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 767934326 250 CTQLTHLYLRRCVRLtDEGLRYLvIYCASIKELSVSDCRFVSDFGLREIAKLESRLRYLSIAHCGRVTDVGIRYVAKYCS 329
Cdd:cd09293   27 HSGLEWLELYMCPIS-DPPLDQL-SNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCP 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934326 330 KLRYLN---ARGCEGITDHGVEYLAKNCTKLKSLDIGKCPlVSDTGLECLALNCF-NLKRLSLKSCESITGQGL-QIVAA 404
Cdd:cd09293  105 KLQTINlgrHRNGHLITDVSLSALGKNCTFLQTVGFAGCD-VTDKGVWELASGCSkSLERLSLNNCRNLTDQSIpAILAS 183

                        170
                 ....*....|....
gi 767934326 405 NCF-DLQTLNVQDC 417
Cdd:cd09293  184 NYFpNLSVLEFRGC 197

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 767934326 138 CLMLETVTVSGCRRLTDRGLYTIAQCCPELRRLEVSGCYNISNEAVFDVVSLCPNLEHLDVSGCSKvtCISLTreasikl 217
Cdd:cd09293   51 CNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCPKLQTINLGRHRN--GHLIT------- 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934326 218 splhgkqisiryldmtdcfvleDEGLHTIAAHCTQLTHLYLRRCvRLTDEGLRYLVIYCA-SIKELSVSDCRFVSDFGLR 296
Cdd:cd09293  122 ----------------------DVSLSALGKNCTFLQTVGFAGC-DVTDKGVWELASGCSkSLERLSLNNCRNLTDQSIP 178

                        170       180
                 ....*....|....*....|....*
gi 767934326 297 EIAKLES--RLRYLSIAHCGRVTDV 319
Cdd:cd09293  179 AILASNYfpNLSVLEFRGCPLITDF 203

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 767934326 250 CTQLTHLYLRRCVRLtDEGLRYLvIYCASIKELSVSDCRFVSDFGLREIAKLESRLRYLSIAHCGRVTDVGIRYVAKYCS 329
Cdd:cd09293   27 HSGLEWLELYMCPIS-DPPLDQL-SNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCP 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934326 330 KLRYLN---ARGCEGITDHGVEYLAKNCTKLKSLDIGKCPlVSDTGLECLALNCF-NLKRLSLKSCESITGQGL-QIVAA 404
Cdd:cd09293  105 KLQTINlgrHRNGHLITDVSLSALGKNCTFLQTVGFAGCD-VTDKGVWELASGCSkSLERLSLNNCRNLTDQSIpAILAS 183

                        170
                 ....*....|....
gi 767934326 405 NCF-DLQTLNVQDC 417
Cdd:cd09293  184 NYFpNLSVLEFRGC 197

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 767934326 138 CLMLETVTVSGCRRLTDRGLYTIAQCCPELRRLEVSGCYNISNEAVFDVVSLCPNLEHLDVSGCSKvtCISLTreasikl 217
Cdd:cd09293   51 CNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCPKLQTINLGRHRN--GHLIT------- 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934326 218 splhgkqisiryldmtdcfvleDEGLHTIAAHCTQLTHLYLRRCvRLTDEGLRYLVIYCA-SIKELSVSDCRFVSDFGLR 296
Cdd:cd09293  122 ----------------------DVSLSALGKNCTFLQTVGFAGC-DVTDKGVWELASGCSkSLERLSLNNCRNLTDQSIP 178

                        170       180
                 ....*....|....*....|....*
gi 767934326 297 EIAKLES--RLRYLSIAHCGRVTDV 319
Cdd:cd09293  179 AILASNYfpNLSVLEFRGCPLITDF 203

A Receptor for Ubiquitination Targets;

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 767934326    70 LPDHSMVQIFSFLPTNQLCRCARVCRRWYNLAWDPRLWRTI 110
Cdd:smart00256   1 LPDEILEEILSKLDPKDLLRLRKVSRKWRSLIDSHDFWFKL 41

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

                           10        20
                   ....*....|....*....|....*.
gi 767934326   328 CSKLRYLNARGCEGITDHGVEYLAKN 353
Cdd:smart00367   1 CPNLRELDLSGCTNITDEGLQALAKG 26

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

                           10        20
                   ....*....|....*....|....*
gi 767934326   190 CPNLEHLDVSGCSKVTCISLTREAS 214
Cdd:smart00367   1 CPNLRELDLSGCTNITDEGLQALAK 25

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 767934326 250 CTQLTHLYLRRCVRLtDEGLRYLvIYCASIKELSVSDCRFVSDFGLREIAKLESRLRYLSIAHCGRVTDVGIRYVAKYCS 329
Cdd:cd09293   27 HSGLEWLELYMCPIS-DPPLDQL-SNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCP 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934326 330 KLRYLN---ARGCEGITDHGVEYLAKNCTKLKSLDIGKCPlVSDTGLECLALNCF-NLKRLSLKSCESITGQGL-QIVAA 404
Cdd:cd09293  105 KLQTINlgrHRNGHLITDVSLSALGKNCTFLQTVGFAGCD-VTDKGVWELASGCSkSLERLSLNNCRNLTDQSIpAILAS 183

                        170
                 ....*....|....
gi 767934326 405 NCF-DLQTLNVQDC 417
Cdd:cd09293  184 NYFpNLSVLEFRGC 197

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 767934326 188 SLCPNLEHLDVSGCSKVtcisltreasikLSPLHGKQIS--IRYLDMTDCFVLEDEGLHTIAAHCTQLTHLYLRRCVRLT 265
Cdd:cd09293   25 ILHSGLEWLELYMCPIS------------DPPLDQLSNCnkLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENIT 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934326 266 DEGLRYLVIYCASIKELSVSD---CRFVSDFGLREIAKLESRLRYLSIAHCGrVTDVGIRYVAKYCSK-LRYLNARGCEG 341
Cdd:cd09293   93 DSGIVALATNCPKLQTINLGRhrnGHLITDVSLSALGKNCTFLQTVGFAGCD-VTDKGVWELASGCSKsLERLSLNNCRN 171

                        170       180       190
                 ....*....|....*....|....*....|.
gi 767934326 342 ITDHGVEY-LAKN-CTKLKSLDIGKCPLVSD 370
Cdd:cd09293  172 LTDQSIPAiLASNyFPNLSVLEFRGCPLITD 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 767934326 279 IKELSVSDCRFVSDFGLREIAKLESRLRYLSIAH---------CGRVTDVGIRYVAKYCSKLRYLNARGCEGITDHGVEY 349
Cdd:cd09293   19 ISQLLRILHSGLEWLELYMCPISDPPLDQLSNCNklkklilpgSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVA 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934326 350 LAKNCTKLKSLDIG---KCPLVSDTGLECLALNCFNLKRLSLKSCEsITGQGLQIVAANCFD-LQTLNVQDC----EVSV 421
Cdd:cd09293   99 LATNCPKLQTINLGrhrNGHLITDVSLSALGKNCTFLQTVGFAGCD-VTDKGVWELASGCSKsLERLSLNNCrnltDQSI 177

                 ...
gi 767934326 422 EAL 424
Cdd:cd09293  178 PAI 180

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

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 767934326   67 IDRLPDHSMVQIFSFLPTNQLCRCARVCRRWYNLAWDPRLWRTI 110
Cdd:pfam12937   1 LSSLPDEILLQIFSYLDPKDLLRLALVCRRWRELASDDSLWRRL 44

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 767934326  69 RLPDHSMVQIFSFLPTNQLCRCARVCRRWYNLAWDPRLWR 108
Cdd:cd22149    3 RLSDEIILSIFKWLPKKTLARCARVCRRWKRLCFDESLWR 42

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 767934326  67 IDRLPDHSMVQIFSFLPTNQLCRCARVCRRWYNLAWDPRLWRTI 110
Cdd:cd22091    1 QEELPDEVLLKIFSYLLEQDLCRAAQVCKRFNTLANDPELWKRL 44

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        40
                  ....*....|....*....|....*....|....*....|...
gi 767934326   67 IDRLPDHSMVQIFSFLPTNQLCRCARVCRRWYNLAWDPRLWRT 109
Cdd:pfam00646   1 LLDLPDDLLLEILSRLDPKDLLRLSLVSKRWRSLVDSLKLWKK 43

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 767934326  70 LPDHSMVQIFSFLPTNQLCRCARVCRRWYNLAWDPRLWRT 109
Cdd:cd22122    4 LPREVWLPVFQYLSPKDLCVCMRVCKTWNRWCCDPSLWKR 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 767934326  68 DRLPDHSMVQIFSFLPTNQLCRCARVCRRWYNLA 101
Cdd:cd09917    1 SDLPDEILLKILSYLDPRDLLRLSLVCKRWRELA 34

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 767934326  68 DRLPDHSMVQIFSFLPTNQLCRCARVCRRWYNLAWDPRLWRTIRL 112
Cdd:cd22104    2 ANLPSVVLVHIFSYLPPRDRLRASSTCRRWREALFHPSLWRSLRL 46

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 767934326  68 DRLPDHSMVQIFSFLPTNQLCRCARVCRRWYNLAWDPRLWRTI 110
Cdd:cd22138    2 QSLPVECQLKIFSFLSEVDKCLAATVCRSWSELIRSPRLWRTV 44

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934326 166 ELRRLEVSGCYNISNEAVFDVVSLCPNLEHLDVSGCSKVTciSLTREASIKLSplhGKQISirylDMTDCFvledeglht 245
Cdd:COG4886   71 LLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNEELS--NLTNLESLDLS---GNQLT----DLPEEL--------- 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934326 246 iaAHCTQLTHLYLRRCvRLTD--EGLRYLviycASIKELSVSDCRfVSDFGlREIAKLeSRLRYLSIAHCgRVTDvgIRY 323
Cdd:COG4886  133 --ANLTNLKELDLSNN-QLTDlpEPLGNL----TNLKSLDLSNNQ-LTDLP-EELGNL-TNLKELDLSNN-QITD--LPE 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934326 324 VAKYCSKLRYLNARGCEgITDHGVEyLAkNCTKLKSLDIGKCPLvsdTGLECLAlNCFNLKRLSLKSCEsITGQGlqiVA 403
Cdd:COG4886  200 PLGNLTNLEELDLSGNQ-LTDLPEP-LA-NLTNLETLDLSNNQL---TDLPELG-NLTNLEELDLSNNQ-LTDLP---PL 268

                        250       260
                 ....*....|....*....|..
gi 767934326 404 ANCFDLQTLNVQDCEVSVEALR 425
Cdd:COG4886  269 ANLTNLKTLDLSNNQLTDLKLK 290

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 767934326  70 LPDHSMVQIFSFLPTNQLCRCARVCRRWYNLAWDPRLWRTIR 111
Cdd:cd22139    4 LPDELWLHIFSFLSPKDLCQVALVCRRFNRLASDESLWKQIC 45

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
                 ....*....|....*....|....*....|....*....
gi 767934326  70 LPDHSMVQIFSFLPTNQLCRCARVCRRWYNLAWDPRLWR 108
Cdd:cd22132    4 LPDSLLLHIFSYLSPKDLLAAGQVCKQWYRVSRDEFLWK 42

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 767934326  66 SIDRLPDHSMVQIFSFLPTNQLCRCA-RVCRRWYNLAWDPRLWRTIRLT 113
Cdd:cd22092    1 NINQLPDSILLKIFSYLSLQERCLSAsLVCKYWRDLCLDSQFWKQIDLS 49

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

                         10        20        30
                 ....*....|....*....|....*....|....
gi 767934326  78 IFSFLPTNQLCRCARVCRRWYNLAWDPRLWRTIR 111
Cdd:cd22109   14 VFSYLDTKSLLRCAEVCREWRDVSRHPALWQRVC 47

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

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 767934326  69 RLPDHSMVQIFSFLPTNQLCRCARVCRRWYNLAWDPRLWRTI 110
Cdd:cd22137    2 QLPDLPMLRIFSFLDAFSLLQAAQVNKQWNKVADSDYLWRNL 43

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 767934326  67 IDRLPDHSMVQIFSFLPTNQLCRCARVCRRWYNLAWDPRLWR 108
Cdd:cd22084    1 LDDLPSDPLLNILSFLDYRDLISCSQVCRRLNQLCSHDPLWK 42

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

                           10        20
                   ....*....|....*....|....*.
gi 767934326   328 CSKLRYLNARGCEGITDHGVEYLAKN 353
Cdd:smart00367   1 CPNLRELDLSGCTNITDEGLQALAKG 26

F-box domain found in F-box only protein 9 (FBXO9) and similar proteins; FBXO9, also called FBX9, cross-immune reaction antigen 1, renal carcinoma antigen NY-REN-57, or VCIA1, 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 TTI1 and TELO2 in a CK2-dependent manner, thereby directly regulating mTOR signaling. FBXO9 acts as an E3 ubiquitin ligase that regulates the stability and activity of peroxisome proliferator-activated receptor gamma (PPARgamma) through ubiquitination. It is also required for adipocyte differentiation. 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 767934326  67 IDRLPDHSMVQIF----SFLPTNQLCRCARVCRRWYNLAWDPRLWR 108
Cdd:cd22089    3 ISALPSEILLYILrwvvSDLDLRSLEQLSLVCRKFYLLARDPSIWR 48

F-box domain found in Arabidopsis thaliana transport inhibitor response 1 protein (TIR1), coronatine-insensitive protein 1 (COI1) and similar proteins; TIR1, also called F-box/LRR-repeat protein 1 (FBL1), is part of an SCF (SKP1-cullin-F-box) protein ligase complex that promotes the ubiquitin-dependent proteolysis of a family of transcriptional regulators known as Aux/IAAs in an auxin-dependent manner. TIR1 is an auxin receptor that plays a potential role in plant hormone signaling. COI1, also called F-box/LRR-repeat protein 2 (FBL2), is the substrate-recruiting module of an SCF ubiquitin E3 ligase complex. It mediates jasmonate signalling by promoting hormone-dependent ubiquitylation and degradation of transcriptional repressor JASMONATE ZIM-domain (JAZ) family proteins. This subfamily also includes Arabidopsis thaliana EIN3-binding F-box protein 1 (EBF1). EBF1, also called F-box/LRR-repeat protein 6 (FBL6), is a component of the SCF(EBF1) E3 ubiquitin ligase complex, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins (probably including EIN3 and EIL1). 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 767934326  67 IDRLPDHSMVQIFSFLPTNQ-LCRCARVCRRWYNL 100
Cdd:cd22159    1 IDLLPDEILELIFSYLSDPWdRNSCSLVCKRWYRL 35

F-box domain found in F-box/WD repeat-containing protein 4 (FBXW4) and similar proteins; FBXW4, also called dactylin, or F-box and WD-40 domain-containing protein 4, probably recognizes and binds to some phosphorylated proteins and promotes their ubiquitination and degradation. It is likely to be involved in key signaling pathways crucial for normal limb development. It may participate in Wnt signaling and act as a novel tumor suppressor that regulates important cellular processes. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 767934326  69 RLPDHSMVQIFSFLPTNQLCRCARVCRRWYNLAWDPRLWRTIR 111
Cdd:cd20090    4 DLPDDLLFLIFSYLDPASLGRLSQVCRRLYRLISRDAVWRRIA 46

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 767934326  67 IDRLPDHSMVQIFSFL-PTNQLCRCARVCRRWYNLA 101
Cdd:cd22110    1 INDLPEEILEYILSYLsPYGDLKSAALVCKRWHRII 36

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

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 767934326  67 IDRLPDHSMVQIFSFLPTNQLCRCARVCRRWYNLAWDPRLWRTI 110
Cdd:cd22093    1 IERLPSEILLKILSYLDASSLLCISCVNKLFYQLANDNALWRKL 44

F-box domain found in F-box/WD repeat-containing proteins, FBXW1A, FBXW1B and similar proteins; FBXW1A, also called E3RSIkappaB, epididymis tissue protein Li 2a, F-box and WD repeats protein beta-TrCP, or pIkappaBalpha-E3 receptor subunit, 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 CTNNB1, NFKBIA, NFKBIB and NFKBIE, as well as phosphorylated NFKB1, ATF4, CDC25A, DLG1, FBXO5, PER1, SMAD3, SMAD4, SNAI1 and probably NFKB2. FBXW1B, also called F-box/WD repeat-containing protein 11 (FBXW11), F-box and WD repeats protein beta-TrCP2, or homologous to Slimb protein (HOS), is the substrate-recognition component of an SCF E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins, such as IFNAR1, CEP68 and CDC25A, as well as phosphorylated CTNNB1, NFKBIA, PER1 and PER2. 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 767934326  72 DHSMVQIFSFLPTNQLCRCARVCRRWYNLAWDPRLWR 108
Cdd:cd22130   14 DHIAENILSYLDAKSLCAAELVCKEWYRVIADGMLWK 50

F-box domain found in F-box only protein 22 (FBXO22) and similar proteins; FBXO22, also called FBX22, or F-box protein FBX22p44, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. It promotes the proteasome-dependent degradation of key sarcomeric proteins, such as alpha-actinin (ACTN2) and filamin-C (FLNC), essential for maintenance of normal contractile function. FBXO22 regulates histone H3 lysine 9 and 36 methylation levels by targeting histone demethylase KDM4A for ubiquitin-mediated proteasomal 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
                 ....*....|....*....|....
gi 767934326  78 IFSFLPTNQLCRCARVCRRWYNLA 101
Cdd:cd22097   11 ILSFLPAKALLRCARVCRLWRDCA 34

F-box domain found in F-box/LRR-repeat protein 10 (FBXL10) and similar proteins; FBXL10 is also called lysine-specific demethylase 2B (KDM2B), CXXC-type zinc finger protein 2 (CXXC2), F-box and leucine-rich repeat protein 10, F-box protein 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. 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 767934326  78 IFSFLPTNQLCRCARVCRRWYNLAWDPRLW 107
Cdd:cd22180   14 VFSYLSHRDLCVCMRVCRTWNRWCCDKRLW 43

F-box domain found in F-box only protein 36 (FBXO36) and similar proteins; FBXO36, also called FBX36, likely functions as 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 767934326  67 IDRLPDHSMVQIFSFLPTNQLCRCARVCRRWYNLAWDPRLWRTIRL 112
Cdd:cd22106    1 LVRLPDKLLLYIISYLDLEDIARLSQTSKRFKKLCNSDELWEKIYM 46

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

                           10        20
                   ....*....|....*....|....
gi 767934326   354 CTKLKSLDIGKCPLVSDTGLECLA 377
Cdd:smart00367   1 CPNLRELDLSGCTNITDEGLQALA 24

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        40
                 ....*....|....*....|....*....|....*....|....*....
gi 767934326  60 PQKEQASIDRLPDHSMVQIFSFLPTNQLCRCARVCRRWYNLAWDPRLWR 108
Cdd:cd22133   11 PQFQRDFISLLPKELALYVLSFLEPKDLLQAAQTCRYWRILAEDNLLWR 59

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
                 ....*....|....*....|....*....|....*....
gi 767934326  69 RLPDHSMVQIFSFLPTNQLCRCARVCRRWYNLAWDPRLW 107
Cdd:cd22155    4 LLPDDTVLGLFGLLNYRDRASLASVCRAWRALGSSHSLW 42

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 767934326  66 SIDRLPDHSMVQIFSFLPTNQLCRCARVCRRWYNLAWDPRLW 107
Cdd:cd22156    1 AFDQLPEDVLMQILRLLGPKDAAKLCLVCKSWRYLVSDNRLW 42

F-box domain found in Saccharomyces cerevisiae mitochondrial distribution and morphology protein 30 (ScMDM30) and similar proteins; ScMDM30 is an F-box protein required for maintenance of fusion-competent mitochondria in yeast. It 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. ScMDM30 recognizes FZO1 and regulates the amount of FZO1. It acts as a regulatory factor for the mitochondrial fusion machinery and is required for mitochondrial DNA maintenance. 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 767934326  66 SIDRLPDHSMVQIFSFLPTNQLCRCARVCRRWYNLAwDPRLWRTI 110
Cdd:cd22143    1 AFDSLPDEILSIIFSHLPQSDLYNLLFVNKHFYSLA-LPELWRSI 44

F-box domain found in F-box only protein 10 (FBXO10) and similar proteins; FBXO10, also called FBX10, or PRMT11, is the substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. The SCF(FBXO10) complex mediates ubiquitination and degradation of BCL2, an anti-apoptotic protein, thereby playing a role in apoptosis by controlling the stability of BCL2. It also associates with the receptor for advanced glycation end products (RAGE) to mediate its ubiquitination and 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
                 ....*....|....*....|...
gi 767934326  78 IFSFLPTNQLCRCARVCRRWYNL 100
Cdd:cd22090   13 ILAYLPVRDLCRCCQVCRAWYEL 35