LysM repeat [Cell wall/membrane/envelope biogenesis];

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 79319963  73 AISHRICRGDSVTSLAVKYAVQVMDIKRLNNMMSDHgIYSRDRLLIPIS 121
Cdd:COG1388 109 PVTYTVKKGDTLWSIARRYGVSVEELKRWNGLSSDT-IRPGQKLKIPAS 156

LysM repeat [Cell wall/membrane/envelope biogenesis];

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 79319963  73 AISHRICRGDSVTSLAVKYAVQVMDIKRLNNMMSDHgIYSRDRLLIPIS 121
Cdd:COG1388 109 PVTYTVKKGDTLWSIARRYGVSVEELKRWNGLSSDT-IRPGQKLKIPAS 156

Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 79319963  74 ISHRICRGDSVTSLAVKYAVQVMDIKRLNNMMSDHGIYSRDRLLI 118
Cdd:cd00118   1 KTYTVKPGDTLWSIAKKYGVTVEELAAANPLINPDCIYPGQKLKI 45

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 79319963   7 DTLIIIFQKLTVADLARASCVCKVWNSVAT 36
Cdd:cd09917   6 EILLKILSYLDPRDLLRLSLVCKRWRELAS 35

LysM repeat [Cell wall/membrane/envelope biogenesis];

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 79319963  73 AISHRICRGDSVTSLAVKYAVQVMDIKRLNNMMSDHgIYSRDRLLIPIS 121
Cdd:COG1388 109 PVTYTVKKGDTLWSIARRYGVSVEELKRWNGLSSDT-IRPGQKLKIPAS 156

Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 79319963  74 ISHRICRGDSVTSLAVKYAVQVMDIKRLNNMMSDHGIYSRDRLLI 118
Cdd:cd00118   1 KTYTVKPGDTLWSIAKKYGVTVEELAAANPLINPDCIYPGQKLKI 45

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 79319963   7 DTLIIIFQKLTVADLARASCVCKVWNSVAT 36
Cdd:cd09917   6 EILLKILSYLDPRDLLRLSLVCKRWRELAS 35

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
                ....*....|....*....|....*..
gi 79319963   6 RDTLIIIFQKLTVADLARASCVCKVWN 32
Cdd:cd22122   6 REVWLPVFQYLSPKDLCVCMRVCKTWN 32

Lysin motif;

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 79319963     76 HRICRGDSVTSLAVKYAVQVMDIKRLNNMMSDHGIYSRDRLLI 118
Cdd:smart00257   2 YTVKKGDTLSSIARRYGISVSDLLELNNILDPDNLQVGQKLKI 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
                ....*....|....*....|....*....|..
gi 79319963   9 LIIIFQKLTVADLARASCVCKVWNSVATEDDL 40
Cdd:cd22091   9 LLKIFSYLLEQDLCRAAQVCKRFNTLANDPEL 40

F-box domain found in F-box/LRR-repeat protein 21 (FBXL21) and similar proteins; FBXL21, also called F-box and leucine-rich repeat protein 21, F-box and leucine-rich repeat protein 3B (FBXL3B), or F-box/LRR-repeat protein 3B, is the substrate-recognition component of the SCF(FBXL21) E3 ubiquitin ligase complex that mainly acts in the cytosol and mediates ubiquitination of CRY proteins (CRY1 and CRY2), leading to CRY protein stabilization, and thus, is involved in circadian rhythm function. It regulates the oscillation of the circadian clock through ubiquitination and stabilization of cryptochromes. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.

                        10        20
                ....*....|....*....|....*...
gi 79319963   7 DTLIIIFQKLTVADLARASCVCKVWNSV 34
Cdd:cd22179   9 HVVLHIFQYLPLVDRARASSVCRRWNEV 36

F-box domain found in the early mitotic inhibitor (EMI) family of F-box proteins; The EMI family includes FBX5 (EMI1) and FBX43 (EMI2), which are anaphase-promoting complex/cyclosome (APC/C) inhibitors that bind APC/C-CCD20 (Cell division cycle protein 20) and/or APC/C-CDH1 (CDC20 homologue 1) 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 79319963   5 CRDTLIIIFQKLTVADLARASCVCKVWNSV 34
Cdd:cd22086   8 CPHILSKILSYLSPEDLCRVSCVSKTWRQI 37