WD40 repeat [General function prediction only];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16117781 311 WRILAEDNLLWREKCKEEGIDEPLHIKRRKVIKPGFIHSPWKSAYIRQHRIDTNWRRGELKSPKVLKGHDDHVITC-LQF 389
Cdd:COG2319   9 LAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVaFSP 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16117781 390 CGNRIVSGSDDNTLKVWSAVTGKCLRTLVGHTGGVWS---SqmRD-NIIISGSTDRTLKVWNAETGECIHTLYGHTSTVR 465
Cdd:COG2319  89 DGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSvafS--PDgKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVT 166

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16117781 466 CMHLH--EKRVVSGSRDATLRVWDIETGQCLHVLMGHVAAVRCVQY--DGRRVVSGAYDFMVKVWDPETETCLHTLQGHT 541
Cdd:COG2319 167 SVAFSpdGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFspDGKLLASGSADGTVRLWDLATGKLLRTLTGHS 246

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16117781 542 NRVYSLQF--DGIHVVSGSLDTSIRVWDVETGNCIHTLTGHQSLTSGMEL--KDNILVSGNADSTVKIWDIKTGQCLQTL 617
Cdd:COG2319 247 GSVRSVAFspDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFspDGKLLASGSDDGTVRLWDLATGKLLRTL 326

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16117781 618 QGpnkHQSAVTCLQF--NKNFVITSSDDGTVKLWDLKTGEFIRNLvtlesGGSGGVVWRIRASNTKLVCAVGSRNGT 692
Cdd:COG2319 327 TG---HTGAVRSVAFspDGKTLASGSDDGTVRLWDLATGELLRTL-----TGHTGAVTSVAFSPDGRTLASGSADGT 395

WD40 repeat [General function prediction only];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16117781 311 WRILAEDNLLWREKCKEEGIDEPLHIKRRKVIKPGFIHSPWKSAYIRQHRIDTNWRRGELKSPKVLKGHDDHVITC-LQF 389
Cdd:COG2319   9 LAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVaFSP 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16117781 390 CGNRIVSGSDDNTLKVWSAVTGKCLRTLVGHTGGVWS---SqmRD-NIIISGSTDRTLKVWNAETGECIHTLYGHTSTVR 465
Cdd:COG2319  89 DGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSvafS--PDgKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVT 166

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16117781 466 CMHLH--EKRVVSGSRDATLRVWDIETGQCLHVLMGHVAAVRCVQY--DGRRVVSGAYDFMVKVWDPETETCLHTLQGHT 541
Cdd:COG2319 167 SVAFSpdGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFspDGKLLASGSADGTVRLWDLATGKLLRTLTGHS 246

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16117781 542 NRVYSLQF--DGIHVVSGSLDTSIRVWDVETGNCIHTLTGHQSLTSGMEL--KDNILVSGNADSTVKIWDIKTGQCLQTL 617
Cdd:COG2319 247 GSVRSVAFspDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFspDGKLLASGSDDGTVRLWDLATGKLLRTL 326

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16117781 618 QGpnkHQSAVTCLQF--NKNFVITSSDDGTVKLWDLKTGEFIRNLvtlesGGSGGVVWRIRASNTKLVCAVGSRNGT 692
Cdd:COG2319 327 TG---HTGAVRSVAFspDGKTLASGSDDGTVRLWDLATGELLRTL-----TGHTGAVTSVAFSPDGRTLASGSADGT 395

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
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 16117781 264 QVKHMMQVIEPQFQRDFISLLPKELALYVLSFLEPKDLLQAAQTCRYWRILAEDNLLWR 322
Cdd:cd22133   1 QVRHMMQVIEPQFQRDFISLLPKELALYVLSFLEPKDLLQAAQTCRYWRILAEDNLLWR 59

protein SPA1-RELATED; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16117781  392 NRIVSGSDDNTLKVWSAVTGKCLRTLVGHTGGVWS---SQMRDNIIISGSTDRTLKVWNAETGECIHTLyGHTSTVRCMH 468
Cdd:PLN00181 546 SQVASSNFEGVVQVWDVARSQLVTEMKEHEKRVWSidySSADPTLLASGSDDGSVKLWSINQGVSIGTI-KTKANICCVQ 624

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16117781  469 LHE---KRVVSGSRDATLRVWDIETGQC-LHVLMGHVAAVRCVQY-DGRRVVSGAYDFMVKVWDPE------TETCLHTL 537
Cdd:PLN00181 625 FPSesgRSLAFGSADHKVYYYDLRNPKLpLCTMIGHSKTVSYVRFvDSSTLVSSSTDNTLKLWDLSmsisgiNETPLHSF 704

                        170       180
                 ....*....|....*....|....
gi 16117781  538 QGHTNrvySLQFDGIHVVSGSLDT 561
Cdd:PLN00181 705 MGHTN---VKNFVGLSVSDGYIAT 725

WD domain, G-beta repeat;

                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 16117781   532 TCLHTLQGHTNRVYSLQF--DGIHVVSGSLDTSIRVWD 567
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFspDGKLLASGSDDGTVKVWD 39

WD40 repeat [General function prediction only];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16117781 311 WRILAEDNLLWREKCKEEGIDEPLHIKRRKVIKPGFIHSPWKSAYIRQHRIDTNWRRGELKSPKVLKGHDDHVITC-LQF 389
Cdd:COG2319   9 LAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVaFSP 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16117781 390 CGNRIVSGSDDNTLKVWSAVTGKCLRTLVGHTGGVWS---SqmRD-NIIISGSTDRTLKVWNAETGECIHTLYGHTSTVR 465
Cdd:COG2319  89 DGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSvafS--PDgKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVT 166

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16117781 466 CMHLH--EKRVVSGSRDATLRVWDIETGQCLHVLMGHVAAVRCVQY--DGRRVVSGAYDFMVKVWDPETETCLHTLQGHT 541
Cdd:COG2319 167 SVAFSpdGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFspDGKLLASGSADGTVRLWDLATGKLLRTLTGHS 246

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16117781 542 NRVYSLQF--DGIHVVSGSLDTSIRVWDVETGNCIHTLTGHQSLTSGMEL--KDNILVSGNADSTVKIWDIKTGQCLQTL 617
Cdd:COG2319 247 GSVRSVAFspDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFspDGKLLASGSDDGTVRLWDLATGKLLRTL 326

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16117781 618 QGpnkHQSAVTCLQF--NKNFVITSSDDGTVKLWDLKTGEFIRNLvtlesGGSGGVVWRIRASNTKLVCAVGSRNGT 692
Cdd:COG2319 327 TG---HTGAVRSVAFspDGKTLASGSDDGTVRLWDLATGELLRTL-----TGHTGAVTSVAFSPDGRTLASGSADGT 395

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 16117781 374 KVLKGHDDhVITCLQF--CGNRIVSGSDDNTLKVWSAVTGKCLRTLVGHTGGV----WSSQmrDNIIISGSTDRTLKVWN 447
Cdd:cd00200   3 RTLKGHTG-GVTCVAFspDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVrdvaASAD--GTYLASGSSDKTIRLWD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16117781 448 AETGECIHTLYGHTSTVRCMHLHEKR--VVSGSRDATLRVWDIETGQCLHVLMGHVAAVRCVQY--DGRRVVSGAYDFMV 523
Cdd:cd00200  80 LETGECVRTLTGHTSYVSSVAFSPDGriLSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFspDGTFVASSSQDGTI 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16117781 524 KVWDPETETCLHTLQGHTNRVYSLQF--DGIHVVSGSLDTSIRVWDVETGNCIHTLTGHQ-SLTSGMELKDN-ILVSGNA 599
Cdd:cd00200 160 KLWDLRTGKCVATLTGHTGEVNSVAFspDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHEnGVNSVAFSPDGyLLASGSE 239

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 16117781 600 DSTVKIWDIKTGQCLQTLQGpnkHQSAVTCLQF--NKNFVITSSDDGTVKLWD 650
Cdd:cd00200 240 DGTIRVWDLRTGECVQTLSG---HTNSVTSLAWspDGKRLASGSADGTIRIWD 289

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
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 16117781 264 QVKHMMQVIEPQFQRDFISLLPKELALYVLSFLEPKDLLQAAQTCRYWRILAEDNLLWR 322
Cdd:cd22133   1 QVRHMMQVIEPQFQRDFISLLPKELALYVLSFLEPKDLLQAAQTCRYWRILAEDNLLWR 59

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 16117781 280 FISLLPKELALYVLSFLEPKDLLQAAQTCRYWRILAEDNLLWRE 323
Cdd:cd22148   1 FISLLPEHLALKILSYLSPKELLIASQVSKTWRRLASSNELWKA 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 16117781 279 DFISLLPKELALYVLSFLEPKDLLQAAQTCRYWRILAEDNLLWREKC 325
Cdd:cd22094   1 DFTRVLPRFLSLYIFSYLDPRSLCRAAQVSWYWKFLCESDELWLPKC 47

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
                ....*....|....*....|....*....|....*....|....*.
gi 16117781 280 FISLLPKELALYVLSFLEPKDLLQAAQTCRYWRILAEDNLLWREKC 325
Cdd:cd22147   1 FLSALPVELSLKILSYLDAKSLCRAAQVSKKWRNLADDDELWKRMC 46

F-box domain found in F-box only protein 4 (FBXO4) and similar proteins; FBXO4, also called FBX4, is a specific substrate-recognition component of an SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex that catalyzes the ubiquitination and subsequent degradation of cyclin D1 and Trx1. It recognizes TERF1 and promotes its ubiquitination together with UBE2D1. 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 16117781 284 LPKELALYVLSFLEPKDLLQAAQTCRYWRILAEDNLLWR 322
Cdd:cd22085   6 LPIDLQLYILSFLSPHDLCQLGLTSHYWHTLVRDPLLWR 44

F-box domain found in F-box/WD repeat-containing protein 8 (FBXW8) and similar proteins; FBXW8, also called F-box and WD-40 domain-containing protein 8, or F-box only protein 29 (FBXO29), is the substrate-recognition component of a Cul7-RING ubiquitin-protein ligase complex, which mediates the ubiquitination and subsequent proteasomal degradation of target proteins, such as GORASP1, IRS1, MAP4K1/HPK1. 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 16117781 284 LPKELALYVLSFLEPKDLLQAAQTCRYWRILAEDNLLWREKC 325
Cdd:cd22134   7 LPRELALKIFQYLSVTDLCRCAQVSKSWKSLAEDELLWYRIC 48

protein SPA1-RELATED; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16117781  392 NRIVSGSDDNTLKVWSAVTGKCLRTLVGHTGGVWS---SQMRDNIIISGSTDRTLKVWNAETGECIHTLyGHTSTVRCMH 468
Cdd:PLN00181 546 SQVASSNFEGVVQVWDVARSQLVTEMKEHEKRVWSidySSADPTLLASGSDDGSVKLWSINQGVSIGTI-KTKANICCVQ 624

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16117781  469 LHE---KRVVSGSRDATLRVWDIETGQC-LHVLMGHVAAVRCVQY-DGRRVVSGAYDFMVKVWDPE------TETCLHTL 537
Cdd:PLN00181 625 FPSesgRSLAFGSADHKVYYYDLRNPKLpLCTMIGHSKTVSYVRFvDSSTLVSSSTDNTLKLWDLSmsisgiNETPLHSF 704

                        170       180
                 ....*....|....*....|....
gi 16117781  538 QGHTNrvySLQFDGIHVVSGSLDT 561
Cdd:PLN00181 705 MGHTN---VKNFVGLSVSDGYIAT 725

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 16117781 281 ISLLPKELALYVLSFLEPKDLLQAAQTCRYWRILAEDN-LLWREKC 325
Cdd:cd22113   1 IELLPPEMSLRIFSQLDVQSLCRASQTCKTWNDLIENSdYLWRPHC 46

F-box domain found in F-box/LRR-repeat protein 13 (FBXL13) and similar proteins; FBXL13, also called F-box and leucine-rich repeat protein 13, or dynein regulatory complex subunit 6, is a component of the nexin-dynein regulatory complex (N-DRC), a key regulator of ciliary/flagellar motility which maintains the alignment and integrity of the distal axoneme and regulates microtubule sliding in motile axonemes. It is also the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. 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 16117781 281 ISLLPKELALYVLSFLEPKDLLQAAQTCRYWRILAEDNLLW 321
Cdd:cd22124   1 ISLLPRKAALKIFSYLDLRDLARCAQVCRSWKVITQSSSLW 41

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        40
                ....*....|....*....|....*....|....*....|...
gi 16117781 283 LLPKELALYVLSFLEPKDLLQAAQTCRYWRILAEDNLLWREKC 325
Cdd:cd22087   3 ALPPEIKLRILSLLDVRSLLSLSQVCRDLNSATNDQLLWRFLL 45

F-box domain found in F-box/LRR-repeat protein 4 (FBXL4) and similar proteins; FBXL4, also called F-box and leucine-rich repeat protein 4, or F-box protein FBL4/FBL5, is part of an SCF (SKP1-cullin-F-box) protein ligase complex. It serves as a clock output molecule that regulates sleep through promotion of rhythmic degradation of the GABA(A) receptor. Biallelic pathogenic variants in FBXL4 are associated with an encephalopathic mtDNA maintenance defect syndrome that is a multi-system disease characterized by lactic acidemia, developmental delay, and hypotonia. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 16117781 281 ISLLPKELALYVLSFLEPKDLLQAAQTCRYWRILAEDNLLWRE 323
Cdd:cd22117   1 FDLLPYELIQLILSYLDLPSLCRLSQTCKLFRKHCYDPLLWKE 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        40
                ....*....|....*....|....*....|....*....|.
gi 16117781 281 ISLLPKELALYVLSFLEPKDLLQAAQTCRYWRILAEDNLLW 321
Cdd:cd22118   1 ISSLPPEIMLKIFSYLNPQDLCRCAQVCTKWSQLARDGSLW 41

WD domain, G-beta repeat;

                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 16117781   532 TCLHTLQGHTNRVYSLQF--DGIHVVSGSLDTSIRVWD 567
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFspDGKLLASGSDDGTVKVWD 39

F-box domain found in F-box/LRR-repeat protein 2 (FBXL2), F-box/LRR-repeat protein 20 (FBXL20) and similar proteins; The family includes FBXL2 and FBXL30. FBXL2, also called F-box and leucine-rich repeat protein 2, or F-box protein FBL2/FBL3, is a calcium-activated substrate-recognition component of an SCF (SKP1-cullin-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Unlike many F-box proteins, FBXL2 does not seem to target phosphodegron within its substrates but rather calmodulin-binding motifs and is thereby antagonized by calmodulin. FBXL20, also called SCRAPPER, F-box and leucine-rich repeat protein 20, or F-box/LRR-repeat protein 2-like, is a component of a synapse-localized SCF-type E3 ubiquitin ligase which regulates neural transmission. It is widely expressed in the central nervous system and plays an important role in the ubiquitin-dependent degradation of regulating synaptic membrane exocytosis 1 (RIM1), which is an important factor in the release of synaptic vesicles. It may also mediate the ubiquitin degradation of E-cadherin resulting in an increased invasive ability of malignant cells. 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 16117781 284 LPKELALYVLSFLEPKDLLQAAQTCRYWRILAEDNLLWR 322
Cdd:cd22115   7 LPKELLLRIFSFLDVVTLCRCAQVSKYWNVLALDGSNWQ 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 16117781    450 TGECIHTLYGHTSTVRCMHLH--EKRVVSGSRDATLRVWD 487
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSpdGKYLASGSDDGTIKLWD 40

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 16117781 281 ISLLPKELALYVLSFLEPKDLLQAAQTCRYWRILAEDNLLWR 322
Cdd:cd22123   1 LDQLPENVLLEILSYLPVRDLLRISRVCKRWRRLVYDKTLWR 42

WD domain, G-beta repeat;

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 16117781   611 GQCLQTLQGpnkHQSAVTCLQFNKN--FVITSSDDGTVKLWD 650
Cdd:pfam00400   1 GKLLKTLEG---HTGSVTSLAFSPDgkLLASGSDDGTVKVWD 39

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
                ....*....|....*....|....*....|...
gi 16117781 279 DFISLLPKELALYVLSFLEPKDLLQAAQTCRYW 311
Cdd:cd22131   1 DFLKLLPLELSFYLLSFLDPESLLTCCLVSKQW 33

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 16117781 277 QRDFISLLPKE----LALYVLSFLEPKDLLQAAQTCRYWRILAEDNLLWRE 323
Cdd:cd22130   1 QRDFISALPAKgldhIAENILSYLDAKSLCAAELVCKEWYRVIADGMLWKK 51

A Receptor for Ubiquitination Targets;

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 16117781    284 LPKELALYVLSFLEPKDLLQAAQTCRYWRILAEDNLLWREK 324
Cdd:smart00256   1 LPDEILEEILSKLDPKDLLRLRKVSRKWRSLIDSHDFWFKL 41

F-box domain found in F-box only protein 17 (FBXO17), F-box only protein 27 (FBXO27) and similar proteins; This subfamily includes FBXO17 and FBXO27. FBXO17 is also called FBX17, F-box only protein 26 (FBX26/FBXO26), or FBG4, while FBXO27 is also called FBX27, or F-box/G-domain protein 5. FBXO17 and FBXO27 are the substrate-recognition components of SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complexes. They can recognize and bind denatured glycoproteins, which are modified with complex-type oligosaccharides. FBXO17 also recognizes sulfated glycans but does not bind high-mannose glycoproteins. 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 16117781 281 ISLLPKELALYVLSFLEPKDLLQAA-QTCRYWRILAEDNLLWREKC 325
Cdd:cd22169   1 LSLLPEELLLLVLSHVPARTLVTRCrLVCRDWRDLVDGPTLWKLKC 46

F-box domain found in F-box only protein 31 (FBXO31) and similar proteins; FBXO31, also called FBX31, or FBXO14, is a component of an SCF (SKP1-cullin-F-box) protein ligase complex that plays a central role in G1 arrest following DNA damage. It specifically recognizes phosphorylated cyclin-D1 (CCND1), promoting its ubiquitination and degradation by the proteasome, resulting in G1 arrest. FBXO31 may act as a tumor 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        40
                ....*....|....*....|....*....|....*....|....*
gi 16117781 284 LPKELALYVLSFLEPKDLLQAAQTCRYWRILAEDNLLWREKCKEE 328
Cdd:cd22102   4 LPPELLVEIFSSLPGTDLPSLAQVCKKFREILNTDTIWQRRCKEE 48

F-box domain found in Arabidopsis thaliana SKP1-interacting partner 22 (AtSKIP22) and similar proteins; AtSKIP22, also called F-box protein SKIP22, is a component of SCF (SKP1/ASK-cullin-F-box protein) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins. It interacts with SKP1A/ASK1 and SPK1B/ASK2. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 16117781 283 LLPKELALYVLSFLEPKDLLQAAQTCRYWRILAEDNLLWREKC 325
Cdd:cd22165   4 RLPTELKLKILELLPGVDLARMACVCSELRFLASNDDLWKQKF 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 16117781    410 TGKCLRTLVGHTGGVWSSQM--RDNIIISGSTDRTLKVWN 447
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 16117781 284 LPKELALYVLSFLEPKDLLQAAQTCRYWRILAEDNLLWR 322
Cdd:cd22091   4 LPDEVLLKIFSYLLEQDLCRAAQVCKRFNTLANDPELWK 42