WD40 repeat [General function prediction only];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579067 110 LRTNWKNRKGAVSELEHVPDTVLCDVHSHDGVVIA-GYTSGDVRVWDTRTWDYVAPFLESEDEedepgmqpnVSFVRI-- 186
Cdd:COG2319    60 LLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLAsASADGTVRLWDLATGLLLRTLTGHTGA---------VRSVAFsp 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579067 187 NSSLAVAAYEDGFLNIWDLRTGKyPVHRFE-HDARIQALALSQDDATVATASAFDVVMLspneegyWQIAAEFEVPKL-- 263
Cdd:COG2319   131 DGKTLASGSADGTVRLWDLATGK-LLRTLTgHSGAVTSVAFSPDGKLLASGSDDGTVRL-------WDLATGKLLRTLtg 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579067 264 ----VQYLEIVPETRRypVAVAAAGDLMYLLKAED-SARTLLYAHGPPVTCLDVSAN--QVAFGvqglgwvYEGSKILVY 336
Cdd:COG2319   203 htgaVRSVAFSPDGKL--LASGSADGTVRLWDLATgKLLRTLTGHSGSVRSVAFSPDgrLLASG-------SADGTVRLW 273

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579067 337 SLEAGRRLLKLGNVLRDFTCVNLS-DSppNLMVSGNMDGRVRIHDLRSGNIALSLSAHQLRVSAVQM--DDWKIVSGGEE 413
Cdd:COG2319   274 DLATGELLRTLTGHSGGVNSVAFSpDG--KLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFspDGKTLASGSDD 351

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1034579067 414 GLVSVWDYRmNQKLWEVYSGH--PVQHISFSSHS--LITA 449
Cdd:COG2319   352 GTVRLWDLA-TGELLRTLTGHtgAVTSVAFSPDGrtLASG 390

WD40 repeat [General function prediction only];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579067 110 LRTNWKNRKGAVSELEHVPDTVLCDVHSHDGVVIA-GYTSGDVRVWDTRTWDYVAPFLESEDEedepgmqpnVSFVRI-- 186
Cdd:COG2319    60 LLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLAsASADGTVRLWDLATGLLLRTLTGHTGA---------VRSVAFsp 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579067 187 NSSLAVAAYEDGFLNIWDLRTGKyPVHRFE-HDARIQALALSQDDATVATASAFDVVMLspneegyWQIAAEFEVPKL-- 263
Cdd:COG2319   131 DGKTLASGSADGTVRLWDLATGK-LLRTLTgHSGAVTSVAFSPDGKLLASGSDDGTVRL-------WDLATGKLLRTLtg 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579067 264 ----VQYLEIVPETRRypVAVAAAGDLMYLLKAED-SARTLLYAHGPPVTCLDVSAN--QVAFGvqglgwvYEGSKILVY 336
Cdd:COG2319   203 htgaVRSVAFSPDGKL--LASGSADGTVRLWDLATgKLLRTLTGHSGSVRSVAFSPDgrLLASG-------SADGTVRLW 273

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579067 337 SLEAGRRLLKLGNVLRDFTCVNLS-DSppNLMVSGNMDGRVRIHDLRSGNIALSLSAHQLRVSAVQM--DDWKIVSGGEE 413
Cdd:COG2319   274 DLATGELLRTLTGHSGGVNSVAFSpDG--KLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFspDGKTLASGSDD 351

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1034579067 414 GLVSVWDYRmNQKLWEVYSGH--PVQHISFSSHS--LITA 449
Cdd:COG2319   352 GTVRLWDLA-TGELLRTLTGHtgAVTSVAFSPDGrtLASG 390

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

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1034579067  37 QLPYELAINIFQYLDRKELGRCAQVSKTWKVIAEDEVLWYRLC 79
Cdd:pfam12937   3 SLPDEILLQIFSYLDPKDLLRLALVCRRWRELASDDSLWRRLC 45

WD40 repeat [General function prediction only];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579067 110 LRTNWKNRKGAVSELEHVPDTVLCDVHSHDGVVIA-GYTSGDVRVWDTRTWDYVAPFLESEDEedepgmqpnVSFVRI-- 186
Cdd:COG2319    60 LLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLAsASADGTVRLWDLATGLLLRTLTGHTGA---------VRSVAFsp 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579067 187 NSSLAVAAYEDGFLNIWDLRTGKyPVHRFE-HDARIQALALSQDDATVATASAFDVVMLspneegyWQIAAEFEVPKL-- 263
Cdd:COG2319   131 DGKTLASGSADGTVRLWDLATGK-LLRTLTgHSGAVTSVAFSPDGKLLASGSDDGTVRL-------WDLATGKLLRTLtg 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579067 264 ----VQYLEIVPETRRypVAVAAAGDLMYLLKAED-SARTLLYAHGPPVTCLDVSAN--QVAFGvqglgwvYEGSKILVY 336
Cdd:COG2319   203 htgaVRSVAFSPDGKL--LASGSADGTVRLWDLATgKLLRTLTGHSGSVRSVAFSPDgrLLASG-------SADGTVRLW 273

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579067 337 SLEAGRRLLKLGNVLRDFTCVNLS-DSppNLMVSGNMDGRVRIHDLRSGNIALSLSAHQLRVSAVQM--DDWKIVSGGEE 413
Cdd:COG2319   274 DLATGELLRTLTGHSGGVNSVAFSpDG--KLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFspDGKTLASGSDD 351

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1034579067 414 GLVSVWDYRmNQKLWEVYSGH--PVQHISFSSHS--LITA 449
Cdd:COG2319   352 GTVRLWDLA-TGELLRTLTGHtgAVTSVAFSPDGrtLASG 390

WD40 repeat [General function prediction only];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579067 137 SHDGVVIA-GYTSGDVRVWDTRTWDYVAPFlesedeedePGMQPNVSFVRI--NSSLAVAAYEDGFLNIWDLRTGKyPVH 213
Cdd:COG2319   129 SPDGKTLAsGSADGTVRLWDLATGKLLRTL---------TGHSGAVTSVAFspDGKLLASGSDDGTVRLWDLATGK-LLR 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579067 214 RFE-HDARIQALALSQDDATVATASAFDVVMLspneegyWQIAAEFEVPKL------VQYLEIVPETRRypVAVAAAGDL 286
Cdd:COG2319   199 TLTgHTGAVRSVAFSPDGKLLASGSADGTVRL-------WDLATGKLLRTLtghsgsVRSVAFSPDGRL--LASGSADGT 269

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579067 287 MYLLKAED-SARTLLYAHGPPVTCLDVSAN--QVAFGvqglgwvYEGSKILVYSLEAGRRLLKLGNVLRDFTCVNLSdsp 363
Cdd:COG2319   270 VRLWDLATgELLRTLTGHSGGVNSVAFSPDgkLLASG-------SDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFS--- 339

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034579067 364 PN--LMVSGNMDGRVRIHDLRSGNIALSLSAHQLRVSAVqmdDW-----KIVSGGEEGLVSVWD 420
Cdd:COG2319   340 PDgkTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSV---AFspdgrTLASGSADGTVRLWD 400

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

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1034579067  37 QLPYELAINIFQYLDRKELGRCAQVSKTWKVIAEDEVLWYRLC 79
Cdd:pfam12937   3 SLPDEILLQIFSYLDPKDLLRLALVCRRWRELASDDSLWRRLC 45

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 1034579067  37 QLPYELAINIFQYLDRKELGRCAQVSKTWKVIAEDEVLWYRLC 79
Cdd:cd22147     4 ALPVELSLKILSYLDAKSLCRAAQVSKKWRNLADDDELWKRMC 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
                  ....*....|....*....|....*....|....*....
gi 1034579067  37 QLPYELAINIFQYLDRKELGRCAQVSKTWKVIAEDEVLW 75
Cdd:cd22124     3 LLPRKAALKIFSYLDLRDLARCAQVCRSWKVITQSSSLW 41

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 1034579067  37 QLPYELAINIFQYLDRKELGRCAQVSKTWKVIAEDEVLW 75
Cdd:cd22115     6 KLPKELLLRIFSFLDVVTLCRCAQVSKYWNVLALDGSNW 44

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        40
                  ....*....|....*....|....*....|....*....|...
gi 1034579067  37 QLPYELAINIFQYLDRKELGRCAQVSKTWKVIAEDEVLWYRLC 79
Cdd:cd22151     2 KLPDDLLQEIFKRLDPKSLARAACVCRRWRAAARSESLWENAC 44

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 1034579067 355 TCVNLSDSPpNLMVSGNMDGRVRIHDLRSGNIALSLSAHQLRVSAVQMDDW--KIVSGGEEGLVSVWDYRMNQKLWEvYS 432
Cdd:cd00200    13 TCVAFSPDG-KLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADgtYLASGSSDKTIRLWDLETGECVRT-LT 90

                          90
                  ....*....|....*..
gi 1034579067 433 GH--PVQHISFSSHSLI 447
Cdd:cd00200    91 GHtsYVSSVAFSPDGRI 107

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 1034579067  37 QLPYELAINIFQYLDRKELGRCAQVSKTWKVIAEDEVLW 75
Cdd:cd22118     3 SLPPEIMLKIFSYLNPQDLCRCAQVCTKWSQLARDGSLW 41

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
                  ....*....|....*....|....*....|....*...
gi 1034579067  38 LPYELAINIFQYLDRKELGRCAQVSKTWKVIAEDEVLW 75
Cdd:cd22148     5 LPEHLALKILSYLSPKELLIASQVSKTWRRLASSNELW 42

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 1034579067  37 QLPYELAINIFQYLDRKELGRCAQVSKTWKVIAE 70
Cdd:cd09917     2 DLPDEILLKILSYLDPRDLLRLSLVCKRWRELAS 35

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        40
                  ....*....|....*....|....*....|....*....|..
gi 1034579067  37 QLPYELAINIFQYLDRKELGRCAQVSKTWKVIAEDEVLWYRL 78
Cdd:cd22091     3 ELPDEVLLKIFSYLLEQDLCRAAQVCKRFNTLANDPELWKRL 44

F-box domain found in F-box only protein 16 (FBXO16) and similar proteins; 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. 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 1034579067  34 FDIQLPYELAINIFQYLDRKELGRCAQVSKTWKVIAEDEVLWYRLC 79
Cdd:cd22172     5 FTRVLPRVLSLYIFSFLDPRSLCRCAQVCWYWKYLTELDQLWMPKC 50

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        40
                  ....*....|....*....|....*....|....*....|.
gi 1034579067  38 LPYELAINIFQYLDRKELGRCAQVSKTWKVIAEDEVLWYRL 78
Cdd:cd22132     4 LPDSLLLHIFSYLSPKDLLAAGQVCKQWYRVSRDEFLWKEL 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
                  ....*....|....*....|....*....|...
gi 1034579067  37 QLPYELAINIFQYLDRKELGRCAQVSKTW-KVI 68
Cdd:cd22131     5 LLPLELSFYLLSFLDPESLLTCCLVSKQWnKVI 37

F-box domain found in F-box only protein 10 (FBXO10) and similar proteins; FBXO10, also called FBX10, or PRMT11, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. The SCF(FBXO10) complex mediates ubiquitination and degradation of BCL2, an anti-apoptotic protein, thereby playing a role in apoptosis by controlling the stability of BCL2. It also associates with the receptor for advanced glycation end products (RAGE) to mediate its ubiquitination and 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 1034579067  38 LPYELAINIFQYLDRKELGRCAQVSKTWK--VIAEDEVLWYRLC 79
Cdd:cd22090     5 LPLELWRLILAYLPVRDLCRCCQVCRAWYelILSLDSTRWKQLY 48

F-box domain found in the JmjC domain-containing histone demethylation protein (JHDM) family; The JHDM family includes F-box/LRR-repeat proteins FBXL10, FBXL11 and FBXL19. FBXL10 is also called lysine-specific demethylase 2B (KDM2B), CXXC-type zinc finger protein 2 (CXXC2), F-box and leucine-rich repeat protein 10 (FBL10), JmjC domain-containing histone demethylation protein 1B (JHDM1B), Jumonji domain-containing EMSY-interactor methyltransferase motif protein, protein JEMMA, protein-containing CXXC domain 2, [Histone-H3]-lysine-36 demethylase 1B, or NDY1. It is a histone demethylase that catalyzes the demethylation of H3K4me3 and H3K36me2, thereby playing a central role in the histone code. It preferentially binds the transcribed region of ribosomal RNA and represses the transcription of ribosomal RNA genes which inhibits cell growth and proliferation. FBXL10 may also serve as the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. FBXL11, also called KDM2A, CXXC8, F-box and leucine-rich repeat protein 11, F-box protein FBL7, F-box protein Lilina, JmjC domain-containing histone demethylation protein 1A (JHDM1A), or [Histone-H3]-lysine-36 demethylase 1A, is a histone H3 lysine 36 (H3K36) demethylase that regulates epithelial mesenchymal transition (EMT) and the metastasis of ovarian cancer. It plays an essential role in embryonic development and homeostasis by regulating cell proliferation and survival. FBXL11 may also recognize and bind to some phosphorylated proteins and promote their ubiquitination and degradation. It associates with centromeres and represses transcription of small non-coding RNAs that are encoded by the clusters of satellite repeats at the centromere. It is required to sustain centromeric integrity and genomic stability, particularly during mitosis. FBXL19, also called F-box and leucine-rich repeat protein 19, is the substrate-recognition component of an SCF-type E3 ubiquitin ligase complex. It acts as a CpG island-binding protein in mouse embryonic stem (ES) cells and has been shown to associate with the CDK-Mediator complex. It promotes H2Bub1 at the promoters of CpG island-containing genes by interacting with RNF20. 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 1034579067  38 LPYELAINIFQYLDRKELGRCAQVSKTWKVIAEDEVLW 75
Cdd:cd22122     4 LPREVWLPVFQYLSPKDLCVCMRVCKTWNRWCCDPSLW 41

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 1034579067  34 FDIqLPYELAINIFQYLDRKELGRCAQVSKTWKVIAEDEVLWYRL 78
Cdd:cd22117     1 FDL-LPYELIQLILSYLDLPSLCRLSQTCKLFRKHCYDPLLWKEL 44

F-box domain found in F-box/WD repeat-containing protein 10 (FBXW10) and similar proteins; FBXW10, also called F-box and WD-40 domain-containing protein 10, or ubiquitin ligase-specificity factor, is a probable substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Its overexpression leads to degradation of CBX5 and CBX1. FBXW10 is negatively regulated in transcription and expression levels by protein O-GlcNAcylation. 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 1034579067  37 QLPYELAINIFQYLDRKELGRCAQVSKTWKVIAEdEVL 74
Cdd:cd22136     4 CLPVHLSKYILSMLDKKSLNNCLCVSQHWRALTE-EVK 40

F-box domain found in F-box only protein 8 (FBXO8) and similar proteins; FBXO8, also called FBX8, or F-box/SEC7 protein FBS, is a novel component of F-box proteins which contains an F-box domain and a putative Sec7 domain. FBX8 was originally identified as a Skp1-binding protein. It is involved in the ubiquitin-dependent proteolytic pathway. It acts as a metastasis suppressor that functions through mTOR signaling pathway. FBXO8 may promote the activation of ADP-ribosylation factor (ARF) through replacement of GDP with GTP. 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 1034579067  33 FFDI-QLPYELAINIFQYLDRKELGRCAQVsktWKVIAEDEVLWYRLC 79
Cdd:cd22088     1 FPDLeELPPELSLTVLSHLNATDLCLASCV---WQDLANDELLWQGLC 45

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
                  ....*....|....*....|....*....|....*....
gi 1034579067  37 QLPYELAINIFQYLDRKELGRCAQVSKTWKVIAEDEVLW 75
Cdd:cd22123     3 QLPENVLLEILSYLPVRDLLRISRVCKRWRRLVYDKTLW 41

F-box domain found in F-box only protein 32 (FBXO32) and similar proteins; FBXO32, also called FBX32, atrogin-1, or muscle atrophy F-box protein (MAFbx), 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 during skeletal muscle atrophy. 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 1034579067  38 LPYELAINIFQYL-DRKELGRCAQVSKTWKVIAEDEVLWYRLC 79
Cdd:cd22103     6 LPLCLQLNIMQRLsDGRDIVSLGQVSPDLQVLSEDRLLWKKLC 48

F-box domain found in uncharacterized F-box protein group similar to F-box only protein 13 (FBXO13); The family corresponds to a group of uncharacterized F-box proteins which show sequence similarity to F-box only protein 13 (FBXO13). FBXO13, also called FBX13, or F-box/LRR-repeat protein 17 (FBL17), or F-box and leucine-rich repeat protein 17 (FBXL17), is the substrate-recognition component of the SCF(FBXL17) E3 ubiquitin ligase complex, a key component of a quality control pathway required to ensure functional dimerization of BTB domain-containing proteins (dimerization quality control, DQC). 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 1034579067  37 QLPYELAINIFQYLDRKELGRCAQVSKTWKVIAEDEVLW 75
Cdd:cd22138     3 SLPVECQLKIFSFLSEVDKCLAATVCRSWSELIRSPRLW 41

F-box domain found in Arabidopsis thaliana SKP1-interacting partner 31 (AtSKIP31) and similar proteins; AtSKIP31, also called F-box protein SKIP31, is a component of SCF(ASK-cullin-F-box) 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 1034579067  38 LPYELAINIFQYLDRKELGRCAQVSKTWKVIAEDEVLWYRL 78
Cdd:cd22166     4 LPPELFRHILKFLSPEDLTSCATVCRFLRGAASDESLWRRL 44

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
                  ....*....|....*....|....*....|....
gi 1034579067  42 LAINIFQYLDRKELGRCAQVSKTWKVIAEDEVLW 75
Cdd:cd22130    16 IAENILSYLDAKSLCAAELVCKEWYRVIADGMLW 49

F-box domain found in F-box only protein 45 (FBXO45) and similar proteins; FBXO45, also called FBX45, or F-box/SPRY domain-containing protein 1, functions as the substrate-recognition component of E3 ubiquitin ligase complexes. It is critical for synaptogenesis, neuronal migration, and synaptic transmission. 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 1034579067  37 QLPYELAINIFQYLDRKELGRCAQVSKTW 65
Cdd:cd22111     3 RLPSRVLEVIFSYLDLPDLRNCSLVCKSW 31