PREDICTED: coiled-coil and C2 domain-containing protein 1A isoform X4 [Cercocebus atys]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||
| C2_Freud-1 | cd08690 | C2 domain found in 5' repressor element under dual repression binding protein-1 (Freud-1); ... |
648-805 | 1.72e-80 | ||||
C2 domain found in 5' repressor element under dual repression binding protein-1 (Freud-1); Freud-1 is a novel calcium-regulated repressor that negatively regulates basal 5-HT1A receptor expression in neurons. It may also play a role in the altered regulation of 5-HT1A receptors associated with anxiety or major depression. Freud-1 contains two DM-14 basic repeats, a helix-loop-helix DNA binding domain, and a C2 domain. The Freud-1 C2 domain is thought to be calcium insensitive and it lacks several acidic residues that mediate calcium binding of the PKC C2 domain. In addition, it contains a poly-basic insert that is not present in calcium-dependent C2 domains and may function as a nuclear localization signal. 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. This cd contains the first C2 repeat, C2A, and has a type-II topology. : Pssm-ID: 176072 [Multi-domain] Cd Length: 155 Bit Score: 258.01 E-value: 1.72e-80
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| DM14 | smart00685 | Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241; |
349-407 | 2.04e-23 | ||||
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241; : Pssm-ID: 128928 [Multi-domain] Cd Length: 59 Bit Score: 93.90 E-value: 2.04e-23
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| DM14 | smart00685 | Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241; |
490-548 | 7.98e-19 | ||||
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241; : Pssm-ID: 128928 [Multi-domain] Cd Length: 59 Bit Score: 80.81 E-value: 7.98e-19
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| DM14 | smart00685 | Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241; |
257-310 | 1.54e-16 | ||||
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241; : Pssm-ID: 128928 [Multi-domain] Cd Length: 59 Bit Score: 74.64 E-value: 1.54e-16
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| DM14 | smart00685 | Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241; |
138-195 | 1.73e-11 | ||||
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241; : Pssm-ID: 128928 [Multi-domain] Cd Length: 59 Bit Score: 60.01 E-value: 1.73e-11
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| PRK12323 super family | cl46901 | DNA polymerase III subunit gamma/tau; |
112-284 | 4.22e-06 | ||||
DNA polymerase III subunit gamma/tau; The actual alignment was detected with superfamily member PRK12323: Pssm-ID: 481241 [Multi-domain] Cd Length: 700 Bit Score: 50.64 E-value: 4.22e-06
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| chemoreceptor_sensor super family | cl00144 | 4-helix bundle ligand binding sensor domain of chemoreceptors such as Tar or Tsr; The ligand ... |
882-949 | 3.64e-04 | ||||
4-helix bundle ligand binding sensor domain of chemoreceptors such as Tar or Tsr; The ligand binding sensor domain of chemoreceptors and related sensor histidine kinases forms homodimers and binds to ligands via the dimerization interface, a feature that appears to be conserved in this domain superfamily. This family includes ligand binding sensor domain of several chemoreceptors, such as Escherichia coli Tar, Tsr, NarQ, NarX, Pseudomonas aeruginosa KinB, Rhodopseudomonas palustris histidine kinase HK9 chemoreceptors, Comamonas testosteroni CNB-2 MCP2201 and Anaeromyxobacter dehalogenans histidine kinase Adeh_2942, among others. The actual alignment was detected with superfamily member cd22899: Pssm-ID: 444710 [Multi-domain] Cd Length: 116 Bit Score: 40.97 E-value: 3.64e-04
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| Name | Accession | Description | Interval | E-value | ||||
| C2_Freud-1 | cd08690 | C2 domain found in 5' repressor element under dual repression binding protein-1 (Freud-1); ... |
648-805 | 1.72e-80 | ||||
C2 domain found in 5' repressor element under dual repression binding protein-1 (Freud-1); Freud-1 is a novel calcium-regulated repressor that negatively regulates basal 5-HT1A receptor expression in neurons. It may also play a role in the altered regulation of 5-HT1A receptors associated with anxiety or major depression. Freud-1 contains two DM-14 basic repeats, a helix-loop-helix DNA binding domain, and a C2 domain. The Freud-1 C2 domain is thought to be calcium insensitive and it lacks several acidic residues that mediate calcium binding of the PKC C2 domain. In addition, it contains a poly-basic insert that is not present in calcium-dependent C2 domains and may function as a nuclear localization signal. 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. This cd contains the first C2 repeat, C2A, and has a type-II topology. Pssm-ID: 176072 [Multi-domain] Cd Length: 155 Bit Score: 258.01 E-value: 1.72e-80
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| DM14 | smart00685 | Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241; |
349-407 | 2.04e-23 | ||||
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241; Pssm-ID: 128928 [Multi-domain] Cd Length: 59 Bit Score: 93.90 E-value: 2.04e-23
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| DM14 | smart00685 | Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241; |
490-548 | 7.98e-19 | ||||
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241; Pssm-ID: 128928 [Multi-domain] Cd Length: 59 Bit Score: 80.81 E-value: 7.98e-19
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| DM14 | smart00685 | Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241; |
257-310 | 1.54e-16 | ||||
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241; Pssm-ID: 128928 [Multi-domain] Cd Length: 59 Bit Score: 74.64 E-value: 1.54e-16
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| DM14 | smart00685 | Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241; |
138-195 | 1.73e-11 | ||||
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241; Pssm-ID: 128928 [Multi-domain] Cd Length: 59 Bit Score: 60.01 E-value: 1.73e-11
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| C2 | pfam00168 | C2 domain; |
655-769 | 2.08e-08 | ||||
C2 domain; Pssm-ID: 425499 [Multi-domain] Cd Length: 104 Bit Score: 52.71 E-value: 2.08e-08
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| C2 | smart00239 | Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ... |
657-759 | 6.40e-08 | ||||
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, protein kinases C, and synaptotagmins (among others). Some do not appear to contain Ca2+-binding sites. Particular C2s appear to bind phospholipids, inositol polyphosphates, and intracellular proteins. Unusual occurrence in perforin. Synaptotagmin and PLC C2s are permuted in sequence with respect to N- and C-terminal beta strands. SMART detects C2 domains using one or both of two profiles. Pssm-ID: 214577 [Multi-domain] Cd Length: 101 Bit Score: 51.33 E-value: 6.40e-08
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| PRK12323 | PRK12323 | DNA polymerase III subunit gamma/tau; |
112-284 | 4.22e-06 | ||||
DNA polymerase III subunit gamma/tau; Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 50.64 E-value: 4.22e-06
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| NarQ_sensor | cd22899 | ligand binding sensor domain of NarQ, and related chemoreceptors; The periplasmic ligand ... |
882-949 | 3.64e-04 | ||||
ligand binding sensor domain of NarQ, and related chemoreceptors; The periplasmic ligand binding sensor domain of NarQ is a histidine kinase receptor that responds to nitrate and nitrite to effect regulation of anaerobic respiration in various bacteria and similar proteins. It forms a homodimer and binds to ligands such as nitrate via the dimerization interface, a feature that appears to be conserved in this domain superfamily. NarQ-NarP sensor-response regulator pair controls Escherichia coli gene expression in response to nitrate and nitrite. NarQ has been shown to interact equally with NarP and NarL response regulators; NarL is the sensor response partner of NarX. Pssm-ID: 438631 [Multi-domain] Cd Length: 116 Bit Score: 40.97 E-value: 3.64e-04
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| DUF3729 | pfam12526 | Protein of unknown function (DUF3729); This family of proteins is found in viruses. Proteins ... |
189-266 | 5.20e-04 | ||||
Protein of unknown function (DUF3729); This family of proteins is found in viruses. Proteins in this family are typically between 145 and 1707 amino acids in length. The family is found in association with pfam01443, pfam01661, pfam05417, pfam01660, pfam00978. There is a single completely conserved residue L that may be functionally important. Pssm-ID: 372164 [Multi-domain] Cd Length: 115 Bit Score: 40.83 E-value: 5.20e-04
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| PspC_subgroup_1 | NF033838 | pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
109-261 | 3.05e-03 | ||||
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 41.54 E-value: 3.05e-03
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| Name | Accession | Description | Interval | E-value | ||||
| C2_Freud-1 | cd08690 | C2 domain found in 5' repressor element under dual repression binding protein-1 (Freud-1); ... |
648-805 | 1.72e-80 | ||||
C2 domain found in 5' repressor element under dual repression binding protein-1 (Freud-1); Freud-1 is a novel calcium-regulated repressor that negatively regulates basal 5-HT1A receptor expression in neurons. It may also play a role in the altered regulation of 5-HT1A receptors associated with anxiety or major depression. Freud-1 contains two DM-14 basic repeats, a helix-loop-helix DNA binding domain, and a C2 domain. The Freud-1 C2 domain is thought to be calcium insensitive and it lacks several acidic residues that mediate calcium binding of the PKC C2 domain. In addition, it contains a poly-basic insert that is not present in calcium-dependent C2 domains and may function as a nuclear localization signal. 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. This cd contains the first C2 repeat, C2A, and has a type-II topology. Pssm-ID: 176072 [Multi-domain] Cd Length: 155 Bit Score: 258.01 E-value: 1.72e-80
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| DM14 | smart00685 | Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241; |
349-407 | 2.04e-23 | ||||
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241; Pssm-ID: 128928 [Multi-domain] Cd Length: 59 Bit Score: 93.90 E-value: 2.04e-23
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| DM14 | smart00685 | Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241; |
490-548 | 7.98e-19 | ||||
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241; Pssm-ID: 128928 [Multi-domain] Cd Length: 59 Bit Score: 80.81 E-value: 7.98e-19
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| DM14 | smart00685 | Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241; |
257-310 | 1.54e-16 | ||||
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241; Pssm-ID: 128928 [Multi-domain] Cd Length: 59 Bit Score: 74.64 E-value: 1.54e-16
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| DM14 | smart00685 | Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241; |
138-195 | 1.73e-11 | ||||
Repeats in fly CG4713, worm Y37H9A.3 and human FLJ20241; Pssm-ID: 128928 [Multi-domain] Cd Length: 59 Bit Score: 60.01 E-value: 1.73e-11
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| C2 | pfam00168 | C2 domain; |
655-769 | 2.08e-08 | ||||
C2 domain; Pssm-ID: 425499 [Multi-domain] Cd Length: 104 Bit Score: 52.71 E-value: 2.08e-08
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| C2 | smart00239 | Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ... |
657-759 | 6.40e-08 | ||||
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, protein kinases C, and synaptotagmins (among others). Some do not appear to contain Ca2+-binding sites. Particular C2s appear to bind phospholipids, inositol polyphosphates, and intracellular proteins. Unusual occurrence in perforin. Synaptotagmin and PLC C2s are permuted in sequence with respect to N- and C-terminal beta strands. SMART detects C2 domains using one or both of two profiles. Pssm-ID: 214577 [Multi-domain] Cd Length: 101 Bit Score: 51.33 E-value: 6.40e-08
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| C2 | cd00030 | C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ... |
657-765 | 2.95e-07 | ||||
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: 49.37 E-value: 2.95e-07
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| PRK12323 | PRK12323 | DNA polymerase III subunit gamma/tau; |
112-284 | 4.22e-06 | ||||
DNA polymerase III subunit gamma/tau; Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 50.64 E-value: 4.22e-06
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| C2A_Tricalbin-like | cd04044 | C2 domain first repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are ... |
657-777 | 5.05e-05 | ||||
C2 domain first repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are present in Tricalbin, a yeast homolog of Synaptotagmin, which is involved in membrane trafficking and sorting. 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. This cd contains the first C2 repeat, C2A, and has a type-II topology. Pssm-ID: 176009 [Multi-domain] Cd Length: 124 Bit Score: 43.70 E-value: 5.05e-05
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| C2_C21orf25-like | cd08678 | C2 domain found in the Human chromosome 21 open reading frame 25 (C21orf25) protein; The ... |
657-773 | 1.82e-04 | ||||
C2 domain found in the Human chromosome 21 open reading frame 25 (C21orf25) protein; The members in this cd are named after the Human C21orf25 which contains a single C2 domain. Several other members contain a C1 domain downstream of the C2 domain. No other information on this protein is currently known. 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: 176060 [Multi-domain] Cd Length: 126 Bit Score: 42.35 E-value: 1.82e-04
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| C2B_Synaptotagmin | cd00276 | C2 domain second repeat present in Synaptotagmin; Synaptotagmin is a membrane-trafficking ... |
657-748 | 2.61e-04 | ||||
C2 domain second repeat present in Synaptotagmin; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. There are several classes of Synaptotagmins. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. 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. This cd contains the second C2 repeat, C2B, and has a type-I topology. Pssm-ID: 175975 [Multi-domain] Cd Length: 134 Bit Score: 41.80 E-value: 2.61e-04
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| NarQ_sensor | cd22899 | ligand binding sensor domain of NarQ, and related chemoreceptors; The periplasmic ligand ... |
882-949 | 3.64e-04 | ||||
ligand binding sensor domain of NarQ, and related chemoreceptors; The periplasmic ligand binding sensor domain of NarQ is a histidine kinase receptor that responds to nitrate and nitrite to effect regulation of anaerobic respiration in various bacteria and similar proteins. It forms a homodimer and binds to ligands such as nitrate via the dimerization interface, a feature that appears to be conserved in this domain superfamily. NarQ-NarP sensor-response regulator pair controls Escherichia coli gene expression in response to nitrate and nitrite. NarQ has been shown to interact equally with NarP and NarL response regulators; NarL is the sensor response partner of NarX. Pssm-ID: 438631 [Multi-domain] Cd Length: 116 Bit Score: 40.97 E-value: 3.64e-04
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| DUF3729 | pfam12526 | Protein of unknown function (DUF3729); This family of proteins is found in viruses. Proteins ... |
189-266 | 5.20e-04 | ||||
Protein of unknown function (DUF3729); This family of proteins is found in viruses. Proteins in this family are typically between 145 and 1707 amino acids in length. The family is found in association with pfam01443, pfam01661, pfam05417, pfam01660, pfam00978. There is a single completely conserved residue L that may be functionally important. Pssm-ID: 372164 [Multi-domain] Cd Length: 115 Bit Score: 40.83 E-value: 5.20e-04
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| PRK13042 | PRK13042 | superantigen-like protein SSL4; Reviewed; |
189-253 | 9.40e-04 | ||||
superantigen-like protein SSL4; Reviewed; Pssm-ID: 183854 [Multi-domain] Cd Length: 291 Bit Score: 42.31 E-value: 9.40e-04
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| PspC_subgroup_1 | NF033838 | pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
109-261 | 3.05e-03 | ||||
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 41.54 E-value: 3.05e-03
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| PRK07994 | PRK07994 | DNA polymerase III subunits gamma and tau; Validated |
199-307 | 4.23e-03 | ||||
DNA polymerase III subunits gamma and tau; Validated Pssm-ID: 236138 [Multi-domain] Cd Length: 647 Bit Score: 41.00 E-value: 4.23e-03
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| PHA02682 | PHA02682 | ORF080 virion core protein; Provisional |
122-301 | 5.10e-03 | ||||
ORF080 virion core protein; Provisional Pssm-ID: 177464 [Multi-domain] Cd Length: 280 Bit Score: 39.84 E-value: 5.10e-03
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| C2C_KIAA1228 | cd04030 | C2 domain third repeat present in uncharacterized human KIAA1228-like proteins; KIAA proteins ... |
649-760 | 5.27e-03 | ||||
C2 domain third repeat present in uncharacterized human KIAA1228-like proteins; KIAA proteins are uncharacterized human proteins. They were compiled by the Kazusa mammalian cDNA project which identified more than 2000 human genes. They are identified by 4 digit codes that precede the KIAA designation. Many KIAA genes are still functionally uncharacterized including KIAA1228. 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. This cd contains the third C2 repeat, C2C, and has a type-II topology. Pssm-ID: 175996 [Multi-domain] Cd Length: 127 Bit Score: 38.02 E-value: 5.27e-03
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| Blast search parameters | ||||
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