zinc finger E-box-binding homeobox 2 [Mus musculus]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| zf-H2C2_2 | pfam13465 | Zinc-finger double domain; |
296-319 | 3.99e-06 | ||
Zinc-finger double domain; : Pssm-ID: 463886 [Multi-domain] Cd Length: 26 Bit Score: 44.28 E-value: 3.99e-06
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| zf-H2C2_2 | pfam13465 | Zinc-finger double domain; |
1041-1066 | 2.81e-05 | ||
Zinc-finger double domain; : Pssm-ID: 463886 [Multi-domain] Cd Length: 26 Bit Score: 41.97 E-value: 2.81e-05
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| zf-C2H2 | pfam00096 | Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ... |
282-304 | 3.00e-05 | ||
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: 41.90 E-value: 3.00e-05
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| zf-H2C2_2 | pfam13465 | Zinc-finger double domain; |
1013-1038 | 1.75e-04 | ||
Zinc-finger double domain; : Pssm-ID: 463886 [Multi-domain] Cd Length: 26 Bit Score: 39.66 E-value: 1.75e-04
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| zf-C2H2 | pfam00096 | Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ... |
241-263 | 8.35e-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: 34.97 E-value: 8.35e-03
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| zf-Di19 super family | cl05267 | Drought induced 19 protein (Di19), zinc-binding; This family consists of several drought ... |
209-263 | 8.52e-03 | ||
Drought induced 19 protein (Di19), zinc-binding; This family consists of several drought induced 19 (Di19) like proteins. Di19 has been found to be strongly expressed in both the roots and leaves of Arabidopsis thaliana during progressive drought. This domain is a zinc-binding domain. The actual alignment was detected with superfamily member pfam05605: Pssm-ID: 428539 Cd Length: 54 Bit Score: 35.74 E-value: 8.52e-03
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| Name | Accession | Description | Interval | E-value | ||
| zf-H2C2_2 | pfam13465 | Zinc-finger double domain; |
296-319 | 3.99e-06 | ||
Zinc-finger double domain; Pssm-ID: 463886 [Multi-domain] Cd Length: 26 Bit Score: 44.28 E-value: 3.99e-06
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| zf-H2C2_2 | pfam13465 | Zinc-finger double domain; |
1041-1066 | 2.81e-05 | ||
Zinc-finger double domain; Pssm-ID: 463886 [Multi-domain] Cd Length: 26 Bit Score: 41.97 E-value: 2.81e-05
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| zf-C2H2 | pfam00096 | Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ... |
282-304 | 3.00e-05 | ||
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: 41.90 E-value: 3.00e-05
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| zf-H2C2_2 | pfam13465 | Zinc-finger double domain; |
1013-1038 | 1.75e-04 | ||
Zinc-finger double domain; Pssm-ID: 463886 [Multi-domain] Cd Length: 26 Bit Score: 39.66 E-value: 1.75e-04
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| ZnF_C2H2 | smart00355 | zinc finger; |
282-304 | 2.25e-03 | ||
zinc finger; Pssm-ID: 197676 Cd Length: 23 Bit Score: 36.67 E-value: 2.25e-03
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| zf-C2H2 | pfam00096 | Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ... |
241-263 | 8.35e-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: 34.97 E-value: 8.35e-03
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| zf-Di19 | pfam05605 | Drought induced 19 protein (Di19), zinc-binding; This family consists of several drought ... |
209-263 | 8.52e-03 | ||
Drought induced 19 protein (Di19), zinc-binding; This family consists of several drought induced 19 (Di19) like proteins. Di19 has been found to be strongly expressed in both the roots and leaves of Arabidopsis thaliana during progressive drought. This domain is a zinc-binding domain. Pssm-ID: 428539 Cd Length: 54 Bit Score: 35.74 E-value: 8.52e-03
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| Name | Accession | Description | Interval | E-value | ||
| zf-H2C2_2 | pfam13465 | Zinc-finger double domain; |
296-319 | 3.99e-06 | ||
Zinc-finger double domain; Pssm-ID: 463886 [Multi-domain] Cd Length: 26 Bit Score: 44.28 E-value: 3.99e-06
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| zf-H2C2_2 | pfam13465 | Zinc-finger double domain; |
1041-1066 | 2.81e-05 | ||
Zinc-finger double domain; Pssm-ID: 463886 [Multi-domain] Cd Length: 26 Bit Score: 41.97 E-value: 2.81e-05
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| zf-C2H2 | pfam00096 | Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ... |
282-304 | 3.00e-05 | ||
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: 41.90 E-value: 3.00e-05
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| zf-H2C2_2 | pfam13465 | Zinc-finger double domain; |
1013-1038 | 1.75e-04 | ||
Zinc-finger double domain; Pssm-ID: 463886 [Multi-domain] Cd Length: 26 Bit Score: 39.66 E-value: 1.75e-04
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| zf-C2H2 | pfam00096 | Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ... |
1027-1049 | 1.79e-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: 36.89 E-value: 1.79e-03
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| ZnF_C2H2 | smart00355 | zinc finger; |
282-304 | 2.25e-03 | ||
zinc finger; Pssm-ID: 197676 Cd Length: 23 Bit Score: 36.67 E-value: 2.25e-03
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| zf-C2H2 | pfam00096 | Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ... |
241-263 | 8.35e-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: 34.97 E-value: 8.35e-03
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| zf-Di19 | pfam05605 | Drought induced 19 protein (Di19), zinc-binding; This family consists of several drought ... |
209-263 | 8.52e-03 | ||
Drought induced 19 protein (Di19), zinc-binding; This family consists of several drought induced 19 (Di19) like proteins. Di19 has been found to be strongly expressed in both the roots and leaves of Arabidopsis thaliana during progressive drought. This domain is a zinc-binding domain. Pssm-ID: 428539 Cd Length: 54 Bit Score: 35.74 E-value: 8.52e-03
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| Blast search parameters | ||||
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