cytosolic arginine sensor for mTORC1 subunit 2 [Mus musculus]
List of domain hits
Name | Accession | Description | Interval | E-value | ||
Castor1_N | pfam18700 | Cytosolic arginine sensor for mTORC1 subunit 1 N-terminal domain; CASTOR1 (Cytosolic arginine ... |
9-69 | 5.43e-33 | ||
Cytosolic arginine sensor for mTORC1 subunit 1 N-terminal domain; CASTOR1 (Cytosolic arginine sensor for mTORC1 subunit 1) has been identified as the cytosolic arginine sensor for the mTORC1 pathway. In the absence of arginine, CASTOR1 binds to GATOR2 and inhibits mTORC1 signaling; whereas in the presence of arginine, CASTOR1 interacts with arginine and no longer associates with GATOR2. The arginine sits in a pocket between the N-terminal domain (NTD) and the C-terminal domain (CTD) of CASTOR1. The CASTOR1-NTD on the opposite side of the arginine-binding site was identified to mediate direct physical interaction with its downstream effector GATOR2, via GATOR2 subunit Mios. : Pssm-ID: 465837 Cd Length: 61 Bit Score: 116.32 E-value: 5.43e-33
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ACT_7 | pfam13840 | ACT domain; The ACT domain is a structural motif of 70-90 amino acids that functions in the ... |
260-321 | 4.71e-18 | ||
ACT domain; The ACT domain is a structural motif of 70-90 amino acids that functions in the control of metabolism, solute transport and signal transduction. They are thus found in a variety of different proteins in a variety of different arrangements. In mammalian phenylalanine hydroxylase the domain forms no contacts but promotes an allosteric effect despite the apparent lack of ligand binding. : Pssm-ID: 433519 [Multi-domain] Cd Length: 65 Bit Score: 76.80 E-value: 4.71e-18
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ACT_7 | pfam13840 | ACT domain; The ACT domain is a structural motif of 70-90 amino acids that functions in the ... |
71-141 | 6.70e-13 | ||
ACT domain; The ACT domain is a structural motif of 70-90 amino acids that functions in the control of metabolism, solute transport and signal transduction. They are thus found in a variety of different proteins in a variety of different arrangements. In mammalian phenylalanine hydroxylase the domain forms no contacts but promotes an allosteric effect despite the apparent lack of ligand binding. : Pssm-ID: 433519 [Multi-domain] Cd Length: 65 Bit Score: 62.93 E-value: 6.70e-13
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Name | Accession | Description | Interval | E-value | |||
Castor1_N | pfam18700 | Cytosolic arginine sensor for mTORC1 subunit 1 N-terminal domain; CASTOR1 (Cytosolic arginine ... |
9-69 | 5.43e-33 | |||
Cytosolic arginine sensor for mTORC1 subunit 1 N-terminal domain; CASTOR1 (Cytosolic arginine sensor for mTORC1 subunit 1) has been identified as the cytosolic arginine sensor for the mTORC1 pathway. In the absence of arginine, CASTOR1 binds to GATOR2 and inhibits mTORC1 signaling; whereas in the presence of arginine, CASTOR1 interacts with arginine and no longer associates with GATOR2. The arginine sits in a pocket between the N-terminal domain (NTD) and the C-terminal domain (CTD) of CASTOR1. The CASTOR1-NTD on the opposite side of the arginine-binding site was identified to mediate direct physical interaction with its downstream effector GATOR2, via GATOR2 subunit Mios. Pssm-ID: 465837 Cd Length: 61 Bit Score: 116.32 E-value: 5.43e-33
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ACT_7 | pfam13840 | ACT domain; The ACT domain is a structural motif of 70-90 amino acids that functions in the ... |
260-321 | 4.71e-18 | |||
ACT domain; The ACT domain is a structural motif of 70-90 amino acids that functions in the control of metabolism, solute transport and signal transduction. They are thus found in a variety of different proteins in a variety of different arrangements. In mammalian phenylalanine hydroxylase the domain forms no contacts but promotes an allosteric effect despite the apparent lack of ligand binding. Pssm-ID: 433519 [Multi-domain] Cd Length: 65 Bit Score: 76.80 E-value: 4.71e-18
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ACT_7 | pfam13840 | ACT domain; The ACT domain is a structural motif of 70-90 amino acids that functions in the ... |
71-141 | 6.70e-13 | |||
ACT domain; The ACT domain is a structural motif of 70-90 amino acids that functions in the control of metabolism, solute transport and signal transduction. They are thus found in a variety of different proteins in a variety of different arrangements. In mammalian phenylalanine hydroxylase the domain forms no contacts but promotes an allosteric effect despite the apparent lack of ligand binding. Pssm-ID: 433519 [Multi-domain] Cd Length: 65 Bit Score: 62.93 E-value: 6.70e-13
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ACT-7 | COG3603 | ACT domain, ACT-7 family [Signal transduction mechanisms]; |
1-132 | 2.29e-11 | |||
ACT domain, ACT-7 family [Signal transduction mechanisms]; Pssm-ID: 442822 [Multi-domain] Cd Length: 120 Bit Score: 60.22 E-value: 2.29e-11
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ACT-7 | COG3603 | ACT domain, ACT-7 family [Signal transduction mechanisms]; |
264-322 | 2.84e-11 | |||
ACT domain, ACT-7 family [Signal transduction mechanisms]; Pssm-ID: 442822 [Multi-domain] Cd Length: 120 Bit Score: 59.83 E-value: 2.84e-11
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Name | Accession | Description | Interval | E-value | |||
Castor1_N | pfam18700 | Cytosolic arginine sensor for mTORC1 subunit 1 N-terminal domain; CASTOR1 (Cytosolic arginine ... |
9-69 | 5.43e-33 | |||
Cytosolic arginine sensor for mTORC1 subunit 1 N-terminal domain; CASTOR1 (Cytosolic arginine sensor for mTORC1 subunit 1) has been identified as the cytosolic arginine sensor for the mTORC1 pathway. In the absence of arginine, CASTOR1 binds to GATOR2 and inhibits mTORC1 signaling; whereas in the presence of arginine, CASTOR1 interacts with arginine and no longer associates with GATOR2. The arginine sits in a pocket between the N-terminal domain (NTD) and the C-terminal domain (CTD) of CASTOR1. The CASTOR1-NTD on the opposite side of the arginine-binding site was identified to mediate direct physical interaction with its downstream effector GATOR2, via GATOR2 subunit Mios. Pssm-ID: 465837 Cd Length: 61 Bit Score: 116.32 E-value: 5.43e-33
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ACT_7 | pfam13840 | ACT domain; The ACT domain is a structural motif of 70-90 amino acids that functions in the ... |
260-321 | 4.71e-18 | |||
ACT domain; The ACT domain is a structural motif of 70-90 amino acids that functions in the control of metabolism, solute transport and signal transduction. They are thus found in a variety of different proteins in a variety of different arrangements. In mammalian phenylalanine hydroxylase the domain forms no contacts but promotes an allosteric effect despite the apparent lack of ligand binding. Pssm-ID: 433519 [Multi-domain] Cd Length: 65 Bit Score: 76.80 E-value: 4.71e-18
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ACT_7 | pfam13840 | ACT domain; The ACT domain is a structural motif of 70-90 amino acids that functions in the ... |
71-141 | 6.70e-13 | |||
ACT domain; The ACT domain is a structural motif of 70-90 amino acids that functions in the control of metabolism, solute transport and signal transduction. They are thus found in a variety of different proteins in a variety of different arrangements. In mammalian phenylalanine hydroxylase the domain forms no contacts but promotes an allosteric effect despite the apparent lack of ligand binding. Pssm-ID: 433519 [Multi-domain] Cd Length: 65 Bit Score: 62.93 E-value: 6.70e-13
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ACT-7 | COG3603 | ACT domain, ACT-7 family [Signal transduction mechanisms]; |
1-132 | 2.29e-11 | |||
ACT domain, ACT-7 family [Signal transduction mechanisms]; Pssm-ID: 442822 [Multi-domain] Cd Length: 120 Bit Score: 60.22 E-value: 2.29e-11
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ACT-7 | COG3603 | ACT domain, ACT-7 family [Signal transduction mechanisms]; |
264-322 | 2.84e-11 | |||
ACT domain, ACT-7 family [Signal transduction mechanisms]; Pssm-ID: 442822 [Multi-domain] Cd Length: 120 Bit Score: 59.83 E-value: 2.84e-11
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Blast search parameters | ||||
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