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Conserved domains on  [gi|8923579|ref|NP_060377|]
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ragulator complex protein LAMTOR1 [Homo sapiens]

Protein Classification

LAMTOR1/MEH1 family protein( domain architecture ID 10634440)

LAMTOR1/MEH1 family protein similar to Homo sapiens ragulator complex protein LAMTOR1 and Saccharomyces cerevisiae protein MEH1

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LAMTOR pfam15454
Late endosomal/lysosomal adaptor and MAPK and MTOR activator; LAMTOR is a family of eukaryotic ...
 21-85 1.17e-18

Late endosomal/lysosomal adaptor and MAPK and MTOR activator; LAMTOR is a family of eukaryotic proteins that have otherwise been referred to as Lipid raft adaptor protein p18, Late endosomal/lysosomal adaptor and MAPK and MTOR activator 1, and Protein associated with DRMs and endosomes. It is found to be one of three small proteins constituting the Rag complex or Ragulator that interact with each other, localize to endosomes and lysosomes, and play positive roles in the MAPK pathway. The complex does this by interacting with the Rag GTPases, recruiting them to lysosomes, and bringing about mTORC1 activation.


:

Pssm-ID: 464726  Cd Length: 69  Bit Score: 75.00  E-value: 1.17e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 8923579     21 LLLDPSSPP---TKALNGAEPNYHSLPSARTDEQALLSSILAKTASNIIDVSAADSQG-MEQHEYMDRA 85
Cdd:pfam15454   1 LLADPQNNSgnkRGYDNGLQQNYQESPPKLTDEQEALNRIVQNTSDNLIDISAMSSSGiVEQHEYMDRA 69
 
Name Accession Description Interval E-value
LAMTOR pfam15454
Late endosomal/lysosomal adaptor and MAPK and MTOR activator; LAMTOR is a family of eukaryotic ...
 21-85 1.17e-18

Late endosomal/lysosomal adaptor and MAPK and MTOR activator; LAMTOR is a family of eukaryotic proteins that have otherwise been referred to as Lipid raft adaptor protein p18, Late endosomal/lysosomal adaptor and MAPK and MTOR activator 1, and Protein associated with DRMs and endosomes. It is found to be one of three small proteins constituting the Rag complex or Ragulator that interact with each other, localize to endosomes and lysosomes, and play positive roles in the MAPK pathway. The complex does this by interacting with the Rag GTPases, recruiting them to lysosomes, and bringing about mTORC1 activation.


Pssm-ID: 464726  Cd Length: 69  Bit Score: 75.00  E-value: 1.17e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 8923579     21 LLLDPSSPP---TKALNGAEPNYHSLPSARTDEQALLSSILAKTASNIIDVSAADSQG-MEQHEYMDRA 85
Cdd:pfam15454   1 LLADPQNNSgnkRGYDNGLQQNYQESPPKLTDEQEALNRIVQNTSDNLIDISAMSSSGiVEQHEYMDRA 69
 
Name Accession Description Interval E-value
LAMTOR pfam15454
Late endosomal/lysosomal adaptor and MAPK and MTOR activator; LAMTOR is a family of eukaryotic ...
 21-85 1.17e-18

Late endosomal/lysosomal adaptor and MAPK and MTOR activator; LAMTOR is a family of eukaryotic proteins that have otherwise been referred to as Lipid raft adaptor protein p18, Late endosomal/lysosomal adaptor and MAPK and MTOR activator 1, and Protein associated with DRMs and endosomes. It is found to be one of three small proteins constituting the Rag complex or Ragulator that interact with each other, localize to endosomes and lysosomes, and play positive roles in the MAPK pathway. The complex does this by interacting with the Rag GTPases, recruiting them to lysosomes, and bringing about mTORC1 activation.


Pssm-ID: 464726  Cd Length: 69  Bit Score: 75.00  E-value: 1.17e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 8923579     21 LLLDPSSPP---TKALNGAEPNYHSLPSARTDEQALLSSILAKTASNIIDVSAADSQG-MEQHEYMDRA 85
Cdd:pfam15454   1 LLADPQNNSgnkRGYDNGLQQNYQESPPKLTDEQEALNRIVQNTSDNLIDISAMSSSGiVEQHEYMDRA 69
 
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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