nervous fingers 2, isoform A [Drosophila melanogaster]
Protein Classification
C2H2-type zinc finger protein( domain architecture ID 10442881)
Cys2His2 (C2H2)-type zinc finger protein may be involved in transcriptional regulation
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| zf-C2H2 | pfam00096 | Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ... |
544-566 | 5.46e-06 | ||
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: 43.44 E-value: 5.46e-06
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| Name | Accession | Description | Interval | E-value | ||
| zf-C2H2 | pfam00096 | Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ... |
544-566 | 5.46e-06 | ||
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: 43.44 E-value: 5.46e-06
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| ZnF_C2H2 | smart00355 | zinc finger; |
544-566 | 3.23e-03 | ||
zinc finger; Pssm-ID: 197676 Cd Length: 23 Bit Score: 35.52 E-value: 3.23e-03
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| Name | Accession | Description | Interval | E-value | ||
| zf-C2H2 | pfam00096 | Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ... |
544-566 | 5.46e-06 | ||
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: 43.44 E-value: 5.46e-06
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| ZnF_C2H2 | smart00355 | zinc finger; |
544-566 | 3.23e-03 | ||
zinc finger; Pssm-ID: 197676 Cd Length: 23 Bit Score: 35.52 E-value: 3.23e-03
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| Blast search parameters | ||||
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