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 221378609 567 TLLRWISAQLHSYQFIpELKEASDVFRNGRVLCALINRYRPDLIDYAATKDMSPVECNELSFAVLERELHIDRVMSAKQS 646
Cdd:cd22198    4 ELLSWCQEQTEGYRGV-KVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQEM 82

                         90       100
                 ....*....|....*....|...
gi 221378609 647 LDLTELESRIWLNYLDQICDLFR 669
Cdd:cd22198   83 ASLAVPDKLSMVSYLSQFYEAFK 105

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 221378609 567 TLLRWISAQLHSYQFIpELKEASDVFRNGRVLCALINRYRPDLIDYAATKDMSPVECNELSFAVLERELHIDRVMSAKQS 646
Cdd:cd22198    4 ELLSWCQEQTEGYRGV-KVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQEM 82

                         90       100
                 ....*....|....*....|...
gi 221378609 647 LDLTELESRIWLNYLDQICDLFR 669
Cdd:cd22198   83 ASLAVPDKLSMVSYLSQFYEAFK 105

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 221378609 128 TRVLVIGAGPCGLRTAIEAQLLGAKVVVLEKRDRI-TRNNVLHLWPFVITDLRNLGAK-------------KFYGKFCAG 193
Cdd:COG0654    4 TDVLIVGGGPAGLALALALARAGIRVTVVERAPPPrPDGRGIALSPRSLELLRRLGLWdrllargapirgiRVRDGSDGR 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221378609 194 SIDHISI-------------RQLQCMLLKVALLLGVEIHEGVSFDhAVEPSGDGggwrAAVTPADHpvSHYEFDVLIGAD 260
Cdd:COG0654   84 VLARFDAaetglpaglvvprADLERALLEAARALGVELRFGTEVT-GLEQDADG----VTVTLADG--RTLRADLVVGAD 156

                 ...
gi 221378609 261 GKR 263
Cdd:COG0654  157 GAR 159

putative bacillithiol system oxidoreductase, YpdA family; Members of this protein family, including YpdA from Bacillus subtilis, are apparent oxidoreductases present only in species with an active bacillithiol system. They have been suggested actually to be thiol disulfide oxidoreductases (TDOR), although the evidence is incomplete. [Unknown function, Enzymes of unknown specificity]

                          10        20
                  ....*....|....*....|....*....
gi 221378609  130 VLVIGAGPCGLRTAIEAQLLGAKVVVLEK 158
Cdd:TIGR04018   2 VIIIGAGPCGLACAIEAQKAGLSYLIIEK 30

FAD binding domain; This family includes members that bind FAD. This family includes the flavoprotein subunits from succinate and fumarate dehydrogenase, aspartate oxidase and the alpha subunit of adenylylsulphate reductase.

                          10        20
                  ....*....|....*....|....*....
gi 221378609  130 VLVIGAGPCGLRTAIEAQLLGAKVVVLEK 158
Cdd:pfam00890   2 VLVIGGGLAGLAAALAAAEAGLKVAVVEK 30

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

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 221378609 568 LLRWISAQLHSYQFIPELKEASDVFRNGRVLCALINRYRPDLIDY 612
Cdd:COG5069  130 LLLWCDEDTGGYKPEVDTFDFFRSWRDGLAFSALIHDSRPDTLDP 174

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 221378609 567 TLLRWISAQLHSYQFIpELKEASDVFRNGRVLCALINRYRPDLIDYAATKDMSPVECNELSFAVLERELHIDRVMSAKQS 646
Cdd:cd22198    4 ELLSWCQEQTEGYRGV-KVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQEM 82

                         90       100
                 ....*....|....*....|...
gi 221378609 647 LDLTELESRIWLNYLDQICDLFR 669
Cdd:cd22198   83 ASLAVPDKLSMVSYLSQFYEAFK 105

calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a nuclear [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-2 acts as a key regulator of the serum response factor (SRF) signaling pathway elicited by nerve growth factor and serum. It mediates oxidation and subsequent depolymerization of nuclear actin, leading to the increased MKL1/MRTF-A presence in the nucleus, promoting SRF:MKL1/MRTF-A-dependent gene transcription. MICAL-2 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 221378609 558 SGDLLPQgaTLLRWISAQLHSYQFIpELKEASDVFRNGRVLCALINRYRPDLIDYAATKDMSPVECNELSFAVLERELHI 637
Cdd:cd21250    1 ESDIRPN--KLLTWCQKQTEGYQNV-NVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGI 77

                         90       100       110
                 ....*....|....*....|....*....|...
gi 221378609 638 DRVMSAKQSLDLTELESRIWLNYLDQICDLFRG 670
Cdd:cd21250   78 PPVTTGKEMASAEEPDKLSMVMYLSKFYELFRG 110

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221378609 568 LLRWISAQLHSYQFIpELKEASDVFRNGRVLCALINRYRPDLIDYAATKDMSPVECNELSFAVLERELHIDRVMSAKQSL 647
Cdd:cd21197    5 LLRWCRRQCEGYPGV-NITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAEDMV 83

                         90       100
                 ....*....|....*....|..
gi 221378609 648 DLTELESRIWLNYLDQICDLFR 669
Cdd:cd21197   84 TMHVPDRLSIITYVSQYYNHFR 105

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221378609 568 LLRWISAQlhsyqfIPELKE---ASDvFRNGRVLCALINRYRPDLIDYAATKD-MSPVECNELSFAVLERELHIDRVMSA 643
Cdd:cd21184    6 LLEWVNSK------IPEYKVknfTTD-WNDGKALAALVDALKPGLIPDNESLDkENPLENATKAMDIAEEELGIPKIITP 78

                         90
                 ....*....|.
gi 221378609 644 KQ--SLDLTEL 652
Cdd:cd21184   79 EDmvSPNVDEL 89

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221378609 592 FRNGRVLCALINRYRPDLIDYAATKDMSPVECNELSFAVLERELHIDRVMSAKQSLDLTELESRIWLNYLDQICDLFR 669
Cdd:cd21253   29 WRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDAEDMVALKVPDKLSILTYVSQYYNYFH 106

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 221378609 128 TRVLVIGAGPCGLRTAIEAQLLGAKVVVLEKRDRI-TRNNVLHLWPFVITDLRNLGAK-------------KFYGKFCAG 193
Cdd:COG0654    4 TDVLIVGGGPAGLALALALARAGIRVTVVERAPPPrPDGRGIALSPRSLELLRRLGLWdrllargapirgiRVRDGSDGR 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221378609 194 SIDHISI-------------RQLQCMLLKVALLLGVEIHEGVSFDhAVEPSGDGggwrAAVTPADHpvSHYEFDVLIGAD 260
Cdd:COG0654   84 VLARFDAaetglpaglvvprADLERALLEAARALGVELRFGTEVT-GLEQDADG----VTVTLADG--RTLRADLVVGAD 156

                 ...
gi 221378609 261 GKR 263
Cdd:COG0654  157 GAR 159

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 221378609 568 LLRWISAQLHSYQFIpELKEASDVFRNGRVLCALINRYRPDLIDYAATKDMSPVECNELSFAVLERELHIDRVMSAkQSL 647
Cdd:cd21189    6 LLLWARRTTEGYPGV-RVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDP-EDV 83

                         90       100
                 ....*....|....*....|.
gi 221378609 648 DLTELESRIWLNYLDQICDLF 668
Cdd:cd21189   84 DVPEPDEKSIITYVSSLYDVF 104

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
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 221378609   567 TLLRWISAQLHSYQFIPeLKEASDVFRNGRVLCALINRYRPDLIDYAA-TKDMSPVECNE 625
Cdd:smart00033   2 TLLRWVNSLLAEYDKPP-VTNFSSDLKDGVALCALLNSLSPGLVDKKKvAASLSRFKKIE 60

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 221378609 568 LLRWISAQLHSYQFIpELKEASDVFRNGRVLCALINRYRPDLIDYAATKDMSPVECNELSFAVLERELHIDRVMSAkQSL 647
Cdd:cd21194    7 LLLWCQRKTAGYPGV-NIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDA-EDV 84

                         90
                 ....*....|....
gi 221378609 648 DLTELESRIWLNYL 661
Cdd:cd21194   85 DVARPDEKSIMTYV 98

Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and conversion]; Succinate dehydrogenase/fumarate reductase, flavoprotein subunit is part of the Pathway/BioSystem: TCA cycle

                         10        20
                 ....*....|....*....|....*....
gi 221378609 130 VLVIGAGPCGLRTAIEAQLLGAKVVVLEK 158
Cdd:COG1053    6 VVVVGSGGAGLRAALEAAEAGLKVLVLEK 34

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 221378609 566 ATLLRWISAQLHSYQFIpELKEASDVFRNGRVLCALINRYRPDLIDYAATKDMSPVECNELSFAVLErELHIDRVMSAKQ 645
Cdd:cd21255    4 QSLLEWCQEVTAGYRGV-RVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFA-SLGVPRLLEPAD 81

                         90       100
                 ....*....|....*....|...
gi 221378609 646 SLDLTELESRIWLNYLDQICDLF 668
Cdd:cd21255   82 MVLLPIPDKLIVMTYLCQLRAHF 104

putative bacillithiol system oxidoreductase, YpdA family; Members of this protein family, including YpdA from Bacillus subtilis, are apparent oxidoreductases present only in species with an active bacillithiol system. They have been suggested actually to be thiol disulfide oxidoreductases (TDOR), although the evidence is incomplete. [Unknown function, Enzymes of unknown specificity]

                          10        20
                  ....*....|....*....|....*....
gi 221378609  130 VLVIGAGPCGLRTAIEAQLLGAKVVVLEK 158
Cdd:TIGR04018   2 VIIIGAGPCGLACAIEAQKAGLSYLIIEK 30

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221378609 568 LLRWISAQLHSYQFIpELKEASDVFRNGRVLCALINRYRPDLIDYAATkDMSPVECN-ELSFAVLERELHIDRVMSAKQS 646
Cdd:cd21291   15 LLLWCQRKTAGYDEV-DVQDFTTSWTDGLAFCALIHRHRPDLIDYDKL-DKKDHRGNmQLAFDIASKEIGIPQLLDVEDV 92

                         90
                 ....*....|....*..
gi 221378609 647 LDLTELESRIWLNYLDQ 663
Cdd:cd21291   93 CDVAKPDERSIMTYVAY 109

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

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221378609 568 LLRWISAQLHSYQfIPELKEASDVFRNGRVLCALINRYRPDLIDYAATKDMSPVECNELSFAVLERELHIDRVMSA 643
Cdd:cd21226    5 LLAWCRQTTEGYD-GVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEA 79

Monoamine oxidase [Amino acid transport and metabolism];

                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 221378609 126 TGTRVLVIGAGPCGLRTAIEAQLLGAKVVVLEKRDRI 162
Cdd:COG1231    6 RGKDVVIVGAGLAGLAAARELRKAGLDVTVLEARDRV 42

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221378609 568 LLRWISAQLHSYQFIpELKEASDVFRNGRVLCALINRYRPDLIDYAATKDMSPVECNELSFAVLERELHIDRVMSAkQSL 647
Cdd:cd21238    7 LLLWSQRMVEGYQGL-RCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP-EDV 84

                         90
                 ....*....|....*....
gi 221378609 648 DLTELESRIWLNYLDQICD 666
Cdd:cd21238   85 DVPQPDEKSIITYVSSLYD 103

calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 (SMTNL1), also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL1 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 221378609 568 LLRWISAQLHSYQFIpELKEASDVFRNGRVLCALINRYRPDLIDYAATKDMSPVECNELSFAVLERELHIDRVMSAKQSL 647
Cdd:cd21260    6 LLEWCRAKTRGYEHV-DIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEVEDMV 84

                         90
                 ....*....|....*..
gi 221378609 648 DLTELESRIWLNYLDQI 664
Cdd:cd21260   85 RMSVPDSKCVYTYIQEL 101

second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and similar proteins; 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 second CH domain. CH domains are actin filament (F-actin) binding motifs.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221378609 567 TLLRWISAQLHSYQFIpELKEASDVFRNGRVLCALINRYRPDLIDYAATKDMSPVECNELSFAVLERELHIDRVMSAkQS 646
Cdd:cd21244    9 ALLLWAQEQCAKVGSI-SVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPRLLEP-ED 86

                         90
                 ....*....|....*..
gi 221378609 647 LDLTELESRIWLNYLDQ 663
Cdd:cd21244   87 VDVVNPDEKSIMTYVAQ 103

calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221378609 592 FRNGRVLCALINRYRPDLIDYAATKDMSPVECNELSFAVLErELHIDRVMSAKQSLDLTELESRIWLNYLDQICDLFRGE 671
Cdd:cd21254   29 WRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFA-SLGISRLLEPSDMVLLAVPDKLTVMTYLYQIRAHFSGQ 107

FAD binding domain; This family includes members that bind FAD. This family includes the flavoprotein subunits from succinate and fumarate dehydrogenase, aspartate oxidase and the alpha subunit of adenylylsulphate reductase.

                          10        20
                  ....*....|....*....|....*....
gi 221378609  130 VLVIGAGPCGLRTAIEAQLLGAKVVVLEK 158
Cdd:pfam00890   2 VLVIGGGLAGLAAALAAAEAGLKVAVVEK 30

Alcohol dehydrogenases of the MDR family; This group contains members identified as related to zinc-dependent alcohol dehydrogenase and other members of the MDR family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group includes various activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 221378609 114 AAHRVYgKGAACTGTRVLVIGAGPCGLRTAIEAQLLGAKVVVLEKRD 160
Cdd:cd08261  148 GAHAVR-RAGVTAGDTVLVVGAGPIGLGVIQVAKARGARVIVVDIDD 193

dihydropyrimidine dehydrogenase subunit A; Provisional

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 221378609 112 ARAAHRVYGKGAACTGTRVLVIGAGPCGLRTAIEAQLLGAKVVVLEKRDRI 162
Cdd:PRK11749 125 AMETGWVLFKRAPKTGKKVAVIGAGPAGLTAAHRLARKGYDVTIFEARDKA 175

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221378609 567 TLLRWISAQLHSYQFIpELKEASDVFRNGRVLCALINRYRPDLIDYAATKDMSPVECNELSFAVLERELHIDRVM 641
Cdd:cd21187    4 TLLAWCRQSTRGYEQV-DVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLL 77

Si-specific NAD(P)(+) transhydrogenase;

                         10        20        30
                 ....*....|....*....|....*....|...
gi 221378609 130 VLVIGAGPCGLRTAIEAQLLGAKVVVLEKRDRI 162
Cdd:PRK05249   8 LVVIGSGPAGEGAAMQAAKLGKRVAVIERYRNV 40

NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport and metabolism, General function prediction only]; NADPH-dependent glutamate synthase beta chain or related oxidoreductase is part of the Pathway/BioSystem: Glutamine biosynthesis

                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 221378609 126 TGTRVLVIGAGPCGLRTAieAQL--LGAKVVVLEKRDRI 162
Cdd:COG0493  120 TGKKVAVVGSGPAGLAAA--YQLarAGHEVTVFEALDKP 156

second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and similar proteins; 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 second CH domain. CH domains are actin filament (F-actin) binding motifs.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221378609 567 TLLRWISAQLhSYQFIPELKEASDVFRNGRVLCALINRYRPDLIDYAATKDMSPVECNELSFAVLERELHIDRVMSAK 644
Cdd:cd21243    9 ALLKWVQNAA-AKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPRLLDPE 85

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

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 221378609 568 LLRWISAQLHSYQFIPELKEASDVFRNGRVLCALINRYRPDLIDY 612
Cdd:COG5069  130 LLLWCDEDTGGYKPEVDTFDFFRSWRDGLAFSALIHDSRPDTLDP 174

FAD binding domain; This domain is involved in FAD binding in a number of enzymes.

                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 221378609  128 TRVLVIGAGPCGLRTAIEAQLLGAKVVVLEKRDRITRN 165
Cdd:pfam01494   2 TDVLIVGGGPAGLMLALLLARAGVRVVLVERHATTSVL 39

Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.

                          10        20        30
                  ....*....|....*....|....*....|..
gi 221378609  128 TRVLVIGAGPCGLRTAIEAQLLGAKVVVLEKR 159
Cdd:pfam07992   1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIEDE 32

Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];

                         10        20        30
                 ....*....|....*....|....*....|....
gi 221378609 129 RVLVIGAGPCGLRTAIEAQLLGAKVVVLEKRDRI 162
Cdd:COG1233    5 DVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTP 38

NADH-dependent fumarate reductase; Provisional

                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 221378609  129 RVLVIGAGPCGLRTAIEAQLLGAKVVVLEKRDRITRN 165
Cdd:PTZ00306  411 RVIVVGGGLAGCSAAIEAASCGAQVILLEKEAKLGGN 447

putative succinate dehydrogenase; Reviewed

                         10        20        30
                 ....*....|....*....|....*....|.
gi 221378609 130 VLVIGAGPCGLRTAIEAQLLGAKVVVLEKRD 160
Cdd:PRK12842  12 VLVIGSGAGGLSAAITARKLGLDVVVLEKEP 42

second 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. The model corresponds to the second CH domain.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221378609 568 LLRWISAQLHSYQFIPELKEASDvFRNGRVLCALINRYRPDLIDYAAT-KDMSPVECNELSFAVLERELHIDRVM 641
Cdd:cd21233    5 LLSWVRQSTRNYPQVNVINFTSS-WSDGLAFNALIHSHRPDLFDWNSVvSQQSATERLDHAFNIARQHLGIEKLL 78

Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and metabolism, General function prediction only]; Threonine dehydrogenase or related Zn-dependent dehydrogenase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway

                         10        20        30
                 ....*....|....*....|....*....|....*
gi 221378609 127 GTRVLVIGAGPCGLRTAIEAQLLGA-KVVVLEKRD 160
Cdd:COG1063  162 GDTVLVIGAGPIGLLAALAARLAGAaRVIVVDRNP 196

hypothetical protein; Provisional

                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 221378609 128 TRVLVIGAGPCGLRTAIEAQLLGAKVVVLEKRDRITRN 165
Cdd:PRK06126   8 TPVLIVGGGPVGLALALDLGRRGVDSILVERKDGTAFN 45