F-box domain found in F-box/WD repeat-containing protein 1A (FBXW1A) and similar proteins; FBXW1A, also called E3RSIkappaB, epididymis tissue protein Li 2a, F-box and WD repeats protein beta-TrCP, or pIkappaBalpha-E3 receptor subunit, 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, such as CTNNB1, NFKBIA, NFKBIB and NFKBIE, as well as phosphorylated NFKB1, ATF4, CDC25A, DLG1, FBXO5, PER1, SMAD3, SMAD4, SNAI1 and probably NFKB2. 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.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819981 302 MLQRDFITALPARGLDHIAENILSYLDAKSLCAAELVCKEWYRVTSDGMLWKKLIERMVR 361
Cdd:cd22182    1 MLQRDFITALPARGLDHIAENILSYLDAKSLCAAELVCKEWYRVTSDGMLWKKLIERMVR 60

WD40 repeat [General function prediction only];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819981 421 QRIHCRSETSKGVYCLQY--DDQKIVSGLRDNTIKIWDKNTLECKRILTGHTGSVLCLQY--DERVIITGSSDSTVRVWD 496
Cdd:COG2319  111 LLLRTLTGHTGAVRSVAFspDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFspDGKLLASGSDDGTVRLWD 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819981 497 VNTGEMLNTLIHHCEAVLHLRF--NNGMMVTCSKDRSIAVWDMASPTditLRRVLVGHRAAVNVVDF--DDKYIVSASGD 572
Cdd:COG2319  191 LATGKLLRTLTGHTGAVRSVAFspDGKLLASGSADGTVRLWDLATGK---LLRTLTGHSGSVRSVAFspDGRLLASGSAD 267

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819981 573 RTIKVWNTSTCEFVRTLNGHKRGIACLQYR--DRLVVSGSSDNTIRLWDIECGACLRVLEGHEELVRCIRF--DNKRIVS 648
Cdd:COG2319  268 GTVRLWDLATGELLRTLTGHSGGVNSVAFSpdGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFspDGKTLAS 347

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578819981 649 GAYDGKIKVWDLvaaldprapAGTLCLRTLVEHSGRVFRLQF--DEFQIVSSSHDDTILIWD 708
Cdd:COG2319  348 GSDDGTVRLWDL---------ATGELLRTLTGHTGAVTSVAFspDGRTLASGSADGTVRLWD 400

D domain of beta-TrCP; This domain is found in eukaryotes, and is approximately 40 amino acids in length. It is found associated with pfam00646, pfam00400. The protein that contains this domain functions as a ubiquitin ligase. Ubiquitination is required to direct proteins towards the proteasome for degradation. This protein is part of the WD40 class of F box proteins. The D domain of these F box proteins is involved in mediating the dimerization of the protein. dimerization is necessary to polyubiquitinate substrates so this D domain is vital in directing substrates towards the proteasome for degradation.

                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 578819981  266 KYFEQWSESDQVEFVEHLISQMCHYQHGHINSYLKPMLQ 304
Cdd:pfam12125   1 KYFDKWNESDQVDFVEHLLSRMCHYQHGHINSYLKPMLQ 39

protein SPA1-RELATED; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819981 566 IVSASGDRTIKVWNTSTCEFVRTLNGHKRGIACLQYRD---RLVVSGSSDNTIRLWDIECGACLRVLEGHEELVrCIRFD 642
Cdd:PLN00181 548 VASSNFEGVVQVWDVARSQLVTEMKEHEKRVWSIDYSSadpTLLASGSDDGSVKLWSINQGVSIGTIKTKANIC-CVQFP 626

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819981 643 N---KRIVSGAYDGKIKVWDLvaaldpRAPAGTLClrTLVEHSGRVFRLQF-DEFQIVSSSHDDTILIWDFLNDPAAQAE 718
Cdd:PLN00181 627 SesgRSLAFGSADHKVYYYDL------RNPKLPLC--TMIGHSKTVSYVRFvDSSTLVSSSTDNTLKLWDLSMSISGINE 698

                 ..
gi 578819981 719 PP 720
Cdd:PLN00181 699 TP 700

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 578819981   459 TLECKRILTGHTGSVLCLQY--DERVIITGSSDSTVRVWD 496
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFspDGKYLASGSDDGTIKLWD 40

A Receptor for Ubiquitination Targets;

                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 578819981   317 DHIAENILSYLDAKSLCAAELVCKEWYRVTSDGMLWKKL 355
Cdd:smart00256   3 DEILEEILSKLDPKDLLRLRKVSRKWRSLIDSHDFWFKL 41

WD40 repeat [General function prediction only];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819981 421 QRIHCRSETSKGVYCLQY--DDQKIVSGLRDNTIKIWDKNTLECKRILTGHTGSVLCLQY--DERVIITGSSDSTVRVWD 496
Cdd:COG2319  111 LLLRTLTGHTGAVRSVAFspDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFspDGKLLASGSDDGTVRLWD 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819981 497 VNTGEMLNTLIHHCEAVLHLRF--NNGMMVTCSKDRSIAVWDMASPTditLRRVLVGHRAAVNVVDF--DDKYIVSASGD 572
Cdd:COG2319  191 LATGKLLRTLTGHTGAVRSVAFspDGKLLASGSADGTVRLWDLATGK---LLRTLTGHSGSVRSVAFspDGRLLASGSAD 267

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819981 573 RTIKVWNTSTCEFVRTLNGHKRGIACLQYR--DRLVVSGSSDNTIRLWDIECGACLRVLEGHEELVRCIRF--DNKRIVS 648
Cdd:COG2319  268 GTVRLWDLATGELLRTLTGHSGGVNSVAFSpdGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFspDGKTLAS 347

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578819981 649 GAYDGKIKVWDLvaaldprapAGTLCLRTLVEHSGRVFRLQF--DEFQIVSSSHDDTILIWD 708
Cdd:COG2319  348 GSDDGTVRLWDL---------ATGELLRTLTGHTGAVTSVAFspDGRTLASGSADGTVRLWD 400

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819981 462 CKRILTGHTGSVLCLQY--DERVIITGSSDSTVRVWDVNTGEMLntlihhceavlhlrfnngmmvtcskdrsiavwdmas 539
Cdd:cd00200    1 LRRTLKGHTGGVTCVAFspDGKLLATGSGDGTIKVWDLETGELL------------------------------------ 44

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819981 540 ptditlrRVLVGHRAAVNVVDF--DDKYIVSASGDRTIKVWNTSTCEFVRTLNGHKRGIACLQYR--DRLVVSGSSDNTI 615
Cdd:cd00200   45 -------RTLKGHTGPVRDVAAsaDGTYLASGSSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSpdGRILSSSSRDKTI 117

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819981 616 RLWDIECGACLRVLEGHEELVRCIRF--DNKRIVSGAYDGKIKVWDLVAALdprapagtlCLRTLVEHSGRVFRLQF--D 691
Cdd:cd00200  118 KVWDVETGKCLTTLRGHTDWVNSVAFspDGTFVASSSQDGTIKLWDLRTGK---------CVATLTGHTGEVNSVAFspD 188

                        250
                 ....*....|....*...
gi 578819981 692 EFQIVSSSHDDTILIWDF 709
Cdd:cd00200  189 GEKLLSSSSDGTIKLWDL 206

WD40 repeat [General function prediction only];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819981 430 SKGVYCLQY--DDQKIVSGLRDNTIKIWDKNTLECKRILTGHTGSVLCLQY--DERVIITGSSDSTVRVWDVNTGEMLNT 505
Cdd:COG2319  204 TGAVRSVAFspDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFspDGRLLASGSADGTVRLWDLATGELLRT 283

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819981 506 LIHHCEAVLHLRF--NNGMMVTCSKDRSIAVWDMASPTditLRRVLVGHRAAVNVVDF--DDKYIVSASGDRTIKVWNTS 581
Cdd:COG2319  284 LTGHSGGVNSVAFspDGKLLASGSDDGTVRLWDLATGK---LLRTLTGHTGAVRSVAFspDGKTLASGSDDGTVRLWDLA 360

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 578819981 582 TCEFVRTLNGHKRGIACLQYR--DRLVVSGSSDNTIRLWDIE 621
Cdd:COG2319  361 TGELLRTLTGHTGAVTSVAFSpdGRTLASGSADGTVRLWDLA 402

F-box domain found in F-box/WD repeat-containing protein 1A (FBXW1A) and similar proteins; FBXW1A, also called E3RSIkappaB, epididymis tissue protein Li 2a, F-box and WD repeats protein beta-TrCP, or pIkappaBalpha-E3 receptor subunit, 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, such as CTNNB1, NFKBIA, NFKBIB and NFKBIE, as well as phosphorylated NFKB1, ATF4, CDC25A, DLG1, FBXO5, PER1, SMAD3, SMAD4, SNAI1 and probably NFKB2. 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.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819981 302 MLQRDFITALPARGLDHIAENILSYLDAKSLCAAELVCKEWYRVTSDGMLWKKLIERMVR 361
Cdd:cd22182    1 MLQRDFITALPARGLDHIAENILSYLDAKSLCAAELVCKEWYRVTSDGMLWKKLIERMVR 60

F-box domain found in F-box/WD repeat-containing protein 1B (FBXW1B) and similar proteins; FBXW1B, also called F-box/WD repeat-containing protein 11 (FBXW11), F-box and WD repeats protein beta-TrCP2, or homologous to Slimb protein (HOS), 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, such as IFNAR1, CEP68 and CDC25A, as well as phosphorylated CTNNB1, NFKBIA, PER1 and PER2. 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.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 578819981 304 QRDFITALPARGLDHIAENILSYLDAKSLCAAELVCKEWYRVTSDGMLWKK 354
Cdd:cd22183    1 QRDFITALPAKGLDHIAENILSYLDAESLCAAELVCKEWQRVISEGMLWKK 51

D domain of beta-TrCP; This domain is found in eukaryotes, and is approximately 40 amino acids in length. It is found associated with F-box domain, WD domain. The protein that contains this domain functions as a ubiquitin ligase. Ubiquitination is required to direct proteins towards the proteasome for degradation. This protein is part of the WD40 class of F box proteins. The D domain of these F box proteins is involved in mediating the dimerisation of the protein. Dimerisation is necessary to polyubiquitinate substrates so this D domain is vital in directing substrates towards the proteasome for degradation.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 578819981   265 VKYFEQWSESDQVEFVEHLISQMCHYQHGHINSYLKPMLQ 304
Cdd:smart01028   1 VKYFEKWSESDQVDFVEHLISRMCHYQHGHINSYLKPMLQ 40

F-box domain found in Schizosaccharomyces pombe Skp1-binding protein 1 (SpPof1) and similar proteins; SpPof1, also called F-box/WD repeat-containing protein pof1, probably recognizes and binds to some phosphorylated proteins and promotes their ubiquitination and degradation. It is required for the inactivation of zip1 via ubiquitination. This subfamily also includes Saccharomyces cerevisiae methionine-requiring protein 30 (ScMET30, also called E3 ubiquitin ligase complex SCF(Met30) subunit MET30), Aspergillus niger sulfur controller B (AnSCONB, also called sulfur metabolite repression control protein B) and Neurospora crassa sulfur controller 2 (NcSCON2, also called sulfur metabolite repression control protein 2). ScMET30 acts as a transcriptional inhibitor that negatively regulates the expression of sulfur amino acid biosynthesis genes. It controls cell cycle function (being required for the G1/S transition and M-phase but not the S-phase), sulfur metabolism, and methionine biosynthesis as part of the E3 ubiquitin ligase complex SCF(Met30). AnSCONB and NcSCON2 are components of the SCF (sconB/scon-2) E3 ubiquitin ligase complexes involved in the regulation of sulfur metabolite repression, probably by mediating the inactivation or degradation of the metR transcription factor. 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.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 578819981 307 FITALPARgldhIAENILSYLDAKSLCAAELVCKEWYRVTSDGMLWKKLI 356
Cdd:cd22147    1 FLSALPVE----LSLKILSYLDAKSLCRAAQVSKKWRNLADDDELWKRMC 46

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.

                         10        20        30
                 ....*....|....*....|....*....|....
gi 578819981 322 NILSYLDAKSLCAAELVCKEWYRVTSDGMLWKKL 355
Cdd:cd22132   11 HIFSYLSPKDLLAAGQVCKQWYRVSRDEFLWKEL 44

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.

                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 578819981   623 GACLRVLEGHEELVRCIRF--DNKRIVSGAYDGKIKVWD 659
Cdd:smart00320   2 GELLKTLKGHTGPVTSVAFspDGKYLASGSDDGTIKLWD 40

A Receptor for Ubiquitination Targets;

                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 578819981   317 DHIAENILSYLDAKSLCAAELVCKEWYRVTSDGMLWKKL 355
Cdd:smart00256   3 DEILEEILSKLDPKDLLRLRKVSRKWRSLIDSHDFWFKL 41

F-box domain found in F-box/WD repeat-containing protein 7 (FBXW7) and similar proteins; FBXW7, also called Archipelago homolog (Ago), F-box and WD-40 domain-containing protein 7, F-box protein FBX30, SEL-10, or Cdc4, 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, such as cyclin-E (CCNE1 or CCNE2), DISC1, JUN, MYC, NOTCH1 released notch intracellular domain (NICD), NOTCH2, MCL1, and probably PSEN1. 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.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819981 294 HINSYLKPMLQRDFITALPARgldhIAENILSYLDAKSLCAAELVCKEWYRVTSDGMLWK 353
Cdd:cd22133    4 HMMQVIEPQFQRDFISLLPKE----LALYVLSFLEPKDLLQAAQTCRYWRILAEDNLLWR 59

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.

                         10        20        30
                 ....*....|....*....|....*....|.
gi 578819981 317 DHIAENILSYLDAKSLCAAELVCKEWYRVTS 347
Cdd:cd09917    5 DEILLKILSYLDPRDLLRLSLVCKRWRELAS 35

F-box domain found in F-box only protein 48 (FBXO48) and similar proteins; FBXO48, also called FBX48, is one of the paralogs of the F-box only protein 7 (FBXO7), which is the causative gene for PARK15 (also known as Parkinsonian-pyramidal disease, PPD). 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.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 578819981 308 ITALPARgldhIAENILSYLDAKSLCAAELVCKEWYRVTSD-GMLWKKL 355
Cdd:cd22113    1 IELLPPE----MSLRIFSQLDVQSLCRASQTCKTWNDLIENsDYLWRPH 45

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 578819981   582 TCEFVRTLNGHKRGIACLQY--RDRLVVSGSSDNTIRLWD 619
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFspDGKYLASGSDDGTIKLWD 40

F-box domain found in F-box only protein 11 (FBXO11) and similar proteins; FBXO11, also called FBX11, protein arginine N-methyltransferase 9 (PRMT9), or vitiligo-associated protein 1 (VIT-1), 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, such as DTL/CDT2, BCL6 and PRDM1/BLIMP1. 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.

                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 578819981 317 DHIAENILSYLDAKSLCAAELVCKEWYRVTSDGMLWKKL 355
Cdd:cd22091    6 DEVLLKIFSYLLEQDLCRAAQVCKRFNTLANDPELWKRL 44

coronin; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819981 518 FNNGMMVTCSKDRSIAVWDMasPTDITLRRV------LVGHRAAVNVVDFD---DKYIVSASGDRTIKVWNTSTCEFVRT 588
Cdd:PTZ00421  86 FDPQKLFTASEDGTIMGWGI--PEEGLTQNIsdpivhLQGHTKKVGIVSFHpsaMNVLASAGADMVVNVWDVERGKAVEV 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819981 589 LNGHKRGIACLQY--RDRLVVSGSSDNTIRLWDIECGACLRVLEGHE--ELVRCIRFDNKRIV-----SGAYDGKIKVWD 659
Cdd:PTZ00421 164 IKCHSDQITSLEWnlDGSLLCTTSKDKKLNIIDPRDGTIVSSVEAHAsaKSQRCLWAKRKDLIitlgcSKSQQRQIMLWD 243

                        170       180       190
                 ....*....|....*....|....*....|...
gi 578819981 660 lvaALDPRAPAGTlclrTLVEHSGRVFRLQFDE 692
Cdd:PTZ00421 244 ---TRKMASPYST----VDLDQSSALFIPFFDE 269

WD domain, G-beta repeat;

                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 578819981  544 TLRRVLVGHRAAVNVVDF--DDKYIVSASGDRTIKVWN 579
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFspDGKLLASGSDDGTVKVWD 39

F-box domain found in F-box only protein 15 (FBXO15) and similar proteins; FBXO15, also called FBX15, has a novel dual molecular function by controlling transcriptional repression and being part of SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligases, which is essential for stress response, gliotoxin production and virulence in the opportunistic human pathogen Aspergillus fumigatus. 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.

                         10        20        30
                 ....*....|....*....|....*....|...
gi 578819981 323 ILSYLDAKSLCAAELVCKEWYRVTSDGMLWKKL 355
Cdd:cd22093   12 ILSYLDASSLLCISCVNKLFYQLANDNALWRKL 44

F-box domain found in epithelial cell-transforming sequence 2 oncogene-like (ECT2L) and similar proteins; ECT2L, also called lung-specific F-box and DH domain-containing protein, or putative guanine nucleotide exchange factor LFDH, may act as a guanine nucleotide exchange factor (GEF). 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.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578819981 306 DFITALPArgldHIAENILSYLDAKSLCAAELVCkeWYrvtsdgmlWKKLIERmvrtDSLWRGLAERRGW 375
Cdd:cd22173    1 DFTTVLPR----FLSLYIFSFLDPRSLCRAAQVS--WH--------WKFLAEQ----DCLWMPKCVKFGW 52

F-box domain found in uncharacterized F-box protein group similar to F-box only protein 3 (FBXO3); This subfamily corresponds to a group of uncharacterized F-box proteins which show sequence similarity to F-box only protein 3 (FBXO3). FBXO3, also called FBX3, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex, that mediates the ubiquitination of HIPK2 and probably that of EP300, leading to rapid degradation by the proteasome. It also promotes ubiquitylation and transcriptional activity of AIRE (autoimmune regulator). 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.

                         10        20        30
                 ....*....|....*....|....*....|...
gi 578819981 323 ILSYLDAKSLCAAELVCKEWYRVTSDGMLWKKL 355
Cdd:cd22139   12 IFSFLSPKDLCQVALVCRRFNRLASDESLWKQI 44

F-box domain found in Arabidopsis thaliana F-box/WD-40 repeat-containing protein 1 (AtFBW1) and similar proteins; AtFBW1, also called WD-40-associated F-box protein 1, is an F-box protein that contains four WD-40 repeats, which are separated from each other by a spacer region. Like other F-box proteins, AtFBW1 may be a component of SCF (Skp1 Cdc53 F-box protein) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins. This subfamily also contains many F-box only proteins that do not have any WD repeat. 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.

                         10        20        30
                 ....*....|....*....|....*....|..
gi 578819981 317 DHIAENILSYLDAKSLCAAELVCKEWYRVTSD 348
Cdd:cd22157    5 DDLVEEILSRLPAKSLLRFRCVCKQWNSLISS 36

F-box domain found in F-box only protein 16 (FBXO16), epithelial cell-transforming sequence 2 oncogene-like (ECT2L) and similar proteins; This family includes FBXO16 and ECT2L. FBXO16, also called FBX16, is part of an SCF (SKP1-cullin-F-box) protein ligase complex. It probably recognizes and binds to some phosphorylated proteins and promotes their ubiquitination and degradation. It functions as a tumor suppressor by attenuating nuclear beta-catenin function. ECT2L, also called lung-specific F-box and DH domain-containing protein, or putative guanine nucleotide exchange factor LFDH, may act as a guanine nucleotide exchange factor (GEF). 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.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 578819981 306 DFITALPARgldhIAENILSYLDAKSLCAAELVCKEWYRVTSDGMLWK 353
Cdd:cd22094    1 DFTRVLPRF----LSLYIFSYLDPRSLCRAAQVSWYWKFLCESDELWL 44

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.

                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 578819981   674 CLRTLVEHSGRVFRLQF--DEFQIVSSSHDDTILIWD 708
Cdd:smart00320   4 LLKTLKGHTGPVTSVAFspDGKYLASGSDDGTIKLWD 40

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.

                         10        20        30
                 ....*....|....*....|....*....|....
gi 578819981 322 NILSYLDAKSLCAAELVCKEWYRVTSDGMLWKKL 355
Cdd:cd22087   11 RILSLLDVRSLLSLSQVCRDLNSATNDQLLWRFL 44

F-box domain found in F-box/WD repeat-containing protein 12 (FBXW12) and similar proteins; FBXW12, also called F-box and WD-40 domain-containing protein 12, or F-box only protein 35 (FBXO35), is the substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins. It functions as an epithelial growth suppressor. 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.

                         10        20        30
                 ....*....|....*....|....*....|...
gi 578819981 323 ILSYLDAKSLCAAELVCKEWYRVTSDGMLWKKL 355
Cdd:cd22137   11 IFSFLDAFSLLQAAQVNKQWNKVADSDYLWRNL 43

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.

                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 578819981 317 DHIAENILSYLDAKSLCAAELVCKEWYRVTSDGMLW 352
Cdd:cd22151    5 DDLLQEIFKRLDPKSLARAACVCRRWRAAARSESLW 40