protein fantom isoform X7 [Mus musculus]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||
| C2-C2_1 | pfam11618 | First C2 domain of RPGR-interacting protein 1; This domain is the first, more N-terminal, C2 ... |
208-349 | 5.98e-76 | ||||
First C2 domain of RPGR-interacting protein 1; This domain is the first, more N-terminal, C2 domain on X-linked retinitis pigmentosa GTPase regulator-interacting proteins, or RPGR-interacting proteins. : Pssm-ID: 463310 Cd Length: 143 Bit Score: 243.69 E-value: 5.98e-76
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| RPGR1_C | pfam18111 | Retinitis pigmentosa G-protein regulator interacting C-terminal; This is the C-terminal domain ... |
705-868 | 6.60e-66 | ||||
Retinitis pigmentosa G-protein regulator interacting C-terminal; This is the C-terminal domain of retinitis pigmentosa G-protein regulator (RPGR) interacting protein-1 present in Homo sapiens. A mutation in RPGR interacting protein-1 can be observed in the eye disease Leber congenital amaurosis. The domain is commonly known as the RPGR-interacting domain (RID) and is thought to have a C2-like fold. : Pssm-ID: 465655 Cd Length: 166 Bit Score: 217.28 E-value: 6.60e-66
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| C2 | cd00030 | C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ... |
403-502 | 8.38e-12 | ||||
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: 62.47 E-value: 8.38e-12
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| Name | Accession | Description | Interval | E-value | ||||
| C2-C2_1 | pfam11618 | First C2 domain of RPGR-interacting protein 1; This domain is the first, more N-terminal, C2 ... |
208-349 | 5.98e-76 | ||||
First C2 domain of RPGR-interacting protein 1; This domain is the first, more N-terminal, C2 domain on X-linked retinitis pigmentosa GTPase regulator-interacting proteins, or RPGR-interacting proteins. Pssm-ID: 463310 Cd Length: 143 Bit Score: 243.69 E-value: 5.98e-76
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| RPGR1_C | pfam18111 | Retinitis pigmentosa G-protein regulator interacting C-terminal; This is the C-terminal domain ... |
705-868 | 6.60e-66 | ||||
Retinitis pigmentosa G-protein regulator interacting C-terminal; This is the C-terminal domain of retinitis pigmentosa G-protein regulator (RPGR) interacting protein-1 present in Homo sapiens. A mutation in RPGR interacting protein-1 can be observed in the eye disease Leber congenital amaurosis. The domain is commonly known as the RPGR-interacting domain (RID) and is thought to have a C2-like fold. Pssm-ID: 465655 Cd Length: 166 Bit Score: 217.28 E-value: 6.60e-66
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| C2 | cd00030 | C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ... |
403-502 | 8.38e-12 | ||||
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: 62.47 E-value: 8.38e-12
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| C2 | smart00239 | Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ... |
403-498 | 9.59e-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: 50.95 E-value: 9.59e-08
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| C2 | pfam00168 | C2 domain; |
403-510 | 1.01e-07 | ||||
C2 domain; Pssm-ID: 425499 [Multi-domain] Cd Length: 104 Bit Score: 50.78 E-value: 1.01e-07
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| Name | Accession | Description | Interval | E-value | ||||
| C2-C2_1 | pfam11618 | First C2 domain of RPGR-interacting protein 1; This domain is the first, more N-terminal, C2 ... |
208-349 | 5.98e-76 | ||||
First C2 domain of RPGR-interacting protein 1; This domain is the first, more N-terminal, C2 domain on X-linked retinitis pigmentosa GTPase regulator-interacting proteins, or RPGR-interacting proteins. Pssm-ID: 463310 Cd Length: 143 Bit Score: 243.69 E-value: 5.98e-76
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| RPGR1_C | pfam18111 | Retinitis pigmentosa G-protein regulator interacting C-terminal; This is the C-terminal domain ... |
705-868 | 6.60e-66 | ||||
Retinitis pigmentosa G-protein regulator interacting C-terminal; This is the C-terminal domain of retinitis pigmentosa G-protein regulator (RPGR) interacting protein-1 present in Homo sapiens. A mutation in RPGR interacting protein-1 can be observed in the eye disease Leber congenital amaurosis. The domain is commonly known as the RPGR-interacting domain (RID) and is thought to have a C2-like fold. Pssm-ID: 465655 Cd Length: 166 Bit Score: 217.28 E-value: 6.60e-66
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| C2 | cd00030 | C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ... |
403-502 | 8.38e-12 | ||||
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: 62.47 E-value: 8.38e-12
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| C2 | smart00239 | Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ... |
403-498 | 9.59e-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: 50.95 E-value: 9.59e-08
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| C2 | pfam00168 | C2 domain; |
403-510 | 1.01e-07 | ||||
C2 domain; Pssm-ID: 425499 [Multi-domain] Cd Length: 104 Bit Score: 50.78 E-value: 1.01e-07
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| C2B_RasGAP | cd08675 | C2 domain second repeat of Ras GTPase activating proteins (GAPs); RasGAPs suppress Ras ... |
403-510 | 1.50e-03 | ||||
C2 domain second repeat of Ras GTPase activating proteins (GAPs); RasGAPs suppress Ras function by enhancing the GTPase activity of Ras proteins resulting in the inactive GDP-bound form of Ras. In this way it can control cellular proliferation and differentiation. The proteins here all contain two tandem C2 domains, a Ras-GAP domain, and a pleckstrin homology (PH)-like 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-I topology. Pssm-ID: 176057 [Multi-domain] Cd Length: 137 Bit Score: 39.66 E-value: 1.50e-03
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| C2B_RasA3 | cd04010 | C2 domain second repeat present in RAS p21 protein activator 3 (RasA3); RasA3 are members of ... |
403-498 | 3.71e-03 | ||||
C2 domain second repeat present in RAS p21 protein activator 3 (RasA3); RasA3 are members of GTPase activating protein 1 (GAP1), a Ras-specific GAP, which suppresses Ras function by enhancing the GTPase activity of Ras proteins resulting in the inactive GDP-bound form of Ras. In this way it can control cellular proliferation and differentiation. RasA3 contains an N-terminal C2 domain, a Ras-GAP domain, a plextrin homology (PH)-like domain, and a Bruton's Tyrosine Kinase (BTK) zinc binding 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. This cd contains the second C2 repeat, C2B, and has a type-I topology. Pssm-ID: 175977 [Multi-domain] Cd Length: 148 Bit Score: 38.92 E-value: 3.71e-03
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| C2A_RIM1alpha | cd04031 | C2 domain first repeat contained in Rab3-interacting molecule (RIM) proteins; RIMs are ... |
397-500 | 9.30e-03 | ||||
C2 domain first repeat contained in Rab3-interacting molecule (RIM) proteins; RIMs are believed to organize specialized sites of the plasma membrane called active zones. They also play a role in controlling neurotransmitter release, plasticity processes, as well as memory and learning. RIM contains an N-terminal zinc finger domain, a PDZ domain, and two C-terminal C2 domains (C2A, C2B). 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-I topology and do not bind Ca2+. Pssm-ID: 175997 [Multi-domain] Cd Length: 125 Bit Score: 37.23 E-value: 9.30e-03
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| Blast search parameters | ||||
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