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Conserved domains on  [gi|308044497|ref|NP_976307|]
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F-box and leucine-rich protein 22 isoform 1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
F-box_FBXL22 cd22129
F-box domain found in F-box/LRR-repeat protein 22 (FBXL22) and similar proteins; FBXL22, also ...
 9-51 5.04e-23

F-box domain found in F-box/LRR-repeat protein 22 (FBXL22) and similar proteins; FBXL22, also called F-box and leucine-rich repeat protein 22, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex that promotes ubiquitination of sarcomeric proteins alpha-actinin-2 (ACTN2) and filamin-C (FLNC). It acts as a cardiac-enriched F-box protein that regulates sarcomeric protein turnover and is essential for maintenance of contractile function in vivo. 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: 438901  Cd Length: 43  Bit Score: 87.94  E-value: 5.04e-23
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 308044497   9 ITQLNRECLLHLFSFLDKDSRKSLARTCSQLHDVFEDPALWSL 51
Cdd:cd22129    1 ITELNRECLLHLFSFLDKDSRRSLSLTCHRLRDVFLDPALWSL 43
 
Name Accession Description Interval E-value
F-box_FBXL22 cd22129
F-box domain found in F-box/LRR-repeat protein 22 (FBXL22) and similar proteins; FBXL22, also ...
 9-51 5.04e-23

F-box domain found in F-box/LRR-repeat protein 22 (FBXL22) and similar proteins; FBXL22, also called F-box and leucine-rich repeat protein 22, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex that promotes ubiquitination of sarcomeric proteins alpha-actinin-2 (ACTN2) and filamin-C (FLNC). It acts as a cardiac-enriched F-box protein that regulates sarcomeric protein turnover and is essential for maintenance of contractile function in vivo. 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: 438901  Cd Length: 43  Bit Score: 87.94  E-value: 5.04e-23
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 308044497   9 ITQLNRECLLHLFSFLDKDSRKSLARTCSQLHDVFEDPALWSL 51
Cdd:cd22129    1 ITELNRECLLHLFSFLDKDSRRSLSLTCHRLRDVFLDPALWSL 43
F-box-like pfam12937
F-box-like; This is an F-box-like family.
 9-49 3.31e-05

F-box-like; This is an F-box-like family.


Pssm-ID: 463757 [Multi-domain]  Cd Length: 45  Bit Score: 40.16  E-value: 3.31e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 308044497    9 ITQLNRECLLHLFSFLDKDSRKSLARTCSQLHDVFEDPALW 49
Cdd:pfam12937   1 LSSLPDEILLQIFSYLDPKDLLRLALVCRRWRELASDDSLW 41
 
Name Accession Description Interval E-value
F-box_FBXL22 cd22129
F-box domain found in F-box/LRR-repeat protein 22 (FBXL22) and similar proteins; FBXL22, also ...
 9-51 5.04e-23

F-box domain found in F-box/LRR-repeat protein 22 (FBXL22) and similar proteins; FBXL22, also called F-box and leucine-rich repeat protein 22, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex that promotes ubiquitination of sarcomeric proteins alpha-actinin-2 (ACTN2) and filamin-C (FLNC). It acts as a cardiac-enriched F-box protein that regulates sarcomeric protein turnover and is essential for maintenance of contractile function in vivo. 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: 438901  Cd Length: 43  Bit Score: 87.94  E-value: 5.04e-23
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 308044497   9 ITQLNRECLLHLFSFLDKDSRKSLARTCSQLHDVFEDPALWSL 51
Cdd:cd22129    1 ITELNRECLLHLFSFLDKDSRRSLSLTCHRLRDVFLDPALWSL 43
F-box_FBXL4 cd22117
F-box domain found in F-box/LRR-repeat protein 4 (FBXL4) and similar proteins; FBXL4, also ...
 12-55 2.92e-05

F-box domain found in F-box/LRR-repeat protein 4 (FBXL4) and similar proteins; FBXL4, also called F-box and leucine-rich repeat protein 4, or F-box protein FBL4/FBL5, is part of an SCF (SKP1-cullin-F-box) protein ligase complex. It serves as a clock output molecule that regulates sleep through promotion of rhythmic degradation of the GABA(A) receptor. Biallelic pathogenic variants in FBXL4 are associated with an encephalopathic mtDNA maintenance defect syndrome that is a multi-system disease characterized by lactic acidemia, developmental delay, and hypotonia. 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: 438889  Cd Length: 47  Bit Score: 40.30  E-value: 2.92e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 308044497  12 LNRECLLHLFSFLDKDSRKSLARTCSQLHDVFEDPALWSLLHFR 55
Cdd:cd22117    4 LPYELIQLILSYLDLPSLCRLSQTCKLFRKHCYDPLLWKELNLQ 47
F-box-like pfam12937
F-box-like; This is an F-box-like family.
 9-49 3.31e-05

F-box-like; This is an F-box-like family.


Pssm-ID: 463757 [Multi-domain]  Cd Length: 45  Bit Score: 40.16  E-value: 3.31e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 308044497    9 ITQLNRECLLHLFSFLDKDSRKSLARTCSQLHDVFEDPALW 49
Cdd:pfam12937   1 LSSLPDEILLQIFSYLDPKDLLRLALVCRRWRELASDDSLW 41
F-box_AtSKIP5-like cd22163
F-box domain found in Arabidopsis thaliana SKP1-interacting partner 5 (AtSKIP5) and similar ...
 9-49 4.03e-04

F-box domain found in Arabidopsis thaliana SKP1-interacting partner 5 (AtSKIP5) and similar proteins; AtSKIP5, also called F-box protein SKIP5, is a component of SCF (SKP1-cullin-F-box protein) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins. It interacts with SKP1A/ASK1. 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: 438934  Cd Length: 46  Bit Score: 37.33  E-value: 4.03e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 308044497   9 ITQLNRECLLHLFSFL-DKDSRKSLARTCSQLHDVFEDPALW 49
Cdd:cd22163    1 INDLDDDCLMHIFSFLtPLPDRFNAARVCKRWRALALDPRSW 42
F-box_unchar cd22138
F-box domain found in uncharacterized F-box protein group similar to F-box only protein 13 ...
 15-53 1.02e-03

F-box domain found in uncharacterized F-box protein group similar to F-box only protein 13 (FBXO13); The family corresponds to a group of uncharacterized F-box proteins which show sequence similarity to F-box only protein 13 (FBXO13). FBXO13, also called FBX13, or F-box/LRR-repeat protein 17 (FBL17), or F-box and leucine-rich repeat protein 17 (FBXL17), is the substrate-recognition component of the SCF(FBXL17) E3 ubiquitin ligase complex, a key component of a quality control pathway required to ensure functional dimerization of BTB domain-containing proteins (dimerization quality control, DQC). 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: 438910  Cd Length: 45  Bit Score: 36.15  E-value: 1.02e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 308044497  15 ECLLHLFSFLDKDSRKSLARTCSQLHDVFEDPALWSLLH 53
Cdd:cd22138    7 ECQLKIFSFLSEVDKCLAATVCRSWSELIRSPRLWRTVD 45
F-box_SF cd09917
F-box domain superfamily; This short domain is commonly found at the N-terminus of various ...
 10-44 2.21e-03

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.


Pssm-ID: 438852  Cd Length: 35  Bit Score: 34.73  E-value: 2.21e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 308044497  10 TQLNRECLLHLFSFLDKDSRKSLARTCSQLHDVFE 44
Cdd:cd09917    1 SDLPDEILLKILSYLDPRDLLRLSLVCKRWRELAS 35
F-box_FBXO7 cd22087
F-box domain found in F-box only protein 7 (FBXO7) and similar proteins; FBXO7, also called ...
 12-52 3.95e-03

F-box domain found in F-box only protein 7 (FBXO7) and similar proteins; FBXO7, also called FBX7, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. It recognizes BIRC2 and DLGAP5. FBXO7 plays a role downstream of PINK1 in the clearance of damaged mitochondria via selective autophagy (mitophagy) by targeting PRKN to dysfunctional depolarized mitochondria. It promotes MFN1 ubiquitination. FBXO7 acts as a cell cycle regulator by enhancing cyclin D/cyclin-dependent kinase 6 (Cdk6) complex formation and stabilizing levels of p27, a cyclin-dependent kinase inhibitor. Mutations in the FBXO7 (PARK15) gene have been implicated in a juvenile form of parkinsonism called parkinsonian pyramidal syndrome (PPS), characterized by Parkinsonian symptoms and pyramidal tract signs. 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: 438859  Cd Length: 45  Bit Score: 34.58  E-value: 3.95e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 308044497  12 LNRECLLHLFSFLDKDSRKSLARTCSQLHDVFEDPALWSLL 52
Cdd:cd22087    4 LPPEIKLRILSLLDVRSLLSLSQVCRDLNSATNDQLLWRFL 44
F-box pfam00646
F-box domain; This domain is approximately 50 amino acids long, and is usually found in the ...
 9-51 8.95e-03

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: 33.28  E-value: 8.95e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 308044497    9 ITQLNRECLLHLFSFLDKDSRKSLARTCSQLHDVFEDPALWSL 51
Cdd:pfam00646   1 LLDLPDDLLLEILSRLDPKDLLRLSLVSKRWRSLVDSLKLWKK 43
 
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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