NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|550544215|ref|NP_001272369|]
View 

rapamycin-insensitive companion of mTOR isoform 3 [Homo sapiens]

Protein Classification

RICTOR_M and RICTOR_phospho domain-containing protein( domain architecture ID 10384678)

protein containing domains RICTOR_M, RasGEF_N_2, RICTOR_V, and RICTOR_phospho

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
RICTOR_N super family cl20619
Rapamycin-insensitive companion of mTOR, N-term; Rictor appears to serve as a scaffolding ...
3-152 6.48e-48

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.


The actual alignment was detected with superfamily member pfam14664:

Pssm-ID: 464246  Cd Length: 372  Bit Score: 175.80  E-value: 6.48e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544215     3 IIATFRSWAGIINLCKPGNSGIQSLIGVLCIPNMEIRRGLLEVLYDIFRLPLPVVTEEFIEALLSVdPGRFQDSWRLSDG 82
Cdd:pfam14664  220 ISSLLKSWPGLMYLSMNDFRPLRSLVDSLRLPSLEVREAILDLLFDLLRIKPPSWTSSFLALTTYG-RVANLDSWSLSEG 298
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 550544215    83 FVAAEAKTILPHRAR-SRPDLMDNYLALILSAFIRNGLLEGLVEVI-TNSDDHISVRATILLGELLHMANTI 152
Cdd:pfam14664  299 FVAAEFKSILPSESSfSRENLVNHYLALLLLVFIEAGLLEALVEVIeESSDSSLSRKATLLLGELLHLANRL 370
RICTOR_phospho pfam14665
Rapamycin-insensitive companion of mTOR, phosphorylation-site; Rictor appears to serve as a ...
800-903 4.45e-44

Rapamycin-insensitive companion of mTOR, phosphorylation-site; 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 short region is the phoshorylation site. Rictor does interact with 14-3-3 in a Thr1135-dependent manner. Rictor can be inhibited by short-term rapamycin treatment showing that Thr1135 is an mTORC1-regulated site.


:

Pssm-ID: 464247  Cd Length: 108  Bit Score: 155.41  E-value: 4.45e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544215   800 FPFFASSKLVKNRILNSLTLPNKKHRSSSDPKGGKLSSESKTSNRRIRTLTEPSVDFNHSDDFTPISTVQKTLQ---LET 876
Cdd:pfam14665    2 FTFLSSSRVVRNRFLNSLTLPKKKLRSSSDPKGGKSSSNKKSGLRRNRTVTEPSSDDNHSGDFFPPVFRVPKSPtqsLET 81
                           90       100
                   ....*....|....*....|....*..
gi 550544215   877 SFMGNKHIEDTGSTPSIGENDLKFTKN 903
Cdd:pfam14665   82 SFVGSKIEEDGGSTPSIGENDLKLPRL 108
RICTOR_M pfam14666
Rapamycin-insensitive companion of mTOR, middle domain; Rictor appears to serve as a ...
352-455 1.20e-40

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: 145.30  E-value: 1.20e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544215   352 SSGMKPERSLQNNGLLTTLSQHYFLFIGTLSCHPHGVKMLEKCSVFQCLLNLCSLKNQDHLLKLTVSSLDYSRDGLARVI 431
Cdd:pfam14666    1 SGITAGDPLFSKQRLETTLSRGYFLFIGVLSSSKNGLKLLEKWNIFTILYHIVELKSRDDLLKLILSSLDYSLDGHPRII 80
                           90       100
                   ....*....|....*....|....
gi 550544215   432 LSKILTAATDACRLYATKHLRVLL 455
Cdd:pfam14666   81 LSKALTSSSESIRLYATKHLRVLL 104
RasGEF_N_2 pfam14663
Rapamycin-insensitive companion of mTOR RasGEF_N domain; Rictor appears to serve as a ...
462-568 3.56e-38

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: 138.49  E-value: 3.56e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544215   462 FNNWGIELLVTQLHDKNKTISSEALDILDEACEDKANLHALIQMKPALSHLGDKGLLLLLRFLSIPKGFSYLNERGYVAK 541
Cdd:pfam14663    1 FEEWGIELLVTQLYDPSPEVVAAAVDVLYEACDDKENLESLVSLRPSLDHLGEIGSPLLLRFLSTPSGFKYLNELGFVEN 80
                           90       100
                   ....*....|....*....|....*..
gi 550544215   542 QLEKWHREYNSKYVDLIEEQLNEALTT 568
Cdd:pfam14663   81 ELDKWFEERNLEYVLKVEEFLAEALTD 107
RICTOR_V pfam14668
Rapamycin-insensitive companion of mTOR, domain 5; Rictor appears to serve as a scaffolding ...
637-706 3.76e-34

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: 125.65  E-value: 3.76e-34
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544215   637 KLKASLWALGNIGSSNWGLNLLQEENVIPDILKLAKQCEVLSIRGTCVYVLGLIAKTKQGCDILKCHNWD 706
Cdd:pfam14668    2 KLKAALWAIGHIGSSPLGIQLLEEYDIVEDIVKIAEESPVLSLRGTAFYVLGLISSTEEGAEILDELGWE 71
 
Name Accession Description Interval E-value
RICTOR_N pfam14664
Rapamycin-insensitive companion of mTOR, N-term; Rictor appears to serve as a scaffolding ...
3-152 6.48e-48

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: 175.80  E-value: 6.48e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544215     3 IIATFRSWAGIINLCKPGNSGIQSLIGVLCIPNMEIRRGLLEVLYDIFRLPLPVVTEEFIEALLSVdPGRFQDSWRLSDG 82
Cdd:pfam14664  220 ISSLLKSWPGLMYLSMNDFRPLRSLVDSLRLPSLEVREAILDLLFDLLRIKPPSWTSSFLALTTYG-RVANLDSWSLSEG 298
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 550544215    83 FVAAEAKTILPHRAR-SRPDLMDNYLALILSAFIRNGLLEGLVEVI-TNSDDHISVRATILLGELLHMANTI 152
Cdd:pfam14664  299 FVAAEFKSILPSESSfSRENLVNHYLALLLLVFIEAGLLEALVEVIeESSDSSLSRKATLLLGELLHLANRL 370
RICTOR_phospho pfam14665
Rapamycin-insensitive companion of mTOR, phosphorylation-site; Rictor appears to serve as a ...
800-903 4.45e-44

Rapamycin-insensitive companion of mTOR, phosphorylation-site; 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 short region is the phoshorylation site. Rictor does interact with 14-3-3 in a Thr1135-dependent manner. Rictor can be inhibited by short-term rapamycin treatment showing that Thr1135 is an mTORC1-regulated site.


Pssm-ID: 464247  Cd Length: 108  Bit Score: 155.41  E-value: 4.45e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544215   800 FPFFASSKLVKNRILNSLTLPNKKHRSSSDPKGGKLSSESKTSNRRIRTLTEPSVDFNHSDDFTPISTVQKTLQ---LET 876
Cdd:pfam14665    2 FTFLSSSRVVRNRFLNSLTLPKKKLRSSSDPKGGKSSSNKKSGLRRNRTVTEPSSDDNHSGDFFPPVFRVPKSPtqsLET 81
                           90       100
                   ....*....|....*....|....*..
gi 550544215   877 SFMGNKHIEDTGSTPSIGENDLKFTKN 903
Cdd:pfam14665   82 SFVGSKIEEDGGSTPSIGENDLKLPRL 108
RICTOR_M pfam14666
Rapamycin-insensitive companion of mTOR, middle domain; Rictor appears to serve as a ...
352-455 1.20e-40

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: 145.30  E-value: 1.20e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544215   352 SSGMKPERSLQNNGLLTTLSQHYFLFIGTLSCHPHGVKMLEKCSVFQCLLNLCSLKNQDHLLKLTVSSLDYSRDGLARVI 431
Cdd:pfam14666    1 SGITAGDPLFSKQRLETTLSRGYFLFIGVLSSSKNGLKLLEKWNIFTILYHIVELKSRDDLLKLILSSLDYSLDGHPRII 80
                           90       100
                   ....*....|....*....|....
gi 550544215   432 LSKILTAATDACRLYATKHLRVLL 455
Cdd:pfam14666   81 LSKALTSSSESIRLYATKHLRVLL 104
RasGEF_N_2 pfam14663
Rapamycin-insensitive companion of mTOR RasGEF_N domain; Rictor appears to serve as a ...
462-568 3.56e-38

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: 138.49  E-value: 3.56e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544215   462 FNNWGIELLVTQLHDKNKTISSEALDILDEACEDKANLHALIQMKPALSHLGDKGLLLLLRFLSIPKGFSYLNERGYVAK 541
Cdd:pfam14663    1 FEEWGIELLVTQLYDPSPEVVAAAVDVLYEACDDKENLESLVSLRPSLDHLGEIGSPLLLRFLSTPSGFKYLNELGFVEN 80
                           90       100
                   ....*....|....*....|....*..
gi 550544215   542 QLEKWHREYNSKYVDLIEEQLNEALTT 568
Cdd:pfam14663   81 ELDKWFEERNLEYVLKVEEFLAEALTD 107
RICTOR_V pfam14668
Rapamycin-insensitive companion of mTOR, domain 5; Rictor appears to serve as a scaffolding ...
637-706 3.76e-34

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: 125.65  E-value: 3.76e-34
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544215   637 KLKASLWALGNIGSSNWGLNLLQEENVIPDILKLAKQCEVLSIRGTCVYVLGLIAKTKQGCDILKCHNWD 706
Cdd:pfam14668    2 KLKAALWAIGHIGSSPLGIQLLEEYDIVEDIVKIAEESPVLSLRGTAFYVLGLISSTEEGAEILDELGWE 71
 
Name Accession Description Interval E-value
RICTOR_N pfam14664
Rapamycin-insensitive companion of mTOR, N-term; Rictor appears to serve as a scaffolding ...
3-152 6.48e-48

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: 175.80  E-value: 6.48e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544215     3 IIATFRSWAGIINLCKPGNSGIQSLIGVLCIPNMEIRRGLLEVLYDIFRLPLPVVTEEFIEALLSVdPGRFQDSWRLSDG 82
Cdd:pfam14664  220 ISSLLKSWPGLMYLSMNDFRPLRSLVDSLRLPSLEVREAILDLLFDLLRIKPPSWTSSFLALTTYG-RVANLDSWSLSEG 298
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 550544215    83 FVAAEAKTILPHRAR-SRPDLMDNYLALILSAFIRNGLLEGLVEVI-TNSDDHISVRATILLGELLHMANTI 152
Cdd:pfam14664  299 FVAAEFKSILPSESSfSRENLVNHYLALLLLVFIEAGLLEALVEVIeESSDSSLSRKATLLLGELLHLANRL 370
RICTOR_phospho pfam14665
Rapamycin-insensitive companion of mTOR, phosphorylation-site; Rictor appears to serve as a ...
800-903 4.45e-44

Rapamycin-insensitive companion of mTOR, phosphorylation-site; 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 short region is the phoshorylation site. Rictor does interact with 14-3-3 in a Thr1135-dependent manner. Rictor can be inhibited by short-term rapamycin treatment showing that Thr1135 is an mTORC1-regulated site.


Pssm-ID: 464247  Cd Length: 108  Bit Score: 155.41  E-value: 4.45e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544215   800 FPFFASSKLVKNRILNSLTLPNKKHRSSSDPKGGKLSSESKTSNRRIRTLTEPSVDFNHSDDFTPISTVQKTLQ---LET 876
Cdd:pfam14665    2 FTFLSSSRVVRNRFLNSLTLPKKKLRSSSDPKGGKSSSNKKSGLRRNRTVTEPSSDDNHSGDFFPPVFRVPKSPtqsLET 81
                           90       100
                   ....*....|....*....|....*..
gi 550544215   877 SFMGNKHIEDTGSTPSIGENDLKFTKN 903
Cdd:pfam14665   82 SFVGSKIEEDGGSTPSIGENDLKLPRL 108
RICTOR_M pfam14666
Rapamycin-insensitive companion of mTOR, middle domain; Rictor appears to serve as a ...
352-455 1.20e-40

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: 145.30  E-value: 1.20e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544215   352 SSGMKPERSLQNNGLLTTLSQHYFLFIGTLSCHPHGVKMLEKCSVFQCLLNLCSLKNQDHLLKLTVSSLDYSRDGLARVI 431
Cdd:pfam14666    1 SGITAGDPLFSKQRLETTLSRGYFLFIGVLSSSKNGLKLLEKWNIFTILYHIVELKSRDDLLKLILSSLDYSLDGHPRII 80
                           90       100
                   ....*....|....*....|....
gi 550544215   432 LSKILTAATDACRLYATKHLRVLL 455
Cdd:pfam14666   81 LSKALTSSSESIRLYATKHLRVLL 104
RasGEF_N_2 pfam14663
Rapamycin-insensitive companion of mTOR RasGEF_N domain; Rictor appears to serve as a ...
462-568 3.56e-38

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: 138.49  E-value: 3.56e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544215   462 FNNWGIELLVTQLHDKNKTISSEALDILDEACEDKANLHALIQMKPALSHLGDKGLLLLLRFLSIPKGFSYLNERGYVAK 541
Cdd:pfam14663    1 FEEWGIELLVTQLYDPSPEVVAAAVDVLYEACDDKENLESLVSLRPSLDHLGEIGSPLLLRFLSTPSGFKYLNELGFVEN 80
                           90       100
                   ....*....|....*....|....*..
gi 550544215   542 QLEKWHREYNSKYVDLIEEQLNEALTT 568
Cdd:pfam14663   81 ELDKWFEERNLEYVLKVEEFLAEALTD 107
RICTOR_V pfam14668
Rapamycin-insensitive companion of mTOR, domain 5; Rictor appears to serve as a scaffolding ...
637-706 3.76e-34

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: 125.65  E-value: 3.76e-34
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544215   637 KLKASLWALGNIGSSNWGLNLLQEENVIPDILKLAKQCEVLSIRGTCVYVLGLIAKTKQGCDILKCHNWD 706
Cdd:pfam14668    2 KLKAALWAIGHIGSSPLGIQLLEEYDIVEDIVKIAEESPVLSLRGTAFYVLGLISSTEEGAEILDELGWE 71
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH