calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called coiled-coil protein DIX1, coiled-coil-DIX1, or DIX domain-containing protein 1, is a positive effector of the Wnt signaling pathway. It activates WNT3A signaling via DVL2 and regulates JNK activation by AXIN1 and DVL2. Members of this family contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048774911  22 QLQAYVAWVNAQLKKRPSVKPVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLSPSNQQEMKSNVERVLQFVASKNIRMHQ 101
Cdd:cd21213     1 QLQAYVAWVNSQLKKRPGIRPVQDLRRDLRDGVALAQLIEILAGEKLPGIDWNPTTDAERKENVEKVLQFMASKRIRMHQ 80

                          90       100
                  ....*....|....*....|....*..
gi 2048774911 102 TSAKDIVEGNLKSIMRLVLALAAHFKP 128
Cdd:cd21213    81 TSAKDIVDGNLKAIMRLILALAAHFKP 107

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048774911 281 EEQLLEQQEHLEKEMEEAKKMISGLQALLLngslpEDEQERpvalcepgvnpeeqlIIIRSRLDQSMEENQDLKKELLKC 360
Cdd:COG1196   339 LEELEEELEEAEEELEEAEAELAEAEEALL-----EAEAEL---------------AEAEEELEELAEELLEALRAAAEL 398

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048774911 361 KQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLDERNRLLGEYKKDLGQKDRLLQQQQAK 440
Cdd:COG1196   399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2048774911 441 LEDALRKLSDASYQ-----QVDLERELEQKDVLLAHRVKG 475
Cdd:COG1196   479 LAELLEELAEAAARlllllEAEADYEGFLEGVKAALLLAG 518

calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called coiled-coil protein DIX1, coiled-coil-DIX1, or DIX domain-containing protein 1, is a positive effector of the Wnt signaling pathway. It activates WNT3A signaling via DVL2 and regulates JNK activation by AXIN1 and DVL2. Members of this family contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048774911  22 QLQAYVAWVNAQLKKRPSVKPVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLSPSNQQEMKSNVERVLQFVASKNIRMHQ 101
Cdd:cd21213     1 QLQAYVAWVNSQLKKRPGIRPVQDLRRDLRDGVALAQLIEILAGEKLPGIDWNPTTDAERKENVEKVLQFMASKRIRMHQ 80

                          90       100
                  ....*....|....*....|....*..
gi 2048774911 102 TSAKDIVEGNLKSIMRLVLALAAHFKP 128
Cdd:cd21213    81 TSAKDIVDGNLKAIMRLILALAAHFKP 107

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 2048774911  24 QAYVAWVNAQLKKRPSVKPVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLSPSNQQEMKsNVERVLQFVASK-NIRMHQT 102
Cdd:pfam00307   5 KELLRWINSHLAEYGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEFDKLE-NINLALDVAEKKlGVPKVLI 83

                          90       100
                  ....*....|....*....|....*
gi 2048774911 103 SAKDIVEGNLKSIMRLVLALAAHFK 127
Cdd:pfam00307  84 EPEDLVEGDNKSVLTYLASLFRRFQ 108

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 2048774911   25 AYVAWVNAQLKKRPSVkPVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLSPSNQQEMK-SNVERVLQFVASKNIRMHQTS 103
Cdd:smart00033   2 TLLRWVNSLLAEYDKP-PVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSRFKKiENINLALSFAEKLGGKVVLFE 80

                           90       100
                   ....*....|....*....|..
gi 2048774911  104 AKDIVEGNlKSIMRLVLALAAH 125
Cdd:smart00033  81 PEDLVEGP-KLILGVIWTLISL 101

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048774911 281 EEQLLEQQEHLEKEMEEAKKMISGLQALLLngslpEDEQERpvalcepgvnpeeqlIIIRSRLDQSMEENQDLKKELLKC 360
Cdd:COG1196   339 LEELEEELEEAEEELEEAEAELAEAEEALL-----EAEAEL---------------AEAEEELEELAEELLEALRAAAEL 398

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048774911 361 KQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLDERNRLLGEYKKDLGQKDRLLQQQQAK 440
Cdd:COG1196   399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2048774911 441 LEDALRKLSDASYQ-----QVDLERELEQKDVLLAHRVKG 475
Cdd:COG1196   479 LAELLEELAEAAARlllllEAEADYEGFLEGVKAALLLAG 518

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048774911  281 EEQLLEQQEHLEKEMEEAKKMISGLQALL--LNGSLPEDEQERpVALCEPGVNPEEQLIIIRSRLDQSMEENQDLKKELL 358
Cdd:TIGR02168  742 VEQLEERIAQLSKELTELEAEIEELEERLeeAEEELAEAEAEI-EELEAQIEQLKEELKALREALDELRAELTLLNEEAA 820

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048774911  359 KCKQEARNLQGIKDALQQRLT--QQDTSVLQLKQELLRANMDkdelhnqnvDLQRKLDERNRLLGEYKKDLGQKDRLLQQ 436
Cdd:TIGR02168  821 NLRERLESLERRIAATERRLEdlEEQIEELSEDIESLAAEIE---------ELEELIEELESELEALLNERASLEEALAL 891

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 2048774911  437 QQAKLEDALRKLSDASYQQVDLERELEQKDVLLAH 471
Cdd:TIGR02168  892 LRSELEELSEELRELESKRSELRRELEELREKLAQ 926

calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called coiled-coil protein DIX1, coiled-coil-DIX1, or DIX domain-containing protein 1, is a positive effector of the Wnt signaling pathway. It activates WNT3A signaling via DVL2 and regulates JNK activation by AXIN1 and DVL2. Members of this family contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048774911  22 QLQAYVAWVNAQLKKRPSVKPVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLSPSNQQEMKSNVERVLQFVASKNIRMHQ 101
Cdd:cd21213     1 QLQAYVAWVNSQLKKRPGIRPVQDLRRDLRDGVALAQLIEILAGEKLPGIDWNPTTDAERKENVEKVLQFMASKRIRMHQ 80

                          90       100
                  ....*....|....*....|....*..
gi 2048774911 102 TSAKDIVEGNLKSIMRLVLALAAHFKP 128
Cdd:cd21213    81 TSAKDIVDGNLKAIMRLILALAAHFKP 107

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 2048774911  22 QLQAYVAWVNAQLKKRPSVKPVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLSPSNQQEMKSNVERVLQFVASKNIRMHQ 101
Cdd:cd21212     1 EIEIYTDWANHYLEKGGHKRIITDLQKDLGDGLTLVNLIEAVAGEKVPGIHSRPKTRAQKLENIQACLQFLAALGVDVQG 80

                          90       100
                  ....*....|....*....|....*
gi 2048774911 102 TSAKDIVEGNLKSIMRLVLALAAHF 126
Cdd:cd21212    81 ITAEDIVDGNLKAILGLFFSLSRYK 105

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 2048774911  24 QAYVAWVNAQLKKRPSVKPVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLSPSNQQEMKsNVERVLQFVASK-NIRMHQT 102
Cdd:pfam00307   5 KELLRWINSHLAEYGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEFDKLE-NINLALDVAEKKlGVPKVLI 83

                          90       100
                  ....*....|....*....|....*
gi 2048774911 103 SAKDIVEGNLKSIMRLVLALAAHFK 127
Cdd:pfam00307  84 EPEDLVEGDNKSVLTYLASLFRRFQ 108

calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (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. NAV3 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 2048774911  26 YVAWVNAQLKKRPSVKPVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLSPSNQQEMKSNVERVLQFVASKNIRMHQTSAK 105
Cdd:cd21286     5 YTDWANHYLAKSGHKRLIKDLQQDIADGVLLAEIIQIIANEKVEDINGCPRSQSQMIENVDVCLSFLAARGVNVQGLSAE 84

                          90
                  ....*....|....*...
gi 2048774911 106 DIVEGNLKSIMRLVLALA 123
Cdd:cd21286    85 EIRNGNLKAILGLFFSLS 102

calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (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. NAV2 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 2048774911  19 NEQQLQAYVAWVNAQLKKRPSVKPVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLSPSNQQEMKSNVERVLQFVASKNIR 98
Cdd:cd21285     8 NGFDKQIYTDWANHYLAKSGHKRLIKDLQQDVTDGVLLAEIIQVVANEKIEDINGCPKNRSQMIENIDACLSFLAAKGIN 87

                          90       100
                  ....*....|....*....|....*
gi 2048774911  99 MHQTSAKDIVEGNLKSIMRLVLALA 123
Cdd:cd21285    88 IQGLSAEEIRNGNLKAILGLFFSLS 112

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 2048774911  22 QLQAYVAWVNAQLKKRPsvKPVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLSPSNQQEMKSNVERVLQFVASKNIRMHQ 101
Cdd:cd21215     5 QKKTFTKWLNTKLSSRG--LSITDLVTDLSDGVRLIQLLEIIGDESLGRYNKNPKMRVQKLENVNKALEFIKSRGVKLTN 82

                          90       100
                  ....*....|....*....|....*
gi 2048774911 102 TSAKDIVEGNLKSIMRLVLALAAHF 126
Cdd:cd21215    83 IGAEDIVDGNLKLILGLLWTLILRF 107

first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic nuclear envelope protein 2 (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, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 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-2 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 2048774911  22 QLQAYVAWVNAQLKKRPSVKPVQDLRQDLRDGVILAYLIEIVAGEKLSgvQLSPSNQQEMKSNVERVLQFVASKNIRMHQ 101
Cdd:cd21242     6 QKRTFTNWINSQLAKHSPPSVVSDLFTDIQDGHRLLDLLEVLSGQQLP--REKGHNVFQCRSNIETALSFLKNKSIKLIN 83

                          90       100
                  ....*....|....*....|....*
gi 2048774911 102 TSAKDIVEGNLKSIMRLVLALAAHF 126
Cdd:cd21242    84 IHVPDIIEGKPSIILGLIWTIILHF 108

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 2048774911  22 QLQAYVAWVNAQLKKRPSVKPVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLSPSNQQEMKSNVERVLQFVASKNIRMHQ 101
Cdd:cd21190     6 QKKTFTNWINSHLAKLSQPIVINDLFVDIKDGTALLRLLEVLSGQKLPIESGRVLQRAHKLSNIRNALDFLTKRCIKLVN 85

                          90       100
                  ....*....|....*....|....*.
gi 2048774911 102 TSAKDIVEGNLKSIMRLVLALAAHFK 127
Cdd:cd21190    86 INSTDIVDGKPSIVLGLIWTIILYFQ 111

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 2048774911  20 EQ---QLQAYVAWVNAQLKKRPSVKPVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLSPSNQQEMKSNVERVLQFVASKN 96
Cdd:cd21241     1 EQervQKKTFTNWINSYLAKRKPPMKVEDLFEDIKDGTKLLALLEVLSGEKLPCEKGRRLKRVHFLSNINTALKFLESKK 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2048774911  97 IRMHQTSAKDIVEGNLKSIMRLVLALAAHFK 127
Cdd:cd21241    81 IKLVNINPTDIVDGKPSIVLGLIWTIILYFQ 111

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 2048774911  22 QLQAYVAWVNAQLKKRPSvkPVQDLRQDLRDGVILAYLIEIVAGEKlsgvqLSPSNQQEMK----SNVERVLQFVASKNI 97
Cdd:cd21246    17 QKKTFTKWVNSHLARVGC--RINDLYTDLRDGRMLIKLLEVLSGER-----LPKPTKGKMRihclENVDKALQFLKEQRV 89

                          90       100
                  ....*....|....*....|....*
gi 2048774911  98 RMHQTSAKDIVEGNlksiMRLVLAL 122
Cdd:cd21246    90 HLENMGSHDIVDGN----HRLTLGL 110

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 2048774911  14 LQEGFNEQQLQAYVAWVNAQLKKRPSVkpVQDLRQDLRDGVILAYLIEIVAGEKlsgvqLSPSNQQEMK----SNVERVL 89
Cdd:cd21193     9 LQEERINIQKKTFTKWINSFLEKANLE--IGDLFTDLSDGKLLLKLLEIISGEK-----LGKPNRGRLRvqkiENVNKAL 81

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2048774911  90 QFVASKnIRMHQTSAKDIVEGNlksiMRLVLAL 122
Cdd:cd21193    82 AFLKTK-VRLENIGAEDIVDGN----PRLILGL 109

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 2048774911  22 QLQAYVAWVNAQLKKRPSvkPVQDLRQDLRDGVILAYLIEIVAGEklsgvQLSPSNQQEMK----SNVERVLQFVASKNI 97
Cdd:cd21318    39 QKKTFTKWVNSHLARVPC--RINDLYTDLRDGYVLTRLLEVLSGE-----QLPKPTRGRMRihslENVDKALQFLKEQRV 111

                          90       100
                  ....*....|....*....|....*
gi 2048774911  98 RMHQTSAKDIVEGNlksiMRLVLAL 122
Cdd:cd21318   112 HLENVGSHDIVDGN----HRLTLGL 132

first calponin homology (CH) domain found in calmin and similar proteins; 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. Calmin 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 2048774911  22 QLQAYVAWVNAQLKKRPSVKPVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLSPSNQQEMKSNVERVLQFVASKNIRMHQ 101
Cdd:cd21191     6 QKRTFTRWINLHLEKCNPPLEVKDLFVDIQDGKILMALLEVLSGQNLLQEYKPSSHRIFRLNNIAKALKFLEDSNVKLVS 85

                          90       100
                  ....*....|....*....|....*.
gi 2048774911 102 TSAKDIVEGNLKSIMRLVLALAAHFK 127
Cdd:cd21191    86 IDAAEIADGNPSLVLGLIWNIILFFQ 111

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 2048774911  22 QLQAYVAWVNAQLKKRPSvKPVQDLRQDLRDGVILAYLIEIVAGEKLsgVQLSPSNQQEMKSNVERVLQFVASKNIRMHQ 101
Cdd:cd21231     7 QKKTFTKWINAQFAKFGK-PPIEDLFTDLQDGRRLLELLEGLTGQKL--VKEKGSTRVHALNNVNKALQVLQKNNVDLVN 83

                          90       100
                  ....*....|....*....|....*.
gi 2048774911 102 TSAKDIVEGNLKSIMRLVLALAAHFK 127
Cdd:cd21231    84 IGSADIVDGNHKLTLGLIWSIILHWQ 109

first calponin homology (CH) domain found in utrophin and similar proteins; 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 link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, utrophin has 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, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs), and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs. This model corresponds to the first CH domain.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048774911  22 QLQAYVAWVNAQLKK--RPsvkPVQDLRQDLRDGVILAYLIEIVAGEKLSgvQLSPSNQQEMKSNVERVLQFVASKNIRM 99
Cdd:cd21232     3 QKKTFTKWINARFSKsgKP---PIKDMFTDLRDGRKLLDLLEGLTGKSLP--KERGSTRVHALNNVNRVLQVLHQNNVEL 77

                          90       100
                  ....*....|....*....|....*...
gi 2048774911 100 HQTSAKDIVEGNLKSIMRLVLALAAHFK 127
Cdd:cd21232    78 VNIGGTDIVDGNHKLTLGLLWSIILHWQ 105

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 2048774911  28 AWVNAQLKKRPSVkpVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLSPSNQQEmKSNVERVLQFVaSKNIRMHQTSAKDI 107
Cdd:cd21221     8 EWINEELADDRIV--VRDLEEDLFDGQVLQALLEKLANEKLEVPEVAQSEEGQ-KQKLAVVLACV-NFLLGLEEDEARWT 83

                          90       100
                  ....*....|....*....|...
gi 2048774911 108 VEG----NLKSIMRLVLALAAHF 126
Cdd:cd21221    84 VDGiynkDLVSILHLLVALAHHY 106

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 2048774911  27 VAWVNAQLKKRPSVkpVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLSPSNQQEmKSNVERVLQFVAS----KNIRMHQT 102
Cdd:cd21304     7 IEWINDELAEQRII--VKDIEEDLYDGQVLQKLLEKLTGVKLEVAEVTQSEVGQ-KQKLRTVLDKINRilnlPRWSQQKW 83

                          90       100
                  ....*....|....*....|....
gi 2048774911 103 SAKDIVEGNLKSIMRLVLALAAHF 126
Cdd:cd21304    84 SVDSIHSKNLVAILHLLVALARHF 107

first calponin homology (CH) domain found in plectin and similar proteins; 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 can also bind muscle proteins such as actin to membrane complexes in muscle. Plectin 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 2048774911  22 QLQAYVAWVNAQLKKrpSVKPVQDLRQDLRDGVILAYLIEIVAGEKLsgvqlsPSNQQEMK----SNVERVLQFVASKNI 97
Cdd:cd21235     7 QKKTFTKWVNKHLIK--AQRHISDLYEDLRDGHNLISLLEVLSGDSL------PREKGRMRfhklQNVQIALDYLRHRQV 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2048774911  98 RMHQTSAKDIVEGNLKSIMRLVLALAAHFKPGSSRTVSQGR 138
Cdd:cd21235    79 KLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 119

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048774911 281 EEQLLEQQEHLEKEMEEAKKMISGLQALLLngslpEDEQERpvalcepgvnpeeqlIIIRSRLDQSMEENQDLKKELLKC 360
Cdd:COG1196   339 LEELEEELEEAEEELEEAEAELAEAEEALL-----EAEAEL---------------AEAEEELEELAEELLEALRAAAEL 398

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048774911 361 KQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLDERNRLLGEYKKDLGQKDRLLQQQQAK 440
Cdd:COG1196   399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2048774911 441 LEDALRKLSDASYQ-----QVDLERELEQKDVLLAHRVKG 475
Cdd:COG1196   479 LAELLEELAEAAARlllllEAEADYEGFLEGVKAALLLAG 518

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048774911  24 QAYVAWVNAQLKKRPSVkpVQDLRQDLRDGVILAYLIEIVAGE--KLSGVQLSPSNQQEMKSNVERVLQFVASKNIRMHQ 101
Cdd:cd21307    19 KAILHFVNKHLGNLGLN--VKDLDSQFADGVILLLLIGQLEGFfiHLSEFFLTPSSTSEMLHNVTLALELLKEGGLLNFP 96

                          90       100
                  ....*....|....*....|....*.
gi 2048774911 102 TSAKDIVEGNLKSIMRLVLALAAHFK 127
Cdd:cd21307    97 VNPEDIVNGDSKATIRVLYCLFSKYK 122

first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A (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 anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-A 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 2048774911  22 QLQAYVAWVNAQLKkrPSVKPVQDLRQDLRDGVILAYLIEIVAGEKL-SGVQLSPSNQQEMKSNVERVLQFVASKNIRMH 100
Cdd:cd21308    21 QQNTFTRWCNEHLK--CVSKRIANLQTDLSDGLRLIALLEVLSQKKMhRKHNQRPTFRQMQLENVSVALEFLDRESIKLV 98

                          90       100
                  ....*....|....*....|....*.
gi 2048774911 101 QTSAKDIVEGNLKSIMRLVLALAAHF 126
Cdd:cd21308    99 SIDSKAIVDGNLKLILGLIWTLILHY 124

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048774911 282 EQLLEQQEHLEKEMEEAKKMISGLQALLlngslpedeQERpvalcepgvnpEEQLIIIRSRLDQSMEENQDLKKELLKCK 361
Cdd:COG1196   235 RELEAELEELEAELEELEAELEELEAEL---------AEL-----------EAELEELRLELEELELELEEAQAEEYELL 294

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048774911 362 QEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLDERNRLLGEYKKDLGQKDRLLQQQQAKL 441
Cdd:COG1196   295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374