stolid, isoform M [Drosophila melanogaster]
calcium channel subunit alpha-2/delta family protein( domain architecture ID 13750223)
calcium channel subunit alpha-2/delta family protein similar to Homo sapiens voltage-dependent calcium channel subunit alpha-2/delta-4 that regulates calcium current density and activation/inactivation kinetics of the calcium channel
List of domain hits
Name | Accession | Description | Interval | E-value | |||||
vWA_VGCC_like | cd01463 | VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five ... |
245-428 | 8.35e-92 | |||||
VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five proteins: alpha 1, beta 1, gamma, alpha 2 and delta. The alpha 2 and delta subunits result from proteolytic processing of a single gene product and carries at its N-terminus the VWA and cache domains, The alpha 2 delta gene family has orthologues in D. melanogaster and C. elegans but none have been detected in aither A. thaliana or yeast. The exact biochemical function of the VWA domain is not known but the alpha 2 delta complex has been shown to regulate various functional properties of the channel complex. : Pssm-ID: 238740 [Multi-domain] Cd Length: 190 Bit Score: 293.53 E-value: 8.35e-92
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VWA_N super family | cl07136 | VWA N-terminal; This domain is found at the N-terminus of proteins containing von Willebrand ... |
130-230 | 4.54e-22 | |||||
VWA N-terminal; This domain is found at the N-terminus of proteins containing von Willebrand factor type A (VWA, pfam00092) and Cache (pfam02743) domains. It has been found in vertebrates, Drosophila and C. elegans but has not yet been identified in other eukaryotes. It is probably involved in the function of some voltage-dependent calcium channel subunits. The actual alignment was detected with superfamily member pfam08399: Pssm-ID: 462464 Cd Length: 122 Bit Score: 92.75 E-value: 4.54e-22
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VGCC_alpha2 super family | cl07190 | Neuronal voltage-dependent calcium channel alpha 2acd; This eukaryotic domain has been found ... |
775-1037 | 1.92e-13 | |||||
Neuronal voltage-dependent calcium channel alpha 2acd; This eukaryotic domain has been found in the neuronal voltage-dependent calcium channel (VGCC) alpha 2a, 2c, and 2d subunits. It is also found in other calcium channel alpha-2 delta subunits to the C-terminus of a Cache domain (pfam02743). The actual alignment was detected with superfamily member pfam08473: Pssm-ID: 462488 Cd Length: 432 Bit Score: 73.95 E-value: 1.92e-13
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PDC2_MCP_like | cd12912 | second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; ... |
511-643 | 2.37e-12 | |||||
second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; Members of this subfamily display varying domain architectures but all contain double PDC (PhoQ/DcuS/CitA) sensor domains. This model represents the second PDC domain of Methyl-accepting chemotaxis proteins (MCPs), Histidine kinases (HKs), and other similar domains. Many members contain both HAMP (HK, Adenylyl cyclase, MCP, and Phosphatase) and MCP domains, which are signalling domains that interact with protein partners to relay a signal. MCPs are part of a transmembrane protein complex that controls bacterial chemotaxis. HK receptors are part of two-component systems (TCS) in bacteria that play a critical role for sensing and adapting to environmental changes. Typically, HK receptors contain an extracellular sensing domain flanked by two transmembrane helices, an intracellular dimerization histidine phosphorylation domain (DHp), and a C-terminal kinase domain, with many variations on this theme. In the case of HKs, signals detected by the sensor domain are transmitted through DHp to the kinase domain, resulting in the phosphorylation of a conserved histidine residue in DHp; phosphotransfer to a conserved aspartate in its cognate response regulator (RR) follows, which leads to the activation of genes for downstream cellular responses. : Pssm-ID: 350337 [Multi-domain] Cd Length: 92 Bit Score: 63.94 E-value: 2.37e-12
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Name | Accession | Description | Interval | E-value | |||||
vWA_VGCC_like | cd01463 | VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five ... |
245-428 | 8.35e-92 | |||||
VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five proteins: alpha 1, beta 1, gamma, alpha 2 and delta. The alpha 2 and delta subunits result from proteolytic processing of a single gene product and carries at its N-terminus the VWA and cache domains, The alpha 2 delta gene family has orthologues in D. melanogaster and C. elegans but none have been detected in aither A. thaliana or yeast. The exact biochemical function of the VWA domain is not known but the alpha 2 delta complex has been shown to regulate various functional properties of the channel complex. Pssm-ID: 238740 [Multi-domain] Cd Length: 190 Bit Score: 293.53 E-value: 8.35e-92
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VWA_N | pfam08399 | VWA N-terminal; This domain is found at the N-terminus of proteins containing von Willebrand ... |
130-230 | 4.54e-22 | |||||
VWA N-terminal; This domain is found at the N-terminus of proteins containing von Willebrand factor type A (VWA, pfam00092) and Cache (pfam02743) domains. It has been found in vertebrates, Drosophila and C. elegans but has not yet been identified in other eukaryotes. It is probably involved in the function of some voltage-dependent calcium channel subunits. Pssm-ID: 462464 Cd Length: 122 Bit Score: 92.75 E-value: 4.54e-22
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VWA | smart00327 | von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ... |
259-436 | 4.02e-15 | |||||
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: 74.80 E-value: 4.02e-15
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VGCC_alpha2 | pfam08473 | Neuronal voltage-dependent calcium channel alpha 2acd; This eukaryotic domain has been found ... |
775-1037 | 1.92e-13 | |||||
Neuronal voltage-dependent calcium channel alpha 2acd; This eukaryotic domain has been found in the neuronal voltage-dependent calcium channel (VGCC) alpha 2a, 2c, and 2d subunits. It is also found in other calcium channel alpha-2 delta subunits to the C-terminus of a Cache domain (pfam02743). Pssm-ID: 462488 Cd Length: 432 Bit Score: 73.95 E-value: 1.92e-13
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VWA | pfam00092 | von Willebrand factor type A domain; |
259-429 | 4.77e-13 | |||||
von Willebrand factor type A domain; Pssm-ID: 459670 [Multi-domain] Cd Length: 174 Bit Score: 68.46 E-value: 4.77e-13
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PDC2_MCP_like | cd12912 | second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; ... |
511-643 | 2.37e-12 | |||||
second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; Members of this subfamily display varying domain architectures but all contain double PDC (PhoQ/DcuS/CitA) sensor domains. This model represents the second PDC domain of Methyl-accepting chemotaxis proteins (MCPs), Histidine kinases (HKs), and other similar domains. Many members contain both HAMP (HK, Adenylyl cyclase, MCP, and Phosphatase) and MCP domains, which are signalling domains that interact with protein partners to relay a signal. MCPs are part of a transmembrane protein complex that controls bacterial chemotaxis. HK receptors are part of two-component systems (TCS) in bacteria that play a critical role for sensing and adapting to environmental changes. Typically, HK receptors contain an extracellular sensing domain flanked by two transmembrane helices, an intracellular dimerization histidine phosphorylation domain (DHp), and a C-terminal kinase domain, with many variations on this theme. In the case of HKs, signals detected by the sensor domain are transmitted through DHp to the kinase domain, resulting in the phosphorylation of a conserved histidine residue in DHp; phosphotransfer to a conserved aspartate in its cognate response regulator (RR) follows, which leads to the activation of genes for downstream cellular responses. Pssm-ID: 350337 [Multi-domain] Cd Length: 92 Bit Score: 63.94 E-value: 2.37e-12
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YfbK | COG2304 | Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ... |
252-434 | 5.31e-11 | |||||
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function prediction only]; Pssm-ID: 441879 [Multi-domain] Cd Length: 289 Bit Score: 65.12 E-value: 5.31e-11
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dCache_1 | pfam02743 | Cache domain; Double cache domain 1 covers the last three strands from the membrane distal ... |
472-562 | 1.63e-10 | |||||
Cache domain; Double cache domain 1 covers the last three strands from the membrane distal PAS-like domain, the first two strands of the membrane proximal domain, and the connecting elements between the two domains. This domain when present in chemoreceptors recognize several signals such as proteinogenic amino acids, GABA, Histamine and polyamines, decanoic acid, Autoinducer-2, purine derivatives, quaternary amines, citrate and taurine, among others. When associated with histidine kinases, it recognizes C3/C4-dicarboxylic acids, Spermine, guanosine and Autoinducer-2 (Mantilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1 https://doi.org/10.1093/femsre/fuab043). Pssm-ID: 460673 [Multi-domain] Cd Length: 237 Bit Score: 62.74 E-value: 1.63e-10
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Name | Accession | Description | Interval | E-value | |||||
vWA_VGCC_like | cd01463 | VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five ... |
245-428 | 8.35e-92 | |||||
VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five proteins: alpha 1, beta 1, gamma, alpha 2 and delta. The alpha 2 and delta subunits result from proteolytic processing of a single gene product and carries at its N-terminus the VWA and cache domains, The alpha 2 delta gene family has orthologues in D. melanogaster and C. elegans but none have been detected in aither A. thaliana or yeast. The exact biochemical function of the VWA domain is not known but the alpha 2 delta complex has been shown to regulate various functional properties of the channel complex. Pssm-ID: 238740 [Multi-domain] Cd Length: 190 Bit Score: 293.53 E-value: 8.35e-92
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VWA_N | pfam08399 | VWA N-terminal; This domain is found at the N-terminus of proteins containing von Willebrand ... |
130-230 | 4.54e-22 | |||||
VWA N-terminal; This domain is found at the N-terminus of proteins containing von Willebrand factor type A (VWA, pfam00092) and Cache (pfam02743) domains. It has been found in vertebrates, Drosophila and C. elegans but has not yet been identified in other eukaryotes. It is probably involved in the function of some voltage-dependent calcium channel subunits. Pssm-ID: 462464 Cd Length: 122 Bit Score: 92.75 E-value: 4.54e-22
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VWA | smart00327 | von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ... |
259-436 | 4.02e-15 | |||||
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: 74.80 E-value: 4.02e-15
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VGCC_alpha2 | pfam08473 | Neuronal voltage-dependent calcium channel alpha 2acd; This eukaryotic domain has been found ... |
775-1037 | 1.92e-13 | |||||
Neuronal voltage-dependent calcium channel alpha 2acd; This eukaryotic domain has been found in the neuronal voltage-dependent calcium channel (VGCC) alpha 2a, 2c, and 2d subunits. It is also found in other calcium channel alpha-2 delta subunits to the C-terminus of a Cache domain (pfam02743). Pssm-ID: 462488 Cd Length: 432 Bit Score: 73.95 E-value: 1.92e-13
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VWA | pfam00092 | von Willebrand factor type A domain; |
259-429 | 4.77e-13 | |||||
von Willebrand factor type A domain; Pssm-ID: 459670 [Multi-domain] Cd Length: 174 Bit Score: 68.46 E-value: 4.77e-13
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vWA_interalpha_trypsin_inhibitor | cd01461 | vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ... |
257-436 | 1.32e-12 | |||||
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- two heavy chains and one light chain (bikunin). Bikunin confers the protease-inhibitor function while the heavy chains are involved in rendering stability to the extracellular matrix by binding to hyaluronic acid. The heavy chains carry the VWA domain with a conserved MIDAS motif. Although the exact role of the VWA domains remains unknown, it has been speculated to be involved in mediating protein-protein interactions with the components of the extracellular matrix. Pssm-ID: 238738 [Multi-domain] Cd Length: 171 Bit Score: 67.24 E-value: 1.32e-12
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PDC2_MCP_like | cd12912 | second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; ... |
511-643 | 2.37e-12 | |||||
second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; Members of this subfamily display varying domain architectures but all contain double PDC (PhoQ/DcuS/CitA) sensor domains. This model represents the second PDC domain of Methyl-accepting chemotaxis proteins (MCPs), Histidine kinases (HKs), and other similar domains. Many members contain both HAMP (HK, Adenylyl cyclase, MCP, and Phosphatase) and MCP domains, which are signalling domains that interact with protein partners to relay a signal. MCPs are part of a transmembrane protein complex that controls bacterial chemotaxis. HK receptors are part of two-component systems (TCS) in bacteria that play a critical role for sensing and adapting to environmental changes. Typically, HK receptors contain an extracellular sensing domain flanked by two transmembrane helices, an intracellular dimerization histidine phosphorylation domain (DHp), and a C-terminal kinase domain, with many variations on this theme. In the case of HKs, signals detected by the sensor domain are transmitted through DHp to the kinase domain, resulting in the phosphorylation of a conserved histidine residue in DHp; phosphotransfer to a conserved aspartate in its cognate response regulator (RR) follows, which leads to the activation of genes for downstream cellular responses. Pssm-ID: 350337 [Multi-domain] Cd Length: 92 Bit Score: 63.94 E-value: 2.37e-12
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vWFA | cd00198 | Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ... |
259-422 | 2.42e-12 | |||||
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: 66.05 E-value: 2.42e-12
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YfbK | COG2304 | Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ... |
252-434 | 5.31e-11 | |||||
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function prediction only]; Pssm-ID: 441879 [Multi-domain] Cd Length: 289 Bit Score: 65.12 E-value: 5.31e-11
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dCache_1 | pfam02743 | Cache domain; Double cache domain 1 covers the last three strands from the membrane distal ... |
472-562 | 1.63e-10 | |||||
Cache domain; Double cache domain 1 covers the last three strands from the membrane distal PAS-like domain, the first two strands of the membrane proximal domain, and the connecting elements between the two domains. This domain when present in chemoreceptors recognize several signals such as proteinogenic amino acids, GABA, Histamine and polyamines, decanoic acid, Autoinducer-2, purine derivatives, quaternary amines, citrate and taurine, among others. When associated with histidine kinases, it recognizes C3/C4-dicarboxylic acids, Spermine, guanosine and Autoinducer-2 (Mantilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1 https://doi.org/10.1093/femsre/fuab043). Pssm-ID: 460673 [Multi-domain] Cd Length: 237 Bit Score: 62.74 E-value: 1.63e-10
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PDC2_HK_sensor | cd18774 | second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins, ... |
511-642 | 3.85e-10 | |||||
second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins, diguanylate-cyclase and similar domains; Histidine kinase (HK) receptors are part of two-component systems (TCS) in bacteria that play a critical role for sensing and adapting to environmental changes. Typically, HK receptors contain an extracellular sensing domain flanked by two transmembrane helices, an intracellular dimerization histidine phosphorylation domain (DHp), and a C-terminal kinase domain, with many variations on this theme. HK receptors in this family contain double PDC (PhoQ/DcuS/CitA) sensor domains. Signals detected by the sensor domain are transmitted through DHp to the kinase domain, resulting in the phosphorylation of a conserved histidine residue in DHp; phosphotransfer to a conserved aspartate in its cognate response regulator (RR) follows, which leads to the activation of genes for downstream cellular responses. The HK family includes not just histidine kinase receptors but also sensors for chemotaxis proteins and diguanylate cyclase receptors, implying a combinatorial molecular evolution. Pssm-ID: 350342 [Multi-domain] Cd Length: 89 Bit Score: 57.84 E-value: 3.85e-10
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ViaA | COG2425 | Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ... |
240-406 | 2.03e-09 | |||||
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain [Function unknown]; Pssm-ID: 441973 [Multi-domain] Cd Length: 263 Bit Score: 60.08 E-value: 2.03e-09
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ChlD | COG1240 | vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ... |
180-429 | 5.24e-09 | |||||
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and metabolism]; Pssm-ID: 440853 [Multi-domain] Cd Length: 262 Bit Score: 58.80 E-value: 5.24e-09
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vWA_subgroup | cd01465 | VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ... |
263-372 | 1.95e-07 | |||||
VWA subgroup: 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. Not much is known about the function of the VWA domain in these proteins. The members do have a conserved MIDAS motif. The biochemical function however is not known. Pssm-ID: 238742 [Multi-domain] Cd Length: 170 Bit Score: 52.28 E-value: 1.95e-07
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vWA_C3HC4_type | cd01466 | VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood ... |
259-421 | 4.83e-07 | |||||
VWA C3HC4-type: 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. Membes of this subgroup belong to Zinc-finger family as they are found fused to RING finger domains. The MIDAS motif is not conserved in all the members of this family. The function of vWA domains however is not known. Pssm-ID: 238743 [Multi-domain] Cd Length: 155 Bit Score: 50.85 E-value: 4.83e-07
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vWFA_subfamily_ECM | cd01450 | Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ... |
259-384 | 6.02e-07 | |||||
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: 238727 [Multi-domain] Cd Length: 161 Bit Score: 50.75 E-value: 6.02e-07
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VWA_2 | pfam13519 | von Willebrand factor type A domain; |
260-354 | 3.63e-06 | |||||
von Willebrand factor type A domain; Pssm-ID: 463909 [Multi-domain] Cd Length: 103 Bit Score: 46.90 E-value: 3.63e-06
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VWA_3 | pfam13768 | von Willebrand factor type A domain; |
258-422 | 5.49e-06 | |||||
von Willebrand factor type A domain; Pssm-ID: 372716 [Multi-domain] Cd Length: 155 Bit Score: 47.78 E-value: 5.49e-06
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vWA_collagen | cd01472 | von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ... |
258-377 | 2.49e-03 | |||||
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This domain has a variety of functions including: intermolecular adhesion, cell migration, signalling, transcription, and DNA repair. In integrins these domains form heterodimers while in vWF it forms homodimers and multimers. There are different interaction surfaces of this domain as seen by its complexes with collagen with either integrin or human vWFA. In integrins collagen binding occurs via the metal ion-dependent adhesion site (MIDAS) and involves three surface loops located on the upper surface of the molecule. In human vWFA, collagen binding is thought to occur on the bottom of the molecule and does not involve the vestigial MIDAS motif. Pssm-ID: 238749 [Multi-domain] Cd Length: 164 Bit Score: 39.90 E-value: 2.49e-03
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Blast search parameters | ||||
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