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Conserved domains on  [gi|1799133592|ref|NP_001364749|]
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F-box domain-containing protein [Caenorhabditis elegans]

Protein Classification

F-box protein( domain architecture ID 10459153)

F-box protein is 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:0019005|GO:0005515|GO:0006511
PubMed:  11178263|31898225
SCOP:  4001927

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FBA_2 pfam07735
F-box associated; Most of these proteins contain pfam00646 at the N terminus, suggesting that ...
196-255 1.35e-10

F-box associated; Most of these proteins contain pfam00646 at the N terminus, suggesting that they are effectors linked with ubiquitination.


:

Pssm-ID: 429626  Cd Length: 67  Bit Score: 56.42  E-value: 1.35e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133592 196 HEILVRNFFSFSASFPEHNFNLNDLLIMNSTHLRIRSSQLAFEDLNIFLKHLKTGLNQTL 255
Cdd:pfam07735   3 QKILIQNLDELTIGDSSVWITLDDLLLINSKKIELDNSRLSLKDLNRFLKHWIKGSNPRL 62
F-box pfam00646
F-box domain; This domain is approximately 50 amino acids long, and is usually found in the ...
7-49 9.36e-05

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: 39.45  E-value: 9.36e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1799133592   7 ILRLPNKIIRNVVENLSFYNQLTFSLCSKATKSCVTPLRHKIR 49
Cdd:pfam00646   1 LLDLPDDLLLEILSRLDPKDLLRLSLVSKRWRSLVDSLKLWKK 43
class_II_aaRS-like_core super family cl00268
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ...
144-202 2.46e-03

Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA synthetases (aaRS) share a common fold and generally attach an amino acid to the 3' OH of ribose of the appropriate tRNA. PheRS is an exception in that it attaches the amino acid at the 2'-OH group, like class I aaRSs. These enzymes are usually homodimers. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. The substrate specificity of this reaction is further determined by additional domains. Intererestingly, this domain is also found is asparagine synthase A (AsnA), in the accessory subunit of mitochondrial polymerase gamma and in the bacterial ATP phosphoribosyltransferase regulatory subunit HisZ.


The actual alignment was detected with superfamily member PRK12293:

Pssm-ID: 444800  Cd Length: 281  Bit Score: 39.21  E-value: 2.46e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1799133592 144 LKRVCEAmkglTARKIFLKNWTDEIVQNVICSIQHKGISFNKKLISNSSSLNHEILVRN 202
Cdd:PRK12293   21 LKREIEN----VASEILYENGFEEIVTPFFSYHQHQSIADEKELIRFSDEKNHQISLRA 75
 
Name Accession Description Interval E-value
FBA_2 pfam07735
F-box associated; Most of these proteins contain pfam00646 at the N terminus, suggesting that ...
196-255 1.35e-10

F-box associated; Most of these proteins contain pfam00646 at the N terminus, suggesting that they are effectors linked with ubiquitination.


Pssm-ID: 429626  Cd Length: 67  Bit Score: 56.42  E-value: 1.35e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133592 196 HEILVRNFFSFSASFPEHNFNLNDLLIMNSTHLRIRSSQLAFEDLNIFLKHLKTGLNQTL 255
Cdd:pfam07735   3 QKILIQNLDELTIGDSSVWITLDDLLLINSKKIELDNSRLSLKDLNRFLKHWIKGSNPRL 62
F-box pfam00646
F-box domain; This domain is approximately 50 amino acids long, and is usually found in the ...
7-49 9.36e-05

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: 39.45  E-value: 9.36e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1799133592   7 ILRLPNKIIRNVVENLSFYNQLTFSLCSKATKSCVTPLRHKIR 49
Cdd:pfam00646   1 LLDLPDDLLLEILSRLDPKDLLRLSLVSKRWRSLVDSLKLWKK 43
hisZ PRK12293
ATP phosphoribosyltransferase regulatory subunit; Provisional
144-202 2.46e-03

ATP phosphoribosyltransferase regulatory subunit; Provisional


Pssm-ID: 183411  Cd Length: 281  Bit Score: 39.21  E-value: 2.46e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1799133592 144 LKRVCEAmkglTARKIFLKNWTDEIVQNVICSIQHKGISFNKKLISNSSSLNHEILVRN 202
Cdd:PRK12293   21 LKREIEN----VASEILYENGFEEIVTPFFSYHQHQSIADEKELIRFSDEKNHQISLRA 75
 
Name Accession Description Interval E-value
FBA_2 pfam07735
F-box associated; Most of these proteins contain pfam00646 at the N terminus, suggesting that ...
196-255 1.35e-10

F-box associated; Most of these proteins contain pfam00646 at the N terminus, suggesting that they are effectors linked with ubiquitination.


Pssm-ID: 429626  Cd Length: 67  Bit Score: 56.42  E-value: 1.35e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133592 196 HEILVRNFFSFSASFPEHNFNLNDLLIMNSTHLRIRSSQLAFEDLNIFLKHLKTGLNQTL 255
Cdd:pfam07735   3 QKILIQNLDELTIGDSSVWITLDDLLLINSKKIELDNSRLSLKDLNRFLKHWIKGSNPRL 62
F-box pfam00646
F-box domain; This domain is approximately 50 amino acids long, and is usually found in the ...
7-49 9.36e-05

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: 39.45  E-value: 9.36e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1799133592   7 ILRLPNKIIRNVVENLSFYNQLTFSLCSKATKSCVTPLRHKIR 49
Cdd:pfam00646   1 LLDLPDDLLLEILSRLDPKDLLRLSLVSKRWRSLVDSLKLWKK 43
hisZ PRK12293
ATP phosphoribosyltransferase regulatory subunit; Provisional
144-202 2.46e-03

ATP phosphoribosyltransferase regulatory subunit; Provisional


Pssm-ID: 183411  Cd Length: 281  Bit Score: 39.21  E-value: 2.46e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1799133592 144 LKRVCEAmkglTARKIFLKNWTDEIVQNVICSIQHKGISFNKKLISNSSSLNHEILVRN 202
Cdd:PRK12293   21 LKREIEN----VASEILYENGFEEIVTPFFSYHQHQSIADEKELIRFSDEKNHQISLRA 75
 
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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