homeobox domain-containing protein may be involved in the transcriptional regulation of key eukaryotic developmental processes; similar to Arabidopsis thaliana homeobox-leucine zipper protein HDG1 that promotes cuticle development probably by modulating the expression of the downstream genes BDG and FDH, possibly repressed in a CFL1-dependent manner
C-terminal lipid-binding START domain of the Arabidopsis homeobox protein GLABRA 2 and related ...
244-468
2.10e-132
C-terminal lipid-binding START domain of the Arabidopsis homeobox protein GLABRA 2 and related proteins; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of the Arabidopsis homeobox protein GLABRA 2 and related proteins. The START domain family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. Most proteins in this subgroup contain an N-terminal homeobox DNA-binding domain, some contain a leucine zipper. ArGLABRA2 plays a role in the differentiation of hairless epidermal cells of the Arabidopsis root. It acts in a cell-position-dependent manner to suppress root hair formation in those cells.
:
Pssm-ID: 176884 Cd Length: 229 Bit Score: 390.86 E-value: 2.10e-132
rod shape-determining protein MreC; MreC (murein formation C) is involved in the rod shape ...
119-195
9.76e-03
rod shape-determining protein MreC; MreC (murein formation C) is involved in the rod shape determination in E. coli, and more generally in cell shape determination of bacteria whether or not they are rod-shaped.
The actual alignment was detected with superfamily member COG1792:
Pssm-ID: 480808 Cd Length: 282 Bit Score: 38.71 E-value: 9.76e-03
C-terminal lipid-binding START domain of the Arabidopsis homeobox protein GLABRA 2 and related ...
244-468
2.10e-132
C-terminal lipid-binding START domain of the Arabidopsis homeobox protein GLABRA 2 and related proteins; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of the Arabidopsis homeobox protein GLABRA 2 and related proteins. The START domain family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. Most proteins in this subgroup contain an N-terminal homeobox DNA-binding domain, some contain a leucine zipper. ArGLABRA2 plays a role in the differentiation of hairless epidermal cells of the Arabidopsis root. It acts in a cell-position-dependent manner to suppress root hair formation in those cells.
Pssm-ID: 176884 Cd Length: 229 Bit Score: 390.86 E-value: 2.10e-132
Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic ...
59-117
2.21e-19
Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic developmental processes; may bind to DNA as monomers or as homo- and/or heterodimers, in a sequence-specific manner.
Pssm-ID: 238039 [Multi-domain] Cd Length: 59 Bit Score: 82.29 E-value: 2.21e-19
C-terminal lipid-binding START domain of the Arabidopsis homeobox protein GLABRA 2 and related ...
244-468
2.10e-132
C-terminal lipid-binding START domain of the Arabidopsis homeobox protein GLABRA 2 and related proteins; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of the Arabidopsis homeobox protein GLABRA 2 and related proteins. The START domain family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. Most proteins in this subgroup contain an N-terminal homeobox DNA-binding domain, some contain a leucine zipper. ArGLABRA2 plays a role in the differentiation of hairless epidermal cells of the Arabidopsis root. It acts in a cell-position-dependent manner to suppress root hair formation in those cells.
Pssm-ID: 176884 Cd Length: 229 Bit Score: 390.86 E-value: 2.10e-132
Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic ...
59-117
2.21e-19
Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic developmental processes; may bind to DNA as monomers or as homo- and/or heterodimers, in a sequence-specific manner.
Pssm-ID: 238039 [Multi-domain] Cd Length: 59 Bit Score: 82.29 E-value: 2.21e-19
Lipid-binding START domain of mammalian STARD1-STARD15 and related proteins; This family ...
367-468
5.08e-07
Lipid-binding START domain of mammalian STARD1-STARD15 and related proteins; This family includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD1-STARD15, and related domains, such as the START domain of the Arabidopsis homeobox protein GLABRA 2. The mammalian STARDs are grouped into 8 subfamilies. This family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. For some members of this family, specific lipids that bind in this pocket are known; these include cholesterol (STARD1/STARD3/ STARD4/STARD5), 25-hydroxycholesterol (STARD5), phosphatidylcholine (STARD2/ STARD7/STARD10), phosphatidylethanolamine (STARD10) and ceramides (STARD11). The START domain is found either alone or in association with other domains. Mammalian STARDs participate in the control of various cellular processes including lipid trafficking between intracellular compartments, lipid metabolism, and modulation of signaling events. Mutation or altered expression of STARDs is linked to diseases such as cancer, genetic disorders, and autoimmune disease. The Arabidopsis homeobox protein GLABRA 2 suppresses root hair formation in hairless epidermal root cells.
Pssm-ID: 176851 [Multi-domain] Cd Length: 193 Bit Score: 50.80 E-value: 5.08e-07
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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