ubiquitin specific protease 32, isoform F [Drosophila melanogaster]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||||
| UBP12 super family | cl35019 | Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
486-1002 | 4.76e-57 | ||||||||
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; The actual alignment was detected with superfamily member COG5560: Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 214.36 E-value: 4.76e-57
|
||||||||||||
| Peptidase_C19 super family | cl02553 | Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
1480-1737 | 5.28e-39 | ||||||||
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyse bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome. The actual alignment was detected with superfamily member cd02674: Pssm-ID: 470612 [Multi-domain] Cd Length: 230 Bit Score: 145.89 E-value: 5.28e-39
|
||||||||||||
| EF-hand_7 | pfam13499 | EF-hand domain pair; |
227-290 | 2.74e-07 | ||||||||
EF-hand domain pair; : Pssm-ID: 463900 [Multi-domain] Cd Length: 67 Bit Score: 49.17 E-value: 2.74e-07
|
||||||||||||
| EFh_PI-PLC super family | cl28895 | EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ... |
198-251 | 9.36e-03 | ||||||||
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) isozymes; PI-PLC isozymes are signaling enzymes that hydrolyze the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. This family corresponds to the four EF-hand motifs containing PI-PLC isozymes, including PI-PLC-beta (1-4), -gamma (1-2), -delta (1,3,4), -epsilon (1), -zeta (1), eta (1-2). Lower eukaryotes such as yeast and slime molds contain only delta-type isozymes. In contrast, other types of isoforms present in higher eukaryotes. This family also includes 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase 1 (PLC1) from fungi. Some homologs from plants contain only two atypical EF-hand motifs and they are not included. All PI-PLC isozymes except sperm-specific PI-PLC-zeta share a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C2 domain. PI-PLC-zeta lacks the PH domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. Most of EF-hand motifs found in PI-PLCs consist of a helix-loop-helix structure, but lack residues critical to metal binding. Moreover, the EF-hand region of most of PI-PLCs may have an important regulatory function, but it has yet to be identified. However, PI-PLC-zeta is a key exception. It is responsible for Ca2+ oscillations in fertilized oocytes and exhibits a high sensitivity to Ca2+ mediated through its EF-hand domain. In addition, PI-PLC-eta2 shows a canonical EF-loop directing Ca2+-sensitivity and thus can amplify transient Ca2+ signals. Also it appears that PI-PLC-delta1 can regulate the binding of PH domain to PIP2 in a Ca2+-dependent manner through its functionally important EF-hand domains. PI-PLCs can be activated by a variety of extracellular ligands, such as growth factors, hormones, cytokines and lipids. Their activation has been implicated in tumorigenesis and/or metastasis linked to migration, proliferation, growth, inflammation, angiogenesis and actin cytoskeleton reorganization. PI-PLC-beta isozymes are activated by G-protein coupled receptor (GPCR) through different mechanisms. However, PI-PLC-gamma isozymes are activated by receptor tyrosine kinase (RTK), such as Rho and Ras GTPases. In contrast, PI-PLC-epsilon are activated by both GPCR and RTK. PI-PLC-delta1 and PLC-eta 1 are activated by GPCR-mediated calcium mobilization. The activation mechanism for PI-PLC-zeta remains unclear. The actual alignment was detected with superfamily member cd15898: Pssm-ID: 333715 [Multi-domain] Cd Length: 137 Bit Score: 38.42 E-value: 9.36e-03
|
||||||||||||
| Name | Accession | Description | Interval | E-value | ||||||||
| UBP12 | COG5560 | Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
486-1002 | 4.76e-57 | ||||||||
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 214.36 E-value: 4.76e-57
|
||||||||||||
| UCH | pfam00443 | Ubiquitin carboxyl-terminal hydrolase; |
741-972 | 2.45e-43 | ||||||||
Ubiquitin carboxyl-terminal hydrolase; Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 161.07 E-value: 2.45e-43
|
||||||||||||
| Peptidase_C19R | cd02674 | A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1480-1737 | 5.28e-39 | ||||||||
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome. Pssm-ID: 239139 [Multi-domain] Cd Length: 230 Bit Score: 145.89 E-value: 5.28e-39
|
||||||||||||
| UCH | pfam00443 | Ubiquitin carboxyl-terminal hydrolase; |
1490-1736 | 2.09e-26 | ||||||||
Ubiquitin carboxyl-terminal hydrolase; Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 111.77 E-value: 2.09e-26
|
||||||||||||
| Peptidase_C19E | cd02661 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
740-918 | 2.89e-23 | ||||||||
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome. Pssm-ID: 239126 [Multi-domain] Cd Length: 304 Bit Score: 102.35 E-value: 2.89e-23
|
||||||||||||
| UBP12 | COG5560 | Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
1461-1739 | 6.81e-23 | ||||||||
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 106.51 E-value: 6.81e-23
|
||||||||||||
| DUSP | smart00695 | Domain in ubiquitin-specific proteases; |
398-559 | 2.15e-17 | ||||||||
Domain in ubiquitin-specific proteases; Pssm-ID: 197831 Cd Length: 88 Bit Score: 78.55 E-value: 2.15e-17
|
||||||||||||
| EF-hand_7 | pfam13499 | EF-hand domain pair; |
227-290 | 2.74e-07 | ||||||||
EF-hand domain pair; Pssm-ID: 463900 [Multi-domain] Cd Length: 67 Bit Score: 49.17 E-value: 2.74e-07
|
||||||||||||
| EFh | cd00051 | EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ... |
234-290 | 1.20e-06 | ||||||||
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers. Pssm-ID: 238008 [Multi-domain] Cd Length: 63 Bit Score: 47.16 E-value: 1.20e-06
|
||||||||||||
| FRQ1 | COG5126 | Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
228-285 | 1.41e-04 | ||||||||
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 43.63 E-value: 1.41e-04
|
||||||||||||
| EFh_PI-PLC | cd15898 | EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ... |
198-251 | 9.36e-03 | ||||||||
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) isozymes; PI-PLC isozymes are signaling enzymes that hydrolyze the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. This family corresponds to the four EF-hand motifs containing PI-PLC isozymes, including PI-PLC-beta (1-4), -gamma (1-2), -delta (1,3,4), -epsilon (1), -zeta (1), eta (1-2). Lower eukaryotes such as yeast and slime molds contain only delta-type isozymes. In contrast, other types of isoforms present in higher eukaryotes. This family also includes 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase 1 (PLC1) from fungi. Some homologs from plants contain only two atypical EF-hand motifs and they are not included. All PI-PLC isozymes except sperm-specific PI-PLC-zeta share a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C2 domain. PI-PLC-zeta lacks the PH domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. Most of EF-hand motifs found in PI-PLCs consist of a helix-loop-helix structure, but lack residues critical to metal binding. Moreover, the EF-hand region of most of PI-PLCs may have an important regulatory function, but it has yet to be identified. However, PI-PLC-zeta is a key exception. It is responsible for Ca2+ oscillations in fertilized oocytes and exhibits a high sensitivity to Ca2+ mediated through its EF-hand domain. In addition, PI-PLC-eta2 shows a canonical EF-loop directing Ca2+-sensitivity and thus can amplify transient Ca2+ signals. Also it appears that PI-PLC-delta1 can regulate the binding of PH domain to PIP2 in a Ca2+-dependent manner through its functionally important EF-hand domains. PI-PLCs can be activated by a variety of extracellular ligands, such as growth factors, hormones, cytokines and lipids. Their activation has been implicated in tumorigenesis and/or metastasis linked to migration, proliferation, growth, inflammation, angiogenesis and actin cytoskeleton reorganization. PI-PLC-beta isozymes are activated by G-protein coupled receptor (GPCR) through different mechanisms. However, PI-PLC-gamma isozymes are activated by receptor tyrosine kinase (RTK), such as Rho and Ras GTPases. In contrast, PI-PLC-epsilon are activated by both GPCR and RTK. PI-PLC-delta1 and PLC-eta 1 are activated by GPCR-mediated calcium mobilization. The activation mechanism for PI-PLC-zeta remains unclear. Pssm-ID: 320029 [Multi-domain] Cd Length: 137 Bit Score: 38.42 E-value: 9.36e-03
|
||||||||||||
| Name | Accession | Description | Interval | E-value | ||||||||
| UBP12 | COG5560 | Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
486-1002 | 4.76e-57 | ||||||||
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 214.36 E-value: 4.76e-57
|
||||||||||||
| UCH | pfam00443 | Ubiquitin carboxyl-terminal hydrolase; |
741-972 | 2.45e-43 | ||||||||
Ubiquitin carboxyl-terminal hydrolase; Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 161.07 E-value: 2.45e-43
|
||||||||||||
| Peptidase_C19R | cd02674 | A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1480-1737 | 5.28e-39 | ||||||||
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome. Pssm-ID: 239139 [Multi-domain] Cd Length: 230 Bit Score: 145.89 E-value: 5.28e-39
|
||||||||||||
| UCH | pfam00443 | Ubiquitin carboxyl-terminal hydrolase; |
1490-1736 | 2.09e-26 | ||||||||
Ubiquitin carboxyl-terminal hydrolase; Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 111.77 E-value: 2.09e-26
|
||||||||||||
| Peptidase_C19 | cd02257 | Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
1486-1737 | 1.92e-23 | ||||||||
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyse bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome. Pssm-ID: 239072 [Multi-domain] Cd Length: 255 Bit Score: 101.41 E-value: 1.92e-23
|
||||||||||||
| Peptidase_C19E | cd02661 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
740-918 | 2.89e-23 | ||||||||
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome. Pssm-ID: 239126 [Multi-domain] Cd Length: 304 Bit Score: 102.35 E-value: 2.89e-23
|
||||||||||||
| UBP12 | COG5560 | Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
1461-1739 | 6.81e-23 | ||||||||
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 106.51 E-value: 6.81e-23
|
||||||||||||
| Peptidase_C19 | cd02257 | Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
742-972 | 1.48e-21 | ||||||||
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyse bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome. Pssm-ID: 239072 [Multi-domain] Cd Length: 255 Bit Score: 96.01 E-value: 1.48e-21
|
||||||||||||
| Peptidase_C19D | cd02660 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1483-1736 | 7.00e-21 | ||||||||
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome. Pssm-ID: 239125 [Multi-domain] Cd Length: 328 Bit Score: 95.90 E-value: 7.00e-21
|
||||||||||||
| Peptidase_C19R | cd02674 | A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
742-930 | 5.92e-20 | ||||||||
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome. Pssm-ID: 239139 [Multi-domain] Cd Length: 230 Bit Score: 90.81 E-value: 5.92e-20
|
||||||||||||
| Peptidase_C19D | cd02660 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
742-924 | 8.25e-20 | ||||||||
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome. Pssm-ID: 239125 [Multi-domain] Cd Length: 328 Bit Score: 92.82 E-value: 8.25e-20
|
||||||||||||
| Peptidase_C19E | cd02661 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1490-1736 | 1.01e-19 | ||||||||
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome. Pssm-ID: 239126 [Multi-domain] Cd Length: 304 Bit Score: 91.95 E-value: 1.01e-19
|
||||||||||||
| DUSP | smart00695 | Domain in ubiquitin-specific proteases; |
398-559 | 2.15e-17 | ||||||||
Domain in ubiquitin-specific proteases; Pssm-ID: 197831 Cd Length: 88 Bit Score: 78.55 E-value: 2.15e-17
|
||||||||||||
| Peptidase_C19K | cd02667 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
742-924 | 3.48e-16 | ||||||||
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome. Pssm-ID: 239132 [Multi-domain] Cd Length: 279 Bit Score: 80.89 E-value: 3.48e-16
|
||||||||||||
| Peptidase_C19H | cd02664 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
742-929 | 2.85e-14 | ||||||||
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome. Pssm-ID: 239129 [Multi-domain] Cd Length: 327 Bit Score: 75.99 E-value: 2.85e-14
|
||||||||||||
| Peptidase_C19K | cd02667 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1486-1737 | 6.43e-14 | ||||||||
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome. Pssm-ID: 239132 [Multi-domain] Cd Length: 279 Bit Score: 73.96 E-value: 6.43e-14
|
||||||||||||
| peptidase_C19C | cd02659 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1494-1739 | 3.84e-13 | ||||||||
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome. Pssm-ID: 239124 [Multi-domain] Cd Length: 334 Bit Score: 72.68 E-value: 3.84e-13
|
||||||||||||
| Peptidase_C19G | cd02663 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1453-1555 | 5.24e-12 | ||||||||
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome. Pssm-ID: 239128 [Multi-domain] Cd Length: 300 Bit Score: 68.88 E-value: 5.24e-12
|
||||||||||||
| DUSP | pfam06337 | DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the ... |
491-556 | 2.56e-11 | ||||||||
DUSP domain; The DUSP (domain present in ubiquitin-specific protease) domain is found at the N-terminus of Ubiquitin-specific proteases. The structure of this domain has been solved. Its tripod-like structure consists of a 3-fold alpha-helical bundle supporting a triple-stranded anti-parallel beta-sheet. Pssm-ID: 399383 Cd Length: 80 Bit Score: 61.23 E-value: 2.56e-11
|
||||||||||||
| Peptidase_C19B | cd02658 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
742-929 | 3.53e-11 | ||||||||
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome. Pssm-ID: 239123 [Multi-domain] Cd Length: 311 Bit Score: 66.58 E-value: 3.53e-11
|
||||||||||||
| COG5533 | COG5533 | Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
1680-1739 | 3.72e-11 | ||||||||
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 65.98 E-value: 3.72e-11
|
||||||||||||
| Peptidase_C19A | cd02657 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
742-971 | 1.64e-10 | ||||||||
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyse bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome. Pssm-ID: 239122 [Multi-domain] Cd Length: 305 Bit Score: 64.27 E-value: 1.64e-10
|
||||||||||||
| peptidase_C19C | cd02659 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
742-925 | 4.41e-10 | ||||||||
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome. Pssm-ID: 239124 [Multi-domain] Cd Length: 334 Bit Score: 63.43 E-value: 4.41e-10
|
||||||||||||
| Peptidase_C19L | cd02668 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1490-1577 | 2.49e-09 | ||||||||
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome. Pssm-ID: 239133 [Multi-domain] Cd Length: 324 Bit Score: 60.90 E-value: 2.49e-09
|
||||||||||||
| Peptidase_C19F | cd02662 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1678-1737 | 2.59e-08 | ||||||||
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome. Pssm-ID: 239127 [Multi-domain] Cd Length: 240 Bit Score: 56.61 E-value: 2.59e-08
|
||||||||||||
| Peptidase_C19O | cd02671 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
736-846 | 4.67e-08 | ||||||||
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome. Pssm-ID: 239136 [Multi-domain] Cd Length: 332 Bit Score: 56.83 E-value: 4.67e-08
|
||||||||||||
| COG5533 | COG5533 | Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
742-848 | 1.13e-07 | ||||||||
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 55.19 E-value: 1.13e-07
|
||||||||||||
| Peptidase_C19B | cd02658 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1473-1538 | 1.98e-07 | ||||||||
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome. Pssm-ID: 239123 [Multi-domain] Cd Length: 311 Bit Score: 55.02 E-value: 1.98e-07
|
||||||||||||
| EF-hand_7 | pfam13499 | EF-hand domain pair; |
227-290 | 2.74e-07 | ||||||||
EF-hand domain pair; Pssm-ID: 463900 [Multi-domain] Cd Length: 67 Bit Score: 49.17 E-value: 2.74e-07
|
||||||||||||
| Peptidase_C19M | cd02669 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
738-921 | 5.47e-07 | ||||||||
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome. Pssm-ID: 239134 [Multi-domain] Cd Length: 440 Bit Score: 54.25 E-value: 5.47e-07
|
||||||||||||
| EFh | cd00051 | EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ... |
234-290 | 1.20e-06 | ||||||||
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers. Pssm-ID: 238008 [Multi-domain] Cd Length: 63 Bit Score: 47.16 E-value: 1.20e-06
|
||||||||||||
| Peptidase_C19F | cd02662 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
742-921 | 1.18e-05 | ||||||||
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome. Pssm-ID: 239127 [Multi-domain] Cd Length: 240 Bit Score: 48.52 E-value: 1.18e-05
|
||||||||||||
| Peptidase_C19O | cd02671 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1679-1736 | 2.88e-05 | ||||||||
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome. Pssm-ID: 239136 [Multi-domain] Cd Length: 332 Bit Score: 48.35 E-value: 2.88e-05
|
||||||||||||
| Peptidase_C19Q | cd02673 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1678-1737 | 5.98e-05 | ||||||||
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome. Pssm-ID: 239138 [Multi-domain] Cd Length: 245 Bit Score: 46.75 E-value: 5.98e-05
|
||||||||||||
| Peptidase_C19I | cd02665 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1681-1736 | 9.99e-05 | ||||||||
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome. Pssm-ID: 239130 [Multi-domain] Cd Length: 228 Bit Score: 45.63 E-value: 9.99e-05
|
||||||||||||
| Peptidase_C19H | cd02664 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1681-1737 | 1.23e-04 | ||||||||
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome. Pssm-ID: 239129 [Multi-domain] Cd Length: 327 Bit Score: 46.33 E-value: 1.23e-04
|
||||||||||||
| FRQ1 | COG5126 | Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
228-285 | 1.41e-04 | ||||||||
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 43.63 E-value: 1.41e-04
|
||||||||||||
| EFh | cd00051 | EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ... |
198-255 | 1.42e-04 | ||||||||
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers. Pssm-ID: 238008 [Multi-domain] Cd Length: 63 Bit Score: 41.38 E-value: 1.42e-04
|
||||||||||||
| FRQ1 | COG5126 | Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
230-293 | 3.43e-04 | ||||||||
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 42.47 E-value: 3.43e-04
|
||||||||||||
| COG5077 | COG5077 | Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
1670-1739 | 3.65e-04 | ||||||||
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 45.63 E-value: 3.65e-04
|
||||||||||||
| Peptidase_C19M | cd02669 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1508-1577 | 1.11e-03 | ||||||||
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome. Pssm-ID: 239134 [Multi-domain] Cd Length: 440 Bit Score: 43.46 E-value: 1.11e-03
|
||||||||||||
| EFh_SPARC_TICN | cd16232 | EF-hand, extracellular calcium-binding (EC) motif, found in testicans; Testicans are nervous ... |
186-285 | 3.75e-03 | ||||||||
EF-hand, extracellular calcium-binding (EC) motif, found in testicans; Testicans are nervous system-expressed proteoglycans that play important roles in the regulation of protease activity, as well as in the determination of age at menarche. Testican-1 (TICN1, also termed protein SPOCK) is a secreted chimeric proteoglycan that is highly expressed in brain and carries both chondroitin and heparan sulfate glycosaminoglycan side chains. It has been implicated in autoimmune disease. It also acts as a regulator of bone morphogenetic protein (BMP) signaling and show critical functions in the nervous system. Testican-2 (TICN2, also termed protein SPOCK2) is an extracellular heparan sulphate proteoglycan highly expressed in brain. It may play regulatory roles in the development of the central nervous system. It also participates in diverse steps of neurogenesis. TICN1, but not TICN2, inhibits cathepsin L. TICN1 also inhibits attachment and neurite outgrowth in cultures of N2A neuroblastoma cells, While TICN2 is able to inhibit neurite outgrowth from primary cerebellar cells. Testicans contain an N-terminal signal peptide, a testican-specific domain followed by a follistatin-like (FS) domain, an extracellular calcium-binding (EC) domain including a pair of EF hands, a thyroglobulin-like domain (TY), and a C-terminal region with two putative glycosaminoglycan attachment sites. The substitution of a ligating Asp residue by Tyr orTyr in the +Y position of EF hand 2 in testican-2 could prevent Ca2+ binding to this site and also cause EF-hand 1 to bind one Ca2+ with low affinity. The substitution of a ligating Asp residue by Phe or Tyr in the +Y position of EF-hand 2 in testicans could prevent Ca2+ binding to this site and also cause EF-hand 1 to bind one Ca2+ ion with low affinity. Pssm-ID: 320011 Cd Length: 108 Bit Score: 38.89 E-value: 3.75e-03
|
||||||||||||
| Peptidase_C19J | cd02666 | A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1661-1747 | 3.82e-03 | ||||||||
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome. Pssm-ID: 239131 [Multi-domain] Cd Length: 343 Bit Score: 41.71 E-value: 3.82e-03
|
||||||||||||
| EFh_PEF_Group_I | cd16180 | Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ... |
233-285 | 6.58e-03 | ||||||||
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds to Group I PEF proteins that have been found not only in higher animals but also in lower animals, plants, fungi and protists. Group I PEF proteins include apoptosis-linked gene 2 protein (ALG-2), peflin and similar proteins. ALG-2, also termed programmed cell death protein 6 (PDCD6), is a widely expressed calcium-binding modulator protein associated with cell proliferation and death, as well as cell survival. It forms a homodimer in the cell or a heterodimer with its closest paralog peflin. Among the PEF proteins, ALG-2 can bind three Ca2+ ions through its EF1, EF3, and EF5 hands, where it is unique in that its EF5 hand binds Ca2+ ion in a canonical coordination. Peflin is a ubiquitously expressed 30-kD PEF protein containing five EF-hand motifs in its C-terminal domain and a longer N-terminal hydrophobic domain (NHB domain) than any other member of the PEF family. The NHB domain harbors nine repeats of a nonapeptide (A/PPGGPYGGP). Peflin may modulate the function of ALG-2 in Ca2+ signaling. It exists only as a heterodimer with ALG-2, and binds two Ca2+ ions through its EF1 and EF3 hands. Its additional EF5 hand is unpaired and does not bind Ca2+ ion but mediates the heterodimerization with ALG-2. The dissociation of heterodimer occurs in the presence of Ca2+. Pssm-ID: 320055 [Multi-domain] Cd Length: 164 Bit Score: 39.43 E-value: 6.58e-03
|
||||||||||||
| EFh_PI-PLC | cd15898 | EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ... |
198-251 | 9.36e-03 | ||||||||
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) isozymes; PI-PLC isozymes are signaling enzymes that hydrolyze the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. This family corresponds to the four EF-hand motifs containing PI-PLC isozymes, including PI-PLC-beta (1-4), -gamma (1-2), -delta (1,3,4), -epsilon (1), -zeta (1), eta (1-2). Lower eukaryotes such as yeast and slime molds contain only delta-type isozymes. In contrast, other types of isoforms present in higher eukaryotes. This family also includes 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase 1 (PLC1) from fungi. Some homologs from plants contain only two atypical EF-hand motifs and they are not included. All PI-PLC isozymes except sperm-specific PI-PLC-zeta share a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C2 domain. PI-PLC-zeta lacks the PH domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. Most of EF-hand motifs found in PI-PLCs consist of a helix-loop-helix structure, but lack residues critical to metal binding. Moreover, the EF-hand region of most of PI-PLCs may have an important regulatory function, but it has yet to be identified. However, PI-PLC-zeta is a key exception. It is responsible for Ca2+ oscillations in fertilized oocytes and exhibits a high sensitivity to Ca2+ mediated through its EF-hand domain. In addition, PI-PLC-eta2 shows a canonical EF-loop directing Ca2+-sensitivity and thus can amplify transient Ca2+ signals. Also it appears that PI-PLC-delta1 can regulate the binding of PH domain to PIP2 in a Ca2+-dependent manner through its functionally important EF-hand domains. PI-PLCs can be activated by a variety of extracellular ligands, such as growth factors, hormones, cytokines and lipids. Their activation has been implicated in tumorigenesis and/or metastasis linked to migration, proliferation, growth, inflammation, angiogenesis and actin cytoskeleton reorganization. PI-PLC-beta isozymes are activated by G-protein coupled receptor (GPCR) through different mechanisms. However, PI-PLC-gamma isozymes are activated by receptor tyrosine kinase (RTK), such as Rho and Ras GTPases. In contrast, PI-PLC-epsilon are activated by both GPCR and RTK. PI-PLC-delta1 and PLC-eta 1 are activated by GPCR-mediated calcium mobilization. The activation mechanism for PI-PLC-zeta remains unclear. Pssm-ID: 320029 [Multi-domain] Cd Length: 137 Bit Score: 38.42 E-value: 9.36e-03
|
||||||||||||
| Blast search parameters | ||||
|
