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 568972440  444 FTCDHCQGLIIGRRMNCNVCDDFDLCYGCYTAKKysYGHLPTHSITAH 491
Cdd:cd02249     1 YSCDGCLKPIVGVRYHCLVCEDFDLCSSCYAKGK--KGHPPDHSFTEI 46

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 568972440  444 FTCDHCQGLIIGRRMNCNVCDDFDLCYGCYTAKKysYGHLPTHSITAH 491
Cdd:cd02249     1 YSCDGCLKPIVGVRYHCLVCEDFDLCSSCYAKGK--KGHPPDHSFTEI 46

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 568972440    394 DISCDGCDEIAPWHRYRCLQCSDMDLCKTCFLGGVKPEGH 433
Cdd:smart00291    4 SYSCDTCGKPIVGVRYHCLVCPDYDLCQSCFAKGSAGGEH 43

Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds calmodulin. Putative zinc finger; binding not yet shown. Four to six cysteine residues in its sequence are responsible for coordinating zinc ions, to reinforce the structure.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 568972440   396 SCDGC--DEIAPWhRYRCLQCSDMDLCKTCFlggvkPEGHGDDHEM 439
Cdd:pfam00569    6 TCNGCsnDPSIGV-RYHCLRCSDYDLCQSCF-----QTHKGGNHQM 45

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 568972440  444 FTCDHCQGLIIGRRMNCNVCDDFDLCYGCYTAKKysYGHLPTHSITAH 491
Cdd:cd02249     1 YSCDGCLKPIVGVRYHCLVCEDFDLCSSCYAKGK--KGHPPDHSFTEI 46

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 568972440    442 MEFTCDHCQGLIIGRRMNCNVCDDFDLCYGCYTAKKYSYGH 482
Cdd:smart00291    3 HSYSCDTCGKPIVGVRYHCLVCPDYDLCQSCFAKGSAGGEH 43

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        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568972440  444 FTCDHCQGLIIGRRMNCNVCDDFDLCYGCYTAkkysyghlPTHsiTAHPMVTI 496
Cdd:cd02340     1 VICDGCQGPIVGVRYKCLVCPDYDLCESCEAK--------GVH--PEHAMLKI 43

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 568972440    394 DISCDGCDEIAPWHRYRCLQCSDMDLCKTCFLGGVKPEGH 433
Cdd:smart00291    4 SYSCDTCGKPIVGVRYHCLVCPDYDLCQSCFAKGSAGGEH 43

Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, 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 568972440  444 FTCDHCQGLIIGR-RMNCNVCDDFDLCYGCYTAKKYSYGHLPTHS 487
Cdd:cd02335     1 YHCDYCSKDITGTiRIKCAECPDFDLCLECFSAGAEIGKHRNDHN 45

Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds calmodulin. Putative zinc finger; binding not yet shown. Four to six cysteine residues in its sequence are responsible for coordinating zinc ions, to reinforce the structure.

                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 568972440   442 MEFTCDHCQ-GLIIGRRMNCNVCDDFDLCYGCYTAKKY 478
Cdd:pfam00569    3 KVYTCNGCSnDPSIGVRYHCLRCSDYDLCQSCFQTHKG 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 568972440  445 TCDHCQGLII-GRRMNCNVCDDFDLCYGCYTAKKYSYGH 482
Cdd:cd02344     2 TCDGCQMFPInGPRFKCRNCDDFDFCENCFKTRKHNTRH 40

Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds calmodulin. Putative zinc finger; binding not yet shown. Four to six cysteine residues in its sequence are responsible for coordinating zinc ions, to reinforce the structure.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 568972440   396 SCDGC--DEIAPWhRYRCLQCSDMDLCKTCFlggvkPEGHGDDHEM 439
Cdd:pfam00569    6 TCNGCsnDPSIGV-RYHCLRCSDYDLCQSCF-----QTHKGGNHQM 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
                  ....*....|....*....|....*....|....*...
gi 568972440  446 CDHCQGL-IIGRRMNCNVCDDFDLCYGCYTAKKYSYGH 482
Cdd:cd02339     3 CDTCRKQgIIGIRWKCAECPNYDLCTTCYHGDKHDLEH 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 568972440  395 ISCDGCD-EIAPWHRYRCLQCS--DMDLCKTCFlggVKPEGHGDDHEMV 440
Cdd:cd02341     1 FKCDSCGiEPIPGTRYHCSECDdgDFDLCQDCV---VKGESHQEDHWLV 46

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 568972440  395 ISCDGCDE--IAPWhRYRCLQCSDMDLCKTCFlggvkpegHGDDHEM 439
Cdd:cd02339     1 IICDTCRKqgIIGI-RWKCAECPNYDLCTTCY--------HGDKHDL 38