SKP1-like 21 [Arabidopsis thaliana]
SKP1-like protein( domain architecture ID 10649839)
SKP1-like protein is a component of E3 ubiquitin ligase SCF complex involved in ubiquitination and subsequent proteasomal degradation of target proteins
List of domain hits
Name | Accession | Description | Interval | E-value | |||
Skp1 | smart00512 | Found in Skp1 protein family; Family of Skp1 (kinetochore protein required for cell cycle ... |
15-116 | 3.63e-24 | |||
Found in Skp1 protein family; Family of Skp1 (kinetochore protein required for cell cycle progression) and elongin C (subunit of RNA polymerase II transcription factor SIII) homologues. : Pssm-ID: 214704 Cd Length: 104 Bit Score: 95.05 E-value: 3.63e-24
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Skp1 | pfam01466 | Skp1 family, dimerization domain; |
117-156 | 1.49e-10 | |||
Skp1 family, dimerization domain; : Pssm-ID: 460222 Cd Length: 48 Bit Score: 55.97 E-value: 1.49e-10
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serpin super family | cl38926 | SERine Proteinase INhibitors (serpin) family; SERine Proteinase INhibitors (serpins) exhibit ... |
132-192 | 3.59e-03 | |||
SERine Proteinase INhibitors (serpin) family; SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans. The actual alignment was detected with superfamily member cd19955: Pssm-ID: 476815 [Multi-domain] Cd Length: 361 Bit Score: 38.79 E-value: 3.59e-03
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Name | Accession | Description | Interval | E-value | |||
Skp1 | smart00512 | Found in Skp1 protein family; Family of Skp1 (kinetochore protein required for cell cycle ... |
15-116 | 3.63e-24 | |||
Found in Skp1 protein family; Family of Skp1 (kinetochore protein required for cell cycle progression) and elongin C (subunit of RNA polymerase II transcription factor SIII) homologues. Pssm-ID: 214704 Cd Length: 104 Bit Score: 95.05 E-value: 3.63e-24
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SKP1 | COG5201 | SCF ubiquitin ligase, SKP1 component [Posttranslational modification, protein turnover, ... |
16-153 | 3.57e-14 | |||
SCF ubiquitin ligase, SKP1 component [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 227528 [Multi-domain] Cd Length: 158 Bit Score: 69.20 E-value: 3.57e-14
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Skp1 | pfam01466 | Skp1 family, dimerization domain; |
117-156 | 1.49e-10 | |||
Skp1 family, dimerization domain; Pssm-ID: 460222 Cd Length: 48 Bit Score: 55.97 E-value: 1.49e-10
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BTB_POZ_SKP1 | cd18322 | BTB (Broad-Complex, Tramtrack and Bric a brac) /POZ (poxvirus and zinc finger) domain found in ... |
17-131 | 1.04e-07 | |||
BTB (Broad-Complex, Tramtrack and Bric a brac) /POZ (poxvirus and zinc finger) domain found in S-phase kinase-associated protein 1 (SKP1) and similar proteins; SKP1 is also called cyclin-A/CDK2-associated protein p19 (p19A), organ of Corti protein 2 (OCP-2), organ of Corti protein II (OCP-II), RNA polymerase II elongation factor-like protein, transcription elongation factor B polypeptide 1-like, or p19skp1. It is an essential component of the SCF (SKP1-CUL1-F-box protein) ubiquitin ligase complex, which mediates the ubiquitination of proteins involved in cell cycle progression, signal transduction and transcription. SKP1 serves as an adaptor protein that links the F-box protein to CUL1. SKP1 and CUL1 are invariant components of all SCF complexes, while F-box proteins are variable substrate binding modules that determine specificity. SKP1 belongs to the BTB/POZ domain family; the domain is a common protein-protein interaction motif of about 100 amino acids. Pssm-ID: 349631 Cd Length: 120 Bit Score: 49.90 E-value: 1.04e-07
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serpin48-like_insects | cd19955 | insect serpins similar to Tenebrio molitor serpin 48; Serpins in insects function within ... |
132-192 | 3.59e-03 | |||
insect serpins similar to Tenebrio molitor serpin 48; Serpins in insects function within development, wound healing and immunity. Tenebrio molitor serpin 48 (SPN48) is highly specific for Spatzle-processing enzyme, an essential component in insect innate immunity. SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans. Pssm-ID: 381071 [Multi-domain] Cd Length: 361 Bit Score: 38.79 E-value: 3.59e-03
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Name | Accession | Description | Interval | E-value | |||
Skp1 | smart00512 | Found in Skp1 protein family; Family of Skp1 (kinetochore protein required for cell cycle ... |
15-116 | 3.63e-24 | |||
Found in Skp1 protein family; Family of Skp1 (kinetochore protein required for cell cycle progression) and elongin C (subunit of RNA polymerase II transcription factor SIII) homologues. Pssm-ID: 214704 Cd Length: 104 Bit Score: 95.05 E-value: 3.63e-24
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SKP1 | COG5201 | SCF ubiquitin ligase, SKP1 component [Posttranslational modification, protein turnover, ... |
16-153 | 3.57e-14 | |||
SCF ubiquitin ligase, SKP1 component [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 227528 [Multi-domain] Cd Length: 158 Bit Score: 69.20 E-value: 3.57e-14
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Skp1 | pfam01466 | Skp1 family, dimerization domain; |
117-156 | 1.49e-10 | |||
Skp1 family, dimerization domain; Pssm-ID: 460222 Cd Length: 48 Bit Score: 55.97 E-value: 1.49e-10
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BTB_POZ_SKP1 | cd18322 | BTB (Broad-Complex, Tramtrack and Bric a brac) /POZ (poxvirus and zinc finger) domain found in ... |
17-131 | 1.04e-07 | |||
BTB (Broad-Complex, Tramtrack and Bric a brac) /POZ (poxvirus and zinc finger) domain found in S-phase kinase-associated protein 1 (SKP1) and similar proteins; SKP1 is also called cyclin-A/CDK2-associated protein p19 (p19A), organ of Corti protein 2 (OCP-2), organ of Corti protein II (OCP-II), RNA polymerase II elongation factor-like protein, transcription elongation factor B polypeptide 1-like, or p19skp1. It is an essential component of the SCF (SKP1-CUL1-F-box protein) ubiquitin ligase complex, which mediates the ubiquitination of proteins involved in cell cycle progression, signal transduction and transcription. SKP1 serves as an adaptor protein that links the F-box protein to CUL1. SKP1 and CUL1 are invariant components of all SCF complexes, while F-box proteins are variable substrate binding modules that determine specificity. SKP1 belongs to the BTB/POZ domain family; the domain is a common protein-protein interaction motif of about 100 amino acids. Pssm-ID: 349631 Cd Length: 120 Bit Score: 49.90 E-value: 1.04e-07
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serpin48-like_insects | cd19955 | insect serpins similar to Tenebrio molitor serpin 48; Serpins in insects function within ... |
132-192 | 3.59e-03 | |||
insect serpins similar to Tenebrio molitor serpin 48; Serpins in insects function within development, wound healing and immunity. Tenebrio molitor serpin 48 (SPN48) is highly specific for Spatzle-processing enzyme, an essential component in insect innate immunity. SERine Proteinase INhibitors (serpins) exhibit conformational polymorphism shifting from native to cleaved, latent, delta, or polymorphic forms. Many serpins, such as antitrypsin and antichymotrypsin, function as serine protease inhibitors which regulate blood coagulation cascades. Non-inhibitory serpins perform many diverse functions such as chaperoning proteins or transporting hormones. Serpins are of medical interest because mutants have been associated with blood clotting disorders, emphysema, cirrhosis, and dementia. A classification based on evolutionary relatedness has resulted in the assignment of serpins to 16 clades designated A-P along with some orphans. Pssm-ID: 381071 [Multi-domain] Cd Length: 361 Bit Score: 38.79 E-value: 3.59e-03
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Blast search parameters | ||||
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