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Conserved domains on  [gi|83415181|ref|NP_001032755|]
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cytosolic arginine sensor for mTORC1 subunit 1 [Homo sapiens]

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 4.44e-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: 116.71  E-value: 4.44e-33
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 83415181     9 RVRVLSVARPGLWLYTHPLIKLLFLPRRSRCKFFSLTETPEDYTLMVDEEGFKELPPSEFL 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 ...
 258-322 1.96e-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: 77.96  E-value: 1.96e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 83415181   258 SSGELWRMVRIGGQPLGFDECGIVAQIAGPLAAADISAYYISTFNFDHALVPEDGIGSVIEVLQR 322
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 ...
 71-137 3.91e-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: 3.91e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 83415181    71 VAEATWLVLNVSSHSgaavQAAGVTKIARSVIAPLAEHHVSVLMLSTYQTDFILVREQDLSVVIHTL 137
Cdd:pfam13840   1 ESEDGWAKLSVVGAG----LDFDVPGVVAKLTSPLAEAGISIFQISSYTTDYVLVPEEDLEKAVRAL 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 4.44e-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: 116.71  E-value: 4.44e-33
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 83415181     9 RVRVLSVARPGLWLYTHPLIKLLFLPRRSRCKFFSLTETPEDYTLMVDEEGFKELPPSEFL 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 ...
 258-322 1.96e-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: 77.96  E-value: 1.96e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 83415181   258 SSGELWRMVRIGGQPLGFDECGIVAQIAGPLAAADISAYYISTFNFDHALVPEDGIGSVIEVLQR 322
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 ...
 71-137 3.91e-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: 3.91e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 83415181    71 VAEATWLVLNVSSHSgaavQAAGVTKIARSVIAPLAEHHVSVLMLSTYQTDFILVREQDLSVVIHTL 137
Cdd:pfam13840   1 ESEDGWAKLSVVGAG----LDFDVPGVVAKLTSPLAEAGISIFQISSYTTDYVLVPEEDLEKAVRAL 63
ACT-7 COG3603
ACT domain, ACT-7 family [Signal transduction mechanisms];
263-322 1.75e-12

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


Pssm-ID: 442822 [Multi-domain]  Cd Length: 120  Bit Score: 63.30  E-value: 1.75e-12
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 83415181 263 WRMVRIGGqPLGFDECGIVAQIAGPLAAADISAYYISTFNFDHALVPEDGIGSVIEVLQR 322
Cdd:COG3603  60 WRALKVEG-PLDFSLTGILASLSSPLAEAGISIFAVSTFDTDYLLVKEADLDRAVAALRA 118
ACT-7 COG3603
ACT domain, ACT-7 family [Signal transduction mechanisms];
41-137 1.61e-08

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


Pssm-ID: 442822 [Multi-domain]  Cd Length: 120  Bit Score: 52.13  E-value: 1.61e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83415181  41 FFSLTETPEDYTLMVDEEgfkeLPPSEflQVAEATWLVLNVSSHSgaavqAAGVTKIARSVIAPLAEHHVSVLMLSTYQT 120
Cdd:COG3603  31 FVSITRTPDELSIVCPEE----RVPAG--VRAERGWRALKVEGPL-----DFSLTGILASLSSPLAEAGISIFAVSTFDT 99

                        90
                ....*....|....*..
gi 83415181 121 DFILVREQDLSVVIHTL 137
Cdd:COG3603 100 DYLLVKEADLDRAVAAL 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 4.44e-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: 116.71  E-value: 4.44e-33
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 83415181     9 RVRVLSVARPGLWLYTHPLIKLLFLPRRSRCKFFSLTETPEDYTLMVDEEGFKELPPSEFL 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 ...
 258-322 1.96e-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: 77.96  E-value: 1.96e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 83415181   258 SSGELWRMVRIGGQPLGFDECGIVAQIAGPLAAADISAYYISTFNFDHALVPEDGIGSVIEVLQR 322
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 ...
 71-137 3.91e-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: 3.91e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 83415181    71 VAEATWLVLNVSSHSgaavQAAGVTKIARSVIAPLAEHHVSVLMLSTYQTDFILVREQDLSVVIHTL 137
Cdd:pfam13840   1 ESEDGWAKLSVVGAG----LDFDVPGVVAKLTSPLAEAGISIFQISSYTTDYVLVPEEDLEKAVRAL 63
ACT-7 COG3603
ACT domain, ACT-7 family [Signal transduction mechanisms];
263-322 1.75e-12

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


Pssm-ID: 442822 [Multi-domain]  Cd Length: 120  Bit Score: 63.30  E-value: 1.75e-12
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 83415181 263 WRMVRIGGqPLGFDECGIVAQIAGPLAAADISAYYISTFNFDHALVPEDGIGSVIEVLQR 322
Cdd:COG3603  60 WRALKVEG-PLDFSLTGILASLSSPLAEAGISIFAVSTFDTDYLLVKEADLDRAVAALRA 118
ACT-7 COG3603
ACT domain, ACT-7 family [Signal transduction mechanisms];
41-137 1.61e-08

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


Pssm-ID: 442822 [Multi-domain]  Cd Length: 120  Bit Score: 52.13  E-value: 1.61e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83415181  41 FFSLTETPEDYTLMVDEEgfkeLPPSEflQVAEATWLVLNVSSHSgaavqAAGVTKIARSVIAPLAEHHVSVLMLSTYQT 120
Cdd:COG3603  31 FVSITRTPDELSIVCPEE----RVPAG--VRAERGWRALKVEGPL-----DFSLTGILASLSSPLAEAGISIFAVSTFDT 99

                        90
                ....*....|....*..
gi 83415181 121 DFILVREQDLSVVIHTL 137
Cdd:COG3603 100 DYLLVKEADLDRAVAAL 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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