coiled-coil and C2 domain-containing protein 2A isoform X3 [Gallus gallus]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| DUF5523 | pfam17661 | Family of unknown function (DUF5523); This is a family of unknown function found in Eukaryotes. ... |
53-299 | 2.49e-107 | |||||
Family of unknown function (DUF5523); This is a family of unknown function found in Eukaryotes. Family members such as the human CC1D2A protein carry the domain architecture where pfam15625 and pfam00168 are found at the C-terminal region of this family. However, other family members such as Swiss:D6R9V3, do not carry either of the above mentioned Pfam families. : Pssm-ID: 465443 Cd Length: 255 Bit Score: 341.18 E-value: 2.49e-107
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| CC2D2AN-C2 | pfam15625 | CC2D2A N-terminal C2 domain; Many ciliary proteins are involved in ciliogenesis and implicated ... |
556-730 | 8.57e-83 | |||||
CC2D2A N-terminal C2 domain; Many ciliary proteins are involved in ciliogenesis and implicated for ciliophathies. A recent study has shown that many of them contain various new versions of C2 domains which are predicted to mediate membrane localizations for Y-shaped linkers of transition zone of cilia. This is the first C2 domain of ciliary CC2D2A proteins which also have another C2 domain (CC2D2AC-C2) and a new inactive transglutaminase-like peptidase domain (CC2D2A-TGL). : Pssm-ID: 464780 Cd Length: 174 Bit Score: 268.88 E-value: 8.57e-83
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| C2 super family | cl14603 | C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ... |
1008-1046 | 9.81e-05 | |||||
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. The actual alignment was detected with superfamily member cd04018: Pssm-ID: 472691 [Multi-domain] Cd Length: 151 Bit Score: 44.16 E-value: 9.81e-05
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| BAR super family | cl12013 | The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects ... |
347-472 | 2.56e-04 | |||||
The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects membrane curvature; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions including organelle biogenesis, membrane trafficking or remodeling, and cell division and migration. Mutations in BAR containing proteins have been linked to diseases and their inactivation in cells leads to altered membrane dynamics. A BAR domain with an additional N-terminal amphipathic helix (an N-BAR) can drive membrane curvature. These N-BAR domains are found in amphiphysins and endophilins, among others. BAR domains are also frequently found alongside domains that determine lipid specificity, such as the Pleckstrin Homology (PH) and Phox Homology (PX) domains which are present in beta centaurins (ACAPs and ASAPs) and sorting nexins, respectively. A FES-CIP4 Homology (FCH) domain together with a coiled coil region is called the F-BAR domain and is present in Pombe/Cdc15 homology (PCH) family proteins, which include Fes/Fes tyrosine kinases, PACSIN or syndapin, CIP4-like proteins, and srGAPs, among others. The Inverse (I)-BAR or IRSp53/MIM homology Domain (IMD) is found in multi-domain proteins, such as IRSp53 and MIM, that act as scaffolding proteins and transducers of a variety of signaling pathways that link membrane dynamics and the underlying actin cytoskeleton. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. The I-BAR domain induces membrane protrusions in the opposite direction compared to classical BAR and F-BAR domains, which produce membrane invaginations. BAR domains that also serve as protein interaction domains include those of arfaptin and OPHN1-like proteins, among others, which bind to Rac and Rho GAP domains, respectively. The actual alignment was detected with superfamily member cd07678: Pssm-ID: 472257 [Multi-domain] Cd Length: 263 Bit Score: 44.61 E-value: 2.56e-04
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| Name | Accession | Description | Interval | E-value | |||||
| DUF5523 | pfam17661 | Family of unknown function (DUF5523); This is a family of unknown function found in Eukaryotes. ... |
53-299 | 2.49e-107 | |||||
Family of unknown function (DUF5523); This is a family of unknown function found in Eukaryotes. Family members such as the human CC1D2A protein carry the domain architecture where pfam15625 and pfam00168 are found at the C-terminal region of this family. However, other family members such as Swiss:D6R9V3, do not carry either of the above mentioned Pfam families. Pssm-ID: 465443 Cd Length: 255 Bit Score: 341.18 E-value: 2.49e-107
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| CC2D2AN-C2 | pfam15625 | CC2D2A N-terminal C2 domain; Many ciliary proteins are involved in ciliogenesis and implicated ... |
556-730 | 8.57e-83 | |||||
CC2D2A N-terminal C2 domain; Many ciliary proteins are involved in ciliogenesis and implicated for ciliophathies. A recent study has shown that many of them contain various new versions of C2 domains which are predicted to mediate membrane localizations for Y-shaped linkers of transition zone of cilia. This is the first C2 domain of ciliary CC2D2A proteins which also have another C2 domain (CC2D2AC-C2) and a new inactive transglutaminase-like peptidase domain (CC2D2A-TGL). Pssm-ID: 464780 Cd Length: 174 Bit Score: 268.88 E-value: 8.57e-83
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| C2C_Ferlin | cd04018 | C2 domain third repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and ... |
1008-1046 | 9.81e-05 | |||||
C2 domain third repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and other proteins, such as Synaptotagmins, are implicated in facilitating the fusion process when cell membranes fuse together. There are six known human Ferlins: Dysferlin (Fer1L1), Otoferlin (Fer1L2), Myoferlin (Fer1L3), Fer1L4, Fer1L5, and Fer1L6. Defects in these genes can lead to a wide range of diseases including muscular dystrophy (dysferlin), deafness (otoferlin), and infertility (fer-1, fertilization factor-1). Structurally they have 6 tandem C2 domains, designated as (C2A-C2F) and a single C-terminal transmembrane domain, though there is a new study that disputes this and claims that there are actually 7 tandem C2 domains with another C2 domain inserted between C2D and C2E. In a subset of them (Dysferlin, Myoferlin, and Fer1) there is an additional conserved domain called DysF. 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: 175985 [Multi-domain] Cd Length: 151 Bit Score: 44.16 E-value: 9.81e-05
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| F-BAR_FCHSD1 | cd07678 | The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH and double SH3 domains 1 ... |
347-472 | 2.56e-04 | |||||
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH and double SH3 domains 1 (FCHSD1); F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. FCH and double SH3 domains 1 (FCHSD1) contains an N-terminal F-BAR domain and two SH3 domains at the C-terminus. It has been characterized only in silico, and its biological function is still unknown. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules. Pssm-ID: 153362 [Multi-domain] Cd Length: 263 Bit Score: 44.61 E-value: 2.56e-04
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| C2 | pfam00168 | C2 domain; |
1012-1116 | 2.89e-04 | |||||
C2 domain; Pssm-ID: 425499 [Multi-domain] Cd Length: 104 Bit Score: 41.54 E-value: 2.89e-04
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| C2 | smart00239 | Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ... |
1012-1112 | 4.53e-03 | |||||
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: 38.24 E-value: 4.53e-03
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| Name | Accession | Description | Interval | E-value | |||||
| DUF5523 | pfam17661 | Family of unknown function (DUF5523); This is a family of unknown function found in Eukaryotes. ... |
53-299 | 2.49e-107 | |||||
Family of unknown function (DUF5523); This is a family of unknown function found in Eukaryotes. Family members such as the human CC1D2A protein carry the domain architecture where pfam15625 and pfam00168 are found at the C-terminal region of this family. However, other family members such as Swiss:D6R9V3, do not carry either of the above mentioned Pfam families. Pssm-ID: 465443 Cd Length: 255 Bit Score: 341.18 E-value: 2.49e-107
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| CC2D2AN-C2 | pfam15625 | CC2D2A N-terminal C2 domain; Many ciliary proteins are involved in ciliogenesis and implicated ... |
556-730 | 8.57e-83 | |||||
CC2D2A N-terminal C2 domain; Many ciliary proteins are involved in ciliogenesis and implicated for ciliophathies. A recent study has shown that many of them contain various new versions of C2 domains which are predicted to mediate membrane localizations for Y-shaped linkers of transition zone of cilia. This is the first C2 domain of ciliary CC2D2A proteins which also have another C2 domain (CC2D2AC-C2) and a new inactive transglutaminase-like peptidase domain (CC2D2A-TGL). Pssm-ID: 464780 Cd Length: 174 Bit Score: 268.88 E-value: 8.57e-83
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| C2C_Ferlin | cd04018 | C2 domain third repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and ... |
1008-1046 | 9.81e-05 | |||||
C2 domain third repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and other proteins, such as Synaptotagmins, are implicated in facilitating the fusion process when cell membranes fuse together. There are six known human Ferlins: Dysferlin (Fer1L1), Otoferlin (Fer1L2), Myoferlin (Fer1L3), Fer1L4, Fer1L5, and Fer1L6. Defects in these genes can lead to a wide range of diseases including muscular dystrophy (dysferlin), deafness (otoferlin), and infertility (fer-1, fertilization factor-1). Structurally they have 6 tandem C2 domains, designated as (C2A-C2F) and a single C-terminal transmembrane domain, though there is a new study that disputes this and claims that there are actually 7 tandem C2 domains with another C2 domain inserted between C2D and C2E. In a subset of them (Dysferlin, Myoferlin, and Fer1) there is an additional conserved domain called DysF. 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: 175985 [Multi-domain] Cd Length: 151 Bit Score: 44.16 E-value: 9.81e-05
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| F-BAR_FCHSD1 | cd07678 | The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH and double SH3 domains 1 ... |
347-472 | 2.56e-04 | |||||
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH and double SH3 domains 1 (FCHSD1); F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. FCH and double SH3 domains 1 (FCHSD1) contains an N-terminal F-BAR domain and two SH3 domains at the C-terminus. It has been characterized only in silico, and its biological function is still unknown. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules. Pssm-ID: 153362 [Multi-domain] Cd Length: 263 Bit Score: 44.61 E-value: 2.56e-04
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| C2 | pfam00168 | C2 domain; |
1012-1116 | 2.89e-04 | |||||
C2 domain; Pssm-ID: 425499 [Multi-domain] Cd Length: 104 Bit Score: 41.54 E-value: 2.89e-04
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| C2_PLC_like | cd00275 | C2 domain present in Phosphoinositide-specific phospholipases C (PLC); PLCs are involved in ... |
1010-1046 | 1.30e-03 | |||||
C2 domain present in Phosphoinositide-specific phospholipases C (PLC); PLCs are involved in the hydrolysis of phosphatidylinositol-4,5-bisphosphate (PIP2) to d-myo-inositol-1,4,5-trisphosphate (1,4,5-IP3) and sn-1,2-diacylglycerol (DAG). 1,4,5-IP3 and DAG are second messengers in eukaryotic signal transduction cascades. PLC is composed of a N-terminal PH domain followed by a series of EF hands, a catalytic TIM barrel and a C-terminal C2 domain. 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. Members here have a type-II topology. Pssm-ID: 175974 [Multi-domain] Cd Length: 128 Bit Score: 40.22 E-value: 1.30e-03
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| C2 | smart00239 | Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ... |
1012-1112 | 4.53e-03 | |||||
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: 38.24 E-value: 4.53e-03
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