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 1938881363 406 SKGVYCLQYDD--QKIVSGLRDNTIKIWDKNTLECKRILTGHTGSVLCLQY--DERVIITGSSDSTVRVWDVNTGEMLNT 481
Cdd:cd00200     9 TGGVTCVAFSPdgKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAAsaDGTYLASGSSDKTIRLWDLETGECVRT 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938881363 482 LIHHCEAVLHLRF--NNGMMVTCSKDRSIAVWDMASPtdiTLRRVLVGHRAAVNVVDF--DDKYIVSASGDRTIKVWNTS 557
Cdd:cd00200    89 LTGHTSYVSSVAFspDGRILSSSSRDKTIKVWDVETG---KCLTTLRGHTDWVNSVAFspDGTFVASSSQDGTIKLWDLR 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938881363 558 TCEFVRTLNGHKRGIACLQYRD--RLVVSGSSDNTIRLWDIECGACLRVLEGHEELVRCIRFDNKR--IVSGAYDGKIKV 633
Cdd:cd00200   166 TGKCVATLTGHTGEVNSVAFSPdgEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGylLASGSEDGTIRV 245

                  ...
gi 1938881363 634 WDL 636
Cdd:cd00200   246 WDL 248

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 1938881363 242 KYFEQWSESDQVEFVEHLISQMCHYQHGHINSYLKPMLQ 280
Cdd:pfam12125   1 KYFDKWNESDQVDFVEHLLSRMCHYQHGHINSYLKPMLQ 39

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 1938881363 406 SKGVYCLQYDD--QKIVSGLRDNTIKIWDKNTLECKRILTGHTGSVLCLQY--DERVIITGSSDSTVRVWDVNTGEMLNT 481
Cdd:cd00200     9 TGGVTCVAFSPdgKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAAsaDGTYLASGSSDKTIRLWDLETGECVRT 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938881363 482 LIHHCEAVLHLRF--NNGMMVTCSKDRSIAVWDMASPtdiTLRRVLVGHRAAVNVVDF--DDKYIVSASGDRTIKVWNTS 557
Cdd:cd00200    89 LTGHTSYVSSVAFspDGRILSSSSRDKTIKVWDVETG---KCLTTLRGHTDWVNSVAFspDGTFVASSSQDGTIKLWDLR 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938881363 558 TCEFVRTLNGHKRGIACLQYRD--RLVVSGSSDNTIRLWDIECGACLRVLEGHEELVRCIRFDNKR--IVSGAYDGKIKV 633
Cdd:cd00200   166 TGKCVATLTGHTGEVNSVAFSPdgEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGylLASGSEDGTIRV 245

                  ...
gi 1938881363 634 WDL 636
Cdd:cd00200   246 WDL 248

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 1938881363 278 MLQRDFITALPARGLDHIAENILSYLDAKSLCAAELVCKEWYRVTSDGMLWKKLIERMVR 337
Cdd:cd22182     1 MLQRDFITALPARGLDHIAENILSYLDAKSLCAAELVCKEWYRVTSDGMLWKKLIERMVR 60

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 1938881363  241 VKYFEQWSESDQVEFVEHLISQMCHYQHGHINSYLKPMLQ 280
Cdd:smart01028   1 VKYFEKWSESDQVDFVEHLISRMCHYQHGHINSYLKPMLQ 40

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 1938881363  435 TLECKRILTGHTGSVLCLQY--DERVIITGSSDSTVRVWD 472
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFspDGKYLASGSDDGTIKLWD 40

WD domain, G-beta repeat;

                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1938881363 599 GACLRVLEGHEELVRCIRF--DNKRIVSGAYDGKIKVWD 635
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFspDGKLLASGSDDGTVKVWD 39

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 1938881363 406 SKGVYCLQYDD--QKIVSGLRDNTIKIWDKNTLECKRILTGHTGSVLCLQY--DERVIITGSSDSTVRVWDVNTGEMLNT 481
Cdd:cd00200     9 TGGVTCVAFSPdgKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAAsaDGTYLASGSSDKTIRLWDLETGECVRT 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938881363 482 LIHHCEAVLHLRF--NNGMMVTCSKDRSIAVWDMASPtdiTLRRVLVGHRAAVNVVDF--DDKYIVSASGDRTIKVWNTS 557
Cdd:cd00200    89 LTGHTSYVSSVAFspDGRILSSSSRDKTIKVWDVETG---KCLTTLRGHTDWVNSVAFspDGTFVASSSQDGTIKLWDLR 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938881363 558 TCEFVRTLNGHKRGIACLQYRD--RLVVSGSSDNTIRLWDIECGACLRVLEGHEELVRCIRFDNKR--IVSGAYDGKIKV 633
Cdd:cd00200   166 TGKCVATLTGHTGEVNSVAFSPdgEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGylLASGSEDGTIRV 245

                  ...
gi 1938881363 634 WDL 636
Cdd:cd00200   246 WDL 248

WD40 repeat [General function prediction only];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938881363 397 QRIHCRSETSKGVYCLQY--DDQKIVSGLRDNTIKIWDKNTLECKRILTGHTGSVLCLQY--DERVIITGSSDSTVRVWD 472
Cdd:COG2319   111 LLLRTLTGHTGAVRSVAFspDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFspDGKLLASGSDDGTVRLWD 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938881363 473 VNTGEMLNTLIHHCEAVLHLRF--NNGMMVTCSKDRSIAVWDMASPTditLRRVLVGHRAAVNVVDF--DDKYIVSASGD 548
Cdd:COG2319   191 LATGKLLRTLTGHTGAVRSVAFspDGKLLASGSADGTVRLWDLATGK---LLRTLTGHSGSVRSVAFspDGRLLASGSAD 267

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938881363 549 RTIKVWNTSTCEFVRTLNGHKRGIACLQYR--DRLVVSGSSDNTIRLWDIECGACLRVLEGHEELVRCIRF--DNKRIVS 624
Cdd:COG2319   268 GTVRLWDLATGELLRTLTGHSGGVNSVAFSpdGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFspDGKTLAS 347

                         250       260       270
                  ....*....|....*....|....*....|
gi 1938881363 625 GAYDGKIKVWDLvaaldprapAGTLCLRTL 654
Cdd:COG2319   348 GSDDGTVRLWDL---------ATGELLRTL 368

WD40 repeat [General function prediction only];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938881363 406 SKGVYCLQY--DDQKIVSGLRDNTIKIWDKNTLECKRILTGHTGSVLCLQY--DERVIITGSSDSTVRVWDVNTGEMLNT 481
Cdd:COG2319   204 TGAVRSVAFspDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFspDGRLLASGSADGTVRLWDLATGELLRT 283

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938881363 482 LIHHCEAVLHLRF--NNGMMVTCSKDRSIAVWDMASPTditLRRVLVGHRAAVNVVDF--DDKYIVSASGDRTIKVWNTS 557
Cdd:COG2319   284 LTGHSGGVNSVAFspDGKLLASGSDDGTVRLWDLATGK---LLRTLTGHTGAVRSVAFspDGKTLASGSDDGTVRLWDLA 360

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1938881363 558 TCEFVRTLNGHKRGIACLQY-RD-RLVVSGSSDNTIRLWDIE 597
Cdd:COG2319   361 TGELLRTLTGHTGAVTSVAFsPDgRTLASGSADGTVRLWDLA 402

WD40 repeat [General function prediction only];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938881363 397 QRIHCRSETSKGVYCLQY--DDQKIVSGLRDNTIKIWDKNTLECKRILTGHTGSVLCLQY--DERVIITGSSDSTVRVWD 472
Cdd:COG2319   237 KLLRTLTGHSGSVRSVAFspDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFspDGKLLASGSDDGTVRLWD 316

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938881363 473 VNTGEMLNTLIHHCEAVLHLRF--NNGMMVTCSKDRSIAVWDMASPTditLRRVLVGHRAAVNVVDF--DDKYIVSASGD 548
Cdd:COG2319   317 LATGKLLRTLTGHTGAVRSVAFspDGKTLASGSDDGTVRLWDLATGE---LLRTLTGHTGAVTSVAFspDGRTLASGSAD 393

                         170
                  ....*....|
gi 1938881363 549 RTIKVWNTST 558
Cdd:COG2319   394 GTVRLWDLAT 403

F-box domain found in F-box/WD repeat-containing proteins, FBXW1A, FBXW1B 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. 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 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 1938881363 280 QRDFITALPARGLDHIAENILSYLDAKSLCAAELVCKEWYRVTSDGMLWKK 330
Cdd:cd22130     1 QRDFISALPAKGLDHIAENILSYLDAKSLCAAELVCKEWYRVIADGMLWKK 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 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 1938881363 242 KYFEQWSESDQVEFVEHLISQMCHYQHGHINSYLKPMLQ 280
Cdd:pfam12125   1 KYFDKWNESDQVDFVEHLLSRMCHYQHGHINSYLKPMLQ 39

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 1938881363 283 FITALPARgldhIAENILSYLDAKSLCAAELVCKEWYRVTSDGMLWKKLI 332
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 1938881363 298 NILSYLDAKSLCAAELVCKEWYRVTSDGMLWKKL 331
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 1938881363  599 GACLRVLEGHEELVRCIRF--DNKRIVSGAYDGKIKVWD 635
Cdd:smart00320   2 GELLKTLKGHTGPVTSVAFspDGKYLASGSDDGTIKLWD 40

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 1938881363 270 HINSYLKPMLQRDFITALPARgldhIAENILSYLDAKSLCAAELVCKEWYRVTSDGMLWK 329
Cdd:cd22133     4 HMMQVIEPQFQRDFISLLPKE----LALYVLSFLEPKDLLQAAQTCRYWRILAEDNLLWR 59

WD domain, G-beta repeat;

                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1938881363 437 ECKRILTGHTGSVLCLQY--DERVIITGSSDSTVRVWD 472
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFspDGKLLASGSDDGTVKVWD 39

F-box domain found in Dictyostelium discoideum Rho GTPase-activating protein gacFF (DdgacFF) and similar proteins; DdgacFF, also called GTPase activating factor for raC protein FF, is a Rho GTPase-activating protein involved in the signal transduction 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        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1938881363 283 FITALParglDHIAENILSYLDAKSLCAAELVCKEWYRVTSDGMLWK 329
Cdd:cd22148     1 FISLLP----EHLALKILSYLSPKELLIASQVSKTWRRLASSNELWK 43

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 1938881363 286 ALPARGLDHIaenILSYLDAKSLCAAELVCKEWYRVTSDGMLWKKL 331
Cdd:cd22109     4 SLRRRDALFC---VFSYLDTKSLLRCAEVCREWRDVSRHPALWQRV 46

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 1938881363 284 ITALPARgldhIAENILSYLDAKSLCAAELVCKEWYRVTSD-GMLWKKL 331
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 1938881363  558 TCEFVRTLNGHKRGIACLQY--RDRLVVSGSSDNTIRLWD 595
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFspDGKYLASGSDDGTIKLWD 40

coronin; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938881363 414 YDDQKIVSGLRDNTIKIWD-------KNTLECKRILTGHTGSVLCLQYD---ERVIITGSSDSTVRVWDVNTGEMLNTLI 483
Cdd:PTZ00421   86 FDPQKLFTASEDGTIMGWGipeegltQNISDPIVHLQGHTKKVGIVSFHpsaMNVLASAGADMVVNVWDVERGKAVEVIK 165

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1938881363 484 HHCEAVLHLRFN--NGMMVTCSKDRSIAVWD 512
Cdd:PTZ00421  166 CHSDQITSLEWNldGSLLCTTSKDKKLNIID 196

DNA-binding beta-propeller fold protein YncE [General function prediction only];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938881363 505 DRSIAVWDMASPTDITLRRVLVGHRAAVNVVDFDDKYI-VSASGDRTIKVWNTSTCEFVRTLN--GHKRGIACLQYRDRL 581
Cdd:COG3391    45 VGAAVGGGGVALLAGLGLGAAAVADADGADAGADGRRLyVANSGSGRVSVIDLATGKVVATIPvgGGPRGLAVDPDGGRL 124

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1938881363 582 VVSGSSDNTIRLWDIECGACLRVLEGHEElVRCIRF--DNKRI-VSGAYDGKIKVwdLVAALDPRA 644
Cdd:COG3391   125 YVADSGNGRVSVIDTATGKVVATIPVGAG-PHGIAVdpDGKRLyVANSGSNTVSV--IVSVIDTAT 187

WD domain, G-beta repeat;

                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1938881363 520 TLRRVLVGHRAAVNVVDF--DDKYIVSASGDRTIKVWN 555
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFspDGKLLASGSDDGTVKVWD 39

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 1938881363 282 DFITALPArgldHIAENILSYLDAKSLCAAELVCkeWYrvtsdgmlWKKLIERmvrtDSLWRGLAERRGW 351
Cdd:cd22173     1 DFTTVLPR----FLSLYIFSFLDPRSLCRAAQVS--WH--------WKFLAEQ----DCLWMPKCVKFGW 52

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 1938881363 282 DFITALPARgldhIAENILSYLDAKSLCAAELVCKEWYRVTS 323
Cdd:cd22131     1 DFLKLLPLE----LSFYLLSFLDPESLLTCCLVSKQWNKVIS 38

protein SPA1-RELATED; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938881363 542 IVSASGDRTIKVWNTSTCEFVRTLNGHKRGIACLQYRD---RLVVSGSSDNTIRLWDIECGACLRVLEGHEELVrCIRFD 618
Cdd:PLN00181  548 VASSNFEGVVQVWDVARSQLVTEMKEHEKRVWSIDYSSadpTLLASGSDDGSVKLWSINQGVSIGTIKTKANIC-CVQFP 626

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1938881363 619 N---KRIVSGAYDGKIKVWDLvaaLDPRAPAGTL 649
Cdd:PLN00181  627 SesgRSLAFGSADHKVYYYDL---RNPKLPLCTM 657

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 1938881363 299 ILSYLDAKSLCAAELVCKEWYRVTSDGMLWKKL 331
Cdd:cd22139    12 IFSFLSPKDLCQVALVCRRFNRLASDESLWKQI 44

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 1938881363 282 DFITALPARgldhIAENILSYLDAKSLCAAELVCKEWYRVTSDGMLWK 329
Cdd:cd22094     1 DFTRVLPRF----LSLYIFSYLDPRSLCRAAQVSWYWKFLCESDELWL 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 1938881363 299 ILSYLDAKSLCAAELVCKEWYRVTSDGMLWKKL 331
Cdd:cd22137    11 IFSFLDAFSLLQAAQVNKQWNKVADSDYLWRNL 43

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 1938881363  475 TGEMLNTLIHHCEAVLHLRF--NNGMMVTCSKDRSIAVWD 512
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFspDGKYLASGSDDGTIKLWD 40

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 1938881363 293 DHIAENILSYLDAKSLCAAELVCKEWYRVTSDGMLW 328
Cdd:cd22151     5 DDLLQEIFKRLDPKSLARAACVCRRWRAAARSESLW 40

F-box domain found in the early mitotic inhibitor (EMI) family of F-box proteins; The EMI family includes FBX5 (EMI1) and FBX43 (EMI2), which are anaphase-promoting complex/cyclosome (APC/C) inhibitors that bind APC/C-CCD20 (Cell division cycle protein 20) and/or APC/C-CDH1 (CDC20 homologue 1) 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
                  ....*....|....*....|....*....
gi 1938881363 290 RGLDHIAENILSYLDAKSLCAAELVCKEW 318
Cdd:cd22086     6 RNCPHILSKILSYLSPEDLCRVSCVSKTW 34

F-box domain found in F-box/LRR-repeat protein 12 (FBXL12) and similar proteins; FBXL12, also called F-box and leucine-rich repeat protein 12, or F-box protein FBL12, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. It mediates the polyubiquitination and proteasomal degradation of calcium/calmodulin dependent protein kinase I (CAMK1) leading to disruption of cyclin D1/CDK4 complex assembly, which results in G1 cell cycle arrest in lung epithelia. It regulates T-cell differentiation in a cell-autonomous manner. 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 1938881363 284 ITALParglDHIAENILSYLDAKSLCAAELVCKEWYRVTSDGMLWK 329
Cdd:cd22123     1 LDQLP----ENVLLEILSYLPVRDLLRISRVCKRWRRLVYDKTLWR 42

F-box domain found in F-box/LRR-repeat protein 7 (FBXL7) and similar proteins; FBXL7, also called F-box and leucine-rich repeat protein 7, or F-box protein FBL6/FBL7, 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 Aurora kinase A (AURKA) during mitosis, causing mitotic arrest. 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 1938881363 293 DHIAENILSYLDAKSLCAAELVCKEWYRVTSDGMLWKKL 331
Cdd:cd22120     6 DDVILQIFSHLPTNQLCRCARVCRRWYNLAWDPRLWTTI 44