terminal uridylyltransferase 4 isoform X37 [Homo sapiens]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||
| TUTase | pfam19088 | TUTase nucleotidyltransferase domain; This nucleotidyltransferase domain is found in TUTase ... |
254-471 | 1.85e-140 | ||||||
TUTase nucleotidyltransferase domain; This nucleotidyltransferase domain is found in TUTase enzymes. Terminal uridyltransferases (TUTases) execute 3' RNA uridylation across protists, fungi, metazoan and plant species. : Pssm-ID: 465974 Cd Length: 218 Bit Score: 429.94 E-value: 1.85e-140
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| NT_PAP_TUTase | cd05402 | Nucleotidyltransferase (NT) domain of poly(A) polymerases and terminal uridylyl transferases; ... |
900-1018 | 6.43e-38 | ||||||
Nucleotidyltransferase (NT) domain of poly(A) polymerases and terminal uridylyl transferases; Poly(A) polymerases (PAPs) catalyze mRNA poly(A) tail synthesis, and terminal uridylyl transferases (TUTases) uridylate RNA. PAPs in this subgroup include human PAP alpha, mouse testis-specific cytoplasmic PAP beta, human nuclear PAP gamma, Saccharomyces cerevisiae PAP1, TRF4 and-5, Schizosaccharomyces pombe caffeine-induced death proteins -1, and -14, Caenorhabditis elegans Germ Line Development-2, and Chlamydomonas reinhardtii MUT68. This family also includes human U6 snRNA-specific TUTase1, and Trypanosoma brucei 3'-TUTase-1,-2, and 4. This family belongs to the Pol beta-like NT superfamily. In the majority of enzymes in this superfamily, two carboxylates, Dx[D/E], together with a third more distal carboxylate, coordinate two divalent metal cations involved in a two-metal ion mechanism of nucleotide addition. For the majority of proteins in this family, these carboxylate residues are conserved. : Pssm-ID: 143392 [Multi-domain] Cd Length: 114 Bit Score: 138.07 E-value: 6.43e-38
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| TRF4 super family | cl34961 | DNA polymerase sigma [Replication, recombination and repair]; |
321-630 | 1.20e-26 | ||||||
DNA polymerase sigma [Replication, recombination and repair]; The actual alignment was detected with superfamily member COG5260: Pssm-ID: 227585 [Multi-domain] Cd Length: 482 Bit Score: 115.64 E-value: 1.20e-26
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| TRF4 super family | cl34961 | DNA polymerase sigma [Replication, recombination and repair]; |
858-1152 | 6.81e-25 | ||||||
DNA polymerase sigma [Replication, recombination and repair]; The actual alignment was detected with superfamily member COG5260: Pssm-ID: 227585 [Multi-domain] Cd Length: 482 Bit Score: 110.25 E-value: 6.81e-25
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| Atrophin-1 super family | cl38111 | Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
1294-1483 | 1.92e-09 | ||||||
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity. The actual alignment was detected with superfamily member pfam03154: Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 62.48 E-value: 1.92e-09
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| rplD super family | cl29916 | 50S ribosomal protein L4; Provisional |
97-199 | 3.18e-04 | ||||||
50S ribosomal protein L4; Provisional The actual alignment was detected with superfamily member PRK14907: Pssm-ID: 184900 [Multi-domain] Cd Length: 295 Bit Score: 44.56 E-value: 3.18e-04
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| PTZ00368 super family | cl31762 | universal minicircle sequence binding protein (UMSBP); Provisional |
1171-1266 | 5.97e-03 | ||||||
universal minicircle sequence binding protein (UMSBP); Provisional The actual alignment was detected with superfamily member PTZ00368: Pssm-ID: 173561 [Multi-domain] Cd Length: 148 Bit Score: 39.02 E-value: 5.97e-03
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| Name | Accession | Description | Interval | E-value | ||||||
| TUTase | pfam19088 | TUTase nucleotidyltransferase domain; This nucleotidyltransferase domain is found in TUTase ... |
254-471 | 1.85e-140 | ||||||
TUTase nucleotidyltransferase domain; This nucleotidyltransferase domain is found in TUTase enzymes. Terminal uridyltransferases (TUTases) execute 3' RNA uridylation across protists, fungi, metazoan and plant species. Pssm-ID: 465974 Cd Length: 218 Bit Score: 429.94 E-value: 1.85e-140
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| NT_PAP_TUTase | cd05402 | Nucleotidyltransferase (NT) domain of poly(A) polymerases and terminal uridylyl transferases; ... |
900-1018 | 6.43e-38 | ||||||
Nucleotidyltransferase (NT) domain of poly(A) polymerases and terminal uridylyl transferases; Poly(A) polymerases (PAPs) catalyze mRNA poly(A) tail synthesis, and terminal uridylyl transferases (TUTases) uridylate RNA. PAPs in this subgroup include human PAP alpha, mouse testis-specific cytoplasmic PAP beta, human nuclear PAP gamma, Saccharomyces cerevisiae PAP1, TRF4 and-5, Schizosaccharomyces pombe caffeine-induced death proteins -1, and -14, Caenorhabditis elegans Germ Line Development-2, and Chlamydomonas reinhardtii MUT68. This family also includes human U6 snRNA-specific TUTase1, and Trypanosoma brucei 3'-TUTase-1,-2, and 4. This family belongs to the Pol beta-like NT superfamily. In the majority of enzymes in this superfamily, two carboxylates, Dx[D/E], together with a third more distal carboxylate, coordinate two divalent metal cations involved in a two-metal ion mechanism of nucleotide addition. For the majority of proteins in this family, these carboxylate residues are conserved. Pssm-ID: 143392 [Multi-domain] Cd Length: 114 Bit Score: 138.07 E-value: 6.43e-38
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| NT_PAP_TUTase | cd05402 | Nucleotidyltransferase (NT) domain of poly(A) polymerases and terminal uridylyl transferases; ... |
375-487 | 3.81e-32 | ||||||
Nucleotidyltransferase (NT) domain of poly(A) polymerases and terminal uridylyl transferases; Poly(A) polymerases (PAPs) catalyze mRNA poly(A) tail synthesis, and terminal uridylyl transferases (TUTases) uridylate RNA. PAPs in this subgroup include human PAP alpha, mouse testis-specific cytoplasmic PAP beta, human nuclear PAP gamma, Saccharomyces cerevisiae PAP1, TRF4 and-5, Schizosaccharomyces pombe caffeine-induced death proteins -1, and -14, Caenorhabditis elegans Germ Line Development-2, and Chlamydomonas reinhardtii MUT68. This family also includes human U6 snRNA-specific TUTase1, and Trypanosoma brucei 3'-TUTase-1,-2, and 4. This family belongs to the Pol beta-like NT superfamily. In the majority of enzymes in this superfamily, two carboxylates, Dx[D/E], together with a third more distal carboxylate, coordinate two divalent metal cations involved in a two-metal ion mechanism of nucleotide addition. For the majority of proteins in this family, these carboxylate residues are conserved. Pssm-ID: 143392 [Multi-domain] Cd Length: 114 Bit Score: 121.51 E-value: 3.81e-32
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| TRF4 | COG5260 | DNA polymerase sigma [Replication, recombination and repair]; |
321-630 | 1.20e-26 | ||||||
DNA polymerase sigma [Replication, recombination and repair]; Pssm-ID: 227585 [Multi-domain] Cd Length: 482 Bit Score: 115.64 E-value: 1.20e-26
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| TRF4 | COG5260 | DNA polymerase sigma [Replication, recombination and repair]; |
858-1152 | 6.81e-25 | ||||||
DNA polymerase sigma [Replication, recombination and repair]; Pssm-ID: 227585 [Multi-domain] Cd Length: 482 Bit Score: 110.25 E-value: 6.81e-25
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| PAP_assoc | pfam03828 | Cid1 family poly A polymerase; This domain is found in poly(A) polymerases and has been shown ... |
1075-1128 | 8.93e-18 | ||||||
Cid1 family poly A polymerase; This domain is found in poly(A) polymerases and has been shown to have polynucleotide adenylyltransferase activity. Proteins in this family have been located to both the nucleus and the cytoplasm. Pssm-ID: 427532 Cd Length: 60 Bit Score: 78.77 E-value: 8.93e-18
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| PAP_assoc | pfam03828 | Cid1 family poly A polymerase; This domain is found in poly(A) polymerases and has been shown ... |
557-606 | 6.22e-13 | ||||||
Cid1 family poly A polymerase; This domain is found in poly(A) polymerases and has been shown to have polynucleotide adenylyltransferase activity. Proteins in this family have been located to both the nucleus and the cytoplasm. Pssm-ID: 427532 Cd Length: 60 Bit Score: 64.90 E-value: 6.22e-13
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| NTP_transf_2 | pfam01909 | Nucleotidyltransferase domain; Members of this family belong to a large family of ... |
908-993 | 4.39e-10 | ||||||
Nucleotidyltransferase domain; Members of this family belong to a large family of nucleotidyltransferases. This family includes kanamycin nucleotidyltransferase (KNTase) which is a plasmid-coded enzyme responsible for some types of bacterial resistance to aminoglycosides. KNTase in-activates antibiotics by catalysing the addition of a nucleotidyl group onto the drug. Pssm-ID: 396474 Cd Length: 91 Bit Score: 57.81 E-value: 4.39e-10
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| Atrophin-1 | pfam03154 | Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
1294-1483 | 1.92e-09 | ||||||
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity. Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 62.48 E-value: 1.92e-09
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| PHA03247 | PHA03247 | large tegument protein UL36; Provisional |
1296-1482 | 5.25e-08 | ||||||
large tegument protein UL36; Provisional Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 58.03 E-value: 5.25e-08
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| KLF3_N | cd21577 | N-terminal domain of Kruppel-like factor 3; Kruppel-like factor 3 (KLF3; also called ... |
1300-1455 | 7.89e-05 | ||||||
N-terminal domain of Kruppel-like factor 3; Kruppel-like factor 3 (KLF3; also called Krueppel-like factor 3 and originally called Basic Kruppel-like Factor/BKLF), was the third member of the KLF family of zinc finger transcription factors to be discovered. KLF3 possesses a wide range of biological impacts on regulating apoptosis, differentiation, and proliferation in various tissues during the entire progression process. It has been proposed as a tumor suppressor in colorectal cancer. It appears to function predominantly as a repressor of transcription, turning genes off by recruiting the C-terminal Binding Protein co-repressors CtBP1 and CtBP2. CtBP docks onto a short motif (residues 61-65) in the N-terminus of KLF3, through the Proline-X-Aspartate-Leucine-Serine (PXDLS) motif. CtBP in turn recruits histone modifying enzymes to alter chromatin and repress gene expression. KLF3 belongs 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 specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domain of KLF3. Pssm-ID: 410554 [Multi-domain] Cd Length: 214 Bit Score: 45.80 E-value: 7.89e-05
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| Amelogenin | smart00818 | Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ... |
1319-1397 | 2.83e-04 | ||||||
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: 43.24 E-value: 2.83e-04
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| rplD | PRK14907 | 50S ribosomal protein L4; Provisional |
97-199 | 3.18e-04 | ||||||
50S ribosomal protein L4; Provisional Pssm-ID: 184900 [Multi-domain] Cd Length: 295 Bit Score: 44.56 E-value: 3.18e-04
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| PTZ00368 | PTZ00368 | universal minicircle sequence binding protein (UMSBP); Provisional |
1171-1266 | 5.97e-03 | ||||||
universal minicircle sequence binding protein (UMSBP); Provisional Pssm-ID: 173561 [Multi-domain] Cd Length: 148 Bit Score: 39.02 E-value: 5.97e-03
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| Name | Accession | Description | Interval | E-value | ||||||
| TUTase | pfam19088 | TUTase nucleotidyltransferase domain; This nucleotidyltransferase domain is found in TUTase ... |
254-471 | 1.85e-140 | ||||||
TUTase nucleotidyltransferase domain; This nucleotidyltransferase domain is found in TUTase enzymes. Terminal uridyltransferases (TUTases) execute 3' RNA uridylation across protists, fungi, metazoan and plant species. Pssm-ID: 465974 Cd Length: 218 Bit Score: 429.94 E-value: 1.85e-140
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| NT_PAP_TUTase | cd05402 | Nucleotidyltransferase (NT) domain of poly(A) polymerases and terminal uridylyl transferases; ... |
900-1018 | 6.43e-38 | ||||||
Nucleotidyltransferase (NT) domain of poly(A) polymerases and terminal uridylyl transferases; Poly(A) polymerases (PAPs) catalyze mRNA poly(A) tail synthesis, and terminal uridylyl transferases (TUTases) uridylate RNA. PAPs in this subgroup include human PAP alpha, mouse testis-specific cytoplasmic PAP beta, human nuclear PAP gamma, Saccharomyces cerevisiae PAP1, TRF4 and-5, Schizosaccharomyces pombe caffeine-induced death proteins -1, and -14, Caenorhabditis elegans Germ Line Development-2, and Chlamydomonas reinhardtii MUT68. This family also includes human U6 snRNA-specific TUTase1, and Trypanosoma brucei 3'-TUTase-1,-2, and 4. This family belongs to the Pol beta-like NT superfamily. In the majority of enzymes in this superfamily, two carboxylates, Dx[D/E], together with a third more distal carboxylate, coordinate two divalent metal cations involved in a two-metal ion mechanism of nucleotide addition. For the majority of proteins in this family, these carboxylate residues are conserved. Pssm-ID: 143392 [Multi-domain] Cd Length: 114 Bit Score: 138.07 E-value: 6.43e-38
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| NT_PAP_TUTase | cd05402 | Nucleotidyltransferase (NT) domain of poly(A) polymerases and terminal uridylyl transferases; ... |
375-487 | 3.81e-32 | ||||||
Nucleotidyltransferase (NT) domain of poly(A) polymerases and terminal uridylyl transferases; Poly(A) polymerases (PAPs) catalyze mRNA poly(A) tail synthesis, and terminal uridylyl transferases (TUTases) uridylate RNA. PAPs in this subgroup include human PAP alpha, mouse testis-specific cytoplasmic PAP beta, human nuclear PAP gamma, Saccharomyces cerevisiae PAP1, TRF4 and-5, Schizosaccharomyces pombe caffeine-induced death proteins -1, and -14, Caenorhabditis elegans Germ Line Development-2, and Chlamydomonas reinhardtii MUT68. This family also includes human U6 snRNA-specific TUTase1, and Trypanosoma brucei 3'-TUTase-1,-2, and 4. This family belongs to the Pol beta-like NT superfamily. In the majority of enzymes in this superfamily, two carboxylates, Dx[D/E], together with a third more distal carboxylate, coordinate two divalent metal cations involved in a two-metal ion mechanism of nucleotide addition. For the majority of proteins in this family, these carboxylate residues are conserved. Pssm-ID: 143392 [Multi-domain] Cd Length: 114 Bit Score: 121.51 E-value: 3.81e-32
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| TRF4 | COG5260 | DNA polymerase sigma [Replication, recombination and repair]; |
321-630 | 1.20e-26 | ||||||
DNA polymerase sigma [Replication, recombination and repair]; Pssm-ID: 227585 [Multi-domain] Cd Length: 482 Bit Score: 115.64 E-value: 1.20e-26
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| TRF4 | COG5260 | DNA polymerase sigma [Replication, recombination and repair]; |
858-1152 | 6.81e-25 | ||||||
DNA polymerase sigma [Replication, recombination and repair]; Pssm-ID: 227585 [Multi-domain] Cd Length: 482 Bit Score: 110.25 E-value: 6.81e-25
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| PAP_assoc | pfam03828 | Cid1 family poly A polymerase; This domain is found in poly(A) polymerases and has been shown ... |
1075-1128 | 8.93e-18 | ||||||
Cid1 family poly A polymerase; This domain is found in poly(A) polymerases and has been shown to have polynucleotide adenylyltransferase activity. Proteins in this family have been located to both the nucleus and the cytoplasm. Pssm-ID: 427532 Cd Length: 60 Bit Score: 78.77 E-value: 8.93e-18
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| PAP_assoc | pfam03828 | Cid1 family poly A polymerase; This domain is found in poly(A) polymerases and has been shown ... |
557-606 | 6.22e-13 | ||||||
Cid1 family poly A polymerase; This domain is found in poly(A) polymerases and has been shown to have polynucleotide adenylyltransferase activity. Proteins in this family have been located to both the nucleus and the cytoplasm. Pssm-ID: 427532 Cd Length: 60 Bit Score: 64.90 E-value: 6.22e-13
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| NTP_transf_2 | pfam01909 | Nucleotidyltransferase domain; Members of this family belong to a large family of ... |
908-993 | 4.39e-10 | ||||||
Nucleotidyltransferase domain; Members of this family belong to a large family of nucleotidyltransferases. This family includes kanamycin nucleotidyltransferase (KNTase) which is a plasmid-coded enzyme responsible for some types of bacterial resistance to aminoglycosides. KNTase in-activates antibiotics by catalysing the addition of a nucleotidyl group onto the drug. Pssm-ID: 396474 Cd Length: 91 Bit Score: 57.81 E-value: 4.39e-10
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| Atrophin-1 | pfam03154 | Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
1294-1483 | 1.92e-09 | ||||||
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity. Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 62.48 E-value: 1.92e-09
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| PHA03247 | PHA03247 | large tegument protein UL36; Provisional |
1296-1482 | 5.25e-08 | ||||||
large tegument protein UL36; Provisional Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 58.03 E-value: 5.25e-08
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| SOBP | pfam15279 | Sine oculis-binding protein; SOBP is associated with syndromic and nonsyndromic intellectual ... |
1313-1436 | 5.97e-06 | ||||||
Sine oculis-binding protein; SOBP is associated with syndromic and nonsyndromic intellectual disability. It carries a zinc-finger of the zf-C2H2 type at the N-terminus, and a highly characteriztic C-terminal PhPhPhPhPhPh motif. The deduced 873-amino acid protein contains an N-terminal nuclear localization signal (NLS), followed by 2 FCS-type zinc finger motifs, a proline-rich region (PR1), a putative RNA-binding motif region, and a C-terminal NLS embedded in a second proline-rich motif. SOBP is expressed in various human tissues, including developing mouse brain at embryonic day 14. In postnatal and adult mouse brain SOBP is expressed in all neurons, with intense staining in the limbic system. Highest expression is in layer V cortical neurons, hippocampus, pyriform cortex, dorsomedial nucleus of thalamus, amygdala, and hypothalamus. Postnatal expression of SOBP in the limbic system corresponds to a time of active synaptogenesis. the family is also referred to as Jackson circler, JXC1. In seven affected siblings from a consanguineous Israeli Arab family with mental retardation, anterior maxillary protrusion, and strabismus mutations were found in this protein. Pssm-ID: 464609 [Multi-domain] Cd Length: 325 Bit Score: 50.20 E-value: 5.97e-06
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| PAT1 | pfam09770 | Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ... |
1288-1403 | 6.56e-06 | ||||||
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: 50.80 E-value: 6.56e-06
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| PHA03377 | PHA03377 | EBNA-3C; Provisional |
1283-1535 | 1.55e-05 | ||||||
EBNA-3C; Provisional Pssm-ID: 177614 [Multi-domain] Cd Length: 1000 Bit Score: 49.67 E-value: 1.55e-05
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| Atrophin-1 | pfam03154 | Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
1305-1489 | 3.12e-05 | ||||||
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity. Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 49.00 E-value: 3.12e-05
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| Pro-rich | pfam15240 | Proline-rich protein; This family includes several eukaryotic proline-rich proteins. |
1294-1413 | 3.87e-05 | ||||||
Proline-rich protein; This family includes several eukaryotic proline-rich proteins. Pssm-ID: 464580 [Multi-domain] Cd Length: 167 Bit Score: 45.80 E-value: 3.87e-05
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| PHA03247 | PHA03247 | large tegument protein UL36; Provisional |
1293-1456 | 7.51e-05 | ||||||
large tegument protein UL36; Provisional Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 47.63 E-value: 7.51e-05
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| KLF3_N | cd21577 | N-terminal domain of Kruppel-like factor 3; Kruppel-like factor 3 (KLF3; also called ... |
1300-1455 | 7.89e-05 | ||||||
N-terminal domain of Kruppel-like factor 3; Kruppel-like factor 3 (KLF3; also called Krueppel-like factor 3 and originally called Basic Kruppel-like Factor/BKLF), was the third member of the KLF family of zinc finger transcription factors to be discovered. KLF3 possesses a wide range of biological impacts on regulating apoptosis, differentiation, and proliferation in various tissues during the entire progression process. It has been proposed as a tumor suppressor in colorectal cancer. It appears to function predominantly as a repressor of transcription, turning genes off by recruiting the C-terminal Binding Protein co-repressors CtBP1 and CtBP2. CtBP docks onto a short motif (residues 61-65) in the N-terminus of KLF3, through the Proline-X-Aspartate-Leucine-Serine (PXDLS) motif. CtBP in turn recruits histone modifying enzymes to alter chromatin and repress gene expression. KLF3 belongs 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 specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domain of KLF3. Pssm-ID: 410554 [Multi-domain] Cd Length: 214 Bit Score: 45.80 E-value: 7.89e-05
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| PRK10263 | PRK10263 | DNA translocase FtsK; Provisional |
1296-1401 | 1.14e-04 | ||||||
DNA translocase FtsK; Provisional Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 47.00 E-value: 1.14e-04
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| Amelogenin | smart00818 | Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ... |
1319-1397 | 2.83e-04 | ||||||
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: 43.24 E-value: 2.83e-04
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| rplD | PRK14907 | 50S ribosomal protein L4; Provisional |
97-199 | 3.18e-04 | ||||||
50S ribosomal protein L4; Provisional Pssm-ID: 184900 [Multi-domain] Cd Length: 295 Bit Score: 44.56 E-value: 3.18e-04
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| PHA03307 | PHA03307 | transcriptional regulator ICP4; Provisional |
1312-1479 | 4.73e-04 | ||||||
transcriptional regulator ICP4; Provisional Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 45.16 E-value: 4.73e-04
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| PTZ00368 | PTZ00368 | universal minicircle sequence binding protein (UMSBP); Provisional |
1171-1266 | 5.97e-03 | ||||||
universal minicircle sequence binding protein (UMSBP); Provisional Pssm-ID: 173561 [Multi-domain] Cd Length: 148 Bit Score: 39.02 E-value: 5.97e-03
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