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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381831  18 IEKQYDPDLEQILIQWITTQCRKGVSQPQPGRENFQNWLKDGTVLCELINSLYPEGQAPVKKIQASTMAFKQMEQISQFL 97
Cdd:cd21280    1 IDKQYDADLEQILIQWITAQCGKQVGRPQPGRENFQNWLKDGTVLCHLINSLYPKGQAPVKKIQASTMAFKQMEQISQFL 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 564381831  98 QAAERYGINTTDIFQTVDLWEGKNMACVQRTLMNLGGLAVARDDGLFSGDPNWFPKK 154
Cdd:cd21280   81 QAAERYGINTTDIFQTVDLWEGKNMASVQRTLMNLGGLAVTRDDGLFVGDPNWFPKK 137

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381831  18 IEKQYDPDLEQILIQWITTQCRKGVSQPQPGRENFQNWLKDGTVLCELINSLYPEGQAPVKKIQASTMAFKQMEQISQFL 97
Cdd:cd21280    1 IDKQYDADLEQILIQWITAQCGKQVGRPQPGRENFQNWLKDGTVLCHLINSLYPKGQAPVKKIQASTMAFKQMEQISQFL 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 564381831  98 QAAERYGINTTDIFQTVDLWEGKNMACVQRTLMNLGGLAVARDDGLFSGDPNWFPKK 154
Cdd:cd21280   81 QAAERYGINTTDIFQTVDLWEGKNMASVQRTLMNLGGLAVTRDDGLFVGDPNWFPKK 137

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381831   24 PDLEQILIQWITTQCRKGVsqPQPGRENFQNWLKDGTVLCELINSLYPEGqapVKKIQASTMAFKQMEQISQFLQAAER- 102
Cdd:pfam00307   1 LELEKELLRWINSHLAEYG--PGVRVTNFTTDLRDGLALCALLNKLAPGL---VDKKKLNKSEFDKLENINLALDVAEKk 75

                          90       100       110
                  ....*....|....*....|....*....|.
gi 564381831  103 YGINTTDIfQTVDLWEGKNMaCVQRTLMNLG 133
Cdd:pfam00307  76 LGVPKVLI-EPEDLVEGDNK-SVLTYLASLF 104

Calponin family repeat;

                          10        20
                  ....*....|....*....|....*
gi 564381831  174 IGLQMGTNRGASQAGMTGYGMPRQI 198
Cdd:pfam00402   1 IGLQMGTNKGASQSGMTAFGAVRHI 25

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381831  18 IEKQYDPDLEQILIQWITTQCRKGVSQPQPGRENFQNWLKDGTVLCELINSLYPEGQAPVKKIQASTMAFKQMEQISQFL 97
Cdd:cd21280    1 IDKQYDADLEQILIQWITAQCGKQVGRPQPGRENFQNWLKDGTVLCHLINSLYPKGQAPVKKIQASTMAFKQMEQISQFL 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 564381831  98 QAAERYGINTTDIFQTVDLWEGKNMACVQRTLMNLGGLAVARDDGLFSGDPNWFPKK 154
Cdd:cd21280   81 QAAERYGINTTDIFQTVDLWEGKNMASVQRTLMNLGGLAVTRDDGLFVGDPNWFPKK 137

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381831  23 DPDLEQILIQWITTQCRKGVSQPQPGRENFQNWLKDGTVLCELINSLYPEGQAPVKKIQASTMAFKQMEQISQFLQAAER 102
Cdd:cd21281    1 DPDLESRLVDWIIIQCGGDIERPQPGRQNFQKWLMDGTILCRLINSLYPPGKEPIKKISETKMAFKQMEKISQFLQAAEA 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 564381831 103 YGINTTDIFQTVDLWEGKNMACVQRTLMNLGGLAVARDD 141
Cdd:cd21281   81 YGVITTDIFQTVDLWEGKDMAAVQRTLMALGSVAVTKDD 119

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381831  22 YDPDLEQILIQWIttqcRKGVSQPQPGRENFQNWLKDGTVLCELINSLYPegqAPVKKIQASTMAFKQMEQISQFLQAAE 101
Cdd:cd21207    2 RDPALEAEALDWI----EAVTGEKLDDGKDYEDVLKDGVILCKLINILKP---GSVKKINTSKMAFKLMENIENFLTACK 74

                         90       100       110
                 ....*....|....*....|....*....|...
gi 564381831 102 RYGINTTDIFQTVDLWEGKNMACVQRTLMNLGG 134
Cdd:cd21207   75 GYGVPKTDLFQTVDLYEKKNIPQVTNCLFALGR 107

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381831  52 FQNWLKDGTVLCELINSLYPegqAPVKKIQASTMAFKQMEQISQFLQAAERYGINTTDIFQTVDLWEGKNMACVQRTLMN 131
Cdd:cd21210   22 LLDALKDGVVLCKLANRILP---ADIRKYKESKMPFVQMENISAFLNAARKLGVPENDLFQTVDLFERKNPAQVLQCLHA 98

                 ..
gi 564381831 132 LG 133
Cdd:cd21210   99 LS 100

Calponin [Cytoskeleton];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381831  14 VQQKIEKQYDPDLEQILIQWITTQCRKGVSQPQpgreNFQNWLKDGTVLCELINSLYPegqAPVKkIQASTMAFKQMEQI 93
Cdd:COG5199    2 VNTKNRCPGMDKQQKEVTLWIETVLGEKFEPPG----DLLSLLKDGVRLCRILNEASP---LDIK-YKESKMPFVQMENI 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381831  94 SQFLQAAERYGINTTDIFQTVDLWEGKNMACVQRTLMNLGGLAVARDDGLFsgdPNWFPKKSKENPRNFS-DNQLQEGKN 172
Cdd:COG5199   74 SSFINGLKKLRVPEYELFQTNDLFEAKDLRQVVICLYSLSRYAQKERMFSG---PFLGPHLATKKPRVFSsQEVLDRSKG 150

                        170
                 ....*....|....*.
gi 564381831 173 VIGLQMGTNRGASQAG 188
Cdd:COG5199  151 AIHLQYGYSDLSEQST 166

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381831  21 QYDPDLEQILIQWITTQCRKGVSqpqpgrENFQNWLKDGTVLCELINSLYPEGqapVKKIQASTMAFKQMEQISQFLQAA 100
Cdd:cd21284    1 KYDPQKEEELRNWIEEVTGMSIG------ENFQKGLKDGVILCELINKLQPGS---IRKINESKLNWHQLENIGNFIKAI 71

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 564381831 101 ERYGINTTDIFQTVDLWEGKNMACVQRTLMNLGGLA 136
Cdd:cd21284   72 QAYGMKPHDIFEANDLFENGNMTQVQTTLLALAGLA 107

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381831    29 ILIQWITTQCRKGVSQPqpgRENFQNWLKDGTVLCELINSLYPeGQAPVKKIQASTMAFKQMEQISQFLQAAERYGINtT 108
Cdd:smart00033   2 TLLRWVNSLLAEYDKPP---VTNFSSDLKDGVALCALLNSLSP-GLVDKKKVAASLSRFKKIENINLALSFAEKLGGK-V 76

                           90       100
                   ....*....|....*....|....*
gi 564381831   109 DIFQTVDLWEG-KNMACVQRTLMNL 132
Cdd:smart00033  77 VLFEPEDLVEGpKLILGVIWTLISL 101

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381831  32 QWITTqCrkgVSQPQPGRENFQNWLKDGTVLCELINSLYPEGqAPVKKIQASTMAFKQMEQISQFLQAAERYGINTTDIF 111
Cdd:cd21206   15 QWIEA-C---LNEELPPTTEFEEELRNGVVLAKLANKFAPKL-VPLKKIYDVGLQFRHTDNINHFLRALKKIGLPKIFHF 89

                         90
                 ....*....|.
gi 564381831 112 QTVDLWEGKNM 122
Cdd:cd21206   90 ETTDLYEKKNI 100

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381831  56 LKDGTVLCELINSLYPeGQAPVKKIQASTmafkQMEQ------ISQFLQAA-ERYGINTTDIFQTVDLWEGKNMACVQRT 128
Cdd:cd21201   36 LRDGVLLCQLLNRLSP-GSVDDREINLRP----QMSQflclknIRTFLQACrTVFGLRSADLFEPEDLYDVTNFGKVIRT 110

                 .
gi 564381831 129 L 129
Cdd:cd21201  111 L 111

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.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564381831  45 PQPGRENFQNWLKDGTVLCELINSLYPE-----GQAPVKKIQASTMAFKQMEQISQFLQAAERYGINTtdiFQTVDL 116
Cdd:cd21203   19 PDPSEEEFRLCLRDGVVLCKLLNKLQPGavpkvVESPDDPDGAAGSAFQYFENVRNFLVAIEEMGLPT---FEASDL 92

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.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564381831  56 LKDGTVLCELINSLYPegqAPVKKI-QASTMAFKQMEQISQFLQAAERYGINTTDIFQTVDLWEGKNMACVQRTLMNL 132
Cdd:cd21202   34 LKNGVVLCRLVNRLKP---GTVEKIyDEPTTEEECLYNFESFLKACQELGILAEEIFDPNDLYSGGNFQKVLSTLERL 108

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381831  56 LKDGTVLCELINSLYPEGqAPVKKI--QASTMAFKQMEQISQFLQA-AERYGINTTDIFQTVDLWEGKNMACVQRTLMNL 132
Cdd:cd21262   36 LRDGVLLCQLLNNLLPHA-VNLREInlRPQMSQFLCLKNIRTFLSTcCEKFGLRKSELFEAFDLFDVRDFGKVIDTLSIL 114

                 ....*.
gi 564381831 133 GGLAVA 138
Cdd:cd21262  115 SWTPIA 120

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381831  48 GRENFQNWLKDGTVLCELINSLYPegqAPVKKIQASTMAFKQMEQISQFLQAAERYGINTTDIFQTVDLWEGKNMACVQR 127
Cdd:cd21278   18 GDKDFRSGLENGILLCELLNAIKP---GLVKKINRLPTPIAGLDNITLFLRGCKELGLKESQLFDPGDLQDTSNRVTIKS 94

                 .
gi 564381831 128 T 128
Cdd:cd21278   95 S 95

second 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 second CH domain. CH domains are actin filament (F-actin) binding motifs.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381831  27 EQILIQWITTQCRKgvSQPQPGR-ENFQNWLKDGTVLCELINSLYPEGQAPVKKIQASTMA--FKQMEQIsqfLQAAERY 103
Cdd:cd21218   12 EEILLRWVNYHLKK--AGPTKKRvTNFSSDLKDGEVYALLLHSLAPELCDKELVLEVLSEEdlEKRAEKV---LQAAEKL 86

                 ....
gi 564381831 104 GINT 107
Cdd:cd21218   87 GCKY 90

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381831  23 DPDLEQILIqwittqcrkgvsqPQPGRENFQNWLKDGTVLCELINSLYPeGQAPVKKI--QASTMAFKQMEQISQFLQAA 100
Cdd:cd21217   17 DPDLKHLLP-------------IDPDGDDLFEALRDGVLLCKLINKIVP-GTIDERKLnkKKPKNIFEATENLNLALNAA 82

                         90       100
                 ....*....|....*....|
gi 564381831 101 ERYGINTTDIfQTVDLWEGK 120
Cdd:cd21217   83 KKIGCKVVNI-GPQDILDGN 101

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381831  37 QCRKGVSQPQpgreNFQNWLKDGTVLCELINSLYPEG----QAPVKKIQASTMAfKQMEQISQFLQAAERYGINTTDIFQ 112
Cdd:cd21272   11 ESRLKVSLPS----DLGAALTDGVVLCHLANHVRPRSvpsiHVPSPAVPKLTMA-KCRRNVENFLEACRRIGVPQEQLCL 85

                         90       100
                 ....*....|....*....|....
gi 564381831 113 TVDLWEGKNMACVQRTLMNLGGLA 136
Cdd:cd21272   86 PLHILEEKGLSQVAVTVQALLELA 109

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564381831  34 ITTQCRKGV----SQPQPgrENFQNWLKDGTVLCELINSLYPEG----QAPVKKIqASTMAFKQMEQISQFLQAAERYGI 105
Cdd:cd21273    5 LRAQLRKTLesrlKVTLP--EDLAEALSNGAVLCQLANQLRPRSvsiiHVPSPAV-PKLSKAKCRKNVENFIEACRKMGV 81

                         90       100
                 ....*....|....*....|....*..
gi 564381831 106 NTTDIFQTVDLWEgKNMACVQRTLMNL 132
Cdd:cd21273   82 PEVDLCSPSDVLL-QGPAAVLRTVLAL 107

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.

                         10        20        30        40        50        60        70
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gi 564381831  56 LKDGTVLCELINSLYPeGQAPVKKI--QASTMAFKQMEQISQFLQAA-ERYGINTTDIFQTVDLWE----GKNMACVQR 127
Cdd:cd21263   36 LRDGVLLCQLLHNLSP-GSIDLKDInfRPQMSQFLCLKNIRTFLKVChDKFGLRNSELFDPFDLFDvrdfGKVISALSR 113