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Conserved domains on  [gi|891715028|ref|NP_001297603|]
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DISP complex protein LRCH3 isoform 4 [Mus musculus]

Protein Classification

leucine-rich repeat and calponin homology domain-containing protein( domain architecture ID 11469455)

leucine-rich repeat (LRR) and calponin homology (CH) domain-containing protein may participate in protein-protein interactions and/or may cross-link actin filaments into bundles and networks; similar to DISP complex protein LRCH3

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CH_SF super family cl00030
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 647-756 1.59e-60

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).


The actual alignment was detected with superfamily member cd21270:

Pssm-ID: 469584  Cd Length: 112  Bit Score: 199.69  E-value: 1.59e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891715028 647 EELKLIDQLRKHIEYRLKVSLPCDLGAALTDGVVLCHLANHVRPRSVPSIHVPSPAVPKLTMAKCRRNVENFLDACRKIG 726
Cdd:cd21270    1 EERELTEQLRENIETRLKVSLPEDLGAALMDGVVLCHLVNHVRPRSVASIHVPSPAVPKLSMAKCRRNVENFLEACRKIG 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 891715028 727 VPQDNLCSPSDILQLNL-SLKRTVETLLSLG 756
Cdd:cd21270   81 VPEADLCSPYDILQLNLrGIRKTVETLLALG 111
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
80-286 6.37e-41

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


:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 155.48  E-value: 6.37e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891715028  80 DLTDTTRADLSRNRLSEIPMEACHFVSLESLNLYQNCIRYIPEAVLNLQALTFLNISRNQLSTLPVHLCNLP-LKVLIAS 158
Cdd:COG4886  111 NLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTnLKELDLS 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891715028 159 NNKLVSLPEEIGHLRHLTELDVSCNEIQTVPSQIGNLEALRDFNVRRNHLLRLPEeLAEVP-LIRLDFSCNKITVIPVCY 237
Cdd:COG4886  191 NNQITDLPEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTDLPE-LGNLTnLEELDLSNNQLTDLPPLA 269

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 891715028 238 rNLRHLQVITLDNNPLQSPPAQICIKGKIHIFKYLNIQACKIAPDLPDY 286
Cdd:COG4886  270 -NLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILL 317
COG5022 super family cl34868
Myosin heavy chain [General function prediction only];
329-501 1.67e-03

Myosin heavy chain [General function prediction only];


The actual alignment was detected with superfamily member COG5022:

Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 41.99  E-value: 1.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891715028  329 TDEFSDLPLRVAEITKEQRLRRESQYQENRSSVAVTNGGVEHDLDQIDYIDScTTEEEENDVKQPK-----SLDTNSLSS 403
Cdd:COG5022   917 SDLIENLEFKTELIARLKKLLNNIDLEEGPSIEYVKLPELNKLHEVESKLKE-TSEEYEDLLKKSTilvreGNKANSELK 995

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891715028  404 QFMAYI-----EQRRISHEVSPVKPIAVREFQKTEDMKRYSH-----QNRVPVEPsLVLSMPPSHNQLSHSDLELHQRRE 473
Cdd:COG5022   996 NFKKELaelskQYGALQESTKQLKELPVEVAELQSASKIISSestelSILKPLQK-LKGLLLLENNQLQARYKALKLRRE 1074

                         170       180
                  ....*....|....*....|....*...
gi 891715028  474 QSIECTRREAQLAALQYEEEKIRTKQIQ 501
Cdd:COG5022  1075 NSLLDDKQLYQLESTENLLKTINVKDLE 1102
 
Name Accession Description Interval E-value
CH_LRCH1 cd21270
calponin homology (CH) domain found in leucine-rich repeat and calponin homology ...
 647-756 1.59e-60

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: 199.69  E-value: 1.59e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891715028 647 EELKLIDQLRKHIEYRLKVSLPCDLGAALTDGVVLCHLANHVRPRSVPSIHVPSPAVPKLTMAKCRRNVENFLDACRKIG 726
Cdd:cd21270    1 EERELTEQLRENIETRLKVSLPEDLGAALMDGVVLCHLVNHVRPRSVASIHVPSPAVPKLSMAKCRRNVENFLEACRKIG 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 891715028 727 VPQDNLCSPSDILQLNL-SLKRTVETLLSLG 756
Cdd:cd21270   81 VPEADLCSPYDILQLNLrGIRKTVETLLALG 111
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
80-286 6.37e-41

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 155.48  E-value: 6.37e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891715028  80 DLTDTTRADLSRNRLSEIPMEACHFVSLESLNLYQNCIRYIPEAVLNLQALTFLNISRNQLSTLPVHLCNLP-LKVLIAS 158
Cdd:COG4886  111 NLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTnLKELDLS 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891715028 159 NNKLVSLPEEIGHLRHLTELDVSCNEIQTVPSQIGNLEALRDFNVRRNHLLRLPEeLAEVP-LIRLDFSCNKITVIPVCY 237
Cdd:COG4886  191 NNQITDLPEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTDLPE-LGNLTnLEELDLSNNQLTDLPPLA 269

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 891715028 238 rNLRHLQVITLDNNPLQSPPAQICIKGKIHIFKYLNIQACKIAPDLPDY 286
Cdd:COG4886  270 -NLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILL 317
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
81-234 2.31e-13

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 73.96  E-value: 2.31e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891715028  81 LTDTTR-ADLSRNRLSEIPMeacHFVS-LESLNLYQNCIRYIPEavlNL-QALTFLNISRNQLSTLPVHL---------- 147
Cdd:PRK15370 239 LPDTIQeMELSINRITELPE---RLPSaLQSLDLFHNKISCLPE---NLpEELRYLSVYDNSIRTLPAHLpsgithlnvq 312

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891715028 148 --------CNLP--LKVLIASNNKLVSLPEEIGhlRHLTELDVSCNEIQTVPSQIGnlEALRDFNVRRNHLLRLPEELAe 217
Cdd:PRK15370 313 snsltalpETLPpgLKTLEAGENALTSLPASLP--PELQVLDVSKNQITVLPETLP--PTITTLDVSRNALTNLPENLP- 387

                        170
                 ....*....|....*..
gi 891715028 218 VPLIRLDFSCNKITVIP 234
Cdd:PRK15370 388 AALQIMQASRNNLVRLP 404
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 653-755 1.33e-12

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: 64.64  E-value: 1.33e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891715028   653 DQLRKHIEYRLKVSLPC---DLGAALTDGVVLCHLANHVRPRSVPSIHVPspavPKLTMAKCRRNVENFLDACRKIGVPQ 729
Cdd:smart00033   1 KTLLRWVNSLLAEYDKPpvtNFSSDLKDGVALCALLNSLSPGLVDKKKVA----ASLSRFKKIENINLALSFAEKLGGKV 76

                           90       100
                   ....*....|....*....|....*.
gi 891715028   730 DNLcSPSDILQLNLSLKRTVETLLSL 755
Cdd:smart00033  77 VLF-EPEDLVEGPKLILGVIWTLISL 101
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 89-212 2.77e-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: 2.77e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891715028  89 LSRNRLSEIPMEAcHFVSLESLNLYQNCIRYIpEAVLNLQALTFLNISRNQLStLPVHLCNLP---------LKVLIASN 159
Cdd:cd21340   53 LQNNQIEKIENLE-NLVNLKKLYLGGNRISVV-EGLENLTNLEELHIENQRLP-PGEKLTFDPrslaalsnsLRVLNISG 129

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 891715028 160 NKLVSLpEEIGHLRHLTELDVSCNEIQTVPSQ---IGNLEALRDFNVRRNHLLRLP 212
Cdd:cd21340  130 NNIDSL-EPLAPLRNLEQLDASNNQISDLEELldlLSSWPSLRELDLTGNPVCKKP 184
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 653-760 1.26e-08

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: 53.44  E-value: 1.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891715028  653 DQLRKHIEYRLKVSLPC----DLGAALTDGVVLCHLANHVRPRSVPSIHVPSPAVpkltmaKCRRNVENFLD-ACRKIGV 727
Cdd:pfam00307   5 KELLRWINSHLAEYGPGvrvtNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEF------DKLENINLALDvAEKKLGV 78

                          90       100       110
                  ....*....|....*....|....*....|...
gi 891715028  728 PQDNLcSPSDILQLNlsLKRTVETLLSLGARAE 760
Cdd:pfam00307  79 PKVLI-EPEDLVEGD--NKSVLTYLASLFRRFQ 108
LRR_8 pfam13855
Leucine rich repeat;
152-208 2.28e-05

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 42.51  E-value: 2.28e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 891715028  152 LKVLIASNNKLVSLPEEI-GHLRHLTELDVSCNEIQTV-PSQIGNLEALRDFNVRRNHL 208
Cdd:pfam13855   3 LRSLDLSNNRLTSLDDGAfKGLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
COG5022 COG5022
Myosin heavy chain [General function prediction only];
329-501 1.67e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 41.99  E-value: 1.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891715028  329 TDEFSDLPLRVAEITKEQRLRRESQYQENRSSVAVTNGGVEHDLDQIDYIDScTTEEEENDVKQPK-----SLDTNSLSS 403
Cdd:COG5022   917 SDLIENLEFKTELIARLKKLLNNIDLEEGPSIEYVKLPELNKLHEVESKLKE-TSEEYEDLLKKSTilvreGNKANSELK 995

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891715028  404 QFMAYI-----EQRRISHEVSPVKPIAVREFQKTEDMKRYSH-----QNRVPVEPsLVLSMPPSHNQLSHSDLELHQRRE 473
Cdd:COG5022   996 NFKKELaelskQYGALQESTKQLKELPVEVAELQSASKIISSestelSILKPLQK-LKGLLLLENNQLQARYKALKLRRE 1074

                         170       180
                  ....*....|....*....|....*...
gi 891715028  474 QSIECTRREAQLAALQYEEEKIRTKQIQ 501
Cdd:COG5022  1075 NSLLDDKQLYQLESTENLLKTINVKDLE 1102
SCP1 COG5199
Calponin [Cytoskeleton];
650-761 3.34e-03

Calponin [Cytoskeleton];


Pssm-ID: 227526 [Multi-domain]  Cd Length: 178  Bit Score: 39.13  E-value: 3.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891715028 650 KLIDQLRKHIEYRL--KVSLPCDLGAALTDGVVLCHLANHVRPRSVPSIHVPSPAVPkltmakcRRNVENFLDACRKIGV 727
Cdd:COG5199   13 KQQKEVTLWIETVLgeKFEPPGDLLSLLKDGVRLCRILNEASPLDIKYKESKMPFVQ-------MENISSFINGLKKLRV 85

                         90       100       110
                 ....*....|....*....|....*....|....
gi 891715028 728 PQDNLCSPSDILQLNlSLKRTVETLLSLGARAEE 761
Cdd:COG5199   86 PEYELFQTNDLFEAK-DLRQVVICLYSLSRYAQK 118
 
Name Accession Description Interval E-value
CH_LRCH1 cd21270
calponin homology (CH) domain found in leucine-rich repeat and calponin homology ...
 647-756 1.59e-60

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: 199.69  E-value: 1.59e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891715028 647 EELKLIDQLRKHIEYRLKVSLPCDLGAALTDGVVLCHLANHVRPRSVPSIHVPSPAVPKLTMAKCRRNVENFLDACRKIG 726
Cdd:cd21270    1 EERELTEQLRENIETRLKVSLPEDLGAALMDGVVLCHLVNHVRPRSVASIHVPSPAVPKLSMAKCRRNVENFLEACRKIG 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 891715028 727 VPQDNLCSPSDILQLNL-SLKRTVETLLSLG 756
Cdd:cd21270   81 VPEADLCSPYDILQLNLrGIRKTVETLLALG 111
CH_LRCH cd21205
calponin homology (CH) domain found in the leucine-rich repeat and calponin homology ...
 650-755 6.38e-57

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: 189.82  E-value: 6.38e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891715028 650 KLIDQLRKHIEYRLKVSLPCDLGAALTDGVVLCHLANHVRPRSVPSIHVPSPAVPKLTMAKCRRNVENFLDACRKIGVPQ 729
Cdd:cd21205    1 EQIEQLRKSIESRLKVTLPDDLGEALMDGVVLCHLANHVRPRSVPSIHVPSPAVPKLSMAKCRRNVENFLEACRKLGVPE 80

                         90       100
                 ....*....|....*....|....*.
gi 891715028 730 DNLCSPSDILQlNLSLKRTVETLLSL 755
Cdd:cd21205   81 ERLCSPGDILE-EKGLVRVAVTVQAL 105
CH_LRCH3 cd21272
calponin homology (CH) domain found in leucine-rich repeat and calponin homology ...
 650-755 1.89e-56

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: 188.66  E-value: 1.89e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891715028 650 KLIDQLRKHIEYRLKVSLPCDLGAALTDGVVLCHLANHVRPRSVPSIHVPSPAVPKLTMAKCRRNVENFLDACRKIGVPQ 729
Cdd:cd21272    1 ELIEQLRKNIESRLKVSLPSDLGAALTDGVVLCHLANHVRPRSVPSIHVPSPAVPKLTMAKCRRNVENFLEACRRIGVPQ 80

                         90       100
                 ....*....|....*....|....*...
gi 891715028 730 DNLCSPSDILQLN--LSLKRTVETLLSL 755
Cdd:cd21272   81 EQLCLPLHILEEKglSQVAVTVQALLEL 108
CH_LRCH2 cd21271
calponin homology (CH) domain found in leucine-rich repeat and calponin homology ...
 647-740 3.51e-49

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: 168.57  E-value: 3.51e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891715028 647 EELKLIDQLRKHIEYRLKVSLPCDLGAALTDGVVLCHLANHVRPRSVPSIHVPSPAVPKLTMAKCRRNVENFLDACRKIG 726
Cdd:cd21271    2 EELELIEQLRENIESRLKVILPEDLGAALMDGVVLCHLANHIRPRSVGSIHVPSPAVPKLSMAKCRRNVENFLDACRKLG 81

                         90
                 ....*....|....
gi 891715028 727 VPQDNLCSPSDILQ 740
Cdd:cd21271   82 VPEDKLCLPHHILE 95
CH_LRCH4 cd21273
calponin homology (CH) domain found in leucine-rich repeat and calponin homology ...
 647-753 4.00e-41

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: 146.20  E-value: 4.00e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891715028 647 EELKLIDQLRKHIEYRLKVSLPCDLGAALTDGVVLCHLANHVRPRSVPSIHVPSPAVPKLTMAKCRRNVENFLDACRKIG 726
Cdd:cd21273    1 DEKELRAQLRKTLESRLKVTLPEDLAEALSNGAVLCQLANQLRPRSVSIIHVPSPAVPKLSKAKCRKNVENFIEACRKMG 80

                         90       100
                 ....*....|....*....|....*...
gi 891715028 727 VPQDNLCSPSDILQLNLS-LKRTVETLL 753
Cdd:cd21273   81 VPEVDLCSPSDVLLQGPAaVLRTVLALL 108
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
80-286 6.37e-41

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 155.48  E-value: 6.37e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891715028  80 DLTDTTRADLSRNRLSEIPMEACHFVSLESLNLYQNCIRYIPEAVLNLQALTFLNISRNQLSTLPVHLCNLP-LKVLIAS 158
Cdd:COG4886  111 NLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTnLKELDLS 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891715028 159 NNKLVSLPEEIGHLRHLTELDVSCNEIQTVPSQIGNLEALRDFNVRRNHLLRLPEeLAEVP-LIRLDFSCNKITVIPVCY 237
Cdd:COG4886  191 NNQITDLPEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTDLPE-LGNLTnLEELDLSNNQLTDLPPLA 269

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 891715028 238 rNLRHLQVITLDNNPLQSPPAQICIKGKIHIFKYLNIQACKIAPDLPDY 286
Cdd:COG4886  270 -NLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILL 317
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
61-254 4.26e-36

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 141.61  E-value: 4.26e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891715028  61 VLSLSGRKLREFPRGAANhdLTDTTRADLSRNRLSEIPMEACHFVSLESLNLYQNCIRYIPEAVLNLQALTFLNISRNQL 140
Cdd:COG4886  117 SLDLSGNQLTDLPEELAN--LTNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQI 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891715028 141 STLPVHLCNLP-LKVLIASNNKLVSLPEEIGHLRHLTELDVSCNEIQTVPSqIGNLEALRDFNVRRNHLLRLPEELAEVP 219
Cdd:COG4886  195 TDLPEPLGNLTnLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTDLPE-LGNLTNLEELDLSNNQLTDLPPLANLTN 273

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 891715028 220 LIRLDFSCNKITVIpvcyrNLRHLQVITLDNNPLQ 254
Cdd:COG4886  274 LKTLDLSNNQLTDL-----KLKELELLLGLNSLLL 303
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
80-285 1.01e-32

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 131.59  E-value: 1.01e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891715028  80 DLTDTTRADLSRNRLSEIPMEACHFVSLESLNLYQNciryipEAVLNLQALTFLNISRNQLSTLPVHLCNLP-LKVLIAS 158
Cdd:COG4886   71 LLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGN------EELSNLTNLESLDLSGNQLTDLPEELANLTnLKELDLS 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891715028 159 NNKLVSLPEEIGHLRHLTELDVSCNEIQTVPSQIGNLEALRDFNVRRNHLLRLPEELAEVP-LIRLDFSCNKITVIPVCY 237
Cdd:COG4886  145 NNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLGNLTnLEELDLSGNQLTDLPEPL 224

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 891715028 238 RNLRHLQVITLDNNPLQSPPAqicIKGKIHIfKYLNIQACKIApDLPD 285
Cdd:COG4886  225 ANLTNLETLDLSNNQLTDLPE---LGNLTNL-EELDLSNNQLT-DLPP 267
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 652-756 1.05e-21

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: 90.48  E-value: 1.05e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891715028 652 IDQLRKHIEYRLKVSLP---CDLGAALTDGVVLCHLANHVRPRSVPSIHVPSpavpkLTMAKCRRNVENFLDACRKIGVP 728
Cdd:cd00014    1 EEELLKWINEVLGEELPvsiTDLFESLRDGVLLCKLINKLSPGSIPKINKKP-----KSPFKKRENINLFLNACKKLGLP 75

                         90       100
                 ....*....|....*....|....*...
gi 891715028 729 QDNLCSPSDILQLNlSLKRTVETLLSLG 756
Cdd:cd00014   76 ELDLFEPEDLYEKG-NLKKVLGTLWALA 102
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
81-234 2.31e-13

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 73.96  E-value: 2.31e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891715028  81 LTDTTR-ADLSRNRLSEIPMeacHFVS-LESLNLYQNCIRYIPEavlNL-QALTFLNISRNQLSTLPVHL---------- 147
Cdd:PRK15370 239 LPDTIQeMELSINRITELPE---RLPSaLQSLDLFHNKISCLPE---NLpEELRYLSVYDNSIRTLPAHLpsgithlnvq 312

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891715028 148 --------CNLP--LKVLIASNNKLVSLPEEIGhlRHLTELDVSCNEIQTVPSQIGnlEALRDFNVRRNHLLRLPEELAe 217
Cdd:PRK15370 313 snsltalpETLPpgLKTLEAGENALTSLPASLP--PELQVLDVSKNQITVLPETLP--PTITTLDVSRNALTNLPENLP- 387

                        170
                 ....*....|....*..
gi 891715028 218 VPLIRLDFSCNKITVIP 234
Cdd:PRK15370 388 AALQIMQASRNNLVRLP 404
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 653-755 1.33e-12

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: 64.64  E-value: 1.33e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891715028   653 DQLRKHIEYRLKVSLPC---DLGAALTDGVVLCHLANHVRPRSVPSIHVPspavPKLTMAKCRRNVENFLDACRKIGVPQ 729
Cdd:smart00033   1 KTLLRWVNSLLAEYDKPpvtNFSSDLKDGVALCALLNSLSPGLVDKKKVA----ASLSRFKKIENINLALSFAEKLGGKV 76

                           90       100
                   ....*....|....*....|....*.
gi 891715028   730 DNLcSPSDILQLNLSLKRTVETLLSL 755
Cdd:smart00033  77 VLF-EPEDLVEGPKLILGVIWTLISL 101
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
61-206 4.91e-12

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 68.81  E-value: 4.91e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891715028  61 VLSLSGRKLREFPRGAANhdLTDTTRADLSRNRLSEIPMEACHFVSLESLNLYQNCIRYIPEaVLNLQALTFLNISRNQL 140
Cdd:COG4886  186 ELDLSNNQITDLPEPLGN--LTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTDLPE-LGNLTNLEELDLSNNQL 262

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 891715028 141 STLPvHLCNLP-LKVLIASNNKLVSLP----EEIGHLRHLTELDVSCNEIQTVPSQIGNLEALRDFNVRRN 206
Cdd:COG4886  263 TDLP-PLANLTnLKTLDLSNNQLTDLKlkelELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKG 332
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 89-212 2.77e-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: 2.77e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891715028  89 LSRNRLSEIPMEAcHFVSLESLNLYQNCIRYIpEAVLNLQALTFLNISRNQLStLPVHLCNLP---------LKVLIASN 159
Cdd:cd21340   53 LQNNQIEKIENLE-NLVNLKKLYLGGNRISVV-EGLENLTNLEELHIENQRLP-PGEKLTFDPrslaalsnsLRVLNISG 129

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 891715028 160 NKLVSLpEEIGHLRHLTELDVSCNEIQTVPSQ---IGNLEALRDFNVRRNHLLRLP 212
Cdd:cd21340  130 NNIDSL-EPLAPLRNLEQLDASNNQISDLEELldlLSSWPSLRELDLTGNPVCKKP 184
CH_VAV cd21201
calponin homology (CH) domain found in VAV proteins; VAV proteins function both as cytoplasmic ...
 668-752 5.68e-11

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: 60.35  E-value: 5.68e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891715028 668 PCDLGAALTDGVVLCHLANHVRPRSVPSIHVpspaVPKLTMAK--CRRNVENFLDACR-KIGVPQDNLCSPSDILQLNlS 744
Cdd:cd21201   29 VFDLAQALRDGVLLCQLLNRLSPGSVDDREI----NLRPQMSQflCLKNIRTFLQACRtVFGLRSADLFEPEDLYDVT-N 103


                 ....*...
gi 891715028 745 LKRTVETL 752
Cdd:cd21201  104 FGKVIRTL 111
CH_LMO7-like cd21208
calponin homology (CH) domain found in LIM domain only protein 7 and similar proteins; This ...
 653-738 2.13e-10

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: 58.89  E-value: 2.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891715028 653 DQLRKHIEYRLKVSLPCDL-GAALTDGVVLCHLANHVRPRSVPSI-HVPSPAVpkltmakCRRNVENFLDACRKIGVPQD 730
Cdd:cd21208    3 KEARTWIEAVTGKKFPSDDfRESLEDGILLCELINAIKPGSIKKInRLPTPIA-------GLDNLNLFLKACEDLGLKDS 75


                 ....*...
gi 891715028 731 NLCSPSDI 738
Cdd:cd21208   76 QLFDPTDL 83
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 88-253 2.62e-10

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 64.10  E-value: 2.62e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891715028  88 DLSRNRLS-EIPMEACHFVSLESLNLYQNCIR-YIPEAVLNLQALTFLNISRNQLS-TLPVHLCNL-PLK-VLIASNNKL 162
Cdd:PLN00113 146 DLSNNMLSgEIPNDIGSFSSLKVLDLGGNVLVgKIPNSLTNLTSLEFLTLASNQLVgQIPRELGQMkSLKwIYLGYNNLS 225

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891715028 163 VSLPEEIGHLRHLTELD-VSCNEIQTVPSQIGNLEALRDFNVRRNHLL-RLPEELAEVP-LIRLDFSCNKIT-VIPVCYR 238
Cdd:PLN00113 226 GEIPYEIGGLTSLNHLDlVYNNLTGPIPSSLGNLKNLQYLFLYQNKLSgPIPPSIFSLQkLISLDLSDNSLSgEIPELVI 305

                        170
                 ....*....|....*
gi 891715028 239 NLRHLQVITLDNNPL 253
Cdd:PLN00113 306 QLQNLEILHLFSNNF 320
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 89-257 2.86e-09

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: 57.87  E-value: 2.86e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891715028  89 LSRNRLSEIP-MEACHfvSLESLNLYQNCIRYIpEAVLNLQALTFLNISRNQLSTLPvHLCNLP-LKVLIASNNKLVSLp 166
Cdd:cd21340    9 LNDKNITKIDnLSLCK--NLKVLYLYDNKITKI-ENLEFLTNLTHLYLQNNQIEKIE-NLENLVnLKKLYLGGNRISVV- 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891715028 167 EEIGHLRHLTELDVSCneiQTVP----------SQIGNLEALRDFNVRRNHlLRLPEELAEVP-LIRLDFSCNKITVI-P 234
Cdd:cd21340   84 EGLENLTNLEELHIEN---QRLPpgekltfdprSLAALSNSLRVLNISGNN-IDSLEPLAPLRnLEQLDASNNQISDLeE 159

                        170       180
                 ....*....|....*....|....*
gi 891715028 235 VC--YRNLRHLQVITLDNNPLQSPP 257
Cdd:cd21340  160 LLdlLSSWPSLRELDLTGNPVCKKP 184
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
131-273 6.85e-09

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 59.33  E-value: 6.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891715028 131 TFLNISRNQLSTLPvHLCNLPLKVLIASNNKLVSLPEEIGhlRHLTELDVSCNEIQTVPSQIGnlEALRDFNVRRNHLLR 210
Cdd:PRK15370 181 TELRLKILGLTTIP-ACIPEQITTLILDNNELKSLPENLQ--GNIKTLYANSNQLTSIPATLP--DTIQEMELSINRITE 255

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 891715028 211 LPEELAEVpLIRLDFSCNKITVIPvcyRNL-RHLQVITLDNNPLQSPPAQIcIKGKIHIFKYLN 273
Cdd:PRK15370 256 LPERLPSA-LQSLDLFHNKISCLP---ENLpEELRYLSVYDNSIRTLPAHL-PSGITHLNVQSN 314
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 80-231 1.09e-08

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 59.09  E-value: 1.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891715028  80 DLTDTTRADLSRNRLS-EIPMEACHFVSLESLNLYQNCIR-YIPEAVLNLQALTFLNISRNQLS-TLPVHLCNLP-LKVL 155
Cdd:PLN00113 258 NLKNLQYLFLYQNKLSgPIPPSIFSLQKLISLDLSDNSLSgEIPELVIQLQNLEILHLFSNNFTgKIPVALTSLPrLQVL 337

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891715028 156 IASNNKLV-SLPEEIGHLRHLTELDVSCNEIQ-------------------------TVPSQIGNLEALRDFNVRRNHLL 209
Cdd:PLN00113 338 QLWSNKFSgEIPKNLGKHNNLTVLDLSTNNLTgeipeglcssgnlfklilfsnslegEIPKSLGACRSLRRVRLQDNSFS 417

                        170       180
                 ....*....|....*....|....
gi 891715028 210 -RLPEELAEVPLIR-LDFSCNKIT 231
Cdd:PLN00113 418 gELPSEFTKLPLVYfLDISNNNLQ 441
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 653-760 1.26e-08

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: 53.44  E-value: 1.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891715028  653 DQLRKHIEYRLKVSLPC----DLGAALTDGVVLCHLANHVRPRSVPSIHVPSPAVpkltmaKCRRNVENFLD-ACRKIGV 727
Cdd:pfam00307   5 KELLRWINSHLAEYGPGvrvtNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEF------DKLENINLALDvAEKKLGV 78

                          90       100       110
                  ....*....|....*....|....*....|...
gi 891715028  728 PQDNLcSPSDILQLNlsLKRTVETLLSLGARAE 760
Cdd:pfam00307  79 PKVLI-EPEDLVEGD--NKSVLTYLASLFRRFQ 108
CH_dMP20-like cd21207
calponin homology (CH) domain found in Drosophila melanogaster muscle-specific protein 20 ...
 670-740 1.45e-08

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: 53.08  E-value: 1.45e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 891715028 670 DLGAALTDGVVLCHLANHVRPRSVPSIHvpspavpklTMA---KCRRNVENFLDACRKIGVPqdnlcsPSDILQ 740
Cdd:cd21207   27 DYEDVLKDGVILCKLINILKPGSVKKIN---------TSKmafKLMENIENFLTACKGYGVP------KTDLFQ 85
CH_SCP1-like cd21210
calponin homology (CH) domain found in Saccharomyces cerevisiae transgelin (SCP1) and similar ...
 668-757 2.06e-08

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: 52.37  E-value: 2.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891715028 668 PCDLGAALTDGVVLCHLANHVRPRSVPSIHvpSPAVPKLTMakcrRNVENFLDACRKIGVPQDNLCSPSDILQlNLSLKR 747
Cdd:cd21210   19 QGDLLDALKDGVVLCKLANRILPADIRKYK--ESKMPFVQM----ENISAFLNAARKLGVPENDLFQTVDLFE-RKNPAQ 91

                         90
                 ....*....|
gi 891715028 748 TVETLLSLGA 757
Cdd:cd21210   92 VLQCLHALSR 101
CH_AtKIN14-like cd21203
calponin homology (CH) domain found in Arabidopsis thaliana Kinesin-like KIN-14 protein family; ...
 670-755 4.52e-08

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: 52.03  E-value: 4.52e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891715028 670 DLGAALTDGVVLCHLANHVRPRSVPSI--HVPSPAVPKLTMAKCRRNVENFLDACRKIGVPqdnLCSPSDILQLNL-SLK 746
Cdd:cd21203   25 EFRLCLRDGVVLCKLLNKLQPGAVPKVveSPDDPDGAAGSAFQYFENVRNFLVAIEEMGLP---TFEASDLEQGGGgSRP 101


                 ....*....
gi 891715028 747 RTVETLLSL 755
Cdd:cd21203  102 RVVDCILAL 110
CH_CNN cd21211
calponin homology (CH) domain found in the calponin family; Calponin is an actin ...
 644-760 6.17e-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: 51.54  E-value: 6.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891715028 644 QREEELklidqlRKHIEYRLKVSLPCDLGAALTDGVVLCHLANHVRPRSVPSIHVPSPAVPKLtmakcrRNVENFLDACR 723
Cdd:cd21211    3 QKEAEL------RTWIEGVTGLSIGPNFQKGLKDGIILCELINKLQPGSVKKINESMQNWHQL------ENIGNFIKAIV 70

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 891715028 724 KIGVPQDNLCSPSDILQlNLSLKRTVETLLSLGARAE 760
Cdd:cd21211   71 SYGMKPHDIFEANDLFE-NGNMTQVQVTLLALAGKAK 106
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 80-208 3.87e-07

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 53.70  E-value: 3.87e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891715028  80 DLTDTTRADLSRNRLS-EIPmEACHFVSLESLNLYQNCIR-YIPEAVLNLQALTFLNISRNQLS-TLPVHLCNLP-LKVL 155
Cdd:PLN00113 450 DMPSLQMLSLARNKFFgGLP-DSFGSKRLENLDLSRNQFSgAVPRKLGSLSELMQLKLSENKLSgEIPDELSSCKkLVSL 528

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 891715028 156 IASNNKLV-SLPEEIGHLRHLTELDVSCNEIQ-TVPSQIGNLEALRDFNVRRNHL 208
Cdd:PLN00113 529 DLSHNQLSgQIPASFSEMPVLSQLDLSQNQLSgEIPKNLGNVESLVQVNISHNHL 583
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
78-285 4.65e-07

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 53.01  E-value: 4.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891715028  78 NHDLTDTTRADLSRNRLSEIPMEACHFVSLESLNLYQNCIRYIPEAVLNLQALTFLNISRNQLSTLPVHLCNLPLKVLIA 157
Cdd:COG4886    1 LLLLLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891715028 158 SNNKLVSLPEEIGHLRHLTELDVSCNEiqtvpsQIGNLEALRdfnvrrnhllrlpeelaevpliRLDFSCNKITVIPVCY 237
Cdd:COG4886   81 LLSLLLLGLTDLGDLTNLTELDLSGNE------ELSNLTNLE----------------------SLDLSGNQLTDLPEEL 132

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 891715028 238 RNLRHLQVITLDNNPLQSPPAQIcikGKIHIFKYLNIQACKIApDLPD 285
Cdd:COG4886  133 ANLTNLKELDLSNNQLTDLPEPL---GNLTNLKSLDLSNNQLT-DLPE 176
CH_PIX cd21202
calponin homology (CH) domain found in the Pak Interactive eXchange factor family; Pak ...
 671-752 7.80e-07

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: 48.30  E-value: 7.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891715028 671 LGAALTDGVVLCHLANHVRPRSVPSIHvPSPavpkLTMAKCRRNVENFLDACRKIGVPQDNLCSPSDILQL--NLSLKRT 748
Cdd:cd21202   30 LSESLKNGVVLCRLVNRLKPGTVEKIY-DEP----TTEEECLYNFESFLKACQELGILAEEIFDPNDLYSGgnFQKVLST 104


                 ....
gi 891715028 749 VETL 752
Cdd:cd21202  105 LERL 108
CH_CNN2 cd21283
calponin homology (CH) domain found in calponin-2; Calponin-2 (CNN2), also called neutral ...
 644-760 1.76e-06

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: 47.23  E-value: 1.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891715028 644 QREEELKLidqlrkHIEYRLKVSLPCDLGAALTDGVVLCHLANHVRPRSVPSIHVPSPAVPKLtmakcrRNVENFLDACR 723
Cdd:cd21283    3 QKEAELRT------WIEGLTGRSIGPDFQKGLKDGVILCELMNKLQPGSVPKINRSMQNWHQL------ENLSNFIKAMV 70

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 891715028 724 KIGVPQDNLCSPSDILQlNLSLKRTVETLLSLGARAE 760
Cdd:cd21283   71 SYGMKPVDLFEANDLFE-SGNMTQVQVSLLALAGMAK 106
PRK15387 PRK15387
type III secretion system effector E3 ubiquitin transferase SspH2;
129-257 2.88e-06

type III secretion system effector E3 ubiquitin transferase SspH2;


Pssm-ID: 185285 [Multi-domain]  Cd Length: 788  Bit Score: 50.93  E-value: 2.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891715028 129 ALTFLNISRNQLSTLPVhlcnLPLKV--LIASNNKLVSLPEEIGHLRhltELDVSCNEIQTVPSQIGNLEALRDFNVRRN 206
Cdd:PRK15387 303 GLQELSVSDNQLASLPA----LPSELckLWAYNNQLTSLPTLPSGLQ---ELSVSDNQLASLPTLPSELYKLWAYNNRLT 375

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 891715028 207 HLLRLPEELAEvplirLDFSCNKITVIPVCYRNLRHLQVitlDNNPLQSPP 257
Cdd:PRK15387 376 SLPALPSGLKE-----LIVSGNRLTSLPVLPSELKELMV---SGNRLTSLP 418
PRK15387 PRK15387
type III secretion system effector E3 ubiquitin transferase SspH2;
89-215 5.50e-06

type III secretion system effector E3 ubiquitin transferase SspH2;


Pssm-ID: 185285 [Multi-domain]  Cd Length: 788  Bit Score: 50.16  E-value: 5.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891715028  89 LSRNRLSEIPMEACHFVSLESlnlYQNCIRYIPEAVLNLQALTflnISRNQLSTLPV-------------HLCNLP---- 151
Cdd:PRK15387 309 VSDNQLASLPALPSELCKLWA---YNNQLTSLPTLPSGLQELS---VSDNQLASLPTlpselyklwaynnRLTSLPalps 382

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 891715028 152 -LKVLIASNNKLVSLPEEIGHLRhltELDVSCNEIQTVPSQIGNLEALrdfNVRRNHLLRLPEEL 215
Cdd:PRK15387 383 gLKELIVSGNRLTSLPVLPSELK---ELMVSGNRLTSLPMLPSGLLSL---SVYRNQLTRLPESL 441
CH_CNN1 cd21282
calponin homology (CH) domain found in calponin-1 and similar proteins; Calponin-1 (CNN1), ...
 644-760 1.17e-05

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: 44.87  E-value: 1.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891715028 644 QREEELklidqlRKHIEYRLKVSLPCDLGAALTDGVVLCHLANHVRPRSVPSIHVPSPAVPKLtmakcrRNVENFLDACR 723
Cdd:cd21282    3 QTEEEL------RVWIEGVTGRRIGDNFMDGLKDGVILCELINKLQPGSVRKINESTQNWHKL------ENIGNFIKAIM 70

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 891715028 724 KIGVPQDNLCSPSDILQlNLSLKRTVETLLSLGARAE 760
Cdd:cd21282   71 HYGVKPHDIFEANDLFE-NTNHTQVQSTLIALASMAK 106
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 663-742 1.47e-05

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: 44.87  E-value: 1.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891715028 663 LKVSLPCDLGA-----ALTDGVVLCHLANHVRPRSVP--SIHVPSPavpkLTMAKCRRNVENFLDACRKIGVPQDNLcSP 735
Cdd:cd21217   20 LKHLLPIDPDGddlfeALRDGVLLCKLINKIVPGTIDerKLNKKKP----KNIFEATENLNLALNAAKKIGCKVVNI-GP 94


                 ....*..
gi 891715028 736 SDILQLN 742
Cdd:cd21217   95 QDILDGN 101
CH_VAV1 cd21262
calponin homology (CH) domain found in VAV1 protein; VAV1 is expressed predominantly in the ...
 669-755 1.62e-05

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: 44.93  E-value: 1.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891715028 669 CDLGAALTDGVVLCHLANHVRPRSVPSIHVpsPAVPKLTMAKCRRNVENFLDAC-RKIGVPQDNLCSPSDILQLNlSLKR 747
Cdd:cd21262   30 CDLAQALRDGVLLCQLLNNLLPHAVNLREI--NLRPQMSQFLCLKNIRTFLSTCcEKFGLRKSELFEAFDLFDVR-DFGK 106


                 ....*...
gi 891715028 748 TVETLLSL 755
Cdd:cd21262  107 VIDTLSIL 114
CH_CNN3 cd21284
calponin homology (CH) domain found in calponin-3; Calponin-3 (CNN3), also called acidic ...
 644-760 1.63e-05

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: 44.51  E-value: 1.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891715028 644 QREEELklidqlRKHIEYRLKVSLPCDLGAALTDGVVLCHLANHVRPRSVPSIHVPSPAVPKLtmakcrRNVENFLDACR 723
Cdd:cd21284    5 QKEEEL------RNWIEEVTGMSIGENFQKGLKDGVILCELINKLQPGSIRKINESKLNWHQL------ENIGNFIKAIQ 72

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 891715028 724 KIGVPQDNLCSPSDILQlNLSLKRTVETLLSLGARAE 760
Cdd:cd21284   73 AYGMKPHDIFEANDLFE-NGNMTQVQTTLLALAGLAK 108
LRR_8 pfam13855
Leucine rich repeat;
152-208 2.28e-05

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 42.51  E-value: 2.28e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 891715028  152 LKVLIASNNKLVSLPEEI-GHLRHLTELDVSCNEIQTV-PSQIGNLEALRDFNVRRNHL 208
Cdd:pfam13855   3 LRSLDLSNNRLTSLDDGAfKGLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
106-173 3.22e-05

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 47.38  E-value: 3.22e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891715028 106 SLESLNLYQNCIRYIPEAVLnlQALTFLNISRNQLSTLPVhlcNLP--LKVLIASNNKLVSLPEEIGHLR 173
Cdd:PRK15370 347 ELQVLDVSKNQITVLPETLP--PTITTLDVSRNALTNLPE---NLPaaLQIMQASRNNLVRLPESLPHFR 411
CH_GAS2-like cd21204
calponin homology (CH) domain found in the growth arrest-specific protein 2 family; The growth ...
 674-729 3.57e-05

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: 44.18  E-value: 3.57e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 891715028 674 ALTDGVVLCHLANHVRPRSVPSIHVPSPAVPKLTM-AKC-----------RRNVENFLDACRKIGVPQ 729
Cdd:cd21204   31 ELRNGVVLCQLAQKIQEAAEKAREAGKKNGPPPSYkLKCnenakpgsffaRDNVANFLRWCRKLGVDE 98
LRR_8 pfam13855
Leucine rich repeat;
173-253 4.40e-05

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 41.74  E-value: 4.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891715028  173 RHLTELDVSCNEIQTV-PSQIGNLEALRdfnvrrnhllrlpeelaevpliRLDFSCNKITVI-PVCYRNLRHLQVITLDN 250
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLdDGAFKGLSNLK----------------------VLDLSNNLLTTLsPGAFSGLPSLRYLDLSG 58


                  ...
gi 891715028  251 NPL 253
Cdd:pfam13855  59 NRL 61
CH_LMO7 cd21277
calponin homology (CH) domain found in LIM domain only protein 7; LIM domain only protein 7 ...
 670-760 7.13e-05

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: 42.90  E-value: 7.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891715028 670 DLGAALTDGVVLCHLANHVRPRSVPSIHVPSPAVPKLTmakcrrNVENFLDACRKIGVPQDNLCSPSDILQL-------- 741
Cdd:cd21277   21 DFRSALENGVLLCDLINKIKPGIIKKINRLSTPIAGLD------NINVFLKACEKLGLKEAQLFHPGDLQDLstrvtvkq 94

                         90       100
                 ....*....|....*....|..
gi 891715028 742 ---NLSLKRTVETLLSLGARAE 760
Cdd:cd21277   95 eetDRRLKNVLITLYWLGRKAQ 116
CH_VAV3 cd21264
calponin homology (CH) domain found in VAV3 protein and similar proteins; VAV3 is ubiquitously ...
 670-755 1.47e-04

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: 41.87  E-value: 1.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891715028 670 DLGAALTDGVVLCHLANHVRPRSV--PSIHVPspavPKLTMAKCRRNVENFLDA-CRKIGVPQDNLCSPSDILQLNlSLK 746
Cdd:cd21264   31 DLAQTLRDGVLLCQLLNNLRPHSInlKEINLR----PQMSQFLCLKNIRTFLSAcCETFGMRKSELFEAFDLFDVR-DFG 105


                 ....*....
gi 891715028 747 RTVETLLSL 755
Cdd:cd21264  106 KVIETLSKL 114
CH_TAGLN2 cd21280
calponin homology (CH) domain found in transgelin-2; Transgelin-2, also called epididymis ...
 675-765 2.68e-04

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: 41.79  E-value: 2.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891715028 675 LTDGVVLCHLANHVRPRSvpsiHVPSPAVPKLTMA-KCRRNVENFLDACRKIGVPqdnlcsPSDILQL-------NL-SL 745
Cdd:cd21280   39 LKDGTVLCHLINSLYPKG----QAPVKKIQASTMAfKQMEQISQFLQAAERYGIN------TTDIFQTvdlwegkNMaSV 108

                         90       100
                 ....*....|....*....|
gi 891715028 746 KRTVETLLSLGARAEESSFV 765
Cdd:cd21280  109 QRTLMNLGGLAVTRDDGLFV 128
CH_IQGAP cd21206
calponin homology (CH) domain found in the IQ motif containing GTPase activating protein ...
 652-728 5.65e-04

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: 40.29  E-value: 5.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891715028 652 IDQLRKHIEYRLKVSLPC--DLGAALTDGVVLCHLANHVRPRSVPSIHVPSpavPKLTMakcrRNVEN---FLDACRKIG 726
Cdd:cd21206   10 LEEAKQWIEACLNEELPPttEFEEELRNGVVLAKLANKFAPKLVPLKKIYD---VGLQF----RHTDNinhFLRALKKIG 82


                 ..
gi 891715028 727 VP 728
Cdd:cd21206   83 LP 84
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
62-234 1.01e-03

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 42.23  E-value: 1.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891715028  62 LSLSGRKLREFPRGAanhDLTDTTRADLSRNRLSEIPMEAcHFVSLESLNLYQNCIRYIPEAVL-NLQALTFLNISRNQL 140
Cdd:COG4886  233 LDLSNNQLTDLPELG---NLTNLEELDLSNNQLTDLPPLA-NLTNLKTLDLSNNQLTDLKLKELeLLLGLNSLLLLLLLL 308

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891715028 141 STLPVHLCNLPLKVLIASNNKLVSLPEEIGHLRHLTELDVSCNEIQTVPSQIGNLEALRDFNVRRNHLLRLPEELAEVPL 220
Cdd:COG4886  309 NLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGLLEATLLTLALLLLT 388

                        170
                 ....*....|....
gi 891715028 221 IRLDFSCNKITVIP 234
Cdd:COG4886  389 LLLLLLTTTAGVLL 402
CH_betaPIX cd21266
calponin homology (CH) domain found in beta-Pak Interactive eXchange factor; Beta-Pak ...
 671-722 1.20e-03

calponin homology (CH) domain found in beta-Pak Interactive eXchange factor; Beta-Pak Interactive eXchange factor (beta-PIX), also called PAK-interacting exchange factor beta, Rho guanine nucleotide exchange factor 7 (ARHGEF7), p85, or Cool (Cloned out of Library)-1, activates small GTPases by exchanging bound GDP for free GTP. It acts as a GEF for both Cdc42 and Rac1, and plays important roles in regulating neuroendocrine exocytosis, focal adhesion maturation, cell migration, synaptic vesicle localization, and insulin secretion. Beta-PIX contains a single copy of the CH domain at its N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409115  Cd Length: 112  Bit Score: 39.13  E-value: 1.20e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 891715028 671 LGAALTDGVVLCHLANHVRPRSVPSIHvPSPAvpklTMAKCRRNVENFLDAC 722
Cdd:cd21266   29 LQASLKDGVVLCRLLERLLPGSIDKVY-PEPR----TESECLSNIREFLRGC 75
COG5022 COG5022
Myosin heavy chain [General function prediction only];
329-501 1.67e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 41.99  E-value: 1.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891715028  329 TDEFSDLPLRVAEITKEQRLRRESQYQENRSSVAVTNGGVEHDLDQIDYIDScTTEEEENDVKQPK-----SLDTNSLSS 403
Cdd:COG5022   917 SDLIENLEFKTELIARLKKLLNNIDLEEGPSIEYVKLPELNKLHEVESKLKE-TSEEYEDLLKKSTilvreGNKANSELK 995

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891715028  404 QFMAYI-----EQRRISHEVSPVKPIAVREFQKTEDMKRYSH-----QNRVPVEPsLVLSMPPSHNQLSHSDLELHQRRE 473
Cdd:COG5022   996 NFKKELaelskQYGALQESTKQLKELPVEVAELQSASKIISSestelSILKPLQK-LKGLLLLENNQLQARYKALKLRRE 1074

                         170       180
                  ....*....|....*....|....*...
gi 891715028  474 QSIECTRREAQLAALQYEEEKIRTKQIQ 501
Cdd:COG5022  1075 NSLLDDKQLYQLESTENLLKTINVKDLE 1102
CH_alphaPIX cd21265
calponin homology (CH) domain found in alpha-Pak Interactive eXchange factor; Alpha-Pak ...
 671-762 2.09e-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: 38.65  E-value: 2.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891715028 671 LGAALTDGVVLCHLANHVRPRSVPSiHVPSPAvpklTMAKCRRNVENFLDACRKIGVpqdNLCSPSDiLQLNLSLKRTVE 750
Cdd:cd21265   31 LKSSLKDGVVLCKLIERLLPGSVEK-YCLEPK----TEADCIGNIKEFLKGCAALKV---ETFEPDD-LYTGENFSKVLS 101

                         90
                 ....*....|..
gi 891715028 751 TLLSLGARAEES 762
Cdd:cd21265  102 TLLAVNKATEDR 113
PRK15387 PRK15387
type III secretion system effector E3 ubiquitin transferase SspH2;
133-261 2.99e-03

type III secretion system effector E3 ubiquitin transferase SspH2;


Pssm-ID: 185285 [Multi-domain]  Cd Length: 788  Bit Score: 41.30  E-value: 2.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891715028 133 LNISRNQLSTLPVhlCnLP--LKVLIASNNKLVSLPEEIGHLRhltELDVSCNEIQTVPSQIGNLEALRDFNVRRNHLLR 210
Cdd:PRK15387 206 LNVGESGLTTLPD--C-LPahITTLVIPDNNLTSLPALPPELR---TLEVSGNQLTSLPVLPPGLLELSIFSNPLTHLPA 279

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 891715028 211 LPEELAEVPLIRldfscNKITVIPVCYRNLRHLQVITLDNNPLQSPPAQIC 261
Cdd:PRK15387 280 LPSGLCKLWIFG-----NQLTSLPVLPPGLQELSVSDNQLASLPALPSELC 325
SCP1 COG5199
Calponin [Cytoskeleton];
650-761 3.34e-03

Calponin [Cytoskeleton];


Pssm-ID: 227526 [Multi-domain]  Cd Length: 178  Bit Score: 39.13  E-value: 3.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891715028 650 KLIDQLRKHIEYRL--KVSLPCDLGAALTDGVVLCHLANHVRPRSVPSIHVPSPAVPkltmakcRRNVENFLDACRKIGV 727
Cdd:COG5199   13 KQQKEVTLWIETVLgeKFEPPGDLLSLLKDGVRLCRILNEASPLDIKYKESKMPFVQ-------MENISSFINGLKKLRV 85

                         90       100       110
                 ....*....|....*....|....*....|....
gi 891715028 728 PQDNLCSPSDILQLNlSLKRTVETLLSLGARAEE 761
Cdd:COG5199   86 PEYELFQTNDLFEAK-DLRQVVICLYSLSRYAQK 118
CH_LIMCH1 cd21278
calponin homology (CH) domain found in LIM and calponin homology domains-containing protein 1; ...
 670-738 3.47e-03

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: 37.92  E-value: 3.47e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 891715028 670 DLGAALTDGVVLCHLANHVRPRSVPSIH-VPSPaVPKLTmakcrrNVENFLDACRKIGVPQDNLCSPSDI 738
Cdd:cd21278   21 DFRSGLENGILLCELLNAIKPGLVKKINrLPTP-IAGLD------NITLFLRGCKELGLKESQLFDPGDL 83
CH_VAV2 cd21263
calponin homology (CH) domain found in VAV2 protein and similar proteins; VAV2 is widely ...
 670-741 3.95e-03

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: 38.01  E-value: 3.95e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 891715028 670 DLGAALTDGVVLCHLANHVRPRSVPSIHVPSPavPKLTMAKCRRNVENFLDACR-KIGVPQDNLCSPSDILQL 741
Cdd:cd21263   31 DLAQALRDGVLLCQLLHNLSPGSIDLKDINFR--PQMSQFLCLKNIRTFLKVCHdKFGLRNSELFDPFDLFDV 101
LRR_8 pfam13855
Leucine rich repeat;
106-162 6.98e-03

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 35.58  E-value: 6.98e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 891715028  106 SLESLNLYQNCIRYI-PEAVLNLQALTFLNISRNQLSTL-PVHLCNLP-LKVLIASNNKL 162
Cdd:pfam13855   2 NLRSLDLSNNRLTSLdDGAFKGLSNLKVLDLSNNLLTTLsPGAFSGLPsLRYLDLSGNRL 61
 
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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