phosphatidylserine decarboxylase 2 [Arabidopsis thaliana]
Protein Classification
PLN02964 family protein( domain architecture ID 11477332)
PLN02964 family protein
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||||||
| PLN02964 | PLN02964 | phosphatidylserine decarboxylase |
1-585 | 0e+00 | |||||||||
phosphatidylserine decarboxylase : Pssm-ID: 215520 [Multi-domain] Cd Length: 644 Bit Score: 1202.76 E-value: 0e+00
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| Name | Accession | Description | Interval | E-value | |||||||||
| PLN02964 | PLN02964 | phosphatidylserine decarboxylase |
1-585 | 0e+00 | |||||||||
phosphatidylserine decarboxylase Pssm-ID: 215520 [Multi-domain] Cd Length: 644 Bit Score: 1202.76 E-value: 0e+00
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| Psd | COG0688 | Phosphatidylserine decarboxylase [Lipid transport and metabolism]; Phosphatidylserine ... |
384-584 | 6.32e-63 | |||||||||
Phosphatidylserine decarboxylase [Lipid transport and metabolism]; Phosphatidylserine decarboxylase is part of the Pathway/BioSystem: Phospholipid biosynthesis Pssm-ID: 440452 [Multi-domain] Cd Length: 243 Bit Score: 207.40 E-value: 6.32e-63
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| PS_Dcarbxylase | pfam02666 | Phosphatidylserine decarboxylase; This is a family of phosphatidylserine decarboxylases, EC:4. ... |
414-584 | 4.22e-56 | |||||||||
Phosphatidylserine decarboxylase; This is a family of phosphatidylserine decarboxylases, EC:4.1.1.65. These enzymes catalyze the reaction: Phosphatidyl-L-serine <=> phosphatidylethanolamine + CO2. Phosphatidylserine decarboxylase plays a central role in the biosynthesis of aminophospholipids by converting phosphatidylserine to phosphatidylethanolamine. Pssm-ID: 396989 [Multi-domain] Cd Length: 198 Bit Score: 187.49 E-value: 4.22e-56
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| PS_decarb | TIGR00163 | phosphatidylserine decarboxylase precursor; Phosphatidylserine decarboxylase is synthesized as ... |
401-566 | 1.42e-31 | |||||||||
phosphatidylserine decarboxylase precursor; Phosphatidylserine decarboxylase is synthesized as a single chain precursor. Generation of the pyruvoyl active site from a Ser is coupled to cleavage of a Gly-Ser bond between the larger (beta) and smaller (alpha chains). It is an integral membrane protein. A closely related family, possibly also active as phosphatidylserine decarboxylase, falls under model TIGR00164. [Fatty acid and phospholipid metabolism, Biosynthesis] Pssm-ID: 272936 [Multi-domain] Cd Length: 238 Bit Score: 122.63 E-value: 1.42e-31
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| EFh | cd00051 | EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ... |
179-240 | 1.20e-08 | |||||||||
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: 51.39 E-value: 1.20e-08
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| XopAW | NF041410 | XopAW family type III secretion system calcium-binding effector; |
179-247 | 5.23e-07 | |||||||||
XopAW family type III secretion system calcium-binding effector; Pssm-ID: 469301 [Multi-domain] Cd Length: 227 Bit Score: 50.83 E-value: 5.23e-07
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| XopAW | NF041410 | XopAW family type III secretion system calcium-binding effector; |
183-240 | 5.16e-06 | |||||||||
XopAW family type III secretion system calcium-binding effector; Pssm-ID: 469301 [Multi-domain] Cd Length: 227 Bit Score: 47.75 E-value: 5.16e-06
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| XopAW | NF041410 | XopAW family type III secretion system calcium-binding effector; |
177-242 | 7.44e-04 | |||||||||
XopAW family type III secretion system calcium-binding effector; Pssm-ID: 469301 [Multi-domain] Cd Length: 227 Bit Score: 41.20 E-value: 7.44e-04
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| Name | Accession | Description | Interval | E-value | |||||||||
| PLN02964 | PLN02964 | phosphatidylserine decarboxylase |
1-585 | 0e+00 | |||||||||
phosphatidylserine decarboxylase Pssm-ID: 215520 [Multi-domain] Cd Length: 644 Bit Score: 1202.76 E-value: 0e+00
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| PRK00723 | PRK00723 | phosphatidylserine decarboxylase; Provisional |
323-584 | 1.31e-67 | |||||||||
phosphatidylserine decarboxylase; Provisional Pssm-ID: 179097 [Multi-domain] Cd Length: 297 Bit Score: 221.33 E-value: 1.31e-67
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| Psd | COG0688 | Phosphatidylserine decarboxylase [Lipid transport and metabolism]; Phosphatidylserine ... |
384-584 | 6.32e-63 | |||||||||
Phosphatidylserine decarboxylase [Lipid transport and metabolism]; Phosphatidylserine decarboxylase is part of the Pathway/BioSystem: Phospholipid biosynthesis Pssm-ID: 440452 [Multi-domain] Cd Length: 243 Bit Score: 207.40 E-value: 6.32e-63
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| PS_Dcarbxylase | pfam02666 | Phosphatidylserine decarboxylase; This is a family of phosphatidylserine decarboxylases, EC:4. ... |
414-584 | 4.22e-56 | |||||||||
Phosphatidylserine decarboxylase; This is a family of phosphatidylserine decarboxylases, EC:4.1.1.65. These enzymes catalyze the reaction: Phosphatidyl-L-serine <=> phosphatidylethanolamine + CO2. Phosphatidylserine decarboxylase plays a central role in the biosynthesis of aminophospholipids by converting phosphatidylserine to phosphatidylethanolamine. Pssm-ID: 396989 [Multi-domain] Cd Length: 198 Bit Score: 187.49 E-value: 4.22e-56
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| psd | PRK00044 | phosphatidylserine decarboxylase; Reviewed |
388-584 | 2.12e-39 | |||||||||
phosphatidylserine decarboxylase; Reviewed Pssm-ID: 234591 Cd Length: 288 Bit Score: 145.74 E-value: 2.12e-39
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| PRK03140 | PRK03140 | phosphatidylserine decarboxylase; Provisional |
388-584 | 7.62e-36 | |||||||||
phosphatidylserine decarboxylase; Provisional Pssm-ID: 179544 [Multi-domain] Cd Length: 259 Bit Score: 135.12 E-value: 7.62e-36
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| PS_decarb | TIGR00163 | phosphatidylserine decarboxylase precursor; Phosphatidylserine decarboxylase is synthesized as ... |
401-566 | 1.42e-31 | |||||||||
phosphatidylserine decarboxylase precursor; Phosphatidylserine decarboxylase is synthesized as a single chain precursor. Generation of the pyruvoyl active site from a Ser is coupled to cleavage of a Gly-Ser bond between the larger (beta) and smaller (alpha chains). It is an integral membrane protein. A closely related family, possibly also active as phosphatidylserine decarboxylase, falls under model TIGR00164. [Fatty acid and phospholipid metabolism, Biosynthesis] Pssm-ID: 272936 [Multi-domain] Cd Length: 238 Bit Score: 122.63 E-value: 1.42e-31
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| PRK03934 | PRK03934 | phosphatidylserine decarboxylase; Provisional |
394-582 | 3.79e-22 | |||||||||
phosphatidylserine decarboxylase; Provisional Pssm-ID: 235177 [Multi-domain] Cd Length: 265 Bit Score: 96.17 E-value: 3.79e-22
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| PRK09629 | PRK09629 | bifunctional thiosulfate sulfurtransferase/phosphatidylserine decarboxylase; Provisional |
398-566 | 1.06e-17 | |||||||||
bifunctional thiosulfate sulfurtransferase/phosphatidylserine decarboxylase; Provisional Pssm-ID: 104071 [Multi-domain] Cd Length: 610 Bit Score: 86.71 E-value: 1.06e-17
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| PTZ00403 | PTZ00403 | phosphatidylserine decarboxylase; Provisional |
399-569 | 1.78e-17 | |||||||||
phosphatidylserine decarboxylase; Provisional Pssm-ID: 173594 Cd Length: 353 Bit Score: 84.13 E-value: 1.78e-17
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| PLN02938 | PLN02938 | phosphatidylserine decarboxylase |
400-583 | 5.08e-16 | |||||||||
phosphatidylserine decarboxylase Pssm-ID: 178526 Cd Length: 428 Bit Score: 80.64 E-value: 5.08e-16
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| FRQ1 | COG5126 | Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
163-240 | 3.08e-10 | |||||||||
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 58.26 E-value: 3.08e-10
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| EFh | cd00051 | EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ... |
179-240 | 1.20e-08 | |||||||||
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: 51.39 E-value: 1.20e-08
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| FRQ1 | COG5126 | Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
176-240 | 1.78e-08 | |||||||||
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 53.26 E-value: 1.78e-08
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| XopAW | NF041410 | XopAW family type III secretion system calcium-binding effector; |
179-247 | 5.23e-07 | |||||||||
XopAW family type III secretion system calcium-binding effector; Pssm-ID: 469301 [Multi-domain] Cd Length: 227 Bit Score: 50.83 E-value: 5.23e-07
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| EFh_CREC | cd15899 | EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin ... |
170-235 | 5.93e-07 | |||||||||
EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin/ERC45/calumenin)-EF hand family contains a group of six EF-hand, low-affinity Ca2+-binding proteins, including reticulocalbin (RCN-1), ER Ca2+-binding protein of 55 kDa (ERC-55, also known as TCBP-49 or E6BP), reticulocalbin-3 (RCN-3), Ca2+-binding protein of 45 kDa (Cab45 and its splice variant Cab45b), and calumenin ( also known as crocalbin or CBP-50). The proteins are not only localized in various parts of the secretory pathway, but also found in the cytosolic compartment and at the cell surface. They interact with different ligands or proteins and have been implicated in the secretory process, chaperone activity, signal transduction as well as in a large variety of disease processes. Pssm-ID: 320021 [Multi-domain] Cd Length: 267 Bit Score: 51.29 E-value: 5.93e-07
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| XopAW | NF041410 | XopAW family type III secretion system calcium-binding effector; |
183-240 | 5.16e-06 | |||||||||
XopAW family type III secretion system calcium-binding effector; Pssm-ID: 469301 [Multi-domain] Cd Length: 227 Bit Score: 47.75 E-value: 5.16e-06
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| EF-hand_7 | pfam13499 | EF-hand domain pair; |
179-239 | 2.01e-05 | |||||||||
EF-hand domain pair; Pssm-ID: 463900 [Multi-domain] Cd Length: 67 Bit Score: 42.63 E-value: 2.01e-05
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| EFh_PI-PLC | cd15898 | EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ... |
178-239 | 3.34e-05 | |||||||||
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: 43.81 E-value: 3.34e-05
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| EFh_CREC_cab45 | cd16225 | EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also ... |
169-234 | 5.15e-05 | |||||||||
EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also termed stromal cell-derived factor 4 (SDF-4), is a soluble, lumenal Golgi resident low-affinity Ca2+-binding protein that contains six copies of the EF-hand Ca2+-binding motif. It is required for secretory pathway calcium ATPase1 (SPCA1)-dependent Ca2+ import into the trans-Golgi network (TGN) and plays an essential role in Ca2+-dependent secretory cargo sorting at the TGN. Pssm-ID: 320023 [Multi-domain] Cd Length: 278 Bit Score: 45.37 E-value: 5.15e-05
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| EFh_CREC_cab45 | cd16225 | EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also ... |
176-235 | 8.59e-05 | |||||||||
EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also termed stromal cell-derived factor 4 (SDF-4), is a soluble, lumenal Golgi resident low-affinity Ca2+-binding protein that contains six copies of the EF-hand Ca2+-binding motif. It is required for secretory pathway calcium ATPase1 (SPCA1)-dependent Ca2+ import into the trans-Golgi network (TGN) and plays an essential role in Ca2+-dependent secretory cargo sorting at the TGN. Pssm-ID: 320023 [Multi-domain] Cd Length: 278 Bit Score: 44.60 E-value: 8.59e-05
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| EF-hand_8 | pfam13833 | EF-hand domain pair; |
190-242 | 1.59e-04 | |||||||||
EF-hand domain pair; Pssm-ID: 404678 [Multi-domain] Cd Length: 54 Bit Score: 39.61 E-value: 1.59e-04
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| C2 | cd00030 | C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ... |
77-144 | 2.80e-04 | |||||||||
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Pssm-ID: 175973 [Multi-domain] Cd Length: 102 Bit Score: 40.51 E-value: 2.80e-04
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| C2_NEDD4_NEDD4L | cd04033 | C2 domain present in the Human neural precursor cell-expressed, developmentally down-regulated ... |
81-167 | 3.08e-04 | |||||||||
C2 domain present in the Human neural precursor cell-expressed, developmentally down-regulated 4 (NEDD4) and NEDD4-like (NEDD4L/NEDD42); Nedd4 and Nedd4-2 are two of the nine members of the Human Nedd4 family. All vertebrates appear to have both Nedd4 and Nedd4-2 genes. They are thought to participate in the regulation of epithelial Na+ channel (ENaC) activity. They also have identical specificity for ubiquitin conjugating enzymes (E2). Nedd4 and Nedd4-2 are composed of a C2 domain, 2-4 WW domains, and a ubiquitin ligase Hect domain. Their WW domains can bind PPxY (PY) or LPSY motifs, and in vitro studies suggest that WW3 and WW4 of both proteins bind PY motifs in the key substrates, with WW3 generally exhibiting higher affinity. Most Nedd4 family members, especially Nedd4-2, also have multiple splice variants, which might play different roles in regulating their substrates. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Pssm-ID: 175999 [Multi-domain] Cd Length: 133 Bit Score: 41.18 E-value: 3.08e-04
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| FRQ1 | COG5126 | Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
173-245 | 4.18e-04 | |||||||||
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 40.93 E-value: 4.18e-04
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| XopAW | NF041410 | XopAW family type III secretion system calcium-binding effector; |
177-242 | 7.44e-04 | |||||||||
XopAW family type III secretion system calcium-binding effector; Pssm-ID: 469301 [Multi-domain] Cd Length: 227 Bit Score: 41.20 E-value: 7.44e-04
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| C2 | pfam00168 | C2 domain; |
73-143 | 1.76e-03 | |||||||||
C2 domain; Pssm-ID: 425499 [Multi-domain] Cd Length: 104 Bit Score: 38.07 E-value: 1.76e-03
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| EF-hand_5 | pfam13202 | EF hand; |
216-239 | 2.64e-03 | |||||||||
EF hand; Pssm-ID: 433035 [Multi-domain] Cd Length: 25 Bit Score: 35.37 E-value: 2.64e-03
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| EFh_PI-PLC | cd15898 | EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ... |
172-246 | 4.63e-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: 37.65 E-value: 4.63e-03
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| EFh_CREC_RCN2_like | cd16227 | EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This ... |
186-237 | 8.03e-03 | |||||||||
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This family corresponds to a group of uncharacterized RCN2-like proteins, which are mainly found in protostomes. Although their biological function remains unclear, they show high sequence similarity with RCN2 (also known as E6BP or TCBP-49), which is an endoplasmic reticulum resident low-affinity Ca2+-binding protein that has been implicated in immunity, redox homeostasis, cell cycle regulation and coagulation. Members in this family contain six copies of the EF-hand Ca2+-binding motif, but may lack a C-terminal His-Asp-Glu-Leu (HDEL) tetrapeptide that is required for retention of RCN2 in the endoplasmic reticulum (ER). Pssm-ID: 320025 [Multi-domain] Cd Length: 263 Bit Score: 38.45 E-value: 8.03e-03
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| Dockerin_II | cd14254 | Type II dockerin repeat domain; Bacterial cohesin domains bind to a complementary protein ... |
187-238 | 8.24e-03 | |||||||||
Type II dockerin repeat domain; Bacterial cohesin domains bind to a complementary protein domain named dockerin, and this interaction is required for the formation of the cellulosome, a cellulose-degrading complex. The cellulosome consists of scaffoldin, a noncatalytic scaffolding polypeptide, that comprises repeating cohesion modules and a single carbohydrate-binding module (CBM). Specific calcium-dependent interactions between cohesins and dockerins appear to be essential for cellulosome assembly. This subfamily represents type II dockerins, which are responsible for mediating attachment of the cellulosome complex to the bacterial cell wall. Pssm-ID: 271213 Cd Length: 54 Bit Score: 34.87 E-value: 8.24e-03
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