methylosome subunit pICln-like [Acanthaster planci]
Voldacs domain-containing protein( domain architecture ID 10507568)
Voldacs (volume decrease after cellular swelling) domain-containing protein similar to Homo sapiens methylosome subunit pICln that is involved in both the assembly of spliceosomal snRNPs and the methylation of Sm proteins
List of domain hits
Name | Accession | Description | Interval | E-value | |||
Voldacs | pfam03517 | Regulator of volume decrease after cellular swelling; ICln is a ubiquitously expressed ... |
33-172 | 4.66e-35 | |||
Regulator of volume decrease after cellular swelling; ICln is a ubiquitously expressed multi-functional protein that plays a critical role in regulating volume decrease in cells after cellular swelling. In plants, ICln induces Cl- currents, thus regulating Cl- homoeostasis in eukaryotes. Structurally, the fold resembles a pleckstrin homology fold, on of whose roles is to recruit and tether their host protein to the cell membrane; and although the surface charges of the ICln fold are not equivalent to those of the PH domain, ICln can be phosphorylated in vitro and the PH-nature of the domain may be the part involving it in the transposition from cytosol to cell membrane during cytotonic swelling. : Pssm-ID: 427344 Cd Length: 139 Bit Score: 121.75 E-value: 4.66e-35
|
|||||||
Name | Accession | Description | Interval | E-value | |||
Voldacs | pfam03517 | Regulator of volume decrease after cellular swelling; ICln is a ubiquitously expressed ... |
33-172 | 4.66e-35 | |||
Regulator of volume decrease after cellular swelling; ICln is a ubiquitously expressed multi-functional protein that plays a critical role in regulating volume decrease in cells after cellular swelling. In plants, ICln induces Cl- currents, thus regulating Cl- homoeostasis in eukaryotes. Structurally, the fold resembles a pleckstrin homology fold, on of whose roles is to recruit and tether their host protein to the cell membrane; and although the surface charges of the ICln fold are not equivalent to those of the PH domain, ICln can be phosphorylated in vitro and the PH-nature of the domain may be the part involving it in the transposition from cytosol to cell membrane during cytotonic swelling. Pssm-ID: 427344 Cd Length: 139 Bit Score: 121.75 E-value: 4.66e-35
|
|||||||
Name | Accession | Description | Interval | E-value | |||
Voldacs | pfam03517 | Regulator of volume decrease after cellular swelling; ICln is a ubiquitously expressed ... |
33-172 | 4.66e-35 | |||
Regulator of volume decrease after cellular swelling; ICln is a ubiquitously expressed multi-functional protein that plays a critical role in regulating volume decrease in cells after cellular swelling. In plants, ICln induces Cl- currents, thus regulating Cl- homoeostasis in eukaryotes. Structurally, the fold resembles a pleckstrin homology fold, on of whose roles is to recruit and tether their host protein to the cell membrane; and although the surface charges of the ICln fold are not equivalent to those of the PH domain, ICln can be phosphorylated in vitro and the PH-nature of the domain may be the part involving it in the transposition from cytosol to cell membrane during cytotonic swelling. Pssm-ID: 427344 Cd Length: 139 Bit Score: 121.75 E-value: 4.66e-35
|
|||||||
Blast search parameters | ||||
|