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Conserved domains on  [gi|1780581131|emb|VYS65684|]
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unnamed protein product [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
F-box_SF super family cl45894
F-box domain superfamily; This short domain is commonly found at the N-terminus of various ...
24-61 9.00e-09

F-box domain superfamily; This short domain is commonly found at the N-terminus of various proteins, and typically co-occurs with one or more other conserved domains or motifs, such as leucine rich repeats, WD40 repeats, kelch, tub, spry, and others. 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. One of the best researched roles of F-box proteins is their participation in SCF (Skp1-Cul1-F-box protein), a multi-protein complex that functions as a ubiquitin E3 ligase, where the role of the F-box protein is to recruit target substrates. Gene families containing the F-box are found greatly expanded in narrow taxonomic lineages, such as flowering plants and nematodes. In this hierarchical classification, many of the subfamilies are named according to their domain architectures.


The actual alignment was detected with superfamily member cd22152:

Pssm-ID: 459239  Cd Length: 45  Bit Score: 48.72  E-value: 9.00e-09
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1780581131  24 DVALNCWARVSRIHYPTLFLVSKNLRSLIASPELEATR 61
Cdd:cd22152     8 DIALQCLARVPRSSHPSLSLVSKSWRSLLSSPELFRVR 45
Kelch_1 pfam01344
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
108-149 4.46e-06

Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six copies of the motif. It has been shown that Swiss:Q04652 is related to Galactose Oxidase for which a structure has been solved. The kelch motif forms a beta sheet. Several of these sheets associate to form a beta propeller structure as found in pfam00064, pfam00400 and pfam00415.


:

Pssm-ID: 396078 [Multi-domain]  Cd Length: 46  Bit Score: 41.44  E-value: 4.46e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1780581131 108 KYSTILLVDSLIYIIGGIVNRQRSNRVLILNSLSHQWSSLPN 149
Cdd:pfam01344   3 SGAGVVVVGGKIYVIGGFDGNQSLNSVEVYDPETNTWSKLPS 44
 
Name Accession Description Interval E-value
F-box_AtAFR-like cd22152
F-box domain found in Arabidopsis thaliana protein ATTENUATED FAR-RED RESPONSE (AtAFR) and ...
24-61 9.00e-09

F-box domain found in Arabidopsis thaliana protein ATTENUATED FAR-RED RESPONSE (AtAFR) and similar proteins; AtAFR, also called SKP1-interacting partner 29 (AtSKIP29), or F-box protein AFR, is a component of SCF (SKP1/ASK-cullin-F-box protein) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins. It is part of the phyA-mediated signaling transduction pathway leading to the regulation of gene expression and hypocotyl elongation in response to red and far-red light exposure. This subfamily also includes many other Arabidopsis thaliana SKP1-interacting partner 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: 438923  Cd Length: 45  Bit Score: 48.72  E-value: 9.00e-09
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1780581131  24 DVALNCWARVSRIHYPTLFLVSKNLRSLIASPELEATR 61
Cdd:cd22152     8 DIALQCLARVPRSSHPSLSLVSKSWRSLLSSPELFRVR 45
Kelch_1 pfam01344
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
108-149 4.46e-06

Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six copies of the motif. It has been shown that Swiss:Q04652 is related to Galactose Oxidase for which a structure has been solved. The kelch motif forms a beta sheet. Several of these sheets associate to form a beta propeller structure as found in pfam00064, pfam00400 and pfam00415.


Pssm-ID: 396078 [Multi-domain]  Cd Length: 46  Bit Score: 41.44  E-value: 4.46e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1780581131 108 KYSTILLVDSLIYIIGGIVNRQRSNRVLILNSLSHQWSSLPN 149
Cdd:pfam01344   3 SGAGVVVVGGKIYVIGGFDGNQSLNSVEVYDPETNTWSKLPS 44
Kelch smart00612
Kelch domain;
118-149 3.48e-04

Kelch domain;


Pssm-ID: 128874 [Multi-domain]  Cd Length: 47  Bit Score: 36.38  E-value: 3.48e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1780581131  118 LIYIIGGIVNRQRSNRVLILNSLSHQWSSLPN 149
Cdd:smart00612   1 KIYVVGGFDGGQRLKSVEVYDPETNKWTPLPS 32
 
Name Accession Description Interval E-value
F-box_AtAFR-like cd22152
F-box domain found in Arabidopsis thaliana protein ATTENUATED FAR-RED RESPONSE (AtAFR) and ...
24-61 9.00e-09

F-box domain found in Arabidopsis thaliana protein ATTENUATED FAR-RED RESPONSE (AtAFR) and similar proteins; AtAFR, also called SKP1-interacting partner 29 (AtSKIP29), or F-box protein AFR, is a component of SCF (SKP1/ASK-cullin-F-box protein) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins. It is part of the phyA-mediated signaling transduction pathway leading to the regulation of gene expression and hypocotyl elongation in response to red and far-red light exposure. This subfamily also includes many other Arabidopsis thaliana SKP1-interacting partner 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: 438923  Cd Length: 45  Bit Score: 48.72  E-value: 9.00e-09
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1780581131  24 DVALNCWARVSRIHYPTLFLVSKNLRSLIASPELEATR 61
Cdd:cd22152     8 DIALQCLARVPRSSHPSLSLVSKSWRSLLSSPELFRVR 45
Kelch_1 pfam01344
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
108-149 4.46e-06

Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six copies of the motif. It has been shown that Swiss:Q04652 is related to Galactose Oxidase for which a structure has been solved. The kelch motif forms a beta sheet. Several of these sheets associate to form a beta propeller structure as found in pfam00064, pfam00400 and pfam00415.


Pssm-ID: 396078 [Multi-domain]  Cd Length: 46  Bit Score: 41.44  E-value: 4.46e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1780581131 108 KYSTILLVDSLIYIIGGIVNRQRSNRVLILNSLSHQWSSLPN 149
Cdd:pfam01344   3 SGAGVVVVGGKIYVIGGFDGNQSLNSVEVYDPETNTWSKLPS 44
Kelch smart00612
Kelch domain;
118-149 3.48e-04

Kelch domain;


Pssm-ID: 128874 [Multi-domain]  Cd Length: 47  Bit Score: 36.38  E-value: 3.48e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1780581131  118 LIYIIGGIVNRQRSNRVLILNSLSHQWSSLPN 149
Cdd:smart00612   1 KIYVVGGFDGGQRLKSVEVYDPETNKWTPLPS 32
Kelch_6 pfam13964
Kelch motif;
106-150 5.94e-04

Kelch motif;


Pssm-ID: 404790 [Multi-domain]  Cd Length: 50  Bit Score: 36.16  E-value: 5.94e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1780581131 106 HPKYSTILLVDSLIYIIGGIVNR-QRSNRVLILNSLSHQWSSLPNI 150
Cdd:pfam13964   1 PRTFHSVVSVGGYIYVFGGYTNAsPALNKLEVYNPLTKSWEELPPL 46
 
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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