C2H2-type zinc finger; This family contains a number of divergent C2H2 type zinc fingers.

                          10        20
                  ....*....|....*....|....
gi 2462517564 525 YSCRICRKSYVRPGSLSTHMKLHH 548
Cdd:pfam13894   1 FKCPICGKSFSSKKSLKRHLKTHH 24

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517564  80 GTFSLVALPHVASAQPIQKPRMSL-PENLKLPIPRYQPPRnskasrkKPILIFPKSGCSKAPAQTQMCPQMSPSPPHHPE 158
Cdd:pfam03154 202 SAPSVPPQGSPATSQPPNQTQSTAaPHTLIQQTPTLHPQR-------LPSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQ 274

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462517564 159 LLYKSSPFEEVPSLEQAPASISTAALTNGSDHGDLRP------PVTNTHGSLNPPATPASSTPEEPAKQDL 223
Cdd:pfam03154 275 MPPMPHSLQTGPSHMQHPVPPQPFPLTPQSSQSQVPPgpspaaPGQSQQRIHTPPSQSQLQSQQPPREQPL 345

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.

                          10        20
                  ....*....|....*....|...
gi 2462517564 497 HRCHVCNHHFQFKQHLRDHMNTH 519
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462517564  80 GTFSLVALPHVASAQPIQKPRMSL-PENLKLPIPRYQPPRnskasrkKPILIFPKSGCSKAPAQTQMCPQMSPSPPHHPE 158
Cdd:pfam03154 202 SAPSVPPQGSPATSQPPNQTQSTAaPHTLIQQTPTLHPQR-------LPSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQ 274

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462517564 159 LLYKSSPFEEVPSLEQAPASISTAALTNGSDHGDLRP------PVTNTHGSLNPPATPASSTPEEPAKQDL 223
Cdd:pfam03154 275 MPPMPHSLQTGPSHMQHPVPPQPFPLTPQSSQSQVPPgpspaaPGQSQQRIHTPPSQSQLQSQQPPREQPL 345

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.

                          10        20
                  ....*....|....*....|...
gi 2462517564 497 HRCHVCNHHFQFKQHLRDHMNTH 519
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23