Calponin family repeat;

                          10        20
                  ....*....|....*....|....*
gi 1721967086 164 IGLQMGTNKCASQAGMTAYGTRRHL 188
Cdd:pfam00402   1 IGLQMGTNKGASQSGMTAFGAVRHI 25

Calponin family repeat;

                          10        20
                  ....*....|....*....|....*
gi 1721967086 242 ISLQMGTNKVASQKGMSVYGLGRQV 266
Cdd:pfam00402   1 IGLQMGTNKGASQSGMTAFGAVRHI 25

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 1721967086  26 LQREEELRYWIEEVTGMPIG----DNFQKGLKDGVILSELINKLQPGSVKKINHSQLNWHKLENLGNFIK-AILAYGMKP 100
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGPgvrvTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEFDKLENINLALDvAEKKLGVPK 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1721967086 101 NDIfEANDLFEnGNLTQVQTTLLALANMAKT 131
Cdd:pfam00307  81 VLI-EPEDLVE-GDNKSVLTYLASLFRRFQA 109

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 1721967086   30 EELRYWIEEVTGMPIG---DNFQKGLKDGVILSELINKLQPGSVKKINHSQ--LNWHKLENLGNFIKAILAYGMKPnDIF 104
Cdd:smart00033   1 KTLLRWVNSLLAEYDKppvTNFSSDLKDGVALCALLNSLSPGLVDKKKVAAslSRFKKIENINLALSFAEKLGGKV-VLF 79

                           90       100
                   ....*....|....*....|..
gi 1721967086  105 EANDLFENGNLT-QVQTTLLAL 125
Cdd:smart00033  80 EPEDLVEGPKLIlGVIWTLISL 101

Calponin family repeat;

                          10        20
                  ....*....|....*....|....*
gi 1721967086 204 ISLQMGTNKGASQAGMSAPGTRRDI 228
Cdd:pfam00402   1 IGLQMGTNKGASQSGMTAFGAVRHI 25

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721967086  25 DLQREEELRYWIEEVTGMPIGDNFQKGLKDGVILSELINKLQPGSVKKINHSQLNWHKLENLGNFIKAILAYGMKPNDIF 104
Cdd:cd21211     1 DHQKEAELRTWIEGVTGLSIGPNFQKGLKDGIILCELINKLQPGSVKKINESMQNWHQLENIGNFIKAIVSYGMKPHDIF 80

                          90       100
                  ....*....|....*....|....*...
gi 1721967086 105 EANDLFENGNLTQVQTTLLALANMAKTK 132
Cdd:cd21211    81 EANDLFENGNMTQVQVTLLALAGKAKTK 108

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721967086  25 DLQREEELRYWIEEVTGMPIGDNFQKGLKDGVILSELINKLQPGSVKKINHSQLNWHKLENLGNFIKAILAYGMKPNDIF 104
Cdd:cd21282     1 DPQTEEELRVWIEGVTGRRIGDNFMDGLKDGVILCELINKLQPGSVRKINESTQNWHKLENIGNFIKAIMHYGVKPHDIF 80

                          90       100
                  ....*....|....*....|....*...
gi 1721967086 105 EANDLFENGNLTQVQTTLLALANMAKTK 132
Cdd:cd21282    81 EANDLFENTNHTQVQSTLIALASMAKTK 108

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).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721967086  29 EEELRYWIEEVTGMPIGD---NFQKGLKDGVILSELINKLQPGSVKKINHSQLN-WHKLENLGNFIKAILAYGMKPNDIF 104
Cdd:cd00014     1 EEELLKWINEVLGEELPVsitDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSpFKKRENINLFLNACKKLGLPELDLF 80

                          90       100
                  ....*....|....*....|...
gi 1721967086 105 EANDLFENGNLTQVQTTLLALAN 127
Cdd:cd00014    81 EPEDLYEKGNLKKVLGTLWALAL 103

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 1721967086  26 LQREEELRYWIEEVTGMPIG----DNFQKGLKDGVILSELINKLQPGSVKKINHSQLNWHKLENLGNFIK-AILAYGMKP 100
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGPgvrvTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEFDKLENINLALDvAEKKLGVPK 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1721967086 101 NDIfEANDLFEnGNLTQVQTTLLALANMAKT 131
Cdd:pfam00307  81 VLI-EPEDLVE-GDNKSVLTYLASLFRRFQA 109

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 1721967086  20 IAQKYDLQREEELRYWIEEVTGMPIG------DNFQKGLKDGVILSELINKLQPGS---VKKINHSQLNWHKLENLGNFI 90
Cdd:cd21280     1 IDKQYDADLEQILIQWITAQCGKQVGrpqpgrENFQNWLKDGTVLCHLINSLYPKGqapVKKIQASTMAFKQMEQISQFL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1721967086  91 KAILAYGMKPNDIFEANDLFENGNLTQVQTTLLALANMAKTK 132
Cdd:cd21280    81 QAAERYGINTTDIFQTVDLWEGKNMASVQRTLMNLGGLAVTR 122

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 1721967086  25 DLQREEELRYWI-----EEVTGMPIG-DNFQKGLKDGVILSELINKLQPGS---VKKINHSQLNWHKLENLGNFIKAILA 95
Cdd:cd21281     1 DPDLESRLVDWIiiqcgGDIERPQPGrQNFQKWLMDGTILCRLINSLYPPGkepIKKISETKMAFKQMEKISQFLQAAEA 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1721967086  96 YGMKPNDIFEANDLFENGNLTQVQTTLLALANMAKTK 132
Cdd:cd21281    81 YGVITTDIFQTVDLWEGKDMAAVQRTLMALGSVAVTK 117

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 1721967086   30 EELRYWIEEVTGMPIG---DNFQKGLKDGVILSELINKLQPGSVKKINHSQ--LNWHKLENLGNFIKAILAYGMKPnDIF 104
Cdd:smart00033   1 KTLLRWVNSLLAEYDKppvTNFSSDLKDGVALCALLNSLSPGLVDKKKVAAslSRFKKIENINLALSFAEKLGGKV-VLF 79

                           90       100
                   ....*....|....*....|..
gi 1721967086  105 EANDLFENGNLT-QVQTTLLAL 125
Cdd:smart00033  80 EPEDLVEGPKLIlGVIWTLISL 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 1721967086  22 QKYD-LQREEELRYWIEEVTG--MPIGDNFQKGLKDGVILSELINKLQPGSV--KKINHSQLNWHKLENLGNFIKAILAY 96
Cdd:cd21206     2 IAYEyLCRLEEAKQWIEACLNeeLPPTTEFEEELRNGVVLAKLANKFAPKLVplKKIYDVGLQFRHTDNINHFLRALKKI 81

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1721967086  97 GMKPNDIFEANDLFENGNLTQVQTTLLALANMAKTKG 133
Cdd:cd21206    82 GLPKIFHFETTDLYEKKNIPKVIYCLHALSLLLFKLG 118

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 1721967086  31 ELRYWIEEVTGMPIGD-NFQKGLKDGVILSELINKLQPGSVKKINHSQLNWHKLENLGNFIKAILAYGMKPNDIFEANDL 109
Cdd:cd21278     4 EAQKWIEQVTGRSFGDkDFRSGLENGILLCELLNAIKPGLVKKINRLPTPIAGLDNITLFLRGCKELGLKESQLFDPGDL 83

                          90
                  ....*....|..
gi 1721967086 110 FENGNLTQVQTT 121
Cdd:cd21278    84 QDTSNRVTIKSS 95

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721967086  31 ELRYWIEEVTGMPIGD-NFQKGLKDGVILSELINKLQPGSVKKINHSQLNWHKLENLGNFIKAILAYGMKPNDIFEANDL 109
Cdd:cd21277     4 EAQRWIEAVTGKNFGNkDFRSALENGVLLCDLINKIKPGIIKKINRLSTPIAGLDNINVFLKACEKLGLKEAQLFHPGDL 83

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        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721967086  28 REEELRYWIEEVTGMPIG-----DNFQKGLKDGVILSELINKLQPGSVKKINHS-QLNWHKL-------ENLGNFIKAIL 94
Cdd:cd21203     1 RRYEAAEWIQNVLGVLVLpdpseEEFRLCLRDGVVLCKLLNKLQPGAVPKVVESpDDPDGAAgsafqyfENVRNFLVAIE 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1721967086  95 AYGMKpndIFEANDL--FENGNLTQVQTTLLAL 125
Cdd:cd21203    81 EMGLP---TFEASDLeqGGGGSRPRVVDCILAL 110

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721967086  30 EELRYWIEEVTGMPIGDNFQKGLKDGVILSELINKLQPGSVKKINHSQLNWHKL------ENLGNFIKAILAYGMKPNDI 103
Cdd:cd21205     4 EQLRKSIESRLKVTLPDDLGEALMDGVVLCHLANHVRPRSVPSIHVPSPAVPKLsmakcrRNVENFLEACRKLGVPEERL 83

                          90       100
                  ....*....|....*....|..
gi 1721967086 104 FEANDLFENGNLTQVQTTLLAL 125
Cdd:cd21205    84 CSPGDILEEKGLVRVAVTVQAL 105

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 1721967086  26 LQREEELRYWieevtgMPI---GDNFQKGLKDGVILSELINKLQPGSV--KKIN-HSQLN-WHKLENLGNFIKAILAYGM 98
Cdd:cd21217    14 LADDPDLKHL------LPIdpdGDDLFEALRDGVLLCKLINKIVPGTIdeRKLNkKKPKNiFEATENLNLALNAAKKIGC 87

                          90
                  ....*....|....
gi 1721967086  99 K-----PNDIFEAN 107
Cdd:cd21217    88 KvvnigPQDILDGN 101

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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1721967086  52 LKDGVILSELINKLQPGSVKKI-NHSQLNWHKLENLGNFIKAILAYGMkpnDIFEANDLFENGNLTQVQTTLLAL 125
Cdd:cd21265    35 LKDGVVLCKLIERLLPGSVEKYcLEPKTEADCIGNIKEFLKGCAALKV---ETFEPDDLYTGENFSKVLSTLLAV 106

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721967086  52 LKDGVILSELINKLQPGSV--KKIN-HSQLN-WHKLENLGNFIKAIL-AYGMKPNDIFEANDLFENGNLTQVQTTLLALA 126
Cdd:cd21264    36 LRDGVLLCQLLNNLRPHSInlKEINlRPQMSqFLCLKNIRTFLSACCeTFGMRKSELFEAFDLFDVRDFGKVIETLSKLS 115

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721967086  22 QKYDLQREEELRYWIEEVTGMPI-GDNFQKGLKDGVILSELINKLQ--------------PGSVKKI----NHSQLNWHK 82
Cdd:cd21204     1 EEALLPMKEDLAEWLNDLLGDDLtPDNFLDELRNGVVLCQLAQKIQeaaekareagkkngPPPSYKLkcneNAKPGSFFA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1721967086  83 LENLGNFIKAILAYGMKPNDIFEANDLFENGNLTQVQTTLLALANMAKTKG 133
Cdd:cd21204    81 RDNVANFLRWCRKLGVDEVLLFESEDLVLHKNPRQVLLCLLELARIAARYG 131

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 1721967086  31 ELRYWIEEVTGMPIGDNFQKGLKDGVILSELINKLQPGSVKKIN------HSQLNWHKLENLGNFIKAILAYGMKPNDIF 104
Cdd:cd21273     8 QLRKTLESRLKVTLPEDLAEALSNGAVLCQLANQLRPRSVSIIHvpspavPKLSKAKCRKNVENFIEACRKMGVPEVDLC 87

                          90       100
                  ....*....|....*....|..
gi 1721967086 105 EANDLFENGNLTQVQTTLLALA 126
Cdd:cd21273    88 SPSDVLLQGPAAVLRTVLALLA 109

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        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721967086  47 NFQKGLKDGVILSELINKLQPGSV--KKIN-HSQLN-WHKLENLGNFIKAIL-AYGMKPNDIFEANDLFENGNLTQVQTT 121
Cdd:cd21263    31 DLAQALRDGVLLCQLLHNLSPGSIdlKDINfRPQMSqFLCLKNIRTFLKVCHdKFGLRNSELFDPFDLFDVRDFGKVISA 110

                  ....*
gi 1721967086 122 LLALA 126
Cdd:cd21263   111 LSRLS 115

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721967086  25 DLQREEELRYWIEEVTGMPIGDNFQKGLKDGVILSELINKLQPGSVKKINHSQLNWHKL------ENLGNFIKAILAYGM 98
Cdd:cd21271     3 ELELIEQLRENIESRLKVILPEDLGAALMDGVVLCHLANHIRPRSVGSIHVPSPAVPKLsmakcrRNVENFLDACRKLGV 82

                          90       100
                  ....*....|....*....|....*..
gi 1721967086  99 KPNDIFEANDLFENGNLTQVQTTLLAL 125
Cdd:cd21271    83 PEDKLCLPHHILEEKGLVKVSVTVQAL 109

third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar proteins; 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 third CH domain. CH domains are actin filament (F-actin) binding motifs.

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gi 1721967086  24 YDLQREEELR---YWIEEVTGMPIGDNFQKGLKDGVILSELINKLQPGSV--KKINHSQ 77
Cdd:cd21300     1 FDAEGEREARvftLWLNSLDVEPAVNDLFEDLRDGLILLQAYDKVIPGSVnwKKVNKAP 59