PREDICTED: homeobox-leucine zipper protein ATHB-15 isoform X1 [Tarenaya hassleriana]
Protein Classification
START_ArGLABRA2_like and MEKHLA domain-containing protein( domain architecture ID 11078723)
protein containing domains homeodomain, bZIP, START_ArGLABRA2_like, and MEKHLA
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||
| START_ArGLABRA2_like | cd08875 | C-terminal lipid-binding START domain of the Arabidopsis homeobox protein GLABRA 2 and related ... |
155-371 | 6.17e-74 | ||||
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: 241.02 E-value: 6.17e-74
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| MEKHLA | pfam08670 | MEKHLA domain; The MEKHLA domain shares similarity with the PAS domain and is found in the 3' ... |
696-838 | 2.02e-67 | ||||
MEKHLA domain; The MEKHLA domain shares similarity with the PAS domain and is found in the 3' end of plant HD-ZIP III homeobox genes, and bacterial proteins. : Pssm-ID: 462555 [Multi-domain] Cd Length: 144 Bit Score: 220.08 E-value: 2.02e-67
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| Homeodomain | pfam00046 | Homeodomain; |
17-75 | 1.76e-17 | ||||
Homeodomain; : Pssm-ID: 459649 [Multi-domain] Cd Length: 57 Bit Score: 76.77 E-value: 1.76e-17
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| bZIP | cd14686 | Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and ... |
69-108 | 4.81e-06 | ||||
Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and dimerization domain; Basic leucine zipper (bZIP) factors comprise one of the most important classes of enhancer-type transcription factors. They act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes including cell survival, learning and memory, lipid metabolism, and cancer progression, among others. They also play important roles in responses to stimuli or stress signals such as cytokines, genotoxic agents, or physiological stresses. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription. : Pssm-ID: 269834 [Multi-domain] Cd Length: 52 Bit Score: 44.46 E-value: 4.81e-06
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| Name | Accession | Description | Interval | E-value | ||||
| START_ArGLABRA2_like | cd08875 | C-terminal lipid-binding START domain of the Arabidopsis homeobox protein GLABRA 2 and related ... |
155-371 | 6.17e-74 | ||||
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: 241.02 E-value: 6.17e-74
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| MEKHLA | pfam08670 | MEKHLA domain; The MEKHLA domain shares similarity with the PAS domain and is found in the 3' ... |
696-838 | 2.02e-67 | ||||
MEKHLA domain; The MEKHLA domain shares similarity with the PAS domain and is found in the 3' end of plant HD-ZIP III homeobox genes, and bacterial proteins. Pssm-ID: 462555 [Multi-domain] Cd Length: 144 Bit Score: 220.08 E-value: 2.02e-67
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| START | pfam01852 | START domain; |
160-370 | 3.03e-54 | ||||
START domain; Pssm-ID: 426476 Cd Length: 205 Bit Score: 186.45 E-value: 3.03e-54
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| START | smart00234 | in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ... |
161-369 | 1.52e-37 | ||||
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and phosphatidylcholine transfer protein Pssm-ID: 214575 Cd Length: 205 Bit Score: 139.49 E-value: 1.52e-37
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| Homeodomain | pfam00046 | Homeodomain; |
17-75 | 1.76e-17 | ||||
Homeodomain; Pssm-ID: 459649 [Multi-domain] Cd Length: 57 Bit Score: 76.77 E-value: 1.76e-17
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| homeodomain | cd00086 | Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic ... |
17-77 | 1.09e-16 | ||||
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: 74.59 E-value: 1.09e-16
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| HOX | smart00389 | Homeodomain; DNA-binding factors that are involved in the transcriptional regulation of key ... |
17-74 | 1.68e-16 | ||||
Homeodomain; DNA-binding factors that are involved in the transcriptional regulation of key developmental processes Pssm-ID: 197696 [Multi-domain] Cd Length: 57 Bit Score: 74.21 E-value: 1.68e-16
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| COG5576 | COG5576 | Homeodomain-containing transcription factor [Transcription]; |
1-112 | 5.86e-13 | ||||
Homeodomain-containing transcription factor [Transcription]; Pssm-ID: 227863 [Multi-domain] Cd Length: 156 Bit Score: 67.46 E-value: 5.86e-13
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| bZIP | cd14686 | Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and ... |
69-108 | 4.81e-06 | ||||
Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and dimerization domain; Basic leucine zipper (bZIP) factors comprise one of the most important classes of enhancer-type transcription factors. They act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes including cell survival, learning and memory, lipid metabolism, and cancer progression, among others. They also play important roles in responses to stimuli or stress signals such as cytokines, genotoxic agents, or physiological stresses. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription. Pssm-ID: 269834 [Multi-domain] Cd Length: 52 Bit Score: 44.46 E-value: 4.81e-06
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| BRLZ | smart00338 | basic region leucin zipper; |
69-119 | 2.00e-04 | ||||
basic region leucin zipper; Pssm-ID: 197664 [Multi-domain] Cd Length: 65 Bit Score: 40.24 E-value: 2.00e-04
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| Name | Accession | Description | Interval | E-value | ||||
| START_ArGLABRA2_like | cd08875 | C-terminal lipid-binding START domain of the Arabidopsis homeobox protein GLABRA 2 and related ... |
155-371 | 6.17e-74 | ||||
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: 241.02 E-value: 6.17e-74
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| MEKHLA | pfam08670 | MEKHLA domain; The MEKHLA domain shares similarity with the PAS domain and is found in the 3' ... |
696-838 | 2.02e-67 | ||||
MEKHLA domain; The MEKHLA domain shares similarity with the PAS domain and is found in the 3' end of plant HD-ZIP III homeobox genes, and bacterial proteins. Pssm-ID: 462555 [Multi-domain] Cd Length: 144 Bit Score: 220.08 E-value: 2.02e-67
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| START | pfam01852 | START domain; |
160-370 | 3.03e-54 | ||||
START domain; Pssm-ID: 426476 Cd Length: 205 Bit Score: 186.45 E-value: 3.03e-54
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| START | smart00234 | in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ... |
161-369 | 1.52e-37 | ||||
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and phosphatidylcholine transfer protein Pssm-ID: 214575 Cd Length: 205 Bit Score: 139.49 E-value: 1.52e-37
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| Homeodomain | pfam00046 | Homeodomain; |
17-75 | 1.76e-17 | ||||
Homeodomain; Pssm-ID: 459649 [Multi-domain] Cd Length: 57 Bit Score: 76.77 E-value: 1.76e-17
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| homeodomain | cd00086 | Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic ... |
17-77 | 1.09e-16 | ||||
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: 74.59 E-value: 1.09e-16
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| HOX | smart00389 | Homeodomain; DNA-binding factors that are involved in the transcriptional regulation of key ... |
17-74 | 1.68e-16 | ||||
Homeodomain; DNA-binding factors that are involved in the transcriptional regulation of key developmental processes Pssm-ID: 197696 [Multi-domain] Cd Length: 57 Bit Score: 74.21 E-value: 1.68e-16
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| START | cd00177 | Lipid-binding START domain of mammalian STARD1-STARD15 and related proteins; This family ... |
198-336 | 1.35e-14 | ||||
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: 73.14 E-value: 1.35e-14
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| COG5576 | COG5576 | Homeodomain-containing transcription factor [Transcription]; |
1-112 | 5.86e-13 | ||||
Homeodomain-containing transcription factor [Transcription]; Pssm-ID: 227863 [Multi-domain] Cd Length: 156 Bit Score: 67.46 E-value: 5.86e-13
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| bZIP | cd14686 | Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and ... |
69-108 | 4.81e-06 | ||||
Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and dimerization domain; Basic leucine zipper (bZIP) factors comprise one of the most important classes of enhancer-type transcription factors. They act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes including cell survival, learning and memory, lipid metabolism, and cancer progression, among others. They also play important roles in responses to stimuli or stress signals such as cytokines, genotoxic agents, or physiological stresses. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription. Pssm-ID: 269834 [Multi-domain] Cd Length: 52 Bit Score: 44.46 E-value: 4.81e-06
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| START_STARD9-like | cd08874 | C-terminal START domain of mammalian STARD9, and related domains; lipid binding; This ... |
211-334 | 1.42e-05 | ||||
C-terminal START domain of mammalian STARD9, and related domains; lipid binding; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD9 (also known as KIAA1300), and related domains. 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. Some members of this subfamily have N-terminal kinesin motor domains. STARD9 interacts with supervillin, a protein important for efficient cytokinesis, perhaps playing a role in coordinating microtubule motors with actin and myosin II functions at membranes. The human gene encoding STARD9 lies within a target region for LGMD2A, an autosomal recessive form of limb-girdle muscular dystrophy. Pssm-ID: 176883 Cd Length: 205 Bit Score: 46.83 E-value: 1.42e-05
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| bZIP_CEBP | cd14693 | Basic leucine zipper (bZIP) domain of CCAAT/enhancer-binding protein (CEBP) and similar ... |
69-113 | 1.32e-04 | ||||
Basic leucine zipper (bZIP) domain of CCAAT/enhancer-binding protein (CEBP) and similar proteins: a DNA-binding and dimerization domain; CEBPs (or C/EBPs) are Basic leucine zipper (bZIP) transcription factors that regulate the cell cycle, differentiation, growth, survival, energy metabolism, innate and adaptive immunity, and inflammation, among others. They are also associated with cancer and viral disease. There are six CEBP proteins in mammalian cells including CEBPA (alpha), CEBPB (beta), CEBPG (gamma), CEBPD (delta), and CEBPE (epsilon), which all contain highly conserved bZIP domains at their C-termini and variations at their N-terminal regions. Each possesses unique properties to regulate cell type-specific growth and differentiation. The sixth isoform, CEBPZ (zeta), lacks an intact DNA-binding domain and is excluded from this subfamily. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription. Pssm-ID: 269841 [Multi-domain] Cd Length: 60 Bit Score: 40.62 E-value: 1.32e-04
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| BRLZ | smart00338 | basic region leucin zipper; |
69-119 | 2.00e-04 | ||||
basic region leucin zipper; Pssm-ID: 197664 [Multi-domain] Cd Length: 65 Bit Score: 40.24 E-value: 2.00e-04
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| bZIP_ATF2 | cd14687 | Basic leucine zipper (bZIP) domain of Activating Transcription Factor-2 (ATF-2) and similar ... |
68-110 | 3.57e-04 | ||||
Basic leucine zipper (bZIP) domain of Activating Transcription Factor-2 (ATF-2) and similar proteins: a DNA-binding and dimerization domain; ATF-2 is a sequence-specific DNA-binding protein that belongs to the Basic leucine zipper (bZIP) family of transcription factors. In response to stress, it activates a variety of genes including cyclin A, cyclin D, and c-Jun. ATF-2 also plays a role in the DNA damage response that is independent of its transcriptional activity. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription. Pssm-ID: 269835 [Multi-domain] Cd Length: 61 Bit Score: 39.43 E-value: 3.57e-04
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| START_RhoGAP | cd08869 | C-terminal lipid-binding START domain of mammalian STARD8, -12, -13 and related proteins, ... |
266-334 | 4.78e-04 | ||||
C-terminal lipid-binding START domain of mammalian STARD8, -12, -13 and related proteins, which also have an N-terminal Rho GTPase-activating protein (RhoGAP) domain; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD8 (also known as deleted in liver cancer 3/DLC3, and Arhgap38), STARD12 (also known as DLC-1, Arhgap7, and p122-RhoGAP), and STARD13 (also known as DLC-2, Arhgap37, and SDCCAG13). 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. Proteins belonging to this subfamily also have a RhoGAP domain. Some, including STARD12, -and -13, also have an N-terminal SAM (sterile alpha motif) domain; these have a SAM-RhoGAP-START domain organization. This subfamily is involved in cancer development. A large spectrum of cancers have dysregulated genes encoding these proteins. The precise function of the START domain in this subfamily is unclear. Pssm-ID: 176878 Cd Length: 197 Bit Score: 42.30 E-value: 4.78e-04
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| bZIP_ATF4 | cd14692 | Basic leucine zipper (bZIP) domain of Activating Transcription Factor-4 (ATF-4) and similar ... |
67-110 | 9.63e-04 | ||||
Basic leucine zipper (bZIP) domain of Activating Transcription Factor-4 (ATF-4) and similar proteins: a DNA-binding and dimerization domain; ATF-4 was also isolated and characterized as the cAMP-response element binding protein 2 (CREB2). It is a Basic leucine zipper (bZIP) transcription factor that has been reported to act as both an activator or repressor. It is a critical component in both the unfolded protein response (UPR) and amino acid response (AAR) pathways. Under certain stress conditions, ATF-4 transcription is increased; accumulation of ATF-4 induces the expression of genes involved in amino acid metabolism and transport, mitochondrial function, redox chemistry, and others that ensure protein synthesis and recovery from stress. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription. Pssm-ID: 269840 [Multi-domain] Cd Length: 63 Bit Score: 38.33 E-value: 9.63e-04
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| START_STARD1_3_like | cd08868 | Cholesterol-binding START domain of mammalian STARD1, -3 and related proteins; This subfamily ... |
208-320 | 1.35e-03 | ||||
Cholesterol-binding START domain of mammalian STARD1, -3 and related proteins; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD1 (also known as StAR) and STARD3 (also known as metastatic lymph node 64/MLN64). 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. This STARD1-like subfamily has a high affinity for cholesterol. STARD1/StAR can reduce macrophage lipid content and inflammatory status. It plays an essential role in steroidogenic tissues: transferring the steroid precursor, cholesterol, from the outer to the inner mitochondrial membrane, across the aqueous space. Mutations in the gene encoding STARD1/StAR can cause lipid congenital adrenal hyperplasia (CAH), an autosomal recessive disorder characterized by a steroid synthesis deficiency and an accumulation of cholesterol in the adrenal glands and the gonads. STARD3 may function in trafficking endosomal cholesterol to a cytosolic acceptor or membrane. In addition to having a cytoplasmic START cholesterol-binding domain, STARD3 also contains an N-terminal MENTAL cholesterol-binding and protein-protein interaction domain. The MENTAL domain contains transmembrane helices and anchors MLN64 to endosome membranes. The gene encoding STARD3 is overexpressed in about 25% of breast cancers. Pssm-ID: 176877 Cd Length: 208 Bit Score: 40.80 E-value: 1.35e-03
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| START_STARD10-like | cd08871 | Lipid-binding START domain of mammalian STARD10 and related proteins; This subfamily includes ... |
255-335 | 3.54e-03 | ||||
Lipid-binding START domain of mammalian STARD10 and related proteins; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD10 (also known as CGI-52, PTCP-like, and SDCCAG28). 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. STARD10 binds phophatidylcholine and phosphatidylethanolamine. This protein is widely expressed and is synthesized constitutively in many organs. It may function in the liver in the export of phospholipids into bile. It is concentrated in the sperm flagellum, and may play a role in energy metabolism. In the mammary gland it may participate in the enrichment of lipids in milk, and be a potential marker of differentiation. Its expression is induced in this gland during gestation and lactation. It is overexpressed in mammary tumors from Neu/ErbB2 transgenic mice, in several breast carcinoma cell lines, and in 35% of primary human breast cancers, and may cooperate with c-erbB receptor signaling in breast oncogenesis. It is a potential marker of disease outcome in breast cancer; loss of STARD10 expression in breast cancer strongly predicts an aggressive disease course. The lipid transfer activity of STRAD10 is downregulated by phosphorylation of its Ser284 by CK2 (casein kinase 2). Pssm-ID: 176880 Cd Length: 222 Bit Score: 39.93 E-value: 3.54e-03
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