second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated protein (ASPM) and similar proteins; ASPM, also called abnormal spindle protein homolog, or Asp homolog, is involved in mitotic spindle regulation and coordination of mitotic processes. It may also have a preferential role in regulating neurogenesis. Members of this family contain two copies of CH domain in the middle region. 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 332205965 1112 NIKLLMDWVNAVCAFYNKKVENFTVSFSDGRVLCYLIHHYHPCYVPFDAICQRTTQTVECTQTGSVvlnsssesddssLD 1191
Cdd:cd21224     1 VLSLLLKWCQAVCAHYGVKVENFTVSFADGRALCYLIHHYLPSLLPLDAIRQPTTQTVDRAQDEAE------------DF 68

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205965 1192 MSLKAFDHENTSELYKELLENEKKNFHLVRSAVRDLGGIPAMINHSDMSNTIPDEKVVITYLSFLCARLL 1261
Cdd:cd21224    69 WVAEFSPSTGDSGLSSELLANEKRNFKLVQQAVAELGGVPALLRASDMSNTIPDEKVVILFLSYLCARLL 138

Abnormal spindle-like microcephaly-assoc'd, ASPM-SPD-2-Hydin; The ASH domain or N-terminal domain of abnormal spindle-like microcephaly-associated protein are found in proteins associated with cilia, flagella, the centrosome and the Golgi complex. The domain is also found in Hydin and OCRL whose deficiencies are associated with hydrocephalus and Lowe oculocerebrorenal syndrome (OCRL), respectively. The fact that Human ASPM protein carries an ASH domain indicates possible roles for ASPM in sperm flagellar or in ependymal cells' cilia. The presence of ASH in centrosomal and ciliary proteins indicates that ASPM may possess roles not only in mitotic spindle regulation, but also in ciliary and flagellar function.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205965    37 PVLSLSHFCRSPFLCFGDVLLGASRTLSLALDNPNEEVAEVKISHFPAADLGFSVSQRCFVLQPKEKIVISVNWTPLKEG 116
Cdd:pfam15780    1 PVLLLAPFSRQPFVCFGDVPVGTSAERLLTVVNPSEEPAEVKVSKVPAPTKGFSVSPLEFTVQPGESQTLTVTWTPTEEG 80

                           90
                   ....*....|....*...
gi 332205965   117 RVREIMTFLVNDVLKHQA 134
Cdd:pfam15780   81 AVRETLQFTVNDVGKHQV 98

Myosin heavy chain [General function prediction only];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205965 1495 KKSTVILQALVRGWLVRKRFLEQRAKIRLLHftaaayyhlnavRIQRAYKLYLAVKNANKqVNSVICIQRWFRARLQEKR 1574
Cdd:COG5022   745 DNIATRIQRAIRGRYLRRRYLQALKRIKKIQ------------VIQHGFRLRRLVDYELK-WRLFIKLQPLLSLLGSRKE 811

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 332205965 1575 FIQKYHSIKKIEHE-GQECLSQRN-------RAASVIQKAVRHFLLRKKQEKFTSGIIKIQALWR 1631
Cdd:COG5022   812 YRSYLACIIKLQKTiKREKKLRETeevefslKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQR 876

second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated protein (ASPM) and similar proteins; ASPM, also called abnormal spindle protein homolog, or Asp homolog, is involved in mitotic spindle regulation and coordination of mitotic processes. It may also have a preferential role in regulating neurogenesis. Members of this family contain two copies of CH domain in the middle region. 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 332205965 1112 NIKLLMDWVNAVCAFYNKKVENFTVSFSDGRVLCYLIHHYHPCYVPFDAICQRTTQTVECTQTGSVvlnsssesddssLD 1191
Cdd:cd21224     1 VLSLLLKWCQAVCAHYGVKVENFTVSFADGRALCYLIHHYLPSLLPLDAIRQPTTQTVDRAQDEAE------------DF 68

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205965 1192 MSLKAFDHENTSELYKELLENEKKNFHLVRSAVRDLGGIPAMINHSDMSNTIPDEKVVITYLSFLCARLL 1261
Cdd:cd21224    69 WVAEFSPSTGDSGLSSELLANEKRNFKLVQQAVAELGGVPALLRASDMSNTIPDEKVVILFLSYLCARLL 138

Abnormal spindle-like microcephaly-assoc'd, ASPM-SPD-2-Hydin; The ASH domain or N-terminal domain of abnormal spindle-like microcephaly-associated protein are found in proteins associated with cilia, flagella, the centrosome and the Golgi complex. The domain is also found in Hydin and OCRL whose deficiencies are associated with hydrocephalus and Lowe oculocerebrorenal syndrome (OCRL), respectively. The fact that Human ASPM protein carries an ASH domain indicates possible roles for ASPM in sperm flagellar or in ependymal cells' cilia. The presence of ASH in centrosomal and ciliary proteins indicates that ASPM may possess roles not only in mitotic spindle regulation, but also in ciliary and flagellar function.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205965    37 PVLSLSHFCRSPFLCFGDVLLGASRTLSLALDNPNEEVAEVKISHFPAADLGFSVSQRCFVLQPKEKIVISVNWTPLKEG 116
Cdd:pfam15780    1 PVLLLAPFSRQPFVCFGDVPVGTSAERLLTVVNPSEEPAEVKVSKVPAPTKGFSVSPLEFTVQPGESQTLTVTWTPTEEG 80

                           90
                   ....*....|....*...
gi 332205965   117 RVREIMTFLVNDVLKHQA 134
Cdd:pfam15780   81 AVRETLQFTVNDVGKHQV 98

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
                    ....*....|....*....|....*....|....*....|....*....
gi 332205965   1114 KLLMDWVNAVCAFYNK-KVENFTVSFSDGRVLCYLIHHYHPCYVPFDAI 1161
Cdd:smart00033    1 KTLLRWVNSLLAEYDKpPVTNFSSDLKDGVALCALLNSLSPGLVDKKKV 49

Myosin heavy chain [General function prediction only];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205965 1495 KKSTVILQALVRGWLVRKRFLEQRAKIRLLHftaaayyhlnavRIQRAYKLYLAVKNANKqVNSVICIQRWFRARLQEKR 1574
Cdd:COG5022   745 DNIATRIQRAIRGRYLRRRYLQALKRIKKIQ------------VIQHGFRLRRLVDYELK-WRLFIKLQPLLSLLGSRKE 811

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 332205965 1575 FIQKYHSIKKIEHE-GQECLSQRN-------RAASVIQKAVRHFLLRKKQEKFTSGIIKIQALWR 1631
Cdd:COG5022   812 YRSYLACIIKLQKTiKREKKLRETeevefslKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQR 876

second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated protein (ASPM) and similar proteins; ASPM, also called abnormal spindle protein homolog, or Asp homolog, is involved in mitotic spindle regulation and coordination of mitotic processes. It may also have a preferential role in regulating neurogenesis. Members of this family contain two copies of CH domain in the middle region. 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 332205965 1112 NIKLLMDWVNAVCAFYNKKVENFTVSFSDGRVLCYLIHHYHPCYVPFDAICQRTTQTVECTQTGSVvlnsssesddssLD 1191
Cdd:cd21224     1 VLSLLLKWCQAVCAHYGVKVENFTVSFADGRALCYLIHHYLPSLLPLDAIRQPTTQTVDRAQDEAE------------DF 68

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205965 1192 MSLKAFDHENTSELYKELLENEKKNFHLVRSAVRDLGGIPAMINHSDMSNTIPDEKVVITYLSFLCARLL 1261
Cdd:cd21224    69 WVAEFSPSTGDSGLSSELLANEKRNFKLVQQAVAELGGVPALLRASDMSNTIPDEKVVILFLSYLCARLL 138

Abnormal spindle-like microcephaly-assoc'd, ASPM-SPD-2-Hydin; The ASH domain or N-terminal domain of abnormal spindle-like microcephaly-associated protein are found in proteins associated with cilia, flagella, the centrosome and the Golgi complex. The domain is also found in Hydin and OCRL whose deficiencies are associated with hydrocephalus and Lowe oculocerebrorenal syndrome (OCRL), respectively. The fact that Human ASPM protein carries an ASH domain indicates possible roles for ASPM in sperm flagellar or in ependymal cells' cilia. The presence of ASH in centrosomal and ciliary proteins indicates that ASPM may possess roles not only in mitotic spindle regulation, but also in ciliary and flagellar function.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205965    37 PVLSLSHFCRSPFLCFGDVLLGASRTLSLALDNPNEEVAEVKISHFPAADLGFSVSQRCFVLQPKEKIVISVNWTPLKEG 116
Cdd:pfam15780    1 PVLLLAPFSRQPFVCFGDVPVGTSAERLLTVVNPSEEPAEVKVSKVPAPTKGFSVSPLEFTVQPGESQTLTVTWTPTEEG 80

                           90
                   ....*....|....*...
gi 332205965   117 RVREIMTFLVNDVLKHQA 134
Cdd:pfam15780   81 AVRETLQFTVNDVGKHQV 98

first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two 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 332205965  962 DFAVTNLAVDLQCGVRLVRTMELLTQNwDLSKKLRIPAIsRLQKMHNVDIVLQVLKSRGIELSDehgntILSKDIVDRHR 1041
Cdd:cd21215    21 GLSITDLVTDLSDGVRLIQLLEIIGDE-SLGRYNKNPKM-RVQKLENVNKALEFIKSRGVKLTN-----IGAEDIVDGNL 93

                          90
                  ....*....|....
gi 332205965 1042 EKTLRLLWKIAFAF 1055
Cdd:cd21215    94 KLILGLLWTLILRF 107

first calponin homology (CH) domain found in the dystrophin family; The dystrophin family includes dystrophin and its paralog, utrophin. Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin is also involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and links the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Members of this family contain two 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 332205965  965 VTNLAVDLQCGVRLVRTMELLTQNWDLSKKLRipaiSRLQKMHNVDIVLQVLKSRGIELSDehgntILSKDIVDRHREKT 1044
Cdd:cd21186    23 IKDLFEDLRDGTRLLALLEVLTGKKLKPEKGR----MRVHHLNNVNRALQVLEQNNVKLVN-----ISSNDIVDGNPKLT 93

                          90
                  ....*....|...
gi 332205965 1045 LRLLWKIAFAFQV 1057
Cdd:cd21186    94 LGLVWSIILHWQV 106

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
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 332205965  1114 KLLMDWVNAVCAFY--NKKVENFTVSFSDGRVLCYLIHHYHPCYVPFDAICQRTTQTVE 1170
Cdd:pfam00307    5 KELLRWINSHLAEYgpGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEFDKLE 63

calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family includes MICAL-L1 and MICAL-L2. MICAL-L1, also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. MICAL-L2, also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this family contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205965 1113 IKLLMDWVNAVCAFY-NKKVENFTVSFSDGRVLCYLIHHYHPCYVPFDAIcqrttqtvectqtgsvvlnsssesddssld 1191
Cdd:cd21197     2 IQALLRWCRRQCEGYpGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSL------------------------------ 51

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 332205965 1192 mslkafDHENtselykeLLENEKKNFHLVRSAVrdlgGIPAMINHSDM-SNTIPDEKVVITYLS 1254
Cdd:cd21197    52 ------KKDN-------WLENNRLAFRVAETSL----GIPALLDAEDMvTMHVPDRLSIITYVS 98

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205965  962 DFAVTNLAVDLQCGVRLVRTMELLtQNWDLSKKLRIPaISRLQKMHNVDIVLQVLKSRGIELSDehgntILSKDIVDRHR 1041
Cdd:cd21227    21 GMSVEDLATDLEDGVKLIALVEIL-QGRKLGRVIKKP-LNQHQKLENVTLALKAMAEDGIKLVN-----IGNEDIVNGNL 93

                          90
                  ....*....|....*.
gi 332205965 1042 EKTLRLLWKIAFAFQV 1057
Cdd:cd21227    94 KLILGLIWHLILRYQI 109

second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two 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 332205965 1105 SFEQYSENIKLLMdWVNAVCAFY-NKKVENFTVSFSDGRVLCYLIHHYHPCYVPFDaicqrttqtvectqtgsvvlnsss 1183
Cdd:cd21216     5 SVEELSAKEGLLL-WCQRKTAPYkNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYD------------------------ 59

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 332205965 1184 esddssldmslkafdhentsELYKellENEKKNFHLVRS-AVRDLgGIPAMINHSDMSNTI-PDEKVVITYLS 1254
Cdd:cd21216    60 --------------------KLRK---DDPRENLNLAFDvAEKHL-DIPKMLDAEDIVNTPrPDERSVMTYVS 108

first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin family includes beta-I, -II, -III, -IV and -V spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Beta-III spectrin is also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5). Beta-V spectrin, also called spectrin beta chain, non-erythrocytic 5 (SPTBN5), is a mammalian ortholog of Drosophila beta H spectrin. Beta-III and Beta-V spectrins may play crucial roles as longer actin-membrane cross-linkers or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Members of this family contain two 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 332205965  958 FDEFDFAVTNLAVDLQCGVRLVRTMELLTqnwdlSKKLRIPA--ISRLQKMHNVDIVLQVLKSRgielsdEHGNTILSKD 1035
Cdd:cd21193    29 LEKANLEIGDLFTDLSDGKLLLKLLEIIS-----GEKLGKPNrgRLRVQKIENVNKALAFLKTK------VRLENIGAED 97

                          90
                  ....*....|....*.
gi 332205965 1036 IVDRHREKTLRLLWKI 1051
Cdd:cd21193    98 IVDGNPRLILGLIWTI 113

first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. This model corresponds to the first CH domain.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205965  965 VTNLAVDLQCGVRLVRTMELLTqNWDLSKKlriPAISRLQKMHNVDIVLQVLKSRGIELSDehgntILSKDIVDRHREKT 1044
Cdd:cd21231    27 IEDLFTDLQDGRRLLELLEGLT-GQKLVKE---KGSTRVHALNNVNKALQVLQKNNVDLVN-----IGSADIVDGNHKLT 97

                          90
                  ....*....|...
gi 332205965 1045 LRLLWKIAFAFQV 1057
Cdd:cd21231    98 LGLIWSIILHWQV 110

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
                  ....*....|....*....|....*....|....*....|....*...
gi 332205965 1113 IKLLMDWVNAVCAFYNK-KVENFTVSFSDGRVLCYLIHHYHPCYVPFD 1159
Cdd:cd00014     1 EEELLKWINEVLGEELPvSITDLFESLRDGVLLCKLINKLSPGSIPKI 48

first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar proteins; Synaptic nuclear envelope protein 1 (SYNE-1), also called nesprin-1, enaptin, KASH domain-containing protein 1 (KASH1), myocyte nuclear envelope protein 1 (MYNE-1), or nuclear envelope spectrin repeat protein 1, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-1 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-1 contains two 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 332205965  965 VTNLAVDLQCGVRLVRTMELLTqnwdlSKKLRIPAISRLQKMH---NVDIVLQVLKSRGIELSDehgntILSKDIVDRHR 1041
Cdd:cd21241    27 VEDLFEDIKDGTKLLALLEVLS-----GEKLPCEKGRRLKRVHflsNINTALKFLESKKIKLVN-----INPTDIVDGKP 96

                          90
                  ....*....|....*..
gi 332205965 1042 EKTLRLLWKIAFAFQVD 1058
Cdd:cd21241    97 SIVLGLIWTIILYFQIE 113

first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. Dystonin contains two 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 332205965  965 VTNLAVDLQCGVRLVRTMELLTQNWDLSKKLRIpaisRLQKMHNVDIVLQVLKSRGIELSDehgntILSKDIVDRHREKT 1044
Cdd:cd21236    37 VNDLYEDLRDGHNLISLLEVLSGDTLPREKGRM----RFHRLQNVQIALDYLKRRQVKLVN-----IRNDDITDGNPKLT 107

                          90
                  ....*....|...
gi 332205965 1045 LRLLWKIAFAFQV 1057
Cdd:cd21236   108 LGLIWTIILHFQI 120

first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. Members of this family contain two copies of the CH domain. The 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 332205965  965 VTNLAVDLQCGVRLVRTMELLTQNwDLSKKLRIPAISRLQKMHNVDIVLQVLKSRGIELSdehgnTILSKDIVDRHREKT 1044
Cdd:cd21228    24 IYNLETDLSDGLRLIALLEVLSQK-RMYKKYNKRPTFRQMKLENVSVALEFLERESIKLV-----SIDSSAIVDGNLKLI 97

                  ....*
gi 332205965 1045 LRLLW 1049
Cdd:cd21228    98 LGLIW 102

calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. This model corresponds to the single CH domain of smoothelin-A. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205965 1114 KLLMDWVNAVCAFY-NKKVENFTVSFSDGRVLCYLIHHYHPcyvpfdaicqrttqtvectqtgsvvlnsssesddssldm 1192
Cdd:cd21258     4 QMLLDWCRAKTRGYeHVDIQNFSSSWSDGMAFCALVHNFFP--------------------------------------- 44

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332205965 1193 slKAFDHENTSElykellENEKKNFHLVRSAVRDLGGIPAMINHSDM--SNTIPDEKVVITYLSFL 1256
Cdd:cd21258    45 --DAFDYSQLSP------QNRRQNFEVAFSAAEMLADCVPLVEVEDMmiMGKKPDSKCVFTYVQSL 102

first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 contains two 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 332205965  965 VTNLAVDLQCGVRLVRTMELLTqnwdlSKKLRIPAISRLQK--MHNVDIVLQVLKSRGIELSDehgntILSKDIVDRHRE 1042
Cdd:cd21317    51 IGDLYTDLRDGRMLIRLLEVLS-----GEQLPKPTKGRMRIhcLENVDKALQFLKEQKVHLEN-----MGSHDIVDGNHR 120

                  ....*....
gi 332205965 1043 KTLRLLWKI 1051
Cdd:cd21317   121 LTLGLIWTI 129

first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two 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 332205965  965 VTNLAVDLQCGVRLVRTMELLTqnwdlSKKLRIPAIS--RLQKMHNVDIVLQVLKSRGIELSDehgntILSKDIVDRHRE 1042
Cdd:cd21246    36 INDLYTDLRDGRMLIKLLEVLS-----GERLPKPTKGkmRIHCLENVDKALQFLKEQRVHLEN-----MGSHDIVDGNHR 105

                  ....*....
gi 332205965 1043 KTLRLLWKI 1051
Cdd:cd21246   106 LTLGLIWTI 114

calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. Members of this subfamily 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 332205965 1116 LMDWVNAVCAFYNK-KVENFTVSFSDGRVLCYLIHHYHPCYVPFDAICQRttqtvectqtgsvvlnsssesddssldmsl 1194
Cdd:cd21254     6 LLAWCKEVTKGYRGvKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPH------------------------------ 55

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 332205965 1195 kafdhentselykELLENEKKNFHLVRSAvrdlgGIPAMINHSDMSN-TIPDEKVVITYL 1253
Cdd:cd21254    56 -------------DIKENNKKAYDGFASL-----GISRLLEPSDMVLlAVPDKLTVMTYL 97

second calponin homology (CH) domain found in the parvin family; The parvin family includes alpha-parvin, beta-parvin, and gamma-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. Members of this family contain two 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 332205965  905 LIDHDPclfckdAEFKASKEILLAFsrdflsgegdLSRHLGLLGLPVNHVQTPFDEfdfavtnlavdlqcGVRLVRTMEL 984
Cdd:cd21222     6 LFDEAP------EKLAEVKELLLQF----------VNKHLAKLNIEVTDLATQFHD--------------GVYLILLIGL 55

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 332205965  985 LTQNWDLSKKLRIPAISRLQKMHNVDIVLQVLKSRGIELsdehgNTILSKDIVDRHREKTLRLLWKI 1051
Cdd:cd21222    56 LEGFFVPLHEYHLTPSTDDEKLHNVKLALELMEDAGIST-----PKIRPEDIVNGDLKSILRVLYSL 117

first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The synaptic nuclear envelope (SYNE) family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Members of this family contain two 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 332205965  965 VTNLAVDLQCGVRLVRTMELLTqnwdlSKKLRIPAISRLQKMH---NVDIVLQVLKSRGIELSDEHgntilSKDIVDRHR 1041
Cdd:cd21190    27 INDLFVDIKDGTALLRLLEVLS-----GQKLPIESGRVLQRAHklsNIRNALDFLTKRCIKLVNIN-----STDIVDGKP 96

                          90
                  ....*....|....*..
gi 332205965 1042 EKTLRLLWKIAFAFQVD 1058
Cdd:cd21190    97 SIVLGLIWTIILYFQIE 113

calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; This family includes neuron navigator 2 (NAV2) and NAV3, both of which contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs. NAV2, also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV3, also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332205965  965 VTNLAVDLQCGVRLVRTMELLTqnwdlskKLRIPAI-----SRLQKMHNVDIVLQVLKSRGIELSDehgntILSKDIVD 1038
Cdd:cd21212    22 ITDLQKDLGDGLTLVNLIEAVA-------GEKVPGIhsrpkTRAQKLENIQACLQFLAALGVDVQG-----ITAEDIVD 88

first calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other members of this family contain two 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 332205965  965 VTNLAVDLQCGVRLVRTMELLTQNWDLSKKLRIPAIsRLQKMHNVDIVLQVLKSRGIELSdehgnTILSKDIVDRHREKT 1044
Cdd:cd21183    24 IHDLATDFSDGLCLIALLENLSTRPLKRSYNRRPAF-QQHYLENVSTALKFIEADHIKLV-----NIGSGDIVNGNIKLI 97

                  ....*..
gi 332205965 1045 LRLLWKI 1051
Cdd:cd21183    98 LGLIWTL 104