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Conserved domains on  [gi|1958665463|ref|XP_038944264|]
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DISP complex protein LRCH3 isoform X16 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CH_LRCH3 cd21272
calponin homology (CH) domain found in leucine-rich repeat and calponin homology ...
 559-667 3.48e-74

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: 234.11  E-value: 3.48e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665463 559 RLIDQLRKHIEYRLKVSLPCDLGAALTDGVVLCHLANHVRPRSVPSIHVPSPAVPKLTMAKCRRNVENFLDACRKIGVPQ 638
Cdd:cd21272     1 ELIEQLRKNIESRLKVSLPSDLGAALTDGVVLCHLANHVRPRSVPSIHVPSPAVPKLTMAKCRRNVENFLEACRRIGVPQ 80

                          90       100
                  ....*....|....*....|....*....
gi 1958665463 639 EQLCLPLHILEEKGLGQVAVTVQALLELA 667
Cdd:cd21272    81 EQLCLPLHILEEKGLSQVAVTVQALLELA 109
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
76-282 2.54e-41

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


:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 155.86  E-value: 2.54e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665463  76 DLTDTTRADLSRNRLSEIPMETCHFVSLESLNLYQNCIRYIPEAVLNLQALTFLNISRNQLSTLPVHLCNLP-LKVLIAS 154
Cdd:COG4886   111 NLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTnLKELDLS 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665463 155 NNKLVSLPEEIGQLRHLTELDVSCNEIQTVPSQIGNLEALRDFNVRRNHLLRLPEeLAEVP-LIRLDFSCNKITVIPVCY 233
Cdd:COG4886   191 NNQITDLPEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTDLPE-LGNLTnLEELDLSNNQLTDLPPLA 269

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1958665463 234 rNLRHLQVITLDNNPLQSPPAQICIKGKIHIFKYLNIQACKIAPDLPDY 282
Cdd:COG4886   270 -NLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILL 317
 
Name Accession Description Interval E-value
CH_LRCH3 cd21272
calponin homology (CH) domain found in leucine-rich repeat and calponin homology ...
 559-667 3.48e-74

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: 234.11  E-value: 3.48e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665463 559 RLIDQLRKHIEYRLKVSLPCDLGAALTDGVVLCHLANHVRPRSVPSIHVPSPAVPKLTMAKCRRNVENFLDACRKIGVPQ 638
Cdd:cd21272     1 ELIEQLRKNIESRLKVSLPSDLGAALTDGVVLCHLANHVRPRSVPSIHVPSPAVPKLTMAKCRRNVENFLEACRRIGVPQ 80

                          90       100
                  ....*....|....*....|....*....
gi 1958665463 639 EQLCLPLHILEEKGLGQVAVTVQALLELA 667
Cdd:cd21272    81 EQLCLPLHILEEKGLSQVAVTVQALLELA 109
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
76-282 2.54e-41

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 155.86  E-value: 2.54e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665463  76 DLTDTTRADLSRNRLSEIPMETCHFVSLESLNLYQNCIRYIPEAVLNLQALTFLNISRNQLSTLPVHLCNLP-LKVLIAS 154
Cdd:COG4886   111 NLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTnLKELDLS 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665463 155 NNKLVSLPEEIGQLRHLTELDVSCNEIQTVPSQIGNLEALRDFNVRRNHLLRLPEeLAEVP-LIRLDFSCNKITVIPVCY 233
Cdd:COG4886   191 NNQITDLPEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTDLPE-LGNLTnLEELDLSNNQLTDLPPLA 269

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1958665463 234 rNLRHLQVITLDNNPLQSPPAQICIKGKIHIFKYLNIQACKIAPDLPDY 282
Cdd:COG4886   270 -NLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILL 317
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
77-230 1.36e-13

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 74.35  E-value: 1.36e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665463  77 LTDTTR-ADLSRNRLSEIPMetcHFVS-LESLNLYQNCIRYIPEavlNL-QALTFLNISRNQLSTLPVHL---------- 143
Cdd:PRK15370  239 LPDTIQeMELSINRITELPE---RLPSaLQSLDLFHNKISCLPE---NLpEELRYLSVYDNSIRTLPAHLpsgithlnvq 312

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665463 144 --------CNLP--LKVLIASNNKLVSLPEEIGQlrHLTELDVSCNEIQTVPSQIGnlEALRDFNVRRNHLLRLPEELAe 213
Cdd:PRK15370  313 snsltalpETLPpgLKTLEAGENALTSLPASLPP--ELQVLDVSKNQITVLPETLP--PTITTLDVSRNALTNLPENLP- 387

                         170
                  ....*....|....*..
gi 1958665463 214 VPLIRLDFSCNKITVIP 230
Cdd:PRK15370  388 AALQIMQASRNNLVRLP 404
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 562-636 1.03e-11

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: 61.56  E-value: 1.03e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958665463  562 DQLRKHIEYRLKVSLPC---DLGAALTDGVVLCHLANHVRPRSVPSIHVPspavPKLTMAKCRRNVENFLDACRKIGV 636
Cdd:smart00033   1 KTLLRWVNSLLAEYDKPpvtNFSSDLKDGVALCALLNSLSPGLVDKKKVA----ASLSRFKKIENINLALSFAEKLGG 74
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 85-208 1.02e-10

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


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 62.11  E-value: 1.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665463  85 LSRNRLSEIPMETcHFVSLESLNLYQNCIRYIpEAVLNLQALTFLNISRNQLStLPVHLCNLP---------LKVLIASN 155
Cdd:cd21340    53 LQNNQIEKIENLE-NLVNLKKLYLGGNRISVV-EGLENLTNLEELHIENQRLP-PGEKLTFDPrslaalsnsLRVLNISG 129

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958665463 156 NKLVSLpEEIGQLRHLTELDVSCNEIQTVPSQ---IGNLEALRDFNVRRNHLLRLP 208
Cdd:cd21340   130 NNIDSL-EPLAPLRNLEQLDASNNQISDLEELldlLSSWPSLRELDLTGNPVCKKP 184
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 562-638 4.55e-07

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: 48.82  E-value: 4.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665463 562 DQLRKHIEYRLKVSLPC----DLGAALTDGVVLCHLANHVRPRSVPSIHVPSPAVpkltmaKCRRNVENFLD-ACRKIGV 636
Cdd:pfam00307   5 KELLRWINSHLAEYGPGvrvtNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEF------DKLENINLALDvAEKKLGV 78


                  ..
gi 1958665463 637 PQ 638
Cdd:pfam00307  79 PK 80
LRR_8 pfam13855
Leucine rich repeat;
169-249 4.03e-05

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 41.74  E-value: 4.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665463 169 RHLTELDVSCNEIQTV-PSQIGNLEALRdfnvrrnhllrlpeelaevpliRLDFSCNKITVI-PVCYRNLRHLQVITLDN 246
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLdDGAFKGLSNLK----------------------VLDLSNNLLTTLsPGAFSGLPSLRYLDLSG 58


                  ...
gi 1958665463 247 NPL 249
Cdd:pfam13855  59 NRL 61
SCP1 COG5199
Calponin [Cytoskeleton];
559-663 2.74e-04

Calponin [Cytoskeleton];


Pssm-ID: 227526 [Multi-domain]  Cd Length: 178  Bit Score: 42.21  E-value: 2.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665463 559 RLIDQLRKHIEYRL--KVSLPCDLGAALTDGVVLCHLANHVRPRSVPSIHVPSPAVPkltmakcRRNVENFLDACRKIGV 636
Cdd:COG5199    13 KQQKEVTLWIETVLgeKFEPPGDLLSLLKDGVRLCRILNEASPLDIKYKESKMPFVQ-------MENISSFINGLKKLRV 85

                          90       100
                  ....*....|....*....|....*..
gi 1958665463 637 PQEQLCLPLHILEEKGLGQVAVTVQAL 663
Cdd:COG5199    86 PEYELFQTNDLFEAKDLRQVVICLYSL 112
 
Name Accession Description Interval E-value
CH_LRCH3 cd21272
calponin homology (CH) domain found in leucine-rich repeat and calponin homology ...
 559-667 3.48e-74

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: 234.11  E-value: 3.48e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665463 559 RLIDQLRKHIEYRLKVSLPCDLGAALTDGVVLCHLANHVRPRSVPSIHVPSPAVPKLTMAKCRRNVENFLDACRKIGVPQ 638
Cdd:cd21272     1 ELIEQLRKNIESRLKVSLPSDLGAALTDGVVLCHLANHVRPRSVPSIHVPSPAVPKLTMAKCRRNVENFLEACRRIGVPQ 80

                          90       100
                  ....*....|....*....|....*....
gi 1958665463 639 EQLCLPLHILEEKGLGQVAVTVQALLELA 667
Cdd:cd21272    81 EQLCLPLHILEEKGLSQVAVTVQALLELA 109
CH_LRCH cd21205
calponin homology (CH) domain found in the leucine-rich repeat and calponin homology ...
 560-665 1.70e-63

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: 205.61  E-value: 1.70e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665463 560 LIDQLRKHIEYRLKVSLPCDLGAALTDGVVLCHLANHVRPRSVPSIHVPSPAVPKLTMAKCRRNVENFLDACRKIGVPQE 639
Cdd:cd21205     2 QIEQLRKSIESRLKVTLPDDLGEALMDGVVLCHLANHVRPRSVPSIHVPSPAVPKLSMAKCRRNVENFLEACRKLGVPEE 81

                          90       100
                  ....*....|....*....|....*.
gi 1958665463 640 QLCLPLHILEEKGLGQVAVTVQALLE 665
Cdd:cd21205    82 RLCSPGDILEEKGLVRVAVTVQALLQ 107
CH_LRCH2 cd21271
calponin homology (CH) domain found in leucine-rich repeat and calponin homology ...
 556-665 1.29e-60

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: 198.23  E-value: 1.29e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665463 556 EELRLIDQLRKHIEYRLKVSLPCDLGAALTDGVVLCHLANHVRPRSVPSIHVPSPAVPKLTMAKCRRNVENFLDACRKIG 635
Cdd:cd21271     2 EELELIEQLRENIESRLKVILPEDLGAALMDGVVLCHLANHIRPRSVGSIHVPSPAVPKLSMAKCRRNVENFLDACRKLG 81

                          90       100       110
                  ....*....|....*....|....*....|
gi 1958665463 636 VPQEQLCLPLHILEEKGLGQVAVTVQALLE 665
Cdd:cd21271    82 VPEDKLCLPHHILEEKGLVKVSVTVQALLD 111
CH_LRCH1 cd21270
calponin homology (CH) domain found in leucine-rich repeat and calponin homology ...
 556-666 3.28e-52

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: 175.81  E-value: 3.28e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665463 556 EELRLIDQLRKHIEYRLKVSLPCDLGAALTDGVVLCHLANHVRPRSVPSIHVPSPAVPKLTMAKCRRNVENFLDACRKIG 635
Cdd:cd21270     1 EERELTEQLRENIETRLKVSLPEDLGAALMDGVVLCHLVNHVRPRSVASIHVPSPAVPKLSMAKCRRNVENFLEACRKIG 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1958665463 636 VPQEQLCLPLHILEEKGLGqVAVTVQALLEL 666
Cdd:cd21270    81 VPEADLCSPYDILQLNLRG-IRKTVETLLAL 110
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
76-282 2.54e-41

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 155.86  E-value: 2.54e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665463  76 DLTDTTRADLSRNRLSEIPMETCHFVSLESLNLYQNCIRYIPEAVLNLQALTFLNISRNQLSTLPVHLCNLP-LKVLIAS 154
Cdd:COG4886   111 NLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTnLKELDLS 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665463 155 NNKLVSLPEEIGQLRHLTELDVSCNEIQTVPSQIGNLEALRDFNVRRNHLLRLPEeLAEVP-LIRLDFSCNKITVIPVCY 233
Cdd:COG4886   191 NNQITDLPEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTDLPE-LGNLTnLEELDLSNNQLTDLPPLA 269

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1958665463 234 rNLRHLQVITLDNNPLQSPPAQICIKGKIHIFKYLNIQACKIAPDLPDY 282
Cdd:COG4886   270 -NLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILL 317
CH_LRCH4 cd21273
calponin homology (CH) domain found in leucine-rich repeat and calponin homology ...
 560-664 5.39e-39

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: 139.26  E-value: 5.39e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665463 560 LIDQLRKHIEYRLKVSLPCDLGAALTDGVVLCHLANHVRPRSVPSIHVPSPAVPKLTMAKCRRNVENFLDACRKIGVPQE 639
Cdd:cd21273     5 LRAQLRKTLESRLKVTLPEDLAEALSNGAVLCQLANQLRPRSVSIIHVPSPAVPKLSKAKCRKNVENFIEACRKMGVPEV 84

                          90       100
                  ....*....|....*....|....*
gi 1958665463 640 QLCLPLHILEEKGLGQVAVTVQALL 664
Cdd:cd21273    85 DLCSPSDVLLQGPAAVLRTVLALLA 109
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
57-250 1.39e-36

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 142.38  E-value: 1.39e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665463  57 VLSLSGRKLREFPRGAANhdLTDTTRADLSRNRLSEIPMETCHFVSLESLNLYQNCIRYIPEAVLNLQALTFLNISRNQL 136
Cdd:COG4886   117 SLDLSGNQLTDLPEELAN--LTNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQI 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665463 137 STLPVHLCNLP-LKVLIASNNKLVSLPEEIGQLRHLTELDVSCNEIQTVPSqIGNLEALRDFNVRRNHLLRLPEELAEVP 215
Cdd:COG4886   195 TDLPEPLGNLTnLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTDLPE-LGNLTNLEELDLSNNQLTDLPPLANLTN 273

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1958665463 216 LIRLDFSCNKITVIpvcyrNLRHLQVITLDNNPLQ 250
Cdd:COG4886   274 LKTLDLSNNQLTDL-----KLKELELLLGLNSLLL 303
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
76-281 7.07e-33

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 131.59  E-value: 7.07e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665463  76 DLTDTTRADLSRNRLSEIPMETCHFVSLESLNLYQNciryipEAVLNLQALTFLNISRNQLSTLPVHLCNLP-LKVLIAS 154
Cdd:COG4886    71 LLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGN------EELSNLTNLESLDLSGNQLTDLPEELANLTnLKELDLS 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665463 155 NNKLVSLPEEIGQLRHLTELDVSCNEIQTVPSQIGNLEALRDFNVRRNHLLRLPEELAEVP-LIRLDFSCNKITVIPVCY 233
Cdd:COG4886   145 NNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLGNLTnLEELDLSGNQLTDLPEPL 224

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1958665463 234 RNLRHLQVITLDNNPLQSPPAqicIKGKIHIfKYLNIQACKIApDLPD 281
Cdd:COG4886   225 ANLTNLETLDLSNNQLTDLPE---LGNLTNL-EELDLSNNQLT-DLPP 267
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 561-663 1.45e-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: 89.71  E-value: 1.45e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665463 561 IDQLRKHIEYRLKVSLP---CDLGAALTDGVVLCHLANHVRPRSVPSIHVPSpavpkLTMAKCRRNVENFLDACRKIGVP 637
Cdd:cd00014     1 EEELLKWINEVLGEELPvsiTDLFESLRDGVLLCKLINKLSPGSIPKINKKP-----KSPFKKRENINLFLNACKKLGLP 75

                          90       100
                  ....*....|....*....|....*.
gi 1958665463 638 QEQLCLPLHILEEKGLGQVAVTVQAL 663
Cdd:cd00014    76 ELDLFEPEDLYEKGNLKKVLGTLWAL 101
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
77-230 1.36e-13

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 74.35  E-value: 1.36e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665463  77 LTDTTR-ADLSRNRLSEIPMetcHFVS-LESLNLYQNCIRYIPEavlNL-QALTFLNISRNQLSTLPVHL---------- 143
Cdd:PRK15370  239 LPDTIQeMELSINRITELPE---RLPSaLQSLDLFHNKISCLPE---NLpEELRYLSVYDNSIRTLPAHLpsgithlnvq 312

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665463 144 --------CNLP--LKVLIASNNKLVSLPEEIGQlrHLTELDVSCNEIQTVPSQIGnlEALRDFNVRRNHLLRLPEELAe 213
Cdd:PRK15370  313 snsltalpETLPpgLKTLEAGENALTSLPASLPP--ELQVLDVSKNQITVLPETLP--PTITTLDVSRNALTNLPENLP- 387

                         170
                  ....*....|....*..
gi 1958665463 214 VPLIRLDFSCNKITVIP 230
Cdd:PRK15370  388 AALQIMQASRNNLVRLP 404
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
74-281 3.82e-13

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 71.89  E-value: 3.82e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665463  74 NHDLTDTTRADLSRNRLSEIPMETCHFVSLESLNLYQNCIRYIPEAVLNLQALTFLNISRNQLSTLPVHLCNLPLKVLIA 153
Cdd:COG4886     1 LLLLLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665463 154 SNNKLVSLPEEIGQLRH-----------------LTELDVSCNEIQTVPSQIGNLEALRDFNVRRNHLLRLPEELAEVP- 215
Cdd:COG4886    81 LLSLLLLGLTDLGDLTNlteldlsgneelsnltnLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLPEPLGNLTn 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958665463 216 LIRLDFSCNKITVIPVCYRNLRHLQVITLDNNPLQSPPAQIcikGKIHIFKYLNIQACKIApDLPD 281
Cdd:COG4886   161 LKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPL---GNLTNLEELDLSGNQLT-DLPE 222
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
57-202 1.43e-12

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 69.96  E-value: 1.43e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665463  57 VLSLSGRKLREFPRGAANhdLTDTTRADLSRNRLSEIPMETCHFVSLESLNLYQNCIRYIPEaVLNLQALTFLNISRNQL 136
Cdd:COG4886   186 ELDLSNNQITDLPEPLGN--LTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTDLPE-LGNLTNLEELDLSNNQL 262

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958665463 137 STLPvHLCNLP-LKVLIASNNKLVSLP----EEIGQLRHLTELDVSCNEIQTVPSQIGNLEALRDFNVRRN 202
Cdd:COG4886   263 TDLP-PLANLTnLKTLDLSNNQLTDLKlkelELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKG 332
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 562-636 1.03e-11

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: 61.56  E-value: 1.03e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958665463  562 DQLRKHIEYRLKVSLPC---DLGAALTDGVVLCHLANHVRPRSVPSIHVPspavPKLTMAKCRRNVENFLDACRKIGV 636
Cdd:smart00033   1 KTLLRWVNSLLAEYDKPpvtNFSSDLKDGVALCALLNSLSPGLVDKKKVA----ASLSRFKKIENINLALSFAEKLGG 74
CH_dMP20-like cd21207
calponin homology (CH) domain found in Drosophila melanogaster muscle-specific protein 20 ...
 579-663 5.19e-11

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: 60.02  E-value: 5.19e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665463 579 DLGAALTDGVVLCHLANHVRPRSVPSIHvpspavpklTMA---KCRRNVENFLDACRKIGVPQEQLCLPLHILEEKGLGQ 655
Cdd:cd21207    27 DYEDVLKDGVILCKLINILKPGSVKKIN---------TSKmafKLMENIENFLTACKGYGVPKTDLFQTVDLYEKKNIPQ 97


                  ....*...
gi 1958665463 656 VAVTVQAL 663
Cdd:cd21207    98 VTNCLFAL 105
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 84-249 6.49e-11

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 65.64  E-value: 6.49e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665463  84 DLSRNRLS-EIPMETCHFVSLESLNLYQNCIR-YIPEAVLNLQALTFLNISRNQLS-TLPVHLCNL-PLK-VLIASNNKL 158
Cdd:PLN00113  146 DLSNNMLSgEIPNDIGSFSSLKVLDLGGNVLVgKIPNSLTNLTSLEFLTLASNQLVgQIPRELGQMkSLKwIYLGYNNLS 225

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665463 159 VSLPEEIGQLRHLTELD-VSCNEIQTVPSQIGNLEALRDFNVRRNHLL-RLPEELAEVP-LIRLDFSCNKIT-VIPVCYR 234
Cdd:PLN00113  226 GEIPYEIGGLTSLNHLDlVYNNLTGPIPSSLGNLKNLQYLFLYQNKLSgPIPPSIFSLQkLISLDLSDNSLSgEIPELVI 305

                         170
                  ....*....|....*
gi 1958665463 235 NLRHLQVITLDNNPL 249
Cdd:PLN00113  306 QLQNLEILHLFSNNF 320
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 85-208 1.02e-10

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


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 62.11  E-value: 1.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665463  85 LSRNRLSEIPMETcHFVSLESLNLYQNCIRYIpEAVLNLQALTFLNISRNQLStLPVHLCNLP---------LKVLIASN 155
Cdd:cd21340    53 LQNNQIEKIENLE-NLVNLKKLYLGGNRISVV-EGLENLTNLEELHIENQRLP-PGEKLTFDPrslaalsnsLRVLNISG 129

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958665463 156 NKLVSLpEEIGQLRHLTELDVSCNEIQTVPSQ---IGNLEALRDFNVRRNHLLRLP 208
Cdd:cd21340   130 NNIDSL-EPLAPLRNLEQLDASNNQISDLEELldlLSSWPSLRELDLTGNPVCKKP 184
CH_VAV cd21201
calponin homology (CH) domain found in VAV proteins; VAV proteins function both as cytoplasmic ...
 577-656 3.07e-10

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: 58.04  E-value: 3.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665463 577 PCDLGAALTDGVVLCHLANHVRPRSVPSIHVpspaVPKLTMAK--CRRNVENFLDACR-KIGVPQEQLCLPLHILEEKGL 653
Cdd:cd21201    29 VFDLAQALRDGVLLCQLLNRLSPGSVDDREI----NLRPQMSQflCLKNIRTFLQACRtVFGLRSADLFEPEDLYDVTNF 104


                  ...
gi 1958665463 654 GQV 656
Cdd:cd21201   105 GKV 107
CH_SCP1-like cd21210
calponin homology (CH) domain found in Saccharomyces cerevisiae transgelin (SCP1) and similar ...
 577-663 1.00e-09

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: 56.22  E-value: 1.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665463 577 PCDLGAALTDGVVLCHLANHVRPRSVPSIHvpSPAVPKLTMakcrRNVENFLDACRKIGVPQEQLCLPLHILEEKGLGQV 656
Cdd:cd21210    19 QGDLLDALKDGVVLCKLANRILPADIRKYK--ESKMPFVQM----ENISAFLNAARKLGVPENDLFQTVDLFERKNPAQV 92


                  ....*..
gi 1958665463 657 AVTVQAL 663
Cdd:cd21210    93 LQCLHAL 99
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 85-253 1.50e-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: 58.64  E-value: 1.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665463  85 LSRNRLSEIP-METCHfvSLESLNLYQNCIRYIpEAVLNLQALTFLNISRNQLSTLPvHLCNLP-LKVLIASNNKLVSLp 162
Cdd:cd21340     9 LNDKNITKIDnLSLCK--NLKVLYLYDNKITKI-ENLEFLTNLTHLYLQNNQIEKIE-NLENLVnLKKLYLGGNRISVV- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665463 163 EEIGQLRHLTELDVSCneiQTVP----------SQIGNLEALRDFNVRRNHlLRLPEELAEVP-LIRLDFSCNKITVI-P 230
Cdd:cd21340    84 EGLENLTNLEELHIEN---QRLPpgekltfdprSLAALSNSLRVLNISGNN-IDSLEPLAPLRnLEQLDASNNQISDLeE 159

                         170       180
                  ....*....|....*....|....*
gi 1958665463 231 VC--YRNLRHLQVITLDNNPLQSPP 253
Cdd:cd21340   160 LLdlLSSWPSLRELDLTGNPVCKKP 184
CH_LMO7-like cd21208
calponin homology (CH) domain found in LIM domain only protein 7 and similar proteins; This ...
 562-641 1.58e-09

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: 56.19  E-value: 1.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665463 562 DQLRKHIEYRLKVSLPCDL-GAALTDGVVLCHLANHVRPRSVPSI-HVPSPAVpkltmakCRRNVENFLDACRKIGVPQE 639
Cdd:cd21208     3 KEARTWIEAVTGKKFPSDDfRESLEDGILLCELINAIKPGSIKKInRLPTPIA-------GLDNLNLFLKACEDLGLKDS 75


                  ..
gi 1958665463 640 QL 641
Cdd:cd21208    76 QL 77
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 76-227 5.91e-09

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 59.48  E-value: 5.91e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665463  76 DLTDTTRADLSRNRLS-EIPMETCHFVSLESLNLYQNCIR-YIPEAVLNLQALTFLNISRNQLS-TLPVHLCNLP-LKVL 151
Cdd:PLN00113  258 NLKNLQYLFLYQNKLSgPIPPSIFSLQKLISLDLSDNSLSgEIPELVIQLQNLEILHLFSNNFTgKIPVALTSLPrLQVL 337

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665463 152 IASNNKLV-SLPEEIGQLRHLTELDVSCNEIQ-------------------------TVPSQIGNLEALRDFNVRRNHLL 205
Cdd:PLN00113  338 QLWSNKFSgEIPKNLGKHNNLTVLDLSTNNLTgeipeglcssgnlfklilfsnslegEIPKSLGACRSLRRVRLQDNSFS 417

                         170       180
                  ....*....|....*....|....
gi 1958665463 206 -RLPEELAEVPLIR-LDFSCNKIT 227
Cdd:PLN00113  418 gELPSEFTKLPLVYfLDISNNNLQ 441
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
115-256 2.00e-08

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 57.78  E-value: 2.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665463 115 YIPEAVlnlqalTFLNISRNQLSTLPVHLcNLPLKVLIASNNKLVSLPE-----------EIGQLRHLTE--------LD 175
Cdd:PRK15370  196 CIPEQI------TTLILDNNELKSLPENL-QGNIKTLYANSNQLTSIPAtlpdtiqemelSINRITELPErlpsalqsLD 268

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665463 176 VSCNEIQTVPSQIGnlEALRDFNVRRNHLLRLPEELAEvPLIRLDFSCNKITVIPVCYRnlRHLQVITLDNNPLQSPPAQ 255
Cdd:PRK15370  269 LFHNKISCLPENLP--EELRYLSVYDNSIRTLPAHLPS-GITHLNVQSNSLTALPETLP--PGLKTLEAGENALTSLPAS 343


                  .
gi 1958665463 256 I 256
Cdd:PRK15370  344 L 344
CH_CNN cd21211
calponin homology (CH) domain found in the calponin family; Calponin is an actin ...
 553-667 4.22e-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: 4.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665463 553 QREEELRlidqlrKHIEYRLKVSLPCDLGAALTDGVVLCHLANHVRPRSVPSIHVPSPAVPKLtmakcrRNVENFLDACR 632
Cdd:cd21211     3 QKEAELR------TWIEGVTGLSIGPNFQKGLKDGIILCELINKLQPGSVKKINESMQNWHQL------ENIGNFIKAIV 70

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1958665463 633 KIGVPQEQLCLPLHILEEKGLGQVAVTVQALLELA 667
Cdd:cd21211    71 SYGMKPHDIFEANDLFENGNMTQVQVTLLALAGKA 105
CH_CNN2 cd21283
calponin homology (CH) domain found in calponin-2; Calponin-2 (CNN2), also called neutral ...
 553-667 2.17e-07

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: 49.54  E-value: 2.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665463 553 QREEELRLidqlrkHIEYRLKVSLPCDLGAALTDGVVLCHLANHVRPRSVPSIHVPSPAVPKLtmakcrRNVENFLDACR 632
Cdd:cd21283     3 QKEAELRT------WIEGLTGRSIGPDFQKGLKDGVILCELMNKLQPGSVPKINRSMQNWHQL------ENLSNFIKAMV 70

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1958665463 633 KIGVPQEQLCLPLHILEEKGLGQVAVTVQALLELA 667
Cdd:cd21283    71 SYGMKPVDLFEANDLFESGNMTQVQVSLLALAGMA 105
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 76-204 2.18e-07

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 54.47  E-value: 2.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665463  76 DLTDTTRADLSRNRLS-EIPmETCHFVSLESLNLYQNCIR-YIPEAVLNLQALTFLNISRNQLS-TLPVHLCNLP-LKVL 151
Cdd:PLN00113  450 DMPSLQMLSLARNKFFgGLP-DSFGSKRLENLDLSRNQFSgAVPRKLGSLSELMQLKLSENKLSgEIPDELSSCKkLVSL 528

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958665463 152 IASNNKLV-SLPEEIGQLRHLTELDVSCNEIQ-TVPSQIGNLEALRDFNVRRNHL 204
Cdd:PLN00113  529 DLSHNQLSgQIPASFSEMPVLSQLDLSQNQLSgEIPKNLGNVESLVQVNISHNHL 583
CH_AtKIN14-like cd21203
calponin homology (CH) domain found in Arabidopsis thaliana Kinesin-like KIN-14 protein family; ...
 579-666 2.33e-07

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: 49.72  E-value: 2.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665463 579 DLGAALTDGVVLCHLANHVRPRSVPSI--HVPSPAVPKLTMAKCRRNVENFLDACRKIGVPQeqlcLPLHILEEKGLGQV 656
Cdd:cd21203    25 EFRLCLRDGVVLCKLLNKLQPGAVPKVveSPDDPDGAAGSAFQYFENVRNFLVAIEEMGLPT----FEASDLEQGGGGSR 100

                          90
                  ....*....|
gi 1958665463 657 AVTVQALLEL 666
Cdd:cd21203   101 PRVVDCILAL 110
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 562-638 4.55e-07

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: 48.82  E-value: 4.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665463 562 DQLRKHIEYRLKVSLPC----DLGAALTDGVVLCHLANHVRPRSVPSIHVPSPAVpkltmaKCRRNVENFLD-ACRKIGV 636
Cdd:pfam00307   5 KELLRWINSHLAEYGPGvrvtNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEF------DKLENINLALDvAEKKLGV 78


                  ..
gi 1958665463 637 PQ 638
Cdd:pfam00307  79 PK 80
CH_VAV1 cd21262
calponin homology (CH) domain found in VAV1 protein; VAV1 is expressed predominantly in the ...
 578-663 5.80e-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: 48.79  E-value: 5.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665463 578 CDLGAALTDGVVLCHLANHVRPRSVPSIHVpsPAVPKLTMAKCRRNVENFLDAC-RKIGVPQEQLCLPLHILEEKGLGQV 656
Cdd:cd21262    30 CDLAQALRDGVLLCQLLNNLLPHAVNLREI--NLRPQMSQFLCLKNIRTFLSTCcEKFGLRKSELFEAFDLFDVRDFGKV 107


                  ....*..
gi 1958665463 657 AVTVQAL 663
Cdd:cd21262   108 IDTLSIL 114
PRK15387 PRK15387
type III secretion system effector E3 ubiquitin transferase SspH2;
125-253 2.18e-06

type III secretion system effector E3 ubiquitin transferase SspH2;


Pssm-ID: 185285 [Multi-domain]  Cd Length: 788  Bit Score: 50.93  E-value: 2.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665463 125 ALTFLNISRNQLSTLPVhlcnLPLKV--LIASNNKLVSLPEEIGQLRhltELDVSCNEIQTVPSQIGNLEALRDFNVRRN 202
Cdd:PRK15387  303 GLQELSVSDNQLASLPA----LPSELckLWAYNNQLTSLPTLPSGLQ---ELSVSDNQLASLPTLPSELYKLWAYNNRLT 375

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958665463 203 HLLRLPEELAEvplirLDFSCNKITVIPVCYRNLRHLQVitlDNNPLQSPP 253
Cdd:PRK15387  376 SLPALPSGLKE-----LIVSGNRLTSLPVLPSELKELMV---SGNRLTSLP 418
PRK15387 PRK15387
type III secretion system effector E3 ubiquitin transferase SspH2;
85-211 2.70e-06

type III secretion system effector E3 ubiquitin transferase SspH2;


Pssm-ID: 185285 [Multi-domain]  Cd Length: 788  Bit Score: 50.93  E-value: 2.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665463  85 LSRNRLSEIPMETCHFVSLESlnlYQNCIRYIPEAVLNLQALTflnISRNQLSTLPV-------------HLCNLP---- 147
Cdd:PRK15387  309 VSDNQLASLPALPSELCKLWA---YNNQLTSLPTLPSGLQELS---VSDNQLASLPTlpselyklwaynnRLTSLPalps 382

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958665463 148 -LKVLIASNNKLVSLPEEIGQLRhltELDVSCNEIQTVPSQIGNLEALrdfNVRRNHLLRLPEEL 211
Cdd:PRK15387  383 gLKELIVSGNRLTSLPVLPSELK---ELMVSGNRLTSLPMLPSGLLSL---SVYRNQLTRLPESL 441
CH_CNN3 cd21284
calponin homology (CH) domain found in calponin-3; Calponin-3 (CNN3), also called acidic ...
 553-667 3.07e-06

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: 46.44  E-value: 3.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665463 553 QREEELRLidqlrkHIEYRLKVSLPCDLGAALTDGVVLCHLANHVRPRSVPSIHVPSPAVPKLtmakcrRNVENFLDACR 632
Cdd:cd21284     5 QKEEELRN------WIEEVTGMSIGENFQKGLKDGVILCELINKLQPGSIRKINESKLNWHQL------ENIGNFIKAIQ 72

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1958665463 633 KIGVPQEQLCLPLHILEEKGLGQVAVTVQALLELA 667
Cdd:cd21284    73 AYGMKPHDIFEANDLFENGNMTQVQTTLLALAGLA 107
CH_PIX cd21202
calponin homology (CH) domain found in the Pak Interactive eXchange factor family; Pak ...
 580-663 5.27e-06

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: 45.99  E-value: 5.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665463 580 LGAALTDGVVLCHLANHVRPRSVPSIHvPSPavpkLTMAKCRRNVENFLDACRKIGVPQEQLCLPLHILEEKGLGQVAVT 659
Cdd:cd21202    30 LSESLKNGVVLCRLVNRLKPGTVEKIY-DEP----TTEEECLYNFESFLKACQELGILAEEIFDPNDLYSGGNFQKVLST 104


                  ....
gi 1958665463 660 VQAL 663
Cdd:cd21202   105 LERL 108
CH_GAS2-like cd21204
calponin homology (CH) domain found in the growth arrest-specific protein 2 family; The growth ...
 583-667 6.98e-06

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: 46.11  E-value: 6.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665463 583 ALTDGVVLCHLANHVRPRSVPSIHVPSPAVPKLTM-AKC-----------RRNVENFLDACRKIGVPQEQLCLPLHILEE 650
Cdd:cd21204    31 ELRNGVVLCQLAQKIQEAAEKAREAGKKNGPPPSYkLKCnenakpgsffaRDNVANFLRWCRKLGVDEVLLFESEDLVLH 110

                          90
                  ....*....|....*..
gi 1958665463 651 KGLGQVAVTvqaLLELA 667
Cdd:cd21204   111 KNPRQVLLC---LLELA 124
CH_CNN1 cd21282
calponin homology (CH) domain found in calponin-1 and similar proteins; Calponin-1 (CNN1), ...
 553-667 9.40e-06

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: 9.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665463 553 QREEELRLidqlrkHIEYRLKVSLPCDLGAALTDGVVLCHLANHVRPRSVPSIHVPSPAVPKLtmakcrRNVENFLDACR 632
Cdd:cd21282     3 QTEEELRV------WIEGVTGRRIGDNFMDGLKDGVILCELINKLQPGSVRKINESTQNWHKL------ENIGNFIKAIM 70

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1958665463 633 KIGVPQEQLCLPLHILEEKGLGQVAVTVQALLELA 667
Cdd:cd21282    71 HYGVKPHDIFEANDLFENTNHTQVQSTLIALASMA 105
LRR_8 pfam13855
Leucine rich repeat;
169-249 4.03e-05

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 41.74  E-value: 4.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665463 169 RHLTELDVSCNEIQTV-PSQIGNLEALRdfnvrrnhllrlpeelaevpliRLDFSCNKITVI-PVCYRNLRHLQVITLDN 246
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLdDGAFKGLSNLK----------------------VLDLSNNLLTTLsPGAFSGLPSLRYLDLSG 58


                  ...
gi 1958665463 247 NPL 249
Cdd:pfam13855  59 NRL 61
CH_VAV3 cd21264
calponin homology (CH) domain found in VAV3 protein and similar proteins; VAV3 is ubiquitously ...
 579-663 5.98e-05

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: 43.03  E-value: 5.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665463 579 DLGAALTDGVVLCHLANHVRPRSV--PSIHVPspavPKLTMAKCRRNVENFLDA-CRKIGVPQEQLCLPLHILEEKGLGQ 655
Cdd:cd21264    31 DLAQTLRDGVLLCQLLNNLRPHSInlKEINLR----PQMSQFLCLKNIRTFLSAcCETFGMRKSELFEAFDLFDVRDFGK 106


                  ....*...
gi 1958665463 656 VAVTVQAL 663
Cdd:cd21264   107 VIETLSKL 114
LRR_8 pfam13855
Leucine rich repeat;
148-204 6.33e-05

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 41.36  E-value: 6.33e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958665463 148 LKVLIASNNKLVSLPEEI-GQLRHLTELDVSCNEIQTV-PSQIGNLEALRDFNVRRNHL 204
Cdd:pfam13855   3 LRSLDLSNNRLTSLDDGAfKGLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
102-169 1.76e-04

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 44.69  E-value: 1.76e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665463 102 SLESLNLYQNCIRYIPEAVLnlQALTFLNISRNQLSTLPVhlcNLP--LKVLIASNNKLVSLPEEIGQLR 169
Cdd:PRK15370  347 ELQVLDVSKNQITVLPETLP--PTITTLDVSRNALTNLPE---NLPaaLQIMQASRNNLVRLPESLPHFR 411
CH_TAGLN2 cd21280
calponin homology (CH) domain found in transgelin-2; Transgelin-2, also called epididymis ...
 584-667 1.78e-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: 42.17  E-value: 1.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665463 584 LTDGVVLCHLANHVRPRSvpsiHVPSPAVPKLTMA-KCRRNVENFLDACRKIGVPQEQLCLPLHILEEKGLGQVAVTVQA 662
Cdd:cd21280    39 LKDGTVLCHLINSLYPKG----QAPVKKIQASTMAfKQMEQISQFLQAAERYGINTTDIFQTVDLWEGKNMASVQRTLMN 114


                  ....*
gi 1958665463 663 LLELA 667
Cdd:cd21280   115 LGGLA 119
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 572-636 2.17e-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: 2.17e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958665463 572 LKVSLPCDLGA-----ALTDGVVLCHLANHVRPRSVP--SIHVPSPavpkLTMAKCRRNVENFLDACRKIGV 636
Cdd:cd21217    20 LKHLLPIDPDGddlfeALRDGVLLCKLINKIVPGTIDerKLNKKKP----KNIFEATENLNLALNAAKKIGC 87
SCP1 COG5199
Calponin [Cytoskeleton];
559-663 2.74e-04

Calponin [Cytoskeleton];


Pssm-ID: 227526 [Multi-domain]  Cd Length: 178  Bit Score: 42.21  E-value: 2.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665463 559 RLIDQLRKHIEYRL--KVSLPCDLGAALTDGVVLCHLANHVRPRSVPSIHVPSPAVPkltmakcRRNVENFLDACRKIGV 636
Cdd:COG5199    13 KQQKEVTLWIETVLgeKFEPPGDLLSLLKDGVRLCRILNEASPLDIKYKESKMPFVQ-------MENISSFINGLKKLRV 85

                          90       100
                  ....*....|....*....|....*..
gi 1958665463 637 PQEQLCLPLHILEEKGLGQVAVTVQAL 663
Cdd:COG5199    86 PEYELFQTNDLFEAKDLRQVVICLYSL 112
CH_IQGAP cd21206
calponin homology (CH) domain found in the IQ motif containing GTPase activating protein ...
 561-637 3.28e-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: 40.67  E-value: 3.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665463 561 IDQLRKHIEYRLKVSLPC--DLGAALTDGVVLCHLANHVRPRSVPSIHVPSpavPKLTMakcrRNVEN---FLDACRKIG 635
Cdd:cd21206    10 LEEAKQWIEACLNEELPPttEFEEELRNGVVLAKLANKFAPKLVPLKKIYD---VGLQF----RHTDNinhFLRALKKIG 82


                  ..
gi 1958665463 636 VP 637
Cdd:cd21206    83 LP 84
CH_LMO7 cd21277
calponin homology (CH) domain found in LIM domain only protein 7; LIM domain only protein 7 ...
 579-644 5.22e-04

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: 40.20  E-value: 5.22e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958665463 579 DLGAALTDGVVLCHLANHVRPRSVPSIHVPSPAVPKLTmakcrrNVENFLDACRKIGVPQEQLCLP 644
Cdd:cd21277    21 DFRSALENGVLLCDLINKIKPGIIKKINRLSTPIAGLD------NINVFLKACEKLGLKEAQLFHP 80
CH_VAV2 cd21263
calponin homology (CH) domain found in VAV2 protein and similar proteins; VAV2 is widely ...
 579-663 7.15e-04

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: 39.94  E-value: 7.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665463 579 DLGAALTDGVVLCHLANHVRPRSVPSIHVPSPavPKLTMAKCRRNVENFLDACR-KIGVPQEQLCLPLHILEEKGLGQVA 657
Cdd:cd21263    31 DLAQALRDGVLLCQLLHNLSPGSIDLKDINFR--PQMSQFLCLKNIRTFLKVCHdKFGLRNSELFDPFDLFDVRDFGKVI 108


                  ....*.
gi 1958665463 658 VTVQAL 663
Cdd:cd21263   109 SALSRL 114
CH_betaPIX cd21266
calponin homology (CH) domain found in beta-Pak Interactive eXchange factor; Beta-Pak ...
 580-631 1.15e-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: 1.15e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958665463 580 LGAALTDGVVLCHLANHVRPRSVPSIHvPSPAvpklTMAKCRRNVENFLDAC 631
Cdd:cd21266    29 LQASLKDGVVLCRLLERLLPGSIDKVY-PEPR----TESECLSNIREFLRGC 75
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
58-230 1.24e-03

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 41.84  E-value: 1.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665463  58 LSLSGRKLREFPRGAanhDLTDTTRADLSRNRLSEIPmETCHFVSLESLNLYQNCIRYIPEAVL-NLQALTFLNISRNQL 136
Cdd:COG4886   233 LDLSNNQLTDLPELG---NLTNLEELDLSNNQLTDLP-PLANLTNLKTLDLSNNQLTDLKLKELeLLLGLNSLLLLLLLL 308

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665463 137 STLPVHLCNLPLKVLIASNNKLVSLPEEIGQLRHLTELDVSCNEIQTVPSQIGNLEALRDFNVRRNHLLRLPEELAEVPL 216
Cdd:COG4886   309 NLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGLLEATLLTLALLLLT 388

                         170
                  ....*....|....
gi 1958665463 217 IRLDFSCNKITVIP 230
Cdd:COG4886   389 LLLLLLTTTAGVLL 402
PRK15387 PRK15387
type III secretion system effector E3 ubiquitin transferase SspH2;
129-257 1.38e-03

type III secretion system effector E3 ubiquitin transferase SspH2;


Pssm-ID: 185285 [Multi-domain]  Cd Length: 788  Bit Score: 42.07  E-value: 1.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665463 129 LNISRNQLSTLPVhlCnLP--LKVLIASNNKLVSLPEEIGQLRhltELDVSCNEIQTVPSQIGNLEALRDFNVRRNHLLR 206
Cdd:PRK15387  206 LNVGESGLTTLPD--C-LPahITTLVIPDNNLTSLPALPPELR---TLEVSGNQLTSLPVLPPGLLELSIFSNPLTHLPA 279

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958665463 207 LPEELAEVPLIRldfscNKITVIPVCYRNLRHLQVITLDNNPLQSPPAQIC 257
Cdd:PRK15387  280 LPSGLCKLWIFG-----NQLTSLPVLPPGLQELSVSDNQLASLPALPSELC 325
CH_TAGLN3 cd21281
calponin homology (CH) domain found in transgelin-3; Transgelin-3, also called neuronal ...
 584-667 1.47e-03

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: 39.17  E-value: 1.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665463 584 LTDGVVLCHLANHVRPRSvpsiHVPSPAVPKLTMA-KCRRNVENFLDACRKIGVPQEQLCLPLHILEEKGLGQVAVTVQA 662
Cdd:cd21281    34 LMDGTILCRLINSLYPPG----KEPIKKISETKMAfKQMEKISQFLQAAEAYGVITTDIFQTVDLWEGKDMAAVQRTLMA 109


                  ....*
gi 1958665463 663 LLELA 667
Cdd:cd21281   110 LGSVA 114
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 99-181 2.80e-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: 40.42  E-value: 2.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665463  99 HFVSLESLNLYQNCIR-----YIPEAVLNLQALTFLNISRNQLSTLPV-HLC------NLPLKVLIASNNKL-----VSL 161
Cdd:cd00116   191 ANCNLEVLDLNNNGLTdegasALAETLASLKSLEVLNLGDNNLTDAGAaALAsallspNISLLTLSLSCNDItddgaKDL 270

                          90       100
                  ....*....|....*....|
gi 1958665463 162 PEEIGQLRHLTELDVSCNEI 181
Cdd:cd00116   271 AEVLAEKESLLELDLRGNKF 290
CH_alphaPIX cd21265
calponin homology (CH) domain found in alpha-Pak Interactive eXchange factor; Alpha-Pak ...
 580-636 4.30e-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: 37.49  E-value: 4.30e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958665463 580 LGAALTDGVVLCHLANHVRPRSVPSiHVPSPAvpklTMAKCRRNVENFLDACRKIGV 636
Cdd:cd21265    31 LKSSLKDGVVLCKLIERLLPGSVEK-YCLEPK----TEADCIGNIKEFLKGCAALKV 82
LRR_8 pfam13855
Leucine rich repeat;
102-158 6.45e-03

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 35.58  E-value: 6.45e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665463 102 SLESLNLYQNCIRYI-PEAVLNLQALTFLNISRNQLSTL-PVHLCNLP-LKVLIASNNKL 158
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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