Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in Saccharomyces cerevisiae as a component of the Antagonist of MEN pathway (AMEN). The AMEN network is activated by MEN (mitotic exit network) via an active Cdc14, and in turn switches off MEN. Amn1 constitutes one of the alternative mechanisms by which MEN may be disrupted. Specifically, Amn1 binds Tem1 (Termination of M-phase, a GTPase that belongs to the RAS superfamily), and disrupts its association with Cdc15, the primary downstream target. Amn1 is a leucine-rich repeat (LRR) protein, with 12 repeats in the S. cerevisiae ortholog. As a negative regulator of the signal transduction pathway MEN, overexpression of AMN1 slows the growth of wild type cells. The function of the vertebrate members of this family has not been determined experimentally, they have fewer LRRs that determine the extent of this model.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249170 193 IEVSTLHGILsqCSKLQNLSLEGLRLSDPIVNTLAKNSNLVRLNLSGCSGFSEFALQTLLSSCSRLDELNLSWCFDFTEK 272
Cdd:cd09293  17 SNISQLLRIL--HSGLEWLELYMCPISDPPLDQLSNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDS 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249170 273 HVqVAVAHVSETITQLNLSGYRKNLQKSDLS--TLVRRCPNLVHLDL-----SDSVM--LKNDCFQEffqlnyLQHLSLS 343
Cdd:cd09293  95 GI-VALATNCPKLQTINLGRHRNGHLITDVSlsALGKNCTFLQTVGFagcdvTDKGVweLASGCSKS------LERLSLN 167

                ..
gi 14249170 344 RC 345
Cdd:cd09293 168 NC 169

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

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 14249170    97 WDSLPDELLLGIFSCLCLPELLKVSGVCKRWYRLASDESLWQTLD 141
Cdd:pfam12937   1 LSSLPDEILLQIFSYLDPKDLLRLALVCRRWRELASDDSLWRRLC 45

Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in Saccharomyces cerevisiae as a component of the Antagonist of MEN pathway (AMEN). The AMEN network is activated by MEN (mitotic exit network) via an active Cdc14, and in turn switches off MEN. Amn1 constitutes one of the alternative mechanisms by which MEN may be disrupted. Specifically, Amn1 binds Tem1 (Termination of M-phase, a GTPase that belongs to the RAS superfamily), and disrupts its association with Cdc15, the primary downstream target. Amn1 is a leucine-rich repeat (LRR) protein, with 12 repeats in the S. cerevisiae ortholog. As a negative regulator of the signal transduction pathway MEN, overexpression of AMN1 slows the growth of wild type cells. The function of the vertebrate members of this family has not been determined experimentally, they have fewer LRRs that determine the extent of this model.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249170 193 IEVSTLHGILsqCSKLQNLSLEGLRLSDPIVNTLAKNSNLVRLNLSGCSGFSEFALQTLLSSCSRLDELNLSWCFDFTEK 272
Cdd:cd09293  17 SNISQLLRIL--HSGLEWLELYMCPISDPPLDQLSNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDS 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249170 273 HVqVAVAHVSETITQLNLSGYRKNLQKSDLS--TLVRRCPNLVHLDL-----SDSVM--LKNDCFQEffqlnyLQHLSLS 343
Cdd:cd09293  95 GI-VALATNCPKLQTINLGRHRNGHLITDVSlsALGKNCTFLQTVGFagcdvTDKGVweLASGCSKS------LERLSLN 167

                ..
gi 14249170 344 RC 345
Cdd:cd09293 168 NC 169

Leucine-rich repeat (LRR) protein [Transcription];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249170 184 QHMDLSNSviEVSTLHGILSQCSKLQNLSLEGLRLSDpIVNTLAKNSNLVRLNLSGCSgFSEFALQtlLSSCSRLDELNL 263
Cdd:COG4886 139 KELDLSNN--QLTDLPEPLGNLTNLKSLDLSNNQLTD-LPEELGNLTNLKELDLSNNQ-ITDLPEP--LGNLTNLEELDL 212

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249170 264 SwcfdftekhvqvavahvsetITQLnlsgyrknlqkSDLSTLVRRCPNLVHLDLSDSvmlKNDCFQEFFQLNYLQHLSLS 343
Cdd:COG4886 213 S--------------------GNQL-----------TDLPEPLANLTNLETLDLSNN---QLTDLPELGNLTNLEELDLS 258

                .
gi 14249170 344 R 344
Cdd:COG4886 259 N 259

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

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 14249170    97 WDSLPDELLLGIFSCLCLPELLKVSGVCKRWYRLASDESLWQTLD 141
Cdd:pfam12937   1 LSSLPDEILLQIFSYLDPKDLLRLALVCRRWRELASDDSLWRRLC 45

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        40
                ....*....|....*....|....*....|....*....|.
gi 14249170  97 WDSLPDELLLGIFSCLCLPELLKVSGVCKRWYRLASDESLW 137
Cdd:cd22149   1 FERLSDEIILSIFKWLPKKTLARCARVCRRWKRLCFDESLW 41

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 14249170  98 DSLPDELLLGIFSCLCLPELLKVSGVCKRWYRLASDESLWQTL 140
Cdd:cd22091   2 EELPDEVLLKIFSYLLEQDLCRAAQVCKRFNTLANDPELWKRL 44

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 14249170  97 WDSLPDELLLGIFSCLCLPELLKVSGVCKRWYRLASDESLW 137
Cdd:cd22139   1 WLCLPDELWLHIFSFLSPKDLCQVALVCRRFNRLASDESLW 41

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 14249170  98 DSLPDELLLGIFSCLCLPELLKVSGVCKRWYRLAS 132
Cdd:cd09917   1 SDLPDEILLKILSYLDPRDLLRLSLVCKRWRELAS 35

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 14249170  97 WDSLPDELLLGIFSCLCLPELLKVSGVCKRWYRLASDESLWQTLDL 142
Cdd:cd22104   1 WANLPSVVLVHIFSYLPPRDRLRASSTCRRWREALFHPSLWRSLRL 46

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 14249170  98 DSLPDELLLGIFSCLCLPELLKVSGVCKRWYRLASDESLWQTL 140
Cdd:cd22151   1 RKLPDDLLQEIFKRLDPKSLARAACVCRRWRAAARSESLWENA 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 14249170  98 DSLPDELLLGIFSCLCLPELLKVSGVCKRWYRLASDESLW 137
Cdd:cd22118   2 SSLPPEIMLKIFSYLNPQDLCRCAQVCTKWSQLARDGSLW 41

F-box domain found in F-box only protein 3 (FBXO3) and similar proteins; FBXO3, also called FBX3, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. It 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 14249170  98 DSLPDELLLGIFSCLCLPELLKVSGVCKRWYRLASDESLWQTL 140
Cdd:cd22084   2 DDLPSDPLLNILSFLDYRDLISCSQVCRRLNQLCSHDPLWKRL 44

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 14249170  98 DSLPDELLLGIFSCLCLPE-LLKVSGVCKRWYRLASDESLWQTLDLT 143
Cdd:cd22092   3 NQLPDSILLKIFSYLSLQErCLSASLVCKYWRDLCLDSQFWKQIDLS 49

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        40
                ....*....|....*....|....*....|....*....|
gi 14249170  99 SLPDELLLGIFSCLCLPELLKVSGVCKRWYRLASDESLWQ 138
Cdd:cd22115   6 KLPKELLLRIFSFLDVVTLCRCAQVSKYWNVLALDGSNWQ 45

F-box domain found in Arabidopsis thaliana protein ARABIDILLO 1 (AtADLO1) and similar proteins; AtADLO1, also called F-box only protein 5 (FBX5), promotes lateral root initiation and development, independently of auxin (IAA) and abscisic acid (ABA). 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 14249170  97 WDSLPDELLLGIFSCLCLPELLKVSGVCKRWYRLASDESLW 137
Cdd:cd22155   2 WTLLPDDTVLGLFGLLNYRDRASLASVCRAWRALGSSHSLW 42

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 14249170  99 SLPDELLLGIFSCLCLPELLKVSGVCKRWYRLASDESLWQTL 140
Cdd:cd22087   3 ALPPEIKLRILSLLDVRSLLSLSQVCRDLNSATNDQLLWRFL 44

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 14249170  98 DSLPDELLLGIFSCLCLPELLKVSGVCKRWYRLASDESLWQTLDL 142
Cdd:cd22117   2 DLLPYELIQLILSYLDLPSLCRLSQTCKLFRKHCYDPLLWKELNL 46

F-box domain found in Saccharomyces cerevisiae cell division control protein 4 (ScCDC4) and similar proteins; ScCDC4 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 is essential for initiation of DNA replication and separation of the spindle pole bodies to form the poles of the mitotic spindle. It also plays a role in bud development, fusion of zygotic nuclei after conjugation and various aspects of sporulation. 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 14249170  99 SLPDELLLGIFSCLCLPELLKVSGVCKRWYRLASDESLWQTL 140
Cdd:cd22141   3 NLPFEISLKIFNYLQFEDLLNSLGVSKKWNKIIRNTALWKKL 44

F-box domain found in F-box/WD repeat-containing protein 9 (FBXW9) and similar proteins; FBXW9, also called F-box and WD-40 domain-containing protein 9, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target 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 14249170  97 WDSLPDELLLGIFSCLCLPELLKV-SGVCKRWYRLASDESLWQT 139
Cdd:cd22135   1 LLSLPPELLLHICSYLDARFVLHVlPLVCKTFRDILSDETTWRI 44

F-box domain found in Arabidopsis thaliana SKP1-interacting partner 5 (AtSKIP5) and similar proteins; AtSKIP5, also called F-box protein SKIP5, is a component of SCF (SKP1-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. 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 14249170  98 DSLPDELLLGIFSCLC-LPELLKVSGVCKRWYRLASDESLW 137
Cdd:cd22163   2 NDLDDDCLMHIFSFLTpLPDRFNAARVCKRWRALALDPRSW 42

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 14249170 100 LPDELLLGIFSCLCLPELLKVSGVCKRWYRLASDESLWQTL 140
Cdd:cd22147   5 LPVELSLKILSYLDAKSLCRAAQVSKKWRNLADDDELWKRM 45

F-box domain found in Arabidopsis thaliana F-box protein FBW2 (AtFBW2) and similar proteins; AtFBW2, also called SKP1-interacting partner 18 (SKIP18), is an F-box protein that contains four tandem WD-40 repeats. It is a component of SCF (SPK1/ASK-cullin-F-box protein) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins. It interacts with CUL1, CUL2 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
                ....*....|....*....|....*....|....
gi 14249170  97 WDSLPDELLLGIFSCLCLPELLKVSGVCKRWYRL 130
Cdd:cd22158   1 WDCLPPDLLELIFSHLPLHDILICRSVCKFWNRL 34

F-box domain found in F-box only protein 42 (FBXO42) and similar proteins; FBXO42, also called FBX42, or just one F-box and Kelch domain-containing protein (JFK), is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. It specifically recognizes p53/TP53, promoting its ubiquitination and degradation. FBXO42 is also involved in the ubiquitin-proteasome system that may play a role in the pathogenesis of Parkinson's disease (PD). 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 14249170  98 DSLPDELLLGIFSCLCL-PELLKVSGVCKRWYRLASD 133
Cdd:cd22110   2 NDLPEEILEYILSYLSPyGDLKSAALVCKRWHRIIKG 38

F-box domain found in Arabidopsis thaliana actin-related protein 8 (AtARP8) and similar proteins; AtARP8, also called F-box protein ARP8, is an F-box protein localized to the nucleolus in Arabidopsis. Unlike other plant nuclear actin-related proteins (ARPs), ARP8 is unique in having an F-box domain and an actin homology domain. It may play a role in nucleolar functions. 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 14249170  96 SWDSLPDELLLGIFSCLCLPELLKVSGVCKRWYRLASDESLW 137
Cdd:cd22156   1 AFDQLPEDVLMQILRLLGPKDAAKLCLVCKSWRYLVSDNRLW 42

F-box domain found in F-box only protein 41 (FBXO41) and similar proteins; FBXO41, also called FBX41, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. It acts as a novel central nervous system (CNS)-specific F-box protein that localizes to the centrosome and the cytoplasm of neurons and promotes neuronal migration. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 14249170  96 SWDSLP-DELLLGIFSCLCLPELLKVSGVCKRWYRLASDESLWQ 138
Cdd:cd22109   1 SLESLRrRDALFCVFSYLDTKSLLRCAEVCREWRDVSRHPALWQ 44

F-box domain found in F-box/LRR-repeat protein 21 (FBXL21) and similar proteins; FBXL21, also called F-box and leucine-rich repeat protein 21, F-box and leucine-rich repeat protein 3B (FBXL3B), or F-box/LRR-repeat protein 3B, is the substrate-recognition component of the SCF(FBXL21) E3 ubiquitin ligase complex that mainly acts in the cytosol and mediates ubiquitination of CRY proteins (CRY1 and CRY2), leading to CRY protein stabilization, and thus, is involved in circadian rhythm function. It regulates the oscillation of the circadian clock through ubiquitination and stabilization of cryptochromes. 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 14249170  95 VSWDSLPDELLLGIFSCLCLPELLKVSGVCKRWYRLASDESLW 137
Cdd:cd22179   1 LDWGNLPHHVVLHIFQYLPLVDRARASSVCRRWNEVFHIPDLW 43