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Conserved domains on  [gi|15235367|ref|NP_192153|]
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F-box family protein [Arabidopsis thaliana]

Protein Classification

F-box protein( domain architecture ID 10458603)

F-box protein may function as the substrate-recognition component of a SCF(Skp1-cullin-F-box) E3 ubiquitin ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins

CATH:  1.20.1280.50
Gene Ontology:  GO:0005515
PubMed:  31898225|11178263
SCOP:  4001927

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
F-box pfam00646
F-box domain; This domain is approximately 50 amino acids long, and is usually found in the ...
6-48 1.23e-04

F-box domain; This domain is approximately 50 amino acids long, and is usually found in the N-terminal half of a variety of proteins. Two motifs that are commonly found associated with the F-box domain are the leucine rich repeats (LRRs; pfam00560 and pfam07723) and the WD repeat (pfam00400). 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: 425796  Cd Length: 43  Bit Score: 39.06  E-value: 1.23e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 15235367     6 FSCIPEDVVFNIFFKLqdDPRNWARLACVCTKFSSIVRNVCCK 48
Cdd:pfam00646   1 LLDLPDDLLLEILSRL--DPKDLLRLSLVSKRWRSLVDSLKLW 41
 
Name Accession Description Interval E-value
F-box pfam00646
F-box domain; This domain is approximately 50 amino acids long, and is usually found in the ...
6-48 1.23e-04

F-box domain; This domain is approximately 50 amino acids long, and is usually found in the N-terminal half of a variety of proteins. Two motifs that are commonly found associated with the F-box domain are the leucine rich repeats (LRRs; pfam00560 and pfam07723) and the WD repeat (pfam00400). 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: 425796  Cd Length: 43  Bit Score: 39.06  E-value: 1.23e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 15235367     6 FSCIPEDVVFNIFFKLqdDPRNWARLACVCTKFSSIVRNVCCK 48
Cdd:pfam00646   1 LLDLPDDLLLEILSRL--DPKDLLRLSLVSKRWRSLVDSLKLW 41
F-box_AtGID2-like cd22151
F-box domain found in Arabidopsis thaliana F-box protein GID2 and similar proteins; AtGID2, ...
7-44 8.77e-04

F-box domain found in Arabidopsis thaliana F-box protein GID2 and similar proteins; AtGID2, also called protein SLEEPY 1, is an essential component of the SCF-type E3 ligase complex, SCF(GID2), a complex that positively regulates the gibberellin signaling pathway. Upon gibberellin treatment, the SCF(GID2) complex mediates the ubiquitination and subsequent degradation of DELLA proteins (GAI, RGA and RGL2), some repressors of the gibberellin pathway, leading to the activation of the pathway. 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: 438922  Cd Length: 44  Bit Score: 36.53  E-value: 8.77e-04
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 15235367   7 SCIPEDVVFNIFFKLqdDPRNWARLACVCTKFSSIVRN 44
Cdd:cd22151   1 RKLPDDLLQEIFKRL--DPKSLARAACVCRRWRAAARS 36
 
Name Accession Description Interval E-value
F-box pfam00646
F-box domain; This domain is approximately 50 amino acids long, and is usually found in the ...
6-48 1.23e-04

F-box domain; This domain is approximately 50 amino acids long, and is usually found in the N-terminal half of a variety of proteins. Two motifs that are commonly found associated with the F-box domain are the leucine rich repeats (LRRs; pfam00560 and pfam07723) and the WD repeat (pfam00400). 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: 425796  Cd Length: 43  Bit Score: 39.06  E-value: 1.23e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 15235367     6 FSCIPEDVVFNIFFKLqdDPRNWARLACVCTKFSSIVRNVCCK 48
Cdd:pfam00646   1 LLDLPDDLLLEILSRL--DPKDLLRLSLVSKRWRSLVDSLKLW 41
F-box_AtGID2-like cd22151
F-box domain found in Arabidopsis thaliana F-box protein GID2 and similar proteins; AtGID2, ...
7-44 8.77e-04

F-box domain found in Arabidopsis thaliana F-box protein GID2 and similar proteins; AtGID2, also called protein SLEEPY 1, is an essential component of the SCF-type E3 ligase complex, SCF(GID2), a complex that positively regulates the gibberellin signaling pathway. Upon gibberellin treatment, the SCF(GID2) complex mediates the ubiquitination and subsequent degradation of DELLA proteins (GAI, RGA and RGL2), some repressors of the gibberellin pathway, leading to the activation of the pathway. 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: 438922  Cd Length: 44  Bit Score: 36.53  E-value: 8.77e-04
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 15235367   7 SCIPEDVVFNIFFKLqdDPRNWARLACVCTKFSSIVRN 44
Cdd:cd22151   1 RKLPDDLLQEIFKRL--DPKSLARAACVCRRWRAAARS 36
 
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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