zinc finger protein 82 homolog [Drosophila yakuba]
Protein Classification
zf-AD domain-containing protein( domain architecture ID 11170943)
zf-AD domain-containing protein
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| zf-AD | pfam07776 | Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical ... |
4-67 | 5.30e-08 | ||
Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical treble-cleft-like zinc co-ordinating fold. The zf-AD domain is thought to be involved in mediating dimer formation, but does not bind to DNA. : Pssm-ID: 462262 Cd Length: 75 Bit Score: 48.61 E-value: 5.30e-08
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| zf-C2H2 | pfam00096 | Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ... |
190-212 | 9.44e-04 | ||
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. : Pssm-ID: 395048 [Multi-domain] Cd Length: 23 Bit Score: 35.74 E-value: 9.44e-04
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| zf-H2C2_2 | pfam13465 | Zinc-finger double domain; |
176-201 | 4.53e-03 | ||
Zinc-finger double domain; : Pssm-ID: 463886 [Multi-domain] Cd Length: 26 Bit Score: 33.50 E-value: 4.53e-03
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| zf-C2H2 | pfam00096 | Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ... |
162-184 | 5.46e-03 | ||
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. : Pssm-ID: 395048 [Multi-domain] Cd Length: 23 Bit Score: 33.43 E-value: 5.46e-03
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| Name | Accession | Description | Interval | E-value | ||
| zf-AD | pfam07776 | Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical ... |
4-67 | 5.30e-08 | ||
Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical treble-cleft-like zinc co-ordinating fold. The zf-AD domain is thought to be involved in mediating dimer formation, but does not bind to DNA. Pssm-ID: 462262 Cd Length: 75 Bit Score: 48.61 E-value: 5.30e-08
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| zf-AD | smart00868 | Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical ... |
4-67 | 1.35e-07 | ||
Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical treble-cleft-like zinc co-ordinating fold. The zf-AD domain is thought to be involved in mediating dimer formation, but does not bind to DNA. Pssm-ID: 214871 Cd Length: 73 Bit Score: 47.51 E-value: 1.35e-07
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| zf-C2H2 | pfam00096 | Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ... |
190-212 | 9.44e-04 | ||
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. Pssm-ID: 395048 [Multi-domain] Cd Length: 23 Bit Score: 35.74 E-value: 9.44e-04
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| zf-H2C2_2 | pfam13465 | Zinc-finger double domain; |
176-201 | 4.53e-03 | ||
Zinc-finger double domain; Pssm-ID: 463886 [Multi-domain] Cd Length: 26 Bit Score: 33.50 E-value: 4.53e-03
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| zf-C2H2 | pfam00096 | Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ... |
162-184 | 5.46e-03 | ||
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. Pssm-ID: 395048 [Multi-domain] Cd Length: 23 Bit Score: 33.43 E-value: 5.46e-03
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| Name | Accession | Description | Interval | E-value | ||
| zf-AD | pfam07776 | Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical ... |
4-67 | 5.30e-08 | ||
Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical treble-cleft-like zinc co-ordinating fold. The zf-AD domain is thought to be involved in mediating dimer formation, but does not bind to DNA. Pssm-ID: 462262 Cd Length: 75 Bit Score: 48.61 E-value: 5.30e-08
|
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| zf-AD | smart00868 | Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical ... |
4-67 | 1.35e-07 | ||
Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical treble-cleft-like zinc co-ordinating fold. The zf-AD domain is thought to be involved in mediating dimer formation, but does not bind to DNA. Pssm-ID: 214871 Cd Length: 73 Bit Score: 47.51 E-value: 1.35e-07
|
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| zf-C2H2 | pfam00096 | Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ... |
190-212 | 9.44e-04 | ||
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. Pssm-ID: 395048 [Multi-domain] Cd Length: 23 Bit Score: 35.74 E-value: 9.44e-04
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| zf-H2C2_2 | pfam13465 | Zinc-finger double domain; |
176-201 | 4.53e-03 | ||
Zinc-finger double domain; Pssm-ID: 463886 [Multi-domain] Cd Length: 26 Bit Score: 33.50 E-value: 4.53e-03
|
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| zf-C2H2 | pfam00096 | Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ... |
162-184 | 5.46e-03 | ||
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. Pssm-ID: 395048 [Multi-domain] Cd Length: 23 Bit Score: 33.43 E-value: 5.46e-03
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| Blast search parameters | ||||
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