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 1034644324 292 CTQLTHLYLRRCVRLtDEGLRYLvIYCASIKELSVSDCRFVSDFGLREIAKLESRLRYLSIAHCGRVTDVGIRYVAKYCS 371
Cdd:cd09293    27 HSGLEWLELYMCPIS-DPPLDQL-SNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCP 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644324 372 KLRYLN---ARGCEGITDHGVEYLAKNCTKLKSLDIGKCPlVSDTGLECLALNCF-NLKRLSLKSCESITGQGL-QIVAA 446
Cdd:cd09293   105 KLQTINlgrHRNGHLITDVSLSALGKNCTFLQTVGFAGCD-VTDKGVWELASGCSkSLERLSLNNCRNLTDQSIpAILAS 183

                         170
                  ....*....|....
gi 1034644324 447 NCF-DLQTLNVQDC 459
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 1034644324 180 CLMLETVTVSGCRRLTDRGLYTIAQCCPELRRLEVSGCYNISNEAVFDVVSLCPNLEHLDVSgcSKVTCISLTreasikl 259
Cdd:cd09293    51 CNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCPKLQTINLG--RHRNGHLIT------- 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644324 260 splhgkqisiryldmtdcfvleDEGLHTIAAHCTQLTHLYLRRCvRLTDEGLRYLVIYCA-SIKELSVSDCRFVSDFGLR 338
Cdd:cd09293   122 ----------------------DVSLSALGKNCTFLQTVGFAGC-DVTDKGVWELASGCSkSLERLSLNNCRNLTDQSIP 178

                         170       180
                  ....*....|....*....|....*
gi 1034644324 339 EIAKLES--RLRYLSIAHCGRVTDV 361
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 1034644324 292 CTQLTHLYLRRCVRLtDEGLRYLvIYCASIKELSVSDCRFVSDFGLREIAKLESRLRYLSIAHCGRVTDVGIRYVAKYCS 371
Cdd:cd09293    27 HSGLEWLELYMCPIS-DPPLDQL-SNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCP 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644324 372 KLRYLN---ARGCEGITDHGVEYLAKNCTKLKSLDIGKCPlVSDTGLECLALNCF-NLKRLSLKSCESITGQGL-QIVAA 446
Cdd:cd09293   105 KLQTINlgrHRNGHLITDVSLSALGKNCTFLQTVGFAGCD-VTDKGVWELASGCSkSLERLSLNNCRNLTDQSIpAILAS 183

                         170
                  ....*....|....
gi 1034644324 447 NCF-DLQTLNVQDC 459
Cdd:cd09293   184 NYFpNLSVLEFRGC 197

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

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1034644324 109 IDRLPDHSMVQIFSFLPTNQLCRCARVCRRWYNLAWDPRLWRTI 152
Cdd:pfam12937   1 LSSLPDEILLQIFSYLDPKDLLRLALVCRRWRELASDDSLWRRL 44

A Receptor for Ubiquitination Targets;

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1034644324  112 LPDHSMVQIFSFLPTNQLCRCARVCRRWYNLAWDPRLWRTI 152
Cdd:smart00256   1 LPDEILEEILSKLDPKDLLRLRKVSRKWRSLIDSHDFWFKL 41

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

                           10        20
                   ....*....|....*....|....*.
gi 1034644324  370 CSKLRYLNARGCEGITDHGVEYLAKN 395
Cdd:smart00367   1 CPNLRELDLSGCTNITDEGLQALAKG 26

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

                           10        20
                   ....*....|....*....|....*
gi 1034644324  232 CPNLEHLDVSGCSKVTCISLTREAS 256
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 1034644324 292 CTQLTHLYLRRCVRLtDEGLRYLvIYCASIKELSVSDCRFVSDFGLREIAKLESRLRYLSIAHCGRVTDVGIRYVAKYCS 371
Cdd:cd09293    27 HSGLEWLELYMCPIS-DPPLDQL-SNCNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCP 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644324 372 KLRYLN---ARGCEGITDHGVEYLAKNCTKLKSLDIGKCPlVSDTGLECLALNCF-NLKRLSLKSCESITGQGL-QIVAA 446
Cdd:cd09293   105 KLQTINlgrHRNGHLITDVSLSALGKNCTFLQTVGFAGCD-VTDKGVWELASGCSkSLERLSLNNCRNLTDQSIpAILAS 183

                         170
                  ....*....|....
gi 1034644324 447 NCF-DLQTLNVQDC 459
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 1034644324 230 SLCPNLEHLDVSGCSKVtcisltreasikLSPLHGKQIS--IRYLDMTDCFVLEDEGLHTIAAHCTQLTHLYLRRCVRLT 307
Cdd:cd09293    25 ILHSGLEWLELYMCPIS------------DPPLDQLSNCnkLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENIT 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644324 308 DEGLRYLVIYCASIKELSVSD---CRFVSDFGLREIAKLESRLRYLSIAHCGrVTDVGIRYVAKYCSK-LRYLNARGCEG 383
Cdd:cd09293    93 DSGIVALATNCPKLQTINLGRhrnGHLITDVSLSALGKNCTFLQTVGFAGCD-VTDKGVWELASGCSKsLERLSLNNCRN 171

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1034644324 384 ITDHGVEY-LAKN-CTKLKSLDIGKCPLVSD 412
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 1034644324 321 IKELSVSDCRFVSDFGLREIAKLESRLRYLSIAH---------CGRVTDVGIRYVAKYCSKLRYLNARGCEGITDHGVEY 391
Cdd:cd09293    19 ISQLLRILHSGLEWLELYMCPISDPPLDQLSNCNklkklilpgSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVA 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644324 392 LAKNCTKLKSLDIG---KCPLVSDTGLECLALNCFNLKRLSLKSCEsITGQGLQIVAANCFD-LQTLNVQDC----EVSV 463
Cdd:cd09293    99 LATNCPKLQTINLGrhrNGHLITDVSLSALGKNCTFLQTVGFAGCD-VTDKGVWELASGCSKsLERLSLNNCrnltDQSI 177

                  ...
gi 1034644324 464 EAL 466
Cdd:cd09293   178 PAI 180

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 1034644324 180 CLMLETVTVSGCRRLTDRGLYTIAQCCPELRRLEVSGCYNISNEAVFDVVSLCPNLEHLDVSgcSKVTCISLTreasikl 259
Cdd:cd09293    51 CNKLKKLILPGSKLIDDEGLIALAQSCPNLQVLDLRACENITDSGIVALATNCPKLQTINLG--RHRNGHLIT------- 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644324 260 splhgkqisiryldmtdcfvleDEGLHTIAAHCTQLTHLYLRRCvRLTDEGLRYLVIYCA-SIKELSVSDCRFVSDFGLR 338
Cdd:cd09293   122 ----------------------DVSLSALGKNCTFLQTVGFAGC-DVTDKGVWELASGCSkSLERLSLNNCRNLTDQSIP 178

                         170       180
                  ....*....|....*....|....*
gi 1034644324 339 EIAKLES--RLRYLSIAHCGRVTDV 361
Cdd:cd09293   179 AILASNYfpNLSVLEFRGCPLITDF 203

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 1034644324 111 RLPDHSMVQIFSFLPTNQLCRCARVCRRWYNLAWDPRLWR 150
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 1034644324 109 IDRLPDHSMVQIFSFLPTNQLCRCARVCRRWYNLAWDPRLWRTI 152
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 1034644324 109 IDRLPDHSMVQIFSFLPTNQLCRCARVCRRWYNLAWDPRLWRT 151
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 1034644324 112 LPDHSMVQIFSFLPTNQLCRCARVCRRWYNLAWDPRLWRT 151
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 1034644324 110 DRLPDHSMVQIFSFLPTNQLCRCARVCRRWYNLA 143
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 1034644324 110 DRLPDHSMVQIFSFLPTNQLCRCARVCRRWYNLAWDPRLWRTIRL 154
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 1034644324 110 DRLPDHSMVQIFSFLPTNQLCRCARVCRRWYNLAWDPRLWRTI 152
Cdd:cd22138     2 QSLPVECQLKIFSFLSEVDKCLAATVCRSWSELIRSPRLWRTV 44

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644324 208 ELRRLEVSGCYNISNEAVFDVVSLCPNLEHLDVSGCSKVTciSLTREASIKLSplhGKQISirylDMTDCFvledeglht 287
Cdd:COG4886    71 LLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNEELS--NLTNLESLDLS---GNQLT----DLPEEL--------- 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644324 288 iaAHCTQLTHLYLRRCvRLTD--EGLRYLviycASIKELSVSDCRfVSDFGlREIAKLeSRLRYLSIAHCgRVTDvgIRY 365
Cdd:COG4886   133 --ANLTNLKELDLSNN-QLTDlpEPLGNL----TNLKSLDLSNNQ-LTDLP-EELGNL-TNLKELDLSNN-QITD--LPE 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034644324 366 VAKYCSKLRYLNARGCEgITDHGVEyLAkNCTKLKSLDIGKCPLvsdTGLECLAlNCFNLKRLSLKSCEsITGQGlqiVA 445
Cdd:COG4886   200 PLGNLTNLEELDLSGNQ-LTDLPEP-LA-NLTNLETLDLSNNQL---TDLPELG-NLTNLEELDLSNNQ-LTDLP---PL 268

                         250       260
                  ....*....|....*....|..
gi 1034644324 446 ANCFDLQTLNVQDCEVSVEALR 467
Cdd:COG4886   269 ANLTNLKTLDLSNNQLTDLKLK 290

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 1034644324 112 LPDHSMVQIFSFLPTNQLCRCARVCRRWYNLAWDPRLWRT 151
Cdd:cd22148     5 LPEHLALKILSYLSPKELLIASQVSKTWRRLASSNELWKA 44

F-box domain found in F-box only proteins FBXO6, FBXO44 and similar proteins; This subfamily includes FBXO6 and FBXO44. FBXO6, also called FBX6, F-box protein that recognizes sugar chains 2 (FBS2), or F-box/G-domain protein 2 (FBG2), is a substrate-recognition component of SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complexes. It is involved in the endoplasmic reticulum-associated degradation pathway (ERAD) for misfolded lumenal proteins, by recognizing and binding sugar chains on unfolded glycoproteins that are retro-translocated into the cytosol and promoting their ubiquitination and subsequent degradation. FBXO6 can recognize and bind denatured glycoproteins, which are modified with not only high-mannose but also complex-type oligosaccharides. It also recognizes sulfated glycans. FBXO6 is involved in DNA damage response by specifically recognizing activated CHEK1 (phosphorylated on 'Ser-345'), promoting its ubiquitination and degradation. FBXO44, also called FBXO6A, FBX44, or F-box/G-domain protein 3 (FBG3), is a substrate-recognition component of an SCF-type E3 ubiquitin ligase complex. It interacts with SKP1 and CUL1. FBXO44 mediates BRCA1 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        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1034644324 107 ASIDRLPDHSMVQIFSFLPTNQL-CRCARVCRRWYNLAWDPRLWRT 151
Cdd:cd22168     2 LTISDLPEDVLLEILSLVPARDLiLSCRLVCSRWRDLVDLPTLWKR 47

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 1034644324 108 SIDRLPDHSMVQIFSFLPTNQLCRCA-RVCRRWYNLAWDPRLWRTIRLT 155
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 1034644324 120 IFSFLPTNQLCRCARVCRRWYNLAWDPRLWRTIR 153
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 1034644324 111 RLPDHSMVQIFSFLPTNQLCRCARVCRRWYNLAWDPRLWRTI 152
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 1034644324 109 IDRLPDHSMVQIFSFLPTNQLCRCARVCRRWYNLAWDPRLWR 150
Cdd:cd22084     1 LDDLPSDPLLNILSFLDYRDLISCSQVCRRLNQLCSHDPLWK 42

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

                           10        20
                   ....*....|....*....|....*.
gi 1034644324  370 CSKLRYLNARGCEGITDHGVEYLAKN 395
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 1034644324 109 IDRLPDHSMVQIF----SFLPTNQLCRCARVCRRWYNLAWDPRLWR 150
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 1034644324 109 IDRLPDHSMVQIFSFLPTNQ-LCRCARVCRRWYNL 142
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 1034644324 111 RLPDHSMVQIFSFLPTNQLCRCARVCRRWYNLAWDPRLWRTIR 153
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 1034644324 109 IDRLPDHSMVQIFSFL-PTNQLCRCARVCRRWYNLA 143
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 1034644324 109 IDRLPDHSMVQIFSFLPTNQLCRCARVCRRWYNLAWDPRLWRTI 152
Cdd:cd22093     1 IERLPSEILLKILSYLDASSLLCISCVNKLFYQLANDNALWRKL 44

F-box domain found in F-box/LRR-repeat protein 11 (FBXL11) and similar proteins; FBXL11, also called lysine-specific demethylase 2A (KDM2A), CXXC-type zinc finger protein (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. 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 1034644324 118 VQIFSFLPTNQLCRCARVCRRWYNLAWDPRLW 149
Cdd:cd22181    14 MSVFRYLSRRELCECMRVCKTWYKWCCDKRLW 45

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 1034644324 114 DHSMVQIFSFLPTNQLCRCARVCRRWYNLAWDPRLWR 150
Cdd:cd22130    14 DHIAENILSYLDAKSLCAAELVCKEWYRVIADGMLWK 50

F-box domain found in Arabidopsis thaliana SKP1-interacting partner 19 (AtSKIP19) and similar proteins; AtSKIP19, also called F-box protein SKIP19, or F-box/LRR-repeat protein 20 (FBL20), 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 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        40
                  ....*....|....*....|....*....|....*....|..
gi 1034644324 112 LPDHSMVQIFSFLPTNQLCRCAR-VCRRWYNLAWDPRLWRTI 152
Cdd:cd22164     5 LPDDLTASILSRLGAIDILTNAQkVCKLWRRICKDPSMWRVI 46

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 1034644324 109 IDRLPDHSMVQIFSFLPTNQLCRCARVCRRWYNLAWDPRLWRTIRL 154
Cdd:cd22106     1 LVRLPDKLLLYIISYLDLEDIARLSQTSKRFKKLCNSDELWEKIYM 46

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

                           10        20
                   ....*....|....*....|....
gi 1034644324  396 CTKLKSLDIGKCPLVSDTGLECLA 419
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 1034644324 102 PQKEQASIDRLPDHSMVQIFSFLPTNQLCRCARVCRRWYNLAWDPRLWR 150
Cdd:cd22133    11 PQFQRDFISLLPKELALYVLSFLEPKDLLQAAQTCRYWRILAEDNLLWR 59

F-box domain found in F-box only protein 17 (FBXO17), F-box only protein 27 (FBXO27) and similar proteins; This subfamily includes FBXO17 and FBXO27. FBXO17 is also called FBX17, F-box only protein 26 (FBX26/FBXO26), or FBG4, while FBXO27 is also called FBX27, or F-box/G-domain protein 5. FBXO17 and FBXO27 are the substrate-recognition components of SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complexes. They can recognize and bind denatured glycoproteins, which are modified with complex-type oligosaccharides. FBXO17 also recognizes sulfated glycans but does not bind high-mannose glycoproteins. 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 1034644324 109 IDRLPDHSMVQIFSFLPTNQLC-RCARVCRRWYNLAWDPRLWR 150
Cdd:cd22169     1 LSLLPEELLLLVLSHVPARTLVtRCRLVCRDWRDLVDGPTLWK 43

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 1034644324 108 SIDRLPDHSMVQIFSFLPTNQLCRCARVCRRWYNLAwDPRLWRTI 152
Cdd:cd22143     1 AFDSLPDEILSIIFSHLPQSDLYNLLFVNKHFYSLA-LPELWRSI 44

F-box domain found in F-box/WD repeat-containing protein 1B (FBXW1B) and similar proteins; 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 (SKP1-CUL1-F-box protein) 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 1034644324 114 DHSMVQIFSFLPTNQLCRCARVCRRWYNLAWDPRLWR 150
Cdd:cd22183    14 DHIAENILSYLDAESLCAAELVCKEWQRVISEGMLWK 50

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

                           10        20
                   ....*....|....*....|....*
gi 1034644324  232 CPNLEHLDVSGCSKVTCISLTREAS 256
Cdd:smart00367   1 CPNLRELDLSGCTNITDEGLQALAK 25