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 1622967090 304 MLQRDFITALPARGLDHIAENILSYLDAKSLCAAELVCKEWYRVTSDGMLWKKLIERMVR 363
Cdd:cd22182     1 MLQRDFITALPARGLDHIAENILSYLDAKSLCAAELVCKEWYRVTSDGMLWKKLIERMVR 60

WD40 repeat [General function prediction only];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967090 423 QRIHCRSETSKGVYCLQY--DDQKIVSGLRDNTIKIWDKNTLECKRILTGHTGSVLCLQY--DERVIITGSSDSTVRVWD 498
Cdd:COG2319   111 LLLRTLTGHTGAVRSVAFspDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFspDGKLLASGSDDGTVRLWD 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967090 499 VNTGEMLNTLIHHCEAVLHLRF--NNGMMVTCSKDRSIAVWDMASPTditLRRVLVGHRAAVNVVDF--DDKYIVSASGD 574
Cdd:COG2319   191 LATGKLLRTLTGHTGAVRSVAFspDGKLLASGSADGTVRLWDLATGK---LLRTLTGHSGSVRSVAFspDGRLLASGSAD 267

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967090 575 RTIKVWNTSTCEFVRTLNGHKRGIACLQYR--DRLVVSGSSDNTIRLWDIECGACLRVLEGHEELVRCIRF--DNKRIVS 650
Cdd:COG2319   268 GTVRLWDLATGELLRTLTGHSGGVNSVAFSpdGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFspDGKTLAS 347

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622967090 651 GAYDGKIKVWDLvaaldprapAGTLCLRTLVEHSGRVFRLQF--DEFQIVSSSHDDTILIWD 710
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 1622967090 268 KYFEQWSESDQVEFVEHLISQMCHYQHGHINSYLKPMLQ 306
Cdd:pfam12125   1 KYFDKWNESDQVDFVEHLLSRMCHYQHGHINSYLKPMLQ 39

protein SPA1-RELATED; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967090 568 IVSASGDRTIKVWNTSTCEFVRTLNGHKRGIACLQYRD---RLVVSGSSDNTIRLWDIECGACLRVLEGHEELVrCIRFD 644
Cdd:PLN00181  548 VASSNFEGVVQVWDVARSQLVTEMKEHEKRVWSIDYSSadpTLLASGSDDGSVKLWSINQGVSIGTIKTKANIC-CVQFP 626

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967090 645 N---KRIVSGAYDGKIKVWDLvaaldpRAPAGTLClrTLVEHSGRVFRLQF-DEFQIVSSSHDDTILIWDFLNDPAAQAE 720
Cdd:PLN00181  627 SesgRSLAFGSADHKVYYYDL------RNPKLPLC--TMIGHSKTVSYVRFvDSSTLVSSSTDNTLKLWDLSMSISGINE 698

                  ..
gi 1622967090 721 PP 722
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 1622967090  461 TLECKRILTGHTGSVLCLQY--DERVIITGSSDSTVRVWD 498
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFspDGKYLASGSDDGTIKLWD 40

WD domain, G-beta repeat;

                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1622967090 625 GACLRVLEGHEELVRCIRF--DNKRIVSGAYDGKIKVWD 661
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFspDGKLLASGSDDGTVKVWD 39

WD40 repeat [General function prediction only];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967090 423 QRIHCRSETSKGVYCLQY--DDQKIVSGLRDNTIKIWDKNTLECKRILTGHTGSVLCLQY--DERVIITGSSDSTVRVWD 498
Cdd:COG2319   111 LLLRTLTGHTGAVRSVAFspDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFspDGKLLASGSDDGTVRLWD 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967090 499 VNTGEMLNTLIHHCEAVLHLRF--NNGMMVTCSKDRSIAVWDMASPTditLRRVLVGHRAAVNVVDF--DDKYIVSASGD 574
Cdd:COG2319   191 LATGKLLRTLTGHTGAVRSVAFspDGKLLASGSADGTVRLWDLATGK---LLRTLTGHSGSVRSVAFspDGRLLASGSAD 267

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967090 575 RTIKVWNTSTCEFVRTLNGHKRGIACLQYR--DRLVVSGSSDNTIRLWDIECGACLRVLEGHEELVRCIRF--DNKRIVS 650
Cdd:COG2319   268 GTVRLWDLATGELLRTLTGHSGGVNSVAFSpdGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFspDGKTLAS 347

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622967090 651 GAYDGKIKVWDLvaaldprapAGTLCLRTLVEHSGRVFRLQF--DEFQIVSSSHDDTILIWD 710
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 1622967090 464 CKRILTGHTGSVLCLQY--DERVIITGSSDSTVRVWDVNTGEMLntlihhceavlhlrfnngmmvtcskdrsiavwdmas 541
Cdd:cd00200     1 LRRTLKGHTGGVTCVAFspDGKLLATGSGDGTIKVWDLETGELL------------------------------------ 44

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967090 542 ptditlrRVLVGHRAAVNVVDF--DDKYIVSASGDRTIKVWNTSTCEFVRTLNGHKRGIACLQYR--DRLVVSGSSDNTI 617
Cdd:cd00200    45 -------RTLKGHTGPVRDVAAsaDGTYLASGSSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSpdGRILSSSSRDKTI 117

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967090 618 RLWDIECGACLRVLEGHEELVRCIRF--DNKRIVSGAYDGKIKVWDLVAALdprapagtlCLRTLVEHSGRVFRLQF--D 693
Cdd:cd00200   118 KVWDVETGKCLTTLRGHTDWVNSVAFspDGTFVASSSQDGTIKLWDLRTGK---------CVATLTGHTGEVNSVAFspD 188

                         250
                  ....*....|....*...
gi 1622967090 694 EFQIVSSSHDDTILIWDF 711
Cdd:cd00200   189 GEKLLSSSSDGTIKLWDL 206

WD40 repeat [General function prediction only];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967090 432 SKGVYCLQY--DDQKIVSGLRDNTIKIWDKNTLECKRILTGHTGSVLCLQY--DERVIITGSSDSTVRVWDVNTGEMLNT 507
Cdd:COG2319   204 TGAVRSVAFspDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFspDGRLLASGSADGTVRLWDLATGELLRT 283

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967090 508 LIHHCEAVLHLRF--NNGMMVTCSKDRSIAVWDMASPTditLRRVLVGHRAAVNVVDF--DDKYIVSASGDRTIKVWNTS 583
Cdd:COG2319   284 LTGHSGGVNSVAFspDGKLLASGSDDGTVRLWDLATGK---LLRTLTGHTGAVRSVAFspDGKTLASGSDDGTVRLWDLA 360

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1622967090 584 TCEFVRTLNGHKRGIACLQY-RD-RLVVSGSSDNTIRLWDIE 623
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 1622967090 304 MLQRDFITALPARGLDHIAENILSYLDAKSLCAAELVCKEWYRVTSDGMLWKKLIERMVR 363
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 1622967090 306 QRDFITALPARGLDHIAENILSYLDAKSLCAAELVCKEWYRVTSDGMLWKK 356
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 1622967090  267 VKYFEQWSESDQVEFVEHLISQMCHYQHGHINSYLKPMLQ 306
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 1622967090 309 FITALPARgldhIAENILSYLDAKSLCAAELVCKEWYRVTSDGMLWKKLI 358
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 1622967090 324 NILSYLDAKSLCAAELVCKEWYRVTSDGMLWKKL 357
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 1622967090  625 GACLRVLEGHEELVRCIRF--DNKRIVSGAYDGKIKVWD 661
Cdd:smart00320   2 GELLKTLKGHTGPVTSVAFspDGKYLASGSDDGTIKLWD 40

WD domain, G-beta repeat;

                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1622967090 625 GACLRVLEGHEELVRCIRF--DNKRIVSGAYDGKIKVWD 661
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFspDGKLLASGSDDGTVKVWD 39

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 1622967090 296 HINSYLKPMLQRDFITALPARgldhIAENILSYLDAKSLCAAELVCKEWYRVTSDGMLWK 355
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 1622967090 319 DHIAENILSYLDAKSLCAAELVCKEWYRVTS 349
Cdd:cd09917     5 DEILLKILSYLDPRDLLRLSLVCKRWRELAS 35

F-box domain found in F-box only protein 41 (FBXO41) and similar proteins; FBXO41, also called FBX41, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. It acts as a novel central nervous system (CNS)-specific F-box protein that localizes to the centrosome and the cytoplasm of neurons and promotes neuronal migration. 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 1622967090 312 ALPARGLDHIaenILSYLDAKSLCAAELVCKEWYRVTSDGMLWKKL 357
Cdd:cd22109     4 SLRRRDALFC---VFSYLDTKSLLRCAEVCREWRDVSRHPALWQRV 46

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 1622967090  584 TCEFVRTLNGHKRGIACLQY--RDRLVVSGSSDNTIRLWD 621
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 1622967090 319 DHIAENILSYLDAKSLCAAELVCKEWYRVTSDGMLWKKL 357
Cdd:cd22091     6 DEVLLKIFSYLLEQDLCRAAQVCKRFNTLANDPELWKRL 44

coronin; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967090 520 FNNGMMVTCSKDRSIAVWDMasPTDITLRRV------LVGHRAAVNVVDFD---DKYIVSASGDRTIKVWNTSTCEFVRT 590
Cdd:PTZ00421   86 FDPQKLFTASEDGTIMGWGI--PEEGLTQNIsdpivhLQGHTKKVGIVSFHpsaMNVLASAGADMVVNVWDVERGKAVEV 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967090 591 LNGHKRGIACLQY--RDRLVVSGSSDNTIRLWDIECGACLRVLEGHE--ELVRCIRFDNKRIV-----SGAYDGKIKVWD 661
Cdd:PTZ00421  164 IKCHSDQITSLEWnlDGSLLCTTSKDKKLNIIDPRDGTIVSSVEAHAsaKSQRCLWAKRKDLIitlgcSKSQQRQIMLWD 243

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1622967090 662 lvaALDPRAPAGTlclrTLVEHSGRVFRLQFDE 694
Cdd:PTZ00421  244 ---TRKMASPYST----VDLDQSSALFIPFFDE 269

WD domain, G-beta repeat;

                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1622967090 546 TLRRVLVGHRAAVNVVDF--DDKYIVSASGDRTIKVWN 581
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 1622967090 325 ILSYLDAKSLCAAELVCKEWYRVTSDGMLWKKL 357
Cdd:cd22093    12 ILSYLDASSLLCISCVNKLFYQLANDNALWRKL 44

F-box domain found in F-box/WD repeat-containing protein 2 (FBXW2) and similar proteins; FBXW2, also called F-box and WD-40 domain-containing protein 2, or protein MD6, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. It acts as a tumor suppressor by promoting SKP2 degradation. 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 1622967090 308 DFITALPARgldhIAENILSYLDAKSLCAAELVCKEWYRVTS 349
Cdd:cd22131     1 DFLKLLPLE----LSFYLLSFLDPESLLTCCLVSKQWNKVIS 38

protein SPA1-RELATED; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967090 474 SVLCLQ-YDERVIITGSSDSTVRVWDVNTGEMLNTLIHHCEAVLHLRFNNG---MMVTCSKDRSIAVWDMASPTDITLrr 549
Cdd:PLN00181  536 SGICWNsYIKSQVASSNFEGVVQVWDVARSQLVTEMKEHEKRVWSIDYSSAdptLLASGSDDGSVKLWSINQGVSIGT-- 613

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622967090 550 vlVGHRAAVNVVDFDD---KYIVSASGDRTIKVWNTSTCEF-VRTLNGHKRGIACLQYRDR-LVVSGSSDNTIRLWDIEC 624
Cdd:PLN00181  614 --IKTKANICCVQFPSesgRSLAFGSADHKVYYYDLRNPKLpLCTMIGHSKTVSYVRFVDSsTLVSSSTDNTLKLWDLSM 691

                  ..
gi 1622967090 625 GA 626
Cdd:PLN00181  692 SI 693

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.

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                  ....*....|....*....|....*....|..
gi 1622967090 319 DHIAENILSYLDAKSLCAAELVCKEWYRVTSD 350
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 1622967090 308 DFITALPARgldhIAENILSYLDAKSLCAAELVCKEWYRVTSDGMLWK 355
Cdd:cd22094     1 DFTRVLPRF----LSLYIFSYLDPRSLCRAAQVSWYWKFLCESDELWL 44

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.

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                  ....*....|....*....|....*....|....
gi 1622967090 324 NILSYLDAKSLCAAELVCKEWYRVTSDGMLWKKL 357
Cdd:cd22087    11 RILSLLDVRSLLSLSQVCRDLNSATNDQLLWRFL 44

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 1622967090  501 TGEMLNTLIHHCEAVLHLRF--NNGMMVTCSKDRSIAVWD 538
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFspDGKYLASGSDDGTIKLWD 40

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 1622967090 325 ILSYLDAKSLCAAELVCKEWYRVTSDGMLWKKL 357
Cdd:cd22137    11 IFSFLDAFSLLQAAQVNKQWNKVADSDYLWRNL 43

F-box domain found in F-box/LRR-repeat protein 5 (FBXL5) and similar proteins; FBXL5, also called F-box and leucine-rich repeat protein 5, F-box protein FBL4/FBL5, or p45SKP2-like protein, is the substrate-recognition component of an SCF (SKP1-cullin-F-box) protein ligase complex that plays a central role in iron homeostasis by promoting the ubiquitination and subsequent degradation of IREB2/IRP2. 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 1622967090 324 NILSYLDAKSLCAAELVCKEWYRVTSDGMLW 354
Cdd:cd22118    11 KIFSYLNPQDLCRCAQVCTKWSQLARDGSLW 41