first calponin homology (CH) domain found in gamma-parvin; Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. It 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 341941231  45 ELQKVLMEWINTTLLPEHIVVRSLEEDMFDGLILHHLFQKLASLKLEVEEISLTSASQRHKLGVILEAVNQNLQVEEKQA 124
Cdd:cd21305    1 ELKEVLIDWINTTLKQEHIVVKSLEEDLYDGLVLHHLLVKLAGVKLEVEEIALTENAQKRKLTVILEAVNQSLQLEESQL 80

                         90       100
                 ....*....|....*....|....*.
gi 341941231 125 KWSVETIFNKDLLATLHLLVALAKRF 150
Cdd:cd21305   81 KWSVELIHNKDLLATLHLLVAIAKHF 106

first calponin homology (CH) domain found in gamma-parvin; Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. It 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 341941231  45 ELQKVLMEWINTTLLPEHIVVRSLEEDMFDGLILHHLFQKLASLKLEVEEISLTSASQRHKLGVILEAVNQNLQVEEKQA 124
Cdd:cd21305    1 ELKEVLIDWINTTLKQEHIVVKSLEEDLYDGLVLHHLLVKLAGVKLEVEEIALTENAQKRKLTVILEAVNQSLQLEESQL 80

                         90       100
                 ....*....|....*....|....*.
gi 341941231 125 KWSVETIFNKDLLATLHLLVALAKRF 150
Cdd:cd21305   81 KWSVELIHNKDLLATLHLLVAIAKHF 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        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941231   44 EELQKVLMEWINTTL--LPEHIVVRSLEEDMFDGLILHHLFQKLASLKLEVEEISLTSASQRHKLGVILEAVNQNLQVeE 121
Cdd:pfam00307   1 LELEKELLRWINSHLaeYGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEFDKLENINLALDVAEKKLGV-P 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 341941231  122 KQAKWSVEtIFNKDLLATLHLLVALAKRFQ 151
Cdd:pfam00307  80 KVLIEPED-LVEGDNKSVLTYLASLFRRFQ 108

first calponin homology (CH) domain found in gamma-parvin; Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. It 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 341941231  45 ELQKVLMEWINTTLLPEHIVVRSLEEDMFDGLILHHLFQKLASLKLEVEEISLTSASQRHKLGVILEAVNQNLQVEEKQA 124
Cdd:cd21305    1 ELKEVLIDWINTTLKQEHIVVKSLEEDLYDGLVLHHLLVKLAGVKLEVEEIALTENAQKRKLTVILEAVNQSLQLEESQL 80

                         90       100
                 ....*....|....*....|....*.
gi 341941231 125 KWSVETIFNKDLLATLHLLVALAKRF 150
Cdd:cd21305   81 KWSVELIHNKDLLATLHLLVAIAKHF 106

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941231  45 ELQKVLMEWINTTLLPEHIVVRSLEEDMFDGLILHHLFQKLASLKLEVEEISLTSASQRHKLGVILEAVNQNLQVEEKQA 124
Cdd:cd21221    1 ELVRVLTEWINEELADDRIVVRDLEEDLFDGQVLQALLEKLANEKLEVPEVAQSEEGQKQKLAVVLACVNFLLGLEEDEA 80

                         90       100
                 ....*....|....*....|....*.
gi 341941231 125 KWSVETIFNKDLLATLHLLVALAKRF 150
Cdd:cd21221   81 RWTVDGIYNKDLVSILHLLVALAHHY 106

second calponin homology (CH) domain found in alpha-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. It is also involved in the reorganization of the actin cytoskeleton, the formation of lamellipodia and ciliogenesis, as well as in the establishement of cell polarity, cell adhesion, cell spreading, and directed cell migration. Alpha-parvin contains 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 341941231 195 QDAFDELFKLAPEKVHAVQEAIVSFVNQKLERLGLSVQSLDTQFADGVILLLLIGQLEGFFLHLKEFYLTPSSPTEMLHN 274
Cdd:cd21337    4 RDAFDTLFDHAPDKLNVVKKTLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEGYFVPLHSFFLTPDSFEQKVLN 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 341941231 275 VTLALDLLKDEGLFSYPVNPEDIVNKDAKSTLRILYSLFQKH 316
Cdd:cd21337   84 VSFAFELMQDGGLEKPKPRPEDIVNCDLKSTLRVLYNLFTKY 125

first calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta parvin subfamily includes alpha-parvin and beta-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. 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 341941231  45 ELQKVLMEWINTTLLPEHIVVRSLEEDMFDGLILHHLFQKLASLKLEVEEISLTSASQRHKLGVILEAVNQNLQVEE-KQ 123
Cdd:cd21304    1 ELIKVLIEWINDELAEQRIIVKDIEEDLYDGQVLQKLLEKLTGVKLEVAEVTQSEVGQKQKLRTVLDKINRILNLPRwSQ 80

                         90       100
                 ....*....|....*....|....*..
gi 341941231 124 AKWSVETIFNKDLLATLHLLVALAKRF 150
Cdd:cd21304   81 QKWSVDSIHSKNLVAILHLLVALARHF 107

first calponin homology (CH) domain found in beta-parvin; 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. It is involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia and also plays a role in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Beta-parvin 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 341941231  45 ELQKVLMEWINTTLLPEHIVVRSLEEDMFDGLILHHLFQKLASLKLEVEEISLTSASQRHKLGVILEAVNQNLQVEEKQA 124
Cdd:cd21336    1 ELVKVLIDWINDVLVEERIIVKDLEEDLYDGQVLQKLLEKLAGRKLNVAEVTQSEIGQKQKLQTVLEAVNDLLRPQGWAI 80

                         90       100
                 ....*....|....*....|....*.
gi 341941231 125 KWSVETIFNKDLLATLHLLVALAKRF 150
Cdd:cd21336   81 KWSVDSIHGKNLVAILHLLVALAMHF 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        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941231   44 EELQKVLMEWINTTL--LPEHIVVRSLEEDMFDGLILHHLFQKLASLKLEVEEISLTSASQRHKLGVILEAVNQNLQVeE 121
Cdd:pfam00307   1 LELEKELLRWINSHLaeYGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEFDKLENINLALDVAEKKLGV-P 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 341941231  122 KQAKWSVEtIFNKDLLATLHLLVALAKRFQ 151
Cdd:pfam00307  80 KVLIEPED-LVEGDNKSVLTYLASLFRRFQ 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 341941231 213 QEAIVSFVNQKL-ERLGLSVQSLDTQFADGVILLLLIGQLEGFflHLKEFYLTPSSPTEMLHNVTLALDLLKDEGLFSYP 291
Cdd:cd00014    1 EEELLKWINEVLgEELPVSITDLFESLRDGVLLCKLINKLSPG--SIPKINKKPKSPFKKRENINLFLNACKKLGLPELD 78

                         90       100
                 ....*....|....*....|...
gi 341941231 292 -VNPEDIV-NKDAKSTLRILYSL 312
Cdd:cd00014   79 lFEPEDLYeKGNLKKVLGTLWAL 101

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        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341941231 220 VNQKLERLGLS--VQSLDTQFADGVILLLLIGQLEGFFLHLkeFYLTPSSPTEMLHNVTLALDLLKDEGLFSYPVNPEDI 297
Cdd:cd21212    9 ANHYLEKGGHKriITDLQKDLGDGLTLVNLIEAVAGEKVPG--IHSRPKTRAQKLENIQACLQFLAALGVDVQGITAEDI 86

                         90
                 ....*....|....*
gi 341941231 298 VNKDAKSTLRILYSL 312
Cdd:cd21212   87 VDGNLKAILGLFFSL 101

first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and 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 341941231 212 VQE-AIVSFVNQKLERLGLS-VQSLDTQFADGVILLLLIGQLEGFFLHlKEFYLTPSSPTEMLHNVTLALDLLKDEGLFS 289
Cdd:cd21225    4 VQIkAFTAWVNSVLEKRGIPkISDLATDLSDGVRLIFFLELVSGKKFP-KKFDLEPKNRIQMIQNLHLAMLFIEEDLKIR 82

                         90       100
                 ....*....|....*....|....*....
gi 341941231 290 YP-VNPEDIVNKDAKSTLRILYSLFQKHS 317
Cdd:cd21225   83 VQgIGAEDFVDNNKKLILGLLWTLYRKYR 111

first 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 the CH domain in the middle region. 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 341941231 230 SVQSLDTQFADGVILLLLIGQLEGFFLHLKEFYLTPSSPTEMLHNVTLALDLLKDEGLFS----YPVNPEDIVNKDAKST 305
Cdd:cd21223   25 AVTNLAVDLRDGVRLCRLVELLTGDWSLLSKLRVPAISRLQKLHNVEVALKALKEAGVLRggdgGGITAKDIVDGHREKT 104

                 ....*..
gi 341941231 306 LRILYSL 312
Cdd:cd21223  105 LALLWRI 111

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 341941231 213 QEAIVSFVNQKLERLGLSVQSLDTQFADGVILLLLIGQLEGFFLHlKEFYLTPSSPTEMLHNVTLALDLLKDEGLFSYPV 292
Cdd:cd21228    6 QNTFTRWCNEHLKCVNKRIYNLETDLSDGLRLIALLEVLSQKRMY-KKYNKRPTFRQMKLENVSVALEFLERESIKLVSI 84

                         90       100
                 ....*....|....*....|....
gi 341941231 293 NPEDIVNKDAKSTLRILYSLFQKH 316
Cdd:cd21228   85 DSSAIVDGNLKLILGLIWTLILHY 108

first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) 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. SPTBN4, also called beta-IV spectrin, or spectrin, non-erythroid beta chain 3 (SPTBN3), is a novel spectrin isolated as an interactor of the receptor tyrosine phosphatase-like protein ICA512. Its mutation associates with congenital myopathy, neuropathy, and central deafness. SPTBN4 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 341941231 168 ESTKTGLKSDKQVEQLTECKSHKdqplqdafdelfKLAPEKVHAVQEAIVSFVNQKLERLGLSVQSLDTQFADGVILLLL 247
Cdd:cd21318    7 ESTERPWDEPAATAKLFECSRIK------------ALADEREAVQKKTFTKWVNSHLARVPCRINDLYTDLRDGYVLTRL 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 341941231 248 IGQLEGfflhlkEFYLTPSSPTEMLH---NVTLALDLLKDEGLFSYPVNPEDIVNKDAKSTLRILYSL 312
Cdd:cd21318   75 LEVLSG------EQLPKPTRGRMRIHsleNVDKALQFLKEQRVHLENVGSHDIVDGNHRLTLGLIWTI 136

first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. 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. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. 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 341941231 220 VNQKLERLGLSVQSLDTQFADGVILLLLIGQLEGFFLHLKEFYLTpsspTEMLHNVTLALDLLKDEGLFSYPVNPEDIVN 299
Cdd:cd21188   12 VNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPRERGRMR----FHRLQNVQTALDFLKYRKIKLVNIRAEDIVD 87

                         90
                 ....*....|....*...
gi 341941231 300 KDAKSTLRILYSL---FQ 314
Cdd:cd21188   88 GNPKLTLGLIWTIilhFQ 105