Telomerase activating protein Est1 [Arabidopsis thaliana]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||
| EST1_DNA_bind | pfam10373 | Est1 DNA/RNA binding domain; Est1 is a protein which recruits or activates telomerase at the ... |
203-533 | 1.67e-62 | ||||||
Est1 DNA/RNA binding domain; Est1 is a protein which recruits or activates telomerase at the site of polymerization. This is the DNA/RNA binding domain of EST1. : Pssm-ID: 431239 Cd Length: 279 Bit Score: 213.81 E-value: 1.67e-62
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| EST1 | pfam10374 | Telomerase activating protein Est1; Est1 is a protein which recruits or activates telomerase ... |
71-190 | 2.40e-17 | ||||||
Telomerase activating protein Est1; Est1 is a protein which recruits or activates telomerase at the site of polymerization. Structurally it resembles a TPR-like repeat. : Pssm-ID: 463062 Cd Length: 98 Bit Score: 78.12 E-value: 2.40e-17
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| SP1-4_N super family | cl41773 | N-terminal domain of transcription factor Specificity Proteins (SP) 1-4; Specificity Proteins ... |
753-888 | 4.73e-03 | ||||||
N-terminal domain of transcription factor Specificity Proteins (SP) 1-4; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. There are many SPs in vertebrates (9 SPs in humans and mice, 7 SPs in chicken, and 11 SPs in teleost fish), but arthropods only have 3 SPs. SPs belong to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP1-4. The actual alignment was detected with superfamily member cd22540: Pssm-ID: 425404 [Multi-domain] Cd Length: 511 Bit Score: 40.68 E-value: 4.73e-03
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| Name | Accession | Description | Interval | E-value | ||||||
| EST1_DNA_bind | pfam10373 | Est1 DNA/RNA binding domain; Est1 is a protein which recruits or activates telomerase at the ... |
203-533 | 1.67e-62 | ||||||
Est1 DNA/RNA binding domain; Est1 is a protein which recruits or activates telomerase at the site of polymerization. This is the DNA/RNA binding domain of EST1. Pssm-ID: 431239 Cd Length: 279 Bit Score: 213.81 E-value: 1.67e-62
|
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| EST1 | pfam10374 | Telomerase activating protein Est1; Est1 is a protein which recruits or activates telomerase ... |
71-190 | 2.40e-17 | ||||||
Telomerase activating protein Est1; Est1 is a protein which recruits or activates telomerase at the site of polymerization. Structurally it resembles a TPR-like repeat. Pssm-ID: 463062 Cd Length: 98 Bit Score: 78.12 E-value: 2.40e-17
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| SP2_N | cd22540 | N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins ... |
753-888 | 4.73e-03 | ||||||
N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. SP2 contains the least conserved DNA-binding domain within the SP subfamily of proteins, and its DNA sequence specificity differs from the other SP proteins. It localizes primarily within subnuclear foci associated with the nuclear matrix, and can activate, or in some cases, repress expression from different promoters. The transcription factor SP2 serves as a paradigm for indirect genomic binding. It does not require its DNA-binding domain for genomic DNA binding and occupies target promoters independently of whether they contain a cognate DNA-binding motif. SP2 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP2. Pssm-ID: 411776 [Multi-domain] Cd Length: 511 Bit Score: 40.68 E-value: 4.73e-03
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| Name | Accession | Description | Interval | E-value | ||||||
| EST1_DNA_bind | pfam10373 | Est1 DNA/RNA binding domain; Est1 is a protein which recruits or activates telomerase at the ... |
203-533 | 1.67e-62 | ||||||
Est1 DNA/RNA binding domain; Est1 is a protein which recruits or activates telomerase at the site of polymerization. This is the DNA/RNA binding domain of EST1. Pssm-ID: 431239 Cd Length: 279 Bit Score: 213.81 E-value: 1.67e-62
|
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| EST1 | pfam10374 | Telomerase activating protein Est1; Est1 is a protein which recruits or activates telomerase ... |
71-190 | 2.40e-17 | ||||||
Telomerase activating protein Est1; Est1 is a protein which recruits or activates telomerase at the site of polymerization. Structurally it resembles a TPR-like repeat. Pssm-ID: 463062 Cd Length: 98 Bit Score: 78.12 E-value: 2.40e-17
|
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| SP2_N | cd22540 | N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins ... |
753-888 | 4.73e-03 | ||||||
N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. SP2 contains the least conserved DNA-binding domain within the SP subfamily of proteins, and its DNA sequence specificity differs from the other SP proteins. It localizes primarily within subnuclear foci associated with the nuclear matrix, and can activate, or in some cases, repress expression from different promoters. The transcription factor SP2 serves as a paradigm for indirect genomic binding. It does not require its DNA-binding domain for genomic DNA binding and occupies target promoters independently of whether they contain a cognate DNA-binding motif. SP2 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP2. Pssm-ID: 411776 [Multi-domain] Cd Length: 511 Bit Score: 40.68 E-value: 4.73e-03
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