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Conserved domains on  [gi|1039772472|ref|XP_017176580|]
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uncharacterized protein LOC69396 isoform X1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
REM super family cl02520
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal domain (RasGef_N), also ...
63-160 1.21e-07

Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal domain (RasGef_N), also called REM domain (Ras exchanger motif). This domain is common in nucleotide exchange factors for Ras-like small GTPases and is typically found immediately N-terminal to the RasGef (Cdc25-like) domain. REM contacts the GTPase and is assumed to participate in the catalytic activity of the exchange factor. Proteins with the REM domain include Sos1 and Sos2, which relay signals from tyrosine-kinase mediated signalling to Ras, RasGRP1-4, RasGRF1,2, CNrasGEF, and RAP-specific nucleotide exchange factors, to name a few.


The actual alignment was detected with superfamily member cd06224:

Pssm-ID: 470601  Cd Length: 122  Bit Score: 49.33  E-value: 1.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772472  63 VEQMIAYIPAAVHYHDQLSISLFLAVYHRYCSTWEVLDLLMKT------------------------AIFSFLAHWLDTF 118
Cdd:cd06224     2 LEALIEHLTSTFDMPDPSFVSTFLLTYRSFTTPTELLEKLIERyeiappenleyndwdkkkskpirlRVLNVLRTWVENY 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1039772472 119 PEHFFDSPNLavMRQLMDYAGRHMPSAEFDKESRELLSRLEE 160
Cdd:cd06224    82 PYDFFDDEEL--LELLEEFLNRLVQEGALLQELKKLLRKLLK 121
 
Name Accession Description Interval E-value
REM cd06224
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal domain (RasGef_N), also ...
63-160 1.21e-07

Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal domain (RasGef_N), also called REM domain (Ras exchanger motif). This domain is common in nucleotide exchange factors for Ras-like small GTPases and is typically found immediately N-terminal to the RasGef (Cdc25-like) domain. REM contacts the GTPase and is assumed to participate in the catalytic activity of the exchange factor. Proteins with the REM domain include Sos1 and Sos2, which relay signals from tyrosine-kinase mediated signalling to Ras, RasGRP1-4, RasGRF1,2, CNrasGEF, and RAP-specific nucleotide exchange factors, to name a few.


Pssm-ID: 100121  Cd Length: 122  Bit Score: 49.33  E-value: 1.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772472  63 VEQMIAYIPAAVHYHDQLSISLFLAVYHRYCSTWEVLDLLMKT------------------------AIFSFLAHWLDTF 118
Cdd:cd06224     2 LEALIEHLTSTFDMPDPSFVSTFLLTYRSFTTPTELLEKLIERyeiappenleyndwdkkkskpirlRVLNVLRTWVENY 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1039772472 119 PEHFFDSPNLavMRQLMDYAGRHMPSAEFDKESRELLSRLEE 160
Cdd:cd06224    82 PYDFFDDEEL--LELLEEFLNRLVQEGALLQELKKLLRKLLK 121
 
Name Accession Description Interval E-value
REM cd06224
Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal domain (RasGef_N), also ...
63-160 1.21e-07

Guanine nucleotide exchange factor for Ras-like GTPases; N-terminal domain (RasGef_N), also called REM domain (Ras exchanger motif). This domain is common in nucleotide exchange factors for Ras-like small GTPases and is typically found immediately N-terminal to the RasGef (Cdc25-like) domain. REM contacts the GTPase and is assumed to participate in the catalytic activity of the exchange factor. Proteins with the REM domain include Sos1 and Sos2, which relay signals from tyrosine-kinase mediated signalling to Ras, RasGRP1-4, RasGRF1,2, CNrasGEF, and RAP-specific nucleotide exchange factors, to name a few.


Pssm-ID: 100121  Cd Length: 122  Bit Score: 49.33  E-value: 1.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772472  63 VEQMIAYIPAAVHYHDQLSISLFLAVYHRYCSTWEVLDLLMKT------------------------AIFSFLAHWLDTF 118
Cdd:cd06224     2 LEALIEHLTSTFDMPDPSFVSTFLLTYRSFTTPTELLEKLIERyeiappenleyndwdkkkskpirlRVLNVLRTWVENY 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1039772472 119 PEHFFDSPNLavMRQLMDYAGRHMPSAEFDKESRELLSRLEE 160
Cdd:cd06224    82 PYDFFDDEEL--LELLEEFLNRLVQEGALLQELKKLLRKLLK 121
 
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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