calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of the molecule interacting with CasL protein (MICAL) and EH domain-binding protein (EHBP) families. MICAL is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). 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. EHBP proteins contain a single CH domain. CH domains are actin filament (F-actin) binding motifs.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694515167  521 YDELLSWCQKQTAGYRNVKVTDLTHSWRSGLALCALIHHFRPDLIDFDSLDQGAAARNNQLAFDVAEQELGILPVLTGAE 600
Cdd:cd22198      2 PEELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQE 81

                           90       100
                   ....*....|....*....|....
gi 1694515167  601 MAAVSEPDRLGLVTYLSQFYEAFR 624
Cdd:cd22198     82 MASLAVPDKLSMVSYLSQFYEAFK 105

The LIM domain of Mical (molecule interacting with CasL); The LIM domain of Mical (molecule interacting with CasL): MICAL is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semapho-rin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM domain and calporin homology domain are known for interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein monooxygenase (MO) is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. In addition, MICAL was characterized to interact with Rab13 and Rab8 to coordinate the assembly of tight junctions and adherens junctions in epithelial cells. Thus, MICAL was also named junctional Rab13-binding protein (JRAB). As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1694515167  725 CYFCGQRVYIVERMSANGHFFHRGCFRCHQCGATLRLGNFAFDEGAGQFYCTLHY 779
Cdd:cd09439      1 CYFCKKRVYVMERLSAEGLFFHRSCFKCSYCGTTLRLGAYAFDRDDGKFYCKPHF 55

Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a Rossmann-fold NAD(P)H/NAD(P)(+) binding (NADB) domain. The NADB domain is found in numerous dehydrogenases of metabolic pathways such as glycolysis, and many other redox enzymes. NAD binding involves numerous hydrogen-bonds and van der Waals contacts, in particular H-bonding of residues in a turn between the first strand and the subsequent helix of the Rossmann-fold topology. Characteristically, this turn exhibits a consensus binding pattern similar to GXGXXG, in which the first 2 glycines participate in NAD(P)-binding, and the third facilitates close packing of the helix to the beta-strand. Typically, proteins in this family contain a second domain in addition to the NADB domain, which is responsible for specifically binding a substrate and catalyzing a particular enzymatic reaction.

                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1694515167   90 TKCLVIGAGPCGLRTAIELAFLGAEVVVVEKRDTFSRN 127
Cdd:pfam01494    2 TDVLIVGGGPAGLMLALLLARAGVRVVLVERHATTSVL 39

2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694515167   88 SNTKCLVIGAGPCGLRTAIELAFLGAEVVVVEKRDTFS---RNNVLHLWPFTILD-------LRALGAKKYYGRFCSGSL 157
Cdd:COG0654      2 MRTDVLIVGGGPAGLALALALARAGIRVTVVERAPPPRpdgRGIALSPRSLELLRrlglwdrLLARGAPIRGIRVRDGSD 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1694515167  158 D-----------------HVSIRQLQLILLKAALILGVEVITGVQFKGSLPPPAGAR 197
Cdd:COG0654     82 GrvlarfdaaetglpaglVVPRADLERALLEAARALGVELRFGTEVTGLEQDADGVT 138

calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of the molecule interacting with CasL protein (MICAL) and EH domain-binding protein (EHBP) families. MICAL is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). 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. EHBP proteins contain a single CH domain. CH domains are actin filament (F-actin) binding motifs.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694515167  521 YDELLSWCQKQTAGYRNVKVTDLTHSWRSGLALCALIHHFRPDLIDFDSLDQGAAARNNQLAFDVAEQELGILPVLTGAE 600
Cdd:cd22198      2 PEELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQE 81

                           90       100
                   ....*....|....*....|....
gi 1694515167  601 MAAVSEPDRLGLVTYLSQFYEAFR 624
Cdd:cd22198     82 MASLAVPDKLSMVSYLSQFYEAFK 105

The LIM domain of Mical (molecule interacting with CasL); The LIM domain of Mical (molecule interacting with CasL): MICAL is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semapho-rin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM domain and calporin homology domain are known for interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein monooxygenase (MO) is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. In addition, MICAL was characterized to interact with Rab13 and Rab8 to coordinate the assembly of tight junctions and adherens junctions in epithelial cells. Thus, MICAL was also named junctional Rab13-binding protein (JRAB). As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1694515167  725 CYFCGQRVYIVERMSANGHFFHRGCFRCHQCGATLRLGNFAFDEGAGQFYCTLHY 779
Cdd:cd09439      1 CYFCKKRVYVMERLSAEGLFFHRSCFKCSYCGTTLRLGAYAFDRDDGKFYCKPHF 55

Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694515167  500 RGSCEERNERAMFSQKDslgvydELLSWCQKQTAGYRN-VKVTDLTHSWRSGLALCALIHHFRPDLIDFDSLDQGAA--A 576
Cdd:COG5069    112 RLTIATINEEGELTKHI------NLLLWCDEDTGGYKPeVDTFDFFRSWRDGLAFSALIHDSRPDTLDPNVLDLQKKnkA 185

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1694515167  577 RNNQLAFDVAEQELGILPVLTGAEMAAVSEPDRLGLVTYLSQFYEAFR 624
Cdd:COG5069    186 LNNFQAFENANKVIGIARLIGVEDIVNVSIPDERSIMTYVSWYIIRFG 233

Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM domains bind protein partners via tyrosine-containing motifs. LIM domains are found in many key regulators of developmental pathways.

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 1694515167   725 CYFCGQRVY-IVERMSANGHFFHRGCFRCHQCGATLRLGNFAFDEgaGQFYCTLH 778
Cdd:smart00132    2 CAGCGKPIYgTERVLRALGKVWHPECFKCATCGKPLSGDTFFEKD--GKLYCKDC 54

LIM domain; This family represents two copies of the LIM structural domain.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1694515167  725 CYFCGQRVYIVERMSANGHFFHRGCFRCHQCGATLRLGNFAFDEgaGQFYCTLHYC 780
Cdd:pfam00412    1 CAGCNRPIYDRELVRALGKVWHPECFRCAVCGKPLTTGDFYEKD--GKLYCKHDYY 54

hypothetical protein; Provisional

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1694515167   87 CSNTKCLVIGAGPCGLRTAIELAFLGAEVVVVEKRDTFSRN 127
Cdd:PRK06126     5 TSETPVLIVGGGPVGLALALDLGRRGVDSILVERKDGTAFN 45

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694515167 1116 EADVSRGREMKKYETwkmRTLQRRAKEEEMKRFHKAQsIQRRLEEIEERYRQLEEQGVGLELSL-----REDRESGGQSE 1190
Cdd:COG1196    301 EQDIARLEERRRELE---ERLEELEEELAELEEELEE-LEEELEELEEELEEAEEELEEAEAELaeaeeALLEAEAELAE 376

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694515167 1191 MINRWLLLVQERNLLVSEESDLmiAAQELDLEERQSLLEQELRRWMDLDDRLKTPQDKAEEEETLNRMLEVVDQRNALIT 1270
Cdd:COG1196    377 AEEELEELAEELLEALRAAAEL--AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454

                          170
                   ....*....|....
gi 1694515167 1271 YLEEKRLKEITEQL 1284
Cdd:COG1196    455 EEEEEALLELLAEL 468

MAEBL; Provisional

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694515167 1101 KDGANEAVGSTDKTPEADVSRGREMKKYETWKMRTLQRRAKEEEMKRFHKAQsIQRRLEE--IEERYRQLEEQGVGLELS 1178
Cdd:PTZ00121  1533 AKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAE-EAKKAEEarIEEVMKLYEEEKKMKAEE 1611

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1694515167 1179 LREDRESGGQSEMINRWLLLVQERNLLVSEESDLMIAAQELDLEERQSLLEQELRRWMDLDDRLKTPQDKAEEEE 1253
Cdd:PTZ00121  1612 AKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEED 1686

2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694515167   88 SNTKCLVIGAGPCGLRTAIELAFLGAEVVVVEKRDTFS---RNNVLHLWPFTILD-------LRALGAKKYYGRFCSGSL 157
Cdd:COG0654      2 MRTDVLIVGGGPAGLALALALARAGIRVTVVERAPPPRpdgRGIALSPRSLELLRrlglwdrLLARGAPIRGIRVRDGSD 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1694515167  158 D-----------------HVSIRQLQLILLKAALILGVEVITGVQFKGSLPPPAGAR 197
Cdd:COG0654     82 GrvlarfdaaetglpaglVVPRADLERALLEAARALGVELRFGTEVTGLEQDADGVT 138

calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of the molecule interacting with CasL protein (MICAL) and EH domain-binding protein (EHBP) families. MICAL is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). 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. EHBP proteins contain a single CH domain. CH domains are actin filament (F-actin) binding motifs.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694515167  521 YDELLSWCQKQTAGYRNVKVTDLTHSWRSGLALCALIHHFRPDLIDFDSLDQGAAARNNQLAFDVAEQELGILPVLTGAE 600
Cdd:cd22198      2 PEELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQE 81

                           90       100
                   ....*....|....*....|....
gi 1694515167  601 MAAVSEPDRLGLVTYLSQFYEAFR 624
Cdd:cd22198     82 MASLAVPDKLSMVSYLSQFYEAFK 105

calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-3 seems to act as a Rab effector protein and plays a role in vesicle trafficking. It is involved in exocytic vesicle tethering and fusion. MICAL3 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694515167  516 DSLGVYDELLSWCQKQTAGYRNVKVTDLTHSWRSGLALCALIHHFRPDLIDFDSLDQGAAARNNQLAFDVAEQELGILPV 595
Cdd:cd21251      2 ESVARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISPI 81

                           90       100       110
                   ....*....|....*....|....*....|
gi 1694515167  596 LTGAEMAAVSEPDRLGLVTYLSQFYEAFRD 625
Cdd:cd21251     82 MTGKEMASVGEPDKLSMVMYLTQFYEMFKD 111

calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like protein 2 (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 subfamily 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 1694515167  524 LLSWCQKQTAGYRNVKVTDLTHSWRSGLALCALIHHFRPDLIDFDSLDQGAAARNNQLAFDVAEQELGILPVLTGAEMAA 603
Cdd:cd21253      6 LQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDAEDMVA 85

                           90       100
                   ....*....|....*....|.
gi 1694515167  604 VSEPDRLGLVTYLSQFYEAFR 624
Cdd:cd21253     86 LKVPDKLSILTYVSQYYNYFH 106

calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). 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. EHBP1L1 may also act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694515167  523 ELLSWCQKQTAGYRNVKVTDLTHSWRSGLALCALIHHFRPDLIDFDSLDQGAAARNNQLAFDVAEQeLGILPVLTGAEMA 602
Cdd:cd21198      5 DLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAK-LGIPRLLDPADMV 83

                           90       100
                   ....*....|....*....|.
gi 1694515167  603 AVSEPDRLGLVTYLSQFYEAF 623
Cdd:cd21198     84 LLSVPDKLSVMTYLHQIRAHF 104

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 1694515167  524 LLSWCQKQTAGYRNVKVTDLTHSWRSGLALCALIHHFRPDLIDFDSLDQGAAARNNQLAFDVAEQELGILPVLTGAEMAA 603
Cdd:cd21216     15 LLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDVAEKHLDIPKMLDAEDIVN 94

                           90       100
                   ....*....|....*....|
gi 1694515167  604 VSEPDRLGLVTYLSQFYEAF 623
Cdd:cd21216     95 TPRPDERSVMTYVSCYYHAF 114

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694515167  522 DELLSWCQKQTAGYRNVKVTDLTHSWRSGLALCALIHHFRPDLIDFDSLDQGAAARNNQLAFDVAEQELGIlPVLTGAEM 601
Cdd:cd21194      5 DALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGI-AKLLDAED 83

                           90       100
                   ....*....|....*....|..
gi 1694515167  602 AAVSEPDRLGLVTYLSQFYEAF 623
Cdd:cd21194     84 VDVARPDEKSIMTYVASYYHYF 105

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694515167  522 DELLSWCQKQTAGYRNVKVTDLTHSWRSGLALCALIHHFRPDLIDFDSLDQGAAARNNQLAFDVAEQELGILPVLTgAEM 601
Cdd:cd21248      5 DALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLD-PED 83

                           90       100
                   ....*....|....*....|..
gi 1694515167  602 AAVSEPDRLGLVTYLSQFYEAF 623
Cdd:cd21248     84 VNVEQPDEKSIITYVVTYYHYF 105

calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar proteins; EHBP1L1 may act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. 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 1694515167  522 DELLSWCQKQTAGYRNVKVTDLTHSWRSGLALCALIHHFRPDLIDFDSLDQGAAARNNQLAFDVAEQeLGILPVLTGAEM 601
Cdd:cd21255      4 QSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFAS-LGVPRLLEPADM 82

                           90       100
                   ....*....|....*....|..
gi 1694515167  602 AAVSEPDRLGLVTYLSQFYEAF 623
Cdd:cd21255     83 VLLPIPDKLIVMTYLCQLRAHF 104

second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) 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. SPTBN5, also called beta-V spectrin, is a mammalian ortholog of Drosophila beta H spectrin that may play a crucial role as a longer actin-membrane cross-linker or to fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. SPTBN5 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 1694515167  524 LLSWCQKQTAGYRNVKVTDLTHSWRSGLALCALIHHFRPDLIDFDSLDQGAAARNNQLAFDVAEQELGILPVLTgAEMAA 603
Cdd:cd21249      9 LLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLLD-PEDVA 87

                           90       100
                   ....*....|....*....|
gi 1694515167  604 VSEPDRLGLVTYLSQFYEAF 623
Cdd:cd21249     88 VPHPDERSIMTYVSLYYHYF 107

second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) 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. SPTB, also called beta-I spectrin, may be involved in anaemia pathogenesis. SPTB 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 1694515167  522 DELLSWCQKQTAGYRNVKVTDLTHSWRSGLALCALIHHFRPDLIDFDSLDQGAAARNNQLAFDVAEQELGILPVLTgAEM 601
Cdd:cd21319      8 DALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITKLLD-PED 86

                           90       100
                   ....*....|....*....|..
gi 1694515167  602 AAVSEPDRLGLVTYLSQFYEAF 623
Cdd:cd21319     87 VFTENPDEKSIITYVVAFYHYF 108

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694515167  522 DELLSWCQKQTAGYRNVKVTDLTHSWRSGLALCALIHHFRPDLIDFDSLDQGAAARNNQLAFDVAEQELGILPVLTgAEM 601
Cdd:cd21189      4 EALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLD-PED 82

                           90       100
                   ....*....|....*....|..
gi 1694515167  602 AAVSEPDRLGLVTYLSQFYEAF 623
Cdd:cd21189     83 VDVPEPDEKSIITYVSSLYDVF 104

calponin homology (CH) domain found in the cytospin family; The cytospin family includes cytospin-A and cytospin-B. Cytospin-A, also called renal carcinoma antigen NY-REN-22, sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like (SPECC1L) protein, is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-B, also called nuclear structure protein 5 (NSP5), sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion partner to PDGFRB in juvenile myelomonocytic leukemia with translocation t(5;17)(q33;p11.2). Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694515167  524 LLSWCQKQTAGYRNVKVTDLTHSWRSGLALCALIHHFRPDLIDFDSLDQGAAARNNQLAFDVAEqELGILPVLTGAEMAA 603
Cdd:cd21199     13 LLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAE-SVGIPTTLTIDEMVS 91

                           90       100
                   ....*....|....*....|
gi 1694515167  604 VSEPDRLGLVTYLSQFYEAF 623
Cdd:cd21199     92 MERPDWQSVMSYVTAIYKHF 111

second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) 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. SPTBN1, also called beta-II spectrin, fodrin beta chain, or spectrin, non-erythroid beta chain 1, is also 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. SPTBN1 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 1694515167  522 DELLSWCQKQTAGYRNVKVTDLTHSWRSGLALCALIHHFRPDLIDFDSLDQGAAARNNQLAFDVAEQELGILPVLTgAEM 601
Cdd:cd21320      5 DALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLD-PED 83

                           90       100
                   ....*....|....*....|..
gi 1694515167  602 AAVSEPDRLGLVTYLSQFYEAF 623
Cdd:cd21320     84 ISVDHPDEKSIITYVVTYYHYF 105

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694515167  524 LLSWCQKQTAGYRNVKVTDLTHSWRSGLALCALIHHFRPDLIDFDSLDQGAAARNNQLAFDVAEQELGILPVLTgAEMAA 603
Cdd:cd21187      5 LLAWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLD-PEDVN 83

                           90
                   ....*....|....*...
gi 1694515167  604 VSEPDRLGLVTYLSQFYE 621
Cdd:cd21187     84 VEQPDKKSILMYVTSLFQ 101

second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also called alpha-actinin skeletal muscle isoform 3, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN3 is a bundling protein. It is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. 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 1694515167  524 LLSWCQKQTAGYRNVKVTDLTHSWRSGLALCALIHHFRPDLIDFDSLDQGAAARNNQLAFDVAEQELGILPVLTGAEMAA 603
Cdd:cd21289     15 LLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKYLDIPKMLDAEDIVN 94

                           90       100
                   ....*....|....*....|...
gi 1694515167  604 VSEPDRLGLVTYLSQFYEAFRDA 626
Cdd:cd21289     95 TPKPDEKAIMTYVSCFYHAFAGA 117