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 1958662450  590 FTCDHCQGLIIGRRMNCNVCDDFDLCYGCYAAKKysYGHLPTHSITAH 637
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 1958662450  590 FTCDHCQGLIIGRRMNCNVCDDFDLCYGCYAAKKysYGHLPTHSITAH 637
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 1958662450   540 DISCDGCDEIAPWHRYRCLQCSDMDLCKTCFLGGVKPEGH 579
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 1958662450  542 SCDGC--DEIAPWhRYRCLQCSDMDLCKTCFlggvkPEGHGDDHEM 585
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 1958662450  590 FTCDHCQGLIIGRRMNCNVCDDFDLCYGCYAAKKysYGHLPTHSITAH 637
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 1958662450   588 MEFTCDHCQGLIIGRRMNCNVCDDFDLCYGCYAAKKYSYGH 628
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 1958662450  590 FTCDHCQGLIIGRRMNCNVCDDFDLCYGCYAAkkysyghlPTHsiTAHPMVTI 642
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 1958662450   540 DISCDGCDEIAPWHRYRCLQCSDMDLCKTCFLGGVKPEGH 579
Cdd:smart00291    4 SYSCDTCGKPIVGVRYHCLVCPDYDLCQSCFAKGSAGGEH 43

Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. CREB-binding protein (CBP) is a large multidomain protein that provides binding sites for transcriptional coactivators, the role of the ZZ domain in CBP/p300 is unclear.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1958662450  590 FTCDHCQgLIIGRRMNCNVCDDFDLCYGCYAAKkysyGHlpTHSITAH 637
Cdd:cd02337      1 YTCNECK-HHVETRWHCTVCEDYDLCITCYNTK----NH--PHKMEKL 41

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        40
                   ....*....|....*....|....*....|....*....|....
gi 1958662450  591 TCDHCQGLII-GRRMNCNVCDDFDLCYGCYAAKKysygHLPTHS 633
Cdd:cd02344      2 TCDGCQMFPInGPRFKCRNCDDFDFCENCFKTRK----HNTRHT 41

Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Human potassium channel modulatory factor 1 or FIGC has been shown to possess intrinsic E3 ubiquitin ligase activity and to promote ubiquitination.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1958662450  591 TCDHCQ-GLIIGRRMNCNVCDDFDLCYGCYAAKKYSYGHLPTHSIT 635
Cdd:cd02338      2 SCDGCGkSNFTGRRYKCLICYDYDLCADCYDSGVTTERHLFDHPMQ 47

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 1958662450  542 SCDGC--DEIAPWhRYRCLQCSDMDLCKTCFlggvkPEGHGDDHEM 585
Cdd:pfam00569    6 TCNGCsnDPSIGV-RYHCLRCSDYDLCQSCF-----QTHKGGNHQM 45

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 1958662450  591 TCDHCQGL-IIGRRMNCNVCDDFDLCYGCYAAKKYSYGHLPTH 632
Cdd:cd02345      2 SCSACRKQdISGIRFPCQVCRDYSLCLGCYTKGRETKRHNSLH 44

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

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1958662450  585 MVNMEFTCDHCQGLIIGR-RMNCNVCDDFDLCYGCYAAKKYSYGHLPTH 632
Cdd:COG5114      1 MGGVKIHCDVCFLDMTDLtFIKCNECPAVDLCLPCFVNGIETGVHSPYH 49

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 1958662450  541 ISCDGCdEIAPWH--RYRCLQCSDMDLCKTCF 570
Cdd:cd02344      1 VTCDGC-QMFPINgpRFKCRNCDDFDFCENCF 31