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 2462625023   7 PLLPDSLVYQIFLSLGPADVLAAGLVCRQWQAVSRDEFLWREQFY 51
Cdd:cd22132     2 PLLPDSLLLHIFSYLSPKDLLAAGQVCKQWYRVSRDEFLWKELFY 46

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.

                           10        20        30
                   ....*....|....*....|....*....|...
gi 2462625023   85 VQTLREHTDQVLHLSFSHSGYQFASCSKDCTVK 117
Cdd:smart00320   5 LKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIK 37

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 2462625023   7 PLLPDSLVYQIFLSLGPADVLAAGLVCRQWQAVSRDEFLWREQFY 51
Cdd:cd22132     2 PLLPDSLLLHIFSYLSPKDLLAAGQVCKQWYRVSRDEFLWKELFY 46

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 2462625023 439 VFDLKTmREVRRALRAHRAYtpndeCFFIFLDVSRDFVASGAEDRHGYIWDRHYNICLARLR-HEDVVNSVVFSPQEQEl 517
Cdd:cd00200   119 VWDVET-GKCLTTLRGHTDW-----VNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATLTgHTGEVNSVAFSPDGEK- 191

                          90
                  ....*....|...
gi 2462625023 518 LLTASDDATIKAW 530
Cdd:cd00200   192 LLSSSSDGTIKLW 204

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.

                           10        20        30
                   ....*....|....*....|....*....|...
gi 2462625023   85 VQTLREHTDQVLHLSFSHSGYQFASCSKDCTVK 117
Cdd:smart00320   5 LKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIK 37

WD domain, G-beta repeat;

                          10        20        30
                  ....*....|....*....|....*....|...
gi 2462625023  85 VQTLREHTDQVLHLSFSHSGYQFASCSKDCTVK 117
Cdd:pfam00400   4 LKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVK 36

WD40 repeat [General function prediction only];

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2462625023  75 RLYDTVPCVEVQTLREHTDQVLHLSFSHSGYQFASCSKDCTVK 117
Cdd:COG2319   145 RLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVR 187

WD domain, G-beta repeat;

                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2462625023 495 CLARLR-HEDVVNSVVFSPQEQeLLLTASDDATIKAW 530
Cdd:pfam00400   3 LLKTLEgHTGSVTSLAFSPDGK-LLASGSDDGTVKVW 38

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 2462625023   7 PLLPDSLVYQIFLSLGPADVLAAGLVCRQWQAVSRDEFLWREQFY 51
Cdd:cd22132     2 PLLPDSLLLHIFSYLSPKDLLAAGQVCKQWYRVSRDEFLWKELFY 46

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 2462625023 439 VFDLKTmREVRRALRAHRAYtpndeCFFIFLDVSRDFVASGAEDRHGYIWDRHYNICLARLR-HEDVVNSVVFSPQEQEl 517
Cdd:cd00200   119 VWDVET-GKCLTTLRGHTDW-----VNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATLTgHTGEVNSVAFSPDGEK- 191

                          90
                  ....*....|...
gi 2462625023 518 LLTASDDATIKAW 530
Cdd:cd00200   192 LLSSSSDGTIKLW 204

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

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2462625023   9 LPDSLVYQIFLSLGPADVLAAGLVCRQWQAVSRDEFLWREQF 50
Cdd:pfam12937   4 LPDEILLQIFSYLDPKDLLRLALVCRRWRELASDDSLWRRLC 45

WD40 repeat [General function prediction only];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625023 420 AVVADPMQPPPIAEEIDLLVFDLKTmREVRRALRAHRAYTPNdecffifLDVSRD--FVASGAEDRHGYIWDRHYNICLA 497
Cdd:COG2319    85 AFSPDGRLLASASADGTVRLWDLAT-GLLLRTLTGHTGAVRS-------VAFSPDgkTLASGSADGTVRLWDLATGKLLR 156

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462625023 498 RLR-HEDVVNSVVFSPQEQeLLLTASDDATIKAW--RSPRTMRVLQAPRPRPRTF-FS----WLAS 555
Cdd:COG2319   157 TLTgHSGAVTSVAFSPDGK-LLASGSDDGTVRLWdlATGKLLRTLTGHTGAVRSVaFSpdgkLLAS 221

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 2462625023 449 RRALRAHRaytpnDECFFIFLDVSRDFVASGAEDRHGYIWDRHYNICLARLR-HEDVVNSVVFSPQeQELLLTASDDATI 527
Cdd:cd00200     2 RRTLKGHT-----GGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKgHTGPVRDVAASAD-GTYLASGSSDKTI 75

                  ...
gi 2462625023 528 KAW 530
Cdd:cd00200    76 RLW 78

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.

                           10        20        30
                   ....*....|....*....|....*....|...
gi 2462625023   85 VQTLREHTDQVLHLSFSHSGYQFASCSKDCTVK 117
Cdd:smart00320   5 LKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIK 37

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 2462625023 389 HVIDIHGHII-GMGLSPDNRYLYVNSRawpNGAVvadpmqpppiaeeidlLVFDLKTMREVRRaLRAHraytpNDECFFI 467
Cdd:cd00200     3 RTLKGHTGGVtCVAFSPDGKLLATGSG---DGTI----------------KVWDLETGELLRT-LKGH-----TGPVRDV 57

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462625023 468 FLDVSRDFVASGAEDRHGYIWDRHYNICLARLR-HEDVVNSVVFSPQEQeLLLTASDDATIKAW 530
Cdd:cd00200    58 AASADGTYLASGSSDKTIRLWDLETGECVRTLTgHTSYVSSVAFSPDGR-ILSSSSRDKTIKVW 120

WD domain, G-beta repeat;

                          10        20        30
                  ....*....|....*....|....*....|...
gi 2462625023  85 VQTLREHTDQVLHLSFSHSGYQFASCSKDCTVK 117
Cdd:pfam00400   4 LKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVK 36

A Receptor for Ubiquitination Targets;

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 2462625023    9 LPDSLVYQIFLSLGPADVLAAGLVCRQWQAVSRDEFLWRE 48
Cdd:smart00256   1 LPDEILEEILSKLDPKDLLRLRKVSRKWRSLIDSHDFWFK 40

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 2462625023   8 LLPDSLVYQIFLSLGPADVLAAGLVCRQWQAVSRDEFLWRE 48
Cdd:cd22148     4 LLPEHLALKILSYLSPKELLIASQVSKTWRRLASSNELWKA 44

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 2462625023   9 LPDSLVYQIFLSLGPADVLAAGLVCRQWQAVSRDEFLW 46
Cdd:cd22114     4 LPDELLLGIFSCLCLPDLLKVSQVCKRWYRLASDESLW 41

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
                  ....*....|....*....|....*....|....*....|...
gi 2462625023  75 RLYDTVPCVEVQTLREHTDQVLHLSFSHSGYQFASCSKDCTVK 117
Cdd:cd00200   118 KVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIK 160

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 2462625023   9 LPDSLVYQIFLSLGPADVLAAGLVCRQWQAVSRDEFLWR 47
Cdd:cd22123     4 LPENVLLEILSYLPVRDLLRISRVCKRWRRLVYDKTLWR 42

F-box domain found in F-box/WD repeat-containing protein 12 (FBXW12) and similar proteins; FBXW12, also called F-box and WD-40 domain-containing protein 12, or F-box only protein 35 (FBXO35), is the substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins. It functions as an epithelial growth suppressor. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.

                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2462625023   9 LPDSLVYQIFLSLGPADVLAAGLVCRQWQAVSRDEFLWR 47
Cdd:cd22137     3 LPDLPMLRIFSFLDAFSLLQAAQVNKQWNKVADSDYLWR 41

F-box domain; This domain is approximately 50 amino acids long, and is usually found in the N-terminal half of a variety of proteins. Two motifs that are commonly found associated with the F-box domain are the leucine rich repeats (LRRs; pfam00560 and pfam07723) and the WD repeat (pfam00400). 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 2462625023   9 LPDSLVYQIFLSLGPADVLAAGLVCRQWQAVSRDEFLWR 47
Cdd:pfam00646   4 LPDDLLLEILSRLDPKDLLRLSLVSKRWRSLVDSLKLWK 42

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 2462625023   8 LLPDSLVYQIFLSLGPADVLAAGLVCRQWQAVSRDEFLW 46
Cdd:cd22124     3 LLPRKAALKIFSYLDLRDLARCAQVCRSWKVITQSSSLW 41

WD40 repeat [General function prediction only];

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2462625023  75 RLYDTVPCVEVQTLREHTDQVLHLSFSHSGYQFASCSKDCTVK 117
Cdd:COG2319   229 RLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVR 271

F-box domain found in F-box only protein 33 (FBXO33) and similar proteins; FBXO33, also called FBX33, 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 exerts similar functions as F-box involved in polyQ pathogenesis (FipoQ) in modulating the ubiquitination and solubility of expanded SCA3-polyQ proteins. 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 2462625023   9 LPDSLVYQIFLSLGPADVLAAGLVCRQWQAVSRDEFLWRE 48
Cdd:cd22104     4 LPSVVLVHIFSYLPPRDRLRASSTCRRWREALFHPSLWRS 43

WD domain, G-beta repeat;

                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2462625023 495 CLARLR-HEDVVNSVVFSPQEQeLLLTASDDATIKAW 530
Cdd:pfam00400   3 LLKTLEgHTGSVTSLAFSPDGK-LLASGSDDGTVKVW 38

F-box domain found in Drosophila melanogaster S-phase kinase-associated protein 2 (DmSKP2) and similar proteins; DmSKP2 is a Drosophila F-box protein that regulates cell proliferation by targeting Dacapo (Dap) for ubiquitination and proteasome-mediated degradation. It plays a role in maintaining diploidy of mitotic cells during development. 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 2462625023   9 LPDSLVYQIFLSLGPADVLAAGLVCRQWQAVSRDEFLWR 47
Cdd:cd22149     4 LSDEIILSIFKWLPKKTLARCARVCRRWKRLCFDESLWR 42

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 2462625023   9 LPDSLVYQIFLSLGPADVLAAGLVCRQWQAVSRDEFLW 46
Cdd:cd22134     7 LPRELALKIFQYLSVTDLCRCAQVSKSWKSLAEDELLW 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 2462625023   8 LLPDSLVYQIFLSLGPADVLAAGLVCRQWQAVSRDEFLWREQF 50
Cdd:cd22147     4 ALPVELSLKILSYLDAKSLCRAAQVSKKWRNLADDDELWKRMC 46

F-box domain found in F-box only protein 13 (FBXO13) and similar proteins; FBXO13, also called FBX13, F-box/LRR-repeat protein 17 (FBL17), or F-box and leucine-rich repeat protein 17 (FBXL17), is the substrate-recognition component of 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        40
                  ....*....|....*....|....*....|....*....|..
gi 2462625023   8 LLPDSLVYQIFLSLGPAD-VLAAGLVCRQWQAVSRDEFLWRE 48
Cdd:cd22092     4 QLPDSILLKIFSYLSLQErCLSASLVCKYWRDLCLDSQFWKQ 45

F-box domain found in F-box only protein 21 (FBXO21) and similar proteins; FBXO21, also called FBX21, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. It facilitates Lys29-linkage and activation of ASK1 (apoptosis signal-regulating kinase 1) and promotes type I interferon production upon viral infection. It also polyubiquitylates EP300-interacting inhibitor of differentiation 1 (EID1) and is required for the efficient degradation of EID1 in both cycling and quiescent 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        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2462625023   7 PLLPDSLVYQIFLS--LGPADVLAAGLVCRQWQAVSRDEFLWREQF 50
Cdd:cd22096     2 LELPDELLEYILCSdnLDHHDIIRLSCTCRRLREVCQSGKVWREKF 47