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Conserved domains on  [gi|58037269|ref|NP_082298|]
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cytosolic arginine sensor for mTORC1 subunit 1 [Mus musculus]

Protein Classification

Graphical summary

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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 1.23e-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: 118.25  E-value: 1.23e-33
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 58037269     9 RVRVLSIARPGLWLYTHPLIKLLFLPCRSRCKFFSLTETPEDYTLMVDEEGFKELPPSEFL 69
Cdd:pfam18700   1 RLRVASIAKEGIQPFTHGLIKLAFLRSKTRCKFFSLTETPEDYTIIVDEEGFKELPQSEHL 61
ACT_7 pfam13840
ACT domain; The ACT domain is a structural motif of 70-90 amino acids that functions in the ...
257-321 2.48e-17

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: 74.87  E-value: 2.48e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 58037269   257 SSGELWRMVRIGGQPLGFDECGIVAQIAGPLAAVDISAYYISTFNFDHALVPEDEIGCVIDILQR 321
Cdd:pfam13840   1 ESEDGWAKLSVVGAGLDFDVPGVVAKLTSPLAEAGISIFQISSYTTDYVLVPEEDLEKAVRALHE 65
ACT_7 pfam13840
ACT domain; The ACT domain is a structural motif of 70-90 amino acids that functions in the ...
71-136 4.16e-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: 63.32  E-value: 4.16e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 58037269    71 VAEATWLVMNVSHSGSVVQAAGVTKiarSVIAPLAEHHVSVLMLSTYQTDFILVREQDLSVVIHTL 136
Cdd:pfam13840   1 ESEDGWAKLSVVGAGLDFDVPGVVA---KLTSPLAEAGISIFQISSYTTDYVLVPEEDLEKAVRAL 63
 
Name Accession Description Interval E-value
Castor1_N pfam18700
Cytosolic arginine sensor for mTORC1 subunit 1 N-terminal domain; CASTOR1 (Cytosolic arginine ...
9-69 1.23e-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: 118.25  E-value: 1.23e-33
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 58037269     9 RVRVLSIARPGLWLYTHPLIKLLFLPCRSRCKFFSLTETPEDYTLMVDEEGFKELPPSEFL 69
Cdd:pfam18700   1 RLRVASIAKEGIQPFTHGLIKLAFLRSKTRCKFFSLTETPEDYTIIVDEEGFKELPQSEHL 61
ACT_7 pfam13840
ACT domain; The ACT domain is a structural motif of 70-90 amino acids that functions in the ...
257-321 2.48e-17

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: 74.87  E-value: 2.48e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 58037269   257 SSGELWRMVRIGGQPLGFDECGIVAQIAGPLAAVDISAYYISTFNFDHALVPEDEIGCVIDILQR 321
Cdd:pfam13840   1 ESEDGWAKLSVVGAGLDFDVPGVVAKLTSPLAEAGISIFQISSYTTDYVLVPEEDLEKAVRALHE 65
ACT_7 pfam13840
ACT domain; The ACT domain is a structural motif of 70-90 amino acids that functions in the ...
71-136 4.16e-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: 63.32  E-value: 4.16e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 58037269    71 VAEATWLVMNVSHSGSVVQAAGVTKiarSVIAPLAEHHVSVLMLSTYQTDFILVREQDLSVVIHTL 136
Cdd:pfam13840   1 ESEDGWAKLSVVGAGLDFDVPGVVA---KLTSPLAEAGISIFQISSYTTDYVLVPEEDLEKAVRAL 63
ACT-7 COG3603
ACT domain, ACT-7 family [Signal transduction mechanisms];
262-321 1.53e-11

ACT domain, ACT-7 family [Signal transduction mechanisms];


Pssm-ID: 442822 [Multi-domain]  Cd Length: 120  Bit Score: 60.60  E-value: 1.53e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037269 262 WRMVRIGGqPLGFDECGIVAQIAGPLAAVDISAYYISTFNFDHALVPEDEIGCVIDILQR 321
Cdd:COG3603  60 WRALKVEG-PLDFSLTGILASLSSPLAEAGISIFAVSTFDTDYLLVKEADLDRAVAALRA 118
ACT-7 COG3603
ACT domain, ACT-7 family [Signal transduction mechanisms];
41-136 1.41e-07

ACT domain, ACT-7 family [Signal transduction mechanisms];


Pssm-ID: 442822 [Multi-domain]  Cd Length: 120  Bit Score: 49.43  E-value: 1.41e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037269  41 FFSLTETPEDYTLMVDEEgfkeLPPSEflQVAEATWLVMNVshsgsvvqaAGV-----TKIARSVIAPLAEHHVSVLMLS 115
Cdd:COG3603  31 FVSITRTPDELSIVCPEE----RVPAG--VRAERGWRALKV---------EGPldfslTGILASLSSPLAEAGISIFAVS 95
                        90       100
                ....*....|....*....|.
gi 58037269 116 TYQTDFILVREQDLSVVIHTL 136
Cdd:COG3603  96 TFDTDYLLVKEADLDRAVAAL 116
 
Name Accession Description Interval E-value
Castor1_N pfam18700
Cytosolic arginine sensor for mTORC1 subunit 1 N-terminal domain; CASTOR1 (Cytosolic arginine ...
9-69 1.23e-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: 118.25  E-value: 1.23e-33
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 58037269     9 RVRVLSIARPGLWLYTHPLIKLLFLPCRSRCKFFSLTETPEDYTLMVDEEGFKELPPSEFL 69
Cdd:pfam18700   1 RLRVASIAKEGIQPFTHGLIKLAFLRSKTRCKFFSLTETPEDYTIIVDEEGFKELPQSEHL 61
ACT_7 pfam13840
ACT domain; The ACT domain is a structural motif of 70-90 amino acids that functions in the ...
257-321 2.48e-17

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: 74.87  E-value: 2.48e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 58037269   257 SSGELWRMVRIGGQPLGFDECGIVAQIAGPLAAVDISAYYISTFNFDHALVPEDEIGCVIDILQR 321
Cdd:pfam13840   1 ESEDGWAKLSVVGAGLDFDVPGVVAKLTSPLAEAGISIFQISSYTTDYVLVPEEDLEKAVRALHE 65
ACT_7 pfam13840
ACT domain; The ACT domain is a structural motif of 70-90 amino acids that functions in the ...
71-136 4.16e-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: 63.32  E-value: 4.16e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 58037269    71 VAEATWLVMNVSHSGSVVQAAGVTKiarSVIAPLAEHHVSVLMLSTYQTDFILVREQDLSVVIHTL 136
Cdd:pfam13840   1 ESEDGWAKLSVVGAGLDFDVPGVVA---KLTSPLAEAGISIFQISSYTTDYVLVPEEDLEKAVRAL 63
ACT-7 COG3603
ACT domain, ACT-7 family [Signal transduction mechanisms];
262-321 1.53e-11

ACT domain, ACT-7 family [Signal transduction mechanisms];


Pssm-ID: 442822 [Multi-domain]  Cd Length: 120  Bit Score: 60.60  E-value: 1.53e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037269 262 WRMVRIGGqPLGFDECGIVAQIAGPLAAVDISAYYISTFNFDHALVPEDEIGCVIDILQR 321
Cdd:COG3603  60 WRALKVEG-PLDFSLTGILASLSSPLAEAGISIFAVSTFDTDYLLVKEADLDRAVAALRA 118
ACT-7 COG3603
ACT domain, ACT-7 family [Signal transduction mechanisms];
41-136 1.41e-07

ACT domain, ACT-7 family [Signal transduction mechanisms];


Pssm-ID: 442822 [Multi-domain]  Cd Length: 120  Bit Score: 49.43  E-value: 1.41e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037269  41 FFSLTETPEDYTLMVDEEgfkeLPPSEflQVAEATWLVMNVshsgsvvqaAGV-----TKIARSVIAPLAEHHVSVLMLS 115
Cdd:COG3603  31 FVSITRTPDELSIVCPEE----RVPAG--VRAERGWRALKV---------EGPldfslTGILASLSSPLAEAGISIFAVS 95
                        90       100
                ....*....|....*....|.
gi 58037269 116 TYQTDFILVREQDLSVVIHTL 136
Cdd:COG3603  96 TFDTDYLLVKEADLDRAVAAL 116
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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