F-box domain found in F-box/LRR-repeat protein 6 (FBXL6) and similar proteins; FBXL6, also called F-box and leucine-rich repeat protein 6, or F-box protein FBL6 (FBL6A), is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 525342666 112 GDRIPLEILVQIFGLLVAADGPMPFLGRAARVCRRWQEAASQPALWH 158
Cdd:cd22119    1 GQRLPPEILVKIFQFAVATEGAVPLLCRLSRVCRLWREVALDPSLWT 47

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 525342666 351 SLEELCLASstCNFVSNEVLGRLLHGSPNLRLLDLRGCARITPAGLQDLP--CRELEQLHLGLYGTSDRLTlakEGSPFL 428
Cdd:cd09293   53 KLKKLILPG--SKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALAtnCPKLQTINLGRHRNGHLIT---DVSLSA 127

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 525342666 429 TQKWCHTLRELDLSGQGFSEKDLEQalaafLSTPGGSHPALCSLNlRGTRVTPSTVSSVI--SGCPGLLYLNLESC 502
Cdd:cd09293  128 LGKNCTFLQTVGFAGCDVTDKGVWE-----LASGCSKSLERLSLN-NCRNLTDQSIPAILasNYFPNLSVLEFRGC 197

F-box domain found in F-box/LRR-repeat protein 6 (FBXL6) and similar proteins; FBXL6, also called F-box and leucine-rich repeat protein 6, or F-box protein FBL6 (FBL6A), is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 525342666 112 GDRIPLEILVQIFGLLVAADGPMPFLGRAARVCRRWQEAASQPALWH 158
Cdd:cd22119    1 GQRLPPEILVKIFQFAVATEGAVPLLCRLSRVCRLWREVALDPSLWT 47

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 525342666 188 LMPNRFSQLQRLTL---------IHWKSqlvgeCCPRLTFLKLSGCHGVTADALVMLAKACCQLHSLDLQH-SMVESTAV 257
Cdd:cd09293   22 LLRILHSGLEWLELymcpisdppLDQLS-----NCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRAcENITDSGI 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342666 258 VSfleeagsrmrklwltyssqttailgalLGSCCPQLQVLEVSTGINRNSIPlQLPVEALQKGCPQLQVLRLLNL----- 332
Cdd:cd09293   97 VA---------------------------LATNCPKLQTINLGRHRNGHLIT-DVSLSALGKNCTFLQTVGFAGCdvtdk 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 525342666 333 -MWlpkppgrGVAPGPGfPSLEELCLASstCNFVSNEVLGRLLHGS--PNLRLLDLRGCARIT 392
Cdd:cd09293  149 gVW-------ELASGCS-KSLERLSLNN--CRNLTDQSIPAILASNyfPNLSVLEFRGCPLIT 201

F-box domain found in F-box/LRR-repeat protein 6 (FBXL6) and similar proteins; FBXL6, also called F-box and leucine-rich repeat protein 6, or F-box protein FBL6 (FBL6A), is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 525342666 112 GDRIPLEILVQIFGLLVAADGPMPFLGRAARVCRRWQEAASQPALWH 158
Cdd:cd22119    1 GQRLPPEILVKIFQFAVATEGAVPLLCRLSRVCRLWREVALDPSLWT 47

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 525342666 188 LMPNRFSQLQRLTL---------IHWKSqlvgeCCPRLTFLKLSGCHGVTADALVMLAKACCQLHSLDLQH-SMVESTAV 257
Cdd:cd09293   22 LLRILHSGLEWLELymcpisdppLDQLS-----NCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRAcENITDSGI 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342666 258 VSfleeagsrmrklwltyssqttailgalLGSCCPQLQVLEVSTGINRNSIPlQLPVEALQKGCPQLQVLRLLNL----- 332
Cdd:cd09293   97 VA---------------------------LATNCPKLQTINLGRHRNGHLIT-DVSLSALGKNCTFLQTVGFAGCdvtdk 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 525342666 333 -MWlpkppgrGVAPGPGfPSLEELCLASstCNFVSNEVLGRLLHGS--PNLRLLDLRGCARIT 392
Cdd:cd09293  149 gVW-------ELASGCS-KSLERLSLNN--CRNLTDQSIPAILASNyfPNLSVLEFRGCPLIT 201

F-box domain found in F-box/LRR-repeat protein 7 (FBXL7) and similar proteins; FBXL7, also called F-box and leucine-rich repeat protein 7, or F-box protein FBL6/FBL7, 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 Aurora kinase A (AURKA) during mitosis, causing mitotic arrest. 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 525342666 113 DRIPLEILVQIFGLLvaadgPMPFLGRAARVCRRWQEAASQPALWHTV 160
Cdd:cd22120    2 DRLPDDVILQIFSHL-----PTNQLCRCARVCRRWYNLAWDPRLWTTI 44

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 525342666 351 SLEELCLASstCNFVSNEVLGRLLHGSPNLRLLDLRGCARITPAGLQDLP--CRELEQLHLGLYGTSDRLTlakEGSPFL 428
Cdd:cd09293   53 KLKKLILPG--SKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALAtnCPKLQTINLGRHRNGHLIT---DVSLSA 127

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 525342666 429 TQKWCHTLRELDLSGQGFSEKDLEQalaafLSTPGGSHPALCSLNlRGTRVTPSTVSSVI--SGCPGLLYLNLESC 502
Cdd:cd09293  128 LGKNCTFLQTVGFAGCDVTDKGVWE-----LASGCSKSLERLSLN-NCRNLTDQSIPAILasNYFPNLSVLEFRGC 197

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        40
                 ....*....|....*....|....*....|....*....|
gi 525342666 113 DRIPLEILVQIFGLLVAADgpmpfLGRAARVCRRWQEAAS 152
Cdd:cd09917    1 SDLPDEILLKILSYLDPRD-----LLRLSLVCKRWRELAS 35

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 525342666 120 LVQIFGLLvaadGPMPFLGRAARVCRRWQEAASQPALWHTVT 161
Cdd:cd22163    9 LMHIFSFL----TPLPDRFNAARVCKRWRALALDPRSWLRVK 46

F-box domain found in F-box/LRR-repeat protein 3 (FBXL3) and similar proteins; FBXL3, also called F-box and leucine-rich repeat protein 3A, or F-box/LRR-repeat protein 3A, is the substrate-recognition component of the SCF(FBXL3) E3 ubiquitin ligase complex that mainly acts in the nucleus and mediates ubiquitination and subsequent degradation of CRY1 and CRY2, and thus, is involved in circadian rhythm function. It plays a key role in the maintenance of both the speed and the robustness of the circadian clock oscillation. 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 525342666 111 WGDrIPLEILVQIFGLLvaadgpmPFLGRA--ARVCRRWQEAASQPALW 157
Cdd:cd22178    3 WGN-LLQDIILQIFQYL-------PLLDRAhaSQVCRNWNQVFHMPDLW 43

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 525342666 118 EILVQIFGLLvaadgPMPFLGRAARVCRRWQEAASQPALWH 158
Cdd:cd22149    7 EIILSIFKWL-----PKKTLARCARVCRRWKRLCFDESLWR 42