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 442616412 278 NSCAGCRKEHIVGIRFRCQVCRDISLCLPCFAVGFAGGRHEPGHRMCEV 326
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 442616412   46 IMDDLQrDYGNYKYTVYRCASKFVALQKIFHTGKIPYKLVLAILDRHNLSGG-LELMVPPFQLTSLLHDVYFACEKlgHF 124
Cdd:pfam09068   3 LMQELQ-DFNNIRFAAYRTAMKLRALQKRLNLDLVDLWNLIEAFDEHGLNSLeNDLLLSVSELEALLSSIYFALNK--RK 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 442616412  125 NQDANYKLDRATGLLANFFWNVYDP---HSISLLEIRITFILLC 165
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 442616412   276 HSNSCAGCRKeHIVGIRFRCQVCRDISLCLPCFAVGFAGGRHE 318
Cdd:smart00291   3 HSYSCDTCGK-PIVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44

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

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 442616412 280 CAGCRKEHIVGIRFRCQVCRDISLCLPCFAVGFAGGRHEPGH 321
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 442616412  81 PYKLVLAILDRHNLSGGLELMVPPFQLTSLLHDVYFACEKLGHFNQDanykLDRATGLLANFFWNVYDP---HSISLLEI 157
Cdd:cd15901    1 DLSTVLSVFDRHGLSGSQDSVLDCEELETILTELYIKLNKRRPDLID----VPRASDLLLNWLLNLYDRnrtGCIRLLSV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616412 158 RITFILLCKlYSSDHLVGDIFGLLADPkSQIISRYAFEQLLATLSKLLSYLGEAKAYGVHNLPLAMEQCFARCPHGVGGl 237
Cdd:cd15901   77 KIALITLCA-ASLLDKYRYLFGQLADS-SGFISRERLTQFLQDLLQIPDLIGESPAFGGHNVEAAVESCFQLARSRVGV- 153

                        170
                 ....*....|
gi 442616412 238 TEPQFHKLWT 247
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 442616412 278 NSCAGCRKEHIVGIRFRCQVCRDISLCLPCFAVGFAGGRHEPGHRMCEV 326
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 442616412 279 SCAGCRKEhIVGIRFRCQVCRDISLCLPCFAVGFagGRHEPGHRMCE 325
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 442616412 280 CAGCRKEHIVGIRFRCQVCRDISLCLPCfavgFAGGRHEPGHR 322
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 442616412 279 SCAGCRKEHIVGIRFRCQVCRDISLCLPCFAVGFAGGRHEPGHRMCE 325
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 442616412 279 SCAGCrKEHIVGIRFRCQVCRDISLCLPCfavgFAGGRHePGHRM 323
Cdd:cd02340    2 ICDGC-QGPIVGVRYKCLVCPDYDLCESC----EAKGVH-PEHAM 40

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 442616412 279 SCAGCRKEHIVGIRFRCQVCRDISLCLPCFAVGFAGGRH 317
Cdd:cd02344    2 TCDGCQMFPINGPRFKCRNCDDFDFCENCFKTRKHNTRH 40

Zinc finger, ZZ type. Zinc finger present in ZZZ3 (ZZ finger containing 3) and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 442616412 280 CAGCRKEHIVGIRFRCQVC--RDISLCLPCFavgFAGGRHEPGHRM 323
Cdd:cd02341    3 CDSCGIEPIPGTRYHCSECddGDFDLCQDCV---VKGESHQEDHWL 45