 93
 
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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