F-box domain found in F-box/WD repeat-containing protein 4 (FBXW4) and similar proteins; FBXW4, also called dactylin, or F-box and WD-40 domain-containing protein 4, probably recognizes and binds to some phosphorylated proteins and promotes their ubiquitination and degradation. It is likely to be involved in key signaling pathways crucial for normal limb development. It may participate in Wnt signaling and act as a novel tumor suppressor that regulates important cellular processes. 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 755563313 165 LWRLPEELLLLICSYLDTRALGRLAQVCRWLRRFTSCDLLWRPIAR 210
Cdd:cd20090    2 LLDLPDDLLFLIFSYLDPASLGRLSQVCRRLYRLISRDAVWRRIAR 47

F-box domain found in F-box/WD repeat-containing protein 4 (FBXW4) and similar proteins; FBXW4, also called dactylin, or F-box and WD-40 domain-containing protein 4, probably recognizes and binds to some phosphorylated proteins and promotes their ubiquitination and degradation. It is likely to be involved in key signaling pathways crucial for normal limb development. It may participate in Wnt signaling and act as a novel tumor suppressor that regulates important cellular processes. 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 755563313 165 LWRLPEELLLLICSYLDTRALGRLAQVCRWLRRFTSCDLLWRPIAR 210
Cdd:cd20090    2 LLDLPDDLLFLIFSYLDPASLGRLSQVCRRLYRLISRDAVWRRIAR 47

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

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 755563313  165 LWRLPEELLLLICSYLDTRALGRLAQVCRWLRRFTSCDLLWR 206
Cdd:pfam12937   1 LSSLPDEILLQIFSYLDPKDLLRLALVCRRWRELASDDSLWR 42

A Receptor for Ubiquitination Targets;

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 755563313   168 LPEELLLLICSYLDTRALGRLAQVCRWLRR-FTSCDLLWR 206
Cdd:smart00256   1 LPDEILEEILSKLDPKDLLRLRKVSRKWRSlIDSHDFWFK 40

F-box domain found in F-box/WD repeat-containing protein 4 (FBXW4) and similar proteins; FBXW4, also called dactylin, or F-box and WD-40 domain-containing protein 4, probably recognizes and binds to some phosphorylated proteins and promotes their ubiquitination and degradation. It is likely to be involved in key signaling pathways crucial for normal limb development. It may participate in Wnt signaling and act as a novel tumor suppressor that regulates important cellular processes. 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 755563313 165 LWRLPEELLLLICSYLDTRALGRLAQVCRWLRRFTSCDLLWRPIAR 210
Cdd:cd20090    2 LLDLPDDLLFLIFSYLDPASLGRLSQVCRRLYRLISRDAVWRRIAR 47

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 755563313 294 RVFSGHDEDV--CHFVLANSHIVSAGGDGKIGVHKIHSTFTVK-YSAHEQEVNCVDC--KGGIIVSGSRDRTAKVWPLAS 368
Cdd:cd00200    3 RTLKGHTGGVtcVAFSPDGKLLATGSGDGTIKVWDLETGELLRtLKGHTGPVRDVAAsaDGTYLASGSSDKTIRLWDLET 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563313 369 grlGQCLHTIQT-EDRVWSIAISP----LLSSFVTGTaccghfspLRIWDLNSGQLIT----HLGSdfppgagVLDVMYE 439
Cdd:cd00200   83 ---GECVRTLTGhTSYVSSVAFSPdgriLSSSSRDKT--------IKVWDVETGKCLTtlrgHTDW-------VNSVAFS 144

                        170       180
                 ....*....|....*....|..
gi 755563313 440 SPSTLLSCG-YDTYVRYWDLRT 460
Cdd:cd00200  145 PDGTFVASSsQDGTIKLWDLRT 166

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 755563313 291 RPFRVFSGHDEDV--CHFVLANSHIVSAGGDGKIGVHKIHSTFTVK-YSAHEQEVNCV--DCKGGIIVSGSRDRTAKVWP 365
Cdd:cd00200  168 KCVATLTGHTGEVnsVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGtLRGHENGVNSVafSPDGYLLASGSEDGTIRVWD 247

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 755563313 366 LASgrlGQCLHTIQ-TEDRVWSIAISPLLSSFVTGTACCGhfspLRIWD 413
Cdd:cd00200  248 LRT---GECVQTLSgHTNSVTSLAWSPDGKRLASGSADGT----IRIWD 289

WD40 repeat [General function prediction only];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563313 286 ASLNRRPFRVFSGHDEDV--CHFVLANSHIVSAGGDGKIGVHKIHSTFTVK-YSAHEQEVNCV----DckGGIIVSGSRD 358
Cdd:COG2319   64 DAAAGALLATLLGHTAAVlsVAFSPDGRLLASASADGTVRLWDLATGLLLRtLTGHTGAVRSVafspD--GKTLASGSAD 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563313 359 RTAKVWPLASGRlgqCLHTIQT-EDRVWSIAISP----LLSSFVTGTaccghfspLRIWDLNSGQLITHLGSdfpPGAGV 433
Cdd:COG2319  142 GTVRLWDLATGK---LLRTLTGhSGAVTSVAFSPdgklLASGSDDGT--------VRLWDLATGKLLRTLTG---HTGAV 207

                        170       180
                 ....*....|....*....|....*....
gi 755563313 434 LDVMYeSP--STLLSCGYDTYVRYWDLRT 460
Cdd:COG2319  208 RSVAF-SPdgKLLASGSADGTVRLWDLAT 235

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 755563313 338 HEQEVNCVDC--KGGIIVSGSRDRTAKVWPLASGRL--GQCLHTIQtedrVWSIAISPLLSSFvtgtACCGHFSPLRIWD 413
Cdd:cd00200    8 HTGGVTCVAFspDGKLLATGSGDGTIKVWDLETGELlrTLKGHTGP----VRDVAASADGTYL----ASGSSDKTIRLWD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563313 414 LNSGQLITHLGSDFppgAGVLDVMYeSPST--LLSCGYDTYVRYWDLRTSTRQTA-------TTCWPQAPPTTVSCGCGT 484
Cdd:cd00200   80 LETGECVRTLTGHT---SYVSSVAF-SPDGriLSSSSRDKTIKVWDVETGKCLTTlrghtdwVNSVAFSPDGTFVASSSQ 155

                 .
gi 755563313 485 D 485
Cdd:cd00200  156 D 156

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 755563313 167 RLPEELLLLICSYLDTRALGRLAQVCRWLRRFTS 200
Cdd:cd09917    2 DLPDEILLKILSYLDPRDLLRLSLVCKRWRELAS 35

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
                 ....*....|....*....|....*....|....*....
gi 755563313 168 LPEELLLLICSYLDTRALGRLAQVCRWLRRFTSCDLLWR 206
Cdd:cd22117    4 LPYELIQLILSYLDLPSLCRLSQTCKLFRKHCYDPLLWK 42

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        40
                 ....*....|....*....|....*....|....*....|.
gi 755563313 168 LPEELLLLICSYLDTRALGRLAQVCRWLRRFTSCDLLWRPI 208
Cdd:cd22139    4 LPDELWLHIFSFLSPKDLCQVALVCRRFNRLASDESLWKQI 44

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 755563313 167 RLPEELLLLICSYLDTRALGRLAQVCRWLRRFTSCDLLWR 206
Cdd:cd22147    4 ALPVELSLKILSYLDAKSLCRAAQVSKKWRNLADDDELWK 43

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 755563313 168 LPEELLLLICSYLDTRALGRLAQVCR-WLRRFTSCDLLWRP 207
Cdd:cd22113    4 LPPEMSLRIFSQLDVQSLCRASQTCKtWNDLIENSDYLWRP 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        40
                 ....*....|....*....|....*....|....*....|
gi 755563313 167 RLPEELLLLICSYLDTRALGRLAQVCRWLRRFTSCDLLWR 206
Cdd:cd22137    2 QLPDLPMLRIFSFLDAFSLLQAAQVNKQWNKVADSDYLWR 41

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 755563313 168 LPEELLLLICSYLDTRALGRLAQVCR-WLRrfTSCD-LLWR 206
Cdd:cd22132    4 LPDSLLLHIFSYLSPKDLLAAGQVCKqWYR--VSRDeFLWK 42

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

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 755563313 167 RLPEELLLLICSYLDTRALGRLAQVCRWLRRFTSCDLLWRPI 208
Cdd:cd22093    3 RLPSEILLKILSYLDASSLLCISCVNKLFYQLANDNALWRKL 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 755563313 168 LPEELLLLICSYLDTRALGRLAQVCRWLRRFTSCDLLWRP 207
Cdd:cd22172    9 LPRVLSLYIFSFLDPRSLCRCAQVCWYWKYLTELDQLWMP 48

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
                 ....*....|....*....|....*....|....*....
gi 755563313 168 LPEELLLLICSYLDTRALGRLAQVCRWLRRFTSCDLLWR 206
Cdd:cd22133   21 LPKELALYVLSFLEPKDLLQAAQTCRYWRILAEDNLLWR 59

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 755563313 168 LPEELLLLICSYLDTRALGRLAQVCRWLRRFTSCDLLWRP 207
Cdd:cd22094    6 LPRFLSLYIFSYLDPRSLCRAAQVSWYWKFLCESDELWLP 45

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 755563313 168 LPEELLLLICSYLDTRALGRLAQVCRWLRRFTSCDLLWR 206
Cdd:cd22091    4 LPDEVLLKIFSYLLEQDLCRAAQVCKRFNTLANDPELWK 42

F-box domain found in F-box/LRR-repeat protein 1 (FBXL1) and similar proteins; FBXL1, also called S-phase kinase-associated protein 2, cyclin-A/CDK2-associated protein p45, F-box protein Skp2, or p45skp2, 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 involved in cell cycle progression, signal transduction and transcription. It specifically recognizes phosphorylated CDKN1B/p27kip and is involved in regulation of G1/S transition. 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 755563313 168 LPEELLLLICSYLDTRALGRLAQVCRWLRRFTSCDLLW 205
Cdd:cd22114    4 LPDELLLGIFSCLCLPDLLKVSQVCKRWYRLASDESLW 41

WD domain, G-beta repeat;

                          10        20        30
                  ....*....|....*....|....*....|...
gi 755563313  334 KYSAHEQEVNCVDC--KGGIIVSGSRDRTAKVW 364
Cdd:pfam00400   6 TLEGHTGSVTSLAFspDGKLLASGSDDGTVKVW 38

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
                 ....*....|....*....|....*....|....*...
gi 755563313 168 LPEELLLLICSYLDTRALGRLAQVCRWLRRFTSCDLLW 205
Cdd:cd22134    7 LPRELALKIFQYLSVTDLCRCAQVSKSWKSLAEDELLW 44

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 755563313 168 LPEELLLLICSYLDTRALGRLAQVCRWLRRFTSCDLLWR 206
Cdd:cd22148    5 LPEHLALKILSYLSPKELLIASQVSKTWRRLASSNELWK 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
                 ....*....|....*....|....*....|....*....
gi 755563313 170 EELLLLICSYLDTRALGRLAQVCR-WlrRFTSCDL-LWR 206
Cdd:cd22109    8 RDALFCVFSYLDTKSLLRCAEVCReW--RDVSRHPaLWQ 44

F-box domain found in Oryza sativa F-box/LRR-repeat Max2 homolog (D3) and similar proteins; D3 is the ortholog of Arabidopsis MORE AXILLARY GROWTH2 (MAX2) and DWARF14 (AtD14) in rice. These proteins are essential signaling components to regulate strigolactone (SL)-repressed plant branching. In rice shoot branching inhibition, the SL-metabolizing alpha/beta hydrolase D14 interacts with the F-box protein D3 to ubiquitinate and degrade the transcription repressor D53. 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 755563313 168 LPEELLLLICSYLDTRALGRLAQVCRWLR 196
Cdd:cd22140    4 LPEDLLLHILSFLNLRDRLNLSLTCKRLR 32