amelogenin precursor [Cavia porcellus]
Protein Classification
Amelogenin domain-containing protein( domain architecture ID 12220051)
Amelogenin domain-containing protein
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||
| Amelogenin | smart00818 | Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ... |
28-226 | 4.37e-48 | ||||
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem to regulate formation of crystallites during the secretory stage of tooth enamel development and are thought to play a major role in the structural organisation and mineralisation of developing enamel. The extracellular matrix of the developing enamel comprises two major classes of protein: the hydrophobic amelogenins and the acidic enamelins. Circular dichroism studies of porcine amelogenin have shown that the protein consists of 3 discrete folding units: the N-terminal region appears to contain beta-strand structures, while the C-terminal region displays characteristics of a random coil conformation. Subsequent studies on the bovine protein have indicated the amelogenin structure to contain a repetitive beta-turn segment and a "beta-spiral" between Gln112 and Leu138, which sequester a (Pro, Leu, Gln) rich region. The beta-spiral offers a probable site for interactions with Ca2+ ions. Muatations in the human amelogenin gene (AMGX) cause X-linked hypoplastic amelogenesis imperfecta, a disease characterised by defective enamel. A 9bp deletion in exon 2 of AMGX results in the loss of codons for Ile5, Leu6, Phe7 and Ala8, and replacement by a new threonine codon, disrupting the 16-residue (Met1-Ala16) amelogenin signal peptide. : Pssm-ID: 197891 [Multi-domain] Cd Length: 165 Bit Score: 155.72 E-value: 4.37e-48
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| Name | Accession | Description | Interval | E-value | ||||
| Amelogenin | smart00818 | Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ... |
28-226 | 4.37e-48 | ||||
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem to regulate formation of crystallites during the secretory stage of tooth enamel development and are thought to play a major role in the structural organisation and mineralisation of developing enamel. The extracellular matrix of the developing enamel comprises two major classes of protein: the hydrophobic amelogenins and the acidic enamelins. Circular dichroism studies of porcine amelogenin have shown that the protein consists of 3 discrete folding units: the N-terminal region appears to contain beta-strand structures, while the C-terminal region displays characteristics of a random coil conformation. Subsequent studies on the bovine protein have indicated the amelogenin structure to contain a repetitive beta-turn segment and a "beta-spiral" between Gln112 and Leu138, which sequester a (Pro, Leu, Gln) rich region. The beta-spiral offers a probable site for interactions with Ca2+ ions. Muatations in the human amelogenin gene (AMGX) cause X-linked hypoplastic amelogenesis imperfecta, a disease characterised by defective enamel. A 9bp deletion in exon 2 of AMGX results in the loss of codons for Ile5, Leu6, Phe7 and Ala8, and replacement by a new threonine codon, disrupting the 16-residue (Met1-Ala16) amelogenin signal peptide. Pssm-ID: 197891 [Multi-domain] Cd Length: 165 Bit Score: 155.72 E-value: 4.37e-48
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| Amelogenin | pfam02948 | Amelogenin; Amelogenins play a role in biomineralization. They seem to regulate the formation ... |
28-226 | 1.06e-37 | ||||
Amelogenin; Amelogenins play a role in biomineralization. They seem to regulate the formation of crystallites during the secretory stage of tooth enamel development. thought to play a major role in the structural organization and mineralization of developing enamel. They are found in the extracellular matrix. Mutations in X-chromosomal amelogenin can cause Amelogenesis imperfecta. Pssm-ID: 460761 [Multi-domain] Cd Length: 179 Bit Score: 129.49 E-value: 1.06e-37
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| KLF1_2_4_N-like | cd22056 | N-terminal domain of Kruppel-like factors with similarity to the N-terminal domains of ... |
78-152 | 8.11e-03 | ||||
N-terminal domain of Kruppel-like factors with similarity to the N-terminal domains of Kruppel-like factor (KLF)1, KLF2, and KLF4; Kruppel/Krueppel-like transcription factors (KLFs) belong to a family of proteins called the Specificity Protein (SP)/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. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specifity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domains of an unknown subfamily of KLFs, predominantly found in fish, related to the N-terminal domains of KLF1, KLF2, and KLF4. Pssm-ID: 409231 [Multi-domain] Cd Length: 339 Bit Score: 36.56 E-value: 8.11e-03
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| Name | Accession | Description | Interval | E-value | ||||
| Amelogenin | smart00818 | Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ... |
28-226 | 4.37e-48 | ||||
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem to regulate formation of crystallites during the secretory stage of tooth enamel development and are thought to play a major role in the structural organisation and mineralisation of developing enamel. The extracellular matrix of the developing enamel comprises two major classes of protein: the hydrophobic amelogenins and the acidic enamelins. Circular dichroism studies of porcine amelogenin have shown that the protein consists of 3 discrete folding units: the N-terminal region appears to contain beta-strand structures, while the C-terminal region displays characteristics of a random coil conformation. Subsequent studies on the bovine protein have indicated the amelogenin structure to contain a repetitive beta-turn segment and a "beta-spiral" between Gln112 and Leu138, which sequester a (Pro, Leu, Gln) rich region. The beta-spiral offers a probable site for interactions with Ca2+ ions. Muatations in the human amelogenin gene (AMGX) cause X-linked hypoplastic amelogenesis imperfecta, a disease characterised by defective enamel. A 9bp deletion in exon 2 of AMGX results in the loss of codons for Ile5, Leu6, Phe7 and Ala8, and replacement by a new threonine codon, disrupting the 16-residue (Met1-Ala16) amelogenin signal peptide. Pssm-ID: 197891 [Multi-domain] Cd Length: 165 Bit Score: 155.72 E-value: 4.37e-48
|
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| Amelogenin | pfam02948 | Amelogenin; Amelogenins play a role in biomineralization. They seem to regulate the formation ... |
28-226 | 1.06e-37 | ||||
Amelogenin; Amelogenins play a role in biomineralization. They seem to regulate the formation of crystallites during the secretory stage of tooth enamel development. thought to play a major role in the structural organization and mineralization of developing enamel. They are found in the extracellular matrix. Mutations in X-chromosomal amelogenin can cause Amelogenesis imperfecta. Pssm-ID: 460761 [Multi-domain] Cd Length: 179 Bit Score: 129.49 E-value: 1.06e-37
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| EIF4E-T | pfam10477 | Nucleocytoplasmic shuttling protein for mRNA cap-binding EIF4E; EIF4E-T is the transporter ... |
39-145 | 3.69e-04 | ||||
Nucleocytoplasmic shuttling protein for mRNA cap-binding EIF4E; EIF4E-T is the transporter protein for shuttling the mRNA cap-binding protein EIF4E protein, targeting it for nuclear import. EIF4E-T contains several key binding domains including two functional leucine-rich NESs (nuclear export signals) between residues 438-447 and 613-638 in the human protein. The other two binding domains are an EIF4E-binding site, between residues 27-42 in Q9EST3, and a bipartite NLS (nuclear localization signals) between 194-211, and these lie in family EIF4E-T_N. EIF4E is the eukaryotic translation initiation factor 4E that is the rate-limiting factor for cap-dependent translation initiation. Pssm-ID: 371079 Cd Length: 646 Bit Score: 41.15 E-value: 3.69e-04
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| PAT1 | pfam09770 | Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ... |
85-168 | 1.79e-03 | ||||
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division. Pssm-ID: 401645 [Multi-domain] Cd Length: 846 Bit Score: 38.86 E-value: 1.79e-03
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| PAT1 | pfam09770 | Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ... |
62-144 | 3.72e-03 | ||||
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division. Pssm-ID: 401645 [Multi-domain] Cd Length: 846 Bit Score: 38.09 E-value: 3.72e-03
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| KLF1_2_4_N-like | cd22056 | N-terminal domain of Kruppel-like factors with similarity to the N-terminal domains of ... |
78-152 | 8.11e-03 | ||||
N-terminal domain of Kruppel-like factors with similarity to the N-terminal domains of Kruppel-like factor (KLF)1, KLF2, and KLF4; Kruppel/Krueppel-like transcription factors (KLFs) belong to a family of proteins called the Specificity Protein (SP)/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. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specifity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domains of an unknown subfamily of KLFs, predominantly found in fish, related to the N-terminal domains of KLF1, KLF2, and KLF4. Pssm-ID: 409231 [Multi-domain] Cd Length: 339 Bit Score: 36.56 E-value: 8.11e-03
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| Blast search parameters | ||||
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