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 30519963 168 QITKEGIEALVRG-CRGLKALLLRGCTQLeDEALKHIQNhCHELVSLNLQSCSRITDDGVVQICRGCHRLQALCLSGCSN 246
Cdd:cd09293  13 QITQSNISQLLRIlHSGLEWLELYMCPIS-DPPLDQLSN-CNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACEN 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30519963 247 LTDASLTALGLNCPRLQVLEAAR---CSHLTDAGFTLLARNCHELEKMDLEECvLITDSTLVQL-SIHCPKLQALSLSHC 322
Cdd:cd09293  91 ITDSGIVALATNCPKLQTINLGRhrnGHLITDVSLSALGKNCTFLQTVGFAGC-DVTDKGVWELaSGCSKSLERLSLNNC 169

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 30519963 323 ELITDEGILHLSSSTCgHERLRVLELDNCLLVTDASLEHLENCRG 367
Cdd:cd09293 170 RNLTDQSIPAILASNY-FPNLSVLEFRGCPLITDFSRIILFKLWQ 213

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 30519963  76 CGGFLRKLSLRGCIGVGDSSLKTFAQNCRNIEHLNLNGCTKITDSTCYSLSRFCSKLKHLDL---TSCVSVTNSSLKGIS 152
Cdd:cd09293  50 NCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCPKLQTINLgrhRNGHLITDVSLSALG 129

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30519963 153 EGCRNLEYLNLSWCDqITKEGIEALVRGC-RGLKALLLRGCTQLEDEALKHI--QNHCHELVSLNLQSCSRITD 223
Cdd:cd09293 130 KNCTFLQTVGFAGCD-VTDKGVWELASGCsKSLERLSLNNCRNLTDQSIPAIlaSNYFPNLSVLEFRGCPLITD 202

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 30519963 168 QITKEGIEALVRG-CRGLKALLLRGCTQLeDEALKHIQNhCHELVSLNLQSCSRITDDGVVQICRGCHRLQALCLSGCSN 246
Cdd:cd09293  13 QITQSNISQLLRIlHSGLEWLELYMCPIS-DPPLDQLSN-CNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACEN 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30519963 247 LTDASLTALGLNCPRLQVLEAAR---CSHLTDAGFTLLARNCHELEKMDLEECvLITDSTLVQL-SIHCPKLQALSLSHC 322
Cdd:cd09293  91 ITDSGIVALATNCPKLQTINLGRhrnGHLITDVSLSALGKNCTFLQTVGFAGC-DVTDKGVWELaSGCSKSLERLSLNNC 169

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 30519963 323 ELITDEGILHLSSSTCgHERLRVLELDNCLLVTDASLEHLENCRG 367
Cdd:cd09293 170 RNLTDQSIPAILASNY-FPNLSVLEFRGCPLITDFSRIILFKLWQ 213

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 30519963  76 CGGFLRKLSLRGCIGVGDSSLKTFAQNCRNIEHLNLNGCTKITDSTCYSLSRFCSKLKHLDL---TSCVSVTNSSLKGIS 152
Cdd:cd09293  50 NCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCPKLQTINLgrhRNGHLITDVSLSALG 129

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30519963 153 EGCRNLEYLNLSWCDqITKEGIEALVRGC-RGLKALLLRGCTQLEDEALKHI--QNHCHELVSLNLQSCSRITD 223
Cdd:cd09293 130 KNCTFLQTVGFAGCD-VTDKGVWELASGCsKSLERLSLNNCRNLTDQSIPAIlaSNYFPNLSVLEFRGCPLITD 202

A Receptor for Ubiquitination Targets;

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 30519963     15 LPKELLLRIFSFLDIVTLCRCAQISKAWNILALDGSNWQR 54
Cdd:smart00256   1 LPDEILEEILSKLDPKDLLRLRKVSRKWRSLIDSHDFWFK 40

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30519963 109 LNLNGCTKITDSTCYSLSRFCSKLKHLDLTSCVSVTNSSLKGISEGCRNLEYLNLSWCDQITKEGIEALVRGCRGLKALL 188
Cdd:COG4886   1 LLLLLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30519963 189 LRGCTQLEDEALKHIQN-------------HCHELVSLNLqSCSRITDDGvvQICRGCHRLQALCLSGCsNLTDASlTAL 255
Cdd:COG4886  81 LLSLLLLGLTDLGDLTNlteldlsgneelsNLTNLESLDL-SGNQLTDLP--EELANLTNLKELDLSNN-QLTDLP-EPL 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30519963 256 GlNCPRLQVLEAARCsHLTDAGFTLLarNCHELEKMDLEECvLITD--STLVQLsihcPKLQALSLSHCELIT-DEGILH 332
Cdd:COG4886 156 G-NLTNLKSLDLSNN-QLTDLPEELG--NLTNLKELDLSNN-QITDlpEPLGNL----TNLEELDLSGNQLTDlPEPLAN 226

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 30519963 333 LSSstcgherLRVLELDNCLLVtdaSLEHLENCRGLERLELYDCQ 377
Cdd:COG4886 227 LTN-------LETLDLSNNQLT---DLPELGNLTNLEELDLSNNQ 261

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 30519963 168 QITKEGIEALVRG-CRGLKALLLRGCTQLeDEALKHIQNhCHELVSLNLQSCSRITDDGVVQICRGCHRLQALCLSGCSN 246
Cdd:cd09293  13 QITQSNISQLLRIlHSGLEWLELYMCPIS-DPPLDQLSN-CNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACEN 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30519963 247 LTDASLTALGLNCPRLQVLEAAR---CSHLTDAGFTLLARNCHELEKMDLEECvLITDSTLVQL-SIHCPKLQALSLSHC 322
Cdd:cd09293  91 ITDSGIVALATNCPKLQTINLGRhrnGHLITDVSLSALGKNCTFLQTVGFAGC-DVTDKGVWELaSGCSKSLERLSLNNC 169

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 30519963 323 ELITDEGILHLSSSTCgHERLRVLELDNCLLVTDASLEHLENCRG 367
Cdd:cd09293 170 RNLTDQSIPAILASNY-FPNLSVLEFRGCPLITDFSRIILFKLWQ 213

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 30519963  80 LRKLSLRGCiGVGDSSLKTFaQNCRNIEHLNLNGCTKITDSTCYSLSRFCSKLKHLDLTSCVSVTNSSLKGISEGCRNLE 159
Cdd:cd09293  30 LEWLELYMC-PISDPPLDQL-SNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCPKLQ 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30519963 160 YLNLSW---CDQITKEGIEALVRGCRGLKALLLRGCtqledealkhiqnhchelvslnlqscsRITDDGVVQICRGC-HR 235
Cdd:cd09293 108 TINLGRhrnGHLITDVSLSALGKNCTFLQTVGFAGC---------------------------DVTDKGVWELASGCsKS 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 30519963 236 LQALCLSGCSNLTDASLTAL--GLNCPRLQVLEAARCSHLTD 275
Cdd:cd09293 161 LERLSLNNCRNLTDQSIPAIlaSNYFPNLSVLEFRGCPLITD 202

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 30519963 193 TQLEDEALKHIQnhCHELVSLNLQSCSRITDDGVVQICrgCHRLQALCLSGCSNLTDASLTALGLNCPRLQVLEAARCSH 272
Cdd:cd09293  15 TQSNISQLLRIL--HSGLEWLELYMCPISDPPLDQLSN--CNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACEN 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30519963 273 LTDAGFTLLARNCHELEKMDL---EECVLITDSTLVQLSIHCPKLQALSLSHCElITDEGILHLSSStCGHErlrvleld 349
Cdd:cd09293  91 ITDSGIVALATNCPKLQTINLgrhRNGHLITDVSLSALGKNCTFLQTVGFAGCD-VTDKGVWELASG-CSKS-------- 160

                       170       180       190
                ....*....|....*....|....*....|....*
gi 30519963 350 ncllvtdaslehlencrgLERLELYDCQQVTRAGI 384
Cdd:cd09293 161 ------------------LERLSLNNCRNLTDQSI 177

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

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 30519963    15 LPKELLLRIFSFLDIVTLCRCAQISKAWNILALDGSNWQRVD 56
Cdd:pfam12937   4 LPDEILLQIFSYLDPKDLLRLALVCRRWRELASDDSLWRRLC 45

F-box domain found in Schizosaccharomyces pombe Skp1-binding protein 1 (SpPof1) and similar proteins; SpPof1, also called F-box/WD repeat-containing protein pof1, probably recognizes and binds to some phosphorylated proteins and promotes their ubiquitination and degradation. It is required for the inactivation of zip1 via ubiquitination. This subfamily also includes Saccharomyces cerevisiae methionine-requiring protein 30 (ScMET30, also called E3 ubiquitin ligase complex SCF(Met30) subunit MET30), Aspergillus niger sulfur controller B (AnSCONB, also called sulfur metabolite repression control protein B) and Neurospora crassa sulfur controller 2 (NcSCON2, also called sulfur metabolite repression control protein 2). ScMET30 acts as a transcriptional inhibitor that negatively regulates the expression of sulfur amino acid biosynthesis genes. It controls cell cycle function (being required for the G1/S transition and M-phase but not the S-phase), sulfur metabolism, and methionine biosynthesis as part of the E3 ubiquitin ligase complex SCF(Met30). AnSCONB and NcSCON2 are components of the SCF (sconB/scon-2) E3 ubiquitin ligase complexes involved in the regulation of sulfur metabolite repression, probably by mediating the inactivation or degradation of the metR transcription factor. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 30519963  15 LPKELLLRIFSFLDIVTLCRCAQISKAWNILALDGSNWQR 54
Cdd:cd22147   5 LPVELSLKILSYLDAKSLCRAAQVSKKWRNLADDDELWKR 44

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 30519963  13 KKLPKELLLRIFSFLDIVTLCRCAQISKAWNILALDGSNW 52
Cdd:cd22094   4 RVLPRFLSLYIFSYLDPRSLCRAAQVSWYWKFLCESDELW 43

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 30519963  14 KLPKELLLRIFSFLDIVTLCRCAQISKAWNILA 46
Cdd:cd09917   2 DLPDEILLKILSYLDPRDLLRLSLVCKRWRELA 34

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
                ....*....|....*....|....*....
gi 30519963  15 LPKELLLRIFSFLDIVTLCRCAQISKAWN 43
Cdd:cd22113   4 LPPEMSLRIFSQLDVQSLCRASQTCKTWN 32

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 30519963  15 LPKELLLRIFSFLDIVTLCRCAQISKAWNILALDGSNWQR 54
Cdd:cd22148   5 LPEHLALKILSYLSPKELLIASQVSKTWRRLASSNELWKA 44

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 30519963  14 KLPKELLLRIFSFLDIVTLCRCAQISKAWNILALDGSNWQR 54
Cdd:cd22091   3 ELPDEVLLKIFSYLLEQDLCRAAQVCKRFNTLANDPELWKR 43

F-box domain found in F-box/WD repeat-containing protein 2 (FBXW2) and similar proteins; FBXW2, also called F-box and WD-40 domain-containing protein 2, or protein MD6, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. It acts as a tumor suppressor by promoting SKP2 degradation. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.

                        10        20        30
                ....*....|....*....|....*....|.
gi 30519963  13 KKLPKELLLRIFSFLDIVTLCRCAQISKAWN 43
Cdd:cd22131   4 KLLPLELSFYLLSFLDPESLLTCCLVSKQWN 34

F-box domain found in uncharacterized F-box protein group similar to F-box only protein 13 (FBXO13); The family corresponds to a group of uncharacterized F-box proteins which show sequence similarity to F-box only protein 13 (FBXO13). FBXO13, also called FBX13, or F-box/LRR-repeat protein 17 (FBL17), or F-box and leucine-rich repeat protein 17 (FBXL17), is the substrate-recognition component of the SCF(FBXL17) E3 ubiquitin ligase complex, a key component of a quality control pathway required to ensure functional dimerization of BTB domain-containing proteins (dimerization quality control, DQC). The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 30519963  14 KLPKELLLRIFSFLDIVTLCRCAQISKAWNILALDGSNWQRVD 56
Cdd:cd22138   3 SLPVECQLKIFSFLSEVDKCLAATVCRSWSELIRSPRLWRTVD 45

Leucine-rich repeat - CC (cysteine-containing) subfamily;

                           10        20
                   ....*....|....*....|....*.
gi 30519963    311 CPKLQALSLSHCELITDEGILHLSSS 336
Cdd:smart00367   1 CPNLRELDLSGCTNITDEGLQALAKG 26

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

                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 30519963  15 LPKELLLRIFSFLDIVTLCRCAQISKAWNILALDGSNWQR 54
Cdd:cd22122   4 LPREVWLPVFQYLSPKDLCVCMRVCKTWNRWCCDPSLWKR 43

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 30519963  13 KKLPKELLLRIFSFLDIVTLCRCAQISKAWNILALDGSNWQRVDLF 58
Cdd:cd22117   2 DLLPYELIQLILSYLDLPSLCRLSQTCKLFRKHCYDPLLWKELNLQ 47

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
                ....*....|....*....|....*....|....*...
gi 30519963  15 LPKELLLRIFSFLDIVTLCRCAQISKAWNILALDGSNW 52
Cdd:cd22120   4 LPDDVILQIFSHLPTNQLCRCARVCRRWYNLAWDPRLW 41

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 30519963  15 LPKELLLRIFSFLDIVTLCRCAQISKAWNILALDGSNWQRV 55
Cdd:cd22139   4 LPDELWLHIFSFLSPKDLCQVALVCRRFNRLASDESLWKQI 44

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 30519963  15 LPKELLLRIFSFLDIVTLCRCAQISKAWNILALDGSNWQ 53
Cdd:cd22133  21 LPKELALYVLSFLEPKDLLQAAQTCRYWRILAEDNLLWR 59

Leucine-rich repeat - CC (cysteine-containing) subfamily;

                           10        20
                   ....*....|....*....|....*.
gi 30519963    155 CRNLEYLNLSWCDQITKEGIEALVRG 180
Cdd:smart00367   1 CPNLRELDLSGCTNITDEGLQALAKG 26

F-box domain found in F-box/WD repeat-containing protein 10 (FBXW10) and similar proteins; FBXW10, also called F-box and WD-40 domain-containing protein 10, or ubiquitin ligase-specificity factor, is a probable substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Its overexpression leads to degradation of CBX5 and CBX1. FBXW10 is negatively regulated in transcription and expression levels by protein O-GlcNAcylation. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.

                        10        20        30
                ....*....|....*....|....*....|....
gi 30519963  13 KKLPKELLLRIFSFLDIVTLCRCAQISKAWNILA 46
Cdd:cd22136   3 RCLPVHLSKYILSMLDKKSLNNCLCVSQHWRALT 36