GLABRA 2 expression modulator (GEM) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain; GEM interacts with CDT1, a pre-replication complex component that is involved in DNA replication, and with TTG1 (Transparent Testa GLABRA 1), a transcriptional regulator of epidermal cell fate. GEM controls the level of histone H3K9 methylation at the promoters of the GLABRA 2 and CAPRICE (CPC) genes, which are essential for epidermis patterning. GEM also regulates cell division in different root cell types. GEM regulates proliferation-differentiation decisions by integrating DNA replication, cell division and transcriptional controls. The GRAM domain is found in glucosyltransferases, myotubularins and other putative membrane-associated proteins. The GRAM domain is part of a larger motif with a pleckstrin homology (PH) domain fold.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228943872 162 NEKLKKTFACYLSTTTGPVAGTIYLSTARVAFCSDRPLCFTAPSGQETWSYYKVVIPLENIGTVNPVTMRENPSERYIQI 241
Cdd:cd13222     1 EEKLLKTFACYLSTSTGPVAGVLYISTKKIAFCSDRPLSFTSPSGQTSWSYYKVVIPLEQLKSVNPSTNVEKPAEKYIQI 80

                          90       100
                  ....*....|....*....|....*....
gi 1228943872 242 VTVDGHDFWFMGFVNYEKASRHLMNSLSE 270
Cdd:cd13222    81 VTVDGHEFWFMGFVNYDKAFKNLQEALRN 109

GLABRA 2 expression modulator (GEM) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain; GEM interacts with CDT1, a pre-replication complex component that is involved in DNA replication, and with TTG1 (Transparent Testa GLABRA 1), a transcriptional regulator of epidermal cell fate. GEM controls the level of histone H3K9 methylation at the promoters of the GLABRA 2 and CAPRICE (CPC) genes, which are essential for epidermis patterning. GEM also regulates cell division in different root cell types. GEM regulates proliferation-differentiation decisions by integrating DNA replication, cell division and transcriptional controls. The GRAM domain is found in glucosyltransferases, myotubularins and other putative membrane-associated proteins. The GRAM domain is part of a larger motif with a pleckstrin homology (PH) domain fold.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228943872 162 NEKLKKTFACYLSTTTGPVAGTIYLSTARVAFCSDRPLCFTAPSGQETWSYYKVVIPLENIGTVNPVTMRENPSERYIQI 241
Cdd:cd13222     1 EEKLLKTFACYLSTSTGPVAGVLYISTKKIAFCSDRPLSFTSPSGQTSWSYYKVVIPLEQLKSVNPSTNVEKPAEKYIQI 80

                          90       100
                  ....*....|....*....|....*....
gi 1228943872 242 VTVDGHDFWFMGFVNYEKASRHLMNSLSE 270
Cdd:cd13222    81 VTVDGHEFWFMGFVNYDKAFKNLQEALRN 109

domain in glucosyltransferases, myotubularins and other putative membrane-associated proteins;

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1228943872  161 PNEKLKKTFACYLSTTtGPVAGTIYLSTARVAFCSDRPLcftapsgqetwSYYKVVIPLENIGTVNPVT 229
Cdd:smart00568   4 EEEKLIADYSCYLSRT-GPVQGRLYISNYRLCFRSNLPG-----------KLTKVVIPLADITRIEKST 60

GLABRA 2 expression modulator (GEM) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain; GEM interacts with CDT1, a pre-replication complex component that is involved in DNA replication, and with TTG1 (Transparent Testa GLABRA 1), a transcriptional regulator of epidermal cell fate. GEM controls the level of histone H3K9 methylation at the promoters of the GLABRA 2 and CAPRICE (CPC) genes, which are essential for epidermis patterning. GEM also regulates cell division in different root cell types. GEM regulates proliferation-differentiation decisions by integrating DNA replication, cell division and transcriptional controls. The GRAM domain is found in glucosyltransferases, myotubularins and other putative membrane-associated proteins. The GRAM domain is part of a larger motif with a pleckstrin homology (PH) domain fold.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228943872 162 NEKLKKTFACYLSTTTGPVAGTIYLSTARVAFCSDRPLCFTAPSGQETWSYYKVVIPLENIGTVNPVTMRENPSERYIQI 241
Cdd:cd13222     1 EEKLLKTFACYLSTSTGPVAGVLYISTKKIAFCSDRPLSFTSPSGQTSWSYYKVVIPLEQLKSVNPSTNVEKPAEKYIQI 80

                          90       100
                  ....*....|....*....|....*....
gi 1228943872 242 VTVDGHDFWFMGFVNYEKASRHLMNSLSE 270
Cdd:cd13222    81 VTVDGHEFWFMGFVNYDKAFKNLQEALRN 109

Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain; Myotubularin-related proteins are a subfamily of protein tyrosine phosphatases (PTPs) that dephosphorylate D3-phosphorylated inositol lipids. Mutations in this family cause the human neuromuscular disorders myotubular myopathy and type 4B Charcot-Marie-Tooth syndrome. 6 of the 13 MTMRs (MTMRs 5, 9-13) contain naturally occurring substitutions of residues required for catalysis by PTP family enzymes. Although these proteins are predicted to be enzymatically inactive, they are thought to function as antagonists of endogenous phosphatase activity or interaction modules. Most MTMRs contain a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, a PTP domain (which may be active or inactive), a SET-interaction domain, and a C-terminal coiled-coil region. In addition some members contain DENN domain N-terminal to the PH-GRAM domain and FYVE, PDZ, and PH domains C-terminal to the coiled-coil region. The GRAM domain, found in myotubularins, glucosyltransferases, and other putative membrane-associated proteins, is part of a larger motif with a pleckstrin homology (PH) domain fold.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228943872 162 NEKLKKTFACYLSTTTGPVAGTIYLSTARVAFCSDrplcftapsgqETWSYYKVVIPLENIGTVNPVTmRENPSERYIQI 241
Cdd:cd10570     1 IEKLGVRFCCALRPRKLPLEGTLYLSTYRLIFSSK-----------ADGDETKLVIPLVDITDVEKIA-GASFLPSGLII 68

                          90       100
                  ....*....|....*....|....*..
gi 1228943872 242 VTVDgHDFWFMGFVNYEKASRHLMNSL 268
Cdd:cd10570    69 TCKD-FRTIKFSFDSEDEAVKVIARVL 94

Autophagy-related protein 26/Sterol 3-beta-glucosyltransferase Pleckstrin homology (PH) domain, repeat 2; ATG26 (also called UGT51/UDP-glycosyltransferase 51), a member of the glycosyltransferase 28 family, resulting in the biosynthesis of sterol glucoside. ATG26 in decane metabolism and autophagy. There are 32 known autophagy-related (ATG) proteins, 17 are components of the core autophagic machinery essential for all autophagy-related pathways and 15 are the additional components required only for certain pathways or species. The core autophagic machinery includes 1) the ATG9 cycling system (ATG1, ATG2, ATG9, ATG13, ATG18, and ATG27), 2) the phosphatidylinositol 3-kinase complex (ATG6/VPS30, ATG14, VPS15, and ATG34), and 3) the ubiquitin-like protein system (ATG3, ATG4, ATG5, ATG7, ATG8, ATG10, ATG12, and ATG16). Less is known about how the core machinery is adapted or modulated with additional components to accommodate the nonselective sequestration of bulk cytosol (autophagosome formation) or selective sequestration of specific cargos (Cvt vesicle, pexophagosome, or bacteria-containing autophagosome formation). The pexophagosome-specific additions include the ATG30-ATG11-ATG17 receptor-adaptors complex, the coiled-coil protein ATG25, and the sterol glucosyltransferase ATG26. ATG26 is necessary for the degradation of medium peroxisomes. It contains 2 GRAM domains and a single PH domain. PH domains are only found in eukaryotes. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. PH domains also have diverse functions. They are often involved in targeting proteins to the plasma membrane, but few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228943872 162 NEKLKKTFACYLSTTTgPVAGTIYLSTARVAFCSDRPLCFTapsgqetwsyyKVVIPLENIGTVNPVTmRENPSeRYIQI 241
Cdd:cd13216     1 TEKLIASYYCYLIRVL-PVYGKLYVSNNYLCFRSLLPGVST-----------KMILPLRDIENVEKEK-GFRFG-YSGLV 66

                          90
                  ....*....|...
gi 1228943872 242 VTVDGHDFWFMGF 254
Cdd:cd13216    67 IVIKGHEELFFEF 79