RecName: Full=Filaggrin-2; Short=FLG-2; AltName: Full=Intermediate filament-associated protein
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||||
| S-100 | cd00213 | S-100: S-100 domain, which represents the largest family within the superfamily of proteins ... |
4-87 | 3.27e-35 | |||||||
S-100: S-100 domain, which represents the largest family within the superfamily of proteins carrying the Ca-binding EF-hand motif. Note that this S-100 hierarchy contains only S-100 EF-hand domains, other EF-hands have been modeled separately. S100 proteins are expressed exclusively in vertebrates, and are implicated in intracellular and extracellular regulatory activities. Intracellularly, S100 proteins act as Ca-signaling or Ca-buffering proteins. The most unusual characteristic of certain S100 proteins is their occurrence in extracellular space, where they act in a cytokine-like manner through RAGE, the receptor for advanced glycation products. Structural data suggest that many S100 members exist within cells as homo- or heterodimers and even oligomers; oligomerization contributes to their functional diversification. Upon binding calcium, most S100 proteins change conformation to a more open structure exposing a hydrophobic cleft. This hydrophobic surface represents the interaction site of S100 proteins with their target proteins. There is experimental evidence showing that many S100 proteins have multiple binding partners with diverse mode of interaction with different targets. In addition to S100 proteins (such as S100A1,-3,-4,-6,-7,-10,-11,and -13), this group includes the ''fused'' gene family, a group of calcium binding S100-related proteins. The ''fused'' gene family includes multifunctional epidermal differentiation proteins - profilaggrin, trichohyalin, repetin, hornerin, and cornulin; functionally these proteins are associated with keratin intermediate filaments and partially crosslinked to the cell envelope. These ''fused'' gene proteins contain N-terminal sequence with two Ca-binding EF-hands motif, which may be associated with calcium signaling in epidermal cells and autoprocessing in a calcium-dependent manner. In contrast to S100 proteins, "fused" gene family proteins contain an extraordinary high number of almost perfect peptide repeats with regular array of polar and charged residues similar to many known cell envelope proteins. : Pssm-ID: 238131 [Multi-domain] Cd Length: 88 Bit Score: 129.92 E-value: 3.27e-35
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| ser_rich_anae_1 super family | cl41472 | serine-rich protein; This serine-rich protein belongs to a family with large size (over 1000 ... |
681-965 | 4.21e-08 | |||||||
serine-rich protein; This serine-rich protein belongs to a family with large size (over 1000 amino acids), which a highly serine-rich central region that averages over 300 aa in length. Species encoding members of this family of proteins tend to be anaerobic bacteria, including Gram-positive bacteria of the human gut microbiome and Chloroflexi from marine sediments. The actual alignment was detected with superfamily member NF033849: Pssm-ID: 468206 [Multi-domain] Cd Length: 1122 Bit Score: 58.86 E-value: 4.21e-08
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| PHA03307 super family | cl33723 | transcriptional regulator ICP4; Provisional |
1475-1878 | 9.01e-07 | |||||||
transcriptional regulator ICP4; Provisional The actual alignment was detected with superfamily member PHA03307: Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 54.79 E-value: 9.01e-07
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| PTZ00449 super family | cl33186 | 104 kDa microneme/rhoptry antigen; Provisional |
1095-1420 | 2.29e-05 | |||||||
104 kDa microneme/rhoptry antigen; Provisional The actual alignment was detected with superfamily member PTZ00449: Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 50.07 E-value: 2.29e-05
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| PTZ00449 super family | cl33186 | 104 kDa microneme/rhoptry antigen; Provisional |
1810-1997 | 9.00e-05 | |||||||
104 kDa microneme/rhoptry antigen; Provisional The actual alignment was detected with superfamily member PTZ00449: Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 48.15 E-value: 9.00e-05
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| Name | Accession | Description | Interval | E-value | |||||||
| S-100 | cd00213 | S-100: S-100 domain, which represents the largest family within the superfamily of proteins ... |
4-87 | 3.27e-35 | |||||||
S-100: S-100 domain, which represents the largest family within the superfamily of proteins carrying the Ca-binding EF-hand motif. Note that this S-100 hierarchy contains only S-100 EF-hand domains, other EF-hands have been modeled separately. S100 proteins are expressed exclusively in vertebrates, and are implicated in intracellular and extracellular regulatory activities. Intracellularly, S100 proteins act as Ca-signaling or Ca-buffering proteins. The most unusual characteristic of certain S100 proteins is their occurrence in extracellular space, where they act in a cytokine-like manner through RAGE, the receptor for advanced glycation products. Structural data suggest that many S100 members exist within cells as homo- or heterodimers and even oligomers; oligomerization contributes to their functional diversification. Upon binding calcium, most S100 proteins change conformation to a more open structure exposing a hydrophobic cleft. This hydrophobic surface represents the interaction site of S100 proteins with their target proteins. There is experimental evidence showing that many S100 proteins have multiple binding partners with diverse mode of interaction with different targets. In addition to S100 proteins (such as S100A1,-3,-4,-6,-7,-10,-11,and -13), this group includes the ''fused'' gene family, a group of calcium binding S100-related proteins. The ''fused'' gene family includes multifunctional epidermal differentiation proteins - profilaggrin, trichohyalin, repetin, hornerin, and cornulin; functionally these proteins are associated with keratin intermediate filaments and partially crosslinked to the cell envelope. These ''fused'' gene proteins contain N-terminal sequence with two Ca-binding EF-hands motif, which may be associated with calcium signaling in epidermal cells and autoprocessing in a calcium-dependent manner. In contrast to S100 proteins, "fused" gene family proteins contain an extraordinary high number of almost perfect peptide repeats with regular array of polar and charged residues similar to many known cell envelope proteins. Pssm-ID: 238131 [Multi-domain] Cd Length: 88 Bit Score: 129.92 E-value: 3.27e-35
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| S_100 | pfam01023 | S-100/ICaBP type calcium binding domain; The S-100 domain is a subfamily of the EF-hand ... |
4-48 | 5.30e-15 | |||||||
S-100/ICaBP type calcium binding domain; The S-100 domain is a subfamily of the EF-hand calcium binding proteins. Pssm-ID: 460028 Cd Length: 45 Bit Score: 70.93 E-value: 5.30e-15
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| ser_rich_anae_1 | NF033849 | serine-rich protein; This serine-rich protein belongs to a family with large size (over 1000 ... |
681-965 | 4.21e-08 | |||||||
serine-rich protein; This serine-rich protein belongs to a family with large size (over 1000 amino acids), which a highly serine-rich central region that averages over 300 aa in length. Species encoding members of this family of proteins tend to be anaerobic bacteria, including Gram-positive bacteria of the human gut microbiome and Chloroflexi from marine sediments. Pssm-ID: 468206 [Multi-domain] Cd Length: 1122 Bit Score: 58.86 E-value: 4.21e-08
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| PHA03307 | PHA03307 | transcriptional regulator ICP4; Provisional |
1475-1878 | 9.01e-07 | |||||||
transcriptional regulator ICP4; Provisional Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 54.79 E-value: 9.01e-07
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| PTZ00449 | PTZ00449 | 104 kDa microneme/rhoptry antigen; Provisional |
1095-1420 | 2.29e-05 | |||||||
104 kDa microneme/rhoptry antigen; Provisional Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 50.07 E-value: 2.29e-05
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| PTZ00449 | PTZ00449 | 104 kDa microneme/rhoptry antigen; Provisional |
1810-1997 | 9.00e-05 | |||||||
104 kDa microneme/rhoptry antigen; Provisional Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 48.15 E-value: 9.00e-05
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| ser_rich_anae_1 | NF033849 | serine-rich protein; This serine-rich protein belongs to a family with large size (over 1000 ... |
629-835 | 4.32e-03 | |||||||
serine-rich protein; This serine-rich protein belongs to a family with large size (over 1000 amino acids), which a highly serine-rich central region that averages over 300 aa in length. Species encoding members of this family of proteins tend to be anaerobic bacteria, including Gram-positive bacteria of the human gut microbiome and Chloroflexi from marine sediments. Pssm-ID: 468206 [Multi-domain] Cd Length: 1122 Bit Score: 42.30 E-value: 4.32e-03
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| Name | Accession | Description | Interval | E-value | |||||||
| S-100 | cd00213 | S-100: S-100 domain, which represents the largest family within the superfamily of proteins ... |
4-87 | 3.27e-35 | |||||||
S-100: S-100 domain, which represents the largest family within the superfamily of proteins carrying the Ca-binding EF-hand motif. Note that this S-100 hierarchy contains only S-100 EF-hand domains, other EF-hands have been modeled separately. S100 proteins are expressed exclusively in vertebrates, and are implicated in intracellular and extracellular regulatory activities. Intracellularly, S100 proteins act as Ca-signaling or Ca-buffering proteins. The most unusual characteristic of certain S100 proteins is their occurrence in extracellular space, where they act in a cytokine-like manner through RAGE, the receptor for advanced glycation products. Structural data suggest that many S100 members exist within cells as homo- or heterodimers and even oligomers; oligomerization contributes to their functional diversification. Upon binding calcium, most S100 proteins change conformation to a more open structure exposing a hydrophobic cleft. This hydrophobic surface represents the interaction site of S100 proteins with their target proteins. There is experimental evidence showing that many S100 proteins have multiple binding partners with diverse mode of interaction with different targets. In addition to S100 proteins (such as S100A1,-3,-4,-6,-7,-10,-11,and -13), this group includes the ''fused'' gene family, a group of calcium binding S100-related proteins. The ''fused'' gene family includes multifunctional epidermal differentiation proteins - profilaggrin, trichohyalin, repetin, hornerin, and cornulin; functionally these proteins are associated with keratin intermediate filaments and partially crosslinked to the cell envelope. These ''fused'' gene proteins contain N-terminal sequence with two Ca-binding EF-hands motif, which may be associated with calcium signaling in epidermal cells and autoprocessing in a calcium-dependent manner. In contrast to S100 proteins, "fused" gene family proteins contain an extraordinary high number of almost perfect peptide repeats with regular array of polar and charged residues similar to many known cell envelope proteins. Pssm-ID: 238131 [Multi-domain] Cd Length: 88 Bit Score: 129.92 E-value: 3.27e-35
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| S-100A10_like | cd05031 | S-100A10_like: S-100A10 domain found in proteins similar to S100A10. S100A10 is a member of ... |
4-87 | 4.25e-20 | |||||||
S-100A10_like: S-100A10 domain found in proteins similar to S100A10. S100A10 is a member of the S100 family of EF-hand superfamily of calcium-binding proteins. Note that the S-100 hierarchy, to which this S-100A1_like group belongs, contains only S-100 EF-hand domains, other EF-hands have been modeled separately. S100 proteins are expressed exclusively in vertebrates, and are implicated in intracellular and extracellular regulatory activities. A unique feature of S100A10 is that it contains mutation in both of the calcium binding sites, making it calcium insensitive. S100A10 has been detected in brain, heart, gastrointestinal tract, kidney, liver, lung, spleen, testes, epidermis, aorta, and thymus. Structural data supports the homo- and hetero-dimeric as well as hetero-tetrameric nature of the protein. S100A10 has multiple binding partners in its calcium free state and is therefore involved in many diverse biological functions. Pssm-ID: 240157 [Multi-domain] Cd Length: 94 Bit Score: 87.09 E-value: 4.25e-20
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| calgranulins | cd05030 | Calgranulins: S-100 domain found in proteins belonging to the Calgranulin subgroup of the S100 ... |
4-87 | 6.93e-16 | |||||||
Calgranulins: S-100 domain found in proteins belonging to the Calgranulin subgroup of the S100 family of EF-hand calcium-modulated proteins, including S100A8, S100A9, and S100A12 . Note that the S-100 hierarchy, to which this Calgranulin group belongs, contains only S-100 EF-hand domains, other EF-hands have been modeled separately. These proteins are expressed mainly in granulocytes, and are involved in inflammation, allergy, and neuritogenesis, as well as in host-parasite response. Calgranulins are modulated not only by calcium, but also by other metals such as zinc and copper. Structural data suggested that calgranulins may exist in multiple structural forms, homodimers, as well as hetero-oligomers. For example, the S100A8/S100A9 complex called calprotectin plays important roles in the regulation of inflammatory processes, wound repair, and regulating zinc-dependent enzymes as well as microbial growth. Pssm-ID: 240156 [Multi-domain] Cd Length: 88 Bit Score: 74.69 E-value: 6.93e-16
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| S_100 | pfam01023 | S-100/ICaBP type calcium binding domain; The S-100 domain is a subfamily of the EF-hand ... |
4-48 | 5.30e-15 | |||||||
S-100/ICaBP type calcium binding domain; The S-100 domain is a subfamily of the EF-hand calcium binding proteins. Pssm-ID: 460028 Cd Length: 45 Bit Score: 70.93 E-value: 5.30e-15
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| S-100Z | cd05026 | S-100Z: S-100Z domain found in proteins similar to S100Z. S100Z is a member of the S100 domain ... |
10-86 | 2.33e-14 | |||||||
S-100Z: S-100Z domain found in proteins similar to S100Z. S100Z is a member of the S100 domain family within the EF-hand Ca2+-binding proteins superfamily. Note that the S-100 hierarchy, to which this S-100Z group belongs, contains only S-100 EF-hand domains, other EF-hands have been modeled separately.S100 proteins exhibit unique patterns of tissue- and cell type-specific expression and have been implicated in the Ca2+-dependent regulation of diverse physiological processes, including cell cycle regulation, differentiation, growth, and metabolic control. S100Z is normally expressed in various tissues, with its highest level of expression being in spleen and leukocytes. The function of S100Z remains unclear. Preliminary structural data suggests that S100Z is homodimer, however a heterodimer with S100P has been reported. S100Z is capable of binding calcium ions. When calcium binds to S110Z, the protein experiences a conformational change, which exposes hydrophobic surfaces on the protein. In comparison with their normal tissue counterparts, S100Z gene expression appears to be deregulated in some tumor tissues. Pssm-ID: 240153 [Multi-domain] Cd Length: 93 Bit Score: 70.67 E-value: 2.33e-14
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| S-100A1 | cd05025 | S-100A1: S-100A1 domain found in proteins similar to S100A1. S100A1 is a calcium-binding ... |
10-87 | 4.99e-14 | |||||||
S-100A1: S-100A1 domain found in proteins similar to S100A1. S100A1 is a calcium-binding protein belonging to a large S100 vertebrate-specific protein family within the EF-hand superfamily of calcium-binding proteins. Note that the S-100 hierarchy, to which this S-100A1 group belongs, contains only S-100 EF-hand domains, other EF-hands have been modeled separately. As is the case with many other members of S100 protein family, S100A1 is implicated in intracellular and extracellular regulatory activities, including interaction with myosin-associated twitchin kinase, actin-capping protein CapZ, sinapsin I, and tubulin. Structural data suggests that S100A1 proteins exist within cells as antiparallel homodimers, while heterodimers with S100A4 and S100B also has been reported. Upon binding calcium S100A1 changes conformation to expose a hydrophobic cleft which is the interaction site of S100A1 with its more that 20 known target proteins. Pssm-ID: 240152 [Multi-domain] Cd Length: 92 Bit Score: 69.53 E-value: 4.99e-14
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| S-100B | cd05027 | S-100B: S-100B domain found in proteins similar to S100B. S100B is a calcium-binding protein ... |
4-87 | 1.37e-12 | |||||||
S-100B: S-100B domain found in proteins similar to S100B. S100B is a calcium-binding protein belonging to a large S100 vertebrate-specific protein family within the EF-hand superfamily of calcium-binding proteins. Note that the S-100 hierarchy, to which this S-100B group belongs, contains only S-100 EF-hand domains, other EF-hands have been modeled separately. S100B is most abundant in glial cells of the central nervous system, predominately in astrocytes. S100B is involved in signal transduction via the inhibition of protein phoshorylation, regulation of enzyme activity and by affecting the calcium homeostasis. Upon calcium binding the S100B homodimer changes conformation to expose a hydrophobic cleft, which represents the interaction site of S100B with its more than 20 known target proteins. These target proteins include several cellular architecture proteins such as tubulin and GFAP; S100B can inhibit polymerization of these oligomeric molecules. Furthermore, S100B inhibits the phosphorylation of multiple kinase substrates including the Alzheimer protein tau and neuromodulin (GAP-43) through a calcium-sensitive interaction with the protein substrates. Pssm-ID: 240154 [Multi-domain] Cd Length: 88 Bit Score: 65.26 E-value: 1.37e-12
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| S-100A11 | cd05023 | S-100A11: S-100A11 domain found in proteins similar to S100A11. S100A11 is a member of the ... |
6-85 | 4.24e-11 | |||||||
S-100A11: S-100A11 domain found in proteins similar to S100A11. S100A11 is a member of the S-100 domain family within EF-hand Ca2+-binding proteins superfamily. Note that the S-100 hierarchy, to which this S-100A11 group belongs, contains only S-100 EF-hand domains, other EF-hands have been modeled separately. S100 proteins exhibit unique patterns of tissue- and cell type-specific expression and have been implicated in the Ca2+-dependent regulation of diverse physiological processes, including cell cycle regulation, differentiation, growth, and metabolic control . S100 proteins have also been associated with a variety of pathological events, including neoplastic transformation and neurodegenerative diseases such as Alzheimer's, usually via over expression of the protein. S100A11 is expressed in smooth muscle and other tissues and involves in calcium-dependent membrane aggregation, which is important for cell vesiculation . As is the case for many other S100 proteins, S100A11 is homodimer, which is able to form a heterodimer with S100B through subunit exchange. Ca2+ binding to S100A11 results in a conformational change in the protein, exposing a hydrophobic surface that interacts with target proteins. In addition to binding to annexin A1 and A6 S100A11 also interacts with actin and transglutaminase. Pssm-ID: 240150 [Multi-domain] Cd Length: 89 Bit Score: 61.32 E-value: 4.24e-11
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| S-100A10 | cd05024 | S-100A10: A subgroup of the S-100A10 domain found in proteins similar to S100A10. S100A10 is a ... |
7-86 | 2.48e-10 | |||||||
S-100A10: A subgroup of the S-100A10 domain found in proteins similar to S100A10. S100A10 is a member of the S100 family of EF-hand superfamily of calcium-binding proteins. Note that the S-100 hierarchy, to which this S-100A10 group belongs, contains only S-100 EF-hand domains, other EF-hands have been modeled separately. S100 proteins are expressed exclusively in vertebrates, and are implicated in intracellular and extracellular regulatory activities. A unique feature of S100A10 is that it contains mutation in both of the calcium binding sites, making it calcium insensitive. S100A10 has been detected in brain, heart, gastrointestinal tract, kidney, liver, lung, spleen, testes, epidermis, aorta, and thymus. Structural data supports the homo- and hetero-dimeric as well as hetero-tetrameric nature of the protein. S100A10 has multiple binding partners in its calcium free state and is therefore involved in many diverse biological functions. Pssm-ID: 240151 [Multi-domain] Cd Length: 91 Bit Score: 59.09 E-value: 2.48e-10
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| S-100A6 | cd05029 | S-100A6: S-100A6 domain found in proteins similar to S100A6. S100A6 is a member of the S100 ... |
11-89 | 4.85e-10 | |||||||
S-100A6: S-100A6 domain found in proteins similar to S100A6. S100A6 is a member of the S100 domain family within EF-hand Ca2+-binding proteins superfamily. Note that the S-100 hierarchy, to which this S-100A6 group belongs, contains only S-100 EF-hand domains, other EF-hands have been modeled separately. S100 proteins exhibit unique patterns of tissue- and cell type-specific expression and have been implicated in the Ca2+-dependent regulation of diverse physiological processes, including cell cycle regulation, differentiation, growth, and metabolic control . S100A6 is normally expressed in the G1 phase of the cell cycle in neuronal cells. The function of S100A6 remains unclear, but evidence suggests that it is involved in cell cycle regulation and exocytosis. S100A6 may also be involved in tumorigenesis; the protein is overexpressed in several tumors. Ca2+ binding to S100A6 leads to a conformational change in the protein, which exposes a hydrophobic surface for interaction with target proteins. Several such proteins have been identified: glyceraldehyde-3-phosphate dehydrogenase , annexins 2, 6 and 11 and Calcyclin-Binding Protein (CacyBP). Pssm-ID: 240155 [Multi-domain] Cd Length: 88 Bit Score: 58.31 E-value: 4.85e-10
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| ser_rich_anae_1 | NF033849 | serine-rich protein; This serine-rich protein belongs to a family with large size (over 1000 ... |
681-965 | 4.21e-08 | |||||||
serine-rich protein; This serine-rich protein belongs to a family with large size (over 1000 amino acids), which a highly serine-rich central region that averages over 300 aa in length. Species encoding members of this family of proteins tend to be anaerobic bacteria, including Gram-positive bacteria of the human gut microbiome and Chloroflexi from marine sediments. Pssm-ID: 468206 [Multi-domain] Cd Length: 1122 Bit Score: 58.86 E-value: 4.21e-08
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| PHA03307 | PHA03307 | transcriptional regulator ICP4; Provisional |
1475-1878 | 9.01e-07 | |||||||
transcriptional regulator ICP4; Provisional Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 54.79 E-value: 9.01e-07
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| S-100A13 | cd05022 | S-100A13: S-100A13 domain found in proteins similar to S100A13. S100A13 is a calcium-binding ... |
6-82 | 2.30e-06 | |||||||
S-100A13: S-100A13 domain found in proteins similar to S100A13. S100A13 is a calcium-binding protein belonging to a large S100 vertebrate-specific protein family within the EF-hand superfamily of calcium-binding proteins. Note that the S-100 hierarchy, to which this S-100A13 group belongs, contains only S-100 EF-hand domains, other EF-hands have been modeled separately. S100A13 is involved in the cellular export of interleukin-1 (IL-1) and of fibroblast growth factor-1 (FGF-1), which plays an important role in angiogenesis and tissue regeneration. Export is based on the CuII-dependent formation of multiprotein complexes containing the S100A13 protein. Assembly of these complexes occurs near the inner surface of the plasma membrane. Binding of two Ca(II) ions per monomer triggers key conformational changes leading to the creation of two identical and symmetrical Cu(II)-binding sites on the surface of the protein, close to the interface between the two monomers. These Cu(II)-binding sites are unique among the S100 proteins, which are reported to bind Cu(II) or Zn(II) ions in addition to Ca(II) ions. In addition, the three-dimensional structure of S100A13 differs significantly from those of other S100 proteins; the hydrophobic pocket that largely contributes to protein-protein interactions in other S100 proteins is absent in S100A13. The structure of S100A13 contains a large patch of negatively charged residues flanked by dense cationic clusters, formed mostly from positively charged residues from the C-terminal end, which plays major role in binding FGF-1. Pssm-ID: 240149 [Multi-domain] Cd Length: 89 Bit Score: 47.72 E-value: 2.30e-06
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| EF-hand_7 | pfam13499 | EF-hand domain pair; |
11-78 | 2.51e-06 | |||||||
EF-hand domain pair; Pssm-ID: 463900 [Multi-domain] Cd Length: 67 Bit Score: 46.86 E-value: 2.51e-06
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| PTZ00449 | PTZ00449 | 104 kDa microneme/rhoptry antigen; Provisional |
1095-1420 | 2.29e-05 | |||||||
104 kDa microneme/rhoptry antigen; Provisional Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 50.07 E-value: 2.29e-05
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| PHA03307 | PHA03307 | transcriptional regulator ICP4; Provisional |
1631-1987 | 3.89e-05 | |||||||
transcriptional regulator ICP4; Provisional Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 49.40 E-value: 3.89e-05
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| PTZ00449 | PTZ00449 | 104 kDa microneme/rhoptry antigen; Provisional |
1810-1997 | 9.00e-05 | |||||||
104 kDa microneme/rhoptry antigen; Provisional Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 48.15 E-value: 9.00e-05
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| EFh | cd00051 | EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ... |
26-78 | 1.12e-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: 42.15 E-value: 1.12e-04
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| PHA03307 | PHA03307 | transcriptional regulator ICP4; Provisional |
1243-1597 | 1.32e-04 | |||||||
transcriptional regulator ICP4; Provisional Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 47.47 E-value: 1.32e-04
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| EFh_PI-PLC | cd15898 | EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ... |
26-81 | 2.05e-04 | |||||||
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: 43.43 E-value: 2.05e-04
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| PHA03247 | PHA03247 | large tegument protein UL36; Provisional |
1635-2035 | 8.27e-04 | |||||||
large tegument protein UL36; Provisional Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 44.93 E-value: 8.27e-04
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| PRK10263 | PRK10263 | DNA translocase FtsK; Provisional |
1090-1202 | 1.31e-03 | |||||||
DNA translocase FtsK; Provisional Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 44.31 E-value: 1.31e-03
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| EFh_PEF_Group_I | cd16180 | Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ... |
26-75 | 1.51e-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: 41.36 E-value: 1.51e-03
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| EFh_PEF | cd15897 | The penta-EF hand (PEF) family; The penta-EF hand (PEF) family contains a group of five ... |
15-74 | 1.65e-03 | |||||||
The penta-EF hand (PEF) family; The penta-EF hand (PEF) family contains a group of five EF-hand calcium-binding proteins, including several classical calpain large catalytic subunits (CAPN1, 2, 3, 8, 9, 11, 12, 13, 14), two calpain small subunits (CAPNS1 and CAPNS2), as well as non-calpain PEF proteins, ALG-2 (apoptosis-linked gene 2, also termed programmed cell death protein 6, PDCD6), peflin, sorcin, and grancalcin. Based on the sequence similarity of EF1 hand, ALG-2 and peflin have been classified into group I PEF proteins. Calcium-dependent protease calpain subfamily members, sorcin and grancalcin, are group II PEF proteins. Calpains (EC 3.4.22.17) are calcium-activated intracellular cysteine proteases that play important roles in the degradation or functional modulation in a variety of substrates. They have been implicated in a number of physiological processes such as cell cycle progression, remodeling of cytoskeletal-cell membrane attachments, signal transduction, gene expression and apoptosis. ALG-2 is a pro-apoptotic factor that forms a homodimer in the cell or a heterodimer with its closest paralog peflin through their EF5s. Peflin is a 30-kD PEF protein with a longer N-terminal hydrophobic domain than any other member of the PEF family, and it contains nine nonapeptide (A/PPGGPYGGP) repeats. It exists only as a heterodimer with ALG-2. The dissociation of heterodimer occurs in the presence of Ca2+. ALG-2 interacts with various proteins in a Ca2+-dependent manner. Sorcin (for soluble resistance-related calcium binding protein) is a soluble resistance-related calcium-binding protein that participates in the regulation of calcium homeostasis in cells. Grancalcin is a cytosolic Ca2+-binding protein specifically expressed in neutrophils and monocytes/macrophages. It plays a key role in leukocyte-specific functions that are responsible for host defense. Grancalcin can form a heterodimer together with sorcin. Members in this family contain five EF-hand motifs attached to an N-terminal region of variable length containing one or more short Gly/Pro-rich sequences. These proteins form homodimers or heterodimers through pairing between the 5th EF-hands from the two molecules. Unlike calmodulin, the PEF domains do not undergo major conformational changes upon binding Ca2+. Pssm-ID: 320054 [Multi-domain] Cd Length: 165 Bit Score: 41.65 E-value: 1.65e-03
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| PHA03307 | PHA03307 | transcriptional regulator ICP4; Provisional |
964-1280 | 1.87e-03 | |||||||
transcriptional regulator ICP4; Provisional Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 43.62 E-value: 1.87e-03
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| PRK12678 | PRK12678 | transcription termination factor Rho; Provisional |
1081-1278 | 1.98e-03 | |||||||
transcription termination factor Rho; Provisional Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 43.35 E-value: 1.98e-03
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| PRK07764 | PRK07764 | DNA polymerase III subunits gamma and tau; Validated |
1632-1826 | 2.93e-03 | |||||||
DNA polymerase III subunits gamma and tau; Validated Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 43.05 E-value: 2.93e-03
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| PTZ00449 | PTZ00449 | 104 kDa microneme/rhoptry antigen; Provisional |
1496-1828 | 2.95e-03 | |||||||
104 kDa microneme/rhoptry antigen; Provisional Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 43.14 E-value: 2.95e-03
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| ser_rich_anae_1 | NF033849 | serine-rich protein; This serine-rich protein belongs to a family with large size (over 1000 ... |
629-835 | 4.32e-03 | |||||||
serine-rich protein; This serine-rich protein belongs to a family with large size (over 1000 amino acids), which a highly serine-rich central region that averages over 300 aa in length. Species encoding members of this family of proteins tend to be anaerobic bacteria, including Gram-positive bacteria of the human gut microbiome and Chloroflexi from marine sediments. Pssm-ID: 468206 [Multi-domain] Cd Length: 1122 Bit Score: 42.30 E-value: 4.32e-03
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| dnaA | PRK14086 | chromosomal replication initiator protein DnaA; |
1559-1745 | 4.69e-03 | |||||||
chromosomal replication initiator protein DnaA; Pssm-ID: 237605 [Multi-domain] Cd Length: 617 Bit Score: 42.12 E-value: 4.69e-03
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| PRK07764 | PRK07764 | DNA polymerase III subunits gamma and tau; Validated |
1790-1970 | 5.62e-03 | |||||||
DNA polymerase III subunits gamma and tau; Validated Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 41.90 E-value: 5.62e-03
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| PRK07764 | PRK07764 | DNA polymerase III subunits gamma and tau; Validated |
1556-1733 | 5.91e-03 | |||||||
DNA polymerase III subunits gamma and tau; Validated Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 41.90 E-value: 5.91e-03
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| PRK10263 | PRK10263 | DNA translocase FtsK; Provisional |
1872-1984 | 6.70e-03 | |||||||
DNA translocase FtsK; Provisional Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 41.99 E-value: 6.70e-03
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| PRK12678 | PRK12678 | transcription termination factor Rho; Provisional |
1508-1744 | 7.01e-03 | |||||||
transcription termination factor Rho; Provisional Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 41.81 E-value: 7.01e-03
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