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Conserved domains on  [gi|356460937|ref|NP_001239061|]
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leucine-rich repeat and calponin homology domain-containing protein 1 isoform 2 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CH_LRCH2 cd21271
calponin homology (CH) domain found in leucine-rich repeat and calponin homology ...
 563-673 2.26e-68

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: 219.03  E-value: 2.26e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356460937 563 REEKELVEQLRESIEMRLKVTLHEDLGAALMDGVVLCHLANHVRPRSVASIHVPSPAVPKLSMAKCRRNVENFLEACRKL 642
Cdd:cd21271    1 REELELIEQLRENIESRLKVILPEDLGAALMDGVVLCHLANHIRPRSVGSIHVPSPAVPKLSMAKCRRNVENFLDACRKL 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 356460937 643 GVPEEKLCLPHHILEEKGLVKVGTTVQALLD 673
Cdd:cd21271   81 GVPEDKLCLPHHILEEKGLVKVSVTVQALLD 111
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
85-262 1.55e-33

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


:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 133.52  E-value: 1.55e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356460937  85 DLSDTVRADLSKNRlvevpmELCQFVSLEILNLYHNCIRVIPEAIVNLQMLTHLNLSRNQLSALPACLCGLP-LKVLIAS 163
Cdd:COG4886   94 DLTNLTELDLSGNE------ELSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLPEPLGNLTnLKSLDLS 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356460937 164 NNKLGSLPEEIGQLKQLMELDVSCNEITALPQQIGQLKSLRELNVRRNYLKVLPPELVDLP-LVKFDFSCNKVLVIPVcF 242
Cdd:COG4886  168 NNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLEELDLSGNQLTDLPEPLANLTnLETLDLSNNQLTDLPE-L 246

                        170       180
                 ....*....|....*....|
gi 356460937 243 REMKQLQVLLLENNPLQSPP 262
Cdd:COG4886  247 GNLTNLEELDLSNNQLTDLP 266
 
Name Accession Description Interval E-value
CH_LRCH2 cd21271
calponin homology (CH) domain found in leucine-rich repeat and calponin homology ...
 563-673 2.26e-68

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: 219.03  E-value: 2.26e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356460937 563 REEKELVEQLRESIEMRLKVTLHEDLGAALMDGVVLCHLANHVRPRSVASIHVPSPAVPKLSMAKCRRNVENFLEACRKL 642
Cdd:cd21271    1 REELELIEQLRENIESRLKVILPEDLGAALMDGVVLCHLANHIRPRSVGSIHVPSPAVPKLSMAKCRRNVENFLDACRKL 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 356460937 643 GVPEEKLCLPHHILEEKGLVKVGTTVQALLD 673
Cdd:cd21271   81 GVPEDKLCLPHHILEEKGLVKVSVTVQALLD 111
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
85-262 1.55e-33

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 133.52  E-value: 1.55e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356460937  85 DLSDTVRADLSKNRlvevpmELCQFVSLEILNLYHNCIRVIPEAIVNLQMLTHLNLSRNQLSALPACLCGLP-LKVLIAS 163
Cdd:COG4886   94 DLTNLTELDLSGNE------ELSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLPEPLGNLTnLKSLDLS 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356460937 164 NNKLGSLPEEIGQLKQLMELDVSCNEITALPQQIGQLKSLRELNVRRNYLKVLPPELVDLP-LVKFDFSCNKVLVIPVcF 242
Cdd:COG4886  168 NNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLEELDLSGNQLTDLPEPLANLTnLETLDLSNNQLTDLPE-L 246

                        170       180
                 ....*....|....*....|
gi 356460937 243 REMKQLQVLLLENNPLQSPP 262
Cdd:COG4886  247 GNLTNLEELDLSNNQLTDLP 266
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
61-264 4.72e-17

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 85.52  E-value: 4.72e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356460937  61 ANSGGLNLSARKLKEFPRTtapghdLSDTVR-ADLSKNRLVEVPMEL----------CQFVS---------LEILNLYHN 120
Cdd:PRK15370 220 GNIKTLYANSNQLTSIPAT------LPDTIQeMELSINRITELPERLpsalqsldlfHNKISclpenlpeeLRYLSVYDN 293

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356460937 121 CIRVIPEAIVNlqMLTHLNLSRNQLSALPACLcGLPLKVLIASNNKLGSLPEEIGqlKQLMELDVSCNEITALPQQIGql 200
Cdd:PRK15370 294 SIRTLPAHLPS--GITHLNVQSNSLTALPETL-PPGLKTLEAGENALTSLPASLP--PELQVLDVSKNQITVLPETLP-- 366

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356460937 201 KSLRELNVRRNYLKVLPPelvDLP--LVKFDFSCNKVLVIPVC---FR-EMKQLQVLLLENNPLQSPPAQ 264
Cdd:PRK15370 367 PTITTLDVSRNALTNLPE---NLPaaLQIMQASRNNLVRLPESlphFRgEGPQPTRIIVEYNPFSERTIQ 433
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 566-671 3.10e-14

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


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 68.88  E-value: 3.10e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356460937   566 KELVEQLRESIEMRLKVTLhEDLGAALMDGVVLCHLANHVRPRSVASIHVPspavPKLSMAKCRRNVENFLEACRKLGvP 645
Cdd:smart00033   1 KTLLRWVNSLLAEYDKPPV-TNFSSDLKDGVALCALLNSLSPGLVDKKKVA----ASLSRFKKIENINLALSFAEKLG-G 74

                           90       100
                   ....*....|....*....|....*..
gi 356460937   646 EEKLCLPHHILE-EKGLVKVGTTVQAL 671
Cdd:smart00033  75 KVVLFEPEDLVEgPKLILGVIWTLISL 101
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 94-211 5.88e-14

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: 71.36  E-value: 5.88e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356460937  94 LSKNRLVEvpME-LCQFVSLEILNLYHNCIRVIpEAIVNLQMLTHLNLSRNQLSA------LPACLCGLP--LKVLIASN 164
Cdd:cd21340   53 LQNNQIEK--IEnLENLVNLKKLYLGGNRISVV-EGLENLTNLEELHIENQRLPPgekltfDPRSLAALSnsLRVLNISG 129

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 356460937 165 NKLGSLpEEIGQLKQLMELDVSCNEIT---ALPQQIGQLKSLRELNVRRN 211
Cdd:cd21340  130 NNIDSL-EPLAPLRNLEQLDASNNQISdleELLDLLSSWPSLRELDLTGN 178
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 562-646 2.34e-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: 49.59  E-value: 2.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356460937  562 MREEKELVEQLRESIEMRLKVTLHEDLGAALMDGVVLCHLANHVRPRSVasihvpSPAVPKLSMAKCRRNVENFLE-ACR 640
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGPGVRVTNFTTDLRDGLALCALLNKLAPGLV------DKKKLNKSEFDKLENINLALDvAEK 74


                  ....*.
gi 356460937  641 KLGVPE 646
Cdd:pfam00307  75 KLGVPK 80
LRR_8 pfam13855
Leucine rich repeat;
93-145 9.94e-07

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 46.36  E-value: 9.94e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 356460937   93 DLSKNRLVEVPMElcQFV---SLEILNLYHNCIRVI-PEAIVNLQMLTHLNLSRNQL 145
Cdd:pfam13855   7 DLSNNRLTSLDDG--AFKglsNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
SCP1 COG5199
Calponin [Cytoskeleton];
559-671 7.94e-04

Calponin [Cytoskeleton];


Pssm-ID: 227526 [Multi-domain]  Cd Length: 178  Bit Score: 41.06  E-value: 7.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356460937 559 MEQMREEKELVEQLREsIEMRLKVTLHE------DLGAALMDGVVLCHLANHVRPrsvASIHVPSPAVPKLSMakcrRNV 632
Cdd:COG5199    2 VNTKNRCPGMDKQQKE-VTLWIETVLGEkfeppgDLLSLLKDGVRLCRILNEASP---LDIKYKESKMPFVQM----ENI 73

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 356460937 633 ENFLEACRKLGVPEEKLCLPHHILEEKGLVKVGTTVQAL 671
Cdd:COG5199   74 SSFINGLKKLRVPEYELFQTNDLFEAKDLRQVVICLYSL 112
 
Name Accession Description Interval E-value
CH_LRCH2 cd21271
calponin homology (CH) domain found in leucine-rich repeat and calponin homology ...
 563-673 2.26e-68

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: 219.03  E-value: 2.26e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356460937 563 REEKELVEQLRESIEMRLKVTLHEDLGAALMDGVVLCHLANHVRPRSVASIHVPSPAVPKLSMAKCRRNVENFLEACRKL 642
Cdd:cd21271    1 REELELIEQLRENIESRLKVILPEDLGAALMDGVVLCHLANHIRPRSVGSIHVPSPAVPKLSMAKCRRNVENFLDACRKL 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 356460937 643 GVPEEKLCLPHHILEEKGLVKVGTTVQALLD 673
Cdd:cd21271   81 GVPEDKLCLPHHILEEKGLVKVSVTVQALLD 111
CH_LRCH cd21205
calponin homology (CH) domain found in the leucine-rich repeat and calponin homology ...
 567-673 1.42e-65

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: 211.39  E-value: 1.42e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356460937 567 ELVEQLRESIEMRLKVTLHEDLGAALMDGVVLCHLANHVRPRSVASIHVPSPAVPKLSMAKCRRNVENFLEACRKLGVPE 646
Cdd:cd21205    1 EQIEQLRKSIESRLKVTLPDDLGEALMDGVVLCHLANHVRPRSVPSIHVPSPAVPKLSMAKCRRNVENFLEACRKLGVPE 80

                         90       100
                 ....*....|....*....|....*..
gi 356460937 647 EKLCLPHHILEEKGLVKVGTTVQALLD 673
Cdd:cd21205   81 ERLCSPGDILEEKGLVRVAVTVQALLQ 107
CH_LRCH3 cd21272
calponin homology (CH) domain found in leucine-rich repeat and calponin homology ...
 567-674 1.34e-59

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: 195.59  E-value: 1.34e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356460937 567 ELVEQLRESIEMRLKVTLHEDLGAALMDGVVLCHLANHVRPRSVASIHVPSPAVPKLSMAKCRRNVENFLEACRKLGVPE 646
Cdd:cd21272    1 ELIEQLRKNIESRLKVSLPSDLGAALTDGVVLCHLANHVRPRSVPSIHVPSPAVPKLTMAKCRRNVENFLEACRRIGVPQ 80

                         90       100
                 ....*....|....*....|....*...
gi 356460937 647 EKLCLPHHILEEKGLVKVGTTVQALLDV 674
Cdd:cd21272   81 EQLCLPLHILEEKGLSQVAVTVQALLEL 108
CH_LRCH1 cd21270
calponin homology (CH) domain found in leucine-rich repeat and calponin homology ...
 564-672 1.33e-55

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: 185.06  E-value: 1.33e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356460937 564 EEKELVEQLRESIEMRLKVTLHEDLGAALMDGVVLCHLANHVRPRSVASIHVPSPAVPKLSMAKCRRNVENFLEACRKLG 643
Cdd:cd21270    1 EERELTEQLRENIETRLKVSLPEDLGAALMDGVVLCHLVNHVRPRSVASIHVPSPAVPKLSMAKCRRNVENFLEACRKIG 80

                         90       100
                 ....*....|....*....|....*....
gi 356460937 644 VPEEKLCLPHHILEEKgLVKVGTTVQALL 672
Cdd:cd21270   81 VPEADLCSPYDILQLN-LRGIRKTVETLL 108
CH_LRCH4 cd21273
calponin homology (CH) domain found in leucine-rich repeat and calponin homology ...
 564-672 3.33e-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: 145.43  E-value: 3.33e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356460937 564 EEKELVEQLRESIEMRLKVTLHEDLGAALMDGVVLCHLANHVRPRSVASIHVPSPAVPKLSMAKCRRNVENFLEACRKLG 643
Cdd:cd21273    1 DEKELRAQLRKTLESRLKVTLPEDLAEALSNGAVLCQLANQLRPRSVSIIHVPSPAVPKLSKAKCRKNVENFIEACRKMG 80

                         90       100
                 ....*....|....*....|....*....
gi 356460937 644 VPEEKLCLPHHILEEKGLVKVGTTVQALL 672
Cdd:cd21273   81 VPEVDLCSPSDVLLQGPAAVLRTVLALLA 109
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
85-262 1.55e-33

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 133.52  E-value: 1.55e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356460937  85 DLSDTVRADLSKNRlvevpmELCQFVSLEILNLYHNCIRVIPEAIVNLQMLTHLNLSRNQLSALPACLCGLP-LKVLIAS 163
Cdd:COG4886   94 DLTNLTELDLSGNE------ELSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLPEPLGNLTnLKSLDLS 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356460937 164 NNKLGSLPEEIGQLKQLMELDVSCNEITALPQQIGQLKSLRELNVRRNYLKVLPPELVDLP-LVKFDFSCNKVLVIPVcF 242
Cdd:COG4886  168 NNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLEELDLSGNQLTDLPEPLANLTnLETLDLSNNQLTDLPE-L 246

                        170       180
                 ....*....|....*....|
gi 356460937 243 REMKQLQVLLLENNPLQSPP 262
Cdd:COG4886  247 GNLTNLEELDLSNNQLTDLP 266
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 569-671 1.28e-19

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: 84.31  E-value: 1.28e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356460937 569 VEQLRESIEMRLKVTLH---EDLGAALMDGVVLCHLANHVRPRSVASIHVPSpavpkLSMAKCRRNVENFLEACRKLGVP 645
Cdd:cd00014    1 EEELLKWINEVLGEELPvsiTDLFESLRDGVLLCKLINKLSPGSIPKINKKP-----KSPFKKRENINLFLNACKKLGLP 75

                         90       100
                 ....*....|....*....|....*.
gi 356460937 646 EEKLCLPHHILEEKGLVKVGTTVQAL 671
Cdd:cd00014   76 ELDLFEPEDLYEKGNLKKVLGTLWAL 101
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
61-264 4.72e-17

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 85.52  E-value: 4.72e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356460937  61 ANSGGLNLSARKLKEFPRTtapghdLSDTVR-ADLSKNRLVEVPMEL----------CQFVS---------LEILNLYHN 120
Cdd:PRK15370 220 GNIKTLYANSNQLTSIPAT------LPDTIQeMELSINRITELPERLpsalqsldlfHNKISclpenlpeeLRYLSVYDN 293

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356460937 121 CIRVIPEAIVNlqMLTHLNLSRNQLSALPACLcGLPLKVLIASNNKLGSLPEEIGqlKQLMELDVSCNEITALPQQIGql 200
Cdd:PRK15370 294 SIRTLPAHLPS--GITHLNVQSNSLTALPETL-PPGLKTLEAGENALTSLPASLP--PELQVLDVSKNQITVLPETLP-- 366

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356460937 201 KSLRELNVRRNYLKVLPPelvDLP--LVKFDFSCNKVLVIPVC---FR-EMKQLQVLLLENNPLQSPPAQ 264
Cdd:PRK15370 367 PTITTLDVSRNALTNLPE---NLPaaLQIMQASRNNLVRLPESlphFRgEGPQPTRIIVEYNPFSERTIQ 433
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 566-671 3.10e-14

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


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 68.88  E-value: 3.10e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356460937   566 KELVEQLRESIEMRLKVTLhEDLGAALMDGVVLCHLANHVRPRSVASIHVPspavPKLSMAKCRRNVENFLEACRKLGvP 645
Cdd:smart00033   1 KTLLRWVNSLLAEYDKPPV-TNFSSDLKDGVALCALLNSLSPGLVDKKKVA----ASLSRFKKIENINLALSFAEKLG-G 74

                           90       100
                   ....*....|....*....|....*..
gi 356460937   646 EEKLCLPHHILE-EKGLVKVGTTVQAL 671
Cdd:smart00033  75 KVVLFEPEDLVEgPKLILGVIWTLISL 101
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 94-211 5.88e-14

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: 71.36  E-value: 5.88e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356460937  94 LSKNRLVEvpME-LCQFVSLEILNLYHNCIRVIpEAIVNLQMLTHLNLSRNQLSA------LPACLCGLP--LKVLIASN 164
Cdd:cd21340   53 LQNNQIEK--IEnLENLVNLKKLYLGGNRISVV-EGLENLTNLEELHIENQRLPPgekltfDPRSLAALSnsLRVLNISG 129

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 356460937 165 NKLGSLpEEIGQLKQLMELDVSCNEIT---ALPQQIGQLKSLRELNVRRN 211
Cdd:cd21340  130 NNIDSL-EPLAPLRNLEQLDASNNQISdleELLDLLSSWPSLRELDLTGN 178
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 82-278 2.76e-12

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 70.26  E-value: 2.76e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356460937  82 PGHDLSDTVRADLSKNRLV-EVPMELCQFVSLEILNLYHNCIR-VIPEAIVNLQMLTHLNLSRNQLSA-LPACLCGL-PL 157
Cdd:PLN00113 135 PRGSIPNLETLDLSNNMLSgEIPNDIGSFSSLKVLDLGGNVLVgKIPNSLTNLTSLEFLTLASNQLVGqIPRELGQMkSL 214

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356460937 158 K-VLIASNNKLGSLPEEIGQLKQLMELDVSCNEITA-LPQQIGQLKSLRELNVRRNYLK-VLPPELVDLP-LVKFDFSCN 233
Cdd:PLN00113 215 KwIYLGYNNLSGEIPYEIGGLTSLNHLDLVYNNLTGpIPSSLGNLKNLQYLFLYQNKLSgPIPPSIFSLQkLISLDLSDN 294

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 356460937 234 KVL-VIPVCFREMKQLQVL-LLENNPLQSPPAQICTKGKVHIFKYLS 278
Cdd:PLN00113 295 SLSgEIPELVIQLQNLEILhLFSNNFTGKIPVALTSLPRLQVLQLWS 341
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
93-225 2.80e-11

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 66.11  E-value: 2.80e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356460937  93 DLSKNRLVEVPMELCQFVSLEILNLYHNCIRVIPEaIVNLQMLTHLNLSRNQLSALPACLCGLPLKVLIASNNKLGSLP- 171
Cdd:COG4886  211 DLSGNQLTDLPEPLANLTNLETLDLSNNQLTDLPE-LGNLTNLEELDLSNNQLTDLPPLANLTNLKTLDLSNNQLTDLKl 289

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 356460937 172 ---EEIGQLKQLMELDVSCNEITALPQQIGQLKSLRELNVRRNYLKVLPPELVDLPL 225
Cdd:COG4886  290 kelELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSL 346
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 67-256 7.05e-11

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 65.64  E-value: 7.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356460937  67 NLSARKLKEFPRTTAPGHdlsdtvrADLSKNRLV-EVPMELCQFVSLEILNLYHNCIR-VIPEAIVNLQMLTHLNLSRNQ 144
Cdd:PLN00113 223 NLSGEIPYEIGGLTSLNH-------LDLVYNNLTgPIPSSLGNLKNLQYLFLYQNKLSgPIPPSIFSLQKLISLDLSDNS 295

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356460937 145 LSA-------------------------LPACLCGLP-LKVL-IASNNKLGSLPEEIGQLKQLMELDVSCNEITA----- 192
Cdd:PLN00113 296 LSGeipelviqlqnleilhlfsnnftgkIPVALTSLPrLQVLqLWSNKFSGEIPKNLGKHNNLTVLDLSTNNLTGeipeg 375

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356460937 193 --------------------LPQQIGQLKSLRELNVRRNYLK-VLPPELVDLPLVKF-DFSCNKVL-VIPVCFREMKQLQ 249
Cdd:PLN00113 376 lcssgnlfklilfsnslegeIPKSLGACRSLRRVRLQDNSFSgELPSEFTKLPLVYFlDISNNNLQgRINSRKWDMPSLQ 455


                 ....*..
gi 356460937 250 VLLLENN 256
Cdd:PLN00113 456 MLSLARN 462
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
73-296 7.43e-11

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 65.49  E-value: 7.43e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356460937  73 LKEFPRTTAPGHDLS-DTVRADLSKNRlvevpMELCqfvsLEILNLyhnciRVIPEAIVnlQMLTHLNLSRNQLSALPAC 151
Cdd:PRK15370 154 VKEAPAKEAANREEAvQRMRDCLKNNK-----TELR----LKILGL-----TTIPACIP--EQITTLILDNNELKSLPEN 217

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356460937 152 LCGlPLKVLIASNNKLGSLPEEIGQLKQLMELD-------------------VSCNEITALPQQIGQlkSLRELNVRRNY 212
Cdd:PRK15370 218 LQG-NIKTLYANSNQLTSIPATLPDTIQEMELSinritelperlpsalqsldLFHNKISCLPENLPE--ELRYLSVYDNS 294

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356460937 213 LKVLPPELVDlPLVKFDFSCNKVLVIPVCFRemKQLQVLLLENNPLQSPPAQICTKGKVhifkyLSIQACQIKTSDSLYL 292
Cdd:PRK15370 295 IRTLPAHLPS-GITHLNVQSNSLTALPETLP--PGLKTLEAGENALTSLPASLPPELQV-----LDVSKNQITVLPETLP 366


                 ....
gi 356460937 293 PTIE 296
Cdd:PRK15370 367 PTIT 370
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 94-262 5.75e-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: 59.80  E-value: 5.75e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356460937  94 LSKNRLVEVPmELCQFVSLEILNLYHNCIRVIpEAIVNLQMLTHLNLSRNQLSALPAcLCGLP-LKVLIASNNKLGSLpE 172
Cdd:cd21340    9 LNDKNITKID-NLSLCKNLKVLYLYDNKITKI-ENLEFLTNLTHLYLQNNQIEKIEN-LENLVnLKKLYLGGNRISVV-E 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356460937 173 EIGQLKQLMELDVSCNEItALPQQI--------GQLKSLRELNVRRNYLKVLPPeLVDLP-LVKFDFSCNK---VLVIPV 240
Cdd:cd21340   85 GLENLTNLEELHIENQRL-PPGEKLtfdprslaALSNSLRVLNISGNNIDSLEP-LAPLRnLEQLDASNNQisdLEELLD 162

                        170       180
                 ....*....|....*....|..
gi 356460937 241 CFREMKQLQVLLLENNPLQSPP 262
Cdd:cd21340  163 LLSSWPSLRELDLTGNPVCKKP 184
CH_VAV cd21201
calponin homology (CH) domain found in VAV proteins; VAV proteins function both as cytoplasmic ...
 587-671 8.65e-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: 56.88  E-value: 8.65e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356460937 587 DLGAALMDGVVLCHLANHVRPRSVaSIHVPSPAvPKLSMAKCRRNVENFLEACR-KLGVPEEKLCLPHHILEEKGLVKVG 665
Cdd:cd21201   31 DLAQALRDGVLLCQLLNRLSPGSV-DDREINLR-PQMSQFLCLKNIRTFLQACRtVFGLRSADLFEPEDLYDVTNFGKVI 108


                 ....*.
gi 356460937 666 TTVQAL 671
Cdd:cd21201  109 RTLSKL 114
CH_SCP1-like cd21210
calponin homology (CH) domain found in Saccharomyces cerevisiae transgelin (SCP1) and similar ...
 570-671 1.58e-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: 55.45  E-value: 1.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356460937 570 EQLRESIEMRLKVTLHE-DLGAALMDGVVLCHLANHVRPRSVASIHvpSPAVPKLSMakcrRNVENFLEACRKLGVPEEK 648
Cdd:cd21210    3 QEAREWIEEVLGEKLAQgDLLDALKDGVVLCKLANRILPADIRKYK--ESKMPFVQM----ENISAFLNAARKLGVPEND 76

                         90       100
                 ....*....|....*....|...
gi 356460937 649 LCLPHHILEEKGLVKVGTTVQAL 671
Cdd:cd21210   77 LFQTVDLFERKNPAQVLQCLHAL 99
CH_dMP20-like cd21207
calponin homology (CH) domain found in Drosophila melanogaster muscle-specific protein 20 ...
 586-671 5.41e-09

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: 54.24  E-value: 5.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356460937 586 EDLGAALMDGVVLCHLANHVRPRSVASIHVPSpavpklsMA-KCRRNVENFLEACRKLGVPEEKLCLPHHILEEKGLVKV 664
Cdd:cd21207   26 KDYEDVLKDGVILCKLINILKPGSVKKINTSK-------MAfKLMENIENFLTACKGYGVPKTDLFQTVDLYEKKNIPQV 98


                 ....*..
gi 356460937 665 GTTVQAL 671
Cdd:cd21207   99 TNCLFAL 105
CH_GAS2-like cd21204
calponin homology (CH) domain found in the growth arrest-specific protein 2 family; The growth ...
 566-662 3.39e-08

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: 52.66  E-value: 3.39e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356460937 566 KELVEQLRESIEMRLKVTLHEDLGA-----ALMDGVVLCHLANHVRPRSVASIHVPSPAVPKLSM-AKC----------- 628
Cdd:cd21204    1 EEALLPMKEDLAEWLNDLLGDDLTPdnfldELRNGVVLCQLAQKIQEAAEKAREAGKKNGPPPSYkLKCnenakpgsffa 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 356460937 629 RRNVENFLEACRKLGVPEEKLclphhiLEEKGLV 662
Cdd:cd21204   81 RDNVANFLRWCRKLGVDEVLL------FESEDLV 108
CH_AtKIN14-like cd21203
calponin homology (CH) domain found in Arabidopsis thaliana Kinesin-like KIN-14 protein family; ...
 586-645 4.92e-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: 51.65  E-value: 4.92e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 356460937 586 EDLGAALMDGVVLCHLANHVRPRSVASI--HVPSPAVPKLSMAKCRRNVENFLEACRKLGVP 645
Cdd:cd21203   24 EEFRLCLRDGVVLCKLLNKLQPGAVPKVveSPDDPDGAAGSAFQYFENVRNFLVAIEEMGLP 85
PRK15387 PRK15387
type III secretion system effector E3 ubiquitin transferase SspH2;
94-264 5.28e-08

type III secretion system effector E3 ubiquitin transferase SspH2;


Pssm-ID: 185285 [Multi-domain]  Cd Length: 788  Bit Score: 56.32  E-value: 5.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356460937  94 LSKNRLVEVPM---ELCQfvsleiLNLYHNCIRVIPEAIVNLQmltHLNLSRNQLSALPAclcgLP--LKVLIASNNKLG 168
Cdd:PRK15387 309 VSDNQLASLPAlpsELCK------LWAYNNQLTSLPTLPSGLQ---ELSVSDNQLASLPT----LPseLYKLWAYNNRLT 375

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356460937 169 SLPEEIGQLKQLMeldVSCNEITALPQQIGQLKSLRELNVRRNYLKVLPPELVDLPLVKfdfscNKVLVIPVCFREMKQL 248
Cdd:PRK15387 376 SLPALPSGLKELI---VSGNRLTSLPVLPSELKELMVSGNRLTSLPMLPSGLLSLSVYR-----NQLTRLPESLIHLSSE 447

                        170
                 ....*....|....*.
gi 356460937 249 QVLLLENNPLQSPPAQ 264
Cdd:PRK15387 448 TTVNLEGNPLSERTLQ 463
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 562-646 2.34e-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: 49.59  E-value: 2.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356460937  562 MREEKELVEQLRESIEMRLKVTLHEDLGAALMDGVVLCHLANHVRPRSVasihvpSPAVPKLSMAKCRRNVENFLE-ACR 640
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGPGVRVTNFTTDLRDGLALCALLNKLAPGLV------DKKKLNKSEFDKLENINLALDvAEK 74


                  ....*.
gi 356460937  641 KLGVPE 646
Cdd:pfam00307  75 KLGVPK 80
CH_PIX cd21202
calponin homology (CH) domain found in the Pak Interactive eXchange factor family; Pak ...
 576-675 2.57e-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: 49.45  E-value: 2.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356460937 576 IEMRLKVTLHED---LGAALMDGVVLCHLANHVRPRSVASIHvPSPavpkLSMAKCRRNVENFLEACRKLGVPEEKLCLP 652
Cdd:cd21202   15 LESPKKETIEDPerfLSESLKNGVVLCRLVNRLKPGTVEKIY-DEP----TTEEECLYNFESFLKACQELGILAEEIFDP 89

                         90       100
                 ....*....|....*....|...
gi 356460937 653 HHILEEKGLVKVGTTVQALLDVT 675
Cdd:cd21202   90 NDLYSGGNFQKVLSTLERLEKVA 112
CH_CNN cd21211
calponin homology (CH) domain found in the calponin family; Calponin is an actin ...
 570-678 3.25e-07

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: 49.23  E-value: 3.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356460937 570 EQLRESIEMRLKVTLHEDLGAALMDGVVLCHLANHVRPRSVASIHVPSPAVPKLsmakcrRNVENFLEACRKLGVPEEKL 649
Cdd:cd21211    6 AELRTWIEGVTGLSIGPNFQKGLKDGIILCELINKLQPGSVKKINESMQNWHQL------ENIGNFIKAIVSYGMKPHDI 79

                         90       100
                 ....*....|....*....|....*....
gi 356460937 650 CLPHHILEEKGLVKVGTTVQALLDVTVTK 678
Cdd:cd21211   80 FEANDLFENGNMTQVQVTLLALAGKAKTK 108
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 93-218 3.69e-07

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 53.70  E-value: 3.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356460937  93 DLSKNRLVE-VPMELCQFVSLEILNLYHNCIR-VIPEAIVNLQMLTHLNLSRNQLSalpaclcglplkvliasnnklGSL 170
Cdd:PLN00113 481 DLSRNQFSGaVPRKLGSLSELMQLKLSENKLSgEIPDELSSCKKLVSLDLSHNQLS---------------------GQI 539

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 356460937 171 PEEIGQLKQLMELDVSCNEITA-LPQQIGQLKSLRELNVRRNYLK-VLPP 218
Cdd:PLN00113 540 PASFSEMPVLSQLDLSQNQLSGeIPKNLGNVESLVQVNISHNHLHgSLPS 589
CH_CNN1 cd21282
calponin homology (CH) domain found in calponin-1 and similar proteins; Calponin-1 (CNN1), ...
 570-678 5.33e-07

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: 48.72  E-value: 5.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356460937 570 EQLRESIEMRLKVTLHEDLGAALMDGVVLCHLANHVRPRSVASIHVPSPAVPKLsmakcrRNVENFLEACRKLGVPeekl 649
Cdd:cd21282    6 EELRVWIEGVTGRRIGDNFMDGLKDGVILCELINKLQPGSVRKINESTQNWHKL------ENIGNFIKAIMHYGVK---- 75

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 356460937 650 clPHHILEEKGL------VKVGTTVQALLDVTVTK 678
Cdd:cd21282   76 --PHDIFEANDLfentnhTQVQSTLIALASMAKTK 108
CH_CNN3 cd21284
calponin homology (CH) domain found in calponin-3; Calponin-3 (CNN3), also called acidic ...
 570-678 6.36e-07

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


Pssm-ID: 409133 [Multi-domain]  Cd Length: 111  Bit Score: 48.36  E-value: 6.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356460937 570 EQLRESIEMRLKVTLHEDLGAALMDGVVLCHLANHVRPRSVASIHVPSPAVPKLsmakcrRNVENFLEACRKLGVPEEKL 649
Cdd:cd21284    8 EELRNWIEEVTGMSIGENFQKGLKDGVILCELINKLQPGSIRKINESKLNWHQL------ENIGNFIKAIQAYGMKPHDI 81

                         90       100
                 ....*....|....*....|....*....
gi 356460937 650 CLPHHILEEKGLVKVGTTVQALLDVTVTK 678
Cdd:cd21284   82 FEANDLFENGNMTQVQTTLLALAGLAKTK 110
LRR_8 pfam13855
Leucine rich repeat;
93-145 9.94e-07

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 46.36  E-value: 9.94e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 356460937   93 DLSKNRLVEVPMElcQFV---SLEILNLYHNCIRVI-PEAIVNLQMLTHLNLSRNQL 145
Cdd:pfam13855   7 DLSNNRLTSLDDG--AFKglsNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 132-235 1.68e-06

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 51.39  E-value: 1.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356460937 132 LQMLthlNLSRNQLSA-LPACLCGLPLKVLIASNNKL-GSLPEEIGQLKQLMELDVSCNEITA-LPQQIGQLKSLRELNV 208
Cdd:PLN00113 454 LQML---SLARNKFFGgLPDSFGSKRLENLDLSRNQFsGAVPRKLGSLSELMQLKLSENKLSGeIPDELSSCKKLVSLDL 530

                         90       100
                 ....*....|....*....|....*....
gi 356460937 209 RRNYLK-VLPPELVDLP-LVKFDFSCNKV 235
Cdd:PLN00113 531 SHNQLSgQIPASFSEMPvLSQLDLSQNQL 559
LRR_8 pfam13855
Leucine rich repeat;
179-258 3.13e-06

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 44.82  E-value: 3.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356460937  179 QLMELDVSCNEITALPQQI-GQLKSLRELNVRRNYLKVLPPElvdlplvkfdfscnkvlvipvCFREMKQLQVLLLENNP 257
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDDGAfKGLSNLKVLDLSNNLLTTLSPG---------------------AFSGLPSLRYLDLSGNR 60


                  .
gi 356460937  258 L 258
Cdd:pfam13855  61 L 61
PLN03150 PLN03150
hypothetical protein; Provisional
 107-233 5.76e-06

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 49.43  E-value: 5.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356460937 107 CQFVS------LEILNLYHNCIR-VIPEAIVNLQMLTHLNLSRNQLSalpaclcglplkvliasnnklGSLPEEIGQLKQ 179
Cdd:PLN03150 409 CQFDStkgkwfIDGLGLDNQGLRgFIPNDISKLRHLQSINLSGNSIR---------------------GNIPPSLGSITS 467

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 356460937 180 LMELDVSCNEIT-ALPQQIGQLKSLRELNVRRNYLK-VLPPELVDLPL--VKFDFSCN 233
Cdd:PLN03150 468 LEVLDLSYNSFNgSIPESLGQLTSLRILNLNGNSLSgRVPAALGGRLLhrASFNFTDN 525
CH_TAGLN3 cd21281
calponin homology (CH) domain found in transgelin-3; Transgelin-3, also called neuronal ...
 592-678 5.82e-06

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: 45.72  E-value: 5.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356460937 592 LMDGVVLCHLANHVRPRSvasiHVPSPAVPKLSMA-KCRRNVENFLEACRKLGVPEEKLCLPHHILEEKGLVKVGTTVQA 670
Cdd:cd21281   34 LMDGTILCRLINSLYPPG----KEPIKKISETKMAfKQMEKISQFLQAAEAYGVITTDIFQTVDLWEGKDMAAVQRTLMA 109


                 ....*...
gi 356460937 671 LLDVTVTK 678
Cdd:cd21281  110 LGSVAVTK 117
LRR_8 pfam13855
Leucine rich repeat;
111-167 7.73e-06

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 43.67  E-value: 7.73e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 356460937  111 SLEILNLYHNCIRVI-PEAIVNLQMLTHLNLSRNQLSAL-PACLCGLP-LKVLIASNNKL 167
Cdd:pfam13855   2 NLRSLDLSNNRLTSLdDGAFKGLSNLKVLDLSNNLLTTLsPGAFSGLPsLRYLDLSGNRL 61
CH_TAGLN2 cd21280
calponin homology (CH) domain found in transgelin-2; Transgelin-2, also called epididymis ...
 561-678 1.85e-05

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


Pssm-ID: 409129 [Multi-domain]  Cd Length: 137  Bit Score: 44.87  E-value: 1.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356460937 561 QMREEKELVEQLRESIEMRLKvtlhedlgaalmDGVVLCHLANHVRPRSVAsihvPSPAVPKLSMA-KCRRNVENFLEAC 639
Cdd:cd21280   20 QCGKQVGRPQPGRENFQNWLK------------DGTVLCHLINSLYPKGQA----PVKKIQASTMAfKQMEQISQFLQAA 83

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 356460937 640 RKLGVPEEKLCLPHHILEEKGLVKVGTTVQALLDVTVTK 678
Cdd:cd21280   84 ERYGINTTDIFQTVDLWEGKNMASVQRTLMNLGGLAVTR 122
LRR_8 pfam13855
Leucine rich repeat;
157-213 1.96e-05

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 42.51  E-value: 1.96e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 356460937  157 LKVLIASNNKLGSLPEEI-GQLKQLMELDVSCNEITAL-PQQIGQLKSLRELNVRRNYL 213
Cdd:pfam13855   3 LRSLDLSNNRLTSLDDGAfKGLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
CH_LMO7-like cd21208
calponin homology (CH) domain found in LIM domain only protein 7 and similar proteins; This ...
 586-649 2.55e-05

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: 43.87  E-value: 2.55e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 356460937 586 EDLGAALMDGVVLCHLANHVRPRSVASI-HVPSPAVpklsmakCRRNVENFLEACRKLGVPEEKL 649
Cdd:cd21208   20 DDFRESLEDGILLCELINAIKPGSIKKInRLPTPIA-------GLDNLNLFLKACEDLGLKDSQL 77
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 125-265 3.33e-05

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 47.15  E-value: 3.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356460937 125 IPEAIVNLQMLTHLNLSRNQLSA-LPACLCGL--PLKVLIASNNKL-GSLPEeiGQLKQLMELDVSCNEITA-LPQQIGQ 199
Cdd:PLN00113  85 ISSAIFRLPYIQTINLSNNQLSGpIPDDIFTTssSLRYLNLSNNNFtGSIPR--GSIPNLETLDLSNNMLSGeIPNDIGS 162

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356460937 200 LKSLRELNVRRNYLK-VLPPELVDLPLVKFDFSCNKVLV--IPVCFREMKQLQVLLLENNPLQSP-PAQI 265
Cdd:PLN00113 163 FSSLKVLDLGGNVLVgKIPNSLTNLTSLEFLTLASNQLVgqIPRELGQMKSLKWIYLGYNNLSGEiPYEI 232
PLN03150 PLN03150
hypothetical protein; Provisional
 65-157 3.72e-05

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 47.12  E-value: 3.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356460937  65 GLNLSARKLKEF-PRTTAPGHDLSDTvraDLSKNRLV-EVPMELCQFVSLEILNLYHNCIR-VIPEAIVNLQMLTHLNLS 141
Cdd:PLN03150 422 GLGLDNQGLRGFiPNDISKLRHLQSI---NLSGNSIRgNIPPSLGSITSLEVLDLSYNSFNgSIPESLGQLTSLRILNLN 498

                         90
                 ....*....|....*..
gi 356460937 142 RNQLSA-LPACLCGLPL 157
Cdd:PLN03150 499 GNSLSGrVPAALGGRLL 515
CH_CNN2 cd21283
calponin homology (CH) domain found in calponin-2; Calponin-2 (CNN2), also called neutral ...
 570-678 4.41e-05

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: 43.00  E-value: 4.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356460937 570 EQLRESIEMRLKVTLHEDLGAALMDGVVLCHLANHVRPRSVASIHVPSPAVPKLsmakcrRNVENFLEACRKLGVPEEKL 649
Cdd:cd21283    6 AELRTWIEGLTGRSIGPDFQKGLKDGVILCELMNKLQPGSVPKINRSMQNWHQL------ENLSNFIKAMVSYGMKPVDL 79

                         90       100
                 ....*....|....*....|....*....
gi 356460937 650 CLPHHILEEKGLVKVGTTVQALLDVTVTK 678
Cdd:cd21283   80 FEANDLFESGNMTQVQVSLLALAGMAKTK 108
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 106-220 5.12e-05

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


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 45.81  E-value: 5.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356460937 106 LCQ----FVSLEILNLYHNCIR-----VIPEAIVNLQMLTHLNLSRNQLSALPAC-LC-GLP-----LKVLIASNNKLG- 168
Cdd:cd00116  185 LAEglkaNCNLEVLDLNNNGLTdegasALAETLASLKSLEVLNLGDNNLTDAGAAaLAsALLspnisLLTLSLSCNDITd 264

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 356460937 169 ----SLPEEIGQLKQLMELDVSCNEITALPQQIGQLkSLRELNVRRNYLKVLPPEL 220
Cdd:cd00116  265 dgakDLAEVLAEKESLLELDLRGNKFGEEGAQLLAE-SLLEPGNELESLWVKDDSF 319
CH_VAV1 cd21262
calponin homology (CH) domain found in VAV1 protein; VAV1 is expressed predominantly in the ...
 587-671 6.02e-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: 43.01  E-value: 6.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356460937 587 DLGAALMDGVVLCHLANHVRPRSVASIHVpsPAVPKLSMAKCRRNVENFLEAC-RKLGVPEEKLCLPHHILEEKGLVKVG 665
Cdd:cd21262   31 DLAQALRDGVLLCQLLNNLLPHAVNLREI--NLRPQMSQFLCLKNIRTFLSTCcEKFGLRKSELFEAFDLFDVRDFGKVI 108


                 ....*.
gi 356460937 666 TTVQAL 671
Cdd:cd21262  109 DTLSIL 114
CH_VAV3 cd21264
calponin homology (CH) domain found in VAV3 protein and similar proteins; VAV3 is ubiquitously ...
 587-639 1.65e-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: 1.65e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 356460937 587 DLGAALMDGVVLCHLANHVRPRSV--ASIHVPspavPKLSMAKCRRNVENFLEAC 639
Cdd:cd21264   31 DLAQTLRDGVLLCQLLNNLRPHSInlKEINLR----PQMSQFLCLKNIRTFLSAC 81
CH_TAGLN-like cd21209
calponin homology (CH) domain found in the transgelin family; The transgelin (TAGLN) family ...
 592-678 2.49e-04

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


Pssm-ID: 409058 [Multi-domain]  Cd Length: 119  Bit Score: 41.34  E-value: 2.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356460937 592 LMDGVVLCHLANHVRPRSVASIHVPSPAvpklSMA-KCRRNVENFLEACRKLGVPEEKLCLPHHILEEKGLVKVGTTVQA 670
Cdd:cd21209   34 LKDGTVLCKLINSLYPEGSKPVKKIQSS----KMAfKQMEQISQFLKAAEDYGVRTTDIFQTVDLWEGKDMAAVQRTLMA 109


                 ....*...
gi 356460937 671 LLDVTVTK 678
Cdd:cd21209  110 LGSLAVTK 117
CH_LMO7 cd21277
calponin homology (CH) domain found in LIM domain only protein 7; LIM domain only protein 7 ...
 586-677 5.42e-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: 5.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356460937 586 EDLGAALMDGVVLCHLANHVRPRSVASIHVPSPAVPKLSmakcrrNVENFLEACRKLGVPEEKLCLPHHI--LEEKGLVK 663
Cdd:cd21277   20 KDFRSALENGVLLCDLINKIKPGIIKKINRLSTPIAGLD------NINVFLKACEKLGLKEAQLFHPGDLqdLSTRVTVK 93

                         90
                 ....*....|....
gi 356460937 664 VGTTVQALLDVTVT 677
Cdd:cd21277   94 QEETDRRLKNVLIT 107
CH_alphaPIX cd21265
calponin homology (CH) domain found in alpha-Pak Interactive eXchange factor; Alpha-Pak ...
 586-644 7.25e-04

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: 39.80  E-value: 7.25e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 356460937 586 EDLGAALMDGVVLCHLANHVRPRSVASiHVPSPAvpklSMAKCRRNVENFLEACRKLGV 644
Cdd:cd21265   29 EFLKSSLKDGVVLCKLIERLLPGSVEK-YCLEPK----TEADCIGNIKEFLKGCAALKV 82
SCP1 COG5199
Calponin [Cytoskeleton];
559-671 7.94e-04

Calponin [Cytoskeleton];


Pssm-ID: 227526 [Multi-domain]  Cd Length: 178  Bit Score: 41.06  E-value: 7.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356460937 559 MEQMREEKELVEQLREsIEMRLKVTLHE------DLGAALMDGVVLCHLANHVRPrsvASIHVPSPAVPKLSMakcrRNV 632
Cdd:COG5199    2 VNTKNRCPGMDKQQKE-VTLWIETVLGEkfeppgDLLSLLKDGVRLCRILNEASP---LDIKYKESKMPFVQM----ENI 73

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 356460937 633 ENFLEACRKLGVPEEKLCLPHHILEEKGLVKVGTTVQAL 671
Cdd:COG5199   74 SSFINGLKKLRVPEYELFQTNDLFEAKDLRQVVICLYSL 112
CH_TAGLN cd21279
calponin homology (CH) domain found in transgelin; Transgelin, also called 22 kDa ...
 592-678 1.07e-03

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


Pssm-ID: 409128 [Multi-domain]  Cd Length: 121  Bit Score: 39.61  E-value: 1.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356460937 592 LMDGVVLCHLANHVRPRSVASIHVPSPavPKLSMAKCRRNVENFLEACRKLGVPEEKLCLPHHILEEKGLVKVGTTVQAL 671
Cdd:cd21279   34 LKNGVVLSKLVNSLYPDGSKPVKIPDN--PPSMVFKQMEQVAQFLKAAEDYGVVKTDMFQTVDLYEGKDMAAVQRTLVAL 111


                 ....*..
gi 356460937 672 LDVTVTK 678
Cdd:cd21279  112 GSLAVTK 118
CH_betaPIX cd21266
calponin homology (CH) domain found in beta-Pak Interactive eXchange factor; Beta-Pak ...
 588-644 1.75e-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: 38.75  E-value: 1.75e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 356460937 588 LGAALMDGVVLCHLANHVRPRSVASIHvPSPAvpklSMAKCRRNVENFLEACRKLGV 644
Cdd:cd21266   29 LQASLKDGVVLCRLLERLLPGSIDKVY-PEPR----TESECLSNIREFLRGCGALRL 80
CH_VAV2 cd21263
calponin homology (CH) domain found in VAV2 protein and similar proteins; VAV2 is widely ...
 587-671 2.63e-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: 38.40  E-value: 2.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356460937 587 DLGAALMDGVVLCHLANHVRPRSVASIHVPSPavPKLSMAKCRRNVENFLEACR-KLGVPEEKLCLPHHILEEKGLVKVG 665
Cdd:cd21263   31 DLAQALRDGVLLCQLLHNLSPGSIDLKDINFR--PQMSQFLCLKNIRTFLKVCHdKFGLRNSELFDPFDLFDVRDFGKVI 108


                 ....*.
gi 356460937 666 TTVQAL 671
Cdd:cd21263  109 SALSRL 114
PRK15387 PRK15387
type III secretion system effector E3 ubiquitin transferase SspH2;
97-263 2.79e-03

type III secretion system effector E3 ubiquitin transferase SspH2;


Pssm-ID: 185285 [Multi-domain]  Cd Length: 788  Bit Score: 40.92  E-value: 2.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356460937  97 NRLVEVPMELCQFVSLEILNLYHNCIRVIPEAIVNLQMLTHlnlSRNQLSALPACLCGLPLkvliaSNNKLGSLPEeigQ 176
Cdd:PRK15387 232 NNLTSLPALPPELRTLEVSGNQLTSLPVLPPGLLELSIFSN---PLTHLPALPSGLCKLWI-----FGNQLTSLPV---L 300

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356460937 177 LKQLMELDVSCNEITALPQQIGQLKSLRELNVRRNYLKVLPPELVDLPLvkfdfSCNKVLVIPVCFREMKQLQVLlleNN 256
Cdd:PRK15387 301 PPGLQELSVSDNQLASLPALPSELCKLWAYNNQLTSLPTLPSGLQELSV-----SDNQLASLPTLPSELYKLWAY---NN 372


                 ....*..
gi 356460937 257 PLQSPPA 263
Cdd:PRK15387 373 RLTSLPA 379
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 585-644 3.22e-03

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: 37.94  E-value: 3.22e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 356460937 585 HEDLGAALMDGVVLCHLANHVRPRSVA--SIHVPSPavpkLSMAKCRRNVENFLEACRKLGV 644
Cdd:cd21217   30 GDDLFEALRDGVLLCKLINKIVPGTIDerKLNKKKP----KNIFEATENLNLALNAAKKIGC 87
CH_IQGAP cd21206
calponin homology (CH) domain found in the IQ motif containing GTPase activating protein ...
 569-646 4.44e-03

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: 37.59  E-value: 4.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356460937 569 VEQLRESIEMRLKVTLH--EDLGAALMDGVVLCHLANHVRPRSVASIHVPSpavPKLSMakcrRNVEN---FLEACRKLG 643
Cdd:cd21206   10 LEEAKQWIEACLNEELPptTEFEEELRNGVVLAKLANKFAPKLVPLKKIYD---VGLQF----RHTDNinhFLRALKKIG 82


                 ...
gi 356460937 644 VPE 646
Cdd:cd21206   83 LPK 85
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 111-213 8.28e-03

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


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 39.00  E-value: 8.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356460937 111 SLEILNLYHNCI-----RVIPEAIVNLQMLTHLNLSRNQLS-----ALPACLCG-LPLKVLIASNNKLG-----SLPEEI 174
Cdd:COG5238  265 TVETLYLSGNQIgaegaIALAKALQGNTTLTSLDLSVNRIGdegaiALAEGLQGnKTLHTLNLAYNGIGaqgaiALAKAL 344

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 356460937 175 GQLKQLMELDVSCNEIT-----ALPQQIGQLKSLRELNVRRNYL 213
Cdd:COG5238  345 QENTTLHSLDLSDNQIGdegaiALAKYLEGNTTLRELNLGKNNI 388
CH_jitterbug-like_rpt3 cd21185
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
 594-645 9.13e-03

third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409034  Cd Length: 98  Bit Score: 36.13  E-value: 9.13e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 356460937 594 DGVVLCHLANhvrprsvaSIHVPSPAVPKLSMAKCRRNVENFLEACRKLGVP 645
Cdd:cd21185   28 DGRLLCGLVN--------ALGGSVPGWPNLDPEESENNIQRGLEAGKSLGVE 71
 
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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