target of rapamycin complex 2 subunit ste20 [Schizosaccharomyces pombe]
Protein Classification
RICTOR family protein( domain architecture ID 10209961)
RICTOR (rapamycin-insensitive companion of mTOR) family protein similar to Schizosaccharomyces pombe target of rapamycin complex 2 subunit ste20 is a component of TORC2, which regulates multiple cellular processes to control cell growth in response to environmental signals
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||
| RICTOR_N | pfam14664 | Rapamycin-insensitive companion of mTOR, N-term; Rictor appears to serve as a scaffolding ... |
235-612 | 1.89e-106 | ||||||
Rapamycin-insensitive companion of mTOR, N-term; Rictor appears to serve as a scaffolding protein that is important for maintaining mTORC2 integrity. The mammalian target of rapamycin (mTOR) is a conserved Ser/Thr kinase that forms two functionally distinct complexes, mTROC1 and mTORC2, important for nutrient and growth-factor signalling. This region is the N-terminal conserved section that may include several individual domains. Rictor can be inhibited in the short-term by rapamycin. : Pssm-ID: 464246 Cd Length: 372 Bit Score: 341.44 E-value: 1.89e-106
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| RICTOR_M | pfam14666 | Rapamycin-insensitive companion of mTOR, middle domain; Rictor appears to serve as a ... |
818-917 | 8.58e-39 | ||||||
Rapamycin-insensitive companion of mTOR, middle domain; Rictor appears to serve as a scaffolding protein that is important for maintaining mTORC2 integrity. The mammalian target of rapamycin (mTOR) is a conserved Ser/Thr kinase that forms two functionally distinct complexes, mTROC1 and mTORC2, important for nutrient and growth-factor signalling. This region is the more conserved central section that may include several individual domains. Rictor can be inhibited in the short-term by rapamycin. : Pssm-ID: 464248 Cd Length: 104 Bit Score: 139.91 E-value: 8.58e-39
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| RasGEF_N_2 | pfam14663 | Rapamycin-insensitive companion of mTOR RasGEF_N domain; Rictor appears to serve as a ... |
926-1024 | 2.98e-37 | ||||||
Rapamycin-insensitive companion of mTOR RasGEF_N domain; Rictor appears to serve as a scaffolding protein that is important for maintaining mTORC2 integrity. The mammalian target of rapamycin (mTOR) is a conserved Ser/Thr kinase that forms two functionally distinct complexes, mTROC1 and mTORC2, important for nutrient and growth-factor signalling. This region is the more conserved central section that may include several individual domains. Rictor can be inhibited in the short-term by rapamycin. : Pssm-ID: 464245 Cd Length: 107 Bit Score: 135.79 E-value: 2.98e-37
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| RICTOR_V | pfam14668 | Rapamycin-insensitive companion of mTOR, domain 5; Rictor appears to serve as a scaffolding ... |
1095-1165 | 1.19e-29 | ||||||
Rapamycin-insensitive companion of mTOR, domain 5; Rictor appears to serve as a scaffolding protein that is important for maintaining mTORC2 integrity. The mammalian target of rapamycin (mTOR) is a conserved Ser/Thr kinase that forms two functionally distinct complexes, mTROC1 and mTORC2, important for nutrient and growth-factor signalling. These long eukaryotic proteins carry several well-conserved domains, and this is No.5. : Pssm-ID: 464249 Cd Length: 71 Bit Score: 112.55 E-value: 1.19e-29
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| HR1 super family | cl00087 | Protein kinase C-related kinase homology region 1 (HR1) domain that binds Rho family small ... |
34-108 | 6.08e-26 | ||||||
Protein kinase C-related kinase homology region 1 (HR1) domain that binds Rho family small GTPases; The HR1 domain, also called the ACC (anti-parallel coiled-coil) finger domain or Rho-binding domain binds small GTPases from the Rho family. It is found in Rho effector proteins including PKC-related kinases such as vertebrate PRK1 (or PKN) and yeast PKC1 protein kinases C, as well as in rhophilins and Rho-associated kinase (ROCK). Rho family members function as molecular switches, cycling between inactive and active forms, controlling a variety of cellular processes. HR1 domains may occur in repeat arrangements (PKN contains three HR1 domains), separated by a short linker region. The actual alignment was detected with superfamily member cd11627: Pssm-ID: 469609 [Multi-domain] Cd Length: 71 Bit Score: 102.07 E-value: 6.08e-26
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| Name | Accession | Description | Interval | E-value | ||||||
| RICTOR_N | pfam14664 | Rapamycin-insensitive companion of mTOR, N-term; Rictor appears to serve as a scaffolding ... |
235-612 | 1.89e-106 | ||||||
Rapamycin-insensitive companion of mTOR, N-term; Rictor appears to serve as a scaffolding protein that is important for maintaining mTORC2 integrity. The mammalian target of rapamycin (mTOR) is a conserved Ser/Thr kinase that forms two functionally distinct complexes, mTROC1 and mTORC2, important for nutrient and growth-factor signalling. This region is the N-terminal conserved section that may include several individual domains. Rictor can be inhibited in the short-term by rapamycin. Pssm-ID: 464246 Cd Length: 372 Bit Score: 341.44 E-value: 1.89e-106
|
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| RICTOR_M | pfam14666 | Rapamycin-insensitive companion of mTOR, middle domain; Rictor appears to serve as a ... |
818-917 | 8.58e-39 | ||||||
Rapamycin-insensitive companion of mTOR, middle domain; Rictor appears to serve as a scaffolding protein that is important for maintaining mTORC2 integrity. The mammalian target of rapamycin (mTOR) is a conserved Ser/Thr kinase that forms two functionally distinct complexes, mTROC1 and mTORC2, important for nutrient and growth-factor signalling. This region is the more conserved central section that may include several individual domains. Rictor can be inhibited in the short-term by rapamycin. Pssm-ID: 464248 Cd Length: 104 Bit Score: 139.91 E-value: 8.58e-39
|
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| RasGEF_N_2 | pfam14663 | Rapamycin-insensitive companion of mTOR RasGEF_N domain; Rictor appears to serve as a ... |
926-1024 | 2.98e-37 | ||||||
Rapamycin-insensitive companion of mTOR RasGEF_N domain; Rictor appears to serve as a scaffolding protein that is important for maintaining mTORC2 integrity. The mammalian target of rapamycin (mTOR) is a conserved Ser/Thr kinase that forms two functionally distinct complexes, mTROC1 and mTORC2, important for nutrient and growth-factor signalling. This region is the more conserved central section that may include several individual domains. Rictor can be inhibited in the short-term by rapamycin. Pssm-ID: 464245 Cd Length: 107 Bit Score: 135.79 E-value: 2.98e-37
|
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| RICTOR_V | pfam14668 | Rapamycin-insensitive companion of mTOR, domain 5; Rictor appears to serve as a scaffolding ... |
1095-1165 | 1.19e-29 | ||||||
Rapamycin-insensitive companion of mTOR, domain 5; Rictor appears to serve as a scaffolding protein that is important for maintaining mTORC2 integrity. The mammalian target of rapamycin (mTOR) is a conserved Ser/Thr kinase that forms two functionally distinct complexes, mTROC1 and mTORC2, important for nutrient and growth-factor signalling. These long eukaryotic proteins carry several well-conserved domains, and this is No.5. Pssm-ID: 464249 Cd Length: 71 Bit Score: 112.55 E-value: 1.19e-29
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| HR1_Ste20-like | cd11627 | Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of ... |
34-108 | 6.08e-26 | ||||||
Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Schizosaccharomyces pombe Ste20-like proteins; This group is composed of predominantly uncharacterized fungal proteins, which contain two known domains: HR1 at the N-terminal region and REM (Ras exchanger motif) at the C-terminal region. One member protein from Schizosaccharomyces pombe is named Ste16 while its gene is called ste20 (a target of rapamycin complex 2 subunit). It is a subunit in the protein kinase TOR complexes in fission yeast. The REM domain is usually found in nucleotide exchange factors for Ras-like small GTPases. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family. Pssm-ID: 212017 [Multi-domain] Cd Length: 71 Bit Score: 102.07 E-value: 6.08e-26
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| Hr1 | smart00742 | Rho effector or protein kinase C-related kinase homology region 1 homologues; Alpha-helical ... |
38-102 | 1.11e-08 | ||||||
Rho effector or protein kinase C-related kinase homology region 1 homologues; Alpha-helical domain found in vertebrate PRK1 and yeast PKC1 protein kinases C. The HR1 in rhophilin bind RhoGTP; those in PRK1 bind RhoA and RhoB. Also called RBD - Rho-binding domain Pssm-ID: 128981 Cd Length: 57 Bit Score: 52.58 E-value: 1.11e-08
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| HR1 | pfam02185 | Hr1 repeat; The HR1 repeat was first described as a three times repeated homology region of ... |
40-105 | 3.32e-07 | ||||||
Hr1 repeat; The HR1 repeat was first described as a three times repeated homology region of the N-terminal non-catalytic part of protein kinase PRK1(PKN). The first two of these repeats were later shown to bind the small G protein rho known to activate PKN in its GTP-bound form. Similar rho-binding domains also occur in a number of other protein kinases and in the rho-binding proteins rhophilin and rhotekin. Recently, the structure of the N-terminal HR1 repeat complexed with RhoA has been determined by X-ray crystallography. It forms an antiparallel coiled-coil fold termed an ACC finger. Pssm-ID: 460478 [Multi-domain] Cd Length: 67 Bit Score: 48.67 E-value: 3.32e-07
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| Name | Accession | Description | Interval | E-value | ||||||
| RICTOR_N | pfam14664 | Rapamycin-insensitive companion of mTOR, N-term; Rictor appears to serve as a scaffolding ... |
235-612 | 1.89e-106 | ||||||
Rapamycin-insensitive companion of mTOR, N-term; Rictor appears to serve as a scaffolding protein that is important for maintaining mTORC2 integrity. The mammalian target of rapamycin (mTOR) is a conserved Ser/Thr kinase that forms two functionally distinct complexes, mTROC1 and mTORC2, important for nutrient and growth-factor signalling. This region is the N-terminal conserved section that may include several individual domains. Rictor can be inhibited in the short-term by rapamycin. Pssm-ID: 464246 Cd Length: 372 Bit Score: 341.44 E-value: 1.89e-106
|
||||||||||
| RICTOR_M | pfam14666 | Rapamycin-insensitive companion of mTOR, middle domain; Rictor appears to serve as a ... |
818-917 | 8.58e-39 | ||||||
Rapamycin-insensitive companion of mTOR, middle domain; Rictor appears to serve as a scaffolding protein that is important for maintaining mTORC2 integrity. The mammalian target of rapamycin (mTOR) is a conserved Ser/Thr kinase that forms two functionally distinct complexes, mTROC1 and mTORC2, important for nutrient and growth-factor signalling. This region is the more conserved central section that may include several individual domains. Rictor can be inhibited in the short-term by rapamycin. Pssm-ID: 464248 Cd Length: 104 Bit Score: 139.91 E-value: 8.58e-39
|
||||||||||
| RasGEF_N_2 | pfam14663 | Rapamycin-insensitive companion of mTOR RasGEF_N domain; Rictor appears to serve as a ... |
926-1024 | 2.98e-37 | ||||||
Rapamycin-insensitive companion of mTOR RasGEF_N domain; Rictor appears to serve as a scaffolding protein that is important for maintaining mTORC2 integrity. The mammalian target of rapamycin (mTOR) is a conserved Ser/Thr kinase that forms two functionally distinct complexes, mTROC1 and mTORC2, important for nutrient and growth-factor signalling. This region is the more conserved central section that may include several individual domains. Rictor can be inhibited in the short-term by rapamycin. Pssm-ID: 464245 Cd Length: 107 Bit Score: 135.79 E-value: 2.98e-37
|
||||||||||
| RICTOR_V | pfam14668 | Rapamycin-insensitive companion of mTOR, domain 5; Rictor appears to serve as a scaffolding ... |
1095-1165 | 1.19e-29 | ||||||
Rapamycin-insensitive companion of mTOR, domain 5; Rictor appears to serve as a scaffolding protein that is important for maintaining mTORC2 integrity. The mammalian target of rapamycin (mTOR) is a conserved Ser/Thr kinase that forms two functionally distinct complexes, mTROC1 and mTORC2, important for nutrient and growth-factor signalling. These long eukaryotic proteins carry several well-conserved domains, and this is No.5. Pssm-ID: 464249 Cd Length: 71 Bit Score: 112.55 E-value: 1.19e-29
|
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| HR1_Ste20-like | cd11627 | Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of ... |
34-108 | 6.08e-26 | ||||||
Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Schizosaccharomyces pombe Ste20-like proteins; This group is composed of predominantly uncharacterized fungal proteins, which contain two known domains: HR1 at the N-terminal region and REM (Ras exchanger motif) at the C-terminal region. One member protein from Schizosaccharomyces pombe is named Ste16 while its gene is called ste20 (a target of rapamycin complex 2 subunit). It is a subunit in the protein kinase TOR complexes in fission yeast. The REM domain is usually found in nucleotide exchange factors for Ras-like small GTPases. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family. Pssm-ID: 212017 [Multi-domain] Cd Length: 71 Bit Score: 102.07 E-value: 6.08e-26
|
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| HR1 | cd00089 | Protein kinase C-related kinase homology region 1 (HR1) domain that binds Rho family small ... |
34-108 | 1.20e-13 | ||||||
Protein kinase C-related kinase homology region 1 (HR1) domain that binds Rho family small GTPases; The HR1 domain, also called the ACC (anti-parallel coiled-coil) finger domain or Rho-binding domain binds small GTPases from the Rho family. It is found in Rho effector proteins including PKC-related kinases such as vertebrate PRK1 (or PKN) and yeast PKC1 protein kinases C, as well as in rhophilins and Rho-associated kinase (ROCK). Rho family members function as molecular switches, cycling between inactive and active forms, controlling a variety of cellular processes. HR1 domains may occur in repeat arrangements (PKN contains three HR1 domains), separated by a short linker region. Pssm-ID: 212008 [Multi-domain] Cd Length: 68 Bit Score: 66.97 E-value: 1.20e-13
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| Hr1 | smart00742 | Rho effector or protein kinase C-related kinase homology region 1 homologues; Alpha-helical ... |
38-102 | 1.11e-08 | ||||||
Rho effector or protein kinase C-related kinase homology region 1 homologues; Alpha-helical domain found in vertebrate PRK1 and yeast PKC1 protein kinases C. The HR1 in rhophilin bind RhoGTP; those in PRK1 bind RhoA and RhoB. Also called RBD - Rho-binding domain Pssm-ID: 128981 Cd Length: 57 Bit Score: 52.58 E-value: 1.11e-08
|
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| HR1 | pfam02185 | Hr1 repeat; The HR1 repeat was first described as a three times repeated homology region of ... |
40-105 | 3.32e-07 | ||||||
Hr1 repeat; The HR1 repeat was first described as a three times repeated homology region of the N-terminal non-catalytic part of protein kinase PRK1(PKN). The first two of these repeats were later shown to bind the small G protein rho known to activate PKN in its GTP-bound form. Similar rho-binding domains also occur in a number of other protein kinases and in the rho-binding proteins rhophilin and rhotekin. Recently, the structure of the N-terminal HR1 repeat complexed with RhoA has been determined by X-ray crystallography. It forms an antiparallel coiled-coil fold termed an ACC finger. Pssm-ID: 460478 [Multi-domain] Cd Length: 67 Bit Score: 48.67 E-value: 3.32e-07
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| Uds1 | pfam15456 | Up-regulated During Septation; Uds1 is a domain family is found mostly in fungi, and is ... |
34-102 | 4.01e-04 | ||||||
Up-regulated During Septation; Uds1 is a domain family is found mostly in fungi, and is typically between 120 and 138 amino acids in length. The GO annotation for the S.pombe protein describes the protein as barrier septum assembly involved in cell cycle cytokinesis, GO:0071937. Many of the uncharacterized members are listed as being involucrin repeat proteins, but this can not be substantiated. Pssm-ID: 434730 [Multi-domain] Cd Length: 119 Bit Score: 41.38 E-value: 4.01e-04
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| HR1_PKN_2 | cd11623 | Second Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein ... |
30-95 | 1.91e-03 | ||||||
Second Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Protein Kinase N; PKN, also called Protein-kinase C-related kinase (PRK), is a serine/threonine protein kinase that can be activated by the small GTPase Rho, and by fatty acids such as arachidonic and linoleic acids. It is involved in many biological processes including cytoskeletal regulation, cell adhesion, vesicle transport, glucose transport, regulation of meiotic maturation and embryonic cell cycles, signaling to the nucleus, and tumorigenesis. In some vertebrates, there are three PKN isoforms from different genes (designated PKN1, PKN2, and PKN3), which show different enzymatic properties, tissue distribution, and varied functions. PKN proteins contain three HR1 domains, a C2 domain, and a kinase domain. This model characterizes the second HR1 domain of PKN. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family. Pssm-ID: 212013 Cd Length: 71 Bit Score: 37.98 E-value: 1.91e-03
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