'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 2217266321 160 WTVEEQKKLEQLLIKYPPeevesRRWQKIADELGNRTAKQVASRVQKYF 208
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 2217266321 160 WTVEEQKKLEQLLIKYPPeevesRRWQKIADELGNRTAKQVASRVQKYF 208
Cdd:cd00167     2 WTEEEDELLLEAVKKYGK-----NNWEKIAKELPGRTPKQCRERWRNLL 45

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

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2217266321  160 WTVEEQKKLEQLLIKYPPeevesRRWQKIADELGNRTAKQVASRVQKYFIK 210
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 2217266321  323 HVGFKCDNCGiEPIQGVRWHCQDCPpemSLDFCDSC 358
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 2217266321 326 FKCDNCGIePIQGVRWHCQDCPpemsldFCDSCSDCLHE-TDIHKEDHQLEPI 377
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 2217266321 160 WTVEEQKKLEQLLIKYPpeevesRRWQKIADELGNRTAKQVASRVQKYF 208
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 2217266321 323 HVGFKCDNCGIEPIQGVRWHCQDCPpemSLDFCDSC 358
Cdd:pfam00569   2 HKVYTCNGCSNDPSIGVRYHCLRCS---DYDLCQSC 34

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 2217266321  323 HVGFKCDNCGiEPIQGVRWHCQDCPpemSLDFCDSC 358
Cdd:smart00291   2 HHSYSCDTCG-KPIVGVRYHCLVCP---DYDLCQSC 33

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 2217266321 328 CDNCGIEPIQGVRWHCQDCPpemSLDFCDSCSDCLHETDIHKEDHQLE 375
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 2217266321 160 WTVEEQKKLEQLLIKYppeeveSRRWQKIADELGNRTAKQVASR 203
Cdd:pfam13921   1 WTEEEDEKLLKLVEKY------GNDWKQIAKELGRRTPKQCFDR 38

UBR-box found in UBR4, UBR5, UBR6/FBOX11, UBR7 and similar proteins; This family includes UBR4 (EC 2.3.2.27), UBR5 (EC 2.3.2.26), UBR6/FBOX11 and UBR7 (EC 2.3.2.27). Both UBR4 (also called 600 kDa retinoblastoma protein-associated factor, or N-recognin-4, or retinoblastoma-associated factor of 600 kDa, or RBAF600, or p600, or zinc finger UBR1-type protein 1) and UBR7 (also called N-recognin-7) are RING-type E3 ubiquitin ligases of the Arg/N-end rule degradation pathway. They recognize and bind to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation. UBR5 (also called E3 ubiquitin-protein ligase, HECT domain-containing 1, E3 ligase identified by differential display (EDD), hyperplastic discs protein homolog (HYD), progestin-induced protein, or N-recognin-5) is a HECT (homologous to E6-AP C-terminus)-type E3 ubiquitin-protein ligase that acts as a key regulator of the ubiquitin proteasome system in both cancer and developmental biology. It is required for Wnt signal responses in Drosophila and human cell lines downstream of activated Armadillo/beta-catenin. It also plays a key role in ciliogenesis by regulating centriolar satellite stability and primary cilia. UBR6 (also called FBOX11, protein arginine N-methyltransferase 9 (PRMT9), or vitiligo-associated protein 1 (VIT-1)), is an E3 ubiquitin ligase and a type II methyltransferase, which functions as a key regulator of tumor initiation and progression. UBR6 is a substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins, such as DTL/CDT2, BCL6 and PRDM1/BLIMP1. UBR6 does not bind N-terminal signals.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217266321 332 GIEPIQGVRWHCQDCPPEMSLDFCDSCSD-ClhetdiHKeDHQLEPIYRSETFLDrdyCVSQG 393
Cdd:cd19671     7 GRKYIKQPWYHCYTCGLIDGLGVCEACARkC------HK-GHDLVYIGYSNFYCD---CGSSG 59