Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Dah (discontinuous actin hexagon) is a membrane associated protein essential for cortical furrow formation in Drosophila.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 17530949 281 NSCAGCRKEHIVGIRFRCQVCRDISLCLPCFAVGFAGGRHEPGHRMCEV 329
Cdd:cd02345   1 LSCSACRKQDISGIRFPCQVCRDYSLCLGCYTKGRETKRHNSLHIMYEL 49

EF hand; Members of this family adopt a helix-loop-helix motif, as per other EF hand domains. However, since they do not contain the canonical pattern of calcium binding residues found in many EF hand domains, they do not bind calcium ions. The main function of this domain is the provision of specificity in beta-dystroglycan recognition, though in dystrophin it serves an additional role: stabilization of the WW domain (pfam00397), enhancing dystroglycan binding.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17530949    46 IMDDLQrDYGNYKYTVYRCASKFVALQKIFHTGKIPYKLVLAILDRHNLSGG-LELMVPPFQLTSLLHDVYFACEKlgHF 124
Cdd:pfam09068   3 LMQELQ-DFNNIRFAAYRTAMKLRALQKRLNLDLVDLWNLIEAFDEHGLNSLeNDLLLSVSELEALLSSIYFALNK--RK 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 17530949   125 NQDANYKLDRATGLLANFFWNVYDPQRRHSISLLEIRITFILLC 168
Cdd:pfam09068  80 PTTHQINVPLSVDLLLNWLLNVYDPERTGKIRVLSFKVALATLC 123

Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain present in dystrophin-like proteins, and CREB-binding protein/p300 homologues. The ZZ in dystrophin appears to bind calmodulin. A missense mutation of one of the conserved cysteines in dystrophin results in a patient with Duchenne muscular dystrophy.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 17530949    279 HSNSCAGCRKeHIVGIRFRCQVCRDISLCLPCFAVGFAGGRHE 321
Cdd:smart00291   3 HSYSCDTCGK-PIVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44

Histone acetyltransferase complex SAGA/ADA, subunit ADA2 [Chromatin structure and dynamics];

                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 17530949 283 CAGCRKEHIVGIRFRCQVCRDISLCLPCFAVGFAGGRHEPGH 324
Cdd:COG5114   8 CDVCFLDMTDLTFIKCNECPAVDLCLPCFVNGIETGVHSPYH 49

EF-hand-like motif found in the dystrophin/dystrobrevin/dystrotelin family; The dystrophin/dystrobrevin/dystrotelin family 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. Dystrophin is the founder member of this family. It is a sub-membrane cytoskeletal protein associated with the inner surface membrane. Dystrophin and its close paralog utrophin have a large N-terminal extension of actin-binding CH domains, up to 24 spectrin repeats, and a WW domain. Its further paralog, dystrophin-related protein 2 (DRP-2), retains only two of the spectrin repeats. Dystrophin, utrophin or DRP2 can form the core of a membrane-bound complex consisting of dystroglycan, sarcoglycans and syntrophins, known as the dystrophin-glycoprotein complex (DGC) that plays an important role in brain development and disease, as well as in the prevention of muscle damage. Dystrobrevins, including alpha- and beta-dystrobrevin, lack the large N-terminal extension found in dystrophin, but alpha-dystrobrevin has a characteristic C-terminal extension. Dystrobrevins are part of the DGC. They physically associate with members of the dystrophin family and with the syntrophins through their homologous C-terminal coiled coil motifs. In contrast, dystrotelins lack both the large N-terminal extension found in dystrophin and the obvious syntrophin-binding sites (SBSs). Dystrotelins are not critical for mammalian development. They may be involved in other forms of cytokinesis. Moreover, dystrotelin is unable to heterodimerize with members of the dystrophin or dystrobrevin families, or to homodimerize.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17530949  81 PYKLVLAILDRHNLSGGLELMVPPFQLTSLLHDVYFACEKLGHFNQDanykLDRATGLLANFFWNVYDPQRRHSISLLEI 160
Cdd:cd15901   1 DLSTVLSVFDRHGLSGSQDSVLDCEELETILTELYIKLNKRRPDLID----VPRASDLLLNWLLNLYDRNRTGCIRLLSV 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17530949 161 RITFILLCKlYSSDHLVGDIFGLLADPkSQIISRYAFEQLLATLSKLLSYLGEAKAYGVHNLPLAMEQCFARCPHGVGGl 240
Cdd:cd15901  77 KIALITLCA-ASLLDKYRYLFGQLADS-SGFISRERLTQFLQDLLQIPDLIGESPAFGGHNVEAAVESCFQLARSRVGV- 153

                       170
                ....*....|
gi 17530949 241 TEPQFHKLWT 250
Cdd:cd15901 154 SEDTFLSWLL 163

Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Dah (discontinuous actin hexagon) is a membrane associated protein essential for cortical furrow formation in Drosophila.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 17530949 281 NSCAGCRKEHIVGIRFRCQVCRDISLCLPCFAVGFAGGRHEPGHRMCEV 329
Cdd:cd02345   1 LSCSACRKQDISGIRFPCQVCRDYSLCLGCYTKGRETKRHNSLHIMYEL 49

Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ZZ motif coordinates one or two zinc ions and most likely participates in ligand binding or molecular scaffolding. Many proteins containing ZZ motifs have other zinc-binding motifs as well, and the majority serve as scaffolds in pathways involving acetyltransferase, protein kinase, or ubiqitin-related activity. ZZ proteins can be grouped into the following functional classes: chromatin modifying, cytoskeletal scaffolding, ubiquitin binding or conjugating, and membrane receptor or ion-channel modifying proteins.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 17530949 282 SCAGCRKEhIVGIRFRCQVCRDISLCLPCFAVGFagGRHEPGHRMCE 328
Cdd:cd02249   2 SCDGCLKP-IVGVRYHCLVCEDFDLCSSCYAKGK--KGHPPDHSFTE 45

Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Mind bomb is an E3 ubiqitin ligase that has been shown to regulate signaling by the Notch ligand Delta in Drosophila melanogaster.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 17530949 283 CAGCRKEHIVGIRFRCQVCRDISLCLPCfavgFAGGRHEPGHR 325
Cdd:cd02339   3 CDTCRKQGIIGIRWKCAECPNYDLCTTC----YHGDKHDLEHR 41

Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Dystrophin attaches actin filaments to an integral membrane glycoprotein complex in muscle cells. The ZZ domain in dystrophin has been shown to be essential for binding to the membrane protein beta-dystroglycan.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 17530949 282 SCAGCRKEHIVGIRFRCQVCRDISLCLPCFAVGFAGGRHEPGHRMCE 328
Cdd:cd02334   2 KCNICKEFPITGFRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHPMKE 48

Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Drosophila ref(2)P appears to control the multiplication of sigma rhabdovirus. NBR1 (Next to BRCA1 gene 1 protein) interacts with fasciculation and elongation protein zeta-1 (FEZ1) and calcium and integrin binding protein (CIB), and may function in cell signalling pathways. Sequestosome 1 is a phosphotyrosine independent ligand for the Lck SH2 domain and binds noncovalently to ubiquitin via its UBA domain.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 17530949 282 SCAGCrKEHIVGIRFRCQVCRDISLCLPCfavgFAGGRHePGHRM 326
Cdd:cd02340   2 ICDGC-QGPIVGVRYKCLVCPDYDLCESC----EAKGVH-PEHAM 40

EF-hand-like motif found in the dystrophins subfamily; This dystrophins subfamily includes dystrophin and its two paralogs, utrophin and DRP-2. Dystrophin is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscle. 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 also involves in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also termed dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homologue that increases dystrophic muscle function and reduces pathology. It is broadly expressed at both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with the dystroglycans (DGs) and the sarcoglycan-dystroglycans, sarcoglycans and sarcospan (SG-SSPN) subcomplex. 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. DRP-2 is mainly expressed in the vertebrate central nervous system (CNS). It is associated with brain membrane fractions and highly enriched in the postsynaptic density. DRP-2 plays a role in the organization of central cholinergic synapses. It interacts with dystroglycan and L-Periaxin to form a transmembrane complex, which plays a role in Schwann cell-basal lamina interactions and in the regulation of the terminal stages of myelination. The dystrophins subfamily has been characterized by a compact cluster of domains comprising a WW domain, four EF-hand-like motifs and a ZZ-domain, followed by two syntrophin binding sites (SBSs) and a looser region with two coiled-coils.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17530949  88 ILDRHNLSGGLELMVPPFQLTSLLHDVYFACEKLGHFNQDANYKLDratgLLANFFWNVYDPQRRHSISLLEIRITFILL 167
Cdd:cd16242   8 AFDQHGLRAQNDKLIDVPDMITCLTTIYEALEEEHPTLVNVPLCVD----LCLNWLLNVYDSGRSGKIRVLSFKVGLVLL 83

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17530949 168 CKlyssDHLVGD---IFGLLADPKSQIISRyafeQLLATLSKLL---SYLGEAKAYGVHNLPLAMEQCF 230
Cdd:cd16242  84 CN----AHLEEKyryLFSLIADPNGCVDQR----RLGLLLHDCIqipRQLGEVAAFGGSNIEPSVRSCF 144

Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential E3 ubiquitin protein ligase and/or guanine nucleotide exchange factor. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding.

                        10        20        30
                ....*....|....*....|....*....|....*....
gi 17530949 282 SCAGCRKEHIVGIRFRCQVCRDISLCLPCFAVGFAGGRH 320
Cdd:cd02344   2 TCDGCQMFPINGPRFKCRNCDDFDFCENCFKTRKHNTRH 40

Zinc finger, ZZ type. Zinc finger present in proteins with an EF_hand motif. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 17530949 282 SCAGCrKEHIVGIRFRCQVCRDISLCLPCFAVGFAGGRHEPGHRM 326
Cdd:cd02343   2 SCDGC-DEIAPWHRYRCLQCTDMDLCKTCFLGGVKPEGHEDDHEM 45