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Conserved domains on  [gi|18413178|ref|NP_567343|]
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F-BOX WITH WD-40 2 [Arabidopsis thaliana]

Protein Classification

F-box/LRR-repeat protein( domain architecture ID 1903223)

F-box/LRR-repeat protein functions as the substrate-recognition component of a SCF (Skp1-Cullin-F-box protein) ubiquitin-protein ligase that is involved in ubiquitin-dependent degradation

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 ...
10-46 2.02e-11

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 cd22158:

Pssm-ID: 459239  Cd Length: 36  Bit Score: 57.85  E-value: 2.02e-11
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 18413178  10 WDELIPDALGLIFSHLPLQEVLTVVPrVCKAWNRAVT 46
Cdd:cd22158   1 WDCLPPDLLELIFSHLPLHDILICRS-VCKFWNRLTT 36
AMN1 super family cl39120
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
63-244 1.34e-08

Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in Saccharomyces cerevisiae as a component of the Antagonist of MEN pathway (AMEN). The AMEN network is activated by MEN (mitotic exit network) via an active Cdc14, and in turn switches off MEN. Amn1 constitutes one of the alternative mechanisms by which MEN may be disrupted. Specifically, Amn1 binds Tem1 (Termination of M-phase, a GTPase that belongs to the RAS superfamily), and disrupts its association with Cdc15, the primary downstream target. Amn1 is a leucine-rich repeat (LRR) protein, with 12 repeats in the S. cerevisiae ortholog. As a negative regulator of the signal transduction pathway MEN, overexpression of AMN1 slows the growth of wild type cells. The function of the vertebrate members of this family has not been determined experimentally, they have fewer LRRs that determine the extent of this model.


The actual alignment was detected with superfamily member cd09293:

Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 54.26  E-value: 1.34e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413178  63 FH-QSDHLDRMLEMLIPRSAGSLRKLsvtGLRN----DSIFSFIaQHAGSLKTLKVPRSGLTNS-GVVNVAEKLSSLTFL 136
Cdd:cd09293   8 LHkLGQITQSNISQLLRILHSGLEWL---ELYMcpisDPPLDQL-SNCNKLKKLILPGSKLIDDeGLIALAQSCPNLQVL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413178 137 DLSYCCKIGPEAIQAIGKHCKSLREF----CRNMHPLDVASVVshddeayAIANTMPKLKRLEIAYHRVSTEGVLKILS- 211
Cdd:cd09293  84 DLRACENITDSGIVALATNCPKLQTInlgrHRNGHLITDVSLS-------ALGKNCTFLQTVGFAGCDVTDKGVWELASg 156
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 18413178 212 CCVFLEFLELRGCW---DVQLDNKFFKEKFPDMKVL 244
Cdd:cd09293 157 CSKSLERLSLNNCRnltDQSIPAILASNYFPNLSVL 192
 
Name Accession Description Interval E-value
F-box_AtFBW2-like cd22158
F-box domain found in Arabidopsis thaliana F-box protein FBW2 (AtFBW2) and similar proteins; ...
10-46 2.02e-11

F-box domain found in Arabidopsis thaliana F-box protein FBW2 (AtFBW2) and similar proteins; AtFBW2, also called SKP1-interacting partner 18 (SKIP18), is an F-box protein that contains four tandem WD-40 repeats. It is a component of SCF (SPK1/ASK-cullin-F-box protein) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins. It interacts with CUL1, CUL2 and SPK1B/ASK2. 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: 438929  Cd Length: 36  Bit Score: 57.85  E-value: 2.02e-11
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 18413178  10 WDELIPDALGLIFSHLPLQEVLTVVPrVCKAWNRAVT 46
Cdd:cd22158   1 WDCLPPDLLELIFSHLPLHDILICRS-VCKFWNRLTT 36
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
63-244 1.34e-08

Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in Saccharomyces cerevisiae as a component of the Antagonist of MEN pathway (AMEN). The AMEN network is activated by MEN (mitotic exit network) via an active Cdc14, and in turn switches off MEN. Amn1 constitutes one of the alternative mechanisms by which MEN may be disrupted. Specifically, Amn1 binds Tem1 (Termination of M-phase, a GTPase that belongs to the RAS superfamily), and disrupts its association with Cdc15, the primary downstream target. Amn1 is a leucine-rich repeat (LRR) protein, with 12 repeats in the S. cerevisiae ortholog. As a negative regulator of the signal transduction pathway MEN, overexpression of AMN1 slows the growth of wild type cells. The function of the vertebrate members of this family has not been determined experimentally, they have fewer LRRs that determine the extent of this model.


Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 54.26  E-value: 1.34e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413178  63 FH-QSDHLDRMLEMLIPRSAGSLRKLsvtGLRN----DSIFSFIaQHAGSLKTLKVPRSGLTNS-GVVNVAEKLSSLTFL 136
Cdd:cd09293   8 LHkLGQITQSNISQLLRILHSGLEWL---ELYMcpisDPPLDQL-SNCNKLKKLILPGSKLIDDeGLIALAQSCPNLQVL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413178 137 DLSYCCKIGPEAIQAIGKHCKSLREF----CRNMHPLDVASVVshddeayAIANTMPKLKRLEIAYHRVSTEGVLKILS- 211
Cdd:cd09293  84 DLRACENITDSGIVALATNCPKLQTInlgrHRNGHLITDVSLS-------ALGKNCTFLQTVGFAGCDVTDKGVWELASg 156
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 18413178 212 CCVFLEFLELRGCW---DVQLDNKFFKEKFPDMKVL 244
Cdd:cd09293 157 CSKSLERLSLNNCRnltDQSIPAILASNYFPNLSVL 192
F-box-like pfam12937
F-box-like; This is an F-box-like family.
10-55 2.56e-04

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


Pssm-ID: 463757 [Multi-domain]  Cd Length: 45  Bit Score: 37.85  E-value: 2.56e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 18413178    10 WDELIPDALGLIFSHLPLQEVLTVVpRVCKAWNRAVTGPYCWQEID 55
Cdd:pfam12937   1 LSSLPDEILLQIFSYLDPKDLLRLA-LVCRRWRELASDDSLWRRLC 45
PRK05917 PRK05917
DNA polymerase III subunit delta'; Validated
25-83 9.90e-03

DNA polymerase III subunit delta'; Validated


Pssm-ID: 102059 [Multi-domain]  Cd Length: 290  Bit Score: 37.08  E-value: 9.90e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 18413178   25 LPLQEVLTVVPRVCKAWNRAVTGPYCWQEIDIELWSNRFHQSdhldrmleMLIPRSAGS 83
Cdd:PRK05917 240 LPLEKVLSIIERAVQALDNSSSAPSCLEWVALQLWSLKNRQQ--------MLIRNRRGS 290
 
Name Accession Description Interval E-value
F-box_AtFBW2-like cd22158
F-box domain found in Arabidopsis thaliana F-box protein FBW2 (AtFBW2) and similar proteins; ...
10-46 2.02e-11

F-box domain found in Arabidopsis thaliana F-box protein FBW2 (AtFBW2) and similar proteins; AtFBW2, also called SKP1-interacting partner 18 (SKIP18), is an F-box protein that contains four tandem WD-40 repeats. It is a component of SCF (SPK1/ASK-cullin-F-box protein) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins. It interacts with CUL1, CUL2 and SPK1B/ASK2. 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: 438929  Cd Length: 36  Bit Score: 57.85  E-value: 2.02e-11
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 18413178  10 WDELIPDALGLIFSHLPLQEVLTVVPrVCKAWNRAVT 46
Cdd:cd22158   1 WDCLPPDLLELIFSHLPLHDILICRS-VCKFWNRLTT 36
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
63-244 1.34e-08

Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in Saccharomyces cerevisiae as a component of the Antagonist of MEN pathway (AMEN). The AMEN network is activated by MEN (mitotic exit network) via an active Cdc14, and in turn switches off MEN. Amn1 constitutes one of the alternative mechanisms by which MEN may be disrupted. Specifically, Amn1 binds Tem1 (Termination of M-phase, a GTPase that belongs to the RAS superfamily), and disrupts its association with Cdc15, the primary downstream target. Amn1 is a leucine-rich repeat (LRR) protein, with 12 repeats in the S. cerevisiae ortholog. As a negative regulator of the signal transduction pathway MEN, overexpression of AMN1 slows the growth of wild type cells. The function of the vertebrate members of this family has not been determined experimentally, they have fewer LRRs that determine the extent of this model.


Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 54.26  E-value: 1.34e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413178  63 FH-QSDHLDRMLEMLIPRSAGSLRKLsvtGLRN----DSIFSFIaQHAGSLKTLKVPRSGLTNS-GVVNVAEKLSSLTFL 136
Cdd:cd09293   8 LHkLGQITQSNISQLLRILHSGLEWL---ELYMcpisDPPLDQL-SNCNKLKKLILPGSKLIDDeGLIALAQSCPNLQVL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413178 137 DLSYCCKIGPEAIQAIGKHCKSLREF----CRNMHPLDVASVVshddeayAIANTMPKLKRLEIAYHRVSTEGVLKILS- 211
Cdd:cd09293  84 DLRACENITDSGIVALATNCPKLQTInlgrHRNGHLITDVSLS-------ALGKNCTFLQTVGFAGCDVTDKGVWELASg 156
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 18413178 212 CCVFLEFLELRGCW---DVQLDNKFFKEKFPDMKVL 244
Cdd:cd09293 157 CSKSLERLSLNNCRnltDQSIPAILASNYFPNLSVL 192
F-box_AtSKIP19-like cd22164
F-box domain found in Arabidopsis thaliana SKP1-interacting partner 19 (AtSKIP19) and similar ...
10-55 4.37e-05

F-box domain found in Arabidopsis thaliana SKP1-interacting partner 19 (AtSKIP19) and similar proteins; AtSKIP19, also called F-box protein SKIP19, or F-box/LRR-repeat protein 20 (FBL20), is a component of SCF (SPK1/ASK-cullin-F-box protein) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins. It interacts with CUL1 and SPK1B/ASK2. 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: 438935 [Multi-domain]  Cd Length: 47  Bit Score: 40.28  E-value: 4.37e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 18413178  10 WDELIPDALGLIFSHLPLQEVLTVVPRVCKAWNRAVTGPYCWQEID 55
Cdd:cd22164   2 WLDLPDDLTASILSRLGAIDILTNAQKVCKLWRRICKDPSMWRVID 47
F-box-like pfam12937
F-box-like; This is an F-box-like family.
10-55 2.56e-04

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


Pssm-ID: 463757 [Multi-domain]  Cd Length: 45  Bit Score: 37.85  E-value: 2.56e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 18413178    10 WDELIPDALGLIFSHLPLQEVLTVVpRVCKAWNRAVTGPYCWQEID 55
Cdd:pfam12937   1 LSSLPDEILLQIFSYLDPKDLLRLA-LVCRRWRELASDDSLWRRLC 45
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
67-236 6.76e-04

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 40.80  E-value: 6.76e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413178  67 DHLDRMLEMLIPRsagsLRKLSVT--GLRNDSIFSF--IAQHAGSLKTLKVPRSGLTNSGVVNVAEKL---SSLTFLDLS 139
Cdd:cd00116 126 RLLAKGLKDLPPA----LEKLVLGrnRLEGASCEALakALRANRDLKELNLANNGIGDAGIRALAEGLkanCNLEVLDLN 201
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413178 140 YCCkIGPEAIQAIG---KHCKSLREfcrnmhpLDVASVVSHDDEAYAIANTMP----KLKRLEIAYHRVSTEGVLKILSC 212
Cdd:cd00116 202 NNG-LTDEGASALAetlASLKSLEV-------LNLGDNNLTDAGAAALASALLspniSLLTLSLSCNDITDDGAKDLAEV 273
                       170       180
                ....*....|....*....|....*..
gi 18413178 213 C---VFLEFLELRGcwdvqldNKFFKE 236
Cdd:cd00116 274 LaekESLLELDLRG-------NKFGEE 293
F-box_FBXW5 cd22132
F-box domain found in F-box/WD repeat-containing protein 5 (FBXW5) and similar proteins; FBXW5, ...
12-54 2.90e-03

F-box domain found in F-box/WD repeat-containing protein 5 (FBXW5) and similar proteins; FBXW5, also called F-box and WD-40 domain-containing protein 5, is the substrate-recognition component of both SCF (SKP1-CUL1-F-box protein) and DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes. 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: 438904 [Multi-domain]  Cd Length: 46  Bit Score: 35.28  E-value: 2.90e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 18413178  12 ELIPDALGL-IFSHLPLQEVLTVvPRVCKAWNRAVTGPYCWQEI 54
Cdd:cd22132   2 PLLPDSLLLhIFSYLSPKDLLAA-GQVCKQWYRVSRDEFLWKEL 44
F-box_FBXL1 cd22114
F-box domain found in F-box/LRR-repeat protein 1 (FBXL1) and similar proteins; FBXL1, also ...
10-43 3.07e-03

F-box domain found in F-box/LRR-repeat protein 1 (FBXL1) and similar proteins; FBXL1, also called S-phase kinase-associated protein 2, cyclin-A/CDK2-associated protein p45, F-box protein Skp2, or p45skp2, 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 involved in cell cycle progression, signal transduction and transcription. It specifically recognizes phosphorylated CDKN1B/p27kip and is involved in regulation of G1/S transition. 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: 438886  Cd Length: 41  Bit Score: 35.08  E-value: 3.07e-03
                        10        20        30
                ....*....|....*....|....*....|....*
gi 18413178  10 WDELiPDALGL-IFSHLPLQEVLTvVPRVCKAWNR 43
Cdd:cd22114   1 WDSL-PDELLLgIFSCLCLPDLLK-VSQVCKRWYR 33
F-box_FBXW9 cd22135
F-box domain found in F-box/WD repeat-containing protein 9 (FBXW9) and similar proteins; FBXW9, ...
10-53 6.44e-03

F-box domain found in F-box/WD repeat-containing protein 9 (FBXW9) and similar proteins; FBXW9, also called F-box and WD-40 domain-containing protein 9, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex that mediates 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: 438907  Cd Length: 45  Bit Score: 34.18  E-value: 6.44e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 18413178  10 WDELIPDALGLIFSHLPLQEVLTVVPRVCKAWNRAVTGPYCWQE 53
Cdd:cd22135   1 LLSLPPELLLHICSYLDARFVLHVLPLVCKTFRDILSDETTWRI 44
FBXL3_LRR-like cd23951
Leucine-rich repeat domain of FBXL3 and related proteins; F-box/LRR-repeat proteins are part ...
104-169 7.80e-03

Leucine-rich repeat domain of FBXL3 and related proteins; F-box/LRR-repeat proteins are part of Skp1-Cul1-F-box-protein (SCF) ubiquitin ligase complexes. They contain an F-Box, which binds to the core complex component SKP and a leucine-rich repeat (LRR) domain which gives substrate binding specificity. FBXL3 (F-box and leucine rich repeat protein 3) and FBXL21 have been shown to bind CRY1 repressors and are involved in regulation of circadian clock.


Pssm-ID: 467830 [Multi-domain]  Cd Length: 349  Bit Score: 37.75  E-value: 7.80e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18413178 104 HAGSLKTLKVPRSGLTNSGVVNVAEKLS-SLTFLDLSYCCKIGPEAIQAIGKHCKSLREFCRNMHPL 169
Cdd:cd23951  92 HSSSLSSLAIDDTPVDDPSLQTLASSSSdTLELLKMKSCPRVSPRGILAVADHCQHLRELSLNYHLL 158
F-box pfam00646
F-box domain; This domain is approximately 50 amino acids long, and is usually found in the ...
10-52 8.17e-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: 33.67  E-value: 8.17e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 18413178    10 WDELIPDALGLIFSHLPLQEVLTVVpRVCKAWNRAVTGPYCWQ 52
Cdd:pfam00646   1 LLDLPDDLLLEILSRLDPKDLLRLS-LVSKRWRSLVDSLKLWK 42
PRK05917 PRK05917
DNA polymerase III subunit delta'; Validated
25-83 9.90e-03

DNA polymerase III subunit delta'; Validated


Pssm-ID: 102059 [Multi-domain]  Cd Length: 290  Bit Score: 37.08  E-value: 9.90e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 18413178   25 LPLQEVLTVVPRVCKAWNRAVTGPYCWQEIDIELWSNRFHQSdhldrmleMLIPRSAGS 83
Cdd:PRK05917 240 LPLEKVLSIIERAVQALDNSSSAPSCLEWVALQLWSLKNRQQ--------MLIRNRRGS 290
 
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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