copine-5 isoform X5 [Hyaena hyaena]
Protein Classification
copine family protein( domain architecture ID 10106945)
copine family protein is typically a C2 domain-containing, calcium-dependent, phospholipid-binding protein that is involved in membrane trafficking, protein-protein interactions, and cell division and growth; lacks the C2 domain
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| vWA_copine_like | cd01459 | VWA Copine: Copines are phospholipid-binding proteins originally identified in paramecium. ... |
2-262 | 1.53e-142 | |||||
VWA Copine: Copines are phospholipid-binding proteins originally identified in paramecium. They are found in human and orthologues have been found in C. elegans and Arabidopsis Thaliana. None have been found in D. Melanogaster or S. Cereviciae. Phylogenetic distribution suggests that copines have been lost in some eukaryotes. No functional properties have been assigned to the VWA domains present in copines. The members of this subgroup contain a functional MIDAS motif based on their preferential binding to magnesium and manganese. However, the MIDAS motif is not totally conserved, in most cases the MIDAS consists of the sequence DxTxS instead of the motif DxSxS that is found in most cases. The C2 domains present in copines mediate phospholipid binding. : Pssm-ID: 238736 Cd Length: 254 Bit Score: 401.75 E-value: 1.53e-142
|
|||||||||
| Name | Accession | Description | Interval | E-value | |||||
| vWA_copine_like | cd01459 | VWA Copine: Copines are phospholipid-binding proteins originally identified in paramecium. ... |
2-262 | 1.53e-142 | |||||
VWA Copine: Copines are phospholipid-binding proteins originally identified in paramecium. They are found in human and orthologues have been found in C. elegans and Arabidopsis Thaliana. None have been found in D. Melanogaster or S. Cereviciae. Phylogenetic distribution suggests that copines have been lost in some eukaryotes. No functional properties have been assigned to the VWA domains present in copines. The members of this subgroup contain a functional MIDAS motif based on their preferential binding to magnesium and manganese. However, the MIDAS motif is not totally conserved, in most cases the MIDAS consists of the sequence DxTxS instead of the motif DxSxS that is found in most cases. The C2 domains present in copines mediate phospholipid binding. Pssm-ID: 238736 Cd Length: 254 Bit Score: 401.75 E-value: 1.53e-142
|
|||||||||
| Copine | pfam07002 | Copine; This family represents a conserved region approximately 220 residues long within ... |
55-270 | 3.52e-124 | |||||
Copine; This family represents a conserved region approximately 220 residues long within eukaryotic copines. Copines are Ca(2+)-dependent phospholipid-binding proteins that are thought to be involved in membrane-trafficking, and may also be involved in cell division and growth. Pssm-ID: 462064 Cd Length: 214 Bit Score: 353.56 E-value: 3.52e-124
|
|||||||||
| VWA | smart00327 | von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ... |
36-201 | 1.75e-09 | |||||
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods. Pssm-ID: 214621 [Multi-domain] Cd Length: 175 Bit Score: 55.92 E-value: 1.75e-09
|
|||||||||
| Name | Accession | Description | Interval | E-value | |||||
| vWA_copine_like | cd01459 | VWA Copine: Copines are phospholipid-binding proteins originally identified in paramecium. ... |
2-262 | 1.53e-142 | |||||
VWA Copine: Copines are phospholipid-binding proteins originally identified in paramecium. They are found in human and orthologues have been found in C. elegans and Arabidopsis Thaliana. None have been found in D. Melanogaster or S. Cereviciae. Phylogenetic distribution suggests that copines have been lost in some eukaryotes. No functional properties have been assigned to the VWA domains present in copines. The members of this subgroup contain a functional MIDAS motif based on their preferential binding to magnesium and manganese. However, the MIDAS motif is not totally conserved, in most cases the MIDAS consists of the sequence DxTxS instead of the motif DxSxS that is found in most cases. The C2 domains present in copines mediate phospholipid binding. Pssm-ID: 238736 Cd Length: 254 Bit Score: 401.75 E-value: 1.53e-142
|
|||||||||
| Copine | pfam07002 | Copine; This family represents a conserved region approximately 220 residues long within ... |
55-270 | 3.52e-124 | |||||
Copine; This family represents a conserved region approximately 220 residues long within eukaryotic copines. Copines are Ca(2+)-dependent phospholipid-binding proteins that are thought to be involved in membrane-trafficking, and may also be involved in cell division and growth. Pssm-ID: 462064 Cd Length: 214 Bit Score: 353.56 E-value: 3.52e-124
|
|||||||||
| VWA | smart00327 | von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ... |
36-201 | 1.75e-09 | |||||
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods. Pssm-ID: 214621 [Multi-domain] Cd Length: 175 Bit Score: 55.92 E-value: 1.75e-09
|
|||||||||
| vWA-TerF-like | pfam10138 | vWA found in TerF C terminus; vWA domain fused to TerD domain typified by the TerF protein. ... |
138-210 | 2.22e-05 | |||||
vWA found in TerF C terminus; vWA domain fused to TerD domain typified by the TerF protein. Some times found as solos. Pssm-ID: 401947 [Multi-domain] Cd Length: 200 Bit Score: 44.59 E-value: 2.22e-05
|
|||||||||
| vWFA | cd00198 | Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ... |
135-213 | 2.05e-03 | |||||
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. Pssm-ID: 238119 [Multi-domain] Cd Length: 161 Bit Score: 38.32 E-value: 2.05e-03
|
|||||||||
| Blast search parameters | ||||
|
