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Conserved domains on  [gi|25155173|ref|NP_741646|]
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F-box domain-containing protein [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FTH pfam01827
FTH domain; This presumed domain is likely to be a protein-protein interaction module. It is ...
 202-342 1.86e-33

FTH domain; This presumed domain is likely to be a protein-protein interaction module. It is found in many proteins from C. elegans. The domain is found associated with the F-box pfam00646. This domain is named FTH after FOG-2 homology domain.


:

Pssm-ID: 396410  Cd Length: 141  Bit Score: 121.53  E-value: 1.86e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25155173   202 LFDALKNVLQSVGVLTTKSVLINWLPSVQIAEILEHFNTEILEDLTIkSSESDENSIKRLVRLEQWKQAKTLTLSPVPHY 281
Cdd:pfam01827   3 IIESFLNILKSKKCLHVKEISLSGLSFSEVASILPYFDAGTLEEIEL-SSESDEDQFEEIVELEQWKNAKSLKIEGSSLS 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25155173   282 SLIVKHLAHFQSLNFDFSEeaFSENDITRLRDeVVLESTKFEYFTCERVQFDATHLLRVFD 342
Cdd:pfam01827  82 SFPIEHLFHFEEFDIKLDS--FSVEDAIKIRD-ILLKSSTFQSCTIRSPDLNPIEIAKVFD 139
HTH_48 super family cl39372
HTH domain in Mos1 transposase; The N-terminal domain of the Mos1 Mariner transposase ...
 16-63 4.94e-07

HTH domain in Mos1 transposase; The N-terminal domain of the Mos1 Mariner transposase comprises two HTH domains. This HTH domain binds in the DNA major groove to the transposons inverted repeats.


The actual alignment was detected with superfamily member pfam17906:

Pssm-ID: 465558 [Multi-domain]  Cd Length: 50  Bit Score: 45.97  E-value: 4.94e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 25155173    16 RALRICILFQLLQEIPVLDAYEAMCKAFGEQFMEYLHFEYWYMGLSNG 63
Cdd:pfam17906   2 IHLRHCILYEFLQGKSAAEAYRNICEVYGEDAVSERTFQRWFARFRSG 49
F-box_CeFBXA-like cd22150
F-box domain found in Caenorhabditis elegans F-box domain-containing proteins (CeFBXA) and ...
 92-126 1.40e-05

F-box domain found in Caenorhabditis elegans F-box domain-containing proteins (CeFBXA) and similar proteins; The family includes a group of uncharacterized Caenorhabditis elegans F-box domain-containing proteins. They may be components of SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


:

Pssm-ID: 438921  Cd Length: 46  Bit Score: 41.70  E-value: 1.40e-05
                        10        20        30
                ....*....|....*....|....*....|....*
gi 25155173  92 ILDKLNPIDRFTAGAVCCSFKSIIDYQRSNLKKFH 126
Cdd:cd22150  12 ILDKLDPIDRLVLRKVSRNLRDIVDNQDPGFKKIS 46
 
Name Accession Description Interval E-value
FTH pfam01827
FTH domain; This presumed domain is likely to be a protein-protein interaction module. It is ...
 202-342 1.86e-33

FTH domain; This presumed domain is likely to be a protein-protein interaction module. It is found in many proteins from C. elegans. The domain is found associated with the F-box pfam00646. This domain is named FTH after FOG-2 homology domain.


Pssm-ID: 396410  Cd Length: 141  Bit Score: 121.53  E-value: 1.86e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25155173   202 LFDALKNVLQSVGVLTTKSVLINWLPSVQIAEILEHFNTEILEDLTIkSSESDENSIKRLVRLEQWKQAKTLTLSPVPHY 281
Cdd:pfam01827   3 IIESFLNILKSKKCLHVKEISLSGLSFSEVASILPYFDAGTLEEIEL-SSESDEDQFEEIVELEQWKNAKSLKIEGSSLS 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25155173   282 SLIVKHLAHFQSLNFDFSEeaFSENDITRLRDeVVLESTKFEYFTCERVQFDATHLLRVFD 342
Cdd:pfam01827  82 SFPIEHLFHFEEFDIKLDS--FSVEDAIKIRD-ILLKSSTFQSCTIRSPDLNPIEIAKVFD 139
HTH_48 pfam17906
HTH domain in Mos1 transposase; The N-terminal domain of the Mos1 Mariner transposase ...
 16-63 4.94e-07

HTH domain in Mos1 transposase; The N-terminal domain of the Mos1 Mariner transposase comprises two HTH domains. This HTH domain binds in the DNA major groove to the transposons inverted repeats.


Pssm-ID: 465558 [Multi-domain]  Cd Length: 50  Bit Score: 45.97  E-value: 4.94e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 25155173    16 RALRICILFQLLQEIPVLDAYEAMCKAFGEQFMEYLHFEYWYMGLSNG 63
Cdd:pfam17906   2 IHLRHCILYEFLQGKSAAEAYRNICEVYGEDAVSERTFQRWFARFRSG 49
F-box_CeFBXA-like cd22150
F-box domain found in Caenorhabditis elegans F-box domain-containing proteins (CeFBXA) and ...
 92-126 1.40e-05

F-box domain found in Caenorhabditis elegans F-box domain-containing proteins (CeFBXA) and similar proteins; The family includes a group of uncharacterized Caenorhabditis elegans F-box domain-containing proteins. They may be components of SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438921  Cd Length: 46  Bit Score: 41.70  E-value: 1.40e-05
                        10        20        30
                ....*....|....*....|....*....|....*
gi 25155173  92 ILDKLNPIDRFTAGAVCCSFKSIIDYQRSNLKKFH 126
Cdd:cd22150  12 ILDKLDPIDRLVLRKVSRNLRDIVDNQDPGFKKIS 46
FBOX smart00256
A Receptor for Ubiquitination Targets;
88-124 5.09e-05

A Receptor for Ubiquitination Targets;


Pssm-ID: 197608  Cd Length: 41  Bit Score: 40.11  E-value: 5.09e-05
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 25155173     88 LQTMILDKLNPIDRFTAGAVCCSFKSIIDYQRSNLKK 124
Cdd:smart00256   5 ILEEILSKLDPKDLLRLRKVSRKWRSLIDSHDFWFKL 41
 
Name Accession Description Interval E-value
FTH pfam01827
FTH domain; This presumed domain is likely to be a protein-protein interaction module. It is ...
 202-342 1.86e-33

FTH domain; This presumed domain is likely to be a protein-protein interaction module. It is found in many proteins from C. elegans. The domain is found associated with the F-box pfam00646. This domain is named FTH after FOG-2 homology domain.


Pssm-ID: 396410  Cd Length: 141  Bit Score: 121.53  E-value: 1.86e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25155173   202 LFDALKNVLQSVGVLTTKSVLINWLPSVQIAEILEHFNTEILEDLTIkSSESDENSIKRLVRLEQWKQAKTLTLSPVPHY 281
Cdd:pfam01827   3 IIESFLNILKSKKCLHVKEISLSGLSFSEVASILPYFDAGTLEEIEL-SSESDEDQFEEIVELEQWKNAKSLKIEGSSLS 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25155173   282 SLIVKHLAHFQSLNFDFSEeaFSENDITRLRDeVVLESTKFEYFTCERVQFDATHLLRVFD 342
Cdd:pfam01827  82 SFPIEHLFHFEEFDIKLDS--FSVEDAIKIRD-ILLKSSTFQSCTIRSPDLNPIEIAKVFD 139
HTH_48 pfam17906
HTH domain in Mos1 transposase; The N-terminal domain of the Mos1 Mariner transposase ...
 16-63 4.94e-07

HTH domain in Mos1 transposase; The N-terminal domain of the Mos1 Mariner transposase comprises two HTH domains. This HTH domain binds in the DNA major groove to the transposons inverted repeats.


Pssm-ID: 465558 [Multi-domain]  Cd Length: 50  Bit Score: 45.97  E-value: 4.94e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 25155173    16 RALRICILFQLLQEIPVLDAYEAMCKAFGEQFMEYLHFEYWYMGLSNG 63
Cdd:pfam17906   2 IHLRHCILYEFLQGKSAAEAYRNICEVYGEDAVSERTFQRWFARFRSG 49
F-box_CeFBXA-like cd22150
F-box domain found in Caenorhabditis elegans F-box domain-containing proteins (CeFBXA) and ...
 92-126 1.40e-05

F-box domain found in Caenorhabditis elegans F-box domain-containing proteins (CeFBXA) and similar proteins; The family includes a group of uncharacterized Caenorhabditis elegans F-box domain-containing proteins. They may be components of SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438921  Cd Length: 46  Bit Score: 41.70  E-value: 1.40e-05
                        10        20        30
                ....*....|....*....|....*....|....*
gi 25155173  92 ILDKLNPIDRFTAGAVCCSFKSIIDYQRSNLKKFH 126
Cdd:cd22150  12 ILDKLDPIDRLVLRKVSRNLRDIVDNQDPGFKKIS 46
FBOX smart00256
A Receptor for Ubiquitination Targets;
88-124 5.09e-05

A Receptor for Ubiquitination Targets;


Pssm-ID: 197608  Cd Length: 41  Bit Score: 40.11  E-value: 5.09e-05
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 25155173     88 LQTMILDKLNPIDRFTAGAVCCSFKSIIDYQRSNLKK 124
Cdd:smart00256   5 ILEEILSKLDPKDLLRLRKVSRKWRSLIDSHDFWFKL 41
 
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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