uncharacterized protein Dmel_CG1233, isoform A [Drosophila melanogaster]
zinc finger family protein( domain architecture ID 706824)
zinc finger family protein may be involved in transcriptional regulation; similar to Schizosaccharomyces pombe E3 ubiquitin-protein ligase hel2, which that plays a key role in the ribosome quality control (RQC), and Homo sapiens histone H4 transcription factor
List of domain hits
Name | Accession | Description | Interval | E-value | |||||
COG5236 super family | cl28715 | Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only]; |
626-855 | 1.77e-04 | |||||
Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only]; The actual alignment was detected with superfamily member COG5236: Pssm-ID: 227561 [Multi-domain] Cd Length: 493 Bit Score: 45.01 E-value: 1.77e-04
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Name | Accession | Description | Interval | E-value | |||||
COG5236 | COG5236 | Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only]; |
626-855 | 1.77e-04 | |||||
Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only]; Pssm-ID: 227561 [Multi-domain] Cd Length: 493 Bit Score: 45.01 E-value: 1.77e-04
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zf-C2H2 | pfam00096 | Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ... |
700-722 | 3.13e-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: 38.82 E-value: 3.13e-04
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Name | Accession | Description | Interval | E-value | |||||
COG5236 | COG5236 | Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only]; |
626-855 | 1.77e-04 | |||||
Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only]; Pssm-ID: 227561 [Multi-domain] Cd Length: 493 Bit Score: 45.01 E-value: 1.77e-04
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zf-C2H2 | pfam00096 | Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ... |
700-722 | 3.13e-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: 38.82 E-value: 3.13e-04
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zf-H2C2_2 | pfam13465 | Zinc-finger double domain; |
690-711 | 5.52e-03 | |||||
Zinc-finger double domain; Pssm-ID: 463886 [Multi-domain] Cd Length: 26 Bit Score: 35.04 E-value: 5.52e-03
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Blast search parameters | ||||
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