calpain-5 [Mus musculus]
Protein Classification
CysPc and Calpain_III domain-containing protein( domain architecture ID 12004716)
protein containing domains CysPc, Calpain_III, and C2_Calpain
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| Peptidase_C2 | pfam00648 | Calpain family cysteine protease; |
27-341 | 0e+00 | |||||
Calpain family cysteine protease; : Pssm-ID: 459889 [Multi-domain] Cd Length: 295 Bit Score: 534.00 E-value: 0e+00
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| Calpain_III | cd00214 | Calpain, subdomain III. Calpains are calcium-activated cytoplasmic cysteine proteinases, ... |
352-498 | 3.15e-59 | |||||
Calpain, subdomain III. Calpains are calcium-activated cytoplasmic cysteine proteinases, participate in cytoskeletal remodeling processes, cell differentiation, apoptosis and signal transduction. Catalytic domain and the two calmodulin-like domains are separated by C2-like domain III. Domain III plays an important role in calcium-induced activation of calpain involving electrostatic interactions with subdomain II. Proposed to mediate calpain's interaction with phospholipids and translocation to cytoplasmic/nuclear membranes. CD includes subdomain III of typical and atypical calpains. : Pssm-ID: 238132 Cd Length: 150 Bit Score: 195.21 E-value: 3.15e-59
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| C2_Calpain | cd04046 | C2 domain present in Calpain proteins; A single C2 domain is found in calpains (EC 3.4.22.52, ... |
515-638 | 6.42e-58 | |||||
C2 domain present in Calpain proteins; A single C2 domain is found in calpains (EC 3.4.22.52, EC 3.4.22.53), calcium-dependent, non-lysosomal cysteine proteases. Caplains are classified as belonging to Clan CA by MEROPS and include six families: C1, C2, C10, C12, C28, and C47. 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: 176011 [Multi-domain] Cd Length: 126 Bit Score: 190.95 E-value: 6.42e-58
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| Name | Accession | Description | Interval | E-value | ||||||
| Peptidase_C2 | pfam00648 | Calpain family cysteine protease; |
27-341 | 0e+00 | ||||||
Calpain family cysteine protease; Pssm-ID: 459889 [Multi-domain] Cd Length: 295 Bit Score: 534.00 E-value: 0e+00
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| CysPc | smart00230 | Calpain-like thiol protease family; Calpain-like thiol protease family (peptidase family C2). ... |
13-351 | 1.45e-175 | ||||||
Calpain-like thiol protease family; Calpain-like thiol protease family (peptidase family C2). Calcium activated neutral protease (large subunit). Pssm-ID: 128526 Cd Length: 318 Bit Score: 501.47 E-value: 1.45e-175
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| CysPc | cd00044 | Calpains, domains IIa, IIb; calcium-dependent cytoplasmic cysteine proteinases, papain-like. ... |
16-341 | 1.44e-139 | ||||||
Calpains, domains IIa, IIb; calcium-dependent cytoplasmic cysteine proteinases, papain-like. Functions in cytoskeletal remodeling processes, cell differentiation, apoptosis and signal transduction. Pssm-ID: 238004 [Multi-domain] Cd Length: 315 Bit Score: 409.41 E-value: 1.44e-139
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| Calpain_III | cd00214 | Calpain, subdomain III. Calpains are calcium-activated cytoplasmic cysteine proteinases, ... |
352-498 | 3.15e-59 | ||||||
Calpain, subdomain III. Calpains are calcium-activated cytoplasmic cysteine proteinases, participate in cytoskeletal remodeling processes, cell differentiation, apoptosis and signal transduction. Catalytic domain and the two calmodulin-like domains are separated by C2-like domain III. Domain III plays an important role in calcium-induced activation of calpain involving electrostatic interactions with subdomain II. Proposed to mediate calpain's interaction with phospholipids and translocation to cytoplasmic/nuclear membranes. CD includes subdomain III of typical and atypical calpains. Pssm-ID: 238132 Cd Length: 150 Bit Score: 195.21 E-value: 3.15e-59
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| Calpain_III | pfam01067 | Calpain large subunit, domain III; The function of the domain III and I are currently unknown. ... |
359-488 | 5.49e-58 | ||||||
Calpain large subunit, domain III; The function of the domain III and I are currently unknown. Domain II is a cysteine protease and domain IV is a calcium binding domain. Calpains are believed to participate in intracellular signaling pathways mediated by calcium ions. Pssm-ID: 460050 Cd Length: 136 Bit Score: 191.22 E-value: 5.49e-58
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| C2_Calpain | cd04046 | C2 domain present in Calpain proteins; A single C2 domain is found in calpains (EC 3.4.22.52, ... |
515-638 | 6.42e-58 | ||||||
C2 domain present in Calpain proteins; A single C2 domain is found in calpains (EC 3.4.22.52, EC 3.4.22.53), calcium-dependent, non-lysosomal cysteine proteases. Caplains are classified as belonging to Clan CA by MEROPS and include six families: C1, C2, C10, C12, C28, and C47. 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: 176011 [Multi-domain] Cd Length: 126 Bit Score: 190.95 E-value: 6.42e-58
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| calpain_III | smart00720 | calpain_III domain; |
354-496 | 1.10e-52 | ||||||
calpain_III domain; Pssm-ID: 214786 Cd Length: 143 Bit Score: 177.56 E-value: 1.10e-52
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| C2 | pfam00168 | C2 domain; |
521-609 | 4.06e-09 | ||||||
C2 domain; Pssm-ID: 425499 [Multi-domain] Cd Length: 104 Bit Score: 54.25 E-value: 4.06e-09
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| Name | Accession | Description | Interval | E-value | ||||||
| Peptidase_C2 | pfam00648 | Calpain family cysteine protease; |
27-341 | 0e+00 | ||||||
Calpain family cysteine protease; Pssm-ID: 459889 [Multi-domain] Cd Length: 295 Bit Score: 534.00 E-value: 0e+00
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| CysPc | smart00230 | Calpain-like thiol protease family; Calpain-like thiol protease family (peptidase family C2). ... |
13-351 | 1.45e-175 | ||||||
Calpain-like thiol protease family; Calpain-like thiol protease family (peptidase family C2). Calcium activated neutral protease (large subunit). Pssm-ID: 128526 Cd Length: 318 Bit Score: 501.47 E-value: 1.45e-175
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| CysPc | cd00044 | Calpains, domains IIa, IIb; calcium-dependent cytoplasmic cysteine proteinases, papain-like. ... |
16-341 | 1.44e-139 | ||||||
Calpains, domains IIa, IIb; calcium-dependent cytoplasmic cysteine proteinases, papain-like. Functions in cytoskeletal remodeling processes, cell differentiation, apoptosis and signal transduction. Pssm-ID: 238004 [Multi-domain] Cd Length: 315 Bit Score: 409.41 E-value: 1.44e-139
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| Calpain_III | cd00214 | Calpain, subdomain III. Calpains are calcium-activated cytoplasmic cysteine proteinases, ... |
352-498 | 3.15e-59 | ||||||
Calpain, subdomain III. Calpains are calcium-activated cytoplasmic cysteine proteinases, participate in cytoskeletal remodeling processes, cell differentiation, apoptosis and signal transduction. Catalytic domain and the two calmodulin-like domains are separated by C2-like domain III. Domain III plays an important role in calcium-induced activation of calpain involving electrostatic interactions with subdomain II. Proposed to mediate calpain's interaction with phospholipids and translocation to cytoplasmic/nuclear membranes. CD includes subdomain III of typical and atypical calpains. Pssm-ID: 238132 Cd Length: 150 Bit Score: 195.21 E-value: 3.15e-59
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| Calpain_III | pfam01067 | Calpain large subunit, domain III; The function of the domain III and I are currently unknown. ... |
359-488 | 5.49e-58 | ||||||
Calpain large subunit, domain III; The function of the domain III and I are currently unknown. Domain II is a cysteine protease and domain IV is a calcium binding domain. Calpains are believed to participate in intracellular signaling pathways mediated by calcium ions. Pssm-ID: 460050 Cd Length: 136 Bit Score: 191.22 E-value: 5.49e-58
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| C2_Calpain | cd04046 | C2 domain present in Calpain proteins; A single C2 domain is found in calpains (EC 3.4.22.52, ... |
515-638 | 6.42e-58 | ||||||
C2 domain present in Calpain proteins; A single C2 domain is found in calpains (EC 3.4.22.52, EC 3.4.22.53), calcium-dependent, non-lysosomal cysteine proteases. Caplains are classified as belonging to Clan CA by MEROPS and include six families: C1, C2, C10, C12, C28, and C47. 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: 176011 [Multi-domain] Cd Length: 126 Bit Score: 190.95 E-value: 6.42e-58
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| calpain_III | smart00720 | calpain_III domain; |
354-496 | 1.10e-52 | ||||||
calpain_III domain; Pssm-ID: 214786 Cd Length: 143 Bit Score: 177.56 E-value: 1.10e-52
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| C2 | pfam00168 | C2 domain; |
521-609 | 4.06e-09 | ||||||
C2 domain; Pssm-ID: 425499 [Multi-domain] Cd Length: 104 Bit Score: 54.25 E-value: 4.06e-09
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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 ... |
518-614 | 2.14e-06 | ||||||
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: 47.16 E-value: 2.14e-06
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| C2_ArfGAP | cd04038 | C2 domain present in Arf GTPase Activating Proteins (GAP); ArfGAP is a GTPase activating ... |
533-636 | 4.79e-05 | ||||||
C2 domain present in Arf GTPase Activating Proteins (GAP); ArfGAP is a GTPase activating protein which regulates the ADP ribosylation factor Arf, a member of the Ras superfamily of GTP-binding proteins. The GTP-bound form of Arf is involved in Golgi morphology and is involved in recruiting coat proteins. ArfGAP is responsible for the GDP-bound form of Arf which is necessary for uncoating the membrane and allowing the Golgi to fuse with an acceptor compartment. These proteins contain an N-terminal ArfGAP domain containing the characteristic zinc finger motif (Cys-x2-Cys-x(16,17)-x2-Cys) and C-terminal C2 domain. C2 domains were first identified in Protein Kinase C (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: 176003 [Multi-domain] Cd Length: 145 Bit Score: 43.85 E-value: 4.79e-05
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| C2A_RIM1alpha | cd04031 | C2 domain first repeat contained in Rab3-interacting molecule (RIM) proteins; RIMs are ... |
521-603 | 1.81e-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: 38.77 E-value: 1.81e-03
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| C2_Rab11-FIP_classI | cd08682 | C2 domain found in Rab11-family interacting proteins (FIP) class I; Rab GTPases recruit ... |
519-611 | 2.07e-03 | ||||||
C2 domain found in Rab11-family interacting proteins (FIP) class I; Rab GTPases recruit various effector proteins to organelles and vesicles. Rab11-family interacting proteins (FIPs) are involved in mediating the role of Rab11. FIPs can be divided into three classes: class I FIPs (Rip11a, Rip11b, RCP, and FIP2) which contain a C2 domain after N-terminus of the protein, class II FIPs (FIP3 and FIP4) which contain two EF-hands and a proline rich region, and class III FIPs (FIP1) which exhibits no homology to known protein domains. All FIP proteins contain a highly conserved, 20-amino acid motif at the C-terminus of the protein, known as Rab11/25 binding domain (RBD). Class I FIPs are thought to bind to endocytic membranes via their C2 domain, which interacts directly with phospholipids. Class II FIPs do not have any membrane binding domains leaving much to speculate about the mechanism involving FIP3 and FIP4 interactions with endocytic membranes. The members in this CD are class I FIPs. The exact function of the Rab11 and FIP interaction is unknown, but there is speculation that it involves the role of forming a targeting complex that recruits a group of proteins involved in membrane transport to organelles. 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: 176064 [Multi-domain] Cd Length: 126 Bit Score: 38.59 E-value: 2.07e-03
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| Blast search parameters | ||||
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