'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric DNA tandem repeatsas part of the capping complex. Binding is sequence dependent for repeats which contain the G/C rich motif [C2-3 A (CA)1-6]. The domain is also found in regulatory transcriptional repressor complexes where it also binds DNA.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1774222124 654 WTVEEQKKLEQLLIKYPPeevesRRWQKIADELGNRTAKQVASRVQKYF 702
Cdd:cd00167     2 WTEEEDELLLEAVKKYGK-----NNWEKIAKELPGRTPKQCRERWRNLL 45

'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric DNA tandem repeatsas part of the capping complex. Binding is sequence dependent for repeats which contain the G/C rich motif [C2-3 A (CA)1-6]. The domain is also found in regulatory transcriptional repressor complexes where it also binds DNA.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1774222124 654 WTVEEQKKLEQLLIKYPPeevesRRWQKIADELGNRTAKQVASRVQKYF 702
Cdd:cd00167     2 WTEEEDELLLEAVKKYGK-----NNWEKIAKELPGRTPKQCRERWRNLL 45

SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1774222124  654 WTVEEQKKLEQLLIKYPPeevesRRWQKIADELGNRTAKQVASRVQKYFIK 704
Cdd:smart00717   4 WTEEEDELLIELVKKYGK-----NNWEKIAKELPGRTAEQCRERWRNLLKP 49

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
                   ....*....|....*....|....*....|....*.
gi 1774222124  817 HVGFKCDNCGiEPIQGVRWHCQDCPpemSLDFCDSC 852
Cdd:smart00291   2 HHSYSCDTCG-KPIVGVRYHCLVCP---DYDLCQSC 33

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        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1774222124 820 FKCDNCGIePIQGVRWHCQDCPpemsldFCDSCSDCLHE-TDIHKEDHQLEPI 871
Cdd:cd02249     1 YSCDGCLK-PIVGVRYHCLVCE------DFDLCSSCYAKgKKGHPPDHSFTEI 46

Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, as well as the SANT domain family.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1774222124 654 WTVEEQKKLEQLLIKYPpeevesRRWQKIADELGNRTAKQVASRVQKYF 702
Cdd:pfam00249   4 WTPEEDELLLEAVEKLG------NRWKKIAKLLPGRTDNQCKNRWQNYL 46

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 1774222124 817 HVGFKCDNCGIEPIQGVRWHCQDCPpemSLDFCDSC 852
Cdd:pfam00569   2 HKVYTCNGCSNDPSIGVRYHCLRCS---DYDLCQSC 34

B-box-type 1 zinc finger (Bbox1); The B-box-type zinc finger is a short zinc binding domain of around 40 amino acid residues in length. It has been found in transcription factors, ribonucleoproteins and proto-oncoproteins, such as in TRIM (tripartite motif) proteins that consist of an N-terminal RING finger (originally called an A-box), followed by 1-2 B-box domains and a coiled-coil domain (also called RBCC for Ring, B-box, Coiled-Coil). The B-box-type zinc finger often presents in combination with other motifs, like RING zinc finger, NHL motif, coiled-coil or RFP domain, in functionally unrelated proteins, most likely mediating protein-protein interactions. Based on different consensus sequences and the spacing of the 7-8 zinc-binding residues, the B-box-type zinc fingers can be divided into two groups, type 1 (Bbox1: C6H2) and type 2 (Bbox2: CHC3H2). This family corresponds to the type 1 B-box (Bbox1).

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1774222124 821 KCDNCGIEPiqgVRWHCQDCppemSLDFCDSCSDCLHETDIHKEDHQLEPI 871
Cdd:cd19757     1 LCDECEERE---ATVYCLEC----EEFLCDDCSDAIHRRGKLTRSHKLVPL 44

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 1774222124 822 CDNCGIEPIQGVRWHCQDCPpemSLDFCDSCSDCLHETDIHKEDHQLE 869
Cdd:cd02338     3 CDGCGKSNFTGRRYKCLICY---DYDLCADCYDSGVTTERHLFDHPMQ 47

Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, as well as the SANT domain family.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1774222124 654 WTVEEQKKLEQLLIKYppeeveSRRWQKIADELGNRTAKQVASR 697
Cdd:pfam13921   1 WTEEEDEKLLKLVEKY------GNDWKQIAKELGRRTPKQCFDR 38